data_7I41
# 
_entry.id   7I41 
# 
_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   7I41         pdb_00007i41 10.2210/pdb7i41/pdb 
WWPDB D_1001408288 ?            ?                   
# 
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                        7I41 
_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-[(1,2-benzoxazol-3-yl)methyl]-6-oxopiperidine-3-carboxamide' 273.287   2   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                           65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                 78.133    3   ?         ? ? ? 
5 water       nat water                                                                18.015    294 ?         ? ? ? 
# 
_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-[(1,2-benzoxazol-3-yl)methyl]-6-oxopiperidine-3-carboxamide' A1B2E 
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 
A1B2E non-polymer         . '(3S)-1-[(1,2-benzoxazol-3-yl)methyl]-6-oxopiperidine-3-carboxamide' ? 'C14 H15 N3 O3'  273.287 
ALA   'L-peptide linking' y ALANINE                                                              ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                             ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                           ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                      ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                             ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                 ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                            ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                      ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                              ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                            ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                           ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                              ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                               ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                           ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                        ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                              ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                               ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                            ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                           ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                             ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                               ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                           ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 ?   ?   ?   C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B2E 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B2E 
_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 A1B2E 1   201 201 A1B2E LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 6   DMS   DMS A . 
F 2 A1B2E 1   201 201 A1B2E LIG C . 
G 4 DMS   1   202 7   DMS   DMS C . 
H 3 ZN    1   203 1   ZN    ZN  C . 
I 4 DMS   1   204 6   DMS   DMS C . 
J 5 HOH   1   301 61  HOH   HOH A . 
J 5 HOH   2   302 95  HOH   HOH A . 
J 5 HOH   3   303 256 HOH   HOH A . 
J 5 HOH   4   304 174 HOH   HOH A . 
J 5 HOH   5   305 161 HOH   HOH A . 
J 5 HOH   6   306 149 HOH   HOH A . 
J 5 HOH   7   307 176 HOH   HOH A . 
J 5 HOH   8   308 166 HOH   HOH A . 
J 5 HOH   9   309 165 HOH   HOH A . 
J 5 HOH   10  310 14  HOH   HOH A . 
J 5 HOH   11  311 190 HOH   HOH A . 
J 5 HOH   12  312 60  HOH   HOH A . 
J 5 HOH   13  313 1   HOH   HOH A . 
J 5 HOH   14  314 250 HOH   HOH A . 
J 5 HOH   15  315 22  HOH   HOH A . 
J 5 HOH   16  316 84  HOH   HOH A . 
J 5 HOH   17  317 93  HOH   HOH A . 
J 5 HOH   18  318 103 HOH   HOH A . 
J 5 HOH   19  319 24  HOH   HOH A . 
J 5 HOH   20  320 22  HOH   HOH A . 
J 5 HOH   21  321 59  HOH   HOH A . 
J 5 HOH   22  322 34  HOH   HOH A . 
J 5 HOH   23  323 116 HOH   HOH A . 
J 5 HOH   24  324 102 HOH   HOH A . 
J 5 HOH   25  325 153 HOH   HOH A . 
J 5 HOH   26  326 152 HOH   HOH A . 
J 5 HOH   27  327 247 HOH   HOH A . 
J 5 HOH   28  328 63  HOH   HOH A . 
J 5 HOH   29  329 56  HOH   HOH A . 
J 5 HOH   30  330 235 HOH   HOH A . 
J 5 HOH   31  331 13  HOH   HOH A . 
J 5 HOH   32  332 99  HOH   HOH A . 
J 5 HOH   33  333 183 HOH   HOH A . 
J 5 HOH   34  334 109 HOH   HOH A . 
J 5 HOH   35  335 141 HOH   HOH A . 
J 5 HOH   36  336 133 HOH   HOH A . 
J 5 HOH   37  337 27  HOH   HOH A . 
J 5 HOH   38  338 241 HOH   HOH A . 
J 5 HOH   39  339 49  HOH   HOH A . 
J 5 HOH   40  340 23  HOH   HOH A . 
J 5 HOH   41  341 5   HOH   HOH A . 
J 5 HOH   42  342 48  HOH   HOH A . 
J 5 HOH   43  343 19  HOH   HOH A . 
J 5 HOH   44  344 26  HOH   HOH A . 
J 5 HOH   45  345 257 HOH   HOH A . 
J 5 HOH   46  346 72  HOH   HOH A . 
J 5 HOH   47  347 160 HOH   HOH A . 
J 5 HOH   48  348 79  HOH   HOH A . 
J 5 HOH   49  349 119 HOH   HOH A . 
J 5 HOH   50  350 21  HOH   HOH A . 
J 5 HOH   51  351 53  HOH   HOH A . 
J 5 HOH   52  352 40  HOH   HOH A . 
J 5 HOH   53  353 70  HOH   HOH A . 
J 5 HOH   54  354 33  HOH   HOH A . 
J 5 HOH   55  355 111 HOH   HOH A . 
J 5 HOH   56  356 140 HOH   HOH A . 
J 5 HOH   57  357 53  HOH   HOH A . 
J 5 HOH   58  358 76  HOH   HOH A . 
J 5 HOH   59  359 85  HOH   HOH A . 
J 5 HOH   60  360 119 HOH   HOH A . 
J 5 HOH   61  361 236 HOH   HOH A . 
J 5 HOH   62  362 18  HOH   HOH A . 
J 5 HOH   63  363 115 HOH   HOH A . 
J 5 HOH   64  364 153 HOH   HOH A . 
J 5 HOH   65  365 71  HOH   HOH A . 
J 5 HOH   66  366 128 HOH   HOH A . 
J 5 HOH   67  367 149 HOH   HOH A . 
J 5 HOH   68  368 35  HOH   HOH A . 
J 5 HOH   69  369 249 HOH   HOH A . 
J 5 HOH   70  370 115 HOH   HOH A . 
J 5 HOH   71  371 230 HOH   HOH A . 
J 5 HOH   72  372 73  HOH   HOH A . 
J 5 HOH   73  373 29  HOH   HOH A . 
J 5 HOH   74  374 19  HOH   HOH A . 
J 5 HOH   75  375 75  HOH   HOH A . 
J 5 HOH   76  376 234 HOH   HOH A . 
J 5 HOH   77  377 66  HOH   HOH A . 
J 5 HOH   78  378 243 HOH   HOH A . 
J 5 HOH   79  379 12  HOH   HOH A . 
J 5 HOH   80  380 47  HOH   HOH A . 
J 5 HOH   81  381 52  HOH   HOH A . 
J 5 HOH   82  382 125 HOH   HOH A . 
J 5 HOH   83  383 56  HOH   HOH A . 
J 5 HOH   84  384 259 HOH   HOH A . 
J 5 HOH   85  385 148 HOH   HOH A . 
J 5 HOH   86  386 171 HOH   HOH A . 
J 5 HOH   87  387 14  HOH   HOH A . 
J 5 HOH   88  388 63  HOH   HOH A . 
J 5 HOH   89  389 84  HOH   HOH A . 
J 5 HOH   90  390 91  HOH   HOH A . 
J 5 HOH   91  391 252 HOH   HOH A . 
J 5 HOH   92  392 163 HOH   HOH A . 
J 5 HOH   93  393 42  HOH   HOH A . 
J 5 HOH   94  394 96  HOH   HOH A . 
J 5 HOH   95  395 12  HOH   HOH A . 
J 5 HOH   96  396 38  HOH   HOH A . 
J 5 HOH   97  397 142 HOH   HOH A . 
J 5 HOH   98  398 23  HOH   HOH A . 
J 5 HOH   99  399 49  HOH   HOH A . 
J 5 HOH   100 400 114 HOH   HOH A . 
J 5 HOH   101 401 112 HOH   HOH A . 
J 5 HOH   102 402 197 HOH   HOH A . 
J 5 HOH   103 403 35  HOH   HOH A . 
J 5 HOH   104 404 106 HOH   HOH A . 
J 5 HOH   105 405 92  HOH   HOH A . 
J 5 HOH   106 406 26  HOH   HOH A . 
J 5 HOH   107 407 251 HOH   HOH A . 
J 5 HOH   108 408 208 HOH   HOH A . 
J 5 HOH   109 409 240 HOH   HOH A . 
J 5 HOH   110 410 62  HOH   HOH A . 
J 5 HOH   111 411 16  HOH   HOH A . 
J 5 HOH   112 412 101 HOH   HOH A . 
J 5 HOH   113 413 102 HOH   HOH A . 
J 5 HOH   114 414 245 HOH   HOH A . 
J 5 HOH   115 415 150 HOH   HOH A . 
J 5 HOH   116 416 77  HOH   HOH A . 
J 5 HOH   117 417 100 HOH   HOH A . 
J 5 HOH   118 418 202 HOH   HOH A . 
J 5 HOH   119 419 147 HOH   HOH A . 
J 5 HOH   120 420 15  HOH   HOH A . 
J 5 HOH   121 421 223 HOH   HOH A . 
J 5 HOH   122 422 114 HOH   HOH A . 
J 5 HOH   123 423 8   HOH   HOH A . 
J 5 HOH   124 424 66  HOH   HOH A . 
J 5 HOH   125 425 126 HOH   HOH A . 
J 5 HOH   126 426 163 HOH   HOH A . 
J 5 HOH   127 427 178 HOH   HOH A . 
J 5 HOH   128 428 127 HOH   HOH A . 
J 5 HOH   129 429 201 HOH   HOH A . 
J 5 HOH   130 430 154 HOH   HOH A . 
J 5 HOH   131 431 165 HOH   HOH A . 
J 5 HOH   132 432 136 HOH   HOH A . 
J 5 HOH   133 433 254 HOH   HOH A . 
J 5 HOH   134 434 150 HOH   HOH A . 
J 5 HOH   135 435 129 HOH   HOH A . 
J 5 HOH   136 436 154 HOH   HOH A . 
J 5 HOH   137 437 132 HOH   HOH A . 
J 5 HOH   138 438 82  HOH   HOH A . 
J 5 HOH   139 439 219 HOH   HOH A . 
J 5 HOH   140 440 221 HOH   HOH A . 
J 5 HOH   141 441 187 HOH   HOH A . 
J 5 HOH   142 442 193 HOH   HOH A . 
K 5 HOH   1   301 34  HOH   HOH C . 
K 5 HOH   2   302 253 HOH   HOH C . 
K 5 HOH   3   303 123 HOH   HOH C . 
K 5 HOH   4   304 237 HOH   HOH C . 
K 5 HOH   5   305 212 HOH   HOH C . 
K 5 HOH   6   306 106 HOH   HOH C . 
K 5 HOH   7   307 80  HOH   HOH C . 
K 5 HOH   8   308 28  HOH   HOH C . 
K 5 HOH   9   309 64  HOH   HOH C . 
K 5 HOH   10  310 78  HOH   HOH C . 
K 5 HOH   11  311 179 HOH   HOH C . 
K 5 HOH   12  312 120 HOH   HOH C . 
K 5 HOH   13  313 64  HOH   HOH C . 
K 5 HOH   14  314 2   HOH   HOH C . 
K 5 HOH   15  315 103 HOH   HOH C . 
K 5 HOH   16  316 155 HOH   HOH C . 
K 5 HOH   17  317 228 HOH   HOH C . 
K 5 HOH   18  318 33  HOH   HOH C . 
K 5 HOH   19  319 50  HOH   HOH C . 
K 5 HOH   20  320 32  HOH   HOH C . 
K 5 HOH   21  321 8   HOH   HOH C . 
K 5 HOH   22  322 81  HOH   HOH C . 
K 5 HOH   23  323 122 HOH   HOH C . 
K 5 HOH   24  324 43  HOH   HOH C . 
K 5 HOH   25  325 246 HOH   HOH C . 
K 5 HOH   26  326 78  HOH   HOH C . 
K 5 HOH   27  327 110 HOH   HOH C . 
K 5 HOH   28  328 51  HOH   HOH C . 
K 5 HOH   29  329 124 HOH   HOH C . 
K 5 HOH   30  330 155 HOH   HOH C . 
K 5 HOH   31  331 65  HOH   HOH C . 
K 5 HOH   32  332 74  HOH   HOH C . 
K 5 HOH   33  333 111 HOH   HOH C . 
K 5 HOH   34  334 98  HOH   HOH C . 
K 5 HOH   35  335 69  HOH   HOH C . 
K 5 HOH   36  336 98  HOH   HOH C . 
K 5 HOH   37  337 31  HOH   HOH C . 
K 5 HOH   38  338 39  HOH   HOH C . 
K 5 HOH   39  339 133 HOH   HOH C . 
K 5 HOH   40  340 51  HOH   HOH C . 
K 5 HOH   41  341 73  HOH   HOH C . 
K 5 HOH   42  342 89  HOH   HOH C . 
K 5 HOH   43  343 20  HOH   HOH C . 
K 5 HOH   44  344 91  HOH   HOH C . 
K 5 HOH   45  345 30  HOH   HOH C . 
K 5 HOH   46  346 107 HOH   HOH C . 
K 5 HOH   47  347 67  HOH   HOH C . 
K 5 HOH   48  348 43  HOH   HOH C . 
K 5 HOH   49  349 90  HOH   HOH C . 
K 5 HOH   50  350 204 HOH   HOH C . 
K 5 HOH   51  351 126 HOH   HOH C . 
K 5 HOH   52  352 80  HOH   HOH C . 
K 5 HOH   53  353 144 HOH   HOH C . 
K 5 HOH   54  354 97  HOH   HOH C . 
K 5 HOH   55  355 38  HOH   HOH C . 
K 5 HOH   56  356 4   HOH   HOH C . 
K 5 HOH   57  357 242 HOH   HOH C . 
K 5 HOH   58  358 248 HOH   HOH C . 
K 5 HOH   59  359 231 HOH   HOH C . 
K 5 HOH   60  360 79  HOH   HOH C . 
K 5 HOH   61  361 83  HOH   HOH C . 
K 5 HOH   62  362 37  HOH   HOH C . 
K 5 HOH   63  363 130 HOH   HOH C . 
K 5 HOH   64  364 16  HOH   HOH C . 
K 5 HOH   65  365 255 HOH   HOH C . 
K 5 HOH   66  366 6   HOH   HOH C . 
K 5 HOH   67  367 87  HOH   HOH C . 
K 5 HOH   68  368 164 HOH   HOH C . 
K 5 HOH   69  369 70  HOH   HOH C . 
K 5 HOH   70  370 54  HOH   HOH C . 
K 5 HOH   71  371 191 HOH   HOH C . 
K 5 HOH   72  372 97  HOH   HOH C . 
K 5 HOH   73  373 244 HOH   HOH C . 
K 5 HOH   74  374 83  HOH   HOH C . 
K 5 HOH   75  375 7   HOH   HOH C . 
K 5 HOH   76  376 29  HOH   HOH C . 
K 5 HOH   77  377 1   HOH   HOH C . 
K 5 HOH   78  378 71  HOH   HOH C . 
K 5 HOH   79  379 167 HOH   HOH C . 
K 5 HOH   80  380 229 HOH   HOH C . 
K 5 HOH   81  381 48  HOH   HOH C . 
K 5 HOH   82  382 44  HOH   HOH C . 
K 5 HOH   83  383 105 HOH   HOH C . 
K 5 HOH   84  384 86  HOH   HOH C . 
K 5 HOH   85  385 62  HOH   HOH C . 
K 5 HOH   86  386 44  HOH   HOH C . 
K 5 HOH   87  387 31  HOH   HOH C . 
K 5 HOH   88  388 124 HOH   HOH C . 
K 5 HOH   89  389 144 HOH   HOH C . 
K 5 HOH   90  390 233 HOH   HOH C . 
K 5 HOH   91  391 89  HOH   HOH C . 
K 5 HOH   92  392 57  HOH   HOH C . 
K 5 HOH   93  393 205 HOH   HOH C . 
K 5 HOH   94  394 158 HOH   HOH C . 
K 5 HOH   95  395 11  HOH   HOH C . 
K 5 HOH   96  396 13  HOH   HOH C . 
K 5 HOH   97  397 127 HOH   HOH C . 
K 5 HOH   98  398 68  HOH   HOH C . 
K 5 HOH   99  399 138 HOH   HOH C . 
K 5 HOH   100 400 3   HOH   HOH C . 
K 5 HOH   101 401 52  HOH   HOH C . 
K 5 HOH   102 402 11  HOH   HOH C . 
K 5 HOH   103 403 85  HOH   HOH C . 
K 5 HOH   104 404 41  HOH   HOH C . 
K 5 HOH   105 405 90  HOH   HOH C . 
K 5 HOH   106 406 50  HOH   HOH C . 
K 5 HOH   107 407 120 HOH   HOH C . 
K 5 HOH   108 408 140 HOH   HOH C . 
K 5 HOH   109 409 238 HOH   HOH C . 
K 5 HOH   110 410 145 HOH   HOH C . 
K 5 HOH   111 411 54  HOH   HOH C . 
K 5 HOH   112 412 148 HOH   HOH C . 
K 5 HOH   113 413 159 HOH   HOH C . 
K 5 HOH   114 414 146 HOH   HOH C . 
K 5 HOH   115 415 105 HOH   HOH C . 
K 5 HOH   116 416 151 HOH   HOH C . 
K 5 HOH   117 417 45  HOH   HOH C . 
K 5 HOH   118 418 117 HOH   HOH C . 
K 5 HOH   119 419 47  HOH   HOH C . 
K 5 HOH   120 420 210 HOH   HOH C . 
K 5 HOH   121 421 239 HOH   HOH C . 
K 5 HOH   122 422 200 HOH   HOH C . 
K 5 HOH   123 423 134 HOH   HOH C . 
K 5 HOH   124 424 143 HOH   HOH C . 
K 5 HOH   125 425 87  HOH   HOH C . 
K 5 HOH   126 426 95  HOH   HOH C . 
K 5 HOH   127 427 198 HOH   HOH C . 
K 5 HOH   128 428 17  HOH   HOH C . 
K 5 HOH   129 429 258 HOH   HOH C . 
K 5 HOH   130 430 137 HOH   HOH C . 
K 5 HOH   131 431 139 HOH   HOH C . 
K 5 HOH   132 432 109 HOH   HOH C . 
K 5 HOH   133 433 104 HOH   HOH C . 
K 5 HOH   134 434 146 HOH   HOH C . 
K 5 HOH   135 435 216 HOH   HOH C . 
K 5 HOH   136 436 185 HOH   HOH C . 
K 5 HOH   137 437 93  HOH   HOH C . 
K 5 HOH   138 438 138 HOH   HOH C . 
K 5 HOH   139 439 135 HOH   HOH C . 
K 5 HOH   140 440 199 HOH   HOH C . 
K 5 HOH   141 441 25  HOH   HOH C . 
K 5 HOH   142 442 123 HOH   HOH C . 
K 5 HOH   143 443 116 HOH   HOH C . 
K 5 HOH   144 444 222 HOH   HOH C . 
K 5 HOH   145 445 142 HOH   HOH C . 
K 5 HOH   146 446 189 HOH   HOH C . 
K 5 HOH   147 447 166 HOH   HOH C . 
K 5 HOH   148 448 218 HOH   HOH C . 
K 5 HOH   149 449 157 HOH   HOH C . 
K 5 HOH   150 450 207 HOH   HOH C . 
K 5 HOH   151 451 141 HOH   HOH C . 
K 5 HOH   152 452 156 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           7I41 
_cell.length_a           72.668 
_cell.length_b           61.457 
_cell.length_c           65.276 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.97 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I41 
_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          7I41 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.29 
_exptl_crystal.density_percent_sol   46.28 
_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   2025-01-17 
_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   0.92201 
_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        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I41 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             38.69 
_reflns.d_resolution_high            1.64 
_reflns.number_obs                   34938 
_reflns.percent_possible_obs         99.1 
_reflns.pdbx_Rmerge_I_obs            0.112 
_reflns.pdbx_netI_over_sigmaI        3.9 
_reflns.pdbx_redundancy              3.3 
_reflns.pdbx_Rrim_I_all              0.132 
_reflns.pdbx_Rpim_I_all              0.069 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     115764 
_reflns.pdbx_chi_squared             0.57 
_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                  1.64 
_reflns_shell.d_res_low                   1.73 
_reflns_shell.number_measured_all         16945 
_reflns_shell.number_unique_obs           5061 
_reflns_shell.Rmerge_I_obs                1.223 
_reflns_shell.pdbx_chi_squared            0.65 
_reflns_shell.pdbx_redundancy             3.3 
_reflns_shell.percent_possible_obs        99.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.1 
_reflns_shell.pdbx_Rrim_I_all             1.447 
_reflns_shell.pdbx_Rpim_I_all             0.760 
_reflns_shell.pdbx_CC_half                0.415 
_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                                 7I41 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     34822 
_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                             38.69 
_refine.ls_d_res_high                            1.639 
_refine.ls_percent_reflns_obs                    98.6 
_refine.ls_R_factor_obs                          0.1887 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1873 
_refine.ls_R_factor_R_free                       0.2171 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.900 
_refine.ls_number_reflns_R_free                  1705 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.950 
_refine.B_iso_mean                               24.49 
_refine.aniso_B[1][1]                            -2.66210 
_refine.aniso_B[2][2]                            0.50860 
_refine.aniso_B[3][3]                            2.15350 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.87860 
_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             0.098 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.095 
_refine.pdbx_overall_SU_R_Blow_DPI               0.103 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.099 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I41 
_refine_analyze.Luzzati_coordinate_error_obs    0.21 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_refine_hist.number_atoms_solvent             294 
_refine_hist.number_atoms_total               2496 
_refine_hist.d_res_high                       1.639 
_refine_hist.d_res_low                        38.69 
# 
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                  0.010 ? 2.00  2261 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.94  ? 2.00  3077 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  750  '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  416  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2261 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.12  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.64 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  276  '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  1957 '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                       1.64 
_refine_ls_shell.d_res_low                        1.65 
_refine_ls_shell.number_reflns_R_work             666 
_refine_ls_shell.R_factor_R_work                  0.2917 
_refine_ls_shell.percent_reflns_obs               91.10 
_refine_ls_shell.R_factor_R_free                  0.2564 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.45 
_refine_ls_shell.number_reflns_R_free             31 
_refine_ls_shell.number_reflns_all                697 
_refine_ls_shell.R_factor_all                     0.2900 
# 
_struct.entry_id                  7I41 
_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-0036423-001 (A71EV2A-x4611)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I41 
_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 2 ? 
G N N 4 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
K 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 7I41 A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I41 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,J   
2 1 B,F,G,H,I,K 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.312 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 H ZN . ZN ? ? C CYS 56  C ZN 203 1_555 ? ? ? ? ? ? ? 2.346 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 H ZN . ZN ? ? C CYS 58  C ZN 203 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 H ZN . ZN ? ? C CYS 116 C ZN 203 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 H ZN . ZN ? ? C HIS 118 C ZN 203 1_555 ? ? ? ? ? ? ? 2.106 ? ? 
# 
_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_555 110.1 ? 
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_555 105.8 ? 
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_555 118.0 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 108.6 ? 
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_555 101.2 ? 
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_555 112.9 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 108.3 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.3 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 119.1 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 108.2 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 100.7 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 113.8 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 4   ? VAL A 6   ? ILE A 10  VAL A 12  
AA1 2 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 3 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 4 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 4   ? N ILE A 10  O VAL A 11  ? O VAL A 17  
AA1 2 3 N VAL A 12  ? N VAL A 18  O LEU A 35  ? O LEU A 41  
AA1 3 4 O VAL A 36  ? O VAL A 42  N TRP A 27  ? N TRP A 33  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7I41 
_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    334 
_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    399 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.15 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     360 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     305 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_555 
_pdbx_validate_symm_contact.dist              2.17 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 125 ? ? -132.75 -32.73 
2 1 SER C 125 ? ? -133.08 -33.96 
# 
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 19.6579 6.7248   18.2819 -0.0286 -0.0248 -0.0148 -0.0014 0.0076  -0.0003 0.9380 1.3310 0.7280 
-0.6704 -0.2326 0.2915 -0.0432 -0.0004 0.0432 0.0316 0.0542 0.0561  0.0294  0.0520  -0.0110 
'X-RAY DIFFRACTION' 2 ? refined 15.2789 -23.8694 14.1150 -0.0313 -0.0114 -0.0109 0.0009  -0.0076 -0.0046 0.7377 1.2074 0.4376 
0.3272  0.2635  0.0511 -0.0643 0.0184  0.0332 0.0225 0.0629 -0.0387 -0.0005 -0.0129 0.0014  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 146 ? A GLU 140 
2  1 Y 1 A ALA 147 ? A ALA 141 
3  1 Y 1 A MET 148 ? A MET 142 
4  1 Y 1 A GLU 149 ? A GLU 143 
5  1 Y 1 A GLN 150 ? A GLN 144 
6  1 Y 1 C GLU 146 ? B GLU 140 
7  1 Y 1 C ALA 147 ? B ALA 141 
8  1 Y 1 C MET 148 ? B MET 142 
9  1 Y 1 C GLU 149 ? B GLU 143 
10 1 Y 1 C GLN 150 ? B GLN 144 
# 
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 
A1B2E N1   N  N N 1   
A1B2E C4   C  N N 2   
A1B2E C5   C  N N 3   
A1B2E C6   C  Y N 4   
A1B2E C7   C  Y N 5   
A1B2E C8   C  Y N 6   
A1B2E C10  C  Y N 7   
A1B2E C13  C  N N 8   
A1B2E O1   O  N N 9   
A1B2E C3   C  N N 10  
A1B2E C2   C  N N 11  
A1B2E C1   C  N S 12  
A1B2E C    C  N N 13  
A1B2E O    O  N N 14  
A1B2E N    N  N N 15  
A1B2E C12  C  Y N 16  
A1B2E O2   O  Y N 17  
A1B2E N2   N  Y N 18  
A1B2E C11  C  Y N 19  
A1B2E C9   C  Y N 20  
A1B2E H8   H  N N 21  
A1B2E H7   H  N N 22  
A1B2E H9   H  N N 23  
A1B2E H11  H  N N 24  
A1B2E H14  H  N N 25  
A1B2E H13  H  N N 26  
A1B2E H6   H  N N 27  
A1B2E H5   H  N N 28  
A1B2E H4   H  N N 29  
A1B2E H3   H  N N 30  
A1B2E H    H  N N 31  
A1B2E H2   H  N N 32  
A1B2E H1   H  N N 33  
A1B2E H12  H  N N 34  
A1B2E H10  H  N N 35  
ALA   N    N  N N 36  
ALA   CA   C  N S 37  
ALA   C    C  N N 38  
ALA   O    O  N N 39  
ALA   CB   C  N N 40  
ALA   OXT  O  N N 41  
ALA   H    H  N N 42  
ALA   H2   H  N N 43  
ALA   HA   H  N N 44  
ALA   HB1  H  N N 45  
ALA   HB2  H  N N 46  
ALA   HB3  H  N N 47  
ALA   HXT  H  N N 48  
ARG   N    N  N N 49  
ARG   CA   C  N S 50  
ARG   C    C  N N 51  
ARG   O    O  N N 52  
ARG   CB   C  N N 53  
ARG   CG   C  N N 54  
ARG   CD   C  N N 55  
ARG   NE   N  N N 56  
ARG   CZ   C  N N 57  
ARG   NH1  N  N N 58  
ARG   NH2  N  N N 59  
ARG   OXT  O  N N 60  
ARG   H    H  N N 61  
ARG   H2   H  N N 62  
ARG   HA   H  N N 63  
ARG   HB2  H  N N 64  
ARG   HB3  H  N N 65  
ARG   HG2  H  N N 66  
ARG   HG3  H  N N 67  
ARG   HD2  H  N N 68  
ARG   HD3  H  N N 69  
ARG   HE   H  N N 70  
ARG   HH11 H  N N 71  
ARG   HH12 H  N N 72  
ARG   HH21 H  N N 73  
ARG   HH22 H  N N 74  
ARG   HXT  H  N N 75  
ASN   N    N  N N 76  
ASN   CA   C  N S 77  
ASN   C    C  N N 78  
ASN   O    O  N N 79  
ASN   CB   C  N N 80  
ASN   CG   C  N N 81  
ASN   OD1  O  N N 82  
ASN   ND2  N  N N 83  
ASN   OXT  O  N N 84  
ASN   H    H  N N 85  
ASN   H2   H  N N 86  
ASN   HA   H  N N 87  
ASN   HB2  H  N N 88  
ASN   HB3  H  N N 89  
ASN   HD21 H  N N 90  
ASN   HD22 H  N N 91  
ASN   HXT  H  N N 92  
ASP   N    N  N N 93  
ASP   CA   C  N S 94  
ASP   C    C  N N 95  
ASP   O    O  N N 96  
ASP   CB   C  N N 97  
ASP   CG   C  N N 98  
ASP   OD1  O  N N 99  
ASP   OD2  O  N N 100 
ASP   OXT  O  N N 101 
ASP   H    H  N N 102 
ASP   H2   H  N N 103 
ASP   HA   H  N N 104 
ASP   HB2  H  N N 105 
ASP   HB3  H  N N 106 
ASP   HD2  H  N N 107 
ASP   HXT  H  N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
DMS   S    S  N N 123 
DMS   O    O  N N 124 
DMS   C1   C  N N 125 
DMS   C2   C  N N 126 
DMS   H11  H  N N 127 
DMS   H12  H  N N 128 
DMS   H13  H  N N 129 
DMS   H21  H  N N 130 
DMS   H22  H  N N 131 
DMS   H23  H  N N 132 
GLN   N    N  N N 133 
GLN   CA   C  N S 134 
GLN   C    C  N N 135 
GLN   O    O  N N 136 
GLN   CB   C  N N 137 
GLN   CG   C  N N 138 
GLN   CD   C  N N 139 
GLN   OE1  O  N N 140 
GLN   NE2  N  N N 141 
GLN   OXT  O  N N 142 
GLN   H    H  N N 143 
GLN   H2   H  N N 144 
GLN   HA   H  N N 145 
GLN   HB2  H  N N 146 
GLN   HB3  H  N N 147 
GLN   HG2  H  N N 148 
GLN   HG3  H  N N 149 
GLN   HE21 H  N N 150 
GLN   HE22 H  N N 151 
GLN   HXT  H  N N 152 
GLU   N    N  N N 153 
GLU   CA   C  N S 154 
GLU   C    C  N N 155 
GLU   O    O  N N 156 
GLU   CB   C  N N 157 
GLU   CG   C  N N 158 
GLU   CD   C  N N 159 
GLU   OE1  O  N N 160 
GLU   OE2  O  N N 161 
GLU   OXT  O  N N 162 
GLU   H    H  N N 163 
GLU   H2   H  N N 164 
GLU   HA   H  N N 165 
GLU   HB2  H  N N 166 
GLU   HB3  H  N N 167 
GLU   HG2  H  N N 168 
GLU   HG3  H  N N 169 
GLU   HE2  H  N N 170 
GLU   HXT  H  N N 171 
GLY   N    N  N N 172 
GLY   CA   C  N N 173 
GLY   C    C  N N 174 
GLY   O    O  N N 175 
GLY   OXT  O  N N 176 
GLY   H    H  N N 177 
GLY   H2   H  N N 178 
GLY   HA2  H  N N 179 
GLY   HA3  H  N N 180 
GLY   HXT  H  N N 181 
HIS   N    N  N N 182 
HIS   CA   C  N S 183 
HIS   C    C  N N 184 
HIS   O    O  N N 185 
HIS   CB   C  N N 186 
HIS   CG   C  Y N 187 
HIS   ND1  N  Y N 188 
HIS   CD2  C  Y N 189 
HIS   CE1  C  Y N 190 
HIS   NE2  N  Y N 191 
HIS   OXT  O  N N 192 
HIS   H    H  N N 193 
HIS   H2   H  N N 194 
HIS   HA   H  N N 195 
HIS   HB2  H  N N 196 
HIS   HB3  H  N N 197 
HIS   HD1  H  N N 198 
HIS   HD2  H  N N 199 
HIS   HE1  H  N N 200 
HIS   HE2  H  N N 201 
HIS   HXT  H  N N 202 
HOH   O    O  N N 203 
HOH   H1   H  N N 204 
HOH   H2   H  N N 205 
ILE   N    N  N N 206 
ILE   CA   C  N S 207 
ILE   C    C  N N 208 
ILE   O    O  N N 209 
ILE   CB   C  N S 210 
ILE   CG1  C  N N 211 
ILE   CG2  C  N N 212 
ILE   CD1  C  N N 213 
ILE   OXT  O  N N 214 
ILE   H    H  N N 215 
ILE   H2   H  N N 216 
ILE   HA   H  N N 217 
ILE   HB   H  N N 218 
ILE   HG12 H  N N 219 
ILE   HG13 H  N N 220 
ILE   HG21 H  N N 221 
ILE   HG22 H  N N 222 
ILE   HG23 H  N N 223 
ILE   HD11 H  N N 224 
ILE   HD12 H  N N 225 
ILE   HD13 H  N N 226 
ILE   HXT  H  N N 227 
LEU   N    N  N N 228 
LEU   CA   C  N S 229 
LEU   C    C  N N 230 
LEU   O    O  N N 231 
LEU   CB   C  N N 232 
LEU   CG   C  N N 233 
LEU   CD1  C  N N 234 
LEU   CD2  C  N N 235 
LEU   OXT  O  N N 236 
LEU   H    H  N N 237 
LEU   H2   H  N N 238 
LEU   HA   H  N N 239 
LEU   HB2  H  N N 240 
LEU   HB3  H  N N 241 
LEU   HG   H  N N 242 
LEU   HD11 H  N N 243 
LEU   HD12 H  N N 244 
LEU   HD13 H  N N 245 
LEU   HD21 H  N N 246 
LEU   HD22 H  N N 247 
LEU   HD23 H  N N 248 
LEU   HXT  H  N N 249 
LYS   N    N  N N 250 
LYS   CA   C  N S 251 
LYS   C    C  N N 252 
LYS   O    O  N N 253 
LYS   CB   C  N N 254 
LYS   CG   C  N N 255 
LYS   CD   C  N N 256 
LYS   CE   C  N N 257 
LYS   NZ   N  N N 258 
LYS   OXT  O  N N 259 
LYS   H    H  N N 260 
LYS   H2   H  N N 261 
LYS   HA   H  N N 262 
LYS   HB2  H  N N 263 
LYS   HB3  H  N N 264 
LYS   HG2  H  N N 265 
LYS   HG3  H  N N 266 
LYS   HD2  H  N N 267 
LYS   HD3  H  N N 268 
LYS   HE2  H  N N 269 
LYS   HE3  H  N N 270 
LYS   HZ1  H  N N 271 
LYS   HZ2  H  N N 272 
LYS   HZ3  H  N N 273 
LYS   HXT  H  N N 274 
MET   N    N  N N 275 
MET   CA   C  N S 276 
MET   C    C  N N 277 
MET   O    O  N N 278 
MET   CB   C  N N 279 
MET   CG   C  N N 280 
MET   SD   S  N N 281 
MET   CE   C  N N 282 
MET   OXT  O  N N 283 
MET   H    H  N N 284 
MET   H2   H  N N 285 
MET   HA   H  N N 286 
MET   HB2  H  N N 287 
MET   HB3  H  N N 288 
MET   HG2  H  N N 289 
MET   HG3  H  N N 290 
MET   HE1  H  N N 291 
MET   HE2  H  N N 292 
MET   HE3  H  N N 293 
MET   HXT  H  N N 294 
PHE   N    N  N N 295 
PHE   CA   C  N S 296 
PHE   C    C  N N 297 
PHE   O    O  N N 298 
PHE   CB   C  N N 299 
PHE   CG   C  Y N 300 
PHE   CD1  C  Y N 301 
PHE   CD2  C  Y N 302 
PHE   CE1  C  Y N 303 
PHE   CE2  C  Y N 304 
PHE   CZ   C  Y N 305 
PHE   OXT  O  N N 306 
PHE   H    H  N N 307 
PHE   H2   H  N N 308 
PHE   HA   H  N N 309 
PHE   HB2  H  N N 310 
PHE   HB3  H  N N 311 
PHE   HD1  H  N N 312 
PHE   HD2  H  N N 313 
PHE   HE1  H  N N 314 
PHE   HE2  H  N N 315 
PHE   HZ   H  N N 316 
PHE   HXT  H  N N 317 
PRO   N    N  N N 318 
PRO   CA   C  N S 319 
PRO   C    C  N N 320 
PRO   O    O  N N 321 
PRO   CB   C  N N 322 
PRO   CG   C  N N 323 
PRO   CD   C  N N 324 
PRO   OXT  O  N N 325 
PRO   H    H  N N 326 
PRO   HA   H  N N 327 
PRO   HB2  H  N N 328 
PRO   HB3  H  N N 329 
PRO   HG2  H  N N 330 
PRO   HG3  H  N N 331 
PRO   HD2  H  N N 332 
PRO   HD3  H  N N 333 
PRO   HXT  H  N N 334 
SER   N    N  N N 335 
SER   CA   C  N S 336 
SER   C    C  N N 337 
SER   O    O  N N 338 
SER   CB   C  N N 339 
SER   OG   O  N N 340 
SER   OXT  O  N N 341 
SER   H    H  N N 342 
SER   H2   H  N N 343 
SER   HA   H  N N 344 
SER   HB2  H  N N 345 
SER   HB3  H  N N 346 
SER   HG   H  N N 347 
SER   HXT  H  N N 348 
THR   N    N  N N 349 
THR   CA   C  N S 350 
THR   C    C  N N 351 
THR   O    O  N N 352 
THR   CB   C  N R 353 
THR   OG1  O  N N 354 
THR   CG2  C  N N 355 
THR   OXT  O  N N 356 
THR   H    H  N N 357 
THR   H2   H  N N 358 
THR   HA   H  N N 359 
THR   HB   H  N N 360 
THR   HG1  H  N N 361 
THR   HG21 H  N N 362 
THR   HG22 H  N N 363 
THR   HG23 H  N N 364 
THR   HXT  H  N N 365 
TRP   N    N  N N 366 
TRP   CA   C  N S 367 
TRP   C    C  N N 368 
TRP   O    O  N N 369 
TRP   CB   C  N N 370 
TRP   CG   C  Y N 371 
TRP   CD1  C  Y N 372 
TRP   CD2  C  Y N 373 
TRP   NE1  N  Y N 374 
TRP   CE2  C  Y N 375 
TRP   CE3  C  Y N 376 
TRP   CZ2  C  Y N 377 
TRP   CZ3  C  Y N 378 
TRP   CH2  C  Y N 379 
TRP   OXT  O  N N 380 
TRP   H    H  N N 381 
TRP   H2   H  N N 382 
TRP   HA   H  N N 383 
TRP   HB2  H  N N 384 
TRP   HB3  H  N N 385 
TRP   HD1  H  N N 386 
TRP   HE1  H  N N 387 
TRP   HE3  H  N N 388 
TRP   HZ2  H  N N 389 
TRP   HZ3  H  N N 390 
TRP   HH2  H  N N 391 
TRP   HXT  H  N N 392 
TYR   N    N  N N 393 
TYR   CA   C  N S 394 
TYR   C    C  N N 395 
TYR   O    O  N N 396 
TYR   CB   C  N N 397 
TYR   CG   C  Y N 398 
TYR   CD1  C  Y N 399 
TYR   CD2  C  Y N 400 
TYR   CE1  C  Y N 401 
TYR   CE2  C  Y N 402 
TYR   CZ   C  Y N 403 
TYR   OH   O  N N 404 
TYR   OXT  O  N N 405 
TYR   H    H  N N 406 
TYR   H2   H  N N 407 
TYR   HA   H  N N 408 
TYR   HB2  H  N N 409 
TYR   HB3  H  N N 410 
TYR   HD1  H  N N 411 
TYR   HD2  H  N N 412 
TYR   HE1  H  N N 413 
TYR   HE2  H  N N 414 
TYR   HH   H  N N 415 
TYR   HXT  H  N N 416 
VAL   N    N  N N 417 
VAL   CA   C  N S 418 
VAL   C    C  N N 419 
VAL   O    O  N N 420 
VAL   CB   C  N N 421 
VAL   CG1  C  N N 422 
VAL   CG2  C  N N 423 
VAL   OXT  O  N N 424 
VAL   H    H  N N 425 
VAL   H2   H  N N 426 
VAL   HA   H  N N 427 
VAL   HB   H  N N 428 
VAL   HG11 H  N N 429 
VAL   HG12 H  N N 430 
VAL   HG13 H  N N 431 
VAL   HG21 H  N N 432 
VAL   HG22 H  N N 433 
VAL   HG23 H  N N 434 
VAL   HXT  H  N N 435 
ZN    ZN   ZN N N 436 
# 
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 
A1B2E N   C    sing N N 1   
A1B2E O   C    doub N N 2   
A1B2E C   C1   sing N N 3   
A1B2E C1  C2   sing N N 4   
A1B2E C2  C3   sing N N 5   
A1B2E C3  C4   sing N N 6   
A1B2E C4  O1   doub N N 7   
A1B2E N1  C4   sing N N 8   
A1B2E C5  N1   sing N N 9   
A1B2E C6  C5   sing N N 10  
A1B2E C6  N2   doub Y N 11  
A1B2E N2  O2   sing Y N 12  
A1B2E O2  C7   sing Y N 13  
A1B2E C7  C8   doub Y N 14  
A1B2E C8  C9   sing Y N 15  
A1B2E C9  C10  doub Y N 16  
A1B2E C10 C11  sing Y N 17  
A1B2E C11 C12  doub Y N 18  
A1B2E C12 C6   sing Y N 19  
A1B2E C7  C12  sing Y N 20  
A1B2E C13 N1   sing N N 21  
A1B2E C1  C13  sing N N 22  
A1B2E C5  H8   sing N N 23  
A1B2E C5  H7   sing N N 24  
A1B2E C8  H9   sing N N 25  
A1B2E C10 H11  sing N N 26  
A1B2E C13 H14  sing N N 27  
A1B2E C13 H13  sing N N 28  
A1B2E C3  H6   sing N N 29  
A1B2E C3  H5   sing N N 30  
A1B2E C2  H4   sing N N 31  
A1B2E C2  H3   sing N N 32  
A1B2E C1  H    sing N N 33  
A1B2E N   H2   sing N N 34  
A1B2E N   H1   sing N N 35  
A1B2E C11 H12  sing N N 36  
A1B2E C9  H10  sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
DMS   S   O    doub N N 120 
DMS   S   C1   sing N N 121 
DMS   S   C2   sing N N 122 
DMS   C1  H11  sing N N 123 
DMS   C1  H12  sing N N 124 
DMS   C1  H13  sing N N 125 
DMS   C2  H21  sing N N 126 
DMS   C2  H22  sing N N 127 
DMS   C2  H23  sing N N 128 
GLN   N   CA   sing N N 129 
GLN   N   H    sing N N 130 
GLN   N   H2   sing N N 131 
GLN   CA  C    sing N N 132 
GLN   CA  CB   sing N N 133 
GLN   CA  HA   sing N N 134 
GLN   C   O    doub N N 135 
GLN   C   OXT  sing N N 136 
GLN   CB  CG   sing N N 137 
GLN   CB  HB2  sing N N 138 
GLN   CB  HB3  sing N N 139 
GLN   CG  CD   sing N N 140 
GLN   CG  HG2  sing N N 141 
GLN   CG  HG3  sing N N 142 
GLN   CD  OE1  doub N N 143 
GLN   CD  NE2  sing N N 144 
GLN   NE2 HE21 sing N N 145 
GLN   NE2 HE22 sing N N 146 
GLN   OXT HXT  sing N N 147 
GLU   N   CA   sing N N 148 
GLU   N   H    sing N N 149 
GLU   N   H2   sing N N 150 
GLU   CA  C    sing N N 151 
GLU   CA  CB   sing N N 152 
GLU   CA  HA   sing N N 153 
GLU   C   O    doub N N 154 
GLU   C   OXT  sing N N 155 
GLU   CB  CG   sing N N 156 
GLU   CB  HB2  sing N N 157 
GLU   CB  HB3  sing N N 158 
GLU   CG  CD   sing N N 159 
GLU   CG  HG2  sing N N 160 
GLU   CG  HG3  sing N N 161 
GLU   CD  OE1  doub N N 162 
GLU   CD  OE2  sing N N 163 
GLU   OE2 HE2  sing N N 164 
GLU   OXT HXT  sing N N 165 
GLY   N   CA   sing N N 166 
GLY   N   H    sing N N 167 
GLY   N   H2   sing N N 168 
GLY   CA  C    sing N N 169 
GLY   CA  HA2  sing N N 170 
GLY   CA  HA3  sing N N 171 
GLY   C   O    doub N N 172 
GLY   C   OXT  sing N N 173 
GLY   OXT HXT  sing N N 174 
HIS   N   CA   sing N N 175 
HIS   N   H    sing N N 176 
HIS   N   H2   sing N N 177 
HIS   CA  C    sing N N 178 
HIS   CA  CB   sing N N 179 
HIS   CA  HA   sing N N 180 
HIS   C   O    doub N N 181 
HIS   C   OXT  sing N N 182 
HIS   CB  CG   sing N N 183 
HIS   CB  HB2  sing N N 184 
HIS   CB  HB3  sing N N 185 
HIS   CG  ND1  sing Y N 186 
HIS   CG  CD2  doub Y N 187 
HIS   ND1 CE1  doub Y N 188 
HIS   ND1 HD1  sing N N 189 
HIS   CD2 NE2  sing Y N 190 
HIS   CD2 HD2  sing N N 191 
HIS   CE1 NE2  sing Y N 192 
HIS   CE1 HE1  sing N N 193 
HIS   NE2 HE2  sing N N 194 
HIS   OXT HXT  sing N N 195 
HOH   O   H1   sing N N 196 
HOH   O   H2   sing N N 197 
ILE   N   CA   sing N N 198 
ILE   N   H    sing N N 199 
ILE   N   H2   sing N N 200 
ILE   CA  C    sing N N 201 
ILE   CA  CB   sing N N 202 
ILE   CA  HA   sing N N 203 
ILE   C   O    doub N N 204 
ILE   C   OXT  sing N N 205 
ILE   CB  CG1  sing N N 206 
ILE   CB  CG2  sing N N 207 
ILE   CB  HB   sing N N 208 
ILE   CG1 CD1  sing N N 209 
ILE   CG1 HG12 sing N N 210 
ILE   CG1 HG13 sing N N 211 
ILE   CG2 HG21 sing N N 212 
ILE   CG2 HG22 sing N N 213 
ILE   CG2 HG23 sing N N 214 
ILE   CD1 HD11 sing N N 215 
ILE   CD1 HD12 sing N N 216 
ILE   CD1 HD13 sing N N 217 
ILE   OXT HXT  sing N N 218 
LEU   N   CA   sing N N 219 
LEU   N   H    sing N N 220 
LEU   N   H2   sing N N 221 
LEU   CA  C    sing N N 222 
LEU   CA  CB   sing N N 223 
LEU   CA  HA   sing N N 224 
LEU   C   O    doub N N 225 
LEU   C   OXT  sing N N 226 
LEU   CB  CG   sing N N 227 
LEU   CB  HB2  sing N N 228 
LEU   CB  HB3  sing N N 229 
LEU   CG  CD1  sing N N 230 
LEU   CG  CD2  sing N N 231 
LEU   CG  HG   sing N N 232 
LEU   CD1 HD11 sing N N 233 
LEU   CD1 HD12 sing N N 234 
LEU   CD1 HD13 sing N N 235 
LEU   CD2 HD21 sing N N 236 
LEU   CD2 HD22 sing N N 237 
LEU   CD2 HD23 sing N N 238 
LEU   OXT HXT  sing N N 239 
LYS   N   CA   sing N N 240 
LYS   N   H    sing N N 241 
LYS   N   H2   sing N N 242 
LYS   CA  C    sing N N 243 
LYS   CA  CB   sing N N 244 
LYS   CA  HA   sing N N 245 
LYS   C   O    doub N N 246 
LYS   C   OXT  sing N N 247 
LYS   CB  CG   sing N N 248 
LYS   CB  HB2  sing N N 249 
LYS   CB  HB3  sing N N 250 
LYS   CG  CD   sing N N 251 
LYS   CG  HG2  sing N N 252 
LYS   CG  HG3  sing N N 253 
LYS   CD  CE   sing N N 254 
LYS   CD  HD2  sing N N 255 
LYS   CD  HD3  sing N N 256 
LYS   CE  NZ   sing N N 257 
LYS   CE  HE2  sing N N 258 
LYS   CE  HE3  sing N N 259 
LYS   NZ  HZ1  sing N N 260 
LYS   NZ  HZ2  sing N N 261 
LYS   NZ  HZ3  sing N N 262 
LYS   OXT HXT  sing N N 263 
MET   N   CA   sing N N 264 
MET   N   H    sing N N 265 
MET   N   H2   sing N N 266 
MET   CA  C    sing N N 267 
MET   CA  CB   sing N N 268 
MET   CA  HA   sing N N 269 
MET   C   O    doub N N 270 
MET   C   OXT  sing N N 271 
MET   CB  CG   sing N N 272 
MET   CB  HB2  sing N N 273 
MET   CB  HB3  sing N N 274 
MET   CG  SD   sing N N 275 
MET   CG  HG2  sing N N 276 
MET   CG  HG3  sing N N 277 
MET   SD  CE   sing N N 278 
MET   CE  HE1  sing N N 279 
MET   CE  HE2  sing N N 280 
MET   CE  HE3  sing N N 281 
MET   OXT HXT  sing N N 282 
PHE   N   CA   sing N N 283 
PHE   N   H    sing N N 284 
PHE   N   H2   sing N N 285 
PHE   CA  C    sing N N 286 
PHE   CA  CB   sing N N 287 
PHE   CA  HA   sing N N 288 
PHE   C   O    doub N N 289 
PHE   C   OXT  sing N N 290 
PHE   CB  CG   sing N N 291 
PHE   CB  HB2  sing N N 292 
PHE   CB  HB3  sing N N 293 
PHE   CG  CD1  doub Y N 294 
PHE   CG  CD2  sing Y N 295 
PHE   CD1 CE1  sing Y N 296 
PHE   CD1 HD1  sing N N 297 
PHE   CD2 CE2  doub Y N 298 
PHE   CD2 HD2  sing N N 299 
PHE   CE1 CZ   doub Y N 300 
PHE   CE1 HE1  sing N N 301 
PHE   CE2 CZ   sing Y N 302 
PHE   CE2 HE2  sing N N 303 
PHE   CZ  HZ   sing N N 304 
PHE   OXT HXT  sing N N 305 
PRO   N   CA   sing N N 306 
PRO   N   CD   sing N N 307 
PRO   N   H    sing N N 308 
PRO   CA  C    sing N N 309 
PRO   CA  CB   sing N N 310 
PRO   CA  HA   sing N N 311 
PRO   C   O    doub N N 312 
PRO   C   OXT  sing N N 313 
PRO   CB  CG   sing N N 314 
PRO   CB  HB2  sing N N 315 
PRO   CB  HB3  sing N N 316 
PRO   CG  CD   sing N N 317 
PRO   CG  HG2  sing N N 318 
PRO   CG  HG3  sing N N 319 
PRO   CD  HD2  sing N N 320 
PRO   CD  HD3  sing N N 321 
PRO   OXT HXT  sing N N 322 
SER   N   CA   sing N N 323 
SER   N   H    sing N N 324 
SER   N   H2   sing N N 325 
SER   CA  C    sing N N 326 
SER   CA  CB   sing N N 327 
SER   CA  HA   sing N N 328 
SER   C   O    doub N N 329 
SER   C   OXT  sing N N 330 
SER   CB  OG   sing N N 331 
SER   CB  HB2  sing N N 332 
SER   CB  HB3  sing N N 333 
SER   OG  HG   sing N N 334 
SER   OXT HXT  sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TRP   N   CA   sing N N 352 
TRP   N   H    sing N N 353 
TRP   N   H2   sing N N 354 
TRP   CA  C    sing N N 355 
TRP   CA  CB   sing N N 356 
TRP   CA  HA   sing N N 357 
TRP   C   O    doub N N 358 
TRP   C   OXT  sing N N 359 
TRP   CB  CG   sing N N 360 
TRP   CB  HB2  sing N N 361 
TRP   CB  HB3  sing N N 362 
TRP   CG  CD1  doub Y N 363 
TRP   CG  CD2  sing Y N 364 
TRP   CD1 NE1  sing Y N 365 
TRP   CD1 HD1  sing N N 366 
TRP   CD2 CE2  doub Y N 367 
TRP   CD2 CE3  sing Y N 368 
TRP   NE1 CE2  sing Y N 369 
TRP   NE1 HE1  sing N N 370 
TRP   CE2 CZ2  sing Y N 371 
TRP   CE3 CZ3  doub Y N 372 
TRP   CE3 HE3  sing N N 373 
TRP   CZ2 CH2  doub Y N 374 
TRP   CZ2 HZ2  sing N N 375 
TRP   CZ3 CH2  sing Y N 376 
TRP   CZ3 HZ3  sing N N 377 
TRP   CH2 HH2  sing N N 378 
TRP   OXT HXT  sing N N 379 
TYR   N   CA   sing N N 380 
TYR   N   H    sing N N 381 
TYR   N   H2   sing N N 382 
TYR   CA  C    sing N N 383 
TYR   CA  CB   sing N N 384 
TYR   CA  HA   sing N N 385 
TYR   C   O    doub N N 386 
TYR   C   OXT  sing N N 387 
TYR   CB  CG   sing N N 388 
TYR   CB  HB2  sing N N 389 
TYR   CB  HB3  sing N N 390 
TYR   CG  CD1  doub Y N 391 
TYR   CG  CD2  sing Y N 392 
TYR   CD1 CE1  sing Y N 393 
TYR   CD1 HD1  sing N N 394 
TYR   CD2 CE2  doub Y N 395 
TYR   CD2 HD2  sing N N 396 
TYR   CE1 CZ   doub Y N 397 
TYR   CE1 HE1  sing N N 398 
TYR   CE2 CZ   sing Y N 399 
TYR   CE2 HE2  sing N N 400 
TYR   CZ  OH   sing N N 401 
TYR   OH  HH   sing N N 402 
TYR   OXT HXT  sing N N 403 
VAL   N   CA   sing N N 404 
VAL   N   H    sing N N 405 
VAL   N   H2   sing N N 406 
VAL   CA  C    sing N N 407 
VAL   CA  CB   sing N N 408 
VAL   CA  HA   sing N N 409 
VAL   C   O    doub N N 410 
VAL   C   OXT  sing N N 411 
VAL   CB  CG1  sing N N 412 
VAL   CB  CG2  sing N N 413 
VAL   CB  HB   sing N N 414 
VAL   CG1 HG11 sing N N 415 
VAL   CG1 HG12 sing N N 416 
VAL   CG1 HG13 sing N N 417 
VAL   CG2 HG21 sing N N 418 
VAL   CG2 HG22 sing N N 419 
VAL   CG2 HG23 sing N N 420 
VAL   OXT HXT  sing N N 421 
# 
_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                    7I41 
_atom_sites.fract_transf_matrix[1][1]   0.013761 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000714 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016272 
_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]   0.015340 
_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   ? 16.374 6.496   8.249  1.00 20.43 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 15.115 6.545   8.985  1.00 21.23 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 14.957 5.359   9.953  1.00 21.32 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 15.604 4.331   9.783  1.00 22.10 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 13.951 6.617   8.003  1.00 22.88 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 13.858 5.393   7.298  1.00 25.78 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 14.085 5.505   10.950 1.00 19.69 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 13.860 4.438   11.914 1.00 19.17 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 13.476 4.974   13.285 1.00 20.15 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 13.859 6.095   13.641 1.00 20.66 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 12.728 4.177   14.069 1.00 18.75 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 12.307 4.642   15.385 1.00 19.42 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 12.246 3.460   16.358 1.00 19.19 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 12.213 2.315   15.914 1.00 17.69 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 10.924 5.282   15.264 1.00 19.87 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 12.213 3.750   17.678 1.00 18.39 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 12.034 2.732   18.697 1.00 17.66 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 10.627 2.942   19.220 1.00 18.16 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 10.264 4.078   19.514 1.00 18.39 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 13.042 2.923   19.853 1.00 16.60 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 14.494 2.864   19.351 1.00 16.48 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 12.827 1.879   20.959 1.00 16.80 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 15.472 3.469   20.393 1.00 18.12 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 9.840  1.875   19.353 1.00 18.04 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 8.471  1.978   19.875 1.00 19.25 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 8.396  1.237   21.176 1.00 19.66 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 8.445  0.024   21.150 1.00 21.64 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 7.466  1.387   18.877 1.00 19.46 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 7.406  2.209   17.618 1.00 20.94 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 6.589  3.325   17.536 1.00 22.79 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 8.215  1.911   16.532 1.00 22.65 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 6.561  4.112   16.398 1.00 24.18 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 8.206  2.700   15.389 1.00 23.97 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 7.360  3.785   15.321 1.00 25.98 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 7.365  4.590   14.213 1.00 29.87 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 8.299  1.930   22.316 1.00 19.62 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 8.262  1.267   23.627 1.00 20.83 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 7.141  1.869   24.444 1.00 22.68 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 7.028  3.095   24.534 1.00 23.13 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 9.637  1.378   24.360 1.00 22.00 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 10.180 2.828   24.329 1.00 21.85 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 9.530  0.876   25.801 1.00 23.23 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 6.219  1.033   24.941 1.00 23.08 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 5.058  1.532   25.676 1.00 23.18 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 4.269  2.521   24.832 1.00 23.97 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 4.048  2.266   23.643 1.00 24.57 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 3.988  3.706   25.379 1.00 23.92 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 3.292  4.733   24.612 1.00 25.27 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 4.244  5.813   24.117 1.00 23.44 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 3.856  6.976   24.014 1.00 23.59 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 2.137  5.338   25.395 1.00 28.97 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 0.996  4.382   25.550 1.00 34.84 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 0.449  3.872   24.570 1.00 36.58 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 0.631  4.122   26.784 1.00 35.56 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 5.491  5.425   23.774 1.00 21.45 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 6.508  6.361   23.320 1.00 20.28 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 7.089  5.925   21.978 1.00 19.04 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 7.197  4.727   21.696 1.00 18.55 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 7.672  6.409   24.345 1.00 20.43 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 7.275  6.972   25.696 1.00 20.88 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 6.706  8.230   25.807 1.00 21.65 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 7.502  6.261   26.862 1.00 22.54 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 6.350  8.759   27.045 1.00 23.18 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 7.147  6.778   28.105 1.00 23.67 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 6.550  8.020   28.190 1.00 24.56 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 6.206  8.557   29.401 1.00 25.97 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 7.498  6.913   21.153 1.00 18.15 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 8.195  6.705   19.885 1.00 18.05 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 9.511  7.501   20.050 1.00 17.82 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 9.472  8.696   20.364 1.00 18.47 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 7.343  7.232   18.701 1.00 19.79 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 8.135  7.534   17.417 1.00 19.70 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 7.220  7.810   16.234 1.00 21.92 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 7.769  8.832   15.333 1.00 24.64 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 8.269  8.584   14.126 1.00 26.85 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 8.332  7.338   13.669 1.00 24.58 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 8.717  9.579   13.369 1.00 25.87 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 10.676 6.848   19.862 1.00 15.77 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 11.964 7.527   19.983 1.00 15.88 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 12.565 7.671   18.581 1.00 16.28 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 12.733 6.667   17.894 1.00 17.11 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 12.931 6.714   20.895 1.00 15.36 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 14.222 7.510   21.171 1.00 14.43 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 12.246 6.296   22.204 1.00 15.20 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 12.883 8.891   18.163 1.00 15.78 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 13.461 9.138   16.837 1.00 16.40 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 14.691 10.014  16.931 1.00 15.98 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 14.881 10.713  17.944 1.00 15.85 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 12.423 9.801   15.866 1.00 17.52 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 11.318 8.846   15.504 1.00 18.69 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 11.868 11.105  16.442 1.00 18.22 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 15.473 10.141  15.812 1.00 14.74 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 16.528 11.164  15.760 1.00 15.17 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 15.814 12.515  15.748 1.00 16.09 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 14.815 12.702  15.010 1.00 15.92 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.338 11.050  14.470 1.00 15.25 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 18.132 9.765   14.396 1.00 16.48 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.686 8.782   13.830 1.00 17.10 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 19.337 9.759   14.951 1.00 16.75 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 16.259 13.443  16.587 1.00 15.83 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 15.617 14.755  16.660 1.00 15.75 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 15.594 15.467  15.288 1.00 15.72 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 14.556 16.032  14.916 1.00 16.80 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 16.284 15.630  17.717 1.00 16.42 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 15.502 16.915  18.046 1.00 17.13 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 16.419 17.792  18.866 1.00 18.48 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 15.789 19.023  19.357 1.00 19.97 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 15.804 20.182  18.712 1.00 20.25 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 16.281 20.258  17.476 1.00 19.21 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 15.302 21.271  19.283 1.00 19.91 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 16.677 15.336  14.502 1.00 14.44 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 16.750 15.993  13.192 1.00 15.72 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 15.803 15.392  12.150 1.00 17.78 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 15.578 16.012  11.105 1.00 19.40 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.204 16.078  12.656 1.00 16.48 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 18.787 14.770  12.182 1.00 17.85 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 19.324 13.849  13.066 1.00 18.18 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 18.945 14.308  10.916 1.00 18.82 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 19.774 12.851  12.311 1.00 18.31 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 19.533 13.073  11.014 1.00 19.37 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 15.239 14.197  12.423 1.00 17.01 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 14.286 13.552  11.521 1.00 17.46 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 12.862 13.568  12.075 1.00 18.17 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 11.975 13.006  11.435 1.00 18.29 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 14.708 12.102  11.205 1.00 18.09 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 16.117 11.934  10.605 1.00 18.40 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 16.430 10.441  10.351 1.00 19.29 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 16.259 12.715  9.309  1.00 19.68 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 12.611 14.206  13.261 1.00 17.61 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 11.255 14.227  13.829 1.00 17.67 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 10.265 14.886  12.870 1.00 18.99 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 10.613 15.849  12.206 1.00 18.67 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 11.266 14.972  15.152 1.00 17.90 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 9.044  14.374  12.797 1.00 20.41 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 8.030  14.914  11.896 1.00 22.34 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 7.211  16.035  12.572 1.00 23.53 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 7.364  16.280  13.767 1.00 22.50 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 7.081  13.745  11.476 1.00 24.66 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 6.363  13.277  12.628 1.00 25.77 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 7.810  12.611  10.790 1.00 25.85 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 6.263  16.673  11.828 1.00 24.94 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 5.336  17.643  12.423 1.00 26.64 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 4.521  16.941  13.540 1.00 24.14 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 4.284  17.527  14.603 1.00 24.59 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 4.355  18.198  11.344 1.00 30.68 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 4.992  19.054  10.294 1.00 38.84 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 5.713  20.185  10.632 1.00 42.56 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 4.959  18.940  8.940  1.00 41.58 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 6.119  20.708  9.483  1.00 43.68 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 5.687  19.995  8.434  1.00 43.72 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 4.130  15.670  13.308 1.00 23.00 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 3.369  14.890  14.285 1.00 23.19 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 4.161  14.570  15.545 1.00 21.74 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 3.617  14.663  16.641 1.00 22.42 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 2.781  13.622  13.691 1.00 25.45 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 1.472  13.869  13.000 1.00 32.03 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 0.575  14.556  13.522 1.00 34.19 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 1.341  13.351  11.798 1.00 32.91 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 5.462  14.267  15.412 1.00 19.82 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 6.311  14.051  16.596 1.00 19.27 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 6.349  15.319  17.464 1.00 18.94 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 6.233  15.217  18.682 1.00 19.45 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 7.748  13.715  16.173 1.00 18.68 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 7.883  12.318  15.626 1.00 22.29 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 7.290  11.394  16.223 1.00 22.32 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 8.621  12.142  14.610 1.00 22.46 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 6.527  16.502  16.839 1.00 18.38 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 6.589  17.754  17.598 1.00 19.41 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 5.245  18.118  18.234 1.00 22.00 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 5.209  18.735  19.296 1.00 23.03 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 7.102  18.918  16.704 1.00 19.31 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 8.607  18.932  16.577 1.00 19.66 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 9.350  18.488  15.530 1.00 20.82 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 9.538  19.401  17.560 1.00 19.17 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 10.700 18.639  15.805 1.00 20.65 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 10.836 19.211  17.040 1.00 19.76 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 9.398  19.989  18.816 1.00 19.80 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 11.982 19.574  17.744 1.00 20.13 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 10.540 20.376  19.496 1.00 20.12 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 11.810 20.128  18.978 1.00 19.55 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 4.142  17.773  17.575 1.00 22.90 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 2.804  18.048  18.117 1.00 23.64 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 2.446  17.124  19.318 1.00 24.39 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 1.481  17.390  20.055 1.00 25.41 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 1.774  17.879  17.028 1.00 23.81 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 3.145  15.996  19.446 1.00 22.57 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 2.926  15.056  20.540 1.00 22.38 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 4.230  14.915  21.364 1.00 22.08 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 4.530  13.841  21.882 1.00 21.94 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 2.482  13.718  19.970 1.00 23.01 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 1.102  13.775  19.342 1.00 26.80 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 0.090  13.801  20.049 1.00 27.98 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 1.039  13.814  18.016 1.00 27.69 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 5.000  15.998  21.476 1.00 20.91 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 6.306  15.995  22.140 1.00 20.99 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 6.243  15.617  23.619 1.00 21.11 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 5.399  16.156  24.357 1.00 22.42 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 6.916  17.404  22.008 1.00 21.02 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 8.286  17.601  22.674 1.00 22.13 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 9.340  16.731  21.980 1.00 21.50 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 8.701  19.085  22.645 1.00 23.07 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 7.142  14.715  24.055 1.00 19.75 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 7.307  14.334  25.455 1.00 20.58 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 8.634  14.925  25.966 1.00 21.56 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 8.687  15.566  27.028 1.00 22.23 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 7.284  12.782  25.632 1.00 21.47 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 7.697  12.389  27.045 1.00 21.76 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 5.895  12.223  25.306 1.00 22.37 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 9.697  14.759  25.181 1.00 21.03 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 11.027 15.235  25.573 1.00 20.88 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 11.921 15.319  24.348 1.00 19.70 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 11.819 14.480  23.455 1.00 19.34 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 11.640 14.239  26.581 1.00 20.61 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 13.105 14.427  26.916 1.00 20.54 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 13.641 15.251  27.859 1.00 21.49 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 14.207 13.714  26.335 1.00 20.16 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 15.018 15.137  27.861 1.00 21.77 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 15.383 14.165  26.968 1.00 20.63 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 14.303 12.672  25.406 1.00 20.42 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 16.639 13.626  26.680 1.00 20.57 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 15.555 12.181  25.084 1.00 20.87 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 16.704 12.665  25.712 1.00 20.62 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 12.794 16.313  24.302 1.00 18.79 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 13.796 16.395  23.216 1.00 18.51 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 15.116 16.944  23.754 1.00 17.37 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 15.118 17.716  24.722 1.00 17.88 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 13.270 17.173  21.988 1.00 20.25 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 12.718 18.568  22.302 1.00 22.02 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 13.738 19.673  22.536 1.00 23.57 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 13.439 20.593  23.335 1.00 25.70 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 14.845 19.614  21.958 1.00 21.90 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 16.240 16.568  23.134 1.00 15.94 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.547 17.081  23.571 1.00 16.63 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 18.420 17.209  22.324 1.00 17.57 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 18.872 16.203  21.787 1.00 17.58 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 18.157 16.154  24.629 1.00 18.02 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 19.422 16.690  25.283 1.00 26.16 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 20.152 17.471  24.626 1.00 26.96 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 19.688 16.325  26.439 1.00 26.40 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 18.627 18.446  21.848 1.00 17.79 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 19.426 18.732  20.661 0.50 18.87 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 19.424 18.701  20.650 0.50 18.77 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 20.872 18.238  20.849 1.00 19.34 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 21.487 17.727  19.902 1.00 20.01 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 19.384 20.233  20.359 0.50 20.53 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 19.371 20.183  20.276 0.50 20.19 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 20.288 20.595  19.330 0.50 22.69 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 20.014 20.964  21.269 0.50 21.89 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 21.409 18.343  22.088 1.00 19.19 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 22.779 17.874  22.340 1.00 20.72 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 22.916 16.330  22.187 1.00 19.84 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 24.014 15.848  21.993 1.00 21.31 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 23.278 18.335  23.706 1.00 22.86 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 22.842 17.475  24.746 1.00 26.84 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 21.815 15.574  22.267 1.00 17.99 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 21.871 14.107  22.106 1.00 17.13 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 21.331 13.627  20.736 1.00 16.87 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 21.381 12.425  20.432 1.00 16.46 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 21.042 13.419  23.219 1.00 17.92 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 21.569 13.646  24.627 1.00 19.36 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 20.709 12.988  25.710 1.00 20.32 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 20.668 11.518  25.603 1.00 21.19 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 20.498 10.695  26.634 1.00 21.38 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 20.351 11.184  27.871 1.00 20.00 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 20.507 9.377   26.450 1.00 18.79 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 20.734 14.559  19.949 1.00 17.42 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 20.040 14.283  18.701 1.00 16.59 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 18.854 13.336  18.945 1.00 15.89 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 18.609 12.464  18.118 1.00 15.46 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 20.978 13.762  17.594 1.00 16.15 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 20.270 13.471  16.272 1.00 18.09 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 19.426 14.295  15.862 1.00 16.77 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 20.552 12.391  15.658 1.00 18.14 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 18.137 13.476  20.078 1.00 15.61 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 16.988 12.615  20.367 1.00 15.44 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 15.699 13.400  20.564 1.00 16.52 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 15.685 14.469  21.169 1.00 15.73 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.184 11.761  21.642 1.00 15.48 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 18.179 10.616  21.597 1.00 16.34 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 18.225 9.940   22.969 1.00 16.69 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.821 9.622   20.477 1.00 16.37 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 14.588 12.774  20.174 1.00 16.54 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 13.254 13.310  20.423 1.00 16.50 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 12.347 12.121  20.751 1.00 17.04 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 12.451 11.055  20.118 1.00 17.65 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 12.718 14.091  19.209 1.00 16.56 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 11.341 14.735  19.416 1.00 17.64 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 11.268 16.098  18.721 1.00 18.75 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 10.235 13.861  18.853 1.00 17.32 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 11.467 12.289  21.742 1.00 17.05 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 10.503 11.261  22.126 1.00 16.57 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 9.116  11.884  22.016 1.00 17.14 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 8.888  12.991  22.529 1.00 17.44 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 10.741 10.716  23.557 1.00 18.03 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 9.630  9.725   23.957 1.00 18.24 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 12.123 10.070  23.673 1.00 17.49 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 8.209  11.199  21.327 1.00 17.75 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 6.810  11.635  21.166 1.00 18.87 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 5.852  10.538  21.717 1.00 22.03 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 6.242  9.371   21.880 1.00 21.50 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 6.503  11.960  19.703 1.00 20.21 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 6.644  10.827  18.850 1.00 21.43 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 4.597  10.913  22.022 1.00 22.98 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 3.624  9.959   22.551 1.00 23.95 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 2.848  9.275   21.439 1.00 25.32 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 2.604  9.863   20.384 1.00 25.25 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 2.661  10.655  23.509 1.00 24.61 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 2.070  11.758  22.850 1.00 25.93 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 2.456  8.020   21.679 1.00 25.78 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 1.680  7.248   20.723 1.00 27.54 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 0.386  6.774   21.395 1.00 30.27 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 0.335  6.658   22.621 1.00 30.88 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 2.479  6.012   20.247 1.00 27.90 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 2.631  5.124   21.347 1.00 29.31 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 3.862  6.359   19.693 1.00 26.64 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? -0.617 6.416   20.604 1.00 32.25 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? -1.856 5.856   21.140 1.00 34.48 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? -1.752 4.306   21.208 1.00 36.42 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? -2.352 3.680   22.089 1.00 37.83 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? -3.049 6.317   20.289 1.00 36.33 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? -2.782 5.979   18.930 1.00 38.29 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? -3.281 7.810   20.379 1.00 36.51 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? -0.990 3.691   20.292 1.00 36.12 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? -0.832 2.244   20.267 1.00 36.33 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 0.387  1.807   21.088 1.00 36.31 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 1.383  2.532   21.175 1.00 36.38 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? -0.689 1.767   18.827 1.00 36.33 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 0.309  0.612   21.676 1.00 35.64 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 1.377  0.027   22.489 1.00 36.27 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 2.550  -0.416  21.605 1.00 35.44 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 2.329  -1.118  20.618 1.00 35.39 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 0.826  -1.185  23.247 1.00 39.58 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 1.836  -1.833  24.178 1.00 46.29 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 2.012  -1.072  25.476 1.00 54.40 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 1.262  -0.134  25.812 1.00 55.78 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 3.016  -1.480  26.248 1.00 56.30 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 3.767  -0.023  21.967 1.00 34.18 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 4.972  -0.294  21.184 1.00 33.50 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 5.466  -1.723  21.137 1.00 33.26 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 5.220  -2.484  22.063 1.00 34.27 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 6.251  -2.058  20.087 1.00 30.89 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 6.771  -3.380  19.830 1.00 29.74 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 8.127  -3.699  20.509 1.00 28.75 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 8.431  -4.875  20.695 1.00 29.74 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 6.846  -3.605  18.319 1.00 30.84 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 7.989  -2.489  17.446 1.00 32.74 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 8.907  -2.685  20.910 1.00 27.14 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 10.272 -2.845  21.457 1.00 25.65 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 10.393 -2.838  22.990 1.00 25.32 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 9.490  -2.370  23.665 1.00 25.99 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 11.177 -1.714  20.886 1.00 25.52 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 11.348 -1.747  19.378 1.00 29.32 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 11.770 -2.813  18.854 1.00 29.12 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 11.082 -0.701  18.718 1.00 27.46 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 11.541 -3.324  23.533 1.00 24.33 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 11.916 -3.301  24.942 1.00 25.30 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 13.398 -2.747  25.039 1.00 24.33 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 14.195 -2.985  24.137 1.00 24.55 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 11.674 -4.667  25.634 1.00 28.82 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 12.653 -5.582  25.183 1.00 30.85 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 10.270 -5.252  25.371 1.00 29.57 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 13.739 -1.970  26.087 1.00 22.51 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 15.020 -1.252  26.188 1.00 21.12 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 16.024 -1.998  27.052 1.00 20.38 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 15.660 -2.479  28.131 1.00 21.26 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 14.777 0.187   26.782 1.00 21.66 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 13.648 0.953   26.052 1.00 23.34 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 16.048 1.039   26.785 1.00 21.62 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 13.950 1.136   24.488 1.00 24.32 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.278 -2.085  26.610 1.00 19.17 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 18.320 -2.705  27.417 1.00 18.97 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 18.643 -1.816  28.629 1.00 19.43 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 18.669 -0.600  28.509 1.00 19.79 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 19.579 -2.923  26.587 1.00 18.38 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 18.935 -2.440  29.786 1.00 19.31 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 19.367 -1.717  31.001 1.00 19.45 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 20.637 -2.471  31.413 1.00 21.20 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 20.594 -3.453  32.160 1.00 21.71 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 18.295 -1.781  32.106 1.00 20.32 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.956 -1.158  31.702 1.00 22.05 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.017 0.344   31.312 1.00 24.09 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 15.681 0.813   30.935 1.00 25.44 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 15.425 1.934   30.270 1.00 25.96 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 16.414 2.726   29.886 1.00 24.16 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 14.177 2.261   29.968 1.00 25.41 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 21.761 -2.103  30.797 1.00 21.69 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 23.000 -2.864  30.929 1.00 22.12 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 24.189 -1.962  30.593 1.00 22.70 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 24.010 -0.818  30.162 1.00 22.30 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 22.940 -4.035  29.939 1.00 22.70 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 22.941 -3.505  28.199 1.00 22.83 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 25.410 -2.537  30.677 1.00 23.77 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 26.614 -1.833  30.249 1.00 25.14 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 27.294 -2.561  29.084 1.00 25.16 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 28.516 -2.530  28.963 1.00 26.17 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 27.605 -1.630  31.413 1.00 28.39 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 28.131 -2.892  32.049 1.00 37.11 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 27.639 -3.996  31.696 1.00 35.70 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 29.043 -2.787  32.898 1.00 45.12 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 26.522 -3.241  28.231 1.00 24.22 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 27.080 -3.958  27.073 1.00 23.50 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 27.864 -2.995  26.184 1.00 22.54 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 27.453 -1.852  26.020 1.00 22.61 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 25.961 -4.636  26.279 1.00 23.49 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 25.339 -6.187  26.997 1.00 25.25 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 28.988 -3.440  25.621 1.00 20.71 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 29.764 -2.653  24.668 1.00 20.44 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 29.925 -3.412  23.330 1.00 20.11 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 30.826 -3.102  22.544 1.00 20.30 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 31.135 -2.258  25.238 1.00 22.26 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 31.120 -1.028  26.146 1.00 27.44 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 32.559 -0.661  26.478 1.00 32.76 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 33.051 -0.926  27.579 1.00 33.68 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 33.282 -0.088  25.512 1.00 31.15 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 29.091 -4.459  23.092 1.00 19.44 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 29.022 -5.195  21.829 1.00 19.52 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 27.510 -5.370  21.522 1.00 19.15 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 26.666 -5.487  22.435 1.00 19.65 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 29.738 -6.563  21.891 1.00 21.48 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 29.029 -7.396  22.788 1.00 23.33 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 31.200 -6.466  22.320 1.00 21.63 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 27.196 -5.458  20.257 1.00 17.44 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 25.810 -5.602  19.821 1.00 17.39 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 25.746 -5.700  18.307 1.00 16.67 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 26.775 -5.874  17.648 1.00 16.88 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 24.549 -5.587  17.748 1.00 16.79 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 24.320 -5.677  16.305 1.00 17.49 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 23.443 -4.485  15.885 1.00 16.89 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 22.451 -4.211  16.558 1.00 17.26 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 23.649 -7.037  15.976 1.00 19.50 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 23.298 -7.163  14.493 1.00 20.07 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 24.526 -8.204  16.408 1.00 19.86 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 23.778 -3.801  14.784 1.00 16.33 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 22.935 -2.694  14.300 1.00 15.54 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 22.427 -2.931  12.895 1.00 16.14 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 23.075 -3.628  12.106 1.00 16.15 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 23.662 -1.328  14.365 1.00 14.71 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 24.675 -1.087  13.264 1.00 14.83 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 25.956 -1.624  13.340 1.00 15.82 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 24.406 -0.203  12.219 1.00 15.74 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 26.919 -1.329  12.380 1.00 17.24 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 25.354 0.060   11.226 1.00 16.46 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 26.608 -0.505  11.315 1.00 17.89 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 27.563 -0.260  10.362 1.00 19.39 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 21.281 -2.297  12.545 1.00 15.88 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 20.783 -2.407  11.189 1.00 15.26 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 21.289 -1.222  10.351 1.00 14.92 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 21.140 -0.066  10.755 1.00 14.71 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 19.241 -2.422  11.172 1.00 15.52 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 18.720 -2.551  9.771  1.00 17.66 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 18.925 -3.710  9.041  1.00 17.86 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 18.054 -1.496  9.154  1.00 18.44 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 18.465 -3.828  7.736  1.00 19.32 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.589 -1.601  7.853  1.00 19.25 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.791 -2.771  7.155  1.00 20.83 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.360 -2.886  5.873  1.00 24.19 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 21.889 -1.534  9.187  1.00 14.99 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 22.443 -0.559  8.240  1.00 15.11 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 21.559 -0.541  6.970  1.00 16.10 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 21.692 -1.426  6.095  1.00 16.72 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 23.879 -0.949  7.896  1.00 15.46 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 24.666 0.148   6.686  1.00 17.91 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 20.641 0.422   6.864  1.00 17.02 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 19.734 0.470   5.717  1.00 18.26 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 20.439 0.684   4.366  1.00 18.54 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 19.986 0.130   3.368  1.00 19.67 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 18.642 1.509   5.922  1.00 21.79 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 19.227 2.794   6.040  1.00 27.22 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 21.603 1.368   4.350  1.00 17.39 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 22.368 1.579   3.101  1.00 17.57 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 23.076 0.303   2.567  1.00 17.86 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 23.680 0.336   1.488  1.00 18.82 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 23.375 2.714   3.239  1.00 18.82 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 24.386 2.396   4.184  1.00 19.57 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 22.995 -0.807  3.323  1.00 16.82 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 23.485 -2.112  2.907  1.00 17.52 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 22.379 -3.198  3.040  1.00 19.19 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 22.635 -4.363  2.721  1.00 18.69 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 24.686 -2.516  3.788  1.00 17.72 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 25.925 -1.655  3.564  1.00 19.51 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 26.623 -1.988  2.240  1.00 19.82 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 27.815 -1.152  2.030  1.00 20.14 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 27.798 0.028   1.411  1.00 21.11 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 26.661 0.516   0.929  1.00 19.64 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 28.924 0.714   1.243  1.00 21.02 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 21.178 -2.846  3.582  1.00 19.30 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 20.097 -3.796  3.859  1.00 21.42 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 20.626 -4.988  4.680  1.00 21.44 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 20.347 -6.144  4.363  1.00 21.54 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 19.472 -4.284  2.541  1.00 23.73 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 18.379 -3.388  2.078  1.00 29.50 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.426 -4.130  1.132  1.00 31.09 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 16.800 -3.159  0.252  1.00 32.78 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.126 -2.989  -1.024 1.00 34.89 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 18.018 -3.797  -1.609 1.00 36.15 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 16.545 -2.034  -1.740 1.00 32.35 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 21.478 -4.694  5.663  1.00 20.99 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 22.147 -5.750  6.433  1.00 20.69 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 22.331 -5.353  7.881  1.00 19.10 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 22.444 -4.160  8.181  1.00 18.54 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 23.585 -5.928  5.881  1.00 24.72 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 23.779 -6.986  4.805  1.00 32.29 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 25.277 -7.095  4.501  1.00 38.81 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 25.645 -8.315  3.685  1.00 44.55 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 25.245 -8.186  2.257  1.00 48.72 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 22.483 -6.353  8.755  1.00 17.62 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 22.827 -6.145  10.155 1.00 16.55 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 24.334 -6.445  10.285 1.00 17.32 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 24.856 -7.382  9.645  1.00 18.98 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 22.037 -7.104  11.071 1.00 16.25 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 20.558 -6.885  11.072 1.00 18.28 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 19.935 -6.139  12.058 1.00 20.41 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 19.623 -7.338  10.222 1.00 18.31 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 18.647 -6.182  11.775 1.00 19.50 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 18.414 -6.882  10.683 1.00 20.42 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 25.033 -5.684  11.116 1.00 16.57 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 26.462 -5.881  11.350 1.00 17.23 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 26.754 -5.930  12.831 1.00 18.32 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 26.200 -5.130  13.608 1.00 18.27 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 27.275 -4.695  10.792 1.00 16.80 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 27.300 -4.608  9.288  1.00 17.91 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 28.085 -5.472  8.530  1.00 19.10 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 26.583 -3.624  8.622  1.00 18.43 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 28.111 -5.395  7.139  1.00 19.81 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 26.610 -3.529  7.236  1.00 19.26 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 27.378 -4.413  6.496  1.00 20.73 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 27.388 -4.308  5.121  1.00 21.40 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 27.674 -6.798  13.251 1.00 18.54 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 28.072 -6.797  14.674 1.00 18.63 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 29.088 -5.648  14.946 1.00 19.85 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 29.931 -5.339  14.078 1.00 20.02 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 28.718 -8.181  14.845 1.00 19.44 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 29.321 -8.459  13.481 1.00 19.66 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 28.388 -7.837  12.462 1.00 17.36 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 29.004 -4.986  16.122 1.00 18.93 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 29.919 -3.896  16.455 1.00 19.38 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 30.447 -3.999  17.878 1.00 19.12 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 29.771 -4.526  18.760 1.00 18.04 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 29.246 -2.488  16.303 1.00 20.53 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 29.218 -2.023  14.848 1.00 21.72 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 27.850 -2.456  16.928 1.00 20.99 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 31.651 -3.444  18.099 1.00 19.18 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 32.202 -3.188  19.429 1.00 19.07 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 32.099 -1.650  19.512 1.00 18.41 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 32.538 -0.979  18.578 1.00 18.74 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 33.664 -3.584  19.515 1.00 21.84 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 33.743 -4.999  19.559 1.00 27.45 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 31.489 -1.094  20.578 1.00 16.92 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 31.311 0.362   20.631 1.00 17.12 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 31.822 0.979   21.939 1.00 18.16 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 31.884 0.293   22.958 1.00 18.67 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 29.834 0.739   20.357 1.00 16.98 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 28.795 -0.018  21.170 1.00 17.20 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 28.254 -1.209  20.703 1.00 18.31 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 28.293 0.513   22.357 1.00 18.11 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 27.289 -1.904  21.457 1.00 18.15 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 27.334 -0.184  23.115 1.00 17.89 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 26.834 -1.376  22.652 1.00 18.17 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 32.177 2.254   21.908 1.00 18.91 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 32.667 2.941   23.106 1.00 20.09 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 31.515 3.283   24.050 1.00 20.67 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 30.350 3.342   23.641 1.00 20.50 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 33.426 4.207   22.722 1.00 21.40 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 32.562 5.081   22.011 1.00 25.52 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 31.828 3.508   25.326 1.00 20.46 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 30.829 3.904   26.313 1.00 21.06 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 30.242 5.283   25.937 1.00 21.75 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 30.911 6.092   25.308 1.00 22.90 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 31.497 3.958   27.711 1.00 23.20 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 31.766 2.566   28.262 1.00 27.21 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 32.147 2.658   29.738 1.00 32.29 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 32.395 1.302   30.327 1.00 37.82 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 33.846 1.007   30.333 1.00 43.88 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 28.981 5.558   26.308 1.00 20.95 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 28.378 6.864   25.991 1.00 20.92 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 29.222 8.047   26.474 1.00 21.04 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 29.674 8.047   27.617 1.00 21.78 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 27.033 6.833   26.743 1.00 21.82 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 26.746 5.375   26.979 1.00 22.87 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 28.079 4.698   27.099 1.00 21.08 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 29.520 8.994   25.572 1.00 20.72 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 30.412 10.095  25.889 1.00 22.58 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 30.155 11.331  25.016 1.00 21.62 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 29.281 11.292  24.141 1.00 21.13 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 31.863 9.620   25.779 1.00 26.29 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 32.223 9.427   24.425 1.00 31.88 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 30.848 12.454  25.331 1.00 21.21 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 30.729 13.763  24.674 1.00 21.76 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 31.735 13.755  23.538 1.00 22.40 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 32.931 13.643  23.801 1.00 23.28 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 31.121 14.843  25.708 1.00 21.97 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 30.731 16.256  25.423 1.00 24.12 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 29.227 16.400  25.135 1.00 23.97 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 31.186 17.203  26.552 1.00 26.18 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 31.256 13.796  22.281 1.00 22.63 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 32.101 13.701  21.087 1.00 23.32 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 31.858 14.852  20.117 1.00 23.85 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 30.695 15.168  19.835 1.00 23.32 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 31.802 12.325  20.421 1.00 24.62 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 32.337 11.174  21.290 1.00 25.57 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 32.370 12.234  19.000 1.00 25.29 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 31.795 9.897   20.975 1.00 27.11 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 32.934 15.455  19.564 1.00 23.84 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 32.766 16.538  18.600 1.00 24.98 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 32.154 16.023  17.273 1.00 25.76 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 32.581 14.994  16.752 1.00 25.34 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 34.110 17.261  18.341 1.00 25.95 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 33.980 18.425  17.385 1.00 27.79 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 34.312 18.284  16.045 1.00 29.00 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 33.433 19.624  17.800 1.00 29.81 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 34.178 19.351  15.161 1.00 30.35 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 33.306 20.690  16.914 1.00 31.03 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 33.680 20.542  15.599 1.00 30.34 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 31.093 16.701  16.787 1.00 25.53 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 30.421 16.364  15.541 1.00 25.87 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 30.456 17.601  14.648 1.00 27.45 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 29.973 18.683  15.033 1.00 27.76 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 28.963 15.890  15.786 1.00 25.38 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 28.305 15.433  14.484 1.00 26.83 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 28.946 14.755  16.809 1.00 24.56 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 31.022 17.436  13.461 1.00 28.00 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 31.144 18.502  12.475 1.00 28.95 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 29.755 19.057  12.062 1.00 28.39 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 28.748 18.355  12.159 1.00 27.71 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 31.860 17.926  11.241 1.00 33.23 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 32.877 18.846  10.611 1.00 43.60 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 33.400 18.247  9.319  1.00 52.74 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 33.318 18.920  8.264  1.00 54.69 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 33.855 17.080  9.361  1.00 55.44 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 29.705 20.332  11.588 1.00 28.23 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 28.449 20.936  11.149 1.00 28.10 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 27.814 20.131  10.020 1.00 28.20 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 28.514 19.505  9.225  1.00 28.58 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 28.696 22.355  10.670 1.00 28.44 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 26.492 20.140  9.962  1.00 28.03 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 25.723 19.513  8.900  1.00 28.50 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 24.557 20.472  8.573  1.00 29.46 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 24.488 21.554  9.170  1.00 30.39 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 25.184 18.172  9.393  1.00 30.17 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 24.227 18.323  10.438 1.00 31.19 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 23.645 20.104  7.656  1.00 29.64 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 22.493 20.967  7.378  1.00 31.26 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 21.534 21.083  8.584  1.00 30.49 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 20.774 22.041  8.699  1.00 30.98 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 21.754 20.571  6.087  1.00 36.76 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 21.409 19.102  5.879  1.00 46.24 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 20.873 18.764  4.493  1.00 58.58 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 20.706 19.694  3.669  1.00 62.10 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 20.619 17.565  4.233  1.00 61.60 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 21.604 20.103  9.500  1.00 28.89 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 20.741 20.023  10.659 1.00 28.06 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 21.261 20.690  11.901 1.00 27.17 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 20.458 21.127  12.712 1.00 27.51 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 20.442 18.565  10.971 1.00 27.81 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 19.830 17.834  9.803  1.00 28.27 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 20.607 17.056  8.964  1.00 29.77 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 18.476 17.929  9.532  1.00 28.71 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 20.041 16.345  7.914  1.00 31.28 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 17.909 17.273  8.447  1.00 30.27 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 18.693 16.472  7.647  1.00 32.02 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 18.149 15.792  6.584  1.00 34.72 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 22.579 20.727  12.085 1.00 26.07 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 23.153 21.294  13.298 1.00 26.04 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 24.427 22.076  13.026 1.00 27.68 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 25.213 21.709  12.150 1.00 27.50 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 23.544 20.170  14.295 1.00 24.81 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 22.428 19.303  14.833 1.00 22.69 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 21.600 19.754  15.847 1.00 23.10 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 22.300 17.978  14.440 1.00 22.74 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 20.595 18.948  16.374 1.00 22.91 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 21.308 17.156  14.969 1.00 21.94 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 20.471 17.636  15.954 1.00 21.88 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 19.463 16.861  16.487 1.00 19.94 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 24.723 23.068  13.881 1.00 29.38 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 26.052 23.691  13.805 1.00 29.81 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 27.089 22.699  14.360 1.00 30.07 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 26.731 21.710  15.039 1.00 30.79 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 25.924 24.882  14.750 1.00 30.91 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 24.928 24.412  15.798 1.00 31.44 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 23.936 23.569  15.036 1.00 29.20 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 28.398 22.995  14.169 1.00 28.87 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 29.458 22.173  14.760 1.00 29.07 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 29.302 22.230  16.290 1.00 28.43 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 29.036 23.308  16.828 1.00 28.56 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 30.821 22.704  14.354 1.00 29.99 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 29.279 21.062  16.951 1.00 26.72 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 29.015 21.037  18.392 1.00 26.02 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 29.494 19.715  19.005 1.00 25.77 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 29.863 18.799  18.268 1.00 26.60 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 27.476 21.183  18.585 1.00 25.45 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 26.709 19.883  18.245 1.00 24.44 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 25.284 20.073  17.744 1.00 23.76 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 24.393 18.971  18.163 1.00 24.34 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 24.401 17.752  17.623 1.00 24.39 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 23.554 16.822  18.052 1.00 22.20 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 25.260 17.453  16.658 1.00 23.89 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 29.424 19.584  20.331 1.00 25.34 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 29.695 18.292  20.975 1.00 25.43 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 28.362 17.602  21.178 1.00 23.95 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 27.448 18.193  21.745 1.00 24.65 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 30.347 18.469  22.352 1.00 26.19 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 31.786 18.903  22.242 1.00 27.51 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 32.810 17.974  22.232 1.00 29.20 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 32.114 20.240  22.075 1.00 29.67 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 34.138 18.372  22.102 1.00 30.88 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 33.430 20.648  21.917 1.00 31.11 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 34.440 19.715  21.940 1.00 32.57 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? 35.726 20.177  21.801 1.00 35.50 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 28.228 16.379  20.689 1.00 21.38 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 27.010 15.607  20.892 1.00 19.49 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 27.275 14.710  22.121 1.00 18.62 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 28.334 14.071  22.198 1.00 19.56 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 26.682 14.751  19.648 1.00 19.40 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 25.476 13.834  19.878 1.00 19.04 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 24.853 13.350  18.604 1.00 19.18 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 24.789 14.092  17.602 1.00 21.40 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 24.326 12.119  18.630 1.00 17.03 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 26.362 14.701  23.092 1.00 16.90 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 26.539 13.903  24.310 1.00 16.74 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 25.866 12.522  24.215 1.00 17.82 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 25.016 12.312  23.326 1.00 18.48 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 25.985 14.676  25.505 1.00 16.42 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 24.588 14.923  25.372 1.00 17.49 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 26.227 11.585  25.135 1.00 16.52 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 25.630 10.234  25.219 1.00 17.11 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 25.797 9.463   23.875 1.00 17.69 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 24.904 8.700   23.480 1.00 17.82 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 24.132 10.323  25.626 1.00 17.83 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 23.921 10.967  26.974 1.00 20.20 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 23.816 10.205  28.134 1.00 22.12 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 23.838 12.284  27.307 1.00 21.02 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 23.668 11.087  29.131 1.00 22.18 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 23.693 12.347  28.678 1.00 21.47 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 26.915 9.710   23.168 1.00 17.36 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 27.159 9.111   21.853 1.00 18.16 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 28.174 7.978   21.968 1.00 17.65 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 29.158 8.104   22.701 1.00 17.43 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 27.723 10.198  20.919 1.00 18.32 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 27.953 9.797   19.461 1.00 20.43 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 26.625 9.416   18.778 1.00 20.71 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 28.588 11.009  18.694 1.00 22.02 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 27.947 6.878   21.241 1.00 17.88 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 28.820 5.706   21.294 1.00 17.66 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 29.375 5.452   19.908 1.00 18.26 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 28.586 5.346   18.970 1.00 18.72 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 27.992 4.491   21.734 1.00 17.43 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 27.382 4.675   23.100 1.00 18.63 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 26.304 3.347   23.671 1.00 20.13 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 24.913 3.480   22.519 1.00 17.04 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 30.704 5.370   19.757 1.00 18.11 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 31.288 5.173   18.437 1.00 19.56 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 31.686 3.741   18.193 1.00 19.01 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 32.126 3.040   19.113 1.00 18.07 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 32.564 6.038   18.263 1.00 21.84 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 32.371 7.547   18.102 1.00 27.05 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 33.689 8.227   17.667 1.00 28.30 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 31.243 7.895   17.104 1.00 29.40 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 31.692 3.388   16.923 1.00 18.20 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 32.111 2.057   16.498 1.00 16.93 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 32.618 2.122   15.059 1.00 16.74 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 32.323 3.075   14.335 1.00 16.59 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 30.922 1.105   16.589 1.00 18.18 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 33.382 1.108   14.663 1.00 16.66 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 33.838 0.959   13.297 1.00 17.81 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 32.756 0.176   12.567 1.00 18.98 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 32.376 -0.925  12.970 1.00 19.82 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? 35.198 0.273   13.223 1.00 19.41 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? 35.565 -0.048  11.771 1.00 19.94 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? 36.263 1.158   13.887 1.00 20.72 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 32.229 0.780   11.530 1.00 19.40 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 31.183 0.187   10.720 1.00 19.51 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 30.715 1.160   9.655  1.00 20.47 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 30.958 2.367   9.750  1.00 21.18 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 30.080 0.641   8.612  1.00 19.57 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 29.570 1.489   7.538  1.00 18.51 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 28.326 2.244   7.947  1.00 18.21 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 27.415 1.666   8.544  1.00 18.72 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 29.290 0.682   6.258  1.00 18.82 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 28.774 1.536   5.136  1.00 19.47 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 29.592 2.431   4.471  1.00 21.41 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 27.512 1.640   4.645  1.00 20.43 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 28.815 3.028   3.574  1.00 22.51 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 27.546 2.581   3.651  1.00 21.14 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 28.237 3.523   7.558  1.00 17.40 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 27.028 4.305   7.776  1.00 16.63 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 27.083 5.524   6.861  1.00 17.20 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 28.175 6.043   6.532  1.00 17.94 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 26.858 4.733   9.229  1.00 17.67 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 27.844 5.669   9.625  1.00 20.67 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 25.924 5.855   6.330  1.00 16.09 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 25.629 7.025   5.512  1.00 16.90 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 24.503 7.841   6.238  1.00 17.88 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 23.804 7.312   7.095  1.00 17.33 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 25.162 6.577   4.112  1.00 17.99 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 26.297 6.052   3.253  1.00 21.04 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 25.885 5.314   1.993  1.00 25.44 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 25.072 5.870   1.220  1.00 26.69 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 26.372 4.179   1.776  1.00 26.28 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 24.344 9.135   5.931  1.00 18.06 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 23.324 9.947   6.640  1.00 17.84 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 21.900 9.344   6.731  1.00 19.02 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 21.265 9.403   7.801  1.00 19.69 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 23.346 11.265  5.856  1.00 18.48 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 24.796 11.396  5.406  1.00 18.92 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 25.138 9.954   4.986  1.00 17.53 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 21.443 8.683   5.659  1.00 18.94 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 20.122 8.050   5.649  1.00 18.42 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 19.994 6.854   6.581  1.00 17.40 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 18.912 6.296   6.736  1.00 17.70 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 21.123 6.370   7.123  1.00 16.31 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 21.122 5.248   8.047  1.00 15.01 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 20.663 5.640   9.463  1.00 14.87 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 20.408 4.745   10.280 1.00 15.32 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 22.521 4.595   8.148  1.00 15.35 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 22.842 3.757   6.932  1.00 17.06 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 21.910 3.179   6.351  1.00 17.14 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 24.028 3.729   6.522  1.00 17.84 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 20.554 6.934   9.782  1.00 14.50 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 20.125 7.402   11.117 1.00 14.42 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 18.767 6.819   11.451 1.00 14.89 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.880 6.767   10.570 1.00 17.06 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 20.092 8.935   11.196 1.00 15.09 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 21.720 9.719   11.218 1.00 18.73 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 18.641 6.287   12.645 1.00 13.29 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.391 5.650   13.051 1.00 14.54 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.503 4.137   13.093 1.00 16.24 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 16.678 3.487   13.725 1.00 16.14 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 18.536 3.555   12.461 1.00 16.25 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 18.754 2.101   12.538 1.00 16.07 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 19.037 1.698   13.981 1.00 16.67 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 19.757 2.400   14.694 1.00 16.76 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 18.437 0.613   14.435 1.00 15.98 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 18.551 0.206   15.828 1.00 17.06 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 19.824 -0.594  16.118 1.00 16.35 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 20.203 -1.483  15.340 1.00 15.37 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.245 -0.537  16.236 1.00 19.19 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 16.149 0.493   16.522 1.00 20.94 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.427 -1.469  17.419 1.00 20.00 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 14.741 -0.135  16.728 1.00 22.33 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 20.440 -0.313  17.266 1.00 15.76 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 21.551 -1.092  17.800 1.00 16.08 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 20.966 -1.915  18.961 1.00 16.09 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 20.313 -1.335  19.846 1.00 15.97 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 22.648 -0.162  18.354 1.00 16.60 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 23.787 -0.845  19.165 1.00 18.36 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 24.613 -1.818  18.292 1.00 18.50 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 24.701 0.202   19.792 1.00 19.62 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 21.182 -3.239  18.966 1.00 16.24 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 20.655 -4.097  20.029 1.00 18.30 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 21.732 -4.987  20.601 1.00 19.63 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 22.601 -5.478  19.866 1.00 20.70 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 19.586 -5.064  19.482 1.00 21.93 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 18.462 -4.466  18.713 1.00 26.39 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.609 -5.593  18.166 1.00 30.03 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 16.919 -6.206  19.288 1.00 32.13 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 15.717 -5.840  19.713 1.00 32.15 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 15.014 -4.948  19.036 1.00 28.34 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 15.205 -6.374  20.813 1.00 29.51 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 21.603 -5.316  21.888 1.00 20.56 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 22.446 -6.323  22.523 1.00 21.21 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 21.484 -7.468  22.974 1.00 21.52 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 20.274 -7.433  22.678 1.00 21.31 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 23.169 -5.717  23.722 1.00 21.21 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 22.033 -5.174  25.022 1.00 19.81 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 21.996 -8.479  23.687 1.00 22.19 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 21.133 -9.593  24.153 1.00 22.82 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 20.005 -9.130  25.092 1.00 22.32 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 19.052 -9.884  25.315 1.00 23.35 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 21.980 -10.676 24.855 1.00 25.65 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 22.605 -10.165 26.160 1.00 30.93 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 23.621 -11.137 26.720 1.00 39.93 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 24.832 -10.849 26.804 1.00 43.17 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 23.146 -12.313 27.116 1.00 39.45 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 20.102 -7.911  25.648 1.00 20.90 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 19.127 -7.382  26.620 1.00 20.94 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 18.032 -6.518  26.037 1.00 20.15 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.074 -6.209  26.750 1.00 20.69 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 19.819 -6.604  27.740 1.00 21.21 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 20.922 -7.357  28.425 1.00 22.96 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 22.254 -7.033  28.219 1.00 24.51 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 20.856 -8.426  29.273 1.00 24.76 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 22.961 -7.900  28.922 1.00 26.29 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 22.166 -8.774  29.571 1.00 26.28 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 18.176 -6.107  24.779 1.00 18.82 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.167 -5.283  24.140 1.00 18.99 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 17.805 -4.141  23.371 1.00 18.57 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 18.984 -4.192  23.022 1.00 19.33 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.024 -3.110  23.107 1.00 17.75 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.479 -1.941  22.354 1.00 17.55 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 18.465 -1.081  23.146 1.00 17.40 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 18.143 -0.654  24.261 1.00 18.12 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 16.271 -1.101  21.905 1.00 18.76 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 16.743 0.170   21.201 1.00 19.77 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 15.356 -1.932  20.991 1.00 19.17 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 19.643 -0.813  22.546 1.00 16.60 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 20.695 0.013   23.139 1.00 17.15 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 20.589 1.494   22.699 1.00 17.20 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 20.774 2.411   23.502 1.00 16.96 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 22.085 -0.560  22.785 1.00 17.54 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 23.222 0.382   23.263 1.00 17.06 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 22.254 -1.959  23.366 1.00 18.06 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 20.355 1.707   21.411 1.00 16.86 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 20.296 3.063   20.867 1.00 16.89 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 20.021 3.098   19.381 1.00 17.22 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 19.684 2.066   18.793 1.00 16.90 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 20.167 4.288   18.748 1.00 16.52 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 19.934 4.379   17.303 1.00 16.43 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 21.083 5.088   16.593 1.00 15.98 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 21.720 5.952   17.168 1.00 15.97 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 18.611 5.121   17.005 1.00 16.65 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 18.546 6.501   17.726 1.00 17.85 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.406 4.249   17.329 1.00 18.14 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.354 7.383   17.217 1.00 20.09 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 21.320 4.755   15.317 1.00 14.47 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 22.364 5.418   14.520 1.00 12.90 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 22.085 6.943   14.481 1.00 14.06 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 20.932 7.342   14.260 1.00 14.94 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 22.396 4.867   13.089 1.00 13.75 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 23.399 5.672   12.245 1.00 14.25 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 22.781 3.372   13.094 1.00 14.78 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 23.099 7.742   14.779 1.00 14.02 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 22.969 9.197   14.801 1.00 15.06 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 24.114 9.886   14.048 1.00 17.14 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 23.923 10.964  13.493 1.00 18.59 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 22.871 9.669   16.260 1.00 16.40 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 22.780 11.081  16.349 1.00 18.66 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 25.338 9.308   14.058 1.00 17.34 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 26.490 9.926   13.361 1.00 19.06 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 27.261 8.866   12.533 1.00 19.64 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 26.949 7.669   12.622 1.00 18.21 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 27.434 10.646  14.382 1.00 20.30 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 28.190 9.683   15.118 1.00 20.28 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 26.711 11.549  15.351 1.00 20.86 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 28.290 9.282   11.781 1.00 20.68 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 29.096 8.339   11.025 1.00 22.34 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 29.955 8.991   9.966  1.00 23.90 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 30.068 10.219  9.930  1.00 23.55 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 30.476 8.164   9.063  1.00 24.53 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 31.327 8.601   7.967  1.00 25.30 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 32.715 8.010   8.096  1.00 25.40 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 33.139 7.657   9.197  1.00 25.75 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 33.386 7.782   6.969  1.00 25.23 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 34.763 7.283   6.916  1.00 25.21 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 34.997 5.969   7.625  1.00 23.89 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? 36.034 5.769   8.278  1.00 24.34 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? 35.698 8.351   7.451  1.00 28.10 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? 35.651 9.585   6.613  1.00 34.38 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? 35.855 9.522   5.404  1.00 35.76 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? 35.377 10.737  7.235  1.00 35.73 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 34.017 5.093   7.548  1.00 22.00 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 34.106 3.792   8.198  1.00 21.23 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 33.749 3.827   9.670  1.00 20.49 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 33.949 2.828   10.375 1.00 21.24 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 33.119 4.922   10.128 1.00 18.67 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 32.631 4.984   11.494 1.00 17.34 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 31.091 5.016   11.528 1.00 16.82 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 30.435 5.386   10.550 1.00 16.03 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 33.184 6.214   12.254 1.00 18.33 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 34.720 6.256   12.497 1.00 21.80 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? 35.155 7.661   12.947 1.00 23.27 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? 35.144 5.227   13.567 1.00 21.03 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 30.529 4.592   12.667 1.00 15.28 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 29.091 4.713   12.915 1.00 15.33 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 28.915 5.059   14.399 1.00 16.14 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 29.601 4.470   15.243 1.00 17.14 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 28.291 3.480   12.493 1.00 16.07 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 28.758 2.248   13.239 1.00 16.43 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 26.785 3.712   12.711 1.00 15.77 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 28.122 6.090   14.681 1.00 15.21 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 27.844 6.574   16.045 1.00 14.77 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 26.400 6.359   16.423 1.00 14.77 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 25.507 6.633   15.621 1.00 15.23 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 26.167 5.910   17.662 1.00 14.73 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 24.825 5.608   18.148 1.00 14.30 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 24.475 6.496   19.335 1.00 14.69 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 25.253 6.606   20.287 1.00 13.60 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 24.738 4.126   18.605 1.00 13.01 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 25.258 3.128   17.572 1.00 13.61 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 24.435 2.648   16.577 1.00 13.71 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 26.575 2.663   17.625 1.00 14.07 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 24.911 1.743   15.623 1.00 14.62 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 27.044 1.737   16.687 1.00 14.69 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 26.208 1.289   15.688 1.00 14.74 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 23.251 7.045   19.311 1.00 13.70 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 22.702 7.835   20.401 1.00 14.22 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 22.177 6.798   21.432 1.00 14.44 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 21.251 6.035   21.127 1.00 15.36 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 21.548 8.697   19.885 1.00 14.94 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 22.767 6.760   22.631 1.00 13.72 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 22.334 5.811   23.674 1.00 14.83 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 20.948 6.178   24.208 1.00 15.50 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 20.634 7.369   24.349 1.00 15.24 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 23.330 5.866   24.853 1.00 17.09 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 23.066 4.840   25.943 1.00 22.78 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 22.876 3.673   25.613 1.00 21.88 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 22.995 5.235   27.124 1.00 24.07 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 20.121 5.151   24.549 1.00 14.02 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 18.826 5.380   25.193 1.00 14.95 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 18.696 4.610   26.517 1.00 16.93 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 17.669 4.734   27.169 1.00 18.11 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.642 5.053   24.267 1.00 15.92 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.677 5.902   22.994 1.00 15.96 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.608 3.561   23.924 1.00 16.28 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 19.722 3.834   26.926 1.00 16.67 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 19.686 2.984   28.119 1.00 17.98 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 19.561 3.730   29.411 1.00 19.66 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 19.058 3.142   30.380 1.00 20.40 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 20.930 2.087   28.177 1.00 18.18 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 20.982 1.043   27.070 1.00 18.88 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 22.266 0.272   27.203 1.00 20.25 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 23.393 1.099   26.813 1.00 20.90 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 24.639 0.655   26.706 1.00 21.66 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 24.926 -0.618  26.989 1.00 19.64 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 25.602 1.470   26.305 1.00 20.45 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 19.999 5.021   29.451 1.00 18.94 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 19.853 5.838   30.667 1.00 19.63 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 18.459 6.433   30.835 1.00 20.23 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 18.158 6.964   31.909 1.00 21.90 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 20.877 6.973   30.715 1.00 20.00 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 20.699 7.978   29.603 1.00 25.01 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 20.473 7.550   28.452 1.00 24.67 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 20.776 9.199   29.886 1.00 26.54 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.607 6.366   29.812 1.00 19.34 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 16.255 6.935   29.861 1.00 19.10 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 15.295 5.969   30.534 1.00 19.87 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 14.453 5.328   29.888 1.00 19.12 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 15.798 7.305   28.439 1.00 18.52 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 16.760 8.276   27.695 1.00 19.99 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 16.292 8.513   26.249 1.00 20.28 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 16.889 9.626   28.450 1.00 21.48 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 15.400 5.883   31.865 1.00 20.54 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 14.616 4.899   32.625 1.00 21.47 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 13.107 5.072   32.508 1.00 21.87 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 12.370 4.076   32.551 1.00 22.14 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 15.050 4.876   34.094 1.00 21.78 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 16.576 4.847   34.349 1.00 24.34 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 16.854 4.628   35.838 1.00 25.84 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.303 3.736   33.505 1.00 25.23 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 12.644 6.326   32.370 1.00 22.02 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 11.220 6.646   32.263 1.00 23.64 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 10.559 6.066   31.003 1.00 24.55 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 9.329  6.052   30.928 1.00 25.02 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 10.997 8.167   32.318 1.00 23.37 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 11.847 8.954   31.345 1.00 23.40 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 13.092 9.472   31.566 1.00 24.07 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 11.492 9.319   30.006 1.00 23.56 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 13.534 10.136  30.440 1.00 24.76 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 12.557 10.085  29.479 1.00 24.27 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 10.353 9.124   29.222 1.00 23.71 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 12.530 10.616  28.191 1.00 24.69 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 10.319 9.674   27.955 1.00 24.34 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 11.400 10.402  27.451 1.00 24.74 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 11.344 5.624   29.999 1.00 25.01 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 10.749 5.026   28.794 1.00 26.30 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 9.931  3.756   29.152 1.00 30.38 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 8.989  3.422   28.443 1.00 29.99 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 11.839 4.648   27.784 1.00 24.98 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 12.450 5.788   26.998 1.00 24.58 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 13.577 5.285   26.101 1.00 24.51 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 11.413 6.478   26.135 1.00 24.73 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 10.314 3.056   30.239 1.00 34.14 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 9.691  1.814   30.720 1.00 38.52 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 8.480  1.994   31.594 1.00 42.67 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 7.986  0.995   32.107 1.00 43.76 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 10.685 1.022   31.568 1.00 41.48 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 11.745 0.339   30.786 1.00 49.12 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 11.476 -0.030  29.630 1.00 50.87 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 12.852 0.161   31.332 1.00 53.07 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 8.040  3.223   31.830 1.00 44.96 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 6.872  3.471   32.661 1.00 47.99 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 6.030  4.568   32.023 1.00 49.96 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 4.834  4.660   32.293 1.00 51.56 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 7.308  3.881   34.077 1.00 51.26 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 8.125  5.159   34.106 1.00 57.21 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 9.162  5.190   35.210 1.00 64.32 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 9.314  6.255   35.850 1.00 65.07 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 9.824  4.150   35.433 1.00 66.63 ? 145 GLU   A OE2 1 
ATOM   1078 N  N   . SER   B 1 1   ? 19.558 -24.662 23.860 1.00 24.53 ? 7   SER   C N   1 
ATOM   1079 C  CA  . SER   B 1 1   ? 20.709 -24.542 22.962 1.00 24.09 ? 7   SER   C CA  1 
ATOM   1080 C  C   . SER   B 1 1   ? 20.727 -25.719 21.943 1.00 23.45 ? 7   SER   C C   1 
ATOM   1081 O  O   . SER   B 1 1   ? 20.061 -26.748 22.163 1.00 22.99 ? 7   SER   C O   1 
ATOM   1082 C  CB  . SER   B 1 1   ? 22.006 -24.532 23.774 1.00 25.75 ? 7   SER   C CB  1 
ATOM   1083 O  OG  . SER   B 1 1   ? 22.233 -25.817 24.342 1.00 29.43 ? 7   SER   C OG  1 
ATOM   1084 N  N   . GLY   B 1 2   ? 21.498 -25.569 20.860 1.00 22.19 ? 8   GLY   C N   1 
ATOM   1085 C  CA  . GLY   B 1 2   ? 21.603 -26.610 19.846 1.00 21.61 ? 8   GLY   C CA  1 
ATOM   1086 C  C   . GLY   B 1 2   ? 21.853 -26.054 18.461 1.00 21.08 ? 8   GLY   C C   1 
ATOM   1087 O  O   . GLY   B 1 2   ? 21.497 -24.909 18.182 1.00 21.21 ? 8   GLY   C O   1 
ATOM   1088 N  N   . ALA   B 1 3   ? 22.484 -26.838 17.590 1.00 19.92 ? 9   ALA   C N   1 
ATOM   1089 C  CA  . ALA   B 1 3   ? 22.818 -26.342 16.234 1.00 19.41 ? 9   ALA   C CA  1 
ATOM   1090 C  C   . ALA   B 1 3   ? 22.753 -27.478 15.220 1.00 19.41 ? 9   ALA   C C   1 
ATOM   1091 O  O   . ALA   B 1 3   ? 22.754 -28.645 15.600 1.00 20.59 ? 9   ALA   C O   1 
ATOM   1092 C  CB  . ALA   B 1 3   ? 24.231 -25.739 16.248 1.00 19.06 ? 9   ALA   C CB  1 
ATOM   1093 N  N   . ILE   B 1 4   ? 22.699 -27.147 13.920 1.00 18.94 ? 10  ILE   C N   1 
ATOM   1094 C  CA  . ILE   B 1 4   ? 22.744 -28.130 12.846 1.00 17.56 ? 10  ILE   C CA  1 
ATOM   1095 C  C   . ILE   B 1 4   ? 24.102 -27.934 12.180 1.00 18.64 ? 10  ILE   C C   1 
ATOM   1096 O  O   . ILE   B 1 4   ? 24.494 -26.801 11.897 1.00 18.25 ? 10  ILE   C O   1 
ATOM   1097 C  CB  . ILE   B 1 4   ? 21.608 -27.873 11.824 1.00 16.76 ? 10  ILE   C CB  1 
ATOM   1098 C  CG1 . ILE   B 1 4   ? 20.234 -27.909 12.493 1.00 16.37 ? 10  ILE   C CG1 1 
ATOM   1099 C  CG2 . ILE   B 1 4   ? 21.683 -28.887 10.650 1.00 17.35 ? 10  ILE   C CG2 1 
ATOM   1100 C  CD1 . ILE   B 1 4   ? 19.157 -27.250 11.577 1.00 17.13 ? 10  ILE   C CD1 1 
ATOM   1101 N  N   . TYR   B 1 5   ? 24.830 -29.030 11.925 1.00 19.68 ? 11  TYR   C N   1 
ATOM   1102 C  CA  . TYR   B 1 5   ? 26.147 -28.939 11.303 1.00 20.29 ? 11  TYR   C CA  1 
ATOM   1103 C  C   . TYR   B 1 5   ? 26.069 -29.645 9.973  1.00 21.43 ? 11  TYR   C C   1 
ATOM   1104 O  O   . TYR   B 1 5   ? 25.964 -30.867 9.948  1.00 21.53 ? 11  TYR   C O   1 
ATOM   1105 C  CB  . TYR   B 1 5   ? 27.214 -29.611 12.192 1.00 20.28 ? 11  TYR   C CB  1 
ATOM   1106 C  CG  . TYR   B 1 5   ? 27.414 -28.830 13.479 1.00 21.32 ? 11  TYR   C CG  1 
ATOM   1107 C  CD1 . TYR   B 1 5   ? 28.256 -27.730 13.521 1.00 21.91 ? 11  TYR   C CD1 1 
ATOM   1108 C  CD2 . TYR   B 1 5   ? 26.678 -29.125 14.616 1.00 22.23 ? 11  TYR   C CD2 1 
ATOM   1109 C  CE1 . TYR   B 1 5   ? 28.404 -26.976 14.678 1.00 22.65 ? 11  TYR   C CE1 1 
ATOM   1110 C  CE2 . TYR   B 1 5   ? 26.817 -28.377 15.778 1.00 22.63 ? 11  TYR   C CE2 1 
ATOM   1111 C  CZ  . TYR   B 1 5   ? 27.691 -27.308 15.808 1.00 23.12 ? 11  TYR   C CZ  1 
ATOM   1112 O  OH  . TYR   B 1 5   ? 27.788 -26.521 16.929 1.00 22.96 ? 11  TYR   C OH  1 
ATOM   1113 N  N   . VAL   B 1 6   ? 26.146 -28.899 8.859  1.00 22.15 ? 12  VAL   C N   1 
ATOM   1114 C  CA  . VAL   B 1 6   ? 26.055 -29.512 7.541  1.00 23.23 ? 12  VAL   C CA  1 
ATOM   1115 C  C   . VAL   B 1 6   ? 27.136 -28.913 6.646  1.00 25.08 ? 12  VAL   C C   1 
ATOM   1116 O  O   . VAL   B 1 6   ? 27.260 -27.693 6.575  1.00 25.43 ? 12  VAL   C O   1 
ATOM   1117 C  CB  . VAL   B 1 6   ? 24.615 -29.356 6.957  1.00 24.01 ? 12  VAL   C CB  1 
ATOM   1118 C  CG1 . VAL   B 1 6   ? 24.102 -27.915 7.085  1.00 24.05 ? 12  VAL   C CG1 1 
ATOM   1119 C  CG2 . VAL   B 1 6   ? 24.556 -29.841 5.511  1.00 24.99 ? 12  VAL   C CG2 1 
ATOM   1120 N  N   . GLY   B 1 7   ? 28.006 -29.747 6.061  1.00 25.85 ? 13  GLY   C N   1 
ATOM   1121 C  CA  . GLY   B 1 7   ? 29.099 -29.242 5.228  1.00 26.35 ? 13  GLY   C CA  1 
ATOM   1122 C  C   . GLY   B 1 7   ? 29.985 -28.302 6.022  1.00 27.17 ? 13  GLY   C C   1 
ATOM   1123 O  O   . GLY   B 1 7   ? 30.295 -28.600 7.180  1.00 28.38 ? 13  GLY   C O   1 
ATOM   1124 N  N   . ASN   B 1 8   ? 30.255 -27.100 5.498  1.00 26.39 ? 14  ASN   C N   1 
ATOM   1125 C  CA  . ASN   B 1 8   ? 31.041 -26.124 6.260  1.00 26.44 ? 14  ASN   C CA  1 
ATOM   1126 C  C   . ASN   B 1 8   ? 30.159 -25.038 6.864  1.00 23.94 ? 14  ASN   C C   1 
ATOM   1127 O  O   . ASN   B 1 8   ? 30.590 -23.886 6.973  1.00 23.66 ? 14  ASN   C O   1 
ATOM   1128 C  CB  . ASN   B 1 8   ? 32.150 -25.522 5.426  1.00 29.67 ? 14  ASN   C CB  1 
ATOM   1129 C  CG  . ASN   B 1 8   ? 33.261 -26.500 5.163  1.00 36.68 ? 14  ASN   C CG  1 
ATOM   1130 O  OD1 . ASN   B 1 8   ? 33.866 -27.060 6.088  1.00 39.11 ? 14  ASN   C OD1 1 
ATOM   1131 N  ND2 . ASN   B 1 8   ? 33.536 -26.724 3.894  1.00 37.91 ? 14  ASN   C ND2 1 
ATOM   1132 N  N   . TYR   B 1 9   ? 28.941 -25.409 7.289  1.00 22.33 ? 15  TYR   C N   1 
ATOM   1133 C  CA  . TYR   B 1 9   ? 27.987 -24.476 7.871  1.00 21.02 ? 15  TYR   C CA  1 
ATOM   1134 C  C   . TYR   B 1 9   ? 27.515 -24.955 9.251  1.00 19.51 ? 15  TYR   C C   1 
ATOM   1135 O  O   . TYR   B 1 9   ? 27.387 -26.153 9.498  1.00 18.48 ? 15  TYR   C O   1 
ATOM   1136 C  CB  . TYR   B 1 9   ? 26.725 -24.387 6.965  1.00 21.19 ? 15  TYR   C CB  1 
ATOM   1137 C  CG  . TYR   B 1 9   ? 26.994 -23.808 5.591  1.00 22.73 ? 15  TYR   C CG  1 
ATOM   1138 C  CD1 . TYR   B 1 9   ? 27.617 -22.575 5.445  1.00 25.01 ? 15  TYR   C CD1 1 
ATOM   1139 C  CD2 . TYR   B 1 9   ? 26.613 -24.487 4.439  1.00 24.70 ? 15  TYR   C CD2 1 
ATOM   1140 C  CE1 . TYR   B 1 9   ? 27.874 -22.042 4.187  1.00 26.74 ? 15  TYR   C CE1 1 
ATOM   1141 C  CE2 . TYR   B 1 9   ? 26.858 -23.961 3.173  1.00 25.82 ? 15  TYR   C CE2 1 
ATOM   1142 C  CZ  . TYR   B 1 9   ? 27.487 -22.737 3.055  1.00 27.87 ? 15  TYR   C CZ  1 
ATOM   1143 O  OH  . TYR   B 1 9   ? 27.724 -22.204 1.810  1.00 30.66 ? 15  TYR   C OH  1 
ATOM   1144 N  N   . ARG   B 1 10  ? 27.215 -23.989 10.133 1.00 18.14 ? 16  ARG   C N   1 
ATOM   1145 C  CA  . ARG   B 1 10  ? 26.618 -24.211 11.461 1.00 17.59 ? 16  ARG   C CA  1 
ATOM   1146 C  C   . ARG   B 1 10  ? 25.343 -23.374 11.460 1.00 17.83 ? 16  ARG   C C   1 
ATOM   1147 O  O   . ARG   B 1 10  ? 25.411 -22.179 11.175 1.00 18.34 ? 16  ARG   C O   1 
ATOM   1148 C  CB  . ARG   B 1 10  ? 27.575 -23.735 12.582 1.00 17.16 ? 16  ARG   C CB  1 
ATOM   1149 C  CG  . ARG   B 1 10  ? 26.927 -23.448 13.937 1.00 18.67 ? 16  ARG   C CG  1 
ATOM   1150 C  CD  . ARG   B 1 10  ? 27.960 -23.243 15.049 1.00 20.85 ? 16  ARG   C CD  1 
ATOM   1151 N  NE  . ARG   B 1 10  ? 27.554 -22.224 16.023 1.00 24.14 ? 16  ARG   C NE  1 
ATOM   1152 C  CZ  . ARG   B 1 10  ? 27.121 -22.485 17.256 1.00 25.10 ? 16  ARG   C CZ  1 
ATOM   1153 N  NH1 . ARG   B 1 10  ? 27.009 -23.746 17.679 1.00 22.18 ? 16  ARG   C NH1 1 
ATOM   1154 N  NH2 . ARG   B 1 10  ? 26.812 -21.485 18.087 1.00 22.97 ? 16  ARG   C NH2 1 
ATOM   1155 N  N   . VAL   B 1 11  ? 24.170 -23.990 11.727 1.00 17.00 ? 17  VAL   C N   1 
ATOM   1156 C  CA  . VAL   B 1 11  ? 22.885 -23.291 11.733 1.00 16.69 ? 17  VAL   C CA  1 
ATOM   1157 C  C   . VAL   B 1 11  ? 22.410 -23.181 13.178 1.00 16.82 ? 17  VAL   C C   1 
ATOM   1158 O  O   . VAL   B 1 11  ? 22.264 -24.218 13.846 1.00 18.00 ? 17  VAL   C O   1 
ATOM   1159 C  CB  . VAL   B 1 11  ? 21.827 -24.053 10.890 1.00 17.59 ? 17  VAL   C CB  1 
ATOM   1160 C  CG1 . VAL   B 1 11  ? 20.532 -23.224 10.773 1.00 18.59 ? 17  VAL   C CG1 1 
ATOM   1161 C  CG2 . VAL   B 1 11  ? 22.370 -24.439 9.523  1.00 16.91 ? 17  VAL   C CG2 1 
ATOM   1162 N  N   . VAL   B 1 12  ? 22.189 -21.968 13.675 1.00 15.50 ? 18  VAL   C N   1 
ATOM   1163 C  CA  . VAL   B 1 12  ? 21.756 -21.757 15.059 1.00 16.87 ? 18  VAL   C CA  1 
ATOM   1164 C  C   . VAL   B 1 12  ? 20.560 -20.824 15.112 1.00 16.59 ? 18  VAL   C C   1 
ATOM   1165 O  O   . VAL   B 1 12  ? 20.334 -20.048 14.169 1.00 16.19 ? 18  VAL   C O   1 
ATOM   1166 C  CB  . VAL   B 1 12  ? 22.908 -21.137 15.938 1.00 18.64 ? 18  VAL   C CB  1 
ATOM   1167 C  CG1 . VAL   B 1 12  ? 24.005 -22.148 16.176 1.00 21.14 ? 18  VAL   C CG1 1 
ATOM   1168 C  CG2 . VAL   B 1 12  ? 23.456 -19.839 15.347 1.00 17.86 ? 18  VAL   C CG2 1 
ATOM   1169 N  N   . ASN   B 1 13  ? 19.870 -20.742 16.291 1.00 16.24 ? 19  ASN   C N   1 
ATOM   1170 C  CA  . ASN   B 1 13  ? 18.863 -19.681 16.480 1.00 17.00 ? 19  ASN   C CA  1 
ATOM   1171 C  C   . ASN   B 1 13  ? 19.634 -18.341 16.446 1.00 17.57 ? 19  ASN   C C   1 
ATOM   1172 O  O   . ASN   B 1 13  ? 20.695 -18.219 17.096 1.00 18.25 ? 19  ASN   C O   1 
ATOM   1173 C  CB  . ASN   B 1 13  ? 18.190 -19.800 17.844 1.00 17.43 ? 19  ASN   C CB  1 
ATOM   1174 C  CG  . ASN   B 1 13  ? 17.346 -21.040 17.973 1.00 19.24 ? 19  ASN   C CG  1 
ATOM   1175 O  OD1 . ASN   B 1 13  ? 17.813 -22.080 18.434 1.00 19.22 ? 19  ASN   C OD1 1 
ATOM   1176 N  ND2 . ASN   B 1 13  ? 16.086 -20.962 17.551 1.00 18.71 ? 19  ASN   C ND2 1 
ATOM   1177 N  N   . ARG   B 1 14  ? 19.147 -17.380 15.663 1.00 17.13 ? 20  ARG   C N   1 
ATOM   1178 C  CA  . ARG   B 1 14  ? 19.828 -16.073 15.555 1.00 17.40 ? 20  ARG   C CA  1 
ATOM   1179 C  C   . ARG   B 1 14  ? 20.006 -15.401 16.935 1.00 17.66 ? 20  ARG   C C   1 
ATOM   1180 O  O   . ARG   B 1 14  ? 21.086 -14.862 17.221 1.00 18.40 ? 20  ARG   C O   1 
ATOM   1181 C  CB  . ARG   B 1 14  ? 19.076 -15.144 14.595 1.00 18.04 ? 20  ARG   C CB  1 
ATOM   1182 C  CG  . ARG   B 1 14  ? 19.851 -13.874 14.210 1.00 19.09 ? 20  ARG   C CG  1 
ATOM   1183 C  CD  . ARG   B 1 14  ? 18.886 -12.959 13.486 1.00 18.85 ? 20  ARG   C CD  1 
ATOM   1184 N  NE  . ARG   B 1 14  ? 19.478 -11.722 12.952 1.00 20.47 ? 20  ARG   C NE  1 
ATOM   1185 C  CZ  . ARG   B 1 14  ? 19.535 -10.574 13.620 1.00 21.38 ? 20  ARG   C CZ  1 
ATOM   1186 N  NH1 . ARG   B 1 14  ? 19.196 -10.528 14.905 1.00 20.15 ? 20  ARG   C NH1 1 
ATOM   1187 N  NH2 . ARG   B 1 14  ? 20.010 -9.478  13.031 1.00 21.10 ? 20  ARG   C NH2 1 
ATOM   1188 N  N   . HIS   B 1 15  ? 19.001 -15.535 17.821 1.00 17.13 ? 21  HIS   C N   1 
ATOM   1189 C  CA  . HIS   B 1 15  ? 19.088 -14.914 19.140 1.00 16.36 ? 21  HIS   C CA  1 
ATOM   1190 C  C   . HIS   B 1 15  ? 20.110 -15.579 20.081 1.00 18.11 ? 21  HIS   C C   1 
ATOM   1191 O  O   . HIS   B 1 15  ? 20.468 -14.986 21.100 1.00 19.15 ? 21  HIS   C O   1 
ATOM   1192 C  CB  . HIS   B 1 15  ? 17.708 -14.793 19.804 1.00 15.40 ? 21  HIS   C CB  1 
ATOM   1193 C  CG  . HIS   B 1 15  ? 17.126 -16.074 20.330 1.00 16.99 ? 21  HIS   C CG  1 
ATOM   1194 N  ND1 . HIS   B 1 15  ? 16.460 -16.957 19.499 1.00 16.83 ? 21  HIS   C ND1 1 
ATOM   1195 C  CD2 . HIS   B 1 15  ? 17.082 -16.545 21.603 1.00 18.57 ? 21  HIS   C CD2 1 
ATOM   1196 C  CE1 . HIS   B 1 15  ? 16.062 -17.959 20.274 1.00 18.75 ? 21  HIS   C CE1 1 
ATOM   1197 N  NE2 . HIS   B 1 15  ? 16.436 -17.770 21.550 1.00 19.22 ? 21  HIS   C NE2 1 
ATOM   1198 N  N   . LEU   B 1 16  ? 20.593 -16.781 19.731 1.00 17.70 ? 22  LEU   C N   1 
ATOM   1199 C  CA  . LEU   B 1 16  ? 21.607 -17.470 20.519 1.00 18.77 ? 22  LEU   C CA  1 
ATOM   1200 C  C   . LEU   B 1 16  ? 22.975 -17.468 19.835 1.00 19.86 ? 22  LEU   C C   1 
ATOM   1201 O  O   . LEU   B 1 16  ? 23.903 -18.087 20.375 1.00 20.41 ? 22  LEU   C O   1 
ATOM   1202 C  CB  . LEU   B 1 16  ? 21.181 -18.926 20.831 1.00 18.00 ? 22  LEU   C CB  1 
ATOM   1203 C  CG  . LEU   B 1 16  ? 19.832 -19.080 21.562 1.00 19.29 ? 22  LEU   C CG  1 
ATOM   1204 C  CD1 . LEU   B 1 16  ? 19.523 -20.564 21.814 1.00 20.24 ? 22  LEU   C CD1 1 
ATOM   1205 C  CD2 . LEU   B 1 16  ? 19.831 -18.297 22.908 1.00 19.74 ? 22  LEU   C CD2 1 
ATOM   1206 N  N   . ALA   B 1 17  ? 23.124 -16.814 18.654 1.00 19.48 ? 23  ALA   C N   1 
ATOM   1207 C  CA  . ALA   B 1 17  ? 24.419 -16.780 17.950 1.00 19.20 ? 23  ALA   C CA  1 
ATOM   1208 C  C   . ALA   B 1 17  ? 25.500 -16.160 18.829 1.00 19.41 ? 23  ALA   C C   1 
ATOM   1209 O  O   . ALA   B 1 17  ? 25.233 -15.222 19.575 1.00 18.83 ? 23  ALA   C O   1 
ATOM   1210 C  CB  . ALA   B 1 17  ? 24.292 -15.997 16.642 1.00 18.46 ? 23  ALA   C CB  1 
ATOM   1211 N  N   . THR   B 1 18  ? 26.716 -16.695 18.766 1.00 20.49 ? 24  THR   C N   1 
ATOM   1212 C  CA  . THR   B 1 18  ? 27.821 -16.198 19.590 1.00 21.47 ? 24  THR   C CA  1 
ATOM   1213 C  C   . THR   B 1 18  ? 28.590 -15.052 18.866 1.00 22.10 ? 24  THR   C C   1 
ATOM   1214 O  O   . THR   B 1 18  ? 28.330 -14.774 17.693 1.00 20.83 ? 24  THR   C O   1 
ATOM   1215 C  CB  . THR   B 1 18  ? 28.789 -17.373 19.876 1.00 23.76 ? 24  THR   C CB  1 
ATOM   1216 O  OG1 . THR   B 1 18  ? 29.384 -17.806 18.645 1.00 24.20 ? 24  THR   C OG1 1 
ATOM   1217 C  CG2 . THR   B 1 18  ? 28.121 -18.522 20.610 1.00 24.75 ? 24  THR   C CG2 1 
ATOM   1218 N  N   . HIS   B 1 19  ? 29.598 -14.430 19.537 1.00 22.92 ? 25  HIS   C N   1 
ATOM   1219 C  CA  . HIS   B 1 19  ? 30.458 -13.443 18.874 1.00 23.74 ? 25  HIS   C CA  1 
ATOM   1220 C  C   . HIS   B 1 19  ? 31.172 -14.134 17.662 1.00 22.96 ? 25  HIS   C C   1 
ATOM   1221 O  O   . HIS   B 1 19  ? 31.323 -13.537 16.594 1.00 23.30 ? 25  HIS   C O   1 
ATOM   1222 C  CB  . HIS   B 1 19  ? 31.534 -12.904 19.869 1.00 26.89 ? 25  HIS   C CB  1 
ATOM   1223 C  CG  . HIS   B 1 19  ? 30.985 -12.043 20.970 1.00 34.00 ? 25  HIS   C CG  1 
ATOM   1224 N  ND1 . HIS   B 1 19  ? 30.149 -10.949 20.713 1.00 37.94 ? 25  HIS   C ND1 1 
ATOM   1225 C  CD2 . HIS   B 1 19  ? 31.201 -12.108 22.304 1.00 37.05 ? 25  HIS   C CD2 1 
ATOM   1226 C  CE1 . HIS   B 1 19  ? 29.896 -10.398 21.891 1.00 38.49 ? 25  HIS   C CE1 1 
ATOM   1227 N  NE2 . HIS   B 1 19  ? 30.502 -11.057 22.878 1.00 39.00 ? 25  HIS   C NE2 1 
ATOM   1228 N  N   . ASN   B 1 20  ? 31.562 -15.405 17.825 1.00 22.86 ? 26  ASN   C N   1 
ATOM   1229 C  CA  . ASN   B 1 20  ? 32.230 -16.164 16.763 1.00 23.41 ? 26  ASN   C CA  1 
ATOM   1230 C  C   . ASN   B 1 20  ? 31.307 -16.447 15.580 1.00 22.54 ? 26  ASN   C C   1 
ATOM   1231 O  O   . ASN   B 1 20  ? 31.740 -16.339 14.435 1.00 22.70 ? 26  ASN   C O   1 
ATOM   1232 C  CB  . ASN   B 1 20  ? 32.847 -17.461 17.298 1.00 26.31 ? 26  ASN   C CB  1 
ATOM   1233 C  CG  . ASN   B 1 20  ? 33.742 -18.141 16.295 1.00 32.42 ? 26  ASN   C CG  1 
ATOM   1234 O  OD1 . ASN   B 1 20  ? 34.820 -17.637 15.956 1.00 34.45 ? 26  ASN   C OD1 1 
ATOM   1235 N  ND2 . ASN   B 1 20  ? 33.316 -19.296 15.793 1.00 34.06 ? 26  ASN   C ND2 1 
ATOM   1236 N  N   . ASP   B 1 21  ? 30.030 -16.751 15.826 1.00 21.57 ? 27  ASP   C N   1 
ATOM   1237 C  CA  . ASP   B 1 21  ? 29.069 -16.938 14.730 1.00 20.71 ? 27  ASP   C CA  1 
ATOM   1238 C  C   . ASP   B 1 21  ? 28.952 -15.641 13.904 1.00 21.14 ? 27  ASP   C C   1 
ATOM   1239 O  O   . ASP   B 1 21  ? 28.959 -15.702 12.681 1.00 22.37 ? 27  ASP   C O   1 
ATOM   1240 C  CB  . ASP   B 1 21  ? 27.677 -17.278 15.277 1.00 19.55 ? 27  ASP   C CB  1 
ATOM   1241 C  CG  . ASP   B 1 21  ? 27.556 -18.700 15.808 1.00 22.05 ? 27  ASP   C CG  1 
ATOM   1242 O  OD1 . ASP   B 1 21  ? 28.098 -19.622 15.163 1.00 22.02 ? 27  ASP   C OD1 1 
ATOM   1243 O  OD2 . ASP   B 1 21  ? 26.902 -18.884 16.874 1.00 22.39 ? 27  ASP   C OD2 1 
ATOM   1244 N  N   . TRP   B 1 22  ? 28.864 -14.472 14.570 1.00 20.42 ? 28  TRP   C N   1 
ATOM   1245 C  CA  . TRP   B 1 22  ? 28.748 -13.190 13.856 1.00 21.59 ? 28  TRP   C CA  1 
ATOM   1246 C  C   . TRP   B 1 22  ? 30.032 -12.821 13.095 1.00 22.63 ? 28  TRP   C C   1 
ATOM   1247 O  O   . TRP   B 1 22  ? 29.967 -12.163 12.057 1.00 23.32 ? 28  TRP   C O   1 
ATOM   1248 C  CB  . TRP   B 1 22  ? 28.332 -12.048 14.821 1.00 21.31 ? 28  TRP   C CB  1 
ATOM   1249 C  CG  . TRP   B 1 22  ? 26.851 -12.023 15.084 1.00 20.88 ? 28  TRP   C CG  1 
ATOM   1250 C  CD1 . TRP   B 1 22  ? 26.191 -12.500 16.180 1.00 21.64 ? 28  TRP   C CD1 1 
ATOM   1251 C  CD2 . TRP   B 1 22  ? 25.848 -11.485 14.209 1.00 20.33 ? 28  TRP   C CD2 1 
ATOM   1252 N  NE1 . TRP   B 1 22  ? 24.837 -12.320 16.029 1.00 22.26 ? 28  TRP   C NE1 1 
ATOM   1253 C  CE2 . TRP   B 1 22  ? 24.603 -11.657 14.846 1.00 21.31 ? 28  TRP   C CE2 1 
ATOM   1254 C  CE3 . TRP   B 1 22  ? 25.893 -10.863 12.956 1.00 20.65 ? 28  TRP   C CE3 1 
ATOM   1255 C  CZ2 . TRP   B 1 22  ? 23.406 -11.261 14.254 1.00 21.44 ? 28  TRP   C CZ2 1 
ATOM   1256 C  CZ3 . TRP   B 1 22  ? 24.710 -10.417 12.394 1.00 21.60 ? 28  TRP   C CZ3 1 
ATOM   1257 C  CH2 . TRP   B 1 22  ? 23.486 -10.654 13.021 1.00 21.85 ? 28  TRP   C CH2 1 
ATOM   1258 N  N   . ALA   B 1 23  ? 31.178 -13.214 13.616 1.00 22.68 ? 29  ALA   C N   1 
ATOM   1259 C  CA  . ALA   B 1 23  ? 32.460 -12.916 12.970 1.00 23.46 ? 29  ALA   C CA  1 
ATOM   1260 C  C   . ALA   B 1 23  ? 32.706 -13.817 11.723 1.00 23.91 ? 29  ALA   C C   1 
ATOM   1261 O  O   . ALA   B 1 23  ? 33.607 -13.530 10.917 1.00 24.61 ? 29  ALA   C O   1 
ATOM   1262 C  CB  . ALA   B 1 23  ? 33.594 -13.096 13.974 1.00 23.03 ? 29  ALA   C CB  1 
ATOM   1263 N  N   . ASN   B 1 24  ? 31.994 -14.946 11.633 1.00 22.38 ? 30  ASN   C N   1 
ATOM   1264 C  CA  . ASN   B 1 24  ? 32.086 -15.894 10.519 1.00 21.71 ? 30  ASN   C CA  1 
ATOM   1265 C  C   . ASN   B 1 24  ? 30.688 -16.022 9.843  1.00 21.08 ? 30  ASN   C C   1 
ATOM   1266 O  O   . ASN   B 1 24  ? 30.300 -17.084 9.391  1.00 20.91 ? 30  ASN   C O   1 
ATOM   1267 C  CB  . ASN   B 1 24  ? 32.566 -17.244 11.042 1.00 22.88 ? 30  ASN   C CB  1 
ATOM   1268 C  CG  . ASN   B 1 24  ? 34.009 -17.179 11.516 1.00 27.11 ? 30  ASN   C CG  1 
ATOM   1269 O  OD1 . ASN   B 1 24  ? 34.962 -17.126 10.717 1.00 28.49 ? 30  ASN   C OD1 1 
ATOM   1270 N  ND2 . ASN   B 1 24  ? 34.221 -17.113 12.830 1.00 26.68 ? 30  ASN   C ND2 1 
ATOM   1271 N  N   . LEU   B 1 25  ? 29.961 -14.922 9.777  1.00 20.80 ? 31  LEU   C N   1 
ATOM   1272 C  CA  . LEU   B 1 25  ? 28.600 -14.893 9.253  1.00 21.24 ? 31  LEU   C CA  1 
ATOM   1273 C  C   . LEU   B 1 25  ? 28.507 -15.256 7.771  1.00 22.10 ? 31  LEU   C C   1 
ATOM   1274 O  O   . LEU   B 1 25  ? 29.280 -14.725 6.968  1.00 23.77 ? 31  LEU   C O   1 
ATOM   1275 C  CB  . LEU   B 1 25  ? 28.020 -13.491 9.473  1.00 21.67 ? 31  LEU   C CB  1 
ATOM   1276 C  CG  . LEU   B 1 25  ? 26.597 -13.254 8.966  1.00 22.38 ? 31  LEU   C CG  1 
ATOM   1277 C  CD1 . LEU   B 1 25  ? 25.599 -14.103 9.738  1.00 23.17 ? 31  LEU   C CD1 1 
ATOM   1278 C  CD2 . LEU   B 1 25  ? 26.234 -11.761 9.088  1.00 23.35 ? 31  LEU   C CD2 1 
ATOM   1279 N  N   . VAL   B 1 26  ? 27.548 -16.123 7.411  1.00 20.85 ? 32  VAL   C N   1 
ATOM   1280 C  CA  . VAL   B 1 26  ? 27.238 -16.495 6.024  1.00 21.36 ? 32  VAL   C CA  1 
ATOM   1281 C  C   . VAL   B 1 26  ? 25.892 -15.865 5.649  1.00 22.09 ? 32  VAL   C C   1 
ATOM   1282 O  O   . VAL   B 1 26  ? 25.768 -15.194 4.621  1.00 22.80 ? 32  VAL   C O   1 
ATOM   1283 C  CB  . VAL   B 1 26  ? 27.208 -18.036 5.831  1.00 21.69 ? 32  VAL   C CB  1 
ATOM   1284 C  CG1 . VAL   B 1 26  ? 26.648 -18.408 4.446  1.00 22.24 ? 32  VAL   C CG1 1 
ATOM   1285 C  CG2 . VAL   B 1 26  ? 28.608 -18.637 6.034  1.00 21.36 ? 32  VAL   C CG2 1 
ATOM   1286 N  N   . TRP   B 1 27  ? 24.899 -16.018 6.528  1.00 21.17 ? 33  TRP   C N   1 
ATOM   1287 C  CA  . TRP   B 1 27  ? 23.557 -15.515 6.271  1.00 21.11 ? 33  TRP   C CA  1 
ATOM   1288 C  C   . TRP   B 1 27  ? 22.794 -15.417 7.569  1.00 21.00 ? 33  TRP   C C   1 
ATOM   1289 O  O   . TRP   B 1 27  ? 22.954 -16.271 8.437  1.00 21.61 ? 33  TRP   C O   1 
ATOM   1290 C  CB  . TRP   B 1 27  ? 22.829 -16.480 5.298  1.00 21.11 ? 33  TRP   C CB  1 
ATOM   1291 C  CG  . TRP   B 1 27  ? 21.349 -16.249 5.101  1.00 21.94 ? 33  TRP   C CG  1 
ATOM   1292 C  CD1 . TRP   B 1 27  ? 20.755 -15.375 4.232  1.00 23.47 ? 33  TRP   C CD1 1 
ATOM   1293 C  CD2 . TRP   B 1 27  ? 20.278 -16.939 5.774  1.00 21.84 ? 33  TRP   C CD2 1 
ATOM   1294 N  NE1 . TRP   B 1 27  ? 19.377 -15.483 4.322  1.00 23.42 ? 33  TRP   C NE1 1 
ATOM   1295 C  CE2 . TRP   B 1 27  ? 19.065 -16.443 5.255  1.00 23.04 ? 33  TRP   C CE2 1 
ATOM   1296 C  CE3 . TRP   B 1 27  ? 20.234 -17.996 6.698  1.00 22.04 ? 33  TRP   C CE3 1 
ATOM   1297 C  CZ2 . TRP   B 1 27  ? 17.819 -16.952 5.654  1.00 23.43 ? 33  TRP   C CZ2 1 
ATOM   1298 C  CZ3 . TRP   B 1 27  ? 18.999 -18.470 7.118  1.00 23.14 ? 33  TRP   C CZ3 1 
ATOM   1299 C  CH2 . TRP   B 1 27  ? 17.814 -17.949 6.601  1.00 23.04 ? 33  TRP   C CH2 1 
ATOM   1300 N  N   . GLU   B 1 28  ? 21.950 -14.402 7.713  1.00 20.40 ? 34  GLU   C N   1 
ATOM   1301 C  CA  . GLU   B 1 28  ? 21.066 -14.319 8.881  1.00 19.31 ? 34  GLU   C CA  1 
ATOM   1302 C  C   . GLU   B 1 28  ? 19.718 -13.730 8.465  1.00 19.01 ? 34  GLU   C C   1 
ATOM   1303 O  O   . GLU   B 1 28  ? 19.658 -12.933 7.512  1.00 18.31 ? 34  GLU   C O   1 
ATOM   1304 C  CB  . GLU   B 1 28  ? 21.703 -13.574 10.077 1.00 19.83 ? 34  GLU   C CB  1 
ATOM   1305 C  CG  . GLU   B 1 28  ? 22.266 -12.189 9.755  1.00 21.58 ? 34  GLU   C CG  1 
ATOM   1306 C  CD  . GLU   B 1 28  ? 21.265 -11.049 9.636  1.00 23.36 ? 34  GLU   C CD  1 
ATOM   1307 O  OE1 . GLU   B 1 28  ? 21.542 -10.102 8.870  1.00 25.19 ? 34  GLU   C OE1 1 
ATOM   1308 O  OE2 . GLU   B 1 28  ? 20.199 -11.099 10.288 1.00 20.96 ? 34  GLU   C OE2 1 
ATOM   1309 N  N   . ASP   B 1 29  ? 18.642 -14.103 9.176  1.00 17.62 ? 35  ASP   C N   1 
ATOM   1310 C  CA  . ASP   B 1 29  ? 17.323 -13.549 8.874  1.00 17.97 ? 35  ASP   C CA  1 
ATOM   1311 C  C   . ASP   B 1 29  ? 16.572 -13.422 10.207 1.00 18.33 ? 35  ASP   C C   1 
ATOM   1312 O  O   . ASP   B 1 29  ? 16.144 -14.423 10.778 1.00 18.02 ? 35  ASP   C O   1 
ATOM   1313 C  CB  . ASP   B 1 29  ? 16.586 -14.431 7.862  1.00 20.08 ? 35  ASP   C CB  1 
ATOM   1314 C  CG  . ASP   B 1 29  ? 15.283 -13.866 7.353  1.00 23.57 ? 35  ASP   C CG  1 
ATOM   1315 O  OD1 . ASP   B 1 29  ? 14.647 -13.098 8.084  1.00 24.87 ? 35  ASP   C OD1 1 
ATOM   1316 O  OD2 . ASP   B 1 29  ? 14.888 -14.217 6.238  1.00 26.30 ? 35  ASP   C OD2 1 
ATOM   1317 N  N   . SER   B 1 30  ? 16.441 -12.173 10.707 1.00 16.93 ? 36  SER   C N   1 
ATOM   1318 C  CA  A SER   B 1 30  ? 15.769 -11.889 11.965 0.50 17.44 ? 36  SER   C CA  1 
ATOM   1319 C  CA  B SER   B 1 30  ? 15.771 -11.920 11.976 0.50 17.53 ? 36  SER   C CA  1 
ATOM   1320 C  C   . SER   B 1 30  ? 14.307 -12.342 11.922 1.00 18.38 ? 36  SER   C C   1 
ATOM   1321 O  O   . SER   B 1 30  ? 13.794 -12.849 12.917 1.00 19.64 ? 36  SER   C O   1 
ATOM   1322 C  CB  A SER   B 1 30  ? 15.875 -10.392 12.281 0.50 18.07 ? 36  SER   C CB  1 
ATOM   1323 C  CB  B SER   B 1 30  ? 15.889 -10.443 12.365 0.50 18.48 ? 36  SER   C CB  1 
ATOM   1324 O  OG  A SER   B 1 30  ? 15.098 -10.023 13.405 0.50 19.63 ? 36  SER   C OG  1 
ATOM   1325 O  OG  B SER   B 1 30  ? 15.178 -9.637  11.442 0.50 20.42 ? 36  SER   C OG  1 
ATOM   1326 N  N   . SER   B 1 31  ? 13.655 -12.206 10.749 1.00 17.58 ? 37  SER   C N   1 
ATOM   1327 C  CA  . SER   B 1 31  ? 12.259 -12.621 10.622 1.00 18.10 ? 37  SER   C CA  1 
ATOM   1328 C  C   . SER   B 1 31  ? 12.088 -14.158 10.790 1.00 18.09 ? 37  SER   C C   1 
ATOM   1329 O  O   . SER   B 1 31  ? 10.989 -14.601 11.082 1.00 18.87 ? 37  SER   C O   1 
ATOM   1330 C  CB  . SER   B 1 31  ? 11.649 -12.127 9.310  1.00 20.50 ? 37  SER   C CB  1 
ATOM   1331 O  OG  . SER   B 1 31  ? 11.960 -12.991 8.226  1.00 24.79 ? 37  SER   C OG  1 
ATOM   1332 N  N   . ARG   B 1 32  ? 13.137 -14.945 10.584 1.00 16.54 ? 38  ARG   C N   1 
ATOM   1333 C  CA  . ARG   B 1 32  ? 13.050 -16.408 10.738 1.00 16.62 ? 38  ARG   C CA  1 
ATOM   1334 C  C   . ARG   B 1 32  ? 13.707 -16.928 12.046 1.00 16.52 ? 38  ARG   C C   1 
ATOM   1335 O  O   . ARG   B 1 32  ? 13.650 -18.133 12.335 1.00 16.65 ? 38  ARG   C O   1 
ATOM   1336 C  CB  . ARG   B 1 32  ? 13.735 -17.117 9.544  1.00 17.76 ? 38  ARG   C CB  1 
ATOM   1337 C  CG  . ARG   B 1 32  ? 13.095 -16.839 8.202  1.00 17.20 ? 38  ARG   C CG  1 
ATOM   1338 C  CD  . ARG   B 1 32  ? 13.821 -17.491 7.026  1.00 17.57 ? 38  ARG   C CD  1 
ATOM   1339 N  NE  . ARG   B 1 32  ? 13.806 -18.951 7.093  1.00 16.37 ? 38  ARG   C NE  1 
ATOM   1340 C  CZ  . ARG   B 1 32  ? 13.844 -19.751 6.030  1.00 18.33 ? 38  ARG   C CZ  1 
ATOM   1341 N  NH1 . ARG   B 1 32  ? 13.885 -19.238 4.796  1.00 17.16 ? 38  ARG   C NH1 1 
ATOM   1342 N  NH2 . ARG   B 1 32  ? 13.784 -21.066 6.183  1.00 19.12 ? 38  ARG   C NH2 1 
ATOM   1343 N  N   . ASP   B 1 33  ? 14.414 -16.048 12.765 1.00 16.49 ? 39  ASP   C N   1 
ATOM   1344 C  CA  . ASP   B 1 33  ? 15.221 -16.372 13.940 1.00 15.67 ? 39  ASP   C CA  1 
ATOM   1345 C  C   . ASP   B 1 33  ? 16.326 -17.354 13.571 1.00 17.15 ? 39  ASP   C C   1 
ATOM   1346 O  O   . ASP   B 1 33  ? 16.635 -18.250 14.358 1.00 17.52 ? 39  ASP   C O   1 
ATOM   1347 C  CB  . ASP   B 1 33  ? 14.377 -16.887 15.138 1.00 15.69 ? 39  ASP   C CB  1 
ATOM   1348 C  CG  . ASP   B 1 33  ? 15.196 -17.222 16.382 1.00 17.30 ? 39  ASP   C CG  1 
ATOM   1349 O  OD1 . ASP   B 1 33  ? 16.114 -16.435 16.721 1.00 15.97 ? 39  ASP   C OD1 1 
ATOM   1350 O  OD2 . ASP   B 1 33  ? 14.945 -18.299 17.011 1.00 17.95 ? 39  ASP   C OD2 1 
ATOM   1351 N  N   . LEU   B 1 34  ? 16.943 -17.203 12.374 1.00 16.66 ? 40  LEU   C N   1 
ATOM   1352 C  CA  . LEU   B 1 34  ? 18.032 -18.096 11.972 1.00 17.27 ? 40  LEU   C CA  1 
ATOM   1353 C  C   . LEU   B 1 34  ? 19.319 -17.342 11.651 1.00 17.85 ? 40  LEU   C C   1 
ATOM   1354 O  O   . LEU   B 1 34  ? 19.297 -16.274 11.039 1.00 17.88 ? 40  LEU   C O   1 
ATOM   1355 C  CB  . LEU   B 1 34  ? 17.689 -18.901 10.707 1.00 16.87 ? 40  LEU   C CB  1 
ATOM   1356 C  CG  . LEU   B 1 34  ? 16.649 -20.014 10.824 1.00 17.79 ? 40  LEU   C CG  1 
ATOM   1357 C  CD1 . LEU   B 1 34  ? 16.453 -20.658 9.436  1.00 17.40 ? 40  LEU   C CD1 1 
ATOM   1358 C  CD2 . LEU   B 1 34  ? 17.077 -21.056 11.878 1.00 19.51 ? 40  LEU   C CD2 1 
ATOM   1359 N  N   . LEU   B 1 35  ? 20.452 -17.999 11.925 1.00 17.15 ? 41  LEU   C N   1 
ATOM   1360 C  CA  . LEU   B 1 35  ? 21.764 -17.475 11.556 1.00 17.47 ? 41  LEU   C CA  1 
ATOM   1361 C  C   . LEU   B 1 35  ? 22.617 -18.680 11.122 1.00 16.94 ? 41  LEU   C C   1 
ATOM   1362 O  O   . LEU   B 1 35  ? 22.558 -19.748 11.735 1.00 16.78 ? 41  LEU   C O   1 
ATOM   1363 C  CB  . LEU   B 1 35  ? 22.435 -16.741 12.729 1.00 17.70 ? 41  LEU   C CB  1 
ATOM   1364 C  CG  . LEU   B 1 35  ? 23.800 -16.105 12.427 1.00 18.43 ? 41  LEU   C CG  1 
ATOM   1365 C  CD1 . LEU   B 1 35  ? 23.956 -14.747 13.127 1.00 18.86 ? 41  LEU   C CD1 1 
ATOM   1366 C  CD2 . LEU   B 1 35  ? 24.950 -17.032 12.859 1.00 19.16 ? 41  LEU   C CD2 1 
ATOM   1367 N  N   . VAL   B 1 36  ? 23.414 -18.502 10.063 1.00 16.95 ? 42  VAL   C N   1 
ATOM   1368 C  CA  . VAL   B 1 36  ? 24.301 -19.542 9.575  1.00 17.26 ? 42  VAL   C CA  1 
ATOM   1369 C  C   . VAL   B 1 36  ? 25.713 -18.953 9.581  1.00 18.59 ? 42  VAL   C C   1 
ATOM   1370 O  O   . VAL   B 1 36  ? 25.933 -17.845 9.066  1.00 18.20 ? 42  VAL   C O   1 
ATOM   1371 C  CB  . VAL   B 1 36  ? 23.915 -20.047 8.154  1.00 17.22 ? 42  VAL   C CB  1 
ATOM   1372 C  CG1 . VAL   B 1 36  ? 24.957 -21.038 7.626  1.00 17.43 ? 42  VAL   C CG1 1 
ATOM   1373 C  CG2 . VAL   B 1 36  ? 22.509 -20.665 8.143  1.00 16.75 ? 42  VAL   C CG2 1 
ATOM   1374 N  N   . SER   B 1 37  ? 26.655 -19.670 10.196 1.00 19.28 ? 43  SER   C N   1 
ATOM   1375 C  CA  . SER   B 1 37  ? 28.071 -19.276 10.223 1.00 19.77 ? 43  SER   C CA  1 
ATOM   1376 C  C   . SER   B 1 37  ? 28.946 -20.380 9.565  1.00 21.94 ? 43  SER   C C   1 
ATOM   1377 O  O   . SER   B 1 37  ? 28.507 -21.526 9.406  1.00 22.09 ? 43  SER   C O   1 
ATOM   1378 C  CB  . SER   B 1 37  ? 28.530 -18.988 11.651 1.00 20.89 ? 43  SER   C CB  1 
ATOM   1379 O  OG  . SER   B 1 37  ? 28.443 -20.142 12.481 1.00 22.97 ? 43  SER   C OG  1 
ATOM   1380 N  N   . SER   B 1 38  ? 30.182 -20.020 9.162  1.00 23.22 ? 44  SER   C N   1 
ATOM   1381 C  CA  . SER   B 1 38  ? 31.061 -20.980 8.509  1.00 24.63 ? 44  SER   C CA  1 
ATOM   1382 C  C   . SER   B 1 38  ? 31.918 -21.708 9.542  1.00 26.25 ? 44  SER   C C   1 
ATOM   1383 O  O   . SER   B 1 38  ? 32.307 -21.133 10.565 1.00 26.27 ? 44  SER   C O   1 
ATOM   1384 C  CB  . SER   B 1 38  ? 31.958 -20.271 7.502  1.00 26.32 ? 44  SER   C CB  1 
ATOM   1385 O  OG  . SER   B 1 38  ? 32.668 -19.230 8.141  1.00 29.52 ? 44  SER   C OG  1 
ATOM   1386 N  N   . THR   B 1 39  ? 32.211 -22.984 9.259  1.00 27.12 ? 45  THR   C N   1 
ATOM   1387 C  CA  . THR   B 1 39  ? 33.032 -23.809 10.135 1.00 29.72 ? 45  THR   C CA  1 
ATOM   1388 C  C   . THR   B 1 39  ? 34.251 -24.323 9.350  1.00 32.64 ? 45  THR   C C   1 
ATOM   1389 O  O   . THR   B 1 39  ? 34.207 -24.403 8.116  1.00 32.87 ? 45  THR   C O   1 
ATOM   1390 C  CB  . THR   B 1 39  ? 32.220 -25.033 10.615 1.00 31.03 ? 45  THR   C CB  1 
ATOM   1391 O  OG1 . THR   B 1 39  ? 31.941 -25.876 9.497  1.00 33.36 ? 45  THR   C OG1 1 
ATOM   1392 C  CG2 . THR   B 1 39  ? 30.922 -24.661 11.285 1.00 30.75 ? 45  THR   C CG2 1 
ATOM   1393 N  N   . THR   B 1 40  ? 35.291 -24.760 10.065 1.00 34.08 ? 46  THR   C N   1 
ATOM   1394 C  CA  . THR   B 1 40  ? 36.454 -25.376 9.434  1.00 36.16 ? 46  THR   C CA  1 
ATOM   1395 C  C   . THR   B 1 40  ? 36.259 -26.906 9.336  1.00 37.28 ? 46  THR   C C   1 
ATOM   1396 O  O   . THR   B 1 40  ? 36.777 -27.529 8.411  1.00 38.47 ? 46  THR   C O   1 
ATOM   1397 C  CB  . THR   B 1 40  ? 37.731 -25.003 10.201 1.00 38.91 ? 46  THR   C CB  1 
ATOM   1398 O  OG1 . THR   B 1 40  ? 37.532 -25.292 11.588 1.00 41.38 ? 46  THR   C OG1 1 
ATOM   1399 C  CG2 . THR   B 1 40  ? 38.069 -23.534 10.053 1.00 39.26 ? 46  THR   C CG2 1 
ATOM   1400 N  N   . ALA   B 1 41  ? 35.521 -27.513 10.288 1.00 36.50 ? 47  ALA   C N   1 
ATOM   1401 C  CA  . ALA   B 1 41  ? 35.273 -28.945 10.296 1.00 36.30 ? 47  ALA   C CA  1 
ATOM   1402 C  C   . ALA   B 1 41  ? 34.026 -29.309 9.487  1.00 36.61 ? 47  ALA   C C   1 
ATOM   1403 O  O   . ALA   B 1 41  ? 33.061 -28.548 9.459  1.00 36.90 ? 47  ALA   C O   1 
ATOM   1404 C  CB  . ALA   B 1 41  ? 35.123 -29.437 11.729 1.00 36.11 ? 47  ALA   C CB  1 
ATOM   1405 N  N   . GLN   B 1 42  ? 34.046 -30.486 8.853  1.00 36.08 ? 48  GLN   C N   1 
ATOM   1406 C  CA  . GLN   B 1 42  ? 32.948 -30.988 8.043  1.00 35.77 ? 48  GLN   C CA  1 
ATOM   1407 C  C   . GLN   B 1 42  ? 31.796 -31.465 8.931  1.00 33.36 ? 48  GLN   C C   1 
ATOM   1408 O  O   . GLN   B 1 42  ? 32.009 -32.264 9.838  1.00 34.10 ? 48  GLN   C O   1 
ATOM   1409 C  CB  . GLN   B 1 42  ? 33.447 -32.152 7.175  1.00 39.63 ? 48  GLN   C CB  1 
ATOM   1410 C  CG  . GLN   B 1 42  ? 32.376 -32.746 6.262  1.00 46.40 ? 48  GLN   C CG  1 
ATOM   1411 C  CD  . GLN   B 1 42  ? 32.101 -31.910 5.035  1.00 54.30 ? 48  GLN   C CD  1 
ATOM   1412 O  OE1 . GLN   B 1 42  ? 32.848 -30.973 4.696  1.00 57.13 ? 48  GLN   C OE1 1 
ATOM   1413 N  NE2 . GLN   B 1 42  ? 31.026 -32.252 4.326  1.00 55.31 ? 48  GLN   C NE2 1 
ATOM   1414 N  N   . GLY   B 1 43  ? 30.591 -30.993 8.627  1.00 30.23 ? 49  GLY   C N   1 
ATOM   1415 C  CA  . GLY   B 1 43  ? 29.368 -31.360 9.334  1.00 28.93 ? 49  GLY   C CA  1 
ATOM   1416 C  C   . GLY   B 1 43  ? 28.668 -32.491 8.617  1.00 28.26 ? 49  GLY   C C   1 
ATOM   1417 O  O   . GLY   B 1 43  ? 28.692 -32.540 7.380  1.00 28.86 ? 49  GLY   C O   1 
ATOM   1418 N  N   . CYS   B 1 44  ? 28.102 -33.449 9.372  1.00 26.84 ? 50  CYS   C N   1 
ATOM   1419 C  CA  . CYS   B 1 44  ? 27.518 -34.624 8.736  1.00 26.97 ? 50  CYS   C CA  1 
ATOM   1420 C  C   . CYS   B 1 44  ? 25.998 -34.749 8.869  1.00 25.87 ? 50  CYS   C C   1 
ATOM   1421 O  O   . CYS   B 1 44  ? 25.480 -35.831 8.570  1.00 25.91 ? 50  CYS   C O   1 
ATOM   1422 C  CB  . CYS   B 1 44  ? 28.219 -35.895 9.200  1.00 28.95 ? 50  CYS   C CB  1 
ATOM   1423 S  SG  . CYS   B 1 44  ? 30.008 -35.901 8.897  1.00 36.49 ? 50  CYS   C SG  1 
ATOM   1424 N  N   . ASP   B 1 45  ? 25.278 -33.683 9.291  1.00 23.83 ? 51  ASP   C N   1 
ATOM   1425 C  CA  . ASP   B 1 45  ? 23.814 -33.768 9.348  1.00 23.98 ? 51  ASP   C CA  1 
ATOM   1426 C  C   . ASP   B 1 45  ? 23.242 -33.742 7.918  1.00 24.17 ? 51  ASP   C C   1 
ATOM   1427 O  O   . ASP   B 1 45  ? 23.803 -33.111 7.013  1.00 23.90 ? 51  ASP   C O   1 
ATOM   1428 C  CB  . ASP   B 1 45  ? 23.184 -32.622 10.178 1.00 24.46 ? 51  ASP   C CB  1 
ATOM   1429 C  CG  . ASP   B 1 45  ? 23.569 -32.637 11.652 1.00 29.00 ? 51  ASP   C CG  1 
ATOM   1430 O  OD1 . ASP   B 1 45  ? 23.955 -33.712 12.155 1.00 30.13 ? 51  ASP   C OD1 1 
ATOM   1431 O  OD2 . ASP   B 1 45  ? 23.507 -31.567 12.299 1.00 28.15 ? 51  ASP   C OD2 1 
ATOM   1432 N  N   . THR   B 1 46  ? 22.154 -34.452 7.717  1.00 23.86 ? 52  THR   C N   1 
ATOM   1433 C  CA  . THR   B 1 46  ? 21.460 -34.499 6.444  1.00 23.76 ? 52  THR   C CA  1 
ATOM   1434 C  C   . THR   B 1 46  ? 20.231 -33.632 6.609  1.00 21.77 ? 52  THR   C C   1 
ATOM   1435 O  O   . THR   B 1 46  ? 19.473 -33.847 7.554  1.00 21.94 ? 52  THR   C O   1 
ATOM   1436 C  CB  . THR   B 1 46  ? 21.008 -35.947 6.140  1.00 26.54 ? 52  THR   C CB  1 
ATOM   1437 O  OG1 . THR   B 1 46  ? 22.173 -36.728 5.836  1.00 29.05 ? 52  THR   C OG1 1 
ATOM   1438 C  CG2 . THR   B 1 46  ? 20.002 -36.024 4.968  1.00 27.14 ? 52  THR   C CG2 1 
ATOM   1439 N  N   . ILE   B 1 47  ? 20.020 -32.685 5.703  1.00 20.04 ? 53  ILE   C N   1 
ATOM   1440 C  CA  . ILE   B 1 47  ? 18.837 -31.836 5.754  1.00 19.48 ? 53  ILE   C CA  1 
ATOM   1441 C  C   . ILE   B 1 47  ? 17.704 -32.516 4.973  1.00 19.23 ? 53  ILE   C C   1 
ATOM   1442 O  O   . ILE   B 1 47  ? 17.942 -33.007 3.854  1.00 19.75 ? 53  ILE   C O   1 
ATOM   1443 C  CB  . ILE   B 1 47  ? 19.129 -30.424 5.140  1.00 20.38 ? 53  ILE   C CB  1 
ATOM   1444 C  CG1 . ILE   B 1 47  ? 20.377 -29.751 5.771  1.00 21.92 ? 53  ILE   C CG1 1 
ATOM   1445 C  CG2 . ILE   B 1 47  ? 17.908 -29.499 5.266  1.00 20.31 ? 53  ILE   C CG2 1 
ATOM   1446 C  CD1 . ILE   B 1 47  ? 20.247 -29.598 7.330  1.00 23.33 ? 53  ILE   C CD1 1 
ATOM   1447 N  N   . ALA   B 1 48  ? 16.490 -32.543 5.535  1.00 17.45 ? 54  ALA   C N   1 
ATOM   1448 C  CA  . ALA   B 1 48  ? 15.346 -33.091 4.820  1.00 17.11 ? 54  ALA   C CA  1 
ATOM   1449 C  C   . ALA   B 1 48  ? 14.958 -32.161 3.665  1.00 16.76 ? 54  ALA   C C   1 
ATOM   1450 O  O   . ALA   B 1 48  ? 15.008 -30.944 3.826  1.00 16.36 ? 54  ALA   C O   1 
ATOM   1451 C  CB  . ALA   B 1 48  ? 14.170 -33.251 5.760  1.00 16.85 ? 54  ALA   C CB  1 
ATOM   1452 N  N   . ARG   B 1 49  ? 14.514 -32.726 2.536  1.00 15.80 ? 55  ARG   C N   1 
ATOM   1453 C  CA  . ARG   B 1 49  ? 14.033 -31.956 1.374  1.00 15.08 ? 55  ARG   C CA  1 
ATOM   1454 C  C   . ARG   B 1 49  ? 12.677 -32.629 1.089  1.00 15.50 ? 55  ARG   C C   1 
ATOM   1455 O  O   . ARG   B 1 49  ? 12.602 -33.606 0.329  1.00 16.35 ? 55  ARG   C O   1 
ATOM   1456 C  CB  . ARG   B 1 49  ? 15.009 -32.097 0.180  1.00 15.71 ? 55  ARG   C CB  1 
ATOM   1457 C  CG  . ARG   B 1 49  ? 16.408 -31.557 0.461  1.00 16.81 ? 55  ARG   C CG  1 
ATOM   1458 C  CD  . ARG   B 1 49  ? 16.463 -30.050 0.861  1.00 18.18 ? 55  ARG   C CD  1 
ATOM   1459 N  NE  . ARG   B 1 49  ? 17.853 -29.641 1.120  1.00 19.14 ? 55  ARG   C NE  1 
ATOM   1460 C  CZ  . ARG   B 1 49  ? 18.218 -28.555 1.803  1.00 21.03 ? 55  ARG   C CZ  1 
ATOM   1461 N  NH1 . ARG   B 1 49  ? 17.303 -27.722 2.282  1.00 17.20 ? 55  ARG   C NH1 1 
ATOM   1462 N  NH2 . ARG   B 1 49  ? 19.505 -28.273 1.976  1.00 23.74 ? 55  ARG   C NH2 1 
ATOM   1463 N  N   . CYS   B 1 50  ? 11.612 -32.140 1.754  1.00 15.59 ? 56  CYS   C N   1 
ATOM   1464 C  CA  . CYS   B 1 50  ? 10.311 -32.805 1.730  1.00 15.88 ? 56  CYS   C CA  1 
ATOM   1465 C  C   . CYS   B 1 50  ? 9.215  -31.864 2.228  1.00 17.46 ? 56  CYS   C C   1 
ATOM   1466 O  O   . CYS   B 1 50  ? 9.502  -30.758 2.692  1.00 17.12 ? 56  CYS   C O   1 
ATOM   1467 C  CB  . CYS   B 1 50  ? 10.404 -34.005 2.675  1.00 15.95 ? 56  CYS   C CB  1 
ATOM   1468 S  SG  . CYS   B 1 50  ? 10.607 -33.516 4.426  1.00 17.76 ? 56  CYS   C SG  1 
ATOM   1469 N  N   . ASP   B 1 51  ? 7.954  -32.353 2.240  1.00 17.78 ? 57  ASP   C N   1 
ATOM   1470 C  CA  . ASP   B 1 51  ? 6.839  -31.615 2.819  1.00 19.42 ? 57  ASP   C CA  1 
ATOM   1471 C  C   . ASP   B 1 51  ? 6.221  -32.390 4.009  1.00 18.22 ? 57  ASP   C C   1 
ATOM   1472 O  O   . ASP   B 1 51  ? 5.021  -32.315 4.247  1.00 18.18 ? 57  ASP   C O   1 
ATOM   1473 C  CB  . ASP   B 1 51  ? 5.773  -31.248 1.777  1.00 20.92 ? 57  ASP   C CB  1 
ATOM   1474 C  CG  . ASP   B 1 51  ? 5.102  -32.418 1.109  1.00 27.06 ? 57  ASP   C CG  1 
ATOM   1475 O  OD1 . ASP   B 1 51  ? 5.485  -33.574 1.396  1.00 26.50 ? 57  ASP   C OD1 1 
ATOM   1476 O  OD2 . ASP   B 1 51  ? 4.179  -32.187 0.308  1.00 32.49 ? 57  ASP   C OD2 1 
ATOM   1477 N  N   . CYS   B 1 52  ? 7.030  -33.175 4.729  1.00 17.03 ? 58  CYS   C N   1 
ATOM   1478 C  CA  . CYS   B 1 52  ? 6.584  -33.925 5.909  1.00 16.03 ? 58  CYS   C CA  1 
ATOM   1479 C  C   . CYS   B 1 52  ? 5.907  -33.035 6.917  1.00 15.41 ? 58  CYS   C C   1 
ATOM   1480 O  O   . CYS   B 1 52  ? 6.293  -31.879 7.095  1.00 15.65 ? 58  CYS   C O   1 
ATOM   1481 C  CB  . CYS   B 1 52  ? 7.757  -34.651 6.571  1.00 16.63 ? 58  CYS   C CB  1 
ATOM   1482 S  SG  . CYS   B 1 52  ? 8.269  -36.165 5.716  1.00 19.81 ? 58  CYS   C SG  1 
ATOM   1483 N  N   . GLN   B 1 53  ? 4.892  -33.579 7.581  1.00 15.03 ? 59  GLN   C N   1 
ATOM   1484 C  CA  . GLN   B 1 53  ? 4.221  -32.900 8.675  1.00 15.48 ? 59  GLN   C CA  1 
ATOM   1485 C  C   . GLN   B 1 53  ? 4.191  -33.781 9.938  1.00 16.89 ? 59  GLN   C C   1 
ATOM   1486 O  O   . GLN   B 1 53  ? 3.367  -33.536 10.816 1.00 17.24 ? 59  GLN   C O   1 
ATOM   1487 C  CB  . GLN   B 1 53  ? 2.792  -32.496 8.288  1.00 15.12 ? 59  GLN   C CB  1 
ATOM   1488 C  CG  . GLN   B 1 53  ? 2.756  -31.167 7.500  1.00 14.22 ? 59  GLN   C CG  1 
ATOM   1489 C  CD  . GLN   B 1 53  ? 1.314  -30.828 7.225  1.00 20.26 ? 59  GLN   C CD  1 
ATOM   1490 O  OE1 . GLN   B 1 53  ? 0.797  -31.082 6.120  1.00 21.17 ? 59  GLN   C OE1 1 
ATOM   1491 N  NE2 . GLN   B 1 53  ? 0.632  -30.336 8.258  1.00 18.38 ? 59  GLN   C NE2 1 
ATOM   1492 N  N   . THR   B 1 54  ? 5.024  -34.837 10.007 1.00 17.61 ? 60  THR   C N   1 
ATOM   1493 C  CA  . THR   B 1 54  ? 5.172  -35.672 11.210 1.00 18.33 ? 60  THR   C CA  1 
ATOM   1494 C  C   . THR   B 1 54  ? 6.677  -35.827 11.397 1.00 18.32 ? 60  THR   C C   1 
ATOM   1495 O  O   . THR   B 1 54  ? 7.437  -35.902 10.419 1.00 18.88 ? 60  THR   C O   1 
ATOM   1496 C  CB  . THR   B 1 54  ? 4.465  -37.036 11.116 1.00 22.35 ? 60  THR   C CB  1 
ATOM   1497 O  OG1 . THR   B 1 54  ? 5.070  -37.806 10.085 1.00 25.39 ? 60  THR   C OG1 1 
ATOM   1498 C  CG2 . THR   B 1 54  ? 2.978  -36.921 10.770 1.00 22.63 ? 60  THR   C CG2 1 
ATOM   1499 N  N   . GLY   B 1 55  ? 7.107  -35.855 12.643 1.00 17.56 ? 61  GLY   C N   1 
ATOM   1500 C  CA  . GLY   B 1 55  ? 8.533  -35.966 12.948 1.00 16.58 ? 61  GLY   C CA  1 
ATOM   1501 C  C   . GLY   B 1 55  ? 8.761  -36.130 14.434 1.00 16.31 ? 61  GLY   C C   1 
ATOM   1502 O  O   . GLY   B 1 55  ? 7.821  -36.384 15.177 1.00 16.68 ? 61  GLY   C O   1 
ATOM   1503 N  N   . VAL   B 1 56  ? 10.009 -36.025 14.875 1.00 16.45 ? 62  VAL   C N   1 
ATOM   1504 C  CA  . VAL   B 1 56  ? 10.382 -36.191 16.296 1.00 16.97 ? 62  VAL   C CA  1 
ATOM   1505 C  C   . VAL   B 1 56  ? 11.307 -35.034 16.687 1.00 15.95 ? 62  VAL   C C   1 
ATOM   1506 O  O   . VAL   B 1 56  ? 12.242 -34.751 15.950 1.00 14.97 ? 62  VAL   C O   1 
ATOM   1507 C  CB  . VAL   B 1 56  ? 11.110 -37.548 16.510 1.00 18.23 ? 62  VAL   C CB  1 
ATOM   1508 C  CG1 . VAL   B 1 56  ? 11.600 -37.710 17.959 1.00 18.98 ? 62  VAL   C CG1 1 
ATOM   1509 C  CG2 . VAL   B 1 56  ? 10.244 -38.720 16.078 1.00 18.89 ? 62  VAL   C CG2 1 
ATOM   1510 N  N   . TYR   B 1 57  ? 11.060 -34.353 17.829 1.00 15.43 ? 63  TYR   C N   1 
ATOM   1511 C  CA  . TYR   B 1 57  ? 11.970 -33.282 18.267 1.00 15.75 ? 63  TYR   C CA  1 
ATOM   1512 C  C   . TYR   B 1 57  ? 12.587 -33.568 19.628 1.00 16.54 ? 63  TYR   C C   1 
ATOM   1513 O  O   . TYR   B 1 57  ? 11.981 -34.274 20.437 1.00 16.15 ? 63  TYR   C O   1 
ATOM   1514 C  CB  . TYR   B 1 57  ? 11.288 -31.885 18.278 1.00 14.84 ? 63  TYR   C CB  1 
ATOM   1515 C  CG  . TYR   B 1 57  ? 10.374 -31.643 19.461 1.00 15.91 ? 63  TYR   C CG  1 
ATOM   1516 C  CD1 . TYR   B 1 57  ? 9.082  -32.152 19.480 1.00 17.05 ? 63  TYR   C CD1 1 
ATOM   1517 C  CD2 . TYR   B 1 57  ? 10.761 -30.807 20.506 1.00 17.06 ? 63  TYR   C CD2 1 
ATOM   1518 C  CE1 . TYR   B 1 57  ? 8.200  -31.847 20.512 1.00 18.74 ? 63  TYR   C CE1 1 
ATOM   1519 C  CE2 . TYR   B 1 57  ? 9.902  -30.528 21.568 1.00 18.23 ? 63  TYR   C CE2 1 
ATOM   1520 C  CZ  . TYR   B 1 57  ? 8.621  -31.049 21.566 1.00 19.94 ? 63  TYR   C CZ  1 
ATOM   1521 O  OH  . TYR   B 1 57  ? 7.763  -30.754 22.605 1.00 21.01 ? 63  TYR   C OH  1 
ATOM   1522 N  N   . TYR   B 1 58  ? 13.766 -32.991 19.901 1.00 16.90 ? 64  TYR   C N   1 
ATOM   1523 C  CA  . TYR   B 1 58  ? 14.388 -33.143 21.206 1.00 16.62 ? 64  TYR   C CA  1 
ATOM   1524 C  C   . TYR   B 1 58  ? 13.982 -31.975 22.104 1.00 16.67 ? 64  TYR   C C   1 
ATOM   1525 O  O   . TYR   B 1 58  ? 14.137 -30.822 21.721 1.00 17.41 ? 64  TYR   C O   1 
ATOM   1526 C  CB  . TYR   B 1 58  ? 15.924 -33.199 21.107 1.00 17.25 ? 64  TYR   C CB  1 
ATOM   1527 C  CG  . TYR   B 1 58  ? 16.543 -33.383 22.479 1.00 19.27 ? 64  TYR   C CG  1 
ATOM   1528 C  CD1 . TYR   B 1 58  ? 16.355 -34.559 23.198 1.00 20.41 ? 64  TYR   C CD1 1 
ATOM   1529 C  CD2 . TYR   B 1 58  ? 17.289 -32.371 23.073 1.00 21.13 ? 64  TYR   C CD2 1 
ATOM   1530 C  CE1 . TYR   B 1 58  ? 16.905 -34.734 24.473 1.00 21.57 ? 64  TYR   C CE1 1 
ATOM   1531 C  CE2 . TYR   B 1 58  ? 17.832 -32.530 24.350 1.00 22.16 ? 64  TYR   C CE2 1 
ATOM   1532 C  CZ  . TYR   B 1 58  ? 17.651 -33.722 25.036 1.00 23.20 ? 64  TYR   C CZ  1 
ATOM   1533 O  OH  . TYR   B 1 58  ? 18.169 -33.881 26.295 1.00 25.84 ? 64  TYR   C OH  1 
ATOM   1534 N  N   . CYS   B 1 59  ? 13.444 -32.303 23.296 1.00 16.61 ? 65  CYS   C N   1 
ATOM   1535 C  CA  . CYS   B 1 59  ? 13.010 -31.339 24.322 1.00 15.87 ? 65  CYS   C CA  1 
ATOM   1536 C  C   . CYS   B 1 59  ? 13.982 -31.396 25.520 1.00 16.63 ? 65  CYS   C C   1 
ATOM   1537 O  O   . CYS   B 1 59  ? 13.858 -32.282 26.368 1.00 17.09 ? 65  CYS   C O   1 
ATOM   1538 C  CB  . CYS   B 1 59  ? 11.593 -31.672 24.749 1.00 15.91 ? 65  CYS   C CB  1 
ATOM   1539 S  SG  . CYS   B 1 59  ? 10.952 -30.585 26.030 1.00 19.04 ? 65  CYS   C SG  1 
ATOM   1540 N  N   . SER   B 1 60  ? 14.955 -30.470 25.588 1.00 17.16 ? 66  SER   C N   1 
ATOM   1541 C  CA  . SER   B 1 60  ? 15.933 -30.509 26.683 1.00 19.89 ? 66  SER   C CA  1 
ATOM   1542 C  C   . SER   B 1 60  ? 15.326 -30.305 28.068 1.00 20.24 ? 66  SER   C C   1 
ATOM   1543 O  O   . SER   B 1 60  ? 15.809 -30.911 29.036 1.00 21.69 ? 66  SER   C O   1 
ATOM   1544 C  CB  . SER   B 1 60  ? 17.085 -29.538 26.459 1.00 24.71 ? 66  SER   C CB  1 
ATOM   1545 O  OG  . SER   B 1 60  ? 16.585 -28.222 26.391 1.00 30.83 ? 66  SER   C OG  1 
ATOM   1546 N  N   . SER   B 1 61  ? 14.207 -29.567 28.172 1.00 19.76 ? 67  SER   C N   1 
ATOM   1547 C  CA  . SER   B 1 61  ? 13.559 -29.358 29.487 1.00 19.98 ? 67  SER   C CA  1 
ATOM   1548 C  C   . SER   B 1 61  ? 12.829 -30.598 30.051 1.00 20.29 ? 67  SER   C C   1 
ATOM   1549 O  O   . SER   B 1 61  ? 12.318 -30.582 31.178 1.00 20.68 ? 67  SER   C O   1 
ATOM   1550 C  CB  . SER   B 1 61  ? 12.622 -28.163 29.451 1.00 19.63 ? 67  SER   C CB  1 
ATOM   1551 O  OG  . SER   B 1 61  ? 11.550 -28.391 28.557 1.00 21.08 ? 67  SER   C OG  1 
ATOM   1552 N  N   . ARG   B 1 62  ? 12.784 -31.677 29.268 1.00 19.64 ? 68  ARG   C N   1 
ATOM   1553 C  CA  . ARG   B 1 62  ? 12.246 -32.973 29.689 1.00 18.95 ? 68  ARG   C CA  1 
ATOM   1554 C  C   . ARG   B 1 62  ? 13.284 -34.112 29.453 1.00 20.55 ? 68  ARG   C C   1 
ATOM   1555 O  O   . ARG   B 1 62  ? 12.989 -35.269 29.769 1.00 21.25 ? 68  ARG   C O   1 
ATOM   1556 C  CB  . ARG   B 1 62  ? 10.966 -33.289 28.885 1.00 18.79 ? 68  ARG   C CB  1 
ATOM   1557 C  CG  . ARG   B 1 62  ? 9.810  -32.348 29.174 1.00 20.11 ? 68  ARG   C CG  1 
ATOM   1558 C  CD  . ARG   B 1 62  ? 9.179  -32.640 30.527 1.00 23.90 ? 68  ARG   C CD  1 
ATOM   1559 N  NE  . ARG   B 1 62  ? 8.064  -31.742 30.820 1.00 28.44 ? 68  ARG   C NE  1 
ATOM   1560 C  CZ  . ARG   B 1 62  ? 8.172  -30.598 31.487 1.00 31.33 ? 68  ARG   C CZ  1 
ATOM   1561 N  NH1 . ARG   B 1 62  ? 9.362  -30.169 31.902 1.00 31.44 ? 68  ARG   C NH1 1 
ATOM   1562 N  NH2 . ARG   B 1 62  ? 7.095  -29.864 31.730 1.00 32.60 ? 68  ARG   C NH2 1 
ATOM   1563 N  N   . ARG   B 1 63  ? 14.466 -33.809 28.851 1.00 20.69 ? 69  ARG   C N   1 
ATOM   1564 C  CA  . ARG   B 1 63  ? 15.505 -34.784 28.488 1.00 22.47 ? 69  ARG   C CA  1 
ATOM   1565 C  C   . ARG   B 1 63  ? 14.877 -35.917 27.671 1.00 23.54 ? 69  ARG   C C   1 
ATOM   1566 O  O   . ARG   B 1 63  ? 15.119 -37.096 27.949 1.00 24.67 ? 69  ARG   C O   1 
ATOM   1567 C  CB  . ARG   B 1 63  ? 16.193 -35.322 29.751 1.00 26.14 ? 69  ARG   C CB  1 
ATOM   1568 C  CG  . ARG   B 1 63  ? 17.297 -34.418 30.241 1.00 31.94 ? 69  ARG   C CG  1 
ATOM   1569 C  CD  . ARG   B 1 63  ? 18.245 -35.155 31.155 1.00 40.71 ? 69  ARG   C CD  1 
ATOM   1570 N  NE  . ARG   B 1 63  ? 18.830 -34.239 32.132 1.00 47.64 ? 69  ARG   C NE  1 
ATOM   1571 C  CZ  . ARG   B 1 63  ? 18.549 -34.248 33.430 1.00 53.14 ? 69  ARG   C CZ  1 
ATOM   1572 N  NH1 . ARG   B 1 63  ? 17.705 -35.145 33.931 1.00 54.03 ? 69  ARG   C NH1 1 
ATOM   1573 N  NH2 . ARG   B 1 63  ? 19.115 -33.364 34.243 1.00 54.32 ? 69  ARG   C NH2 1 
ATOM   1574 N  N   . LYS   B 1 64  ? 13.976 -35.559 26.735 1.00 22.93 ? 70  LYS   C N   1 
ATOM   1575 C  CA  . LYS   B 1 64  ? 13.231 -36.572 25.991 1.00 23.39 ? 70  LYS   C CA  1 
ATOM   1576 C  C   . LYS   B 1 64  ? 12.998 -36.135 24.552 1.00 20.96 ? 70  LYS   C C   1 
ATOM   1577 O  O   . LYS   B 1 64  ? 12.894 -34.937 24.288 1.00 20.20 ? 70  LYS   C O   1 
ATOM   1578 C  CB  . LYS   B 1 64  ? 11.810 -36.709 26.615 1.00 27.13 ? 70  LYS   C CB  1 
ATOM   1579 C  CG  . LYS   B 1 64  ? 11.622 -37.781 27.672 1.00 36.67 ? 70  LYS   C CG  1 
ATOM   1580 C  CD  . LYS   B 1 64  ? 10.142 -37.834 28.050 1.00 43.20 ? 70  LYS   C CD  1 
ATOM   1581 C  CE  . LYS   B 1 64  ? 9.754  -39.067 28.841 1.00 49.35 ? 70  LYS   C CE  1 
ATOM   1582 N  NZ  . LYS   B 1 64  ? 10.200 -38.989 30.265 1.00 52.17 ? 70  LYS   C NZ  1 
ATOM   1583 N  N   . HIS   B 1 65  ? 12.757 -37.116 23.661 1.00 19.44 ? 71  HIS   C N   1 
ATOM   1584 C  CA  . HIS   B 1 65  ? 12.329 -36.864 22.300 1.00 18.55 ? 71  HIS   C CA  1 
ATOM   1585 C  C   . HIS   B 1 65  ? 10.820 -37.115 22.272 1.00 19.09 ? 71  HIS   C C   1 
ATOM   1586 O  O   . HIS   B 1 65  ? 10.327 -38.063 22.916 1.00 21.03 ? 71  HIS   C O   1 
ATOM   1587 C  CB  . HIS   B 1 65  ? 13.036 -37.804 21.288 1.00 18.73 ? 71  HIS   C CB  1 
ATOM   1588 C  CG  . HIS   B 1 65  ? 14.516 -37.610 21.205 1.00 19.24 ? 71  HIS   C CG  1 
ATOM   1589 N  ND1 . HIS   B 1 65  ? 15.096 -36.852 20.194 1.00 22.82 ? 71  HIS   C ND1 1 
ATOM   1590 C  CD2 . HIS   B 1 65  ? 15.494 -38.086 21.995 1.00 19.83 ? 71  HIS   C CD2 1 
ATOM   1591 C  CE1 . HIS   B 1 65  ? 16.400 -36.915 20.398 1.00 21.08 ? 71  HIS   C CE1 1 
ATOM   1592 N  NE2 . HIS   B 1 65  ? 16.688 -37.645 21.459 1.00 20.96 ? 71  HIS   C NE2 1 
ATOM   1593 N  N   . TYR   B 1 66  ? 10.080 -36.300 21.518 1.00 16.84 ? 72  TYR   C N   1 
ATOM   1594 C  CA  . TYR   B 1 66  ? 8.631  -36.457 21.377 1.00 17.39 ? 72  TYR   C CA  1 
ATOM   1595 C  C   . TYR   B 1 66  ? 8.228  -36.519 19.928 1.00 17.93 ? 72  TYR   C C   1 
ATOM   1596 O  O   . TYR   B 1 66  ? 8.671  -35.678 19.122 1.00 18.31 ? 72  TYR   C O   1 
ATOM   1597 C  CB  . TYR   B 1 66  ? 7.872  -35.277 21.987 1.00 18.10 ? 72  TYR   C CB  1 
ATOM   1598 C  CG  . TYR   B 1 66  ? 7.942  -35.189 23.488 1.00 19.22 ? 72  TYR   C CG  1 
ATOM   1599 C  CD1 . TYR   B 1 66  ? 7.170  -36.023 24.288 1.00 20.58 ? 72  TYR   C CD1 1 
ATOM   1600 C  CD2 . TYR   B 1 66  ? 8.752  -34.247 24.115 1.00 20.28 ? 72  TYR   C CD2 1 
ATOM   1601 C  CE1 . TYR   B 1 66  ? 7.225  -35.940 25.678 1.00 22.14 ? 72  TYR   C CE1 1 
ATOM   1602 C  CE2 . TYR   B 1 66  ? 8.807  -34.151 25.499 1.00 21.77 ? 72  TYR   C CE2 1 
ATOM   1603 C  CZ  . TYR   B 1 66  ? 8.039  -34.997 26.278 1.00 23.83 ? 72  TYR   C CZ  1 
ATOM   1604 O  OH  . TYR   B 1 66  ? 8.112  -34.900 27.651 1.00 26.68 ? 72  TYR   C OH  1 
ATOM   1605 N  N   . PRO   B 1 67  ? 7.380  -37.506 19.588 1.00 18.58 ? 73  PRO   C N   1 
ATOM   1606 C  CA  . PRO   B 1 67  ? 6.870  -37.578 18.210 1.00 19.08 ? 73  PRO   C CA  1 
ATOM   1607 C  C   . PRO   B 1 67  ? 5.744  -36.544 18.047 1.00 18.79 ? 73  PRO   C C   1 
ATOM   1608 O  O   . PRO   B 1 67  ? 4.880  -36.468 18.923 1.00 18.63 ? 73  PRO   C O   1 
ATOM   1609 C  CB  . PRO   B 1 67  ? 6.380  -39.029 18.096 1.00 19.88 ? 73  PRO   C CB  1 
ATOM   1610 C  CG  . PRO   B 1 67  ? 5.982  -39.410 19.499 1.00 21.14 ? 73  PRO   C CG  1 
ATOM   1611 C  CD  . PRO   B 1 67  ? 6.852  -38.602 20.446 1.00 18.86 ? 73  PRO   C CD  1 
ATOM   1612 N  N   . VAL   B 1 68  ? 5.767  -35.718 16.987 1.00 17.59 ? 74  VAL   C N   1 
ATOM   1613 C  CA  . VAL   B 1 68  ? 4.706  -34.710 16.806 1.00 17.85 ? 74  VAL   C CA  1 
ATOM   1614 C  C   . VAL   B 1 68  ? 4.237  -34.608 15.359 1.00 17.25 ? 74  VAL   C C   1 
ATOM   1615 O  O   . VAL   B 1 68  ? 4.984  -34.932 14.451 1.00 17.52 ? 74  VAL   C O   1 
ATOM   1616 C  CB  . VAL   B 1 68  ? 5.173  -33.290 17.253 1.00 18.96 ? 74  VAL   C CB  1 
ATOM   1617 C  CG1 . VAL   B 1 68  ? 5.201  -33.154 18.765 1.00 20.26 ? 74  VAL   C CG1 1 
ATOM   1618 C  CG2 . VAL   B 1 68  ? 6.522  -32.924 16.629 1.00 18.85 ? 74  VAL   C CG2 1 
ATOM   1619 N  N   . SER   B 1 69  ? 3.005  -34.153 15.163 1.00 15.89 ? 75  SER   C N   1 
ATOM   1620 C  CA  . SER   B 1 69  ? 2.501  -33.671 13.882 1.00 16.37 ? 75  SER   C CA  1 
ATOM   1621 C  C   . SER   B 1 69  ? 2.785  -32.146 13.946 1.00 16.41 ? 75  SER   C C   1 
ATOM   1622 O  O   . SER   B 1 69  ? 2.685  -31.519 15.029 1.00 17.06 ? 75  SER   C O   1 
ATOM   1623 C  CB  . SER   B 1 69  ? 0.985  -33.858 13.764 1.00 18.61 ? 75  SER   C CB  1 
ATOM   1624 O  OG  . SER   B 1 69  ? 0.680  -35.225 13.595 1.00 23.40 ? 75  SER   C OG  1 
ATOM   1625 N  N   . PHE   B 1 70  ? 3.117  -31.539 12.796 1.00 15.30 ? 76  PHE   C N   1 
ATOM   1626 C  CA  . PHE   B 1 70  ? 3.428  -30.124 12.778 1.00 15.41 ? 76  PHE   C CA  1 
ATOM   1627 C  C   . PHE   B 1 70  ? 2.849  -29.454 11.544 1.00 16.53 ? 76  PHE   C C   1 
ATOM   1628 O  O   . PHE   B 1 70  ? 2.583  -30.111 10.538 1.00 17.19 ? 76  PHE   C O   1 
ATOM   1629 C  CB  . PHE   B 1 70  ? 4.948  -29.888 12.971 1.00 13.77 ? 76  PHE   C CB  1 
ATOM   1630 C  CG  . PHE   B 1 70  ? 5.871  -30.603 12.000 1.00 14.26 ? 76  PHE   C CG  1 
ATOM   1631 C  CD1 . PHE   B 1 70  ? 6.334  -31.882 12.265 1.00 15.07 ? 76  PHE   C CD1 1 
ATOM   1632 C  CD2 . PHE   B 1 70  ? 6.325  -29.966 10.853 1.00 14.32 ? 76  PHE   C CD2 1 
ATOM   1633 C  CE1 . PHE   B 1 70  ? 7.242  -32.507 11.393 1.00 15.72 ? 76  PHE   C CE1 1 
ATOM   1634 C  CE2 . PHE   B 1 70  ? 7.187  -30.601 9.975  1.00 14.59 ? 76  PHE   C CE2 1 
ATOM   1635 C  CZ  . PHE   B 1 70  ? 7.663  -31.854 10.257 1.00 15.42 ? 76  PHE   C CZ  1 
ATOM   1636 N  N   . SER   B 1 71  ? 2.653  -28.141 11.616 1.00 16.90 ? 77  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 71  ? 2.016  -27.402 10.532 1.00 17.91 ? 77  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 71  ? 2.940  -27.099 9.349  1.00 19.13 ? 77  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 71  ? 4.136  -27.410 9.384  1.00 18.81 ? 77  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 71  ? 1.375  -26.122 11.085 1.00 17.70 ? 77  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 71  ? 2.339  -25.142 11.452 1.00 18.99 ? 77  SER   C OG  1 
ATOM   1642 N  N   . LYS   B 1 72  ? 2.386  -26.484 8.285  1.00 18.78 ? 78  LYS   C N   1 
ATOM   1643 C  CA  . LYS   B 1 72  ? 3.182  -26.044 7.139  1.00 19.37 ? 78  LYS   C CA  1 
ATOM   1644 C  C   . LYS   B 1 72  ? 3.894  -24.725 7.499  1.00 20.00 ? 78  LYS   C C   1 
ATOM   1645 O  O   . LYS   B 1 72  ? 3.326  -23.914 8.233  1.00 21.06 ? 78  LYS   C O   1 
ATOM   1646 C  CB  . LYS   B 1 72  ? 2.245  -25.801 5.940  1.00 22.70 ? 78  LYS   C CB  1 
ATOM   1647 C  CG  . LYS   B 1 72  ? 1.607  -27.093 5.433  1.00 27.54 ? 78  LYS   C CG  1 
ATOM   1648 C  CD  . LYS   B 1 72  ? 1.029  -26.865 4.047  1.00 35.51 ? 78  LYS   C CD  1 
ATOM   1649 C  CE  . LYS   B 1 72  ? 0.555  -28.131 3.387  1.00 44.12 ? 78  LYS   C CE  1 
ATOM   1650 N  NZ  . LYS   B 1 72  ? 1.670  -28.856 2.686  1.00 49.92 ? 78  LYS   C NZ  1 
ATOM   1651 N  N   . PRO   B 1 73  ? 5.099  -24.479 6.973  1.00 19.66 ? 79  PRO   C N   1 
ATOM   1652 C  CA  . PRO   B 1 73  ? 5.820  -23.222 7.294  1.00 19.71 ? 79  PRO   C CA  1 
ATOM   1653 C  C   . PRO   B 1 73  ? 5.002  -21.982 6.958  1.00 20.69 ? 79  PRO   C C   1 
ATOM   1654 O  O   . PRO   B 1 73  ? 4.398  -21.901 5.882  1.00 20.54 ? 79  PRO   C O   1 
ATOM   1655 C  CB  . PRO   B 1 73  ? 7.090  -23.293 6.433  1.00 20.69 ? 79  PRO   C CB  1 
ATOM   1656 C  CG  . PRO   B 1 73  ? 7.255  -24.736 6.088  1.00 21.67 ? 79  PRO   C CG  1 
ATOM   1657 C  CD  . PRO   B 1 73  ? 5.870  -25.330 6.042  1.00 19.27 ? 79  PRO   C CD  1 
ATOM   1658 N  N   . SER   B 1 74  ? 4.853  -21.075 7.941  1.00 21.29 ? 80  SER   C N   1 
ATOM   1659 C  CA  . SER   B 1 74  ? 3.984  -19.919 7.745  1.00 22.09 ? 80  SER   C CA  1 
ATOM   1660 C  C   . SER   B 1 74  ? 4.390  -18.739 8.626  1.00 21.36 ? 80  SER   C C   1 
ATOM   1661 O  O   . SER   B 1 74  ? 5.353  -18.845 9.404  1.00 20.60 ? 80  SER   C O   1 
ATOM   1662 C  CB  . SER   B 1 74  ? 2.527  -20.328 7.977  1.00 26.04 ? 80  SER   C CB  1 
ATOM   1663 O  OG  . SER   B 1 74  ? 2.290  -20.560 9.357  1.00 29.98 ? 80  SER   C OG  1 
ATOM   1664 N  N   . LEU   B 1 75  ? 3.727  -17.575 8.410  1.00 20.68 ? 81  LEU   C N   1 
ATOM   1665 C  CA  . LEU   B 1 75  ? 3.973  -16.305 9.092  1.00 22.19 ? 81  LEU   C CA  1 
ATOM   1666 C  C   . LEU   B 1 75  ? 3.090  -16.320 10.320 1.00 22.47 ? 81  LEU   C C   1 
ATOM   1667 O  O   . LEU   B 1 75  ? 1.853  -16.365 10.170 1.00 22.43 ? 81  LEU   C O   1 
ATOM   1668 C  CB  . LEU   B 1 75  ? 3.473  -15.163 8.160  1.00 23.44 ? 81  LEU   C CB  1 
ATOM   1669 C  CG  . LEU   B 1 75  ? 4.385  -14.036 7.647  1.00 27.69 ? 81  LEU   C CG  1 
ATOM   1670 C  CD1 . LEU   B 1 75  ? 3.572  -12.792 7.310  1.00 29.71 ? 81  LEU   C CD1 1 
ATOM   1671 C  CD2 . LEU   B 1 75  ? 5.535  -13.741 8.506  1.00 27.64 ? 81  LEU   C CD2 1 
ATOM   1672 N  N   . ILE   B 1 76  ? 3.690  -16.338 11.527 1.00 21.80 ? 82  ILE   C N   1 
ATOM   1673 C  CA  . ILE   B 1 76  ? 2.958  -16.441 12.801 1.00 22.45 ? 82  ILE   C CA  1 
ATOM   1674 C  C   . ILE   B 1 76  ? 3.349  -15.330 13.784 1.00 22.80 ? 82  ILE   C C   1 
ATOM   1675 O  O   . ILE   B 1 76  ? 4.540  -15.082 13.963 1.00 22.09 ? 82  ILE   C O   1 
ATOM   1676 C  CB  . ILE   B 1 76  ? 3.262  -17.851 13.392 1.00 24.22 ? 82  ILE   C CB  1 
ATOM   1677 C  CG1 . ILE   B 1 76  ? 2.574  -18.946 12.538 1.00 26.32 ? 82  ILE   C CG1 1 
ATOM   1678 C  CG2 . ILE   B 1 76  ? 2.860  -17.964 14.869 1.00 25.63 ? 82  ILE   C CG2 1 
ATOM   1679 C  CD1 . ILE   B 1 76  ? 3.092  -20.292 12.732 1.00 28.83 ? 82  ILE   C CD1 1 
ATOM   1680 N  N   . PHE   B 1 77  ? 2.369  -14.690 14.451 1.00 22.85 ? 83  PHE   C N   1 
ATOM   1681 C  CA  . PHE   B 1 77  ? 2.681  -13.631 15.413 1.00 24.55 ? 83  PHE   C CA  1 
ATOM   1682 C  C   . PHE   B 1 77  ? 3.411  -14.170 16.654 1.00 24.56 ? 83  PHE   C C   1 
ATOM   1683 O  O   . PHE   B 1 77  ? 3.005  -15.181 17.223 1.00 24.88 ? 83  PHE   C O   1 
ATOM   1684 C  CB  . PHE   B 1 77  ? 1.410  -12.854 15.828 1.00 25.58 ? 83  PHE   C CB  1 
ATOM   1685 C  CG  . PHE   B 1 77  ? 1.681  -11.696 16.759 1.00 26.49 ? 83  PHE   C CG  1 
ATOM   1686 C  CD1 . PHE   B 1 77  ? 1.465  -11.814 18.117 1.00 27.82 ? 83  PHE   C CD1 1 
ATOM   1687 C  CD2 . PHE   B 1 77  ? 2.230  -10.519 16.284 1.00 27.69 ? 83  PHE   C CD2 1 
ATOM   1688 C  CE1 . PHE   B 1 77  ? 1.739  -10.747 18.979 1.00 29.01 ? 83  PHE   C CE1 1 
ATOM   1689 C  CE2 . PHE   B 1 77  ? 2.508  -9.461  17.144 1.00 28.88 ? 83  PHE   C CE2 1 
ATOM   1690 C  CZ  . PHE   B 1 77  ? 2.272  -9.587  18.487 1.00 28.57 ? 83  PHE   C CZ  1 
ATOM   1691 N  N   . VAL   B 1 78  ? 4.525  -13.532 17.024 1.00 23.92 ? 84  VAL   C N   1 
ATOM   1692 C  CA  . VAL   B 1 78  ? 5.328  -13.890 18.198 1.00 23.12 ? 84  VAL   C CA  1 
ATOM   1693 C  C   . VAL   B 1 78  ? 5.472  -12.635 19.091 1.00 24.69 ? 84  VAL   C C   1 
ATOM   1694 O  O   . VAL   B 1 78  ? 5.916  -11.586 18.621 1.00 25.25 ? 84  VAL   C O   1 
ATOM   1695 C  CB  . VAL   B 1 78  ? 6.734  -14.418 17.814 1.00 22.21 ? 84  VAL   C CB  1 
ATOM   1696 C  CG1 . VAL   B 1 78  ? 7.534  -14.807 19.072 1.00 22.78 ? 84  VAL   C CG1 1 
ATOM   1697 C  CG2 . VAL   B 1 78  ? 6.646  -15.615 16.859 1.00 21.58 ? 84  VAL   C CG2 1 
ATOM   1698 N  N   . GLU   B 1 79  ? 5.171  -12.768 20.373 1.00 25.64 ? 85  GLU   C N   1 
ATOM   1699 C  CA  . GLU   B 1 79  ? 5.230  -11.711 21.372 1.00 27.27 ? 85  GLU   C CA  1 
ATOM   1700 C  C   . GLU   B 1 79  ? 6.634  -11.194 21.561 1.00 27.39 ? 85  GLU   C C   1 
ATOM   1701 O  O   . GLU   B 1 79  ? 7.591  -11.952 21.379 1.00 27.92 ? 85  GLU   C O   1 
ATOM   1702 C  CB  . GLU   B 1 79  ? 4.768  -12.287 22.721 1.00 32.35 ? 85  GLU   C CB  1 
ATOM   1703 C  CG  . GLU   B 1 79  ? 3.386  -12.910 22.677 1.00 40.71 ? 85  GLU   C CG  1 
ATOM   1704 C  CD  . GLU   B 1 79  ? 2.249  -11.915 22.799 1.00 49.91 ? 85  GLU   C CD  1 
ATOM   1705 O  OE1 . GLU   B 1 79  ? 1.082  -12.346 22.669 1.00 51.37 ? 85  GLU   C OE1 1 
ATOM   1706 O  OE2 . GLU   B 1 79  ? 2.515  -10.711 23.028 1.00 53.03 ? 85  GLU   C OE2 1 
ATOM   1707 N  N   . ALA   B 1 80  ? 6.771  -9.938  22.013 1.00 27.32 ? 86  ALA   C N   1 
ATOM   1708 C  CA  . ALA   B 1 80  ? 8.092  -9.359  22.285 1.00 27.02 ? 86  ALA   C CA  1 
ATOM   1709 C  C   . ALA   B 1 80  ? 8.833  -10.169 23.342 1.00 26.70 ? 86  ALA   C C   1 
ATOM   1710 O  O   . ALA   B 1 80  ? 8.227  -10.829 24.177 1.00 27.07 ? 86  ALA   C O   1 
ATOM   1711 C  CB  . ALA   B 1 80  ? 7.953  -7.902  22.761 1.00 27.01 ? 86  ALA   C CB  1 
ATOM   1712 N  N   . SER   B 1 81  ? 10.147 -10.161 23.268 1.00 25.77 ? 87  SER   C N   1 
ATOM   1713 C  CA  . SER   B 1 81  ? 11.021 -10.823 24.229 1.00 25.04 ? 87  SER   C CA  1 
ATOM   1714 C  C   . SER   B 1 81  ? 12.251 -9.890  24.337 1.00 26.22 ? 87  SER   C C   1 
ATOM   1715 O  O   . SER   B 1 81  ? 12.282 -8.828  23.683 1.00 27.26 ? 87  SER   C O   1 
ATOM   1716 C  CB  . SER   B 1 81  ? 11.416 -12.225 23.721 1.00 25.11 ? 87  SER   C CB  1 
ATOM   1717 O  OG  . SER   B 1 81  ? 12.220 -12.148 22.555 1.00 24.23 ? 87  SER   C OG  1 
ATOM   1718 N  N   . GLU   B 1 82  ? 13.258 -10.237 25.162 1.00 26.10 ? 88  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 82  ? 14.462 -9.393  25.235 1.00 26.63 ? 88  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 82  ? 15.254 -9.393  23.919 1.00 26.36 ? 88  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 82  ? 16.001 -8.450  23.651 1.00 26.94 ? 88  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 82  ? 15.361 -9.817  26.398 1.00 29.78 ? 88  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 82  ? 14.815 -9.361  27.732 1.00 35.93 ? 88  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 82  ? 15.615 -9.833  28.932 1.00 46.05 ? 88  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 82  ? 16.763 -10.304 28.750 1.00 45.69 ? 88  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 82  ? 15.091 -9.722  30.067 1.00 50.45 ? 88  GLU   C OE2 1 
ATOM   1727 N  N   . TYR   B 1 83  ? 15.051 -10.426 23.085 1.00 25.24 ? 89  TYR   C N   1 
ATOM   1728 C  CA  . TYR   B 1 83  ? 15.733 -10.621 21.829 1.00 24.74 ? 89  TYR   C CA  1 
ATOM   1729 C  C   . TYR   B 1 83  ? 15.077 -9.958  20.629 1.00 24.74 ? 89  TYR   C C   1 
ATOM   1730 O  O   . TYR   B 1 83  ? 15.782 -9.659  19.662 1.00 26.47 ? 89  TYR   C O   1 
ATOM   1731 C  CB  . TYR   B 1 83  ? 15.840 -12.125 21.565 1.00 24.80 ? 89  TYR   C CB  1 
ATOM   1732 C  CG  . TYR   B 1 83  ? 16.512 -12.872 22.689 1.00 25.90 ? 89  TYR   C CG  1 
ATOM   1733 C  CD1 . TYR   B 1 83  ? 17.886 -12.804 22.872 1.00 27.17 ? 89  TYR   C CD1 1 
ATOM   1734 C  CD2 . TYR   B 1 83  ? 15.774 -13.629 23.584 1.00 27.05 ? 89  TYR   C CD2 1 
ATOM   1735 C  CE1 . TYR   B 1 83  ? 18.508 -13.474 23.915 1.00 28.62 ? 89  TYR   C CE1 1 
ATOM   1736 C  CE2 . TYR   B 1 83  ? 16.394 -14.354 24.596 1.00 28.69 ? 89  TYR   C CE2 1 
ATOM   1737 C  CZ  . TYR   B 1 83  ? 17.764 -14.282 24.751 1.00 30.01 ? 89  TYR   C CZ  1 
ATOM   1738 O  OH  . TYR   B 1 83  ? 18.393 -15.005 25.734 1.00 32.66 ? 89  TYR   C OH  1 
ATOM   1739 N  N   . TYR   B 1 84  ? 13.750 -9.841  20.619 1.00 22.67 ? 90  TYR   C N   1 
ATOM   1740 C  CA  . TYR   B 1 84  ? 13.042 -9.279  19.474 1.00 23.00 ? 90  TYR   C CA  1 
ATOM   1741 C  C   . TYR   B 1 84  ? 11.859 -8.432  19.876 1.00 24.61 ? 90  TYR   C C   1 
ATOM   1742 O  O   . TYR   B 1 84  ? 11.172 -8.738  20.858 1.00 24.15 ? 90  TYR   C O   1 
ATOM   1743 C  CB  . TYR   B 1 84  ? 12.430 -10.420 18.626 1.00 22.18 ? 90  TYR   C CB  1 
ATOM   1744 C  CG  . TYR   B 1 84  ? 13.422 -11.344 17.977 1.00 21.66 ? 90  TYR   C CG  1 
ATOM   1745 C  CD1 . TYR   B 1 84  ? 13.642 -12.620 18.477 1.00 21.34 ? 90  TYR   C CD1 1 
ATOM   1746 C  CD2 . TYR   B 1 84  ? 14.129 -10.953 16.850 1.00 22.08 ? 90  TYR   C CD2 1 
ATOM   1747 C  CE1 . TYR   B 1 84  ? 14.531 -13.485 17.868 1.00 21.06 ? 90  TYR   C CE1 1 
ATOM   1748 C  CE2 . TYR   B 1 84  ? 15.026 -11.807 16.237 1.00 22.47 ? 90  TYR   C CE2 1 
ATOM   1749 C  CZ  . TYR   B 1 84  ? 15.186 -13.087 16.722 1.00 22.18 ? 90  TYR   C CZ  1 
ATOM   1750 O  OH  . TYR   B 1 84  ? 16.102 -13.888 16.125 1.00 22.72 ? 90  TYR   C OH  1 
ATOM   1751 N  N   . PRO   B 1 85  ? 11.503 -7.439  19.037 1.00 25.24 ? 91  PRO   C N   1 
ATOM   1752 C  CA  . PRO   B 1 85  ? 10.235 -6.760  19.249 1.00 25.50 ? 91  PRO   C CA  1 
ATOM   1753 C  C   . PRO   B 1 85  ? 9.074  -7.711  18.895 1.00 25.39 ? 91  PRO   C C   1 
ATOM   1754 O  O   . PRO   B 1 85  ? 9.285  -8.712  18.205 1.00 24.62 ? 91  PRO   C O   1 
ATOM   1755 C  CB  . PRO   B 1 85  ? 10.291 -5.620  18.217 1.00 26.56 ? 91  PRO   C CB  1 
ATOM   1756 C  CG  . PRO   B 1 85  ? 11.111 -6.163  17.107 1.00 26.59 ? 91  PRO   C CG  1 
ATOM   1757 C  CD  . PRO   B 1 85  ? 12.167 -6.993  17.788 1.00 25.00 ? 91  PRO   C CD  1 
ATOM   1758 N  N   . ALA   B 1 86  ? 7.830  -7.365  19.251 1.00 25.72 ? 92  ALA   C N   1 
ATOM   1759 C  CA  . ALA   B 1 86  ? 6.649  -8.146  18.824 1.00 25.91 ? 92  ALA   C CA  1 
ATOM   1760 C  C   . ALA   B 1 86  ? 6.610  -8.083  17.280 1.00 25.44 ? 92  ALA   C C   1 
ATOM   1761 O  O   . ALA   B 1 86  ? 6.867  -7.015  16.709 1.00 25.14 ? 92  ALA   C O   1 
ATOM   1762 C  CB  . ALA   B 1 86  ? 5.368  -7.536  19.394 1.00 25.92 ? 92  ALA   C CB  1 
ATOM   1763 N  N   . ARG   B 1 87  ? 6.474  -9.242  16.618 1.00 24.90 ? 93  ARG   C N   1 
ATOM   1764 C  CA  . ARG   B 1 87  ? 6.577  -9.267  15.161 1.00 23.44 ? 93  ARG   C CA  1 
ATOM   1765 C  C   . ARG   B 1 87  ? 5.985  -10.575 14.624 1.00 23.75 ? 93  ARG   C C   1 
ATOM   1766 O  O   . ARG   B 1 87  ? 5.672  -11.482 15.401 1.00 24.59 ? 93  ARG   C O   1 
ATOM   1767 C  CB  . ARG   B 1 87  ? 8.095  -9.208  14.794 1.00 22.58 ? 93  ARG   C CB  1 
ATOM   1768 C  CG  . ARG   B 1 87  ? 8.830  -10.554 15.070 1.00 21.93 ? 93  ARG   C CG  1 
ATOM   1769 C  CD  . ARG   B 1 87  ? 10.308 -10.415 15.379 1.00 22.10 ? 93  ARG   C CD  1 
ATOM   1770 N  NE  . ARG   B 1 87  ? 11.103 -11.542 14.896 1.00 22.34 ? 93  ARG   C NE  1 
ATOM   1771 C  CZ  . ARG   B 1 87  ? 11.116 -12.753 15.456 1.00 23.24 ? 93  ARG   C CZ  1 
ATOM   1772 N  NH1 . ARG   B 1 87  ? 11.880 -13.714 14.953 1.00 20.55 ? 93  ARG   C NH1 1 
ATOM   1773 N  NH2 . ARG   B 1 87  ? 10.338 -13.017 16.503 1.00 23.81 ? 93  ARG   C NH2 1 
ATOM   1774 N  N   . TYR   B 1 88  ? 5.893  -10.696 13.302 1.00 23.60 ? 94  TYR   C N   1 
ATOM   1775 C  CA  . TYR   B 1 88  ? 5.501  -11.965 12.695 1.00 24.23 ? 94  TYR   C CA  1 
ATOM   1776 C  C   . TYR   B 1 88  ? 6.791  -12.698 12.344 1.00 22.52 ? 94  TYR   C C   1 
ATOM   1777 O  O   . TYR   B 1 88  ? 7.644  -12.138 11.644 1.00 23.48 ? 94  TYR   C O   1 
ATOM   1778 C  CB  . TYR   B 1 88  ? 4.714  -11.723 11.415 1.00 25.83 ? 94  TYR   C CB  1 
ATOM   1779 C  CG  . TYR   B 1 88  ? 3.306  -11.262 11.694 1.00 28.93 ? 94  TYR   C CG  1 
ATOM   1780 C  CD1 . TYR   B 1 88  ? 2.270  -12.170 11.810 1.00 30.56 ? 94  TYR   C CD1 1 
ATOM   1781 C  CD2 . TYR   B 1 88  ? 3.022  -9.921  11.910 1.00 31.15 ? 94  TYR   C CD2 1 
ATOM   1782 C  CE1 . TYR   B 1 88  ? 0.975  -11.756 12.076 1.00 32.62 ? 94  TYR   C CE1 1 
ATOM   1783 C  CE2 . TYR   B 1 88  ? 1.731  -9.497  12.194 1.00 32.84 ? 94  TYR   C CE2 1 
ATOM   1784 C  CZ  . TYR   B 1 88  ? 0.710  -10.424 12.276 1.00 34.32 ? 94  TYR   C CZ  1 
ATOM   1785 O  OH  . TYR   B 1 88  ? -0.584 -10.065 12.558 1.00 38.68 ? 94  TYR   C OH  1 
ATOM   1786 N  N   . GLN   B 1 89  ? 6.941  -13.935 12.835 1.00 19.79 ? 95  GLN   C N   1 
ATOM   1787 C  CA  . GLN   B 1 89  ? 8.096  -14.743 12.487 1.00 19.37 ? 95  GLN   C CA  1 
ATOM   1788 C  C   . GLN   B 1 89  ? 7.695  -15.597 11.273 1.00 19.38 ? 95  GLN   C C   1 
ATOM   1789 O  O   . GLN   B 1 89  ? 6.616  -16.195 11.275 1.00 20.34 ? 95  GLN   C O   1 
ATOM   1790 C  CB  . GLN   B 1 89  ? 8.526  -15.616 13.680 1.00 20.44 ? 95  GLN   C CB  1 
ATOM   1791 C  CG  . GLN   B 1 89  ? 9.662  -16.584 13.308 1.00 22.10 ? 95  GLN   C CG  1 
ATOM   1792 C  CD  . GLN   B 1 89  ? 10.410 -17.100 14.510 1.00 20.79 ? 95  GLN   C CD  1 
ATOM   1793 O  OE1 . GLN   B 1 89  ? 10.588 -16.395 15.506 1.00 20.36 ? 95  GLN   C OE1 1 
ATOM   1794 N  NE2 . GLN   B 1 89  ? 10.900 -18.347 14.405 1.00 18.81 ? 95  GLN   C NE2 1 
ATOM   1795 N  N   . SER   B 1 90  ? 8.532  -15.625 10.221 1.00 17.88 ? 96  SER   C N   1 
ATOM   1796 C  CA  . SER   B 1 90  ? 8.190  -16.377 9.002  1.00 17.34 ? 96  SER   C CA  1 
ATOM   1797 C  C   . SER   B 1 90  ? 8.804  -17.786 9.011  1.00 17.26 ? 96  SER   C C   1 
ATOM   1798 O  O   . SER   B 1 90  ? 9.721  -18.050 9.809  1.00 17.37 ? 96  SER   C O   1 
ATOM   1799 C  CB  . SER   B 1 90  ? 8.641  -15.608 7.757  1.00 17.65 ? 96  SER   C CB  1 
ATOM   1800 O  OG  . SER   B 1 90  ? 10.051 -15.418 7.777  1.00 18.36 ? 96  SER   C OG  1 
ATOM   1801 N  N   . HIS   B 1 91  ? 8.323  -18.666 8.102  1.00 16.56 ? 97  HIS   C N   1 
ATOM   1802 C  CA  . HIS   B 1 91  ? 8.837  -20.035 7.917  1.00 16.88 ? 97  HIS   C CA  1 
ATOM   1803 C  C   . HIS   B 1 91  ? 8.759  -20.839 9.247  1.00 17.93 ? 97  HIS   C C   1 
ATOM   1804 O  O   . HIS   B 1 91  ? 9.667  -21.615 9.555  1.00 17.85 ? 97  HIS   C O   1 
ATOM   1805 C  CB  . HIS   B 1 91  ? 10.297 -19.992 7.371  1.00 17.03 ? 97  HIS   C CB  1 
ATOM   1806 C  CG  . HIS   B 1 91  ? 10.419 -19.324 6.029  1.00 18.50 ? 97  HIS   C CG  1 
ATOM   1807 N  ND1 . HIS   B 1 91  ? 10.376 -20.054 4.846  1.00 20.54 ? 97  HIS   C ND1 1 
ATOM   1808 C  CD2 . HIS   B 1 91  ? 10.524 -18.010 5.720  1.00 19.40 ? 97  HIS   C CD2 1 
ATOM   1809 C  CE1 . HIS   B 1 91  ? 10.470 -19.164 3.861  1.00 21.03 ? 97  HIS   C CE1 1 
ATOM   1810 N  NE2 . HIS   B 1 91  ? 10.526 -17.919 4.336  1.00 20.17 ? 97  HIS   C NE2 1 
ATOM   1811 N  N   . LEU   B 1 92  ? 7.721  -20.559 10.069 1.00 16.63 ? 98  LEU   C N   1 
ATOM   1812 C  CA  . LEU   B 1 92  ? 7.585  -21.194 11.382 1.00 16.50 ? 98  LEU   C CA  1 
ATOM   1813 C  C   . LEU   B 1 92  ? 6.516  -22.283 11.340 1.00 16.71 ? 98  LEU   C C   1 
ATOM   1814 O  O   . LEU   B 1 92  ? 5.500  -22.100 10.687 1.00 17.36 ? 98  LEU   C O   1 
ATOM   1815 C  CB  . LEU   B 1 92  ? 7.173  -20.109 12.402 1.00 16.21 ? 98  LEU   C CB  1 
ATOM   1816 C  CG  . LEU   B 1 92  ? 7.082  -20.526 13.868 1.00 18.23 ? 98  LEU   C CG  1 
ATOM   1817 C  CD1 . LEU   B 1 92  ? 8.459  -20.939 14.412 1.00 17.78 ? 98  LEU   C CD1 1 
ATOM   1818 C  CD2 . LEU   B 1 92  ? 6.581  -19.343 14.710 1.00 21.20 ? 98  LEU   C CD2 1 
ATOM   1819 N  N   . MET   B 1 93  ? 6.749  -23.418 12.007 1.00 16.31 ? 99  MET   C N   1 
ATOM   1820 C  CA  . MET   B 1 93  ? 5.751  -24.512 12.032 1.00 16.53 ? 99  MET   C CA  1 
ATOM   1821 C  C   . MET   B 1 93  ? 5.397  -24.819 13.469 1.00 17.31 ? 99  MET   C C   1 
ATOM   1822 O  O   . MET   B 1 93  ? 6.288  -24.900 14.312 1.00 17.88 ? 99  MET   C O   1 
ATOM   1823 C  CB  . MET   B 1 93  ? 6.333  -25.782 11.401 1.00 17.43 ? 99  MET   C CB  1 
ATOM   1824 C  CG  . MET   B 1 93  ? 6.861  -25.536 10.030 1.00 19.11 ? 99  MET   C CG  1 
ATOM   1825 S  SD  . MET   B 1 93  ? 7.888  -26.859 9.392  1.00 21.66 ? 99  MET   C SD  1 
ATOM   1826 C  CE  . MET   B 1 93  ? 9.344  -26.693 10.364 1.00 15.17 ? 99  MET   C CE  1 
ATOM   1827 N  N   . LEU   B 1 94  ? 4.119  -24.982 13.757 1.00 16.59 ? 100 LEU   C N   1 
ATOM   1828 C  CA  . LEU   B 1 94  ? 3.669  -25.237 15.127 1.00 17.15 ? 100 LEU   C CA  1 
ATOM   1829 C  C   . LEU   B 1 94  ? 3.244  -26.680 15.351 1.00 17.18 ? 100 LEU   C C   1 
ATOM   1830 O  O   . LEU   B 1 94  ? 2.768  -27.353 14.429 1.00 17.06 ? 100 LEU   C O   1 
ATOM   1831 C  CB  . LEU   B 1 94  ? 2.471  -24.328 15.502 1.00 18.22 ? 100 LEU   C CB  1 
ATOM   1832 C  CG  . LEU   B 1 94  ? 2.717  -22.809 15.489 1.00 19.77 ? 100 LEU   C CG  1 
ATOM   1833 C  CD1 . LEU   B 1 94  ? 1.448  -22.061 16.000 1.00 20.77 ? 100 LEU   C CD1 1 
ATOM   1834 C  CD2 . LEU   B 1 94  ? 3.916  -22.446 16.390 1.00 21.29 ? 100 LEU   C CD2 1 
ATOM   1835 N  N   . ALA   B 1 95  ? 3.429  -27.163 16.588 1.00 16.37 ? 101 ALA   C N   1 
ATOM   1836 C  CA  . ALA   B 1 95  ? 3.028  -28.492 17.050 1.00 16.87 ? 101 ALA   C CA  1 
ATOM   1837 C  C   . ALA   B 1 95  ? 2.466  -28.343 18.480 1.00 17.77 ? 101 ALA   C C   1 
ATOM   1838 O  O   . ALA   B 1 95  ? 2.749  -27.369 19.170 1.00 17.90 ? 101 ALA   C O   1 
ATOM   1839 C  CB  . ALA   B 1 95  ? 4.222  -29.440 17.057 1.00 16.85 ? 101 ALA   C CB  1 
ATOM   1840 N  N   . VAL   B 1 96  ? 1.669  -29.311 18.913 1.00 17.90 ? 102 VAL   C N   1 
ATOM   1841 C  CA  . VAL   B 1 96  ? 1.162  -29.378 20.263 1.00 18.56 ? 102 VAL   C CA  1 
ATOM   1842 C  C   . VAL   B 1 96  ? 2.241  -30.126 21.024 1.00 20.32 ? 102 VAL   C C   1 
ATOM   1843 O  O   . VAL   B 1 96  ? 2.527  -31.287 20.733 1.00 21.06 ? 102 VAL   C O   1 
ATOM   1844 C  CB  . VAL   B 1 96  ? -0.190 -30.131 20.308 1.00 19.06 ? 102 VAL   C CB  1 
ATOM   1845 C  CG1 . VAL   B 1 96  ? -0.644 -30.350 21.749 1.00 19.01 ? 102 VAL   C CG1 1 
ATOM   1846 C  CG2 . VAL   B 1 96  ? -1.239 -29.377 19.485 1.00 18.81 ? 102 VAL   C CG2 1 
ATOM   1847 N  N   . GLY   B 1 97  ? 2.899  -29.429 21.930 1.00 21.33 ? 103 GLY   C N   1 
ATOM   1848 C  CA  . GLY   B 1 97  ? 3.968  -30.039 22.705 1.00 22.66 ? 103 GLY   C CA  1 
ATOM   1849 C  C   . GLY   B 1 97  ? 4.594  -29.108 23.698 1.00 23.45 ? 103 GLY   C C   1 
ATOM   1850 O  O   . GLY   B 1 97  ? 4.369  -27.893 23.647 1.00 24.50 ? 103 GLY   C O   1 
ATOM   1851 N  N   . HIS   B 1 98  ? 5.442  -29.668 24.561 1.00 22.53 ? 104 HIS   C N   1 
ATOM   1852 C  CA  . HIS   B 1 98  ? 6.091  -28.858 25.573 1.00 22.01 ? 104 HIS   C CA  1 
ATOM   1853 C  C   . HIS   B 1 98  ? 7.348  -28.173 25.069 1.00 20.84 ? 104 HIS   C C   1 
ATOM   1854 O  O   . HIS   B 1 98  ? 8.181  -28.789 24.386 1.00 20.03 ? 104 HIS   C O   1 
ATOM   1855 C  CB  . HIS   B 1 98  ? 6.452  -29.719 26.796 1.00 22.72 ? 104 HIS   C CB  1 
ATOM   1856 C  CG  . HIS   B 1 98  ? 7.083  -28.916 27.895 1.00 22.59 ? 104 HIS   C CG  1 
ATOM   1857 N  ND1 . HIS   B 1 98  ? 6.346  -27.995 28.642 1.00 24.40 ? 104 HIS   C ND1 1 
ATOM   1858 C  CD2 . HIS   B 1 98  ? 8.379  -28.875 28.296 1.00 22.40 ? 104 HIS   C CD2 1 
ATOM   1859 C  CE1 . HIS   B 1 98  ? 7.215  -27.449 29.489 1.00 24.90 ? 104 HIS   C CE1 1 
ATOM   1860 N  NE2 . HIS   B 1 98  ? 8.446  -27.970 29.333 1.00 23.90 ? 104 HIS   C NE2 1 
ATOM   1861 N  N   . SER   B 1 99  ? 7.527  -26.916 25.481 1.00 19.61 ? 105 SER   C N   1 
ATOM   1862 C  CA  . SER   B 1 99  ? 8.757  -26.197 25.188 1.00 19.60 ? 105 SER   C CA  1 
ATOM   1863 C  C   . SER   B 1 99  ? 8.921  -24.999 26.109 1.00 20.31 ? 105 SER   C C   1 
ATOM   1864 O  O   . SER   B 1 99  ? 7.943  -24.397 26.559 1.00 21.75 ? 105 SER   C O   1 
ATOM   1865 C  CB  . SER   B 1 99  ? 8.854  -25.783 23.721 1.00 21.47 ? 105 SER   C CB  1 
ATOM   1866 O  OG  . SER   B 1 99  ? 7.879  -24.808 23.438 1.00 25.40 ? 105 SER   C OG  1 
ATOM   1867 N  N   . GLU   B 1 100 ? 10.154 -24.730 26.467 1.00 19.84 ? 106 GLU   C N   1 
ATOM   1868 C  CA  . GLU   B 1 100 ? 10.555 -23.610 27.307 1.00 20.40 ? 106 GLU   C CA  1 
ATOM   1869 C  C   . GLU   B 1 100 ? 11.656 -22.846 26.542 1.00 20.47 ? 106 GLU   C C   1 
ATOM   1870 O  O   . GLU   B 1 100 ? 12.256 -23.404 25.608 1.00 20.10 ? 106 GLU   C O   1 
ATOM   1871 C  CB  . GLU   B 1 100 ? 11.091 -24.150 28.640 1.00 22.36 ? 106 GLU   C CB  1 
ATOM   1872 C  CG  . GLU   B 1 100 ? 9.976  -24.706 29.498 1.00 27.67 ? 106 GLU   C CG  1 
ATOM   1873 C  CD  . GLU   B 1 100 ? 10.418 -25.455 30.741 1.00 34.26 ? 106 GLU   C CD  1 
ATOM   1874 O  OE1 . GLU   B 1 100 ? 11.516 -25.165 31.268 1.00 37.61 ? 106 GLU   C OE1 1 
ATOM   1875 O  OE2 . GLU   B 1 100 ? 9.663  -26.343 31.184 1.00 33.38 ? 106 GLU   C OE2 1 
ATOM   1876 N  N   . PRO   B 1 101 ? 11.953 -21.577 26.895 1.00 20.55 ? 107 PRO   C N   1 
ATOM   1877 C  CA  . PRO   B 1 101 ? 12.965 -20.825 26.120 1.00 20.87 ? 107 PRO   C CA  1 
ATOM   1878 C  C   . PRO   B 1 101 ? 14.322 -21.538 25.900 1.00 21.42 ? 107 PRO   C C   1 
ATOM   1879 O  O   . PRO   B 1 101 ? 14.865 -21.498 24.781 1.00 20.80 ? 107 PRO   C O   1 
ATOM   1880 C  CB  . PRO   B 1 101 ? 13.113 -19.513 26.932 1.00 21.82 ? 107 PRO   C CB  1 
ATOM   1881 C  CG  . PRO   B 1 101 ? 11.734 -19.314 27.543 1.00 21.91 ? 107 PRO   C CG  1 
ATOM   1882 C  CD  . PRO   B 1 101 ? 11.327 -20.727 27.937 1.00 20.46 ? 107 PRO   C CD  1 
ATOM   1883 N  N   . GLY   B 1 102 ? 14.834 -22.233 26.926 1.00 21.28 ? 108 GLY   C N   1 
ATOM   1884 C  CA  . GLY   B 1 102 ? 16.104 -22.973 26.853 1.00 20.93 ? 108 GLY   C CA  1 
ATOM   1885 C  C   . GLY   B 1 102 ? 16.076 -24.191 25.934 1.00 19.70 ? 108 GLY   C C   1 
ATOM   1886 O  O   . GLY   B 1 102 ? 17.107 -24.815 25.648 1.00 19.63 ? 108 GLY   C O   1 
ATOM   1887 N  N   . ASP   B 1 103 ? 14.872 -24.555 25.462 1.00 18.23 ? 109 ASP   C N   1 
ATOM   1888 C  CA  . ASP   B 1 103 ? 14.710 -25.651 24.508 1.00 17.00 ? 109 ASP   C CA  1 
ATOM   1889 C  C   . ASP   B 1 103 ? 15.063 -25.238 23.075 1.00 16.77 ? 109 ASP   C C   1 
ATOM   1890 O  O   . ASP   B 1 103 ? 15.196 -26.117 22.210 1.00 16.80 ? 109 ASP   C O   1 
ATOM   1891 C  CB  . ASP   B 1 103 ? 13.259 -26.193 24.525 1.00 17.62 ? 109 ASP   C CB  1 
ATOM   1892 C  CG  . ASP   B 1 103 ? 12.973 -27.026 25.755 1.00 19.20 ? 109 ASP   C CG  1 
ATOM   1893 O  OD1 . ASP   B 1 103 ? 13.908 -27.650 26.270 1.00 18.64 ? 109 ASP   C OD1 1 
ATOM   1894 O  OD2 . ASP   B 1 103 ? 11.827 -27.002 26.227 1.00 20.37 ? 109 ASP   C OD2 1 
ATOM   1895 N  N   . CYS   B 1 104 ? 15.220 -23.917 22.807 1.00 16.70 ? 110 CYS   C N   1 
ATOM   1896 C  CA  . CYS   B 1 104 ? 15.577 -23.429 21.459 1.00 17.29 ? 110 CYS   C CA  1 
ATOM   1897 C  C   . CYS   B 1 104 ? 16.839 -24.099 20.961 1.00 16.52 ? 110 CYS   C C   1 
ATOM   1898 O  O   . CYS   B 1 104 ? 17.774 -24.234 21.735 1.00 16.48 ? 110 CYS   C O   1 
ATOM   1899 C  CB  . CYS   B 1 104 ? 15.708 -21.910 21.426 1.00 17.49 ? 110 CYS   C CB  1 
ATOM   1900 S  SG  . CYS   B 1 104 ? 14.112 -21.052 21.519 1.00 19.55 ? 110 CYS   C SG  1 
ATOM   1901 N  N   . GLY   B 1 105 ? 16.845 -24.545 19.715 1.00 16.29 ? 111 GLY   C N   1 
ATOM   1902 C  CA  . GLY   B 1 105 ? 18.004 -25.235 19.171 1.00 17.07 ? 111 GLY   C CA  1 
ATOM   1903 C  C   . GLY   B 1 105 ? 17.829 -26.741 19.098 1.00 18.27 ? 111 GLY   C C   1 
ATOM   1904 O  O   . GLY   B 1 105 ? 18.577 -27.407 18.381 1.00 18.52 ? 111 GLY   C O   1 
ATOM   1905 N  N   . GLY   B 1 106 ? 16.823 -27.290 19.811 1.00 17.36 ? 112 GLY   C N   1 
ATOM   1906 C  CA  . GLY   B 1 106 ? 16.514 -28.722 19.736 1.00 17.33 ? 112 GLY   C CA  1 
ATOM   1907 C  C   . GLY   B 1 106 ? 16.074 -29.073 18.322 1.00 17.25 ? 112 GLY   C C   1 
ATOM   1908 O  O   . GLY   B 1 106 ? 15.323 -28.314 17.695 1.00 17.52 ? 112 GLY   C O   1 
ATOM   1909 N  N   . ILE   B 1 107 ? 16.596 -30.180 17.778 1.00 16.43 ? 113 ILE   C N   1 
ATOM   1910 C  CA  . ILE   B 1 107 ? 16.331 -30.526 16.400 1.00 16.68 ? 113 ILE   C CA  1 
ATOM   1911 C  C   . ILE   B 1 107 ? 15.013 -31.267 16.222 1.00 15.79 ? 113 ILE   C C   1 
ATOM   1912 O  O   . ILE   B 1 107 ? 14.660 -32.138 17.024 1.00 16.75 ? 113 ILE   C O   1 
ATOM   1913 C  CB  . ILE   B 1 107 ? 17.568 -31.282 15.828 1.00 19.62 ? 113 ILE   C CB  1 
ATOM   1914 C  CG1 . ILE   B 1 107 ? 18.699 -30.278 15.452 1.00 22.08 ? 113 ILE   C CG1 1 
ATOM   1915 C  CG2 . ILE   B 1 107 ? 17.232 -32.169 14.638 1.00 20.57 ? 113 ILE   C CG2 1 
ATOM   1916 C  CD1 . ILE   B 1 107 ? 20.026 -30.953 15.118 1.00 25.54 ? 113 ILE   C CD1 1 
ATOM   1917 N  N   . LEU   B 1 108 ? 14.309 -30.927 15.145 1.00 13.88 ? 114 LEU   C N   1 
ATOM   1918 C  CA  . LEU   B 1 108 ? 13.116 -31.638 14.686 1.00 14.26 ? 114 LEU   C CA  1 
ATOM   1919 C  C   . LEU   B 1 108 ? 13.559 -32.443 13.459 1.00 15.31 ? 114 LEU   C C   1 
ATOM   1920 O  O   . LEU   B 1 108 ? 14.175 -31.874 12.546 1.00 14.57 ? 114 LEU   C O   1 
ATOM   1921 C  CB  . LEU   B 1 108 ? 12.012 -30.652 14.266 1.00 14.20 ? 114 LEU   C CB  1 
ATOM   1922 C  CG  . LEU   B 1 108 ? 10.785 -31.264 13.549 1.00 15.61 ? 114 LEU   C CG  1 
ATOM   1923 C  CD1 . LEU   B 1 108 ? 9.965  -32.257 14.447 1.00 14.78 ? 114 LEU   C CD1 1 
ATOM   1924 C  CD2 . LEU   B 1 108 ? 9.861  -30.154 13.030 1.00 17.00 ? 114 LEU   C CD2 1 
ATOM   1925 N  N   . ARG   B 1 109 ? 13.301 -33.762 13.449 1.00 16.02 ? 115 ARG   C N   1 
ATOM   1926 C  CA  . ARG   B 1 109 ? 13.692 -34.617 12.316 1.00 16.93 ? 115 ARG   C CA  1 
ATOM   1927 C  C   . ARG   B 1 109 ? 12.538 -35.446 11.809 1.00 16.66 ? 115 ARG   C C   1 
ATOM   1928 O  O   . ARG   B 1 109 ? 11.713 -35.905 12.594 1.00 16.89 ? 115 ARG   C O   1 
ATOM   1929 C  CB  . ARG   B 1 109 ? 14.753 -35.645 12.737 1.00 19.45 ? 115 ARG   C CB  1 
ATOM   1930 C  CG  . ARG   B 1 109 ? 15.956 -35.121 13.456 1.00 26.05 ? 115 ARG   C CG  1 
ATOM   1931 C  CD  . ARG   B 1 109 ? 16.826 -36.283 13.889 1.00 31.12 ? 115 ARG   C CD  1 
ATOM   1932 N  NE  . ARG   B 1 109 ? 17.365 -36.916 12.695 1.00 36.56 ? 115 ARG   C NE  1 
ATOM   1933 C  CZ  . ARG   B 1 109 ? 18.531 -36.598 12.145 1.00 39.23 ? 115 ARG   C CZ  1 
ATOM   1934 N  NH1 . ARG   B 1 109 ? 19.354 -35.752 12.757 1.00 38.93 ? 115 ARG   C NH1 1 
ATOM   1935 N  NH2 . ARG   B 1 109 ? 18.897 -37.147 11.001 1.00 39.65 ? 115 ARG   C NH2 1 
ATOM   1936 N  N   . CYS   B 1 110 ? 12.523 -35.719 10.504 1.00 16.92 ? 116 CYS   C N   1 
ATOM   1937 C  CA  . CYS   B 1 110 ? 11.553 -36.642 9.913  1.00 17.86 ? 116 CYS   C CA  1 
ATOM   1938 C  C   . CYS   B 1 110 ? 12.364 -37.835 9.336  1.00 18.84 ? 116 CYS   C C   1 
ATOM   1939 O  O   . CYS   B 1 110 ? 13.598 -37.923 9.513  1.00 17.95 ? 116 CYS   C O   1 
ATOM   1940 C  CB  . CYS   B 1 110 ? 10.750 -35.937 8.822  1.00 17.49 ? 116 CYS   C CB  1 
ATOM   1941 S  SG  . CYS   B 1 110 ? 11.765 -35.389 7.429  1.00 16.80 ? 116 CYS   C SG  1 
ATOM   1942 N  N   . GLN   B 1 111 ? 11.688 -38.747 8.619  1.00 20.20 ? 117 GLN   C N   1 
ATOM   1943 C  CA  . GLN   B 1 111 ? 12.375 -39.903 8.033  1.00 21.94 ? 117 GLN   C CA  1 
ATOM   1944 C  C   . GLN   B 1 111 ? 13.449 -39.479 6.994  1.00 22.43 ? 117 GLN   C C   1 
ATOM   1945 O  O   . GLN   B 1 111 ? 14.301 -40.284 6.641  1.00 24.00 ? 117 GLN   C O   1 
ATOM   1946 C  CB  . GLN   B 1 111 ? 11.344 -40.833 7.375  1.00 25.21 ? 117 GLN   C CB  1 
ATOM   1947 C  CG  . GLN   B 1 111 ? 10.653 -40.212 6.154  1.00 29.42 ? 117 GLN   C CG  1 
ATOM   1948 C  CD  . GLN   B 1 111 ? 9.581  -41.109 5.582  1.00 36.40 ? 117 GLN   C CD  1 
ATOM   1949 O  OE1 . GLN   B 1 111 ? 8.395  -40.752 5.546  1.00 37.88 ? 117 GLN   C OE1 1 
ATOM   1950 N  NE2 . GLN   B 1 111 ? 9.970  -42.293 5.118  1.00 37.67 ? 117 GLN   C NE2 1 
ATOM   1951 N  N   . HIS   B 1 112 ? 13.440 -38.211 6.535  1.00 20.70 ? 118 HIS   C N   1 
ATOM   1952 C  CA  . HIS   B 1 112 ? 14.364 -37.725 5.511  1.00 19.64 ? 118 HIS   C CA  1 
ATOM   1953 C  C   . HIS   B 1 112 ? 15.570 -36.963 6.047  1.00 20.72 ? 118 HIS   C C   1 
ATOM   1954 O  O   . HIS   B 1 112 ? 16.469 -36.665 5.276  1.00 21.82 ? 118 HIS   C O   1 
ATOM   1955 C  CB  . HIS   B 1 112 ? 13.626 -36.833 4.509  1.00 19.13 ? 118 HIS   C CB  1 
ATOM   1956 C  CG  . HIS   B 1 112 ? 12.435 -37.478 3.875  1.00 19.89 ? 118 HIS   C CG  1 
ATOM   1957 N  ND1 . HIS   B 1 112 ? 11.156 -37.075 4.191  1.00 19.44 ? 118 HIS   C ND1 1 
ATOM   1958 C  CD2 . HIS   B 1 112 ? 12.370 -38.476 2.953  1.00 21.31 ? 118 HIS   C CD2 1 
ATOM   1959 C  CE1 . HIS   B 1 112 ? 10.339 -37.846 3.478  1.00 20.86 ? 118 HIS   C CE1 1 
ATOM   1960 N  NE2 . HIS   B 1 112 ? 11.017 -38.719 2.726  1.00 21.91 ? 118 HIS   C NE2 1 
ATOM   1961 N  N   . GLY   B 1 113 ? 15.571 -36.609 7.331  1.00 19.34 ? 119 GLY   C N   1 
ATOM   1962 C  CA  . GLY   B 1 113 ? 16.675 -35.854 7.906  1.00 18.22 ? 119 GLY   C CA  1 
ATOM   1963 C  C   . GLY   B 1 113 ? 16.190 -34.690 8.753  1.00 16.91 ? 119 GLY   C C   1 
ATOM   1964 O  O   . GLY   B 1 113 ? 15.047 -34.682 9.211  1.00 17.00 ? 119 GLY   C O   1 
ATOM   1965 N  N   . VAL   B 1 114 ? 17.043 -33.706 8.957  1.00 15.68 ? 120 VAL   C N   1 
ATOM   1966 C  CA  . VAL   B 1 114 ? 16.726 -32.521 9.771  1.00 16.63 ? 120 VAL   C CA  1 
ATOM   1967 C  C   . VAL   B 1 114 ? 15.715 -31.594 9.102  1.00 17.49 ? 120 VAL   C C   1 
ATOM   1968 O  O   . VAL   B 1 114 ? 15.942 -31.134 7.965  1.00 18.47 ? 120 VAL   C O   1 
ATOM   1969 C  CB  . VAL   B 1 114 ? 18.020 -31.751 10.115 1.00 17.91 ? 120 VAL   C CB  1 
ATOM   1970 C  CG1 . VAL   B 1 114 ? 17.674 -30.483 10.884 1.00 18.63 ? 120 VAL   C CG1 1 
ATOM   1971 C  CG2 . VAL   B 1 114 ? 18.975 -32.653 10.929 1.00 19.13 ? 120 VAL   C CG2 1 
ATOM   1972 N  N   . VAL   B 1 115 ? 14.628 -31.269 9.825  1.00 16.15 ? 121 VAL   C N   1 
ATOM   1973 C  CA  . VAL   B 1 115 ? 13.571 -30.381 9.344  1.00 15.70 ? 121 VAL   C CA  1 
ATOM   1974 C  C   . VAL   B 1 115 ? 13.784 -28.932 9.796  1.00 15.90 ? 121 VAL   C C   1 
ATOM   1975 O  O   . VAL   B 1 115 ? 13.558 -27.986 9.029  1.00 15.26 ? 121 VAL   C O   1 
ATOM   1976 C  CB  . VAL   B 1 115 ? 12.174 -30.903 9.821  1.00 16.12 ? 121 VAL   C CB  1 
ATOM   1977 C  CG1 . VAL   B 1 115 ? 11.069 -29.918 9.450  1.00 17.12 ? 121 VAL   C CG1 1 
ATOM   1978 C  CG2 . VAL   B 1 115 ? 11.881 -32.280 9.242  1.00 16.66 ? 121 VAL   C CG2 1 
ATOM   1979 N  N   . GLY   B 1 116 ? 14.173 -28.770 11.052 1.00 15.83 ? 122 GLY   C N   1 
ATOM   1980 C  CA  . GLY   B 1 116 ? 14.326 -27.439 11.620 1.00 16.08 ? 122 GLY   C CA  1 
ATOM   1981 C  C   . GLY   B 1 116 ? 14.718 -27.464 13.080 1.00 15.33 ? 122 GLY   C C   1 
ATOM   1982 O  O   . GLY   B 1 116 ? 15.081 -28.514 13.607 1.00 15.10 ? 122 GLY   C O   1 
ATOM   1983 N  N   . ILE   B 1 117 ? 14.640 -26.305 13.755 1.00 15.01 ? 123 ILE   C N   1 
ATOM   1984 C  CA  . ILE   B 1 117 ? 15.019 -26.252 15.172 1.00 15.96 ? 123 ILE   C CA  1 
ATOM   1985 C  C   . ILE   B 1 117 ? 13.984 -25.517 16.000 1.00 16.43 ? 123 ILE   C C   1 
ATOM   1986 O  O   . ILE   B 1 117 ? 13.342 -24.597 15.512 1.00 16.86 ? 123 ILE   C O   1 
ATOM   1987 C  CB  . ILE   B 1 117 ? 16.398 -25.576 15.350 1.00 16.95 ? 123 ILE   C CB  1 
ATOM   1988 C  CG1 . ILE   B 1 117 ? 16.457 -24.197 14.656 1.00 17.66 ? 123 ILE   C CG1 1 
ATOM   1989 C  CG2 . ILE   B 1 117 ? 17.550 -26.477 14.888 1.00 18.08 ? 123 ILE   C CG2 1 
ATOM   1990 C  CD1 . ILE   B 1 117 ? 17.759 -23.379 15.055 1.00 18.30 ? 123 ILE   C CD1 1 
ATOM   1991 N  N   . VAL   B 1 118 ? 13.850 -25.873 17.288 1.00 15.71 ? 124 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 118 ? 12.908 -25.194 18.185 1.00 15.54 ? 124 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 118 ? 13.264 -23.689 18.235 1.00 15.70 ? 124 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 118 ? 14.438 -23.357 18.365 1.00 15.32 ? 124 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 118 ? 12.951 -25.797 19.608 1.00 15.30 ? 124 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 118 ? 12.076 -24.969 20.560 1.00 16.53 ? 124 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 118 ? 12.512 -27.269 19.596 1.00 15.80 ? 124 VAL   C CG2 1 
ATOM   1998 N  N   . SER   B 1 119 ? 12.271 -22.822 18.057 1.00 16.40 ? 125 SER   C N   1 
ATOM   1999 C  CA  . SER   B 1 119 ? 12.455 -21.380 18.042 1.00 16.35 ? 125 SER   C CA  1 
ATOM   2000 C  C   . SER   B 1 119 ? 11.421 -20.648 18.912 1.00 18.95 ? 125 SER   C C   1 
ATOM   2001 O  O   . SER   B 1 119 ? 11.729 -19.596 19.485 1.00 20.13 ? 125 SER   C O   1 
ATOM   2002 C  CB  . SER   B 1 119 ? 12.414 -20.875 16.598 1.00 17.16 ? 125 SER   C CB  1 
ATOM   2003 O  OG  . SER   B 1 119 ? 12.566 -19.466 16.530 1.00 18.03 ? 125 SER   C OG  1 
ATOM   2004 N  N   . THR   B 1 120 ? 10.184 -21.162 18.989 1.00 19.00 ? 126 THR   C N   1 
ATOM   2005 C  CA  . THR   B 1 120 ? 9.136  -20.516 19.810 1.00 18.93 ? 126 THR   C CA  1 
ATOM   2006 C  C   . THR   B 1 120 ? 8.397  -21.565 20.706 1.00 20.82 ? 126 THR   C C   1 
ATOM   2007 O  O   . THR   B 1 120 ? 8.605  -22.772 20.550 1.00 19.83 ? 126 THR   C O   1 
ATOM   2008 C  CB  . THR   B 1 120 ? 8.122  -19.750 18.906 1.00 19.48 ? 126 THR   C CB  1 
ATOM   2009 O  OG1 . THR   B 1 120 ? 7.267  -20.695 18.253 1.00 19.88 ? 126 THR   C OG1 1 
ATOM   2010 C  CG2 . THR   B 1 120 ? 8.791  -18.851 17.891 1.00 18.75 ? 126 THR   C CG2 1 
ATOM   2011 N  N   . GLY   B 1 121 ? 7.545  -21.104 21.620 1.00 22.49 ? 127 GLY   C N   1 
ATOM   2012 C  CA  . GLY   B 1 121 ? 6.779  -22.010 22.469 1.00 24.60 ? 127 GLY   C CA  1 
ATOM   2013 C  C   . GLY   B 1 121 ? 5.970  -21.324 23.544 1.00 26.47 ? 127 GLY   C C   1 
ATOM   2014 O  O   . GLY   B 1 121 ? 5.966  -20.098 23.626 1.00 25.12 ? 127 GLY   C O   1 
ATOM   2015 N  N   . GLY   B 1 122 ? 5.367  -22.136 24.414 1.00 29.51 ? 128 GLY   C N   1 
ATOM   2016 C  CA  . GLY   B 1 122 ? 4.466  -21.688 25.473 1.00 31.01 ? 128 GLY   C CA  1 
ATOM   2017 C  C   . GLY   B 1 122 ? 3.018  -21.992 25.115 1.00 32.14 ? 128 GLY   C C   1 
ATOM   2018 O  O   . GLY   B 1 122 ? 2.722  -22.293 23.956 1.00 32.01 ? 128 GLY   C O   1 
ATOM   2019 N  N   . ASN   B 1 123 ? 2.083  -21.929 26.095 1.00 32.37 ? 129 ASN   C N   1 
ATOM   2020 C  CA  . ASN   B 1 123 ? 0.662  -22.227 25.810 1.00 32.37 ? 129 ASN   C CA  1 
ATOM   2021 C  C   . ASN   B 1 123 ? 0.441  -23.649 25.272 1.00 28.89 ? 129 ASN   C C   1 
ATOM   2022 O  O   . ASN   B 1 123 ? -0.527 -23.891 24.545 1.00 28.21 ? 129 ASN   C O   1 
ATOM   2023 C  CB  . ASN   B 1 123 ? 0.069  -21.221 24.814 1.00 35.94 ? 129 ASN   C CB  1 
ATOM   2024 C  CG  . ASN   B 1 123 ? -0.746 -20.113 25.419 1.00 40.29 ? 129 ASN   C CG  1 
ATOM   2025 O  OD1 . ASN   B 1 123 ? -0.746 -19.897 26.632 1.00 42.53 ? 129 ASN   C OD1 1 
ATOM   2026 N  ND2 . ASN   B 1 123 ? -1.448 -19.388 24.561 1.00 40.75 ? 129 ASN   C ND2 1 
ATOM   2027 N  N   . GLY   B 1 124 ? 1.317  -24.564 25.630 1.00 26.37 ? 130 GLY   C N   1 
ATOM   2028 C  CA  . GLY   B 1 124 ? 1.195  -25.943 25.176 1.00 24.57 ? 130 GLY   C CA  1 
ATOM   2029 C  C   . GLY   B 1 124 ? 1.543  -26.145 23.713 1.00 22.81 ? 130 GLY   C C   1 
ATOM   2030 O  O   . GLY   B 1 124 ? 1.215  -27.188 23.152 1.00 23.34 ? 130 GLY   C O   1 
ATOM   2031 N  N   . LEU   B 1 125 ? 2.227  -25.181 23.089 1.00 21.30 ? 131 LEU   C N   1 
ATOM   2032 C  CA  . LEU   B 1 125 ? 2.663  -25.313 21.709 1.00 20.97 ? 131 LEU   C CA  1 
ATOM   2033 C  C   . LEU   B 1 125 ? 4.200  -25.240 21.615 1.00 20.99 ? 131 LEU   C C   1 
ATOM   2034 O  O   . LEU   B 1 125 ? 4.878  -24.752 22.524 1.00 22.82 ? 131 LEU   C O   1 
ATOM   2035 C  CB  . LEU   B 1 125 ? 2.069  -24.188 20.847 1.00 22.13 ? 131 LEU   C CB  1 
ATOM   2036 C  CG  . LEU   B 1 125 ? 0.532  -24.044 20.902 1.00 25.33 ? 131 LEU   C CG  1 
ATOM   2037 C  CD1 . LEU   B 1 125 ? 0.096  -22.698 20.341 1.00 26.59 ? 131 LEU   C CD1 1 
ATOM   2038 C  CD2 . LEU   B 1 125 ? -0.141 -25.188 20.172 1.00 25.64 ? 131 LEU   C CD2 1 
ATOM   2039 N  N   . VAL   B 1 126 ? 4.743  -25.770 20.522 1.00 18.12 ? 132 VAL   C N   1 
ATOM   2040 C  CA  . VAL   B 1 126 ? 6.167  -25.659 20.266 1.00 18.17 ? 132 VAL   C CA  1 
ATOM   2041 C  C   . VAL   B 1 126 ? 6.278  -25.210 18.787 1.00 18.33 ? 132 VAL   C C   1 
ATOM   2042 O  O   . VAL   B 1 126 ? 5.535  -25.704 17.915 1.00 17.44 ? 132 VAL   C O   1 
ATOM   2043 C  CB  . VAL   B 1 126 ? 6.948  -26.959 20.590 1.00 19.33 ? 132 VAL   C CB  1 
ATOM   2044 C  CG1 . VAL   B 1 126 ? 6.298  -28.180 19.966 1.00 20.07 ? 132 VAL   C CG1 1 
ATOM   2045 C  CG2 . VAL   B 1 126 ? 8.451  -26.853 20.225 1.00 19.45 ? 132 VAL   C CG2 1 
ATOM   2046 N  N   . GLY   B 1 127 ? 7.165  -24.250 18.538 1.00 17.23 ? 133 GLY   C N   1 
ATOM   2047 C  CA  . GLY   B 1 127 ? 7.369  -23.746 17.187 1.00 16.86 ? 133 GLY   C CA  1 
ATOM   2048 C  C   . GLY   B 1 127 ? 8.766  -24.026 16.685 1.00 16.87 ? 133 GLY   C C   1 
ATOM   2049 O  O   . GLY   B 1 127 ? 9.744  -23.819 17.414 1.00 16.23 ? 133 GLY   C O   1 
ATOM   2050 N  N   . PHE   B 1 128 ? 8.868  -24.457 15.417 1.00 16.67 ? 134 PHE   C N   1 
ATOM   2051 C  CA  . PHE   B 1 128 ? 10.138 -24.826 14.799 1.00 15.81 ? 134 PHE   C CA  1 
ATOM   2052 C  C   . PHE   B 1 128 ? 10.426 -23.942 13.606 1.00 15.52 ? 134 PHE   C C   1 
ATOM   2053 O  O   . PHE   B 1 128 ? 9.555  -23.740 12.759 1.00 14.73 ? 134 PHE   C O   1 
ATOM   2054 C  CB  . PHE   B 1 128 ? 10.122 -26.286 14.310 1.00 15.12 ? 134 PHE   C CB  1 
ATOM   2055 C  CG  . PHE   B 1 128 ? 9.640  -27.282 15.348 1.00 15.33 ? 134 PHE   C CG  1 
ATOM   2056 C  CD1 . PHE   B 1 128 ? 10.516 -27.819 16.271 1.00 15.72 ? 134 PHE   C CD1 1 
ATOM   2057 C  CD2 . PHE   B 1 128 ? 8.312  -27.692 15.378 1.00 15.10 ? 134 PHE   C CD2 1 
ATOM   2058 C  CE1 . PHE   B 1 128 ? 10.072 -28.728 17.218 1.00 15.53 ? 134 PHE   C CE1 1 
ATOM   2059 C  CE2 . PHE   B 1 128 ? 7.867  -28.599 16.340 1.00 15.99 ? 134 PHE   C CE2 1 
ATOM   2060 C  CZ  . PHE   B 1 128 ? 8.755  -29.117 17.248 1.00 15.76 ? 134 PHE   C CZ  1 
ATOM   2061 N  N   . ALA   B 1 129 ? 11.657 -23.416 13.553 1.00 15.00 ? 135 ALA   C N   1 
ATOM   2062 C  CA  . ALA   B 1 129 ? 12.133 -22.624 12.420 1.00 15.00 ? 135 ALA   C CA  1 
ATOM   2063 C  C   . ALA   B 1 129 ? 12.519 -23.646 11.312 1.00 15.56 ? 135 ALA   C C   1 
ATOM   2064 O  O   . ALA   B 1 129 ? 13.454 -24.440 11.495 1.00 14.58 ? 135 ALA   C O   1 
ATOM   2065 C  CB  . ALA   B 1 129 ? 13.379 -21.844 12.839 1.00 14.70 ? 135 ALA   C CB  1 
ATOM   2066 N  N   . ASP   B 1 130 ? 11.811 -23.628 10.184 1.00 15.57 ? 136 ASP   C N   1 
ATOM   2067 C  CA  . ASP   B 1 130 ? 12.092 -24.557 9.063  1.00 15.89 ? 136 ASP   C CA  1 
ATOM   2068 C  C   . ASP   B 1 130 ? 13.435 -24.254 8.411  1.00 16.35 ? 136 ASP   C C   1 
ATOM   2069 O  O   . ASP   B 1 130 ? 13.778 -23.081 8.260  1.00 15.93 ? 136 ASP   C O   1 
ATOM   2070 C  CB  . ASP   B 1 130 ? 10.985 -24.420 7.986  1.00 17.81 ? 136 ASP   C CB  1 
ATOM   2071 C  CG  . ASP   B 1 130 ? 11.083 -25.437 6.867  1.00 21.88 ? 136 ASP   C CG  1 
ATOM   2072 O  OD1 . ASP   B 1 130 ? 11.223 -26.615 7.171  1.00 19.45 ? 136 ASP   C OD1 1 
ATOM   2073 O  OD2 . ASP   B 1 130 ? 11.061 -25.032 5.689  1.00 23.78 ? 136 ASP   C OD2 1 
ATOM   2074 N  N   . VAL   B 1 131 ? 14.174 -25.288 7.975  1.00 16.24 ? 137 VAL   C N   1 
ATOM   2075 C  CA  . VAL   B 1 131 ? 15.425 -25.089 7.194  1.00 16.30 ? 137 VAL   C CA  1 
ATOM   2076 C  C   . VAL   B 1 131 ? 15.382 -25.856 5.853  1.00 17.68 ? 137 VAL   C C   1 
ATOM   2077 O  O   . VAL   B 1 131 ? 16.340 -25.781 5.090  1.00 18.75 ? 137 VAL   C O   1 
ATOM   2078 C  CB  . VAL   B 1 131 ? 16.706 -25.489 7.974  1.00 16.82 ? 137 VAL   C CB  1 
ATOM   2079 C  CG1 . VAL   B 1 131 ? 16.829 -24.683 9.267  1.00 17.29 ? 137 VAL   C CG1 1 
ATOM   2080 C  CG2 . VAL   B 1 131 ? 16.725 -27.003 8.248  1.00 15.80 ? 137 VAL   C CG2 1 
ATOM   2081 N  N   . ARG   B 1 132 ? 14.278 -26.569 5.548  1.00 16.84 ? 138 ARG   C N   1 
ATOM   2082 C  CA  . ARG   B 1 132 ? 14.156 -27.401 4.348  1.00 16.42 ? 138 ARG   C CA  1 
ATOM   2083 C  C   . ARG   B 1 132 ? 14.211 -26.640 3.040  1.00 16.58 ? 138 ARG   C C   1 
ATOM   2084 O  O   . ARG   B 1 132 ? 14.570 -27.234 2.023  1.00 18.74 ? 138 ARG   C O   1 
ATOM   2085 C  CB  . ARG   B 1 132 ? 12.884 -28.225 4.390  1.00 14.54 ? 138 ARG   C CB  1 
ATOM   2086 C  CG  . ARG   B 1 132 ? 12.866 -29.270 5.503  1.00 11.83 ? 138 ARG   C CG  1 
ATOM   2087 C  CD  . ARG   B 1 132 ? 11.525 -29.967 5.500  1.00 15.44 ? 138 ARG   C CD  1 
ATOM   2088 N  NE  . ARG   B 1 132 ? 10.472 -29.088 6.028  1.00 16.15 ? 138 ARG   C NE  1 
ATOM   2089 C  CZ  . ARG   B 1 132 ? 9.218  -29.464 6.244  1.00 17.31 ? 138 ARG   C CZ  1 
ATOM   2090 N  NH1 . ARG   B 1 132 ? 8.824  -30.694 5.939  1.00 15.57 ? 138 ARG   C NH1 1 
ATOM   2091 N  NH2 . ARG   B 1 132 ? 8.346  -28.616 6.777  1.00 16.91 ? 138 ARG   C NH2 1 
ATOM   2092 N  N   . ASP   B 1 133 ? 13.838 -25.355 3.048  1.00 15.52 ? 139 ASP   C N   1 
ATOM   2093 C  CA  . ASP   B 1 133 ? 13.903 -24.515 1.837  1.00 16.53 ? 139 ASP   C CA  1 
ATOM   2094 C  C   . ASP   B 1 133 ? 15.285 -23.968 1.546  1.00 17.80 ? 139 ASP   C C   1 
ATOM   2095 O  O   . ASP   B 1 133 ? 15.502 -23.444 0.441  1.00 19.63 ? 139 ASP   C O   1 
ATOM   2096 C  CB  . ASP   B 1 133 ? 12.896 -23.344 1.904  1.00 18.63 ? 139 ASP   C CB  1 
ATOM   2097 C  CG  . ASP   B 1 133 ? 13.232 -22.363 3.011  1.00 22.54 ? 139 ASP   C CG  1 
ATOM   2098 O  OD1 . ASP   B 1 133 ? 13.534 -22.828 4.146  1.00 22.12 ? 139 ASP   C OD1 1 
ATOM   2099 O  OD2 . ASP   B 1 133 ? 13.187 -21.133 2.751  1.00 23.59 ? 139 ASP   C OD2 1 
ATOM   2100 N  N   . LEU   B 1 134 ? 16.237 -24.090 2.490  1.00 17.05 ? 140 LEU   C N   1 
ATOM   2101 C  CA  . LEU   B 1 134 ? 17.594 -23.560 2.330  1.00 18.51 ? 140 LEU   C CA  1 
ATOM   2102 C  C   . LEU   B 1 134 ? 18.461 -24.526 1.554  1.00 19.13 ? 140 LEU   C C   1 
ATOM   2103 O  O   . LEU   B 1 134 ? 19.339 -25.207 2.124  1.00 20.22 ? 140 LEU   C O   1 
ATOM   2104 C  CB  . LEU   B 1 134 ? 18.195 -23.234 3.709  1.00 19.28 ? 140 LEU   C CB  1 
ATOM   2105 C  CG  . LEU   B 1 134 ? 17.342 -22.264 4.563  1.00 20.59 ? 140 LEU   C CG  1 
ATOM   2106 C  CD1 . LEU   B 1 134 ? 17.980 -22.068 5.958  1.00 21.27 ? 140 LEU   C CD1 1 
ATOM   2107 C  CD2 . LEU   B 1 134 ? 17.186 -20.899 3.865  1.00 21.75 ? 140 LEU   C CD2 1 
ATOM   2108 N  N   . LEU   B 1 135 ? 18.217 -24.617 0.240  1.00 18.56 ? 141 LEU   C N   1 
ATOM   2109 C  CA  . LEU   B 1 135 ? 18.889 -25.601 -0.604 1.00 19.51 ? 141 LEU   C CA  1 
ATOM   2110 C  C   . LEU   B 1 135 ? 20.400 -25.441 -0.651 1.00 21.45 ? 141 LEU   C C   1 
ATOM   2111 O  O   . LEU   B 1 135 ? 21.100 -26.450 -0.788 1.00 23.35 ? 141 LEU   C O   1 
ATOM   2112 C  CB  . LEU   B 1 135 ? 18.306 -25.605 -2.025 1.00 18.90 ? 141 LEU   C CB  1 
ATOM   2113 C  CG  . LEU   B 1 135 ? 16.783 -25.604 -2.139 1.00 18.85 ? 141 LEU   C CG  1 
ATOM   2114 C  CD1 . LEU   B 1 135 ? 16.359 -25.769 -3.596 1.00 19.86 ? 141 LEU   C CD1 1 
ATOM   2115 C  CD2 . LEU   B 1 135 ? 16.103 -26.687 -1.233 1.00 20.01 ? 141 LEU   C CD2 1 
ATOM   2116 N  N   . TRP   B 1 136 ? 20.904 -24.186 -0.540 1.00 21.90 ? 142 TRP   C N   1 
ATOM   2117 C  CA  . TRP   B 1 136 ? 22.340 -23.894 -0.572 1.00 22.74 ? 142 TRP   C CA  1 
ATOM   2118 C  C   . TRP   B 1 136 ? 23.119 -24.510 0.601  1.00 23.42 ? 142 TRP   C C   1 
ATOM   2119 O  O   . TRP   B 1 136 ? 24.352 -24.552 0.546  1.00 23.35 ? 142 TRP   C O   1 
ATOM   2120 C  CB  . TRP   B 1 136 ? 22.582 -22.375 -0.616 1.00 22.93 ? 142 TRP   C CB  1 
ATOM   2121 C  CG  . TRP   B 1 136 ? 21.874 -21.617 0.478  1.00 22.61 ? 142 TRP   C CG  1 
ATOM   2122 C  CD1 . TRP   B 1 136 ? 20.627 -21.064 0.423  1.00 22.83 ? 142 TRP   C CD1 1 
ATOM   2123 C  CD2 . TRP   B 1 136 ? 22.404 -21.292 1.779  1.00 21.82 ? 142 TRP   C CD2 1 
ATOM   2124 N  NE1 . TRP   B 1 136 ? 20.346 -20.420 1.610  1.00 22.87 ? 142 TRP   C NE1 1 
ATOM   2125 C  CE2 . TRP   B 1 136 ? 21.433 -20.530 2.446  1.00 22.38 ? 142 TRP   C CE2 1 
ATOM   2126 C  CE3 . TRP   B 1 136 ? 23.642 -21.508 2.409  1.00 22.14 ? 142 TRP   C CE3 1 
ATOM   2127 C  CZ2 . TRP   B 1 136 ? 21.633 -20.037 3.735  1.00 22.46 ? 142 TRP   C CZ2 1 
ATOM   2128 C  CZ3 . TRP   B 1 136 ? 23.845 -20.997 3.680  1.00 22.49 ? 142 TRP   C CZ3 1 
ATOM   2129 C  CH2 . TRP   B 1 136 ? 22.842 -20.286 4.335  1.00 22.44 ? 142 TRP   C CH2 1 
ATOM   2130 N  N   . LEU   B 1 137 ? 22.428 -24.970 1.675  1.00 23.21 ? 143 LEU   C N   1 
ATOM   2131 C  CA  . LEU   B 1 137 ? 23.137 -25.605 2.796  1.00 24.23 ? 143 LEU   C CA  1 
ATOM   2132 C  C   . LEU   B 1 137 ? 23.885 -26.875 2.319  1.00 27.46 ? 143 LEU   C C   1 
ATOM   2133 O  O   . LEU   B 1 137 ? 24.901 -27.228 2.913  1.00 27.59 ? 143 LEU   C O   1 
ATOM   2134 C  CB  . LEU   B 1 137 ? 22.152 -26.000 3.905  1.00 22.72 ? 143 LEU   C CB  1 
ATOM   2135 C  CG  . LEU   B 1 137 ? 21.651 -24.862 4.789  1.00 22.43 ? 143 LEU   C CG  1 
ATOM   2136 C  CD1 . LEU   B 1 137 ? 20.591 -25.367 5.766  1.00 21.56 ? 143 LEU   C CD1 1 
ATOM   2137 C  CD2 . LEU   B 1 137 ? 22.806 -24.213 5.534  1.00 22.77 ? 143 LEU   C CD2 1 
ATOM   2138 N  N   . ASP   B 1 138 ? 23.362 -27.554 1.277  1.00 29.98 ? 144 ASP   C N   1 
ATOM   2139 C  CA  . ASP   B 1 138 ? 23.894 -28.800 0.710  1.00 33.99 ? 144 ASP   C CA  1 
ATOM   2140 C  C   . ASP   B 1 138 ? 25.014 -28.621 -0.289 1.00 37.77 ? 144 ASP   C C   1 
ATOM   2141 O  O   . ASP   B 1 138 ? 25.435 -29.613 -0.879 1.00 38.68 ? 144 ASP   C O   1 
ATOM   2142 C  CB  . ASP   B 1 138 ? 22.787 -29.550 -0.034 1.00 35.81 ? 144 ASP   C CB  1 
ATOM   2143 C  CG  . ASP   B 1 138 ? 21.788 -30.224 0.849  1.00 40.91 ? 144 ASP   C CG  1 
ATOM   2144 O  OD1 . ASP   B 1 138 ? 22.166 -30.621 1.969  1.00 42.64 ? 144 ASP   C OD1 1 
ATOM   2145 O  OD2 . ASP   B 1 138 ? 20.622 -30.372 0.418  1.00 43.93 ? 144 ASP   C OD2 1 
ATOM   2146 N  N   . GLU   B 1 139 ? 25.452 -27.391 -0.546 1.00 39.81 ? 145 GLU   C N   1 
ATOM   2147 C  CA  . GLU   B 1 139 ? 26.531 -27.146 -1.491 1.00 42.75 ? 145 GLU   C CA  1 
ATOM   2148 C  C   . GLU   B 1 139 ? 27.473 -26.083 -0.926 1.00 44.79 ? 145 GLU   C C   1 
ATOM   2149 O  O   . GLU   B 1 139 ? 28.620 -25.981 -1.367 1.00 46.27 ? 145 GLU   C O   1 
ATOM   2150 C  CB  . GLU   B 1 139 ? 25.952 -26.702 -2.836 1.00 45.89 ? 145 GLU   C CB  1 
ATOM   2151 C  CG  . GLU   B 1 139 ? 25.180 -25.403 -2.754 1.00 51.79 ? 145 GLU   C CG  1 
ATOM   2152 C  CD  . GLU   B 1 139 ? 24.040 -25.323 -3.748 1.00 60.95 ? 145 GLU   C CD  1 
ATOM   2153 O  OE1 . GLU   B 1 139 ? 23.842 -24.242 -4.351 1.00 63.19 ? 145 GLU   C OE1 1 
ATOM   2154 O  OE2 . GLU   B 1 139 ? 23.346 -26.350 -3.926 1.00 63.64 ? 145 GLU   C OE2 1 
HETATM 2155 N  N1  . A1B2E C 2 .   ? 25.148 14.027  10.246 1.00 25.67 ? 201 A1B2E A N1  1 
HETATM 2156 C  C4  . A1B2E C 2 .   ? 23.977 14.120  9.554  1.00 25.05 ? 201 A1B2E A C4  1 
HETATM 2157 C  C5  . A1B2E C 2 .   ? 26.400 14.024  9.504  1.00 27.51 ? 201 A1B2E A C5  1 
HETATM 2158 C  C6  . A1B2E C 2 .   ? 26.732 12.739  8.796  1.00 29.21 ? 201 A1B2E A C6  1 
HETATM 2159 C  C7  . A1B2E C 2 .   ? 26.985 10.560  8.392  1.00 29.59 ? 201 A1B2E A C7  1 
HETATM 2160 C  C8  . A1B2E C 2 .   ? 26.809 9.189   8.406  1.00 28.95 ? 201 A1B2E A C8  1 
HETATM 2161 C  C10 . A1B2E C 2 .   ? 25.103 9.509   10.075 1.00 28.73 ? 201 A1B2E A C10 1 
HETATM 2162 C  C13 . A1B2E C 2 .   ? 25.331 14.119  11.701 1.00 24.48 ? 201 A1B2E A C13 1 
HETATM 2163 O  O1  . A1B2E C 2 .   ? 23.933 14.084  8.331  1.00 25.88 ? 201 A1B2E A O1  1 
HETATM 2164 C  C3  . A1B2E C 2 .   ? 22.713 14.358  10.338 1.00 24.60 ? 201 A1B2E A C3  1 
HETATM 2165 C  C2  . A1B2E C 2 .   ? 22.939 14.878  11.758 1.00 24.06 ? 201 A1B2E A C2  1 
HETATM 2166 C  C1  . A1B2E C 2 .   ? 24.003 14.026  12.468 1.00 24.00 ? 201 A1B2E A C1  1 
HETATM 2167 C  C   . A1B2E C 2 .   ? 24.192 14.475  13.908 1.00 23.35 ? 201 A1B2E A C   1 
HETATM 2168 O  O   . A1B2E C 2 .   ? 24.628 15.594  14.173 1.00 23.04 ? 201 A1B2E A O   1 
HETATM 2169 N  N   . A1B2E C 2 .   ? 23.843 13.604  14.842 1.00 22.65 ? 201 A1B2E A N   1 
HETATM 2170 C  C12 . A1B2E C 2 .   ? 26.285 11.419  9.223  1.00 29.03 ? 201 A1B2E A C12 1 
HETATM 2171 O  O2  . A1B2E C 2 .   ? 27.765 11.265  7.534  1.00 30.97 ? 201 A1B2E A O2  1 
HETATM 2172 N  N2  . A1B2E C 2 .   ? 27.566 12.661  7.818  1.00 30.57 ? 201 A1B2E A N2  1 
HETATM 2173 C  C11 . A1B2E C 2 .   ? 25.318 10.880  10.067 1.00 28.88 ? 201 A1B2E A C11 1 
HETATM 2174 C  C9  . A1B2E C 2 .   ? 25.853 8.671   9.267  1.00 28.92 ? 201 A1B2E A C9  1 
HETATM 2175 ZN ZN  . ZN    D 3 .   ? 23.128 -5.504  27.053 1.00 22.63 2 202 ZN    A ZN  1 
HETATM 2176 S  S   . DMS   E 4 .   ? 15.403 -0.296  12.128 1.00 41.53 ? 203 DMS   A S   1 
HETATM 2177 O  O   . DMS   E 4 .   ? 16.419 -0.886  13.046 1.00 39.57 ? 203 DMS   A O   1 
HETATM 2178 C  C1  . DMS   E 4 .   ? 14.472 0.996   13.048 1.00 41.18 ? 203 DMS   A C1  1 
HETATM 2179 C  C2  . DMS   E 4 .   ? 13.992 -1.433  12.059 1.00 41.80 ? 203 DMS   A C2  1 
HETATM 2180 N  N1  . A1B2E F 2 .   ? 11.000 -16.451 22.869 1.00 26.44 ? 201 A1B2E C N1  1 
HETATM 2181 C  C4  . A1B2E F 2 .   ? 12.236 -16.431 23.440 1.00 26.30 ? 201 A1B2E C C4  1 
HETATM 2182 C  C5  . A1B2E F 2 .   ? 9.842  -16.412 23.752 1.00 27.69 ? 201 A1B2E C C5  1 
HETATM 2183 C  C6  . A1B2E F 2 .   ? 9.508  -17.716 24.432 1.00 29.18 ? 201 A1B2E C C6  1 
HETATM 2184 C  C7  . A1B2E F 2 .   ? 9.162  -19.895 24.801 1.00 29.25 ? 201 A1B2E C C7  1 
HETATM 2185 C  C8  . A1B2E F 2 .   ? 9.254  -21.271 24.739 1.00 28.77 ? 201 A1B2E C C8  1 
HETATM 2186 C  C10 . A1B2E F 2 .   ? 10.806 -21.007 22.917 1.00 28.38 ? 201 A1B2E C C10 1 
HETATM 2187 C  C13 . A1B2E F 2 .   ? 10.672 -16.361 21.438 1.00 24.72 ? 201 A1B2E C C13 1 
HETATM 2188 O  O1  . A1B2E F 2 .   ? 12.405 -16.520 24.650 1.00 27.15 ? 201 A1B2E C O1  1 
HETATM 2189 C  C3  . A1B2E F 2 .   ? 13.428 -16.264 22.530 1.00 24.81 ? 201 A1B2E C C3  1 
HETATM 2190 C  C2  . A1B2E F 2 .   ? 13.084 -15.743 21.137 1.00 23.83 ? 201 A1B2E C C2  1 
HETATM 2191 C  C1  . A1B2E F 2 .   ? 11.907 -16.528 20.542 1.00 23.85 ? 201 A1B2E C C1  1 
HETATM 2192 C  C   . A1B2E F 2 .   ? 11.596 -16.052 19.132 1.00 22.97 ? 201 A1B2E C C   1 
HETATM 2193 O  O   . A1B2E F 2 .   ? 11.174 -14.908 18.924 1.00 22.30 ? 201 A1B2E C O   1 
HETATM 2194 N  N   . A1B2E F 2 .   ? 11.809 -16.931 18.163 1.00 21.50 ? 201 A1B2E C N   1 
HETATM 2195 C  C12 . A1B2E F 2 .   ? 9.823  -19.053 23.920 1.00 28.85 ? 201 A1B2E C C12 1 
HETATM 2196 O  O2  . A1B2E F 2 .   ? 8.528  -19.171 25.760 1.00 29.84 ? 201 A1B2E C O2  1 
HETATM 2197 N  N2  . A1B2E F 2 .   ? 8.784  -17.778 25.495 1.00 29.90 ? 201 A1B2E C N2  1 
HETATM 2198 C  C11 . A1B2E F 2 .   ? 10.668 -19.626 22.971 1.00 28.26 ? 201 A1B2E C C11 1 
HETATM 2199 C  C9  . A1B2E F 2 .   ? 10.092 -21.823 23.779 1.00 28.61 ? 201 A1B2E C C9  1 
HETATM 2200 S  S   . DMS   G 4 .   ? 3.692  -20.055 19.254 1.00 67.26 ? 202 DMS   C S   1 
HETATM 2201 O  O   . DMS   G 4 .   ? 4.675  -19.040 18.756 1.00 67.06 ? 202 DMS   C O   1 
HETATM 2202 C  C1  . DMS   G 4 .   ? 3.171  -19.592 20.937 1.00 67.24 ? 202 DMS   C C1  1 
HETATM 2203 C  C2  . DMS   G 4 .   ? 4.556  -21.546 19.773 1.00 67.19 ? 202 DMS   C C2  1 
HETATM 2204 ZN ZN  . ZN    H 3 .   ? 10.481 -35.587 5.520  1.00 17.77 2 203 ZN    C ZN  1 
HETATM 2205 S  S   . DMS   I 4 .   ? 19.890 -31.425 19.482 1.00 49.62 ? 204 DMS   C S   1 
HETATM 2206 O  O   . DMS   I 4 .   ? 18.460 -31.647 19.197 1.00 48.04 ? 204 DMS   C O   1 
HETATM 2207 C  C1  . DMS   I 4 .   ? 20.134 -30.768 21.159 1.00 49.56 ? 204 DMS   C C1  1 
HETATM 2208 C  C2  . DMS   I 4 .   ? 20.576 -29.967 18.647 1.00 49.38 ? 204 DMS   C C2  1 
HETATM 2209 O  O   . HOH   J 5 .   ? 11.572 -1.865  27.982 1.00 31.07 ? 301 HOH   A O   1 
HETATM 2210 O  O   . HOH   J 5 .   ? 14.953 22.066  24.660 1.00 35.50 ? 302 HOH   A O   1 
HETATM 2211 O  O   . HOH   J 5 .   ? -1.821 15.460  20.266 1.00 36.07 ? 303 HOH   A O   1 
HETATM 2212 O  O   . HOH   J 5 .   ? -0.418 15.459  15.717 1.00 44.11 ? 304 HOH   A O   1 
HETATM 2213 O  O   . HOH   J 5 .   ? 12.913 -4.673  20.530 1.00 40.84 ? 305 HOH   A O   1 
HETATM 2214 O  O   . HOH   J 5 .   ? 35.758 10.982  9.799  1.00 47.28 ? 306 HOH   A O   1 
HETATM 2215 O  O   . HOH   J 5 .   ? 34.894 14.759  25.123 1.00 45.13 ? 307 HOH   A O   1 
HETATM 2216 O  O   . HOH   J 5 .   ? 14.402 -5.542  27.150 1.00 32.90 ? 308 HOH   A O   1 
HETATM 2217 O  O   . HOH   J 5 .   ? 35.530 -0.341  28.275 1.00 63.05 ? 309 HOH   A O   1 
HETATM 2218 O  O   . HOH   J 5 .   ? 25.500 17.753  12.682 1.00 23.08 ? 310 HOH   A O   1 
HETATM 2219 O  O   . HOH   J 5 .   ? 34.958 14.027  16.102 1.00 34.56 ? 311 HOH   A O   1 
HETATM 2220 O  O   . HOH   J 5 .   ? 27.018 19.079  14.863 1.00 22.31 ? 312 HOH   A O   1 
HETATM 2221 O  O   . HOH   J 5 .   ? 12.990 -0.887  33.766 1.00 51.86 ? 313 HOH   A O   1 
HETATM 2222 O  O   . HOH   J 5 .   ? 23.814 7.492   28.254 1.00 25.63 ? 314 HOH   A O   1 
HETATM 2223 O  O   . HOH   J 5 .   ? 23.827 1.839   -0.695 1.00 17.78 ? 315 HOH   A O   1 
HETATM 2224 O  O   . HOH   J 5 .   ? 11.086 21.096  24.457 1.00 30.71 ? 316 HOH   A O   1 
HETATM 2225 O  O   . HOH   J 5 .   ? 17.122 20.669  22.843 1.00 21.33 ? 317 HOH   A O   1 
HETATM 2226 O  O   . HOH   J 5 .   ? 22.580 6.689   1.692  1.00 22.85 ? 318 HOH   A O   1 
HETATM 2227 O  O   . HOH   J 5 .   ? 6.408  2.979   28.947 1.00 50.13 ? 319 HOH   A O   1 
HETATM 2228 O  O   . HOH   J 5 .   ? 7.007  15.505  29.099 1.00 42.03 ? 320 HOH   A O   1 
HETATM 2229 O  O   . HOH   J 5 .   ? 28.578 -6.159  3.612  1.00 30.34 ? 321 HOH   A O   1 
HETATM 2230 O  O   . HOH   J 5 .   ? 14.974 8.500   13.314 1.00 17.78 ? 322 HOH   A O   1 
HETATM 2231 O  O   . HOH   J 5 .   ? 16.198 -0.747  4.756  1.00 34.57 ? 323 HOH   A O   1 
HETATM 2232 O  O   . HOH   J 5 .   ? 4.001  20.087  15.345 1.00 35.01 ? 324 HOH   A O   1 
HETATM 2233 O  O   . HOH   J 5 .   ? 30.742 19.999  7.807  1.00 41.60 ? 325 HOH   A O   1 
HETATM 2234 O  O   . HOH   J 5 .   ? 28.518 15.977  10.907 1.00 35.55 ? 326 HOH   A O   1 
HETATM 2235 O  O   . HOH   J 5 .   ? 6.571  -1.916  24.329 1.00 37.41 ? 327 HOH   A O   1 
HETATM 2236 O  O   . HOH   J 5 .   ? 18.664 -11.720 27.258 1.00 41.14 ? 328 HOH   A O   1 
HETATM 2237 O  O   . HOH   J 5 .   ? 32.206 2.852   5.071  1.00 33.29 ? 329 HOH   A O   1 
HETATM 2238 O  O   . HOH   J 5 .   ? 28.458 16.961  8.267  1.00 38.06 ? 330 HOH   A O   1 
HETATM 2239 O  O   . HOH   J 5 .   ? 34.469 -0.811  16.671 1.00 15.67 ? 331 HOH   A O   1 
HETATM 2240 O  O   . HOH   J 5 .   ? 35.021 -6.345  21.548 1.00 51.63 ? 332 HOH   A O   1 
HETATM 2241 O  O   . HOH   J 5 .   ? 31.016 -2.195  29.995 1.00 43.77 ? 333 HOH   A O   1 
HETATM 2242 O  O   . HOH   J 5 .   ? 17.781 -7.609  21.581 1.00 28.19 ? 334 HOH   A O   1 
HETATM 2243 O  O   . HOH   J 5 .   ? 24.890 15.110  5.968  1.00 52.41 ? 335 HOH   A O   1 
HETATM 2244 O  O   . HOH   J 5 .   ? 20.365 -7.646  2.053  1.00 43.51 ? 336 HOH   A O   1 
HETATM 2245 O  O   . HOH   J 5 .   ? 22.210 8.948   3.023  1.00 21.39 ? 337 HOH   A O   1 
HETATM 2246 O  O   . HOH   J 5 .   ? 23.610 10.986  21.358 1.00 16.89 ? 338 HOH   A O   1 
HETATM 2247 O  O   . HOH   J 5 .   ? 20.177 2.074   9.293  1.00 16.26 ? 339 HOH   A O   1 
HETATM 2248 O  O   . HOH   J 5 .   ? 29.764 7.259   4.622  1.00 32.21 ? 340 HOH   A O   1 
HETATM 2249 O  O   . HOH   J 5 .   ? 7.344  7.722   31.904 1.00 39.17 ? 341 HOH   A O   1 
HETATM 2250 O  O   . HOH   J 5 .   ? 11.188 -0.276  15.933 1.00 24.90 ? 342 HOH   A O   1 
HETATM 2251 O  O   . HOH   J 5 .   ? 19.973 11.747  8.601  1.00 22.91 ? 343 HOH   A O   1 
HETATM 2252 O  O   . HOH   J 5 .   ? 4.266  4.100   28.126 1.00 47.08 ? 344 HOH   A O   1 
HETATM 2253 O  O   . HOH   J 5 .   ? 37.099 7.457   3.982  1.00 38.56 ? 345 HOH   A O   1 
HETATM 2254 O  O   . HOH   J 5 .   ? 4.119  9.948   18.022 1.00 42.47 ? 346 HOH   A O   1 
HETATM 2255 O  O   . HOH   J 5 .   ? 23.958 3.985   29.438 1.00 24.47 ? 347 HOH   A O   1 
HETATM 2256 O  O   . HOH   J 5 .   ? 25.123 4.364   -1.142 1.00 21.87 ? 348 HOH   A O   1 
HETATM 2257 O  O   . HOH   J 5 .   ? 17.369 0.292   2.369  1.00 36.31 ? 349 HOH   A O   1 
HETATM 2258 O  O   . HOH   J 5 .   ? 22.948 20.803  20.214 1.00 27.69 ? 350 HOH   A O   1 
HETATM 2259 O  O   . HOH   J 5 .   ? 22.941 -11.090 30.966 1.00 53.97 ? 351 HOH   A O   1 
HETATM 2260 O  O   . HOH   J 5 .   ? 3.339  2.627   19.154 1.00 31.40 ? 352 HOH   A O   1 
HETATM 2261 O  O   . HOH   J 5 .   ? 28.071 3.103   -0.193 1.00 23.72 ? 353 HOH   A O   1 
HETATM 2262 O  O   . HOH   J 5 .   ? 5.031  10.815  12.281 1.00 41.79 ? 354 HOH   A O   1 
HETATM 2263 O  O   . HOH   J 5 .   ? 2.689  8.565   26.049 1.00 36.48 ? 355 HOH   A O   1 
HETATM 2264 O  O   . HOH   J 5 .   ? 23.750 16.638  27.477 1.00 57.46 ? 356 HOH   A O   1 
HETATM 2265 O  O   . HOH   J 5 .   ? 17.204 18.451  15.486 1.00 17.33 ? 357 HOH   A O   1 
HETATM 2266 O  O   . HOH   J 5 .   ? 30.785 5.212   7.731  1.00 22.97 ? 358 HOH   A O   1 
HETATM 2267 O  O   . HOH   J 5 .   ? 8.867  3.942   11.883 1.00 36.78 ? 359 HOH   A O   1 
HETATM 2268 O  O   . HOH   J 5 .   ? 16.898 4.448   5.937  1.00 29.02 ? 360 HOH   A O   1 
HETATM 2269 O  O   . HOH   J 5 .   ? 19.470 -5.976  32.870 1.00 44.85 ? 361 HOH   A O   1 
HETATM 2270 O  O   . HOH   J 5 .   ? 28.342 0.829   26.783 1.00 26.30 ? 362 HOH   A O   1 
HETATM 2271 O  O   . HOH   J 5 .   ? 16.513 8.960   6.815  1.00 26.99 ? 363 HOH   A O   1 
HETATM 2272 O  O   . HOH   J 5 .   ? 18.391 22.179  7.129  1.00 48.67 ? 364 HOH   A O   1 
HETATM 2273 O  O   . HOH   J 5 .   ? 4.969  3.067   21.023 1.00 28.77 ? 365 HOH   A O   1 
HETATM 2274 O  O   . HOH   J 5 .   ? 29.727 25.901  15.836 1.00 49.85 ? 366 HOH   A O   1 
HETATM 2275 O  O   . HOH   J 5 .   ? 34.526 3.438   26.297 1.00 28.51 ? 367 HOH   A O   1 
HETATM 2276 O  O   . HOH   J 5 .   ? 30.351 -5.826  26.445 1.00 30.83 ? 368 HOH   A O   1 
HETATM 2277 O  O   . HOH   J 5 .   ? 25.347 1.700   29.829 1.00 28.84 ? 369 HOH   A O   1 
HETATM 2278 O  O   . HOH   J 5 .   ? 3.482  18.148  23.579 1.00 29.83 ? 370 HOH   A O   1 
HETATM 2279 O  O   . HOH   J 5 .   ? 28.924 12.300  11.566 1.00 31.93 ? 371 HOH   A O   1 
HETATM 2280 O  O   . HOH   J 5 .   ? 29.426 6.447   30.010 1.00 39.29 ? 372 HOH   A O   1 
HETATM 2281 O  O   . HOH   J 5 .   ? 29.831 -2.234  8.410  1.00 26.96 ? 373 HOH   A O   1 
HETATM 2282 O  O   . HOH   J 5 .   ? 32.094 8.687   4.538  1.00 42.31 ? 374 HOH   A O   1 
HETATM 2283 O  O   . HOH   J 5 .   ? 35.633 14.657  20.263 1.00 28.09 ? 375 HOH   A O   1 
HETATM 2284 O  O   . HOH   J 5 .   ? 4.030  19.975  21.642 1.00 28.15 ? 376 HOH   A O   1 
HETATM 2285 O  O   . HOH   J 5 .   ? 17.340 2.047   9.298  1.00 22.23 ? 377 HOH   A O   1 
HETATM 2286 O  O   . HOH   J 5 .   ? 21.590 9.900   23.268 1.00 16.51 ? 378 HOH   A O   1 
HETATM 2287 O  O   . HOH   J 5 .   ? 18.292 -5.192  30.514 1.00 29.42 ? 379 HOH   A O   1 
HETATM 2288 O  O   . HOH   J 5 .   ? 15.646 12.150  30.556 1.00 42.77 ? 380 HOH   A O   1 
HETATM 2289 O  O   . HOH   J 5 .   ? 30.135 -2.206  3.476  1.00 41.17 ? 381 HOH   A O   1 
HETATM 2290 O  O   . HOH   J 5 .   ? 4.726  10.697  14.979 1.00 44.86 ? 382 HOH   A O   1 
HETATM 2291 O  O   . HOH   J 5 .   ? 22.526 -6.196  0.430  1.00 58.95 ? 383 HOH   A O   1 
HETATM 2292 O  O   . HOH   J 5 .   ? 21.366 13.759  6.916  1.00 45.62 ? 384 HOH   A O   1 
HETATM 2293 O  O   . HOH   J 5 .   ? 14.750 -4.032  16.235 1.00 31.15 ? 385 HOH   A O   1 
HETATM 2294 O  O   . HOH   J 5 .   ? 16.396 18.647  27.225 1.00 52.59 ? 386 HOH   A O   1 
HETATM 2295 O  O   . HOH   J 5 .   ? 17.787 20.004  13.380 1.00 25.26 ? 387 HOH   A O   1 
HETATM 2296 O  O   . HOH   J 5 .   ? 11.482 10.636  9.706  1.00 48.07 ? 388 HOH   A O   1 
HETATM 2297 O  O   . HOH   J 5 .   ? 29.009 -7.836  25.732 1.00 63.20 ? 389 HOH   A O   1 
HETATM 2298 O  O   . HOH   J 5 .   ? 32.276 14.767  12.952 1.00 40.31 ? 390 HOH   A O   1 
HETATM 2299 O  O   . HOH   J 5 .   ? 19.763 -4.739  15.309 1.00 29.37 ? 391 HOH   A O   1 
HETATM 2300 O  O   . HOH   J 5 .   ? 27.820 25.812  18.004 1.00 62.19 ? 392 HOH   A O   1 
HETATM 2301 O  O   . HOH   J 5 .   ? 24.872 -8.649  24.628 1.00 44.22 ? 393 HOH   A O   1 
HETATM 2302 O  O   . HOH   J 5 .   ? 19.966 13.970  29.001 1.00 30.68 ? 394 HOH   A O   1 
HETATM 2303 O  O   . HOH   J 5 .   ? 12.335 18.450  26.406 1.00 29.33 ? 395 HOH   A O   1 
HETATM 2304 O  O   . HOH   J 5 .   ? 12.125 -2.852  15.839 1.00 37.18 ? 396 HOH   A O   1 
HETATM 2305 O  O   . HOH   J 5 .   ? 20.470 20.477  24.293 1.00 30.64 ? 397 HOH   A O   1 
HETATM 2306 O  O   . HOH   J 5 .   ? 30.587 -3.153  11.924 1.00 34.36 ? 398 HOH   A O   1 
HETATM 2307 O  O   . HOH   J 5 .   ? 32.068 22.180  10.975 1.00 39.74 ? 399 HOH   A O   1 
HETATM 2308 O  O   . HOH   J 5 .   ? 24.077 17.520  6.060  1.00 38.52 ? 400 HOH   A O   1 
HETATM 2309 O  O   . HOH   J 5 .   ? 6.763  16.206  8.827  1.00 39.39 ? 401 HOH   A O   1 
HETATM 2310 O  O   . HOH   J 5 .   ? 29.405 25.634  12.942 1.00 40.38 ? 402 HOH   A O   1 
HETATM 2311 O  O   . HOH   J 5 .   ? 3.808  14.571  10.414 1.00 31.09 ? 403 HOH   A O   1 
HETATM 2312 O  O   . HOH   J 5 .   ? 25.976 -8.495  22.514 1.00 43.84 ? 404 HOH   A O   1 
HETATM 2313 O  O   . HOH   J 5 .   ? 28.745 22.103  21.983 1.00 39.05 ? 405 HOH   A O   1 
HETATM 2314 O  O   . HOH   J 5 .   ? 33.048 -2.776  15.367 1.00 27.82 ? 406 HOH   A O   1 
HETATM 2315 O  O   . HOH   J 5 .   ? 12.608 17.972  13.294 1.00 37.03 ? 407 HOH   A O   1 
HETATM 2316 O  O   . HOH   J 5 .   ? 19.788 -9.812  20.723 1.00 43.85 ? 408 HOH   A O   1 
HETATM 2317 O  O   . HOH   J 5 .   ? 27.948 11.926  27.719 1.00 24.71 ? 409 HOH   A O   1 
HETATM 2318 O  O   . HOH   J 5 .   ? 31.631 12.823  9.171  1.00 54.28 ? 410 HOH   A O   1 
HETATM 2319 O  O   . HOH   J 5 .   ? 15.186 23.248  16.855 1.00 24.90 ? 411 HOH   A O   1 
HETATM 2320 O  O   . HOH   J 5 .   ? 22.473 -8.607  19.626 1.00 39.25 ? 412 HOH   A O   1 
HETATM 2321 O  O   . HOH   J 5 .   ? 11.213 2.080   12.272 1.00 30.10 ? 413 HOH   A O   1 
HETATM 2322 O  O   . HOH   J 5 .   ? 13.221 8.549   11.118 1.00 22.74 ? 414 HOH   A O   1 
HETATM 2323 O  O   . HOH   J 5 .   ? 26.844 19.362  24.634 1.00 52.31 ? 415 HOH   A O   1 
HETATM 2324 O  O   . HOH   J 5 .   ? 32.763 5.415   4.629  1.00 49.74 ? 416 HOH   A O   1 
HETATM 2325 O  O   . HOH   J 5 .   ? 31.832 -7.173  18.094 1.00 39.76 ? 417 HOH   A O   1 
HETATM 2326 O  O   . HOH   J 5 .   ? 2.367  13.986  25.350 1.00 53.63 ? 418 HOH   A O   1 
HETATM 2327 O  O   . HOH   J 5 .   ? 16.156 -5.288  12.611 1.00 32.15 ? 419 HOH   A O   1 
HETATM 2328 O  O   . HOH   J 5 .   ? 16.056 8.561   34.014 1.00 31.97 ? 420 HOH   A O   1 
HETATM 2329 O  O   . HOH   J 5 .   ? 4.429  6.240   13.507 1.00 55.01 ? 421 HOH   A O   1 
HETATM 2330 O  O   . HOH   J 5 .   ? 11.938 15.519  9.016  1.00 51.42 ? 422 HOH   A O   1 
HETATM 2331 O  O   . HOH   J 5 .   ? 31.503 10.335  14.260 1.00 42.04 ? 423 HOH   A O   1 
HETATM 2332 O  O   . HOH   J 5 .   ? 16.670 10.325  32.183 1.00 37.71 ? 424 HOH   A O   1 
HETATM 2333 O  O   . HOH   J 5 .   ? 18.013 10.841  6.665  1.00 27.40 ? 425 HOH   A O   1 
HETATM 2334 O  O   . HOH   J 5 .   ? 23.148 22.858  18.510 1.00 43.40 ? 426 HOH   A O   1 
HETATM 2335 O  O   . HOH   J 5 .   ? 6.687  -0.245  28.474 1.00 54.54 ? 427 HOH   A O   1 
HETATM 2336 O  O   . HOH   J 5 .   ? 16.651 -6.563  5.161  1.00 58.91 ? 428 HOH   A O   1 
HETATM 2337 O  O   . HOH   J 5 .   ? 26.009 18.183  26.763 1.00 50.31 ? 429 HOH   A O   1 
HETATM 2338 O  O   . HOH   J 5 .   ? 8.958  17.926  8.961  1.00 49.54 ? 430 HOH   A O   1 
HETATM 2339 O  O   . HOH   J 5 .   ? 33.076 0.780   6.102  1.00 35.11 ? 431 HOH   A O   1 
HETATM 2340 O  O   . HOH   J 5 .   ? 13.895 21.632  14.653 1.00 27.88 ? 432 HOH   A O   1 
HETATM 2341 O  O   . HOH   J 5 .   ? 28.124 1.625   29.402 1.00 31.48 ? 433 HOH   A O   1 
HETATM 2342 O  O   . HOH   J 5 .   ? 31.123 -2.808  5.765  1.00 33.95 ? 434 HOH   A O   1 
HETATM 2343 O  O   . HOH   J 5 .   ? 8.631  -2.386  27.738 1.00 43.75 ? 435 HOH   A O   1 
HETATM 2344 O  O   . HOH   J 5 .   ? 37.027 21.012  8.460  1.00 64.86 ? 436 HOH   A O   1 
HETATM 2345 O  O   . HOH   J 5 .   ? 9.320  21.768  12.271 1.00 33.54 ? 437 HOH   A O   1 
HETATM 2346 O  O   . HOH   J 5 .   ? 31.403 -3.816  9.866  1.00 30.14 ? 438 HOH   A O   1 
HETATM 2347 O  O   . HOH   J 5 .   ? 3.584  7.667   16.337 1.00 58.77 ? 439 HOH   A O   1 
HETATM 2348 O  O   . HOH   J 5 .   ? 34.775 11.482  15.007 1.00 52.03 ? 440 HOH   A O   1 
HETATM 2349 O  O   . HOH   J 5 .   ? 2.847  3.914   16.864 1.00 40.75 ? 441 HOH   A O   1 
HETATM 2350 O  O   . HOH   J 5 .   ? 28.381 -9.017  6.394  1.00 56.42 ? 442 HOH   A O   1 
HETATM 2351 O  O   . HOH   K 5 .   ? 13.421 -23.841 31.144 1.00 50.37 ? 301 HOH   C O   1 
HETATM 2352 O  O   . HOH   K 5 .   ? 23.738 -9.359  7.854  1.00 26.84 ? 302 HOH   C O   1 
HETATM 2353 O  O   . HOH   K 5 .   ? 22.019 -32.520 3.660  1.00 30.34 ? 303 HOH   C O   1 
HETATM 2354 O  O   . HOH   K 5 .   ? 2.714  -30.806 3.950  1.00 35.94 ? 304 HOH   C O   1 
HETATM 2355 O  O   . HOH   K 5 .   ? 21.047 -27.106 -4.732 1.00 50.20 ? 305 HOH   C O   1 
HETATM 2356 O  O   . HOH   K 5 .   ? 29.939 -10.279 10.303 1.00 47.80 ? 306 HOH   C O   1 
HETATM 2357 O  O   . HOH   K 5 .   ? 6.847  -36.605 29.146 1.00 40.91 ? 307 HOH   C O   1 
HETATM 2358 O  O   . HOH   K 5 .   ? 12.278 -29.275 33.423 1.00 22.51 ? 308 HOH   C O   1 
HETATM 2359 O  O   . HOH   K 5 .   ? 23.821 -37.340 9.889  1.00 55.65 ? 309 HOH   C O   1 
HETATM 2360 O  O   . HOH   K 5 .   ? 1.179  -33.510 20.573 1.00 34.17 ? 310 HOH   C O   1 
HETATM 2361 O  O   . HOH   K 5 .   ? 24.743 -20.559 20.513 1.00 53.86 ? 311 HOH   C O   1 
HETATM 2362 O  O   . HOH   K 5 .   ? 20.007 -8.435  7.555  1.00 43.06 ? 312 HOH   C O   1 
HETATM 2363 O  O   . HOH   K 5 .   ? 26.143 -33.016 5.826  1.00 43.61 ? 313 HOH   C O   1 
HETATM 2364 O  O   . HOH   K 5 .   ? 23.570 -31.316 14.915 1.00 32.69 ? 314 HOH   C O   1 
HETATM 2365 O  O   . HOH   K 5 .   ? 10.306 -27.384 33.511 1.00 29.63 ? 315 HOH   C O   1 
HETATM 2366 O  O   . HOH   K 5 .   ? 7.672  -14.204 22.742 1.00 45.63 ? 316 HOH   C O   1 
HETATM 2367 O  O   . HOH   K 5 .   ? 4.146  -35.911 21.400 1.00 27.96 ? 317 HOH   C O   1 
HETATM 2368 O  O   . HOH   K 5 .   ? 16.983 -37.904 2.997  1.00 35.47 ? 318 HOH   C O   1 
HETATM 2369 O  O   . HOH   K 5 .   ? 9.916  -26.046 3.505  1.00 19.00 ? 319 HOH   C O   1 
HETATM 2370 O  O   . HOH   K 5 .   ? 20.449 -22.452 18.590 1.00 16.87 ? 320 HOH   C O   1 
HETATM 2371 O  O   . HOH   K 5 .   ? 10.066 -22.704 4.842  1.00 22.83 ? 321 HOH   C O   1 
HETATM 2372 O  O   . HOH   K 5 .   ? 8.079  -13.239 25.317 1.00 47.61 ? 322 HOH   C O   1 
HETATM 2373 O  O   . HOH   K 5 .   ? 17.937 -10.089 9.288  1.00 21.39 ? 323 HOH   C O   1 
HETATM 2374 O  O   . HOH   K 5 .   ? 10.588 -12.776 20.527 1.00 22.69 ? 324 HOH   C O   1 
HETATM 2375 O  O   . HOH   K 5 .   ? 29.447 -27.983 9.662  1.00 27.00 ? 325 HOH   C O   1 
HETATM 2376 O  O   . HOH   K 5 .   ? 6.464  -23.245 28.512 1.00 47.13 ? 326 HOH   C O   1 
HETATM 2377 O  O   . HOH   K 5 .   ? 31.326 -10.828 16.533 1.00 32.08 ? 327 HOH   C O   1 
HETATM 2378 O  O   . HOH   K 5 .   ? 18.301 -30.802 30.112 1.00 37.54 ? 328 HOH   C O   1 
HETATM 2379 O  O   . HOH   K 5 .   ? 3.634  -23.259 3.656  1.00 31.76 ? 329 HOH   C O   1 
HETATM 2380 O  O   . HOH   K 5 .   ? 14.192 -19.628 0.718  1.00 36.15 ? 330 HOH   C O   1 
HETATM 2381 O  O   . HOH   K 5 .   ? 31.001 -21.325 12.953 1.00 31.93 ? 331 HOH   C O   1 
HETATM 2382 O  O   . HOH   K 5 .   ? 15.385 -28.798 23.070 1.00 19.08 ? 332 HOH   C O   1 
HETATM 2383 O  O   . HOH   K 5 .   ? 34.505 -10.974 10.521 1.00 40.77 ? 333 HOH   C O   1 
HETATM 2384 O  O   . HOH   K 5 .   ? 22.214 -12.371 17.382 1.00 26.99 ? 334 HOH   C O   1 
HETATM 2385 O  O   . HOH   K 5 .   ? 22.779 -36.198 12.177 1.00 41.71 ? 335 HOH   C O   1 
HETATM 2386 O  O   . HOH   K 5 .   ? 27.594 -15.037 2.561  1.00 43.56 ? 336 HOH   C O   1 
HETATM 2387 O  O   . HOH   K 5 .   ? 9.812  -40.119 0.675  1.00 49.58 ? 337 HOH   C O   1 
HETATM 2388 O  O   . HOH   K 5 .   ? 11.302 -19.495 11.553 1.00 18.90 ? 338 HOH   C O   1 
HETATM 2389 O  O   . HOH   K 5 .   ? 27.557 -27.511 2.187  1.00 42.16 ? 339 HOH   C O   1 
HETATM 2390 O  O   . HOH   K 5 .   ? 26.377 -22.768 -0.543 1.00 47.54 ? 340 HOH   C O   1 
HETATM 2391 O  O   . HOH   K 5 .   ? 18.211 -28.696 22.871 1.00 24.71 ? 341 HOH   C O   1 
HETATM 2392 O  O   . HOH   K 5 .   ? 11.384 -14.040 5.717  1.00 55.20 ? 342 HOH   C O   1 
HETATM 2393 O  O   . HOH   K 5 .   ? 8.401  -28.201 2.864  1.00 20.78 ? 343 HOH   C O   1 
HETATM 2394 O  O   . HOH   K 5 .   ? 16.226 -38.464 10.287 1.00 44.34 ? 344 HOH   C O   1 
HETATM 2395 O  O   . HOH   K 5 .   ? 8.873  -11.463 18.469 1.00 21.59 ? 345 HOH   C O   1 
HETATM 2396 O  O   . HOH   K 5 .   ? 29.564 -9.237  18.573 1.00 65.08 ? 346 HOH   C O   1 
HETATM 2397 O  O   . HOH   K 5 .   ? 16.323 -19.088 24.022 1.00 21.38 ? 347 HOH   C O   1 
HETATM 2398 O  O   . HOH   K 5 .   ? 31.221 -26.410 -2.323 1.00 52.93 ? 348 HOH   C O   1 
HETATM 2399 O  O   . HOH   K 5 .   ? 0.781  -31.428 17.090 1.00 18.11 ? 349 HOH   C O   1 
HETATM 2400 O  O   . HOH   K 5 .   ? 21.389 -36.614 9.820  1.00 38.76 ? 350 HOH   C O   1 
HETATM 2401 O  O   . HOH   K 5 .   ? 18.086 -11.731 5.515  1.00 37.97 ? 351 HOH   C O   1 
HETATM 2402 O  O   . HOH   K 5 .   ? 14.435 -22.176 29.718 1.00 26.28 ? 352 HOH   C O   1 
HETATM 2403 O  O   . HOH   K 5 .   ? 7.099  -38.832 7.169  1.00 42.49 ? 353 HOH   C O   1 
HETATM 2404 O  O   . HOH   K 5 .   ? 4.692  -25.477 25.259 1.00 34.63 ? 354 HOH   C O   1 
HETATM 2405 O  O   . HOH   K 5 .   ? 30.568 -20.373 18.919 1.00 36.49 ? 355 HOH   C O   1 
HETATM 2406 O  O   . HOH   K 5 .   ? 12.972 -20.590 9.366  1.00 17.35 ? 356 HOH   C O   1 
HETATM 2407 O  O   . HOH   K 5 .   ? 26.288 -33.150 13.680 1.00 32.27 ? 357 HOH   C O   1 
HETATM 2408 O  O   . HOH   K 5 .   ? 18.451 -12.321 16.986 1.00 20.16 ? 358 HOH   C O   1 
HETATM 2409 O  O   . HOH   K 5 .   ? 10.982 -36.271 31.522 1.00 38.48 ? 359 HOH   C O   1 
HETATM 2410 O  O   . HOH   K 5 .   ? 19.693 -22.304 25.454 1.00 31.68 ? 360 HOH   C O   1 
HETATM 2411 O  O   . HOH   K 5 .   ? 8.034  -5.357  14.684 1.00 43.58 ? 361 HOH   C O   1 
HETATM 2412 O  O   . HOH   K 5 .   ? -0.394 -15.317 14.012 1.00 31.68 ? 362 HOH   C O   1 
HETATM 2413 O  O   . HOH   K 5 .   ? 0.595  -16.594 17.877 1.00 27.24 ? 363 HOH   C O   1 
HETATM 2414 O  O   . HOH   K 5 .   ? 9.524  -10.017 11.192 1.00 42.09 ? 364 HOH   C O   1 
HETATM 2415 O  O   . HOH   K 5 .   ? 18.300 -10.920 19.105 1.00 34.17 ? 365 HOH   C O   1 
HETATM 2416 O  O   . HOH   K 5 .   ? 12.479 -6.283  22.360 1.00 25.14 ? 366 HOH   C O   1 
HETATM 2417 O  O   . HOH   K 5 .   ? 8.471  -38.426 9.507  1.00 31.99 ? 367 HOH   C O   1 
HETATM 2418 O  O   . HOH   K 5 .   ? 13.317 -12.598 26.804 1.00 34.35 ? 368 HOH   C O   1 
HETATM 2419 O  O   . HOH   K 5 .   ? 5.407  -17.803 25.283 1.00 59.44 ? 369 HOH   C O   1 
HETATM 2420 O  O   . HOH   K 5 .   ? 5.544  -32.332 29.535 1.00 64.65 ? 370 HOH   C O   1 
HETATM 2421 O  O   . HOH   K 5 .   ? 19.323 -27.079 25.427 1.00 37.03 ? 371 HOH   C O   1 
HETATM 2422 O  O   . HOH   K 5 .   ? 20.729 -28.577 -2.712 1.00 42.34 ? 372 HOH   C O   1 
HETATM 2423 O  O   . HOH   K 5 .   ? 5.525  -29.043 7.253  1.00 17.67 ? 373 HOH   C O   1 
HETATM 2424 O  O   . HOH   K 5 .   ? 14.215 -16.599 3.654  1.00 29.21 ? 374 HOH   C O   1 
HETATM 2425 O  O   . HOH   K 5 .   ? 3.630  -36.084 6.850  1.00 25.41 ? 375 HOH   C O   1 
HETATM 2426 O  O   . HOH   K 5 .   ? 0.340  -29.227 25.024 1.00 42.05 ? 376 HOH   C O   1 
HETATM 2427 O  O   . HOH   K 5 .   ? 7.862  -34.988 0.509  1.00 21.82 ? 377 HOH   C O   1 
HETATM 2428 O  O   . HOH   K 5 .   ? 19.820 -31.591 27.040 1.00 37.15 ? 378 HOH   C O   1 
HETATM 2429 O  O   . HOH   K 5 .   ? 28.510 -33.256 12.260 1.00 36.42 ? 379 HOH   C O   1 
HETATM 2430 O  O   . HOH   K 5 .   ? 7.123  -18.122 21.805 1.00 28.77 ? 380 HOH   C O   1 
HETATM 2431 O  O   . HOH   K 5 .   ? 36.555 -31.981 9.075  1.00 48.63 ? 381 HOH   C O   1 
HETATM 2432 O  O   . HOH   K 5 .   ? 14.963 -35.484 1.591  1.00 23.88 ? 382 HOH   C O   1 
HETATM 2433 O  O   . HOH   K 5 .   ? 22.090 -15.022 23.565 1.00 43.66 ? 383 HOH   C O   1 
HETATM 2434 O  O   . HOH   K 5 .   ? 14.914 -35.566 16.908 1.00 24.51 ? 384 HOH   C O   1 
HETATM 2435 O  O   . HOH   K 5 .   ? 6.523  -18.146 5.817  1.00 22.84 ? 385 HOH   C O   1 
HETATM 2436 O  O   . HOH   K 5 .   ? 24.020 -29.022 18.890 1.00 33.00 ? 386 HOH   C O   1 
HETATM 2437 O  O   . HOH   K 5 .   ? 19.461 -7.451  15.136 1.00 29.42 ? 387 HOH   C O   1 
HETATM 2438 O  O   . HOH   K 5 .   ? 18.318 -18.234 1.499  1.00 40.94 ? 388 HOH   C O   1 
HETATM 2439 O  O   . HOH   K 5 .   ? 16.400 -8.353  17.047 1.00 36.26 ? 389 HOH   C O   1 
HETATM 2440 O  O   . HOH   K 5 .   ? 3.500  -27.538 27.823 1.00 38.38 ? 390 HOH   C O   1 
HETATM 2441 O  O   . HOH   K 5 .   ? -2.356 -30.375 8.508  1.00 23.91 ? 391 HOH   C O   1 
HETATM 2442 O  O   . HOH   K 5 .   ? 32.824 -16.942 6.201  1.00 52.14 ? 392 HOH   C O   1 
HETATM 2443 O  O   . HOH   K 5 .   ? 4.245  -30.288 30.873 1.00 51.65 ? 393 HOH   C O   1 
HETATM 2444 O  O   . HOH   K 5 .   ? 14.426 -10.111 8.351  1.00 41.80 ? 394 HOH   C O   1 
HETATM 2445 O  O   . HOH   K 5 .   ? 5.694  -32.659 24.375 1.00 22.14 ? 395 HOH   C O   1 
HETATM 2446 O  O   . HOH   K 5 .   ? 4.350  -8.252  22.618 1.00 33.19 ? 396 HOH   C O   1 
HETATM 2447 O  O   . HOH   K 5 .   ? 16.423 -7.618  14.664 1.00 40.52 ? 397 HOH   C O   1 
HETATM 2448 O  O   . HOH   K 5 .   ? 29.167 -14.807 22.503 1.00 45.03 ? 398 HOH   C O   1 
HETATM 2449 O  O   . HOH   K 5 .   ? 23.242 -12.986 19.172 1.00 35.06 ? 399 HOH   C O   1 
HETATM 2450 O  O   . HOH   K 5 .   ? 12.262 -9.636  12.431 1.00 36.55 ? 400 HOH   C O   1 
HETATM 2451 O  O   . HOH   K 5 .   ? 31.170 -28.814 11.813 1.00 30.28 ? 401 HOH   C O   1 
HETATM 2452 O  O   . HOH   K 5 .   ? 11.014 -36.008 -0.628 1.00 34.72 ? 402 HOH   C O   1 
HETATM 2453 O  O   . HOH   K 5 .   ? -3.236 -18.470 27.650 1.00 43.89 ? 403 HOH   C O   1 
HETATM 2454 O  O   . HOH   K 5 .   ? 22.310 -12.324 5.515  1.00 32.19 ? 404 HOH   C O   1 
HETATM 2455 O  O   . HOH   K 5 .   ? 21.527 -34.990 35.216 1.00 60.67 ? 405 HOH   C O   1 
HETATM 2456 O  O   . HOH   K 5 .   ? 1.937  -17.556 5.897  1.00 36.23 ? 406 HOH   C O   1 
HETATM 2457 O  O   . HOH   K 5 .   ? 10.832 -15.054 3.203  1.00 45.76 ? 407 HOH   C O   1 
HETATM 2458 O  O   . HOH   K 5 .   ? 24.824 -23.996 19.877 1.00 35.02 ? 408 HOH   C O   1 
HETATM 2459 O  O   . HOH   K 5 .   ? 4.104  -33.495 22.317 1.00 32.58 ? 409 HOH   C O   1 
HETATM 2460 O  O   . HOH   K 5 .   ? 32.205 -16.631 20.648 1.00 27.02 ? 410 HOH   C O   1 
HETATM 2461 O  O   . HOH   K 5 .   ? 6.374  -8.099  11.587 1.00 31.66 ? 411 HOH   C O   1 
HETATM 2462 O  O   . HOH   K 5 .   ? 8.045  -39.515 24.576 1.00 54.43 ? 412 HOH   C O   1 
HETATM 2463 O  O   . HOH   K 5 .   ? 1.387  -34.197 17.915 1.00 23.89 ? 413 HOH   C O   1 
HETATM 2464 O  O   . HOH   K 5 .   ? 21.805 -12.064 21.196 1.00 49.41 ? 414 HOH   C O   1 
HETATM 2465 O  O   . HOH   K 5 .   ? 22.505 -22.526 20.588 1.00 24.11 ? 415 HOH   C O   1 
HETATM 2466 O  O   . HOH   K 5 .   ? 16.466 -20.385 0.173  1.00 41.68 ? 416 HOH   C O   1 
HETATM 2467 O  O   . HOH   K 5 .   ? 31.429 -21.884 4.552  1.00 47.52 ? 417 HOH   C O   1 
HETATM 2468 O  O   . HOH   K 5 .   ? 12.824 -42.247 3.446  1.00 57.78 ? 418 HOH   C O   1 
HETATM 2469 O  O   . HOH   K 5 .   ? 12.174 -39.181 12.766 1.00 37.82 ? 419 HOH   C O   1 
HETATM 2470 O  O   . HOH   K 5 .   ? 17.813 -12.851 3.021  1.00 56.80 ? 420 HOH   C O   1 
HETATM 2471 O  O   . HOH   K 5 .   ? 16.103 -17.475 25.948 1.00 50.79 ? 421 HOH   C O   1 
HETATM 2472 O  O   . HOH   K 5 .   ? 17.622 -38.768 24.511 1.00 53.81 ? 422 HOH   C O   1 
HETATM 2473 O  O   . HOH   K 5 .   ? 26.734 -21.697 21.527 1.00 47.95 ? 423 HOH   C O   1 
HETATM 2474 O  O   . HOH   K 5 .   ? 6.908  -36.456 2.811  1.00 28.34 ? 424 HOH   C O   1 
HETATM 2475 O  O   . HOH   K 5 .   ? 31.109 -16.222 4.251  1.00 74.97 ? 425 HOH   C O   1 
HETATM 2476 O  O   . HOH   K 5 .   ? 20.641 -9.109  17.900 1.00 39.34 ? 426 HOH   C O   1 
HETATM 2477 O  O   . HOH   K 5 .   ? 2.657  -29.534 26.890 1.00 39.97 ? 427 HOH   C O   1 
HETATM 2478 O  O   . HOH   K 5 .   ? 24.428 -15.978 23.302 1.00 59.17 ? 428 HOH   C O   1 
HETATM 2479 O  O   . HOH   K 5 .   ? 4.805  -28.694 4.713  1.00 41.56 ? 429 HOH   C O   1 
HETATM 2480 O  O   . HOH   K 5 .   ? 31.306 -11.738 8.546  1.00 59.54 ? 430 HOH   C O   1 
HETATM 2481 O  O   . HOH   K 5 .   ? -0.249 -34.542 10.044 1.00 57.24 ? 431 HOH   C O   1 
HETATM 2482 O  O   . HOH   K 5 .   ? 29.182 -22.156 20.927 1.00 39.68 ? 432 HOH   C O   1 
HETATM 2483 O  O   . HOH   K 5 .   ? 33.071 -8.741  19.802 1.00 61.61 ? 433 HOH   C O   1 
HETATM 2484 O  O   . HOH   K 5 .   ? 18.269 -20.089 25.810 1.00 31.78 ? 434 HOH   C O   1 
HETATM 2485 O  O   . HOH   K 5 .   ? 31.930 -22.850 15.063 1.00 38.07 ? 435 HOH   C O   1 
HETATM 2486 O  O   . HOH   K 5 .   ? 30.576 -31.295 13.328 1.00 46.06 ? 436 HOH   C O   1 
HETATM 2487 O  O   . HOH   K 5 .   ? 8.601  -23.752 2.579  1.00 37.29 ? 437 HOH   C O   1 
HETATM 2488 O  O   . HOH   K 5 .   ? -2.395 -33.021 9.263  1.00 31.36 ? 438 HOH   C O   1 
HETATM 2489 O  O   . HOH   K 5 .   ? 25.875 -9.974  19.329 1.00 44.15 ? 439 HOH   C O   1 
HETATM 2490 O  O   . HOH   K 5 .   ? 33.055 -9.287  11.785 1.00 37.43 ? 440 HOH   C O   1 
HETATM 2491 O  O   . HOH   K 5 .   ? 25.695 -33.081 16.011 1.00 48.95 ? 441 HOH   C O   1 
HETATM 2492 O  O   . HOH   K 5 .   ? 32.091 -27.253 13.612 1.00 39.65 ? 442 HOH   C O   1 
HETATM 2493 O  O   . HOH   K 5 .   ? 5.830  -27.576 2.756  1.00 32.63 ? 443 HOH   C O   1 
HETATM 2494 O  O   . HOH   K 5 .   ? 31.772 -35.967 12.119 1.00 38.93 ? 444 HOH   C O   1 
HETATM 2495 O  O   . HOH   K 5 .   ? 16.224 -17.338 1.559  1.00 52.24 ? 445 HOH   C O   1 
HETATM 2496 O  O   . HOH   K 5 .   ? 26.403 -18.666 24.145 1.00 58.73 ? 446 HOH   C O   1 
HETATM 2497 O  O   . HOH   K 5 .   ? 15.391 -39.851 2.050  1.00 48.87 ? 447 HOH   C O   1 
HETATM 2498 O  O   . HOH   K 5 .   ? 5.439  -39.493 23.304 1.00 32.49 ? 448 HOH   C O   1 
HETATM 2499 O  O   . HOH   K 5 .   ? 20.857 -19.556 -3.011 1.00 38.15 ? 449 HOH   C O   1 
HETATM 2500 O  O   . HOH   K 5 .   ? 35.737 -10.204 8.179  1.00 67.33 ? 450 HOH   C O   1 
HETATM 2501 O  O   . HOH   K 5 .   ? 29.832 -8.578  8.450  1.00 49.00 ? 451 HOH   C O   1 
HETATM 2502 O  O   . HOH   K 5 .   ? 8.752  -12.033 29.473 1.00 62.11 ? 452 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   ? 0.2592 0.2631 0.2541 0.0032  -0.0141 0.0026  7   SER   A N   
2    C CA  . SER   A 1   ? 0.2648 0.2707 0.2712 0.0017  -0.0163 0.0009  7   SER   A CA  
3    C C   . SER   A 1   ? 0.2630 0.2697 0.2773 -0.0013 -0.0147 -0.0023 7   SER   A C   
4    O O   . SER   A 1   ? 0.2746 0.2801 0.2850 -0.0015 -0.0140 -0.0043 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2850 0.2926 0.2918 0.0049  -0.0232 -0.0013 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3224 0.3305 0.3268 0.0057  -0.0272 -0.0061 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2385 0.2464 0.2634 -0.0031 -0.0135 -0.0026 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2297 0.2368 0.2616 -0.0055 -0.0106 -0.0045 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2401 0.2470 0.2786 -0.0066 -0.0060 -0.0025 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2475 0.2543 0.2831 -0.0059 -0.0046 0.0002  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2195 0.2258 0.2669 -0.0082 -0.0033 -0.0038 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2267 0.2323 0.2789 -0.0084 0.0018  -0.0017 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2243 0.2259 0.2789 -0.0093 0.0075  -0.0017 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2052 0.2052 0.2617 -0.0105 0.0069  -0.0038 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2271 0.2368 0.2910 -0.0086 -0.0001 -0.0024 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2153 0.2145 0.2690 -0.0081 0.0132  0.0007  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2074 0.2014 0.2622 -0.0078 0.0199  0.0019  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2090 0.2044 0.2768 -0.0089 0.0238  0.0024  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2104 0.2087 0.2797 -0.0077 0.0235  0.0032  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1995 0.1893 0.2417 -0.0042 0.0236  0.0042  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2015 0.1917 0.2331 -0.0031 0.0196  0.0033  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2049 0.1878 0.2455 -0.0025 0.0314  0.0064  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2259 0.2150 0.2476 0.0006  0.0207  0.0041  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2046 0.1980 0.2828 -0.0111 0.0280  0.0018  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2142 0.2097 0.3076 -0.0124 0.0331  0.0022  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2227 0.2103 0.3138 -0.0110 0.0438  0.0059  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2488 0.2312 0.3422 -0.0126 0.0472  0.0059  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2092 0.2097 0.3206 -0.0165 0.0293  -0.0022 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2251 0.2332 0.3373 -0.0164 0.0187  -0.0056 11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2438 0.2583 0.3637 -0.0153 0.0163  -0.0059 11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2498 0.2577 0.3530 -0.0163 0.0116  -0.0079 11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2602 0.2800 0.3784 -0.0139 0.0069  -0.0080 11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2656 0.2788 0.3664 -0.0149 0.0028  -0.0100 11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2866 0.3056 0.3949 -0.0137 0.0004  -0.0100 11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3360 0.3589 0.4400 -0.0113 -0.0078 -0.0112 11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2249 0.2104 0.3103 -0.0074 0.0495  0.0092  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2450 0.2217 0.3246 -0.0045 0.0605  0.0135  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2651 0.2432 0.3534 -0.0034 0.0677  0.0154  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2697 0.2526 0.3565 -0.0015 0.0644  0.0146  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2695 0.2401 0.3263 0.0012  0.0602  0.0156  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2684 0.2443 0.3176 0.0034  0.0533  0.0138  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2913 0.2523 0.3391 0.0063  0.0714  0.0204  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2674 0.2419 0.3676 -0.0049 0.0778  0.0177  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2644 0.2409 0.3755 -0.0041 0.0861  0.0195  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2649 0.2536 0.3922 -0.0069 0.0783  0.0152  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2663 0.2614 0.4060 -0.0115 0.0704  0.0108  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2644 0.2558 0.3887 -0.0032 0.0792  0.0159  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2735 0.2755 0.4110 -0.0046 0.0717  0.0122  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2550 0.2582 0.3775 -0.0023 0.0612  0.0107  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2542 0.2622 0.3798 -0.0005 0.0578  0.0096  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3155 0.3206 0.4645 -0.0024 0.0798  0.0136  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3818 0.3889 0.5532 -0.0062 0.0891  0.0140  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3950 0.4092 0.5855 -0.0115 0.0840  0.0100  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3938 0.3944 0.5630 -0.0033 0.1029  0.0187  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2361 0.2351 0.3438 -0.0024 0.0563  0.0105  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2255 0.2251 0.3200 -0.0008 0.0476  0.0092  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2089 0.2112 0.3033 -0.0042 0.0390  0.0068  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2026 0.2029 0.2994 -0.0066 0.0401  0.0064  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2366 0.2286 0.3109 0.0034  0.0505  0.0111  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2453 0.2335 0.3147 0.0083  0.0581  0.0130  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2523 0.2441 0.3262 0.0099  0.0569  0.0119  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2725 0.2528 0.3311 0.0122  0.0666  0.0160  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2748 0.2628 0.3431 0.0149  0.0639  0.0131  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2905 0.2668 0.3422 0.0178  0.0737  0.0176  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2985 0.2789 0.3556 0.0190  0.0724  0.0159  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3203 0.2965 0.3698 0.0250  0.0794  0.0170  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1977 0.2035 0.2884 -0.0038 0.0308  0.0054  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1973 0.2047 0.2840 -0.0057 0.0230  0.0036  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2006 0.2048 0.2717 -0.0036 0.0208  0.0046  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2092 0.2137 0.2787 -0.0017 0.0204  0.0051  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2133 0.2277 0.3109 -0.0065 0.0160  0.0014  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2148 0.2299 0.3037 -0.0063 0.0080  0.0005  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2377 0.2590 0.3360 -0.0060 0.0008  -0.0020 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2756 0.2964 0.3640 -0.0035 -0.0048 -0.0007 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3061 0.3269 0.3873 -0.0030 -0.0105 -0.0017 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2765 0.2981 0.3591 -0.0049 -0.0122 -0.0047 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2973 0.3165 0.3692 -0.0003 -0.0139 0.0004  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1788 0.1803 0.2400 -0.0039 0.0196  0.0045  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1846 0.1845 0.2342 -0.0024 0.0176  0.0046  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1897 0.1919 0.2371 -0.0041 0.0115  0.0039  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2001 0.2027 0.2472 -0.0053 0.0100  0.0030  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1829 0.1783 0.2225 -0.0005 0.0210  0.0050  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1742 0.1694 0.2047 0.0011  0.0185  0.0039  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1820 0.1735 0.2219 0.0019  0.0282  0.0065  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1836 0.1867 0.2291 -0.0037 0.0087  0.0044  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1923 0.1966 0.2343 -0.0044 0.0044  0.0046  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1896 0.1923 0.2254 -0.0043 0.0046  0.0052  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1884 0.1895 0.2242 -0.0035 0.0067  0.0047  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2039 0.2104 0.2514 -0.0038 0.0006  0.0052  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2150 0.2246 0.2706 -0.0043 -0.0012 0.0033  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2119 0.2174 0.2631 -0.0024 0.0018  0.0063  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1753 0.1782 0.2066 -0.0049 0.0026  0.0061  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1819 0.1835 0.2108 -0.0054 0.0036  0.0068  19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1932 0.1926 0.2258 -0.0048 0.0034  0.0084  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1904 0.1899 0.2246 -0.0034 0.0012  0.0099  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1846 0.1864 0.2085 -0.0058 0.0029  0.0083  19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.2008 0.2046 0.2209 -0.0060 0.0032  0.0066  19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.2090 0.2134 0.2273 -0.0054 0.0014  0.0060  19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2039 0.2089 0.2236 -0.0067 0.0050  0.0053  19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1900 0.1873 0.2243 -0.0051 0.0052  0.0075  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1888 0.1829 0.2267 -0.0042 0.0054  0.0087  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1900 0.1814 0.2259 -0.0038 0.0046  0.0126  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.2036 0.1934 0.2412 -0.0016 0.0032  0.0145  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1974 0.1891 0.2374 -0.0049 0.0071  0.0061  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2064 0.1939 0.2503 -0.0035 0.0076  0.0065  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2238 0.2085 0.2698 -0.0047 0.0087  0.0030  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2433 0.2229 0.2928 -0.0032 0.0093  0.0023  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2477 0.2217 0.2999 -0.0038 0.0103  0.0047  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2354 0.2082 0.2865 -0.0055 0.0111  0.0088  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2440 0.2129 0.2996 -0.0023 0.0109  0.0033  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1752 0.1662 0.2071 -0.0052 0.0057  0.0139  21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1943 0.1813 0.2219 -0.0040 0.0063  0.0184  21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.2216 0.2100 0.2441 -0.0007 0.0025  0.0200  21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2451 0.2295 0.2623 0.0021  0.0021  0.0239  21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.2050 0.1909 0.2302 -0.0062 0.0100  0.0197  21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2225 0.2130 0.2429 -0.0064 0.0094  0.0186  21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2242 0.2195 0.2471 -0.0080 0.0089  0.0144  21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2376 0.2276 0.2498 -0.0044 0.0094  0.0212  21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2269 0.2246 0.2443 -0.0074 0.0087  0.0146  21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2435 0.2381 0.2542 -0.0052 0.0088  0.0183  21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.2095 0.2031 0.2336 -0.0007 -0.0005 0.0169  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.2151 0.2111 0.2372 0.0021  -0.0052 0.0167  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.2202 0.2192 0.2510 0.0033  -0.0078 0.0148  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2201 0.2224 0.2524 0.0053  -0.0125 0.0133  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.2231 0.2224 0.2419 0.0011  -0.0064 0.0140  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2303 0.2278 0.2410 0.0004  -0.0035 0.0155  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2416 0.2421 0.2493 0.0000  -0.0049 0.0124  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2508 0.2441 0.2527 0.0037  -0.0034 0.0198  22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.2112 0.2093 0.2486 0.0023  -0.0050 0.0143  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.2079 0.2091 0.2545 0.0037  -0.0063 0.0127  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.2241 0.2257 0.2719 0.0078  -0.0108 0.0142  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2239 0.2204 0.2651 0.0100  -0.0109 0.0177  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.2101 0.2091 0.2608 0.0030  -0.0022 0.0122  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.2371 0.2446 0.2936 0.0092  -0.0143 0.0117  24  THR   A N   
135  C CA  . THR   A 18  ? 0.2602 0.2697 0.3189 0.0141  -0.0200 0.0122  24  THR   A CA  
136  C C   . THR   A 18  ? 0.2729 0.2818 0.3393 0.0165  -0.0185 0.0132  24  THR   A C   
137  O O   . THR   A 18  ? 0.2591 0.2664 0.3293 0.0142  -0.0131 0.0129  24  THR   A O   
138  C CB  . THR   A 18  ? 0.2839 0.3017 0.3515 0.0142  -0.0254 0.0075  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2916 0.3141 0.3736 0.0114  -0.0219 0.0048  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.3013 0.3193 0.3615 0.0124  -0.0272 0.0057  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2895 0.3000 0.3582 0.0220  -0.0237 0.0139  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.3079 0.3188 0.3855 0.0251  -0.0228 0.0143  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2685 0.2870 0.3617 0.0222  -0.0200 0.0102  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2730 0.2899 0.3712 0.0221  -0.0149 0.0105  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.3580 0.3713 0.4365 0.0324  -0.0303 0.0150  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4698 0.4738 0.5321 0.0368  -0.0317 0.0203  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.5228 0.5162 0.5781 0.0366  -0.0258 0.0249  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.5082 0.5116 0.5601 0.0420  -0.0381 0.0215  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.5440 0.5302 0.5856 0.0411  -0.0275 0.0296  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.5439 0.5356 0.5817 0.0450  -0.0349 0.0280  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2492 0.2752 0.3497 0.0199  -0.0226 0.0064  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2442 0.2767 0.3602 0.0169  -0.0188 0.0031  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.2289 0.2565 0.3407 0.0127  -0.0102 0.0041  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.2344 0.2632 0.3544 0.0125  -0.0045 0.0037  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2668 0.3074 0.3929 0.0151  -0.0234 -0.0015 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3427 0.3922 0.4823 0.0195  -0.0307 -0.0047 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3650 0.4181 0.5160 0.0221  -0.0291 -0.0047 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3530 0.4062 0.4911 0.0213  -0.0394 -0.0078 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.2109 0.2328 0.3092 0.0102  -0.0092 0.0055  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.2075 0.2247 0.3002 0.0074  -0.0023 0.0061  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2055 0.2179 0.2963 0.0096  0.0014  0.0076  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2116 0.2231 0.3044 0.0093  0.0071  0.0068  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.2059 0.2186 0.2852 0.0052  -0.0029 0.0072  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2504 0.2662 0.3302 0.0029  -0.0049 0.0053  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2469 0.2657 0.3353 0.0012  -0.0022 0.0034  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2560 0.2704 0.3270 0.0028  -0.0086 0.0058  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.2012 0.2098 0.2873 0.0121  -0.0015 0.0096  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.2166 0.2195 0.3013 0.0141  0.0017  0.0104  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2444 0.2511 0.3406 0.0173  0.0035  0.0093  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2587 0.2617 0.3548 0.0186  0.0081  0.0086  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.2200 0.2163 0.2974 0.0160  -0.0011 0.0134  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.2296 0.2204 0.2969 0.0126  0.0003  0.0143  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2467 0.2371 0.3071 0.0112  -0.0019 0.0160  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.2262 0.2119 0.2903 0.0106  0.0042  0.0128  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2481 0.2340 0.3026 0.0080  0.0010  0.0160  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2367 0.2200 0.2939 0.0075  0.0042  0.0137  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2344 0.2174 0.3007 0.0115  0.0075  0.0103  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2435 0.2230 0.2983 0.0049  0.0067  0.0116  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2415 0.2197 0.3034 0.0094  0.0094  0.0080  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2361 0.2133 0.2934 0.0059  0.0087  0.0084  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2498 0.2639 0.3565 0.0191  -0.0002 0.0086  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2526 0.2723 0.3733 0.0221  0.0017  0.0072  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2586 0.2816 0.3866 0.0197  0.0090  0.0054  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2668 0.2931 0.4054 0.0221  0.0134  0.0046  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2484 0.2764 0.3798 0.0247  -0.0052 0.0061  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2372 0.2597 0.3604 0.0155  0.0107  0.0050  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2331 0.2567 0.3605 0.0136  0.0183  0.0043  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2374 0.2528 0.3486 0.0125  0.0222  0.0052  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2367 0.2513 0.3455 0.0104  0.0263  0.0053  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2354 0.2656 0.3733 0.0101  0.0169  0.0028  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2738 0.3137 0.4308 0.0115  0.0132  0.0005  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2826 0.3270 0.4535 0.0126  0.0188  -0.0001 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2834 0.3271 0.4414 0.0120  0.0038  -0.0009 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2282 0.2374 0.3289 0.0141  0.0205  0.0056  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2361 0.2387 0.3228 0.0133  0.0222  0.0052  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2397 0.2397 0.3225 0.0153  0.0296  0.0044  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2549 0.2547 0.3422 0.0187  0.0339  0.0041  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2404 0.2373 0.3210 0.0147  0.0194  0.0049  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2604 0.2514 0.3292 0.0139  0.0199  0.0031  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2536 0.2459 0.3173 0.0102  0.0171  0.0037  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2749 0.2601 0.3416 0.0151  0.0181  0.0021  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2264 0.2240 0.3000 0.0141  0.0312  0.0043  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2411 0.2345 0.3064 0.0172  0.0377  0.0039  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2598 0.2478 0.3114 0.0187  0.0348  0.0013  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2720 0.2558 0.3169 0.0230  0.0373  -0.0008 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2523 0.2462 0.3173 0.0157  0.0419  0.0058  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2624 0.2501 0.3143 0.0202  0.0482  0.0060  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2564 0.2557 0.3379 0.0141  0.0457  0.0073  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2541 0.2427 0.3024 0.0154  0.0293  0.0008  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2566 0.2418 0.2951 0.0160  0.0261  -0.0023 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2404 0.2275 0.2806 0.0116  0.0207  -0.0020 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2337 0.2240 0.2769 0.0089  0.0197  0.0003  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2575 0.2406 0.2851 0.0189  0.0288  -0.0032 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2601 0.2417 0.2788 0.0197  0.0244  -0.0071 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2752 0.2537 0.2875 0.0233  0.0228  -0.0119 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2551 0.2392 0.2716 0.0170  0.0209  -0.0073 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2798 0.2595 0.2878 0.0227  0.0179  -0.0154 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2634 0.2466 0.2737 0.0191  0.0172  -0.0123 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2565 0.2435 0.2757 0.0137  0.0207  -0.0042 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2626 0.2486 0.2704 0.0178  0.0136  -0.0140 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2629 0.2517 0.2784 0.0125  0.0173  -0.0056 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2615 0.2501 0.2719 0.0145  0.0140  -0.0103 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2303 0.2150 0.2688 0.0109  0.0175  -0.0047 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2258 0.2119 0.2655 0.0068  0.0138  -0.0042 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2130 0.1974 0.2494 0.0066  0.0116  -0.0088 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2211 0.2022 0.2559 0.0092  0.0117  -0.0126 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2459 0.2315 0.2921 0.0049  0.0124  -0.0010 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2686 0.2497 0.3183 0.0068  0.0129  -0.0019 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2899 0.2662 0.3394 0.0056  0.0118  -0.0052 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.3180 0.2902 0.3684 0.0080  0.0126  -0.0081 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2687 0.2455 0.3181 0.0023  0.0103  -0.0053 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1942 0.1810 0.2303 0.0036  0.0095  -0.0091 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2029 0.1897 0.2393 0.0028  0.0071  -0.0142 35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.2124 0.2012 0.2540 -0.0019 0.0063  -0.0123 35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2121 0.2046 0.2514 -0.0028 0.0062  -0.0106 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2224 0.2114 0.2510 0.0064  0.0060  -0.0178 35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.3247 0.3149 0.3543 0.0068  0.0022  -0.0248 35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3316 0.3226 0.3701 0.0024  0.0009  -0.0263 35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3303 0.3207 0.3522 0.0118  0.0006  -0.0290 35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2142 0.1994 0.2623 -0.0045 0.0067  -0.0123 36  SER   A N   
241  C CA  A SER   A 30  ? 0.2262 0.2117 0.2791 -0.0086 0.0076  -0.0098 36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2249 0.2105 0.2776 -0.0086 0.0076  -0.0097 36  SER   A CA  
243  C C   . SER   A 30  ? 0.2296 0.2205 0.2847 -0.0104 0.0063  -0.0139 36  SER   A C   
244  O O   . SER   A 30  ? 0.2369 0.2307 0.2926 -0.0126 0.0075  -0.0111 36  SER   A O   
245  C CB  A SER   A 30  ? 0.2472 0.2261 0.3069 -0.0106 0.0093  -0.0093 36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2429 0.2219 0.3023 -0.0106 0.0094  -0.0089 36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2731 0.2512 0.3378 -0.0145 0.0116  -0.0069 36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2631 0.2406 0.3280 -0.0112 0.0080  -0.0158 36  SER   A OG  
249  N N   . SER   A 31  ? 0.2270 0.2196 0.2827 -0.0086 0.0034  -0.0210 37  SER   A N   
250  C CA  . SER   A 31  ? 0.2432 0.2421 0.3020 -0.0094 0.0011  -0.0259 37  SER   A CA  
251  C C   . SER   A 31  ? 0.2331 0.2369 0.2839 -0.0071 0.0007  -0.0235 37  SER   A C   
252  O O   . SER   A 31  ? 0.2487 0.2582 0.3026 -0.0081 -0.0004 -0.0256 37  SER   A O   
253  C CB  . SER   A 31  ? 0.2694 0.2692 0.3298 -0.0068 -0.0032 -0.0348 37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3236 0.3241 0.3721 -0.0006 -0.0052 -0.0363 37  SER   A OG  
255  N N   . ARG   A 32  ? 0.2133 0.2150 0.2554 -0.0042 0.0019  -0.0194 38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.2036 0.2083 0.2387 -0.0023 0.0021  -0.0172 38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.2007 0.2049 0.2354 -0.0048 0.0045  -0.0109 38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1965 0.2025 0.2265 -0.0038 0.0047  -0.0092 38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.2176 0.2198 0.2435 0.0029  0.0024  -0.0173 38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2371 0.2395 0.2591 0.0074  -0.0005 -0.0236 38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2542 0.2526 0.2651 0.0133  0.0014  -0.0226 38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2675 0.2661 0.2717 0.0153  0.0034  -0.0190 38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2745 0.2700 0.2677 0.0215  0.0049  -0.0188 38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2605 0.2529 0.2466 0.0269  0.0043  -0.0222 38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2437 0.2383 0.2319 0.0228  0.0071  -0.0153 38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2074 0.2083 0.2461 -0.0072 0.0059  -0.0077 39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1979 0.1976 0.2349 -0.0081 0.0071  -0.0023 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1905 0.1900 0.2233 -0.0057 0.0069  -0.0008 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1854 0.1862 0.2159 -0.0060 0.0067  0.0015  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1916 0.1941 0.2280 -0.0099 0.0079  -0.0006 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2179 0.2188 0.2505 -0.0098 0.0083  0.0043  39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.2022 0.1994 0.2356 -0.0095 0.0085  0.0070  39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.2192 0.2225 0.2474 -0.0094 0.0080  0.0049  39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1877 0.1855 0.2200 -0.0034 0.0073  -0.0024 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1861 0.1836 0.2168 -0.0015 0.0086  -0.0008 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1991 0.1945 0.2340 -0.0005 0.0096  0.0004  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1895 0.1824 0.2257 0.0004  0.0098  -0.0013 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1887 0.1857 0.2137 0.0016  0.0100  -0.0029 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.2006 0.1995 0.2208 0.0022  0.0094  -0.0036 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.2081 0.2048 0.2210 0.0068  0.0111  -0.0050 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.2003 0.2002 0.2215 0.0002  0.0096  -0.0008 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1980 0.1946 0.2358 -0.0004 0.0103  0.0026  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1958 0.1919 0.2392 0.0011  0.0115  0.0034  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.2011 0.1990 0.2475 0.0016  0.0142  0.0040  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.2082 0.2078 0.2545 0.0000  0.0132  0.0045  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1949 0.1915 0.2429 0.0004  0.0087  0.0055  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2061 0.2030 0.2612 0.0026  0.0094  0.0062  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2208 0.2148 0.2769 0.0034  0.0073  0.0077  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1981 0.1998 0.2601 0.0025  0.0083  0.0068  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.2006 0.1975 0.2498 0.0039  0.0181  0.0039  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1924 0.1904 0.2468 0.0042  0.0223  0.0049  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1949 0.1957 0.2605 0.0049  0.0232  0.0054  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1993 0.1985 0.2647 0.0073  0.0241  0.0049  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2149 0.2087 0.2616 0.0073  0.0282  0.0049  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2151 0.2091 0.2689 0.0074  0.0345  0.0068  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2123 0.2040 0.2482 0.0075  0.0265  0.0041  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1976 0.2029 0.2739 0.0031  0.0226  0.0056  43  SER   A N   
298  C CA  . SER   A 37  ? 0.2057 0.2156 0.2957 0.0039  0.0230  0.0054  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2413 0.2534 0.3422 0.0029  0.0293  0.0055  43  SER   A C   
300  O O   . SER   A 37  ? 0.2363 0.2462 0.3344 0.0010  0.0320  0.0059  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2193 0.2337 0.3148 0.0030  0.0152  0.0048  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2333 0.2503 0.3306 0.0003  0.0120  0.0036  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2476 0.2638 0.3618 0.0042  0.0325  0.0054  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2547 0.2733 0.3821 0.0029  0.0399  0.0056  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2637 0.2901 0.4082 -0.0007 0.0350  0.0029  44  SER   A C   
306  O O   . SER   A 38  ? 0.2596 0.2913 0.4084 -0.0003 0.0264  0.0009  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2602 0.2799 0.3949 0.0063  0.0469  0.0064  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2725 0.2977 0.4149 0.0079  0.0408  0.0049  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2663 0.2928 0.4203 -0.0038 0.0406  0.0027  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2800 0.3139 0.4526 -0.0076 0.0363  -0.0011 45  THR   A CA  
311  C C   . THR   A 39  ? 0.3058 0.3440 0.5003 -0.0092 0.0454  -0.0014 45  THR   A C   
312  O O   . THR   A 39  ? 0.3166 0.3491 0.5075 -0.0077 0.0567  0.0024  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2881 0.3177 0.4544 -0.0110 0.0345  -0.0020 45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3092 0.3314 0.4730 -0.0119 0.0457  0.0012  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2808 0.3059 0.4256 -0.0096 0.0275  -0.0012 45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3202 0.3681 0.5372 -0.0120 0.0410  -0.0061 46  THR   A N   
317  C CA  . THR   A 40  ? 0.3383 0.3914 0.5805 -0.0145 0.0499  -0.0071 46  THR   A CA  
318  C C   . THR   A 40  ? 0.3622 0.4106 0.6112 -0.0200 0.0555  -0.0077 46  THR   A C   
319  O O   . THR   A 40  ? 0.3766 0.4229 0.6380 -0.0219 0.0681  -0.0054 46  THR   A O   
320  C CB  . THR   A 40  ? 0.3491 0.4163 0.6151 -0.0145 0.0418  -0.0129 46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3727 0.4436 0.6385 -0.0160 0.0285  -0.0180 46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3519 0.4224 0.6128 -0.0086 0.0386  -0.0116 46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3619 0.4080 0.6026 -0.0221 0.0469  -0.0104 47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3645 0.4052 0.6107 -0.0270 0.0512  -0.0114 47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3773 0.4039 0.5984 -0.0253 0.0586  -0.0051 47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3872 0.4098 0.5852 -0.0211 0.0548  -0.0025 47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3615 0.4070 0.6120 -0.0295 0.0379  -0.0184 47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3695 0.3886 0.5961 -0.0282 0.0690  -0.0031 48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3896 0.3949 0.5938 -0.0259 0.0765  0.0028  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3853 0.3871 0.5740 -0.0262 0.0667  0.0005  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3795 0.3846 0.5805 -0.0305 0.0604  -0.0051 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4299 0.4275 0.6466 -0.0289 0.0909  0.0057  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5277 0.5102 0.7209 -0.0252 0.0996  0.0125  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6378 0.6152 0.8138 -0.0183 0.1082  0.0190  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6505 0.6347 0.8341 -0.0168 0.1102  0.0191  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6740 0.6390 0.8259 -0.0134 0.1132  0.0242  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3801 0.3757 0.5430 -0.0216 0.0653  0.0041  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3776 0.3706 0.5248 -0.0211 0.0566  0.0024  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3784 0.3625 0.5230 -0.0229 0.0600  0.0026  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3932 0.3690 0.5400 -0.0229 0.0715  0.0065  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3505 0.3351 0.4880 -0.0237 0.0507  -0.0012 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.3395 0.3161 0.4745 -0.0252 0.0520  -0.0021 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3381 0.3049 0.4494 -0.0203 0.0555  0.0028  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3544 0.3118 0.4636 -0.0206 0.0605  0.0039  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3498 0.3323 0.4898 -0.0279 0.0401  -0.0094 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.3787 0.3668 0.4986 -0.0238 0.0284  -0.0102 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3227 0.2912 0.4174 -0.0157 0.0531  0.0054  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3132 0.2750 0.3863 -0.0105 0.0540  0.0086  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3153 0.2692 0.3776 -0.0052 0.0639  0.0146  51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3211 0.2759 0.3903 -0.0052 0.0698  0.0167  51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3127 0.2819 0.3751 -0.0085 0.0444  0.0068  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3574 0.3325 0.4239 -0.0116 0.0349  0.0018  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3568 0.3278 0.4218 -0.0124 0.0339  -0.0001 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.3302 0.3132 0.4001 -0.0125 0.0287  -0.0002 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.3113 0.2578 0.3556 0.0000  0.0653  0.0172  52  THR   A N   
356  C CA  . THR   A 46  ? 0.3313 0.2700 0.3601 0.0071  0.0726  0.0224  52  THR   A CA  
357  C C   . THR   A 46  ? 0.3242 0.2655 0.3347 0.0125  0.0648  0.0210  52  THR   A C   
358  O O   . THR   A 46  ? 0.3263 0.2708 0.3355 0.0110  0.0578  0.0179  52  THR   A O   
359  C CB  . THR   A 46  ? 0.3810 0.3063 0.4079 0.0090  0.0838  0.0272  52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4108 0.3314 0.4299 0.0103  0.0805  0.0262  52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3833 0.3073 0.4327 0.0022  0.0909  0.0272  52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.3055 0.2462 0.3035 0.0185  0.0659  0.0227  53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2906 0.2360 0.2759 0.0227  0.0579  0.0201  53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2898 0.2272 0.2573 0.0309  0.0598  0.0222  53  ILE   A C   
365  O O   . ILE   A 47  ? 0.3070 0.2348 0.2659 0.0363  0.0684  0.0268  53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2963 0.2466 0.2799 0.0245  0.0563  0.0189  53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3095 0.2668 0.3103 0.0177  0.0553  0.0174  53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2968 0.2531 0.2717 0.0273  0.0475  0.0149  53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3161 0.2816 0.3265 0.0114  0.0464  0.0136  53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2752 0.2165 0.2368 0.0325  0.0524  0.0192  54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2802 0.2156 0.2250 0.0413  0.0525  0.0205  54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2901 0.2261 0.2223 0.0487  0.0513  0.0198  54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2902 0.2346 0.2271 0.0463  0.0461  0.0160  54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2708 0.2123 0.2151 0.0410  0.0445  0.0166  54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.2974 0.2237 0.2126 0.0584  0.0558  0.0232  55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.3044 0.2304 0.2042 0.0676  0.0536  0.0218  55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.3326 0.2556 0.2174 0.0767  0.0497  0.0212  55  ARG   A C   
378  O O   . ARG   A 49  ? 0.3478 0.2587 0.2185 0.0846  0.0564  0.0265  55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.3218 0.2372 0.2131 0.0723  0.0645  0.0274  55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.3371 0.2556 0.2451 0.0636  0.0693  0.0282  55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.3559 0.2867 0.2729 0.0590  0.0607  0.0219  55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.3670 0.2999 0.2997 0.0518  0.0657  0.0233  55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.3663 0.3087 0.3115 0.0456  0.0601  0.0193  55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.3409 0.2912 0.2858 0.0449  0.0500  0.0138  55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.3541 0.2982 0.3132 0.0402  0.0648  0.0208  55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.3336 0.2676 0.2231 0.0753  0.0394  0.0150  56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.3423 0.2759 0.2222 0.0827  0.0348  0.0137  56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.3428 0.2911 0.2287 0.0820  0.0231  0.0055  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.3308 0.2879 0.2285 0.0750  0.0195  0.0015  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.3486 0.2782 0.2357 0.0778  0.0384  0.0168  56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.3384 0.2809 0.2483 0.0641  0.0332  0.0123  56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.3575 0.3083 0.2372 0.0887  0.0176  0.0029  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.3669 0.3324 0.2558 0.0874  0.0073  -0.0050 57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.3625 0.3325 0.2608 0.0834  0.0060  -0.0054 57  ASP   A C   
395  O O   . ASP   A 51  ? 0.3714 0.3507 0.2725 0.0867  -0.0010 -0.0106 57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.4113 0.3799 0.2874 0.0996  -0.0001 -0.0101 57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.5303 0.4903 0.3892 0.1117  0.0008  -0.0069 57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.5171 0.4665 0.3729 0.1107  0.0088  0.0002  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.6338 0.5977 0.4827 0.1224  -0.0067 -0.0117 57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.3508 0.3147 0.2547 0.0766  0.0127  -0.0005 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.3380 0.3050 0.2497 0.0729  0.0119  -0.0011 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.3160 0.2982 0.2421 0.0668  0.0053  -0.0072 58  CYS   A C   
403  O O   . CYS   A 52  ? 0.3125 0.2999 0.2466 0.0607  0.0040  -0.0090 58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.3391 0.2975 0.2559 0.0656  0.0192  0.0038  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.3722 0.3117 0.2755 0.0723  0.0285  0.0111  58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2895 0.2782 0.2192 0.0685  0.0017  -0.0101 59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2766 0.2789 0.2209 0.0625  -0.0026 -0.0150 59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2707 0.2730 0.2204 0.0582  0.0000  -0.0137 59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2665 0.2792 0.2258 0.0558  -0.0025 -0.0172 59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2952 0.3088 0.2418 0.0688  -0.0099 -0.0214 59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3588 0.3772 0.3067 0.0696  -0.0144 -0.0256 59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.4194 0.4511 0.3742 0.0744  -0.0225 -0.0334 59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4345 0.4661 0.3793 0.0847  -0.0273 -0.0363 59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3892 0.4327 0.3614 0.0676  -0.0239 -0.0372 59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2683 0.2586 0.2119 0.0578  0.0055  -0.0089 60  THR   A N   
416  C CA  . THR   A 54  ? 0.2685 0.2569 0.2163 0.0536  0.0079  -0.0081 60  THR   A CA  
417  C C   . THR   A 54  ? 0.2668 0.2455 0.2153 0.0474  0.0128  -0.0043 60  THR   A C   
418  O O   . THR   A 54  ? 0.2778 0.2481 0.2208 0.0491  0.0162  -0.0011 60  THR   A O   
419  C CB  . THR   A 54  ? 0.2976 0.2806 0.2379 0.0610  0.0087  -0.0077 60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3294 0.2983 0.2588 0.0657  0.0130  -0.0031 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2962 0.2892 0.2363 0.0684  0.0034  -0.0117 60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2425 0.2224 0.1976 0.0411  0.0134  -0.0050 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2431 0.2161 0.2016 0.0351  0.0167  -0.0029 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.2311 0.2071 0.1953 0.0299  0.0155  -0.0050 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.2321 0.2133 0.1960 0.0317  0.0136  -0.0073 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.2318 0.2048 0.2012 0.0241  0.0164  -0.0046 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.2388 0.2138 0.2120 0.0200  0.0145  -0.0070 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.2275 0.2074 0.2070 0.0146  0.0128  -0.0068 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.2319 0.2090 0.2149 0.0127  0.0144  -0.0050 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2677 0.2323 0.2409 0.0194  0.0166  -0.0077 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2734 0.2395 0.2496 0.0159  0.0137  -0.0113 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2767 0.2351 0.2429 0.0255  0.0188  -0.0074 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.2178 0.2043 0.1985 0.0126  0.0101  -0.0083 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.2049 0.1949 0.1904 0.0084  0.0083  -0.0078 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2128 0.2023 0.1983 0.0065  0.0059  -0.0099 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2148 0.2035 0.1954 0.0085  0.0054  -0.0120 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1915 0.1893 0.1782 0.0080  0.0077  -0.0068 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1920 0.1948 0.1765 0.0086  0.0073  -0.0077 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2046 0.2099 0.1868 0.0120  0.0084  -0.0089 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.2026 0.2079 0.1875 0.0063  0.0065  -0.0069 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.2209 0.2316 0.2025 0.0125  0.0094  -0.0094 63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.2115 0.2205 0.1936 0.0073  0.0077  -0.0069 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.2289 0.2409 0.2101 0.0101  0.0096  -0.0082 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.2470 0.2630 0.2266 0.0112  0.0120  -0.0080 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2076 0.1978 0.1978 0.0034  0.0038  -0.0098 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.2001 0.1904 0.1891 0.0027  0.0002  -0.0124 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1956 0.1912 0.1802 0.0033  -0.0009 -0.0108 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1908 0.1895 0.1786 0.0019  -0.0003 -0.0081 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.2013 0.1900 0.1985 -0.0002 -0.0022 -0.0139 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.2286 0.2181 0.2242 0.0001  -0.0075 -0.0176 64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2337 0.2193 0.2254 0.0015  -0.0092 -0.0220 64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.2370 0.2304 0.2334 -0.0002 -0.0112 -0.0171 64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2531 0.2392 0.2416 0.0028  -0.0150 -0.0263 64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2483 0.2421 0.2410 0.0015  -0.0168 -0.0208 64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2708 0.2612 0.2594 0.0031  -0.0190 -0.0257 64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.3149 0.3057 0.2983 0.0057  -0.0253 -0.0302 64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1988 0.1946 0.1760 0.0057  -0.0018 -0.0124 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.2013 0.2005 0.1725 0.0070  -0.0013 -0.0103 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.2161 0.2135 0.1821 0.0084  -0.0060 -0.0123 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.2270 0.2220 0.1862 0.0111  -0.0079 -0.0159 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.2070 0.2078 0.1727 0.0098  0.0022  -0.0103 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.2393 0.2432 0.1979 0.0117  0.0053  -0.0071 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.2264 0.2250 0.1952 0.0073  -0.0085 -0.0107 66  SER   A N   
464  C CA  . SER   A 60  ? 0.2442 0.2416 0.2081 0.0097  -0.0142 -0.0131 66  SER   A CA  
465  C C   . SER   A 60  ? 0.2528 0.2492 0.2022 0.0145  -0.0137 -0.0122 66  SER   A C   
466  O O   . SER   A 60  ? 0.2703 0.2647 0.2124 0.0179  -0.0187 -0.0164 66  SER   A O   
467  C CB  . SER   A 60  ? 0.2863 0.2855 0.2563 0.0084  -0.0169 -0.0112 66  SER   A CB  
468  O OG  . SER   A 60  ? 0.3554 0.3557 0.3231 0.0084  -0.0127 -0.0055 66  SER   A OG  
469  N N   . SER   A 61  ? 0.2392 0.2369 0.1846 0.0150  -0.0073 -0.0074 67  SER   A N   
470  C CA  . SER   A 61  ? 0.2467 0.2428 0.1782 0.0198  -0.0045 -0.0055 67  SER   A CA  
471  C C   . SER   A 61  ? 0.2532 0.2479 0.1775 0.0229  -0.0039 -0.0097 67  SER   A C   
472  O O   . SER   A 61  ? 0.2702 0.2633 0.1818 0.0276  -0.0014 -0.0087 67  SER   A O   
473  C CB  . SER   A 61  ? 0.2616 0.2596 0.1940 0.0189  0.0032  0.0008  67  SER   A CB  
474  O OG  . SER   A 61  ? 0.2669 0.2686 0.2082 0.0159  0.0077  0.0006  67  SER   A OG  
475  N N   . ARG   A 62  ? 0.2376 0.2321 0.1694 0.0206  -0.0057 -0.0140 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.2492 0.2410 0.1754 0.0234  -0.0060 -0.0187 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.2700 0.2581 0.2011 0.0221  -0.0128 -0.0253 68  ARG   A C   
478  O O   . ARG   A 62  ? 0.2661 0.2506 0.1935 0.0242  -0.0137 -0.0302 68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.2491 0.2433 0.1809 0.0222  -0.0001 -0.0174 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.2710 0.2697 0.2006 0.0234  0.0070  -0.0125 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.2800 0.2770 0.1959 0.0290  0.0097  -0.0132 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.2825 0.2840 0.1986 0.0297  0.0179  -0.0081 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.2965 0.2978 0.2080 0.0302  0.0213  -0.0031 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.2812 0.2785 0.1863 0.0311  0.0164  -0.0024 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.2932 0.2983 0.2073 0.0302  0.0299  0.0013  68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2679 0.2567 0.2088 0.0185  -0.0167 -0.0257 69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.2925 0.2787 0.2425 0.0161  -0.0219 -0.0316 69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.2925 0.2748 0.2474 0.0145  -0.0182 -0.0332 69  ARG   A C   
489  O O   . ARG   A 63  ? 0.2950 0.2726 0.2506 0.0150  -0.0209 -0.0391 69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.3250 0.3090 0.2675 0.0199  -0.0293 -0.0384 69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.3967 0.3837 0.3403 0.0206  -0.0354 -0.0387 69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.4177 0.4032 0.3604 0.0231  -0.0449 -0.0479 69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.4408 0.4290 0.3759 0.0275  -0.0508 -0.0476 69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.4744 0.4607 0.3907 0.0350  -0.0537 -0.0487 69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.4958 0.4779 0.4000 0.0385  -0.0517 -0.0513 69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.4442 0.4323 0.3526 0.0399  -0.0586 -0.0472 69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2854 0.2696 0.2428 0.0133  -0.0121 -0.0281 70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2820 0.2626 0.2415 0.0135  -0.0083 -0.0287 70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.2588 0.2410 0.2257 0.0112  -0.0042 -0.0240 70  LYS   A C   
500  O O   . LYS   A 64  ? 0.2496 0.2370 0.2179 0.0100  -0.0031 -0.0200 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.3359 0.3178 0.2853 0.0180  -0.0050 -0.0281 70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.4363 0.4135 0.3771 0.0219  -0.0071 -0.0337 70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.5207 0.5002 0.4537 0.0263  -0.0021 -0.0321 70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.5979 0.5719 0.5227 0.0307  -0.0029 -0.0377 70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.6548 0.6275 0.5687 0.0338  -0.0069 -0.0413 70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.2408 0.2180 0.2108 0.0113  -0.0016 -0.0244 71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.2258 0.2035 0.1995 0.0110  0.0023  -0.0203 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2370 0.2166 0.2046 0.0153  0.0051  -0.0195 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2607 0.2371 0.2232 0.0183  0.0051  -0.0225 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2226 0.1923 0.2023 0.0095  0.0042  -0.0206 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2457 0.2144 0.2346 0.0050  0.0023  -0.0217 71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2700 0.2405 0.2651 0.0027  0.0043  -0.0181 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2451 0.2117 0.2388 0.0028  -0.0016 -0.0266 71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2556 0.2254 0.2599 -0.0009 0.0022  -0.0205 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2679 0.2358 0.2723 -0.0010 -0.0019 -0.0259 71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.2252 0.2103 0.1942 0.0160  0.0070  -0.0163 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.2332 0.2221 0.1993 0.0202  0.0090  -0.0161 72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2466 0.2351 0.2146 0.0222  0.0104  -0.0141 72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2443 0.2340 0.2159 0.0198  0.0102  -0.0120 72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.2244 0.2227 0.1913 0.0198  0.0096  -0.0150 72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.2399 0.2388 0.2017 0.0200  0.0094  -0.0163 72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2572 0.2552 0.2132 0.0239  0.0107  -0.0187 72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.2462 0.2464 0.2077 0.0171  0.0080  -0.0149 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.2687 0.2665 0.2176 0.0252  0.0107  -0.0199 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2592 0.2592 0.2134 0.0186  0.0078  -0.0157 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.2805 0.2792 0.2279 0.0227  0.0093  -0.0183 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.2925 0.2902 0.2304 0.0252  0.0093  -0.0191 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2510 0.2380 0.2156 0.0273  0.0116  -0.0148 73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2522 0.2393 0.2165 0.0308  0.0122  -0.0130 73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2621 0.2612 0.2307 0.0315  0.0109  -0.0134 73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2611 0.2676 0.2321 0.0314  0.0110  -0.0150 73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2664 0.2473 0.2250 0.0370  0.0135  -0.0139 73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2682 0.2526 0.2261 0.0372  0.0133  -0.0169 73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2383 0.2230 0.1983 0.0310  0.0123  -0.0174 73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2493 0.2504 0.2195 0.0320  0.0099  -0.0123 74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2493 0.2615 0.2255 0.0323  0.0081  -0.0139 74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2464 0.2596 0.2203 0.0382  0.0060  -0.0147 74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2381 0.2425 0.2050 0.0409  0.0068  -0.0126 74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2608 0.2763 0.2429 0.0260  0.0077  -0.0129 74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2740 0.2925 0.2590 0.0216  0.0090  -0.0126 74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2703 0.2777 0.2496 0.0241  0.0081  -0.0105 74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.2415 0.2658 0.2216 0.0405  0.0035  -0.0180 75  SER   A N   
543  C CA  . SER   A 69  ? 0.2389 0.2670 0.2185 0.0460  -0.0002 -0.0202 75  SER   A CA  
544  C C   . SER   A 69  ? 0.2250 0.2603 0.2140 0.0402  -0.0018 -0.0219 75  SER   A C   
545  O O   . SER   A 69  ? 0.2235 0.2662 0.2222 0.0353  -0.0006 -0.0230 75  SER   A O   
546  C CB  . SER   A 69  ? 0.2697 0.3070 0.2530 0.0521  -0.0029 -0.0242 75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3467 0.3759 0.3202 0.0583  -0.0015 -0.0225 75  SER   A OG  
548  N N   . PHE   A 70  ? 0.2083 0.2405 0.1941 0.0410  -0.0035 -0.0217 76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.2061 0.2437 0.2008 0.0355  -0.0047 -0.0234 76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.2173 0.2597 0.2130 0.0400  -0.0099 -0.0281 76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2286 0.2670 0.2138 0.0478  -0.0121 -0.0285 76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.2081 0.2372 0.1999 0.0300  -0.0015 -0.0191 76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.2184 0.2365 0.1988 0.0335  0.0002  -0.0157 76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.2371 0.2470 0.2116 0.0339  0.0036  -0.0124 76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.2323 0.2474 0.2084 0.0359  -0.0008 -0.0159 76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2415 0.2406 0.2074 0.0365  0.0065  -0.0090 76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2365 0.2409 0.2023 0.0393  0.0024  -0.0122 76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2441 0.2406 0.2058 0.0392  0.0065  -0.0085 76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.2202 0.2705 0.2279 0.0356  -0.0119 -0.0318 77  SER   A N   
560  C CA  . SER   A 71  ? 0.2326 0.2880 0.2426 0.0395  -0.0178 -0.0379 77  SER   A CA  
561  C C   . SER   A 71  ? 0.2465 0.2928 0.2460 0.0410  -0.0179 -0.0360 77  SER   A C   
562  O O   . SER   A 71  ? 0.2483 0.2865 0.2440 0.0366  -0.0131 -0.0306 77  SER   A O   
563  C CB  . SER   A 71  ? 0.2394 0.3057 0.2680 0.0335  -0.0194 -0.0430 77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2917 0.3536 0.3242 0.0254  -0.0149 -0.0392 77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2450 0.2927 0.2396 0.0478  -0.0233 -0.0409 78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2590 0.2983 0.2428 0.0504  -0.0231 -0.0398 78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2639 0.3040 0.2584 0.0418  -0.0218 -0.0404 78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2706 0.3190 0.2805 0.0360  -0.0232 -0.0440 78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2877 0.3298 0.2641 0.0605  -0.0305 -0.0464 78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.3453 0.3824 0.3060 0.0708  -0.0307 -0.0439 78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.4139 0.4507 0.3621 0.0823  -0.0376 -0.0492 78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.4920 0.5224 0.4227 0.0938  -0.0375 -0.0460 78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.5622 0.6049 0.5003 0.0990  -0.0452 -0.0528 78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2594 0.2904 0.2462 0.0410  -0.0184 -0.0365 79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2560 0.2869 0.2519 0.0339  -0.0171 -0.0369 79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2515 0.2900 0.2579 0.0334  -0.0232 -0.0455 79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2624 0.3024 0.2626 0.0408  -0.0287 -0.0512 79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2749 0.2954 0.2586 0.0366  -0.0137 -0.0330 79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2947 0.3088 0.2654 0.0422  -0.0104 -0.0279 79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2704 0.2906 0.2401 0.0473  -0.0150 -0.0317 79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2405 0.2838 0.2629 0.0252  -0.0222 -0.0467 80  SER   A N   
582  C CA  . SER   A 74  ? 0.2569 0.3077 0.2932 0.0233  -0.0272 -0.0552 80  SER   A CA  
583  C C   . SER   A 74  ? 0.2403 0.2904 0.2906 0.0139  -0.0234 -0.0539 80  SER   A C   
584  O O   . SER   A 74  ? 0.2370 0.2811 0.2847 0.0098  -0.0175 -0.0462 80  SER   A O   
585  C CB  . SER   A 74  ? 0.2972 0.3592 0.3425 0.0253  -0.0312 -0.0605 80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3635 0.4289 0.4187 0.0189  -0.0260 -0.0562 80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2287 0.2840 0.2934 0.0113  -0.0271 -0.0617 81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2315 0.2850 0.3104 0.0030  -0.0237 -0.0615 81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2320 0.2928 0.3264 -0.0028 -0.0201 -0.0606 81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2360 0.3070 0.3416 -0.0018 -0.0242 -0.0677 81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2306 0.2861 0.3180 0.0037  -0.0300 -0.0719 81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2560 0.3062 0.3544 -0.0029 -0.0271 -0.0724 81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2621 0.3008 0.3478 -0.0034 -0.0217 -0.0635 81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2786 0.3310 0.3850 -0.0013 -0.0345 -0.0844 81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2364 0.2926 0.3307 -0.0078 -0.0126 -0.0519 82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2397 0.3012 0.3452 -0.0125 -0.0075 -0.0493 82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2452 0.3012 0.3599 -0.0197 -0.0006 -0.0447 82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2448 0.2913 0.3499 -0.0203 0.0019  -0.0388 82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2612 0.3215 0.3528 -0.0093 -0.0049 -0.0424 82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2734 0.3395 0.3585 -0.0020 -0.0108 -0.0469 82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2665 0.3293 0.3650 -0.0135 0.0020  -0.0377 82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.2995 0.3613 0.3692 0.0018  -0.0091 -0.0411 82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2368 0.2987 0.3703 -0.0249 0.0031  -0.0470 83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.2508 0.3060 0.3922 -0.0314 0.0110  -0.0417 83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.2673 0.3163 0.3954 -0.0311 0.0179  -0.0307 83  PHE   A C   
606  O O   . PHE   A 77  ? 0.2618 0.3157 0.3854 -0.0289 0.0192  -0.0287 83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2524 0.3151 0.4185 -0.0371 0.0146  -0.0466 83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.2758 0.3299 0.4503 -0.0435 0.0241  -0.0405 83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.2913 0.3442 0.4663 -0.0458 0.0339  -0.0324 83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.3027 0.3484 0.4816 -0.0463 0.0238  -0.0420 83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.3098 0.3532 0.4902 -0.0506 0.0434  -0.0258 83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.3191 0.3553 0.5047 -0.0515 0.0331  -0.0357 83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.3107 0.3456 0.4965 -0.0535 0.0430  -0.0273 83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.2705 0.3085 0.3912 -0.0324 0.0213  -0.0242 84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.2813 0.3128 0.3890 -0.0315 0.0267  -0.0146 84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.3014 0.3254 0.4160 -0.0359 0.0347  -0.0093 84  VAL   A C   
617  O O   . VAL   A 78  ? 0.3061 0.3234 0.4251 -0.0379 0.0346  -0.0100 84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.2829 0.3082 0.3731 -0.0272 0.0225  -0.0115 84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.3074 0.3275 0.3847 -0.0256 0.0263  -0.0032 84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.2727 0.3038 0.3568 -0.0229 0.0156  -0.0166 84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.3083 0.3324 0.4231 -0.0369 0.0423  -0.0039 85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.3216 0.3375 0.4409 -0.0402 0.0518  0.0028  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.3236 0.3269 0.4283 -0.0378 0.0519  0.0096  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.3203 0.3225 0.4100 -0.0334 0.0461  0.0107  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.3761 0.3943 0.4923 -0.0395 0.0596  0.0082  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.5024 0.5193 0.6349 -0.0446 0.0707  0.0107  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.6206 0.6380 0.7454 -0.0424 0.0793  0.0174  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.6502 0.6575 0.7701 -0.0424 0.0891  0.0261  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.6525 0.6794 0.7746 -0.0397 0.0761  0.0141  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.3230 0.3165 0.4332 -0.0406 0.0589  0.0143  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.3297 0.3113 0.4268 -0.0376 0.0593  0.0210  86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.3387 0.3176 0.4153 -0.0318 0.0598  0.0283  86  ALA   A C   
633  O O   . ALA   A 80  ? 0.3433 0.3256 0.4168 -0.0311 0.0644  0.0308  86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.3347 0.3054 0.4406 -0.0410 0.0684  0.0258  86  ALA   A CB  
635  N N   . SER   A 81  ? 0.3427 0.3161 0.4063 -0.0275 0.0548  0.0309  87  SER   A N   
636  C CA  . SER   A 81  ? 0.3560 0.3262 0.4007 -0.0216 0.0539  0.0369  87  SER   A CA  
637  C C   . SER   A 81  ? 0.3744 0.3335 0.4115 -0.0183 0.0535  0.0423  87  SER   A C   
638  O O   . SER   A 81  ? 0.3846 0.3385 0.4316 -0.0211 0.0550  0.0414  87  SER   A O   
639  C CB  . SER   A 81  ? 0.3765 0.3550 0.4148 -0.0191 0.0450  0.0319  87  SER   A CB  
640  O OG  . SER   A 81  ? 0.3886 0.3673 0.4290 -0.0188 0.0382  0.0280  87  SER   A OG  
641  N N   . GLU   A 82  ? 0.3835 0.3389 0.4037 -0.0120 0.0511  0.0471  88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.4095 0.3556 0.4228 -0.0078 0.0495  0.0517  88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.3965 0.3455 0.4164 -0.0085 0.0418  0.0460  88  GLU   A C   
644  O O   . GLU   A 82  ? 0.4051 0.3467 0.4252 -0.0066 0.0414  0.0483  88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.4868 0.4290 0.4807 0.0000  0.0477  0.0574  88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.6067 0.5579 0.5924 0.0027  0.0404  0.0534  88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.7709 0.7178 0.7372 0.0107  0.0389  0.0583  88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.8220 0.7584 0.7792 0.0152  0.0435  0.0656  88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.8090 0.7625 0.7689 0.0130  0.0330  0.0545  88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.3712 0.3304 0.3962 -0.0107 0.0363  0.0389  89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.3579 0.3206 0.3878 -0.0107 0.0299  0.0336  89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.3420 0.3051 0.3853 -0.0153 0.0307  0.0283  89  TYR   A C   
653  O O   . TYR   A 83  ? 0.3457 0.3074 0.3920 -0.0144 0.0275  0.0258  89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.3529 0.3247 0.3791 -0.0097 0.0241  0.0294  89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.3628 0.3347 0.3766 -0.0050 0.0217  0.0329  89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.3832 0.3573 0.3905 -0.0045 0.0238  0.0341  89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.3707 0.3408 0.3796 -0.0006 0.0169  0.0343  89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.4065 0.3805 0.4015 0.0003  0.0207  0.0360  89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.3938 0.3644 0.3918 0.0042  0.0134  0.0362  89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.4180 0.3903 0.4084 0.0046  0.0151  0.0368  89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.4559 0.4286 0.4348 0.0098  0.0110  0.0376  89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.3242 0.2903 0.3763 -0.0198 0.0346  0.0258  90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.3186 0.2865 0.3843 -0.0239 0.0340  0.0190  90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.3361 0.3016 0.4139 -0.0289 0.0410  0.0191  90  TYR   A C   
665  O O   . TYR   A 84  ? 0.3336 0.3010 0.4105 -0.0298 0.0459  0.0224  90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.2988 0.2775 0.3665 -0.0243 0.0286  0.0116  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.2738 0.2555 0.3328 -0.0203 0.0226  0.0102  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.2793 0.2589 0.3397 -0.0189 0.0195  0.0071  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.2755 0.2624 0.3262 -0.0182 0.0206  0.0112  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.2780 0.2604 0.3320 -0.0155 0.0154  0.0061  90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.2663 0.2557 0.3114 -0.0152 0.0161  0.0098  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.2656 0.2529 0.3127 -0.0140 0.0139  0.0074  90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.2418 0.2312 0.2848 -0.0113 0.0109  0.0065  90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.3543 0.3171 0.4451 -0.0324 0.0413  0.0141  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.3543 0.3173 0.4611 -0.0382 0.0473  0.0119  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.3507 0.3272 0.4645 -0.0401 0.0439  0.0046  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.3599 0.3436 0.4663 -0.0368 0.0366  0.0006  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.3663 0.3236 0.4847 -0.0407 0.0460  0.0063  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.3746 0.3352 0.4846 -0.0364 0.0370  0.0016  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.3521 0.3126 0.4447 -0.0312 0.0359  0.0089  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.3291 0.3092 0.4587 -0.0452 0.0492  0.0023  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.3240 0.3177 0.4630 -0.0466 0.0455  -0.0056 92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.3129 0.3109 0.4563 -0.0457 0.0360  -0.0160 92  ALA   A C   
684  O O   . ALA   A 86  ? 0.3143 0.3058 0.4650 -0.0476 0.0354  -0.0192 92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.3279 0.3245 0.4870 -0.0527 0.0531  -0.0070 92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.2909 0.2979 0.4265 -0.0417 0.0288  -0.0203 93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.2812 0.2910 0.4163 -0.0391 0.0201  -0.0291 93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2760 0.2968 0.4062 -0.0351 0.0140  -0.0339 93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2863 0.3118 0.4126 -0.0344 0.0165  -0.0299 93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.2821 0.2829 0.4019 -0.0351 0.0184  -0.0247 93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.2746 0.2772 0.3769 -0.0303 0.0170  -0.0192 93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.2726 0.2667 0.3633 -0.0279 0.0184  -0.0119 93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.2835 0.2800 0.3612 -0.0231 0.0143  -0.0113 93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.2853 0.2860 0.3552 -0.0213 0.0141  -0.0083 93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.2605 0.2622 0.3207 -0.0175 0.0111  -0.0079 93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.2773 0.2808 0.3495 -0.0234 0.0176  -0.0058 93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2701 0.2941 0.3986 -0.0316 0.0063  -0.0421 94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2715 0.3036 0.3913 -0.0262 0.0006  -0.0455 94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2611 0.2874 0.3613 -0.0211 -0.0004 -0.0401 94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2738 0.2935 0.3692 -0.0197 -0.0016 -0.0405 94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2768 0.3151 0.4031 -0.0236 -0.0074 -0.0572 94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2833 0.3306 0.4315 -0.0282 -0.0078 -0.0643 94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2996 0.3582 0.4519 -0.0263 -0.0102 -0.0675 94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.3057 0.3499 0.4718 -0.0346 -0.0049 -0.0674 94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.3099 0.3782 0.4852 -0.0306 -0.0102 -0.0744 94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.3134 0.3661 0.5027 -0.0397 -0.0042 -0.0739 94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.3259 0.3914 0.5204 -0.0377 -0.0070 -0.0776 94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3511 0.4261 0.5715 -0.0431 -0.0060 -0.0847 94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.2312 0.2598 0.3212 -0.0186 0.0006  -0.0352 95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.2142 0.2382 0.2882 -0.0142 -0.0001 -0.0307 95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.2042 0.2324 0.2709 -0.0082 -0.0056 -0.0361 95  GLN   A C   
712  O O   . GLN   A 89  ? 0.2126 0.2482 0.2825 -0.0069 -0.0077 -0.0396 95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.2157 0.2387 0.2828 -0.0148 0.0040  -0.0229 95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.2169 0.2362 0.2704 -0.0107 0.0031  -0.0193 95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.2214 0.2380 0.2696 -0.0118 0.0063  -0.0123 95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2492 0.2630 0.3008 -0.0148 0.0096  -0.0086 95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1971 0.2135 0.2363 -0.0088 0.0056  -0.0105 95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1872 0.2106 0.2443 -0.0040 -0.0076 -0.0370 96  SER   A N   
719  C CA  . SER   A 90  ? 0.1878 0.2132 0.2352 0.0030  -0.0120 -0.0413 96  SER   A CA  
720  C C   . SER   A 90  ? 0.2067 0.2295 0.2408 0.0067  -0.0097 -0.0352 96  SER   A C   
721  O O   . SER   A 90  ? 0.2170 0.2360 0.2494 0.0039  -0.0054 -0.0285 96  SER   A O   
722  C CB  . SER   A 90  ? 0.1865 0.2074 0.2299 0.0065  -0.0146 -0.0459 96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2046 0.2178 0.2422 0.0061  -0.0105 -0.0401 96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1930 0.2172 0.2175 0.0134  -0.0126 -0.0378 97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.2060 0.2263 0.2179 0.0175  -0.0099 -0.0324 97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.2116 0.2338 0.2268 0.0134  -0.0069 -0.0275 97  HIS   A C   
727  O O   . HIS   A 91  ? 0.2168 0.2342 0.2260 0.0133  -0.0033 -0.0219 97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2204 0.2325 0.2247 0.0187  -0.0061 -0.0281 97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2533 0.2625 0.2516 0.0239  -0.0083 -0.0327 97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2836 0.2892 0.2676 0.0322  -0.0085 -0.0332 97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2619 0.2707 0.2660 0.0224  -0.0103 -0.0371 97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2862 0.2898 0.2668 0.0359  -0.0109 -0.0382 97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2724 0.2779 0.2654 0.0299  -0.0123 -0.0411 97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.2017 0.2309 0.2271 0.0102  -0.0081 -0.0299 98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.2104 0.2413 0.2383 0.0068  -0.0050 -0.0257 98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.2031 0.2390 0.2284 0.0110  -0.0068 -0.0277 98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1971 0.2390 0.2261 0.0142  -0.0111 -0.0337 98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.2067 0.2414 0.2479 0.0006  -0.0034 -0.0262 98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.2325 0.2683 0.2755 -0.0026 0.0007  -0.0216 98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2413 0.2698 0.2756 -0.0033 0.0032  -0.0154 98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2474 0.2858 0.3035 -0.0082 0.0035  -0.0219 98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.2088 0.2423 0.2283 0.0115  -0.0041 -0.0233 99  MET   A N   
743  C CA  . MET   A 93  ? 0.2061 0.2429 0.2220 0.0160  -0.0053 -0.0246 99  MET   A CA  
744  C C   . MET   A 93  ? 0.2106 0.2511 0.2322 0.0124  -0.0024 -0.0227 99  MET   A C   
745  O O   . MET   A 93  ? 0.2188 0.2545 0.2378 0.0091  0.0008  -0.0182 99  MET   A O   
746  C CB  . MET   A 93  ? 0.2104 0.2388 0.2130 0.0205  -0.0038 -0.0209 99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2298 0.2533 0.2247 0.0249  -0.0050 -0.0217 99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2574 0.2695 0.2381 0.0297  -0.0009 -0.0164 99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2180 0.2257 0.2037 0.0219  0.0037  -0.0113 99  MET   A CE  
750  N N   . LEU   A 94  ? 0.2032 0.2524 0.2325 0.0134  -0.0037 -0.0265 100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.2186 0.2714 0.2530 0.0105  0.0001  -0.0247 100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.2141 0.2668 0.2415 0.0152  0.0003  -0.0241 100 LEU   A C   
753  O O   . LEU   A 94  ? 0.2031 0.2572 0.2265 0.0213  -0.0031 -0.0269 100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.2386 0.3020 0.2893 0.0078  0.0002  -0.0291 100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.3012 0.3644 0.3621 0.0016  0.0019  -0.0292 100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.3076 0.3808 0.3866 -0.0018 0.0041  -0.0328 100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.3360 0.3905 0.3906 -0.0023 0.0065  -0.0223 100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.2045 0.2561 0.2308 0.0131  0.0044  -0.0209 101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1907 0.2417 0.2109 0.0172  0.0053  -0.0206 101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1861 0.2402 0.2098 0.0146  0.0100  -0.0190 101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1832 0.2368 0.2105 0.0097  0.0129  -0.0166 101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2144 0.2545 0.2219 0.0189  0.0053  -0.0174 101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1848 0.2415 0.2067 0.0186  0.0110  -0.0201 102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1987 0.2571 0.2209 0.0176  0.0160  -0.0185 102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.2217 0.2694 0.2301 0.0180  0.0166  -0.0154 102 VAL   A C   
766  O O   . VAL   A 96  ? 0.2368 0.2788 0.2375 0.0215  0.0143  -0.0160 102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.2143 0.2811 0.2419 0.0220  0.0169  -0.0218 102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.2220 0.2888 0.2468 0.0221  0.0229  -0.0198 102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.2213 0.3002 0.2658 0.0210  0.0158  -0.0259 102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.2288 0.2735 0.2347 0.0145  0.0194  -0.0124 103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.2370 0.2728 0.2314 0.0148  0.0191  -0.0105 103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.2506 0.2845 0.2429 0.0117  0.0217  -0.0071 103 GLY   A C   
773  O O   . GLY   A 97  ? 0.2558 0.2933 0.2558 0.0085  0.0239  -0.0055 103 GLY   A O   
774  N N   . HIS   A 98  ? 0.2447 0.2726 0.2264 0.0131  0.0216  -0.0062 104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.2340 0.2589 0.2105 0.0118  0.0235  -0.0028 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.2310 0.2521 0.2086 0.0088  0.0200  -0.0012 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.2389 0.2565 0.2157 0.0085  0.0155  -0.0030 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.2440 0.2638 0.2073 0.0156  0.0234  -0.0034 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.2560 0.2723 0.2115 0.0160  0.0249  0.0002  104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.2798 0.2983 0.2354 0.0162  0.0320  0.0041  104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.2726 0.2831 0.2205 0.0165  0.0203  0.0005  104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.2988 0.3117 0.2445 0.0175  0.0317  0.0073  104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.2846 0.2932 0.2255 0.0180  0.0239  0.0048  104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.2202 0.2413 0.1997 0.0067  0.0227  0.0024  105 SER   A N   
785  C CA  . SER   A 99  ? 0.2116 0.2289 0.1914 0.0046  0.0196  0.0042  105 SER   A CA  
786  C C   . SER   A 99  ? 0.2203 0.2355 0.1975 0.0042  0.0238  0.0090  105 SER   A C   
787  O O   . SER   A 99  ? 0.2276 0.2456 0.2085 0.0036  0.0302  0.0110  105 SER   A O   
788  C CB  . SER   A 99  ? 0.2206 0.2401 0.2106 0.0016  0.0176  0.0029  105 SER   A CB  
789  O OG  . SER   A 99  ? 0.2539 0.2782 0.2535 -0.0006 0.0213  0.0033  105 SER   A OG  
790  N N   . GLU   A 100 ? 0.2104 0.2204 0.1805 0.0053  0.0207  0.0108  106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.2236 0.2294 0.1890 0.0061  0.0235  0.0159  106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.2348 0.2386 0.2058 0.0038  0.0195  0.0165  106 GLU   A C   
793  O O   . GLU   A 100 ? 0.2260 0.2311 0.2015 0.0026  0.0144  0.0130  106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.2444 0.2455 0.1936 0.0116  0.0219  0.0168  106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.2852 0.2870 0.2271 0.0146  0.0276  0.0173  106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.3481 0.3456 0.2728 0.0209  0.0248  0.0162  106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.3691 0.3614 0.2835 0.0244  0.0225  0.0188  106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.3595 0.3586 0.2806 0.0229  0.0244  0.0123  106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.2383 0.2384 0.2094 0.0035  0.0225  0.0212  107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.2343 0.2325 0.2112 0.0017  0.0191  0.0217  107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.2503 0.2480 0.2244 0.0035  0.0112  0.0189  107 PRO   A C   
802  O O   . PRO   A 101 ? 0.2554 0.2547 0.2381 0.0012  0.0084  0.0167  107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.2458 0.2379 0.2186 0.0030  0.0239  0.0279  107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.2506 0.2437 0.2244 0.0020  0.0323  0.0302  107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.2343 0.2310 0.2009 0.0047  0.0303  0.0267  107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.2535 0.2494 0.2166 0.0078  0.0079  0.0183  108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.2468 0.2433 0.2097 0.0093  0.0002  0.0146  108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.2302 0.2302 0.2008 0.0065  -0.0022 0.0093  108 GLY   A C   
809  O O   . GLY   A 102 ? 0.2325 0.2333 0.2066 0.0066  -0.0075 0.0060  108 GLY   A O   
810  N N   . ASP   A 103 ? 0.2147 0.2169 0.1879 0.0045  0.0018  0.0085  109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.1958 0.1999 0.1746 0.0028  0.0005  0.0045  109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.1903 0.1955 0.1793 -0.0002 0.0006  0.0043  109 ASP   A C   
813  O O   . ASP   A 103 ? 0.1946 0.2000 0.1874 -0.0010 -0.0002 0.0016  109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.1999 0.2060 0.1772 0.0030  0.0044  0.0035  109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.2255 0.2301 0.1925 0.0065  0.0039  0.0022  109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.2287 0.2309 0.1916 0.0082  -0.0009 -0.0003 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.2360 0.2421 0.1997 0.0077  0.0085  0.0033  109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.1844 0.1894 0.1771 -0.0014 0.0021  0.0070  110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.1804 0.1860 0.1814 -0.0035 0.0023  0.0066  110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.1854 0.1904 0.1899 -0.0034 -0.0010 0.0047  110 CYS   A C   
821  O O   . CYS   A 104 ? 0.2136 0.2181 0.2165 -0.0020 -0.0045 0.0045  110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.1883 0.1926 0.1923 -0.0043 0.0040  0.0095  110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.2334 0.2389 0.2393 -0.0060 0.0092  0.0108  110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.1635 0.1688 0.1725 -0.0044 0.0001  0.0031  111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1779 0.1824 0.1922 -0.0048 -0.0013 0.0016  111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.2002 0.2033 0.2134 -0.0046 -0.0012 -0.0009 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.1976 0.1993 0.2164 -0.0054 -0.0003 -0.0019 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.2026 0.2056 0.2091 -0.0036 -0.0011 -0.0016 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.2018 0.2024 0.2067 -0.0030 -0.0006 -0.0039 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.2094 0.2081 0.2158 -0.0026 0.0031  -0.0033 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.2104 0.2109 0.2155 -0.0019 0.0047  -0.0020 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.2012 0.1958 0.2103 -0.0029 0.0045  -0.0043 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.2161 0.2072 0.2248 -0.0015 0.0087  -0.0029 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.2103 0.1996 0.2114 0.0018  0.0101  -0.0032 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1992 0.1869 0.1977 0.0023  0.0091  -0.0049 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.2422 0.2288 0.2583 -0.0031 0.0113  -0.0030 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2607 0.2503 0.2846 -0.0049 0.0112  -0.0020 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2556 0.2355 0.2686 -0.0008 0.0167  -0.0012 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2754 0.2625 0.3106 -0.0074 0.0137  -0.0026 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.2040 0.1933 0.2015 0.0046  0.0120  -0.0019 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.2110 0.1985 0.2016 0.0089  0.0131  -0.0022 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.2147 0.1941 0.2028 0.0114  0.0175  -0.0001 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.2130 0.1914 0.2023 0.0116  0.0196  0.0016  114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.2163 0.2097 0.2048 0.0112  0.0114  -0.0030 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.2410 0.2338 0.2228 0.0170  0.0116  -0.0038 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.2433 0.2365 0.2230 0.0184  0.0111  -0.0051 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.2543 0.2542 0.2369 0.0188  0.0090  -0.0058 114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.2199 0.1929 0.2044 0.0137  0.0197  0.0001  115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.2502 0.2136 0.2315 0.0165  0.0253  0.0030  115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2720 0.2308 0.2431 0.0231  0.0265  0.0038  115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2855 0.2462 0.2547 0.0242  0.0238  0.0016  115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2959 0.2527 0.2847 0.0124  0.0283  0.0030  115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3470 0.3082 0.3474 0.0063  0.0262  0.0012  115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3924 0.3475 0.4010 0.0029  0.0281  -0.0004 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.4213 0.3675 0.4320 0.0037  0.0361  0.0033  115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.4181 0.3645 0.4388 0.0007  0.0398  0.0046  115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.3639 0.3189 0.3941 -0.0035 0.0351  0.0020  115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.3876 0.3252 0.4084 0.0023  0.0486  0.0088  115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2887 0.2401 0.2524 0.0282  0.0310  0.0072  116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.3029 0.2474 0.2555 0.0358  0.0329  0.0087  116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.3118 0.2420 0.2637 0.0362  0.0413  0.0130  116 CYS   A C   
862  O O   . CYS   A 110 ? 0.3063 0.2346 0.2687 0.0298  0.0446  0.0136  116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.3055 0.2525 0.2479 0.0432  0.0311  0.0091  116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.2910 0.2320 0.2297 0.0448  0.0370  0.0132  116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.3274 0.2475 0.2681 0.0436  0.0450  0.0160  117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.3407 0.2455 0.2808 0.0441  0.0545  0.0208  117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.3354 0.2360 0.2766 0.0433  0.0614  0.0250  117 GLN   A C   
868  O O   . GLN   A 111 ? 0.3505 0.2400 0.2966 0.0411  0.0702  0.0287  117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.3853 0.2790 0.3104 0.0541  0.0576  0.0242  117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.4573 0.3514 0.3664 0.0641  0.0567  0.0266  117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.5793 0.4649 0.4729 0.0751  0.0572  0.0288  117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.6196 0.5139 0.5067 0.0813  0.0495  0.0254  117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.5807 0.4492 0.4691 0.0780  0.0666  0.0346  117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.3159 0.2248 0.2535 0.0451  0.0581  0.0243  118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.3178 0.2232 0.2545 0.0458  0.0646  0.0281  118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.2997 0.2130 0.2530 0.0367  0.0640  0.0260  118 HIS   A C   
877  O O   . HIS   A 112 ? 0.3070 0.2168 0.2622 0.0365  0.0706  0.0292  118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.3257 0.2335 0.2467 0.0547  0.0618  0.0283  118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.3560 0.2571 0.2593 0.0655  0.0612  0.0300  118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.3740 0.2846 0.2728 0.0694  0.0513  0.0251  118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.3883 0.2739 0.2784 0.0734  0.0695  0.0362  118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.4046 0.3065 0.2879 0.0797  0.0528  0.0278  118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.4120 0.2980 0.2884 0.0828  0.0638  0.0349  118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.2758 0.1994 0.2400 0.0300  0.0563  0.0208  119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.2704 0.2016 0.2496 0.0223  0.0546  0.0186  119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.2602 0.2043 0.2413 0.0201  0.0450  0.0140  119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2707 0.2182 0.2454 0.0226  0.0397  0.0118  119 GLY   A O   
888  N N   . VAL   A 114 ? 0.2445 0.1952 0.2348 0.0157  0.0433  0.0128  120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.2374 0.1988 0.2304 0.0132  0.0355  0.0093  120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.2379 0.2026 0.2207 0.0183  0.0326  0.0087  120 VAL   A C   
891  O O   . VAL   A 114 ? 0.2495 0.2115 0.2276 0.0219  0.0360  0.0104  120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2470 0.2132 0.2526 0.0079  0.0349  0.0086  120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2564 0.2317 0.2632 0.0062  0.0278  0.0060  120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2487 0.2136 0.2663 0.0028  0.0356  0.0074  120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.2264 0.1973 0.2070 0.0187  0.0266  0.0057  121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.2337 0.2096 0.2082 0.0226  0.0227  0.0036  121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.2294 0.2129 0.2112 0.0184  0.0189  0.0014  121 VAL   A C   
898  O O   . VAL   A 115 ? 0.2265 0.2119 0.2061 0.0208  0.0176  0.0000  121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.2393 0.2179 0.2093 0.0255  0.0192  0.0015  121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2314 0.2175 0.1994 0.0286  0.0142  -0.0022 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2518 0.2215 0.2128 0.0311  0.0230  0.0039  121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.2211 0.2085 0.2109 0.0130  0.0169  0.0008  122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.2175 0.2108 0.2136 0.0094  0.0138  -0.0005 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.2188 0.2147 0.2206 0.0048  0.0120  -0.0004 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.2156 0.2088 0.2177 0.0040  0.0127  0.0000  122 GLY   A O   
906  N N   . ILE   A 117 ? 0.2073 0.2075 0.2130 0.0023  0.0096  -0.0009 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.2046 0.2066 0.2131 -0.0006 0.0078  -0.0004 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1976 0.2039 0.2057 -0.0013 0.0065  -0.0010 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1961 0.2046 0.2059 -0.0012 0.0064  -0.0019 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.2056 0.2073 0.2198 -0.0027 0.0072  0.0008  123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.2197 0.2222 0.2362 -0.0026 0.0075  0.0011  123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.2243 0.2228 0.2420 -0.0029 0.0089  0.0010  123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2462 0.2488 0.2683 -0.0041 0.0065  0.0024  123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1788 0.1858 0.1851 -0.0021 0.0057  -0.0006 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1579 0.1683 0.1640 -0.0028 0.0061  -0.0003 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.1711 0.1818 0.1814 -0.0047 0.0064  0.0014  124 VAL   A C   
917  O O   . VAL   A 118 ? 0.1827 0.1910 0.1940 -0.0053 0.0053  0.0028  124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.1704 0.1803 0.1718 -0.0024 0.0056  0.0003  124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.1760 0.1885 0.1769 -0.0029 0.0078  0.0018  124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1851 0.1940 0.1826 -0.0004 0.0055  -0.0017 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.1684 0.1819 0.1825 -0.0056 0.0077  0.0006  125 SER   A N   
922  C CA  . SER   A 119 ? 0.1801 0.1927 0.1992 -0.0076 0.0085  0.0018  125 SER   A CA  
923  C C   . SER   A 119 ? 0.2047 0.2194 0.2272 -0.0093 0.0115  0.0027  125 SER   A C   
924  O O   . SER   A 119 ? 0.2234 0.2353 0.2478 -0.0109 0.0135  0.0055  125 SER   A O   
925  C CB  . SER   A 119 ? 0.1958 0.2086 0.2189 -0.0072 0.0075  -0.0010 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.2231 0.2343 0.2516 -0.0092 0.0082  -0.0006 125 SER   A OG  
927  N N   . THR   A 120 ? 0.2050 0.2246 0.2292 -0.0089 0.0126  0.0005  126 THR   A N   
928  C CA  . THR   A 120 ? 0.2239 0.2464 0.2537 -0.0109 0.0167  0.0013  126 THR   A CA  
929  C C   . THR   A 120 ? 0.2318 0.2573 0.2571 -0.0090 0.0185  0.0015  126 THR   A C   
930  O O   . THR   A 120 ? 0.2160 0.2411 0.2346 -0.0064 0.0160  0.0004  126 THR   A O   
931  C CB  . THR   A 120 ? 0.2341 0.2615 0.2759 -0.0128 0.0165  -0.0032 126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.2315 0.2648 0.2741 -0.0103 0.0138  -0.0077 126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.2412 0.2654 0.2862 -0.0137 0.0140  -0.0047 126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.2425 0.2708 0.2725 -0.0104 0.0236  0.0028  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.2637 0.2952 0.2901 -0.0082 0.0261  0.0027  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.2819 0.3144 0.3118 -0.0096 0.0335  0.0060  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.2755 0.3063 0.3130 -0.0129 0.0370  0.0080  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.2916 0.3254 0.3151 -0.0068 0.0364  0.0070  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.3007 0.3350 0.3256 -0.0071 0.0449  0.0106  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.2957 0.3394 0.3300 -0.0066 0.0479  0.0071  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.2947 0.3452 0.3384 -0.0070 0.0433  0.0016  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.2947 0.3389 0.3251 -0.0046 0.0551  0.0099  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.2878 0.3416 0.3284 -0.0037 0.0595  0.0071  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.2696 0.3288 0.3093 -0.0003 0.0527  0.0013  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.2673 0.3365 0.3211 -0.0004 0.0524  -0.0034 129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.3145 0.3756 0.3774 -0.0090 0.0637  0.0054  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.3957 0.4505 0.4601 -0.0121 0.0728  0.0119  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.4177 0.4684 0.4728 -0.0097 0.0810  0.0173  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.4100 0.4626 0.4850 -0.0171 0.0720  0.0118  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.2532 0.3057 0.2771 0.0030  0.0471  0.0013  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.2435 0.2983 0.2646 0.0067  0.0412  -0.0034 130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.2317 0.2880 0.2587 0.0055  0.0341  -0.0069 130 GLY   A C   
953  O O   . GLY   A 124 ? 0.2410 0.2993 0.2668 0.0090  0.0298  -0.0105 130 GLY   A O   
954  N N   . LEU   A 125 ? 0.2081 0.2619 0.2393 0.0015  0.0327  -0.0056 131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.1903 0.2440 0.2244 0.0011  0.0262  -0.0087 131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.1906 0.2347 0.2138 0.0005  0.0230  -0.0060 131 LEU   A C   
957  O O   . LEU   A 125 ? 0.1846 0.2232 0.2013 -0.0005 0.0253  -0.0020 131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.1957 0.2552 0.2455 -0.0027 0.0263  -0.0112 131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.2305 0.3018 0.2959 -0.0026 0.0280  -0.0157 131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2419 0.3177 0.3245 -0.0077 0.0292  -0.0180 131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.2193 0.2957 0.2842 0.0026  0.0215  -0.0212 131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.1723 0.2147 0.1936 0.0019  0.0178  -0.0083 132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.1776 0.2124 0.1925 0.0010  0.0152  -0.0063 132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1861 0.2218 0.2054 0.0011  0.0117  -0.0089 132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1971 0.2365 0.2177 0.0043  0.0096  -0.0123 132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1925 0.2213 0.1967 0.0035  0.0136  -0.0056 132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.1975 0.2271 0.1996 0.0074  0.0119  -0.0084 132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.1919 0.2145 0.1930 0.0019  0.0113  -0.0039 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.1745 0.2073 0.1961 -0.0016 0.0112  -0.0076 133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1680 0.2006 0.1924 -0.0012 0.0082  -0.0102 133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1726 0.1982 0.1904 -0.0006 0.0070  -0.0081 133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1804 0.2022 0.1962 -0.0026 0.0080  -0.0049 133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1737 0.1978 0.1883 0.0025  0.0049  -0.0100 134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1720 0.1898 0.1815 0.0033  0.0050  -0.0079 134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1768 0.1936 0.1878 0.0041  0.0040  -0.0095 134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1620 0.1816 0.1730 0.0070  0.0020  -0.0131 134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1593 0.1736 0.1615 0.0073  0.0054  -0.0078 134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1674 0.1824 0.1674 0.0076  0.0060  -0.0074 134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1704 0.1817 0.1688 0.0056  0.0069  -0.0054 134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1717 0.1913 0.1716 0.0105  0.0054  -0.0098 134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1830 0.1942 0.1783 0.0064  0.0073  -0.0058 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1803 0.2001 0.1777 0.0113  0.0064  -0.0096 134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1835 0.1986 0.1780 0.0093  0.0074  -0.0076 134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1653 0.1781 0.1770 0.0022  0.0050  -0.0073 135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1725 0.1832 0.1846 0.0034  0.0046  -0.0084 135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1794 0.1858 0.1835 0.0079  0.0060  -0.0078 135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1928 0.1954 0.1955 0.0074  0.0084  -0.0048 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1812 0.1893 0.1972 0.0003  0.0057  -0.0058 135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1718 0.1784 0.1711 0.0126  0.0046  -0.0108 136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1910 0.1919 0.1805 0.0181  0.0069  -0.0094 136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.2014 0.1971 0.1903 0.0181  0.0105  -0.0070 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1963 0.1931 0.1895 0.0165  0.0095  -0.0084 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2214 0.2238 0.2042 0.0245  0.0036  -0.0137 136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.3001 0.2957 0.2699 0.0319  0.0063  -0.0117 136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2910 0.2827 0.2577 0.0324  0.0095  -0.0081 136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3198 0.3129 0.2820 0.0374  0.0057  -0.0136 136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1863 0.1759 0.1705 0.0201  0.0153  -0.0033 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1997 0.1846 0.1838 0.0208  0.0200  -0.0009 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.2311 0.2089 0.2032 0.0280  0.0246  0.0010  137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.2479 0.2213 0.2190 0.0295  0.0299  0.0033  137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.2089 0.1933 0.2027 0.0155  0.0229  0.0022  137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.2044 0.1946 0.2073 0.0100  0.0185  0.0010  137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.2151 0.1959 0.2076 0.0154  0.0256  0.0044  137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.2315 0.2078 0.1939 0.0331  0.0231  0.0002  138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.2556 0.2237 0.2040 0.0412  0.0277  0.0027  138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.2809 0.2464 0.2195 0.0477  0.0281  0.0012  138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.2970 0.2538 0.2243 0.0540  0.0347  0.0050  138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.2609 0.2289 0.2012 0.0460  0.0245  0.0016  138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.2678 0.2353 0.2144 0.0414  0.0258  0.0039  138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.2877 0.2557 0.2262 0.0471  0.0223  0.0023  138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.2905 0.2693 0.2343 0.0459  0.0143  -0.0035 138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2995 0.2826 0.2410 0.0496  0.0098  -0.0063 138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.2793 0.2559 0.2113 0.0555  0.0122  -0.0036 138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2778 0.2715 0.2275 0.0474  0.0036  -0.0117 138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.2684 0.2405 0.2108 0.0467  0.0218  -0.0044 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.2810 0.2507 0.2143 0.0530  0.0214  -0.0072 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.2882 0.2545 0.2259 0.0507  0.0276  -0.0044 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.3138 0.2762 0.2420 0.0568  0.0292  -0.0058 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.2819 0.2592 0.2188 0.0528  0.0122  -0.0152 139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.3377 0.3211 0.2917 0.0432  0.0099  -0.0167 139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.3296 0.3149 0.2927 0.0367  0.0117  -0.0131 139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.3551 0.3406 0.3126 0.0427  0.0065  -0.0215 139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.2718 0.2398 0.2233 0.0427  0.0307  -0.0011 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.2669 0.2335 0.2255 0.0403  0.0361  0.0012  140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.2809 0.2396 0.2344 0.0438  0.0463  0.0071  140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.2681 0.2264 0.2322 0.0387  0.0512  0.0109  140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.2516 0.2243 0.2276 0.0311  0.0338  0.0016  140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2663 0.2456 0.2476 0.0274  0.0254  -0.0031 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2638 0.2476 0.2590 0.0198  0.0239  -0.0017 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2859 0.2653 0.2649 0.0302  0.0227  -0.0076 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.2971 0.2491 0.2341 0.0529  0.0499  0.0075  141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.3146 0.2571 0.2440 0.0575  0.0612  0.0140  141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.3155 0.2575 0.2579 0.0533  0.0698  0.0176  141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.3195 0.2562 0.2656 0.0523  0.0792  0.0232  141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.3288 0.2636 0.2352 0.0696  0.0632  0.0138  141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.3647 0.3015 0.2584 0.0753  0.0531  0.0086  141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.3951 0.3229 0.2640 0.0889  0.0558  0.0092  141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.3743 0.3125 0.2719 0.0718  0.0506  0.0103  141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.3129 0.2603 0.2634 0.0509  0.0669  0.0143  142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.3284 0.2770 0.2927 0.0475  0.0741  0.0168  142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.3314 0.2851 0.3161 0.0382  0.0746  0.0187  142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.3325 0.2875 0.3306 0.0356  0.0814  0.0211  142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.3223 0.2755 0.2903 0.0475  0.0695  0.0122  142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.3182 0.2786 0.2924 0.0424  0.0577  0.0071  142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.3297 0.2908 0.2941 0.0451  0.0495  0.0020  142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.3119 0.2794 0.3037 0.0342  0.0533  0.0066  142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.3323 0.3001 0.3082 0.0384  0.0416  -0.0010 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.3199 0.2911 0.3110 0.0322  0.0438  0.0020  142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.3071 0.2783 0.3155 0.0288  0.0564  0.0092  142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.3190 0.2961 0.3229 0.0255  0.0384  0.0012  142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.3088 0.2866 0.3294 0.0228  0.0495  0.0075  142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.3143 0.2942 0.3314 0.0214  0.0411  0.0041  142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.3349 0.2923 0.3231 0.0336  0.0673  0.0171  143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.3439 0.3056 0.3497 0.0256  0.0669  0.0180  143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.3962 0.3517 0.4066 0.0255  0.0779  0.0230  143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.3839 0.3430 0.4124 0.0195  0.0800  0.0233  143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.3265 0.2914 0.3314 0.0223  0.0583  0.0157  143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.3181 0.2902 0.3256 0.0196  0.0484  0.0114  143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.3172 0.2916 0.3225 0.0172  0.0419  0.0098  143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.3127 0.2908 0.3363 0.0145  0.0468  0.0108  143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.4525 0.3982 0.4465 0.0323  0.0848  0.0265  144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.5104 0.4473 0.5058 0.0332  0.0968  0.0322  144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.5628 0.4962 0.5624 0.0355  0.1089  0.0360  144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.5794 0.5041 0.5793 0.0368  0.1207  0.0414  144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.5590 0.4854 0.5318 0.0413  0.0994  0.0352  144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.6563 0.5835 0.6266 0.0392  0.0916  0.0332  144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.6713 0.6035 0.6582 0.0311  0.0884  0.0315  144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.7139 0.6369 0.6655 0.0463  0.0883  0.0330  144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.5892 0.5281 0.5912 0.0367  0.1072  0.0336  145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.6268 0.5632 0.6333 0.0395  0.1191  0.0369  145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.6417 0.5893 0.6672 0.0345  0.1147  0.0330  145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.6568 0.6061 0.6962 0.0336  0.1237  0.0350  145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.6796 0.6074 0.6605 0.0508  0.1234  0.0385  145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.7569 0.6896 0.7273 0.0537  0.1112  0.0322  145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.8591 0.7836 0.8014 0.0645  0.1098  0.0317  145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.8718 0.7967 0.8039 0.0700  0.1066  0.0279  145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.8945 0.8121 0.8249 0.0677  0.1114  0.0347  145 GLU   A OE2 
1078 N N   . SER   B 1   ? 0.3187 0.3046 0.3087 0.0134  -0.0312 -0.0098 7   SER   C N   
1079 C CA  . SER   B 1   ? 0.3077 0.2973 0.3104 0.0133  -0.0333 -0.0104 7   SER   C CA  
1080 C C   . SER   B 1   ? 0.2959 0.2896 0.3056 0.0126  -0.0305 -0.0094 7   SER   C C   
1081 O O   . SER   B 1   ? 0.2923 0.2844 0.2969 0.0122  -0.0290 -0.0078 7   SER   C O   
1082 C CB  . SER   B 1   ? 0.3297 0.3147 0.3339 0.0140  -0.0407 -0.0108 7   SER   C CB  
1083 O OG  . SER   B 1   ? 0.3786 0.3597 0.3799 0.0140  -0.0437 -0.0089 7   SER   C OG  
1084 N N   . GLY   B 2   ? 0.2745 0.2731 0.2956 0.0121  -0.0297 -0.0105 8   GLY   C N   
1085 C CA  . GLY   B 2   ? 0.2637 0.2659 0.2913 0.0113  -0.0266 -0.0105 8   GLY   C CA  
1086 C C   . GLY   B 2   ? 0.2524 0.2607 0.2877 0.0097  -0.0227 -0.0118 8   GLY   C C   
1087 O O   . GLY   B 2   ? 0.2542 0.2639 0.2880 0.0089  -0.0216 -0.0117 8   GLY   C O   
1088 N N   . ALA   B 3   ? 0.2340 0.2454 0.2774 0.0091  -0.0207 -0.0131 9   ALA   C N   
1089 C CA  . ALA   B 3   ? 0.2237 0.2405 0.2731 0.0069  -0.0164 -0.0144 9   ALA   C CA  
1090 C C   . ALA   B 3   ? 0.2221 0.2411 0.2741 0.0058  -0.0121 -0.0158 9   ALA   C C   
1091 O O   . ALA   B 3   ? 0.2377 0.2543 0.2903 0.0072  -0.0133 -0.0161 9   ALA   C O   
1092 C CB  . ALA   B 3   ? 0.2150 0.2342 0.2750 0.0069  -0.0184 -0.0159 9   ALA   C CB  
1093 N N   . ILE   B 4   ? 0.2145 0.2376 0.2675 0.0030  -0.0073 -0.0166 10  ILE   C N   
1094 C CA  . ILE   B 4   ? 0.1959 0.2208 0.2506 0.0015  -0.0028 -0.0189 10  ILE   C CA  
1095 C C   . ILE   B 4   ? 0.2046 0.2339 0.2699 0.0004  0.0000  -0.0219 10  ILE   C C   
1096 O O   . ILE   B 4   ? 0.1982 0.2301 0.2652 -0.0014 0.0006  -0.0212 10  ILE   C O   
1097 C CB  . ILE   B 4   ? 0.1885 0.2140 0.2343 -0.0018 0.0006  -0.0176 10  ILE   C CB  
1098 C CG1 . ILE   B 4   ? 0.1874 0.2097 0.2250 -0.0008 -0.0019 -0.0146 10  ILE   C CG1 
1099 C CG2 . ILE   B 4   ? 0.1955 0.2221 0.2415 -0.0038 0.0053  -0.0205 10  ILE   C CG2 
1100 C CD1 . ILE   B 4   ? 0.1989 0.2221 0.2298 -0.0039 -0.0002 -0.0126 10  ILE   C CD1 
1101 N N   . TYR   B 5   ? 0.2146 0.2450 0.2881 0.0015  0.0019  -0.0253 11  TYR   C N   
1102 C CA  . TYR   B 5   ? 0.2164 0.2521 0.3023 0.0007  0.0055  -0.0288 11  TYR   C CA  
1103 C C   . TYR   B 5   ? 0.2307 0.2683 0.3151 -0.0018 0.0127  -0.0323 11  TYR   C C   
1104 O O   . TYR   B 5   ? 0.2322 0.2677 0.3183 -0.0001 0.0132  -0.0347 11  TYR   C O   
1105 C CB  . TYR   B 5   ? 0.2118 0.2473 0.3114 0.0046  0.0014  -0.0307 11  TYR   C CB  
1106 C CG  . TYR   B 5   ? 0.2257 0.2588 0.3257 0.0064  -0.0061 -0.0275 11  TYR   C CG  
1107 C CD1 . TYR   B 5   ? 0.2296 0.2662 0.3368 0.0053  -0.0068 -0.0274 11  TYR   C CD1 
1108 C CD2 . TYR   B 5   ? 0.2421 0.2688 0.3336 0.0086  -0.0119 -0.0245 11  TYR   C CD2 
1109 C CE1 . TYR   B 5   ? 0.2402 0.2738 0.3466 0.0067  -0.0139 -0.0249 11  TYR   C CE1 
1110 C CE2 . TYR   B 5   ? 0.2489 0.2726 0.3384 0.0099  -0.0184 -0.0221 11  TYR   C CE2 
1111 C CZ  . TYR   B 5   ? 0.2515 0.2784 0.3484 0.0091  -0.0196 -0.0225 11  TYR   C CZ  
1112 O OH  . TYR   B 5   ? 0.2518 0.2750 0.3456 0.0100  -0.0262 -0.0205 11  TYR   C OH  
1113 N N   . VAL   B 6   ? 0.2399 0.2809 0.3207 -0.0062 0.0182  -0.0327 12  VAL   C N   
1114 C CA  . VAL   B 6   ? 0.2546 0.2968 0.3313 -0.0094 0.0253  -0.0363 12  VAL   C CA  
1115 C C   . VAL   B 6   ? 0.2739 0.3220 0.3570 -0.0128 0.0319  -0.0389 12  VAL   C C   
1116 O O   . VAL   B 6   ? 0.2784 0.3281 0.3598 -0.0154 0.0313  -0.0358 12  VAL   C O   
1117 C CB  . VAL   B 6   ? 0.2714 0.3097 0.3312 -0.0124 0.0251  -0.0332 12  VAL   C CB  
1118 C CG1 . VAL   B 6   ? 0.2742 0.3122 0.3274 -0.0145 0.0221  -0.0280 12  VAL   C CG1 
1119 C CG2 . VAL   B 6   ? 0.2859 0.3246 0.3391 -0.0167 0.0321  -0.0368 12  VAL   C CG2 
1120 N N   . GLY   B 7   ? 0.2794 0.3308 0.3718 -0.0127 0.0380  -0.0449 13  GLY   C N   
1121 C CA  . GLY   B 7   ? 0.2811 0.3390 0.3811 -0.0162 0.0455  -0.0480 13  GLY   C CA  
1122 C C   . GLY   B 7   ? 0.2859 0.3478 0.3988 -0.0150 0.0419  -0.0457 13  GLY   C C   
1123 O O   . GLY   B 7   ? 0.2980 0.3590 0.4212 -0.0100 0.0352  -0.0452 13  GLY   C O   
1124 N N   . ASN   B 8   ? 0.2757 0.3407 0.3861 -0.0198 0.0446  -0.0433 14  ASN   C N   
1125 C CA  . ASN   B 8   ? 0.2714 0.3395 0.3935 -0.0191 0.0404  -0.0408 14  ASN   C CA  
1126 C C   . ASN   B 8   ? 0.2453 0.3083 0.3561 -0.0195 0.0329  -0.0343 14  ASN   C C   
1127 O O   . ASN   B 8   ? 0.2400 0.3047 0.3542 -0.0218 0.0314  -0.0315 14  ASN   C O   
1128 C CB  . ASN   B 8   ? 0.3068 0.3823 0.4381 -0.0238 0.0482  -0.0428 14  ASN   C CB  
1129 C CG  . ASN   B 8   ? 0.3876 0.4695 0.5366 -0.0220 0.0546  -0.0498 14  ASN   C CG  
1130 O OD1 . ASN   B 8   ? 0.4125 0.4958 0.5776 -0.0165 0.0498  -0.0517 14  ASN   C OD1 
1131 N ND2 . ASN   B 8   ? 0.4029 0.4885 0.5490 -0.0266 0.0654  -0.0538 14  ASN   C ND2 
1132 N N   . TYR   B 9   ? 0.2310 0.2877 0.3298 -0.0171 0.0282  -0.0321 15  TYR   C N   
1133 C CA  . TYR   B 9   ? 0.2194 0.2713 0.3080 -0.0170 0.0217  -0.0268 15  TYR   C CA  
1134 C C   . TYR   B 9   ? 0.2017 0.2492 0.2905 -0.0113 0.0142  -0.0258 15  TYR   C C   
1135 O O   . TYR   B 9   ? 0.1886 0.2348 0.2788 -0.0084 0.0141  -0.0281 15  TYR   C O   
1136 C CB  . TYR   B 9   ? 0.2284 0.2768 0.3000 -0.0205 0.0236  -0.0245 15  TYR   C CB  
1137 C CG  . TYR   B 9   ? 0.2487 0.2994 0.3153 -0.0270 0.0301  -0.0242 15  TYR   C CG  
1138 C CD1 . TYR   B 9   ? 0.2757 0.3286 0.3461 -0.0303 0.0302  -0.0217 15  TYR   C CD1 
1139 C CD2 . TYR   B 9   ? 0.2771 0.3272 0.3341 -0.0304 0.0359  -0.0262 15  TYR   C CD2 
1140 C CE1 . TYR   B 9   ? 0.2990 0.3535 0.3636 -0.0371 0.0363  -0.0208 15  TYR   C CE1 
1141 C CE2 . TYR   B 9   ? 0.2932 0.3446 0.3433 -0.0372 0.0420  -0.0258 15  TYR   C CE2 
1142 C CZ  . TYR   B 9   ? 0.3172 0.3708 0.3709 -0.0406 0.0423  -0.0228 15  TYR   C CZ  
1143 O OH  . TYR   B 9   ? 0.3549 0.4093 0.4005 -0.0480 0.0483  -0.0217 15  TYR   C OH  
1144 N N   . ARG   B 10  ? 0.1860 0.2306 0.2724 -0.0101 0.0080  -0.0224 16  ARG   C N   
1145 C CA  . ARG   B 10  ? 0.1820 0.2216 0.2649 -0.0057 0.0012  -0.0209 16  ARG   C CA  
1146 C C   . ARG   B 10  ? 0.1904 0.2263 0.2608 -0.0068 -0.0006 -0.0173 16  ARG   C C   
1147 O O   . ARG   B 10  ? 0.1970 0.2332 0.2666 -0.0093 -0.0011 -0.0153 16  ARG   C O   
1148 C CB  . ARG   B 10  ? 0.1733 0.2127 0.2661 -0.0033 -0.0047 -0.0210 16  ARG   C CB  
1149 C CG  . ARG   B 10  ? 0.1967 0.2300 0.2824 -0.0002 -0.0118 -0.0188 16  ARG   C CG  
1150 C CD  . ARG   B 10  ? 0.2217 0.2539 0.3165 0.0021  -0.0182 -0.0194 16  ARG   C CD  
1151 N NE  . ARG   B 10  ? 0.2674 0.2946 0.3552 0.0030  -0.0238 -0.0175 16  ARG   C NE  
1152 C CZ  . ARG   B 10  ? 0.2839 0.3052 0.3645 0.0059  -0.0291 -0.0169 16  ARG   C CZ  
1153 N NH1 . ARG   B 10  ? 0.2480 0.2673 0.3273 0.0080  -0.0301 -0.0172 16  ARG   C NH1 
1154 N NH2 . ARG   B 10  ? 0.2607 0.2773 0.3347 0.0064  -0.0335 -0.0160 16  ARG   C NH2 
1155 N N   . VAL   B 11  ? 0.1840 0.2164 0.2454 -0.0052 -0.0016 -0.0163 17  VAL   C N   
1156 C CA  . VAL   B 11  ? 0.1844 0.2139 0.2359 -0.0058 -0.0031 -0.0133 17  VAL   C CA  
1157 C C   . VAL   B 11  ? 0.1881 0.2137 0.2371 -0.0020 -0.0082 -0.0124 17  VAL   C C   
1158 O O   . VAL   B 11  ? 0.2040 0.2279 0.2520 0.0005  -0.0092 -0.0133 17  VAL   C O   
1159 C CB  . VAL   B 11  ? 0.1985 0.2277 0.2423 -0.0075 0.0000  -0.0129 17  VAL   C CB  
1160 C CG1 . VAL   B 11  ? 0.2144 0.2414 0.2506 -0.0084 -0.0019 -0.0096 17  VAL   C CG1 
1161 C CG2 . VAL   B 11  ? 0.1886 0.2208 0.2332 -0.0113 0.0055  -0.0147 17  VAL   C CG2 
1162 N N   . VAL   B 12  ? 0.1726 0.1962 0.2200 -0.0016 -0.0113 -0.0110 18  VAL   C N   
1163 C CA  . VAL   B 12  ? 0.1926 0.2122 0.2363 0.0018  -0.0154 -0.0109 18  VAL   C CA  
1164 C C   . VAL   B 12  ? 0.1916 0.2092 0.2294 0.0019  -0.0160 -0.0092 18  VAL   C C   
1165 O O   . VAL   B 12  ? 0.1859 0.2048 0.2243 -0.0007 -0.0150 -0.0077 18  VAL   C O   
1166 C CB  . VAL   B 12  ? 0.2136 0.2316 0.2629 0.0030  -0.0199 -0.0120 18  VAL   C CB  
1167 C CG1 . VAL   B 12  ? 0.2425 0.2618 0.2989 0.0040  -0.0207 -0.0136 18  VAL   C CG1 
1168 C CG2 . VAL   B 12  ? 0.2016 0.2211 0.2558 0.0005  -0.0203 -0.0113 18  VAL   C CG2 
1169 N N   . ASN   B 13  ? 0.1900 0.2041 0.2228 0.0047  -0.0181 -0.0095 19  ASN   C N   
1170 C CA  . ASN   B 13  ? 0.2013 0.2136 0.2311 0.0055  -0.0187 -0.0089 19  ASN   C CA  
1171 C C   . ASN   B 13  ? 0.2074 0.2184 0.2416 0.0048  -0.0218 -0.0091 19  ASN   C C   
1172 O O   . ASN   B 13  ? 0.2157 0.2251 0.2524 0.0054  -0.0246 -0.0105 19  ASN   C O   
1173 C CB  . ASN   B 13  ? 0.2099 0.2187 0.2336 0.0085  -0.0196 -0.0101 19  ASN   C CB  
1174 C CG  . ASN   B 13  ? 0.2339 0.2437 0.2533 0.0088  -0.0167 -0.0094 19  ASN   C CG  
1175 O OD1 . ASN   B 13  ? 0.2346 0.2434 0.2522 0.0092  -0.0170 -0.0097 19  ASN   C OD1 
1176 N ND2 . ASN   B 13  ? 0.2269 0.2386 0.2455 0.0086  -0.0143 -0.0083 19  ASN   C ND2 
1177 N N   . ARG   B 14  ? 0.2013 0.2125 0.2369 0.0031  -0.0218 -0.0075 20  ARG   C N   
1178 C CA  . ARG   B 14  ? 0.2040 0.2133 0.2440 0.0019  -0.0249 -0.0072 20  ARG   C CA  
1179 C C   . ARG   B 14  ? 0.2092 0.2137 0.2481 0.0051  -0.0288 -0.0098 20  ARG   C C   
1180 O O   . ARG   B 14  ? 0.2178 0.2208 0.2606 0.0044  -0.0319 -0.0106 20  ARG   C O   
1181 C CB  . ARG   B 14  ? 0.2119 0.2208 0.2527 -0.0002 -0.0253 -0.0045 20  ARG   C CB  
1182 C CG  . ARG   B 14  ? 0.2242 0.2312 0.2699 -0.0027 -0.0283 -0.0032 20  ARG   C CG  
1183 C CD  . ARG   B 14  ? 0.2219 0.2268 0.2676 -0.0039 -0.0299 -0.0004 20  ARG   C CD  
1184 N NE  . ARG   B 14  ? 0.2419 0.2442 0.2916 -0.0071 -0.0331 0.0019  20  ARG   C NE  
1185 C CZ  . ARG   B 14  ? 0.2540 0.2514 0.3070 -0.0053 -0.0374 0.0009  20  ARG   C CZ  
1186 N NH1 . ARG   B 14  ? 0.2397 0.2345 0.2916 -0.0005 -0.0386 -0.0031 20  ARG   C NH1 
1187 N NH2 . ARG   B 14  ? 0.2501 0.2447 0.3068 -0.0088 -0.0405 0.0037  20  ARG   C NH2 
1188 N N   . HIS   B 15  ? 0.2052 0.2073 0.2384 0.0082  -0.0282 -0.0114 21  HIS   C N   
1189 C CA  . HIS   B 15  ? 0.1984 0.1952 0.2282 0.0109  -0.0312 -0.0144 21  HIS   C CA  
1190 C C   . HIS   B 15  ? 0.2221 0.2169 0.2492 0.0115  -0.0336 -0.0160 21  HIS   C C   
1191 O O   . HIS   B 15  ? 0.2380 0.2276 0.2620 0.0129  -0.0373 -0.0184 21  HIS   C O   
1192 C CB  . HIS   B 15  ? 0.1885 0.1836 0.2131 0.0138  -0.0290 -0.0162 21  HIS   C CB  
1193 C CG  . HIS   B 15  ? 0.2102 0.2068 0.2284 0.0148  -0.0255 -0.0164 21  HIS   C CG  
1194 N ND1 . HIS   B 15  ? 0.2063 0.2076 0.2257 0.0135  -0.0220 -0.0139 21  HIS   C ND1 
1195 C CD2 . HIS   B 15  ? 0.2342 0.2273 0.2441 0.0164  -0.0254 -0.0185 21  HIS   C CD2 
1196 C CE1 . HIS   B 15  ? 0.2327 0.2337 0.2458 0.0145  -0.0198 -0.0145 21  HIS   C CE1 
1197 N NE2 . HIS   B 15  ? 0.2426 0.2385 0.2492 0.0161  -0.0216 -0.0170 21  HIS   C NE2 
1198 N N   . LEU   B 16  ? 0.2153 0.2137 0.2437 0.0104  -0.0321 -0.0147 22  LEU   C N   
1199 C CA  . LEU   B 16  ? 0.2296 0.2261 0.2574 0.0110  -0.0353 -0.0156 22  LEU   C CA  
1200 C C   . LEU   B 16  ? 0.2388 0.2387 0.2772 0.0088  -0.0369 -0.0150 22  LEU   C C   
1201 O O   . LEU   B 16  ? 0.2451 0.2443 0.2860 0.0092  -0.0400 -0.0156 22  LEU   C O   
1202 C CB  . LEU   B 16  ? 0.2214 0.2185 0.2438 0.0118  -0.0329 -0.0150 22  LEU   C CB  
1203 C CG  . LEU   B 16  ? 0.2421 0.2366 0.2543 0.0135  -0.0304 -0.0155 22  LEU   C CG  
1204 C CD1 . LEU   B 16  ? 0.2554 0.2503 0.2631 0.0135  -0.0284 -0.0142 22  LEU   C CD1 
1205 C CD2 . LEU   B 16  ? 0.2525 0.2403 0.2570 0.0151  -0.0337 -0.0181 22  LEU   C CD2 
1206 N N   . ALA   B 17  ? 0.2305 0.2342 0.2756 0.0062  -0.0349 -0.0136 23  ALA   C N   
1207 C CA  . ALA   B 17  ? 0.2220 0.2297 0.2777 0.0036  -0.0351 -0.0131 23  ALA   C CA  
1208 C C   . ALA   B 17  ? 0.2242 0.2288 0.2846 0.0040  -0.0413 -0.0145 23  ALA   C C   
1209 O O   . ALA   B 17  ? 0.2201 0.2192 0.2761 0.0051  -0.0451 -0.0155 23  ALA   C O   
1210 C CB  . ALA   B 17  ? 0.2105 0.2212 0.2698 0.0001  -0.0322 -0.0110 23  ALA   C CB  
1211 N N   . THR   B 18  ? 0.2336 0.2415 0.3035 0.0032  -0.0426 -0.0150 24  THR   C N   
1212 C CA  . THR   B 18  ? 0.2447 0.2501 0.3209 0.0033  -0.0493 -0.0161 24  THR   C CA  
1213 C C   . THR   B 18  ? 0.2484 0.2565 0.3350 -0.0002 -0.0497 -0.0153 24  THR   C C   
1214 O O   . THR   B 18  ? 0.2303 0.2424 0.3188 -0.0029 -0.0443 -0.0136 24  THR   C O   
1215 C CB  . THR   B 18  ? 0.2702 0.2783 0.3542 0.0043  -0.0512 -0.0169 24  THR   C CB  
1216 O OG1 . THR   B 18  ? 0.2693 0.2855 0.3649 0.0020  -0.0456 -0.0165 24  THR   C OG1 
1217 C CG2 . THR   B 18  ? 0.2873 0.2918 0.3612 0.0072  -0.0516 -0.0170 24  THR   C CG2 
1218 N N   . HIS   B 19  ? 0.2571 0.2630 0.3507 -0.0007 -0.0562 -0.0162 25  HIS   C N   
1219 C CA  . HIS   B 19  ? 0.2625 0.2715 0.3679 -0.0045 -0.0566 -0.0152 25  HIS   C CA  
1220 C C   . HIS   B 19  ? 0.2454 0.2641 0.3627 -0.0074 -0.0499 -0.0143 25  HIS   C C   
1221 O O   . HIS   B 19  ? 0.2469 0.2695 0.3688 -0.0114 -0.0455 -0.0125 25  HIS   C O   
1222 C CB  . HIS   B 19  ? 0.3011 0.3067 0.4139 -0.0045 -0.0655 -0.0166 25  HIS   C CB  
1223 C CG  . HIS   B 19  ? 0.3983 0.3939 0.4998 -0.0026 -0.0718 -0.0181 25  HIS   C CG  
1224 N ND1 . HIS   B 19  ? 0.4516 0.4431 0.5467 -0.0032 -0.0707 -0.0177 25  HIS   C ND1 
1225 C CD2 . HIS   B 19  ? 0.4412 0.4298 0.5369 -0.0003 -0.0794 -0.0203 25  HIS   C CD2 
1226 C CE1 . HIS   B 19  ? 0.4645 0.4471 0.5509 -0.0010 -0.0769 -0.0202 25  HIS   C CE1 
1227 N NE2 . HIS   B 19  ? 0.4721 0.4524 0.5574 0.0006  -0.0822 -0.0218 25  HIS   C NE2 
1228 N N   . ASN   B 20  ? 0.2416 0.2638 0.3633 -0.0054 -0.0489 -0.0157 26  ASN   C N   
1229 C CA  . ASN   B 20  ? 0.2417 0.2729 0.3749 -0.0074 -0.0421 -0.0160 26  ASN   C CA  
1230 C C   . ASN   B 20  ? 0.2326 0.2662 0.3574 -0.0091 -0.0336 -0.0149 26  ASN   C C   
1231 O O   . ASN   B 20  ? 0.2305 0.2702 0.3617 -0.0131 -0.0273 -0.0144 26  ASN   C O   
1232 C CB  . ASN   B 20  ? 0.2753 0.3084 0.4160 -0.0042 -0.0441 -0.0181 26  ASN   C CB  
1233 C CG  . ASN   B 20  ? 0.3443 0.3870 0.5004 -0.0060 -0.0375 -0.0195 26  ASN   C CG  
1234 O OD1 . ASN   B 20  ? 0.3632 0.4113 0.5345 -0.0088 -0.0370 -0.0199 26  ASN   C OD1 
1235 N ND2 . ASN   B 20  ? 0.3654 0.4102 0.5184 -0.0046 -0.0319 -0.0207 26  ASN   C ND2 
1236 N N   . ASP   B 21  ? 0.2268 0.2557 0.3370 -0.0067 -0.0332 -0.0144 27  ASP   C N   
1237 C CA  . ASP   B 21  ? 0.2183 0.2486 0.3200 -0.0086 -0.0265 -0.0130 27  ASP   C CA  
1238 C C   . ASP   B 21  ? 0.2240 0.2542 0.3249 -0.0130 -0.0251 -0.0103 27  ASP   C C   
1239 O O   . ASP   B 21  ? 0.2384 0.2725 0.3392 -0.0169 -0.0190 -0.0091 27  ASP   C O   
1240 C CB  . ASP   B 21  ? 0.2101 0.2350 0.2978 -0.0053 -0.0276 -0.0126 27  ASP   C CB  
1241 C CG  . ASP   B 21  ? 0.2423 0.2671 0.3283 -0.0020 -0.0275 -0.0143 27  ASP   C CG  
1242 O OD1 . ASP   B 21  ? 0.2380 0.2679 0.3308 -0.0027 -0.0233 -0.0155 27  ASP   C OD1 
1243 O OD2 . ASP   B 21  ? 0.2512 0.2707 0.3288 0.0012  -0.0313 -0.0145 27  ASP   C OD2 
1244 N N   . TRP   B 22  ? 0.2171 0.2420 0.3168 -0.0127 -0.0310 -0.0094 28  TRP   C N   
1245 C CA  . TRP   B 22  ? 0.2325 0.2560 0.3319 -0.0168 -0.0309 -0.0065 28  TRP   C CA  
1246 C C   . TRP   B 22  ? 0.2396 0.2688 0.3514 -0.0219 -0.0283 -0.0056 28  TRP   C C   
1247 O O   . TRP   B 22  ? 0.2485 0.2785 0.3591 -0.0269 -0.0250 -0.0026 28  TRP   C O   
1248 C CB  . TRP   B 22  ? 0.2328 0.2484 0.3286 -0.0148 -0.0382 -0.0065 28  TRP   C CB  
1249 C CG  . TRP   B 22  ? 0.2330 0.2437 0.3166 -0.0116 -0.0385 -0.0064 28  TRP   C CG  
1250 C CD1 . TRP   B 22  ? 0.2463 0.2532 0.3229 -0.0067 -0.0407 -0.0088 28  TRP   C CD1 
1251 C CD2 . TRP   B 22  ? 0.2285 0.2376 0.3063 -0.0135 -0.0366 -0.0035 28  TRP   C CD2 
1252 N NE1 . TRP   B 22  ? 0.2578 0.2621 0.3259 -0.0053 -0.0394 -0.0080 28  TRP   C NE1 
1253 C CE2 . TRP   B 22  ? 0.2450 0.2502 0.3143 -0.0092 -0.0376 -0.0047 28  TRP   C CE2 
1254 C CE3 . TRP   B 22  ? 0.2318 0.2421 0.3108 -0.0187 -0.0343 0.0003  28  TRP   C CE3 
1255 C CZ2 . TRP   B 22  ? 0.2490 0.2523 0.3132 -0.0095 -0.0368 -0.0025 28  TRP   C CZ2 
1256 C CZ3 . TRP   B 22  ? 0.2473 0.2543 0.3193 -0.0193 -0.0345 0.0029  28  TRP   C CZ3 
1257 C CH2 . TRP   B 22  ? 0.2535 0.2576 0.3192 -0.0145 -0.0357 0.0014  28  TRP   C CH2 
1258 N N   . ALA   B 23  ? 0.2350 0.2679 0.3588 -0.0211 -0.0298 -0.0079 29  ALA   C N   
1259 C CA  . ALA   B 23  ? 0.2379 0.2774 0.3761 -0.0258 -0.0269 -0.0075 29  ALA   C CA  
1260 C C   . ALA   B 23  ? 0.2402 0.2876 0.3807 -0.0288 -0.0168 -0.0082 29  ALA   C C   
1261 O O   . ALA   B 23  ? 0.2438 0.2973 0.3941 -0.0338 -0.0119 -0.0076 29  ALA   C O   
1262 C CB  . ALA   B 23  ? 0.2272 0.2684 0.3793 -0.0236 -0.0325 -0.0101 29  ALA   C CB  
1263 N N   . ASN   B 24  ? 0.2235 0.2709 0.3560 -0.0256 -0.0138 -0.0098 30  ASN   C N   
1264 C CA  . ASN   B 24  ? 0.2130 0.2665 0.3454 -0.0278 -0.0046 -0.0113 30  ASN   C CA  
1265 C C   . ASN   B 24  ? 0.2123 0.2616 0.3270 -0.0286 -0.0020 -0.0092 30  ASN   C C   
1266 O O   . ASN   B 24  ? 0.2112 0.2621 0.3210 -0.0276 0.0027  -0.0111 30  ASN   C O   
1267 C CB  . ASN   B 24  ? 0.2239 0.2807 0.3646 -0.0232 -0.0042 -0.0155 30  ASN   C CB  
1268 C CG  . ASN   B 24  ? 0.2691 0.3313 0.4296 -0.0230 -0.0064 -0.0174 30  ASN   C CG  
1269 O OD1 . ASN   B 24  ? 0.2801 0.3498 0.4527 -0.0270 -0.0001 -0.0185 30  ASN   C OD1 
1270 N ND2 . ASN   B 24  ? 0.2636 0.3218 0.4281 -0.0189 -0.0155 -0.0179 30  ASN   C ND2 
1271 N N   . LEU   B 25  ? 0.2135 0.2572 0.3197 -0.0303 -0.0056 -0.0055 31  LEU   C N   
1272 C CA  . LEU   B 25  ? 0.2255 0.2647 0.3167 -0.0308 -0.0050 -0.0031 31  LEU   C CA  
1273 C C   . LEU   B 25  ? 0.2375 0.2798 0.3225 -0.0362 0.0028  -0.0021 31  LEU   C C   
1274 O O   . LEU   B 25  ? 0.2564 0.3017 0.3452 -0.0420 0.0068  -0.0007 31  LEU   C O   
1275 C CB  . LEU   B 25  ? 0.2345 0.2673 0.3214 -0.0317 -0.0110 0.0007  31  LEU   C CB  
1276 C CG  . LEU   B 25  ? 0.2495 0.2774 0.3234 -0.0322 -0.0120 0.0037  31  LEU   C CG  
1277 C CD1 . LEU   B 25  ? 0.2620 0.2880 0.3304 -0.0262 -0.0136 0.0015  31  LEU   C CD1 
1278 C CD2 . LEU   B 25  ? 0.2642 0.2859 0.3371 -0.0335 -0.0179 0.0074  31  LEU   C CD2 
1279 N N   . VAL   B 26  ? 0.2254 0.2665 0.3003 -0.0349 0.0049  -0.0027 32  VAL   C N   
1280 C CA  . VAL   B 26  ? 0.2347 0.2768 0.3001 -0.0400 0.0113  -0.0018 32  VAL   C CA  
1281 C C   . VAL   B 26  ? 0.2504 0.2861 0.3029 -0.0415 0.0072  0.0028  32  VAL   C C   
1282 O O   . VAL   B 26  ? 0.2624 0.2961 0.3078 -0.0476 0.0085  0.0066  32  VAL   C O   
1283 C CB  . VAL   B 26  ? 0.2382 0.2834 0.3027 -0.0378 0.0165  -0.0064 32  VAL   C CB  
1284 C CG1 . VAL   B 26  ? 0.2498 0.2941 0.3012 -0.0430 0.0219  -0.0056 32  VAL   C CG1 
1285 C CG2 . VAL   B 26  ? 0.2267 0.2787 0.3061 -0.0368 0.0209  -0.0110 32  VAL   C CG2 
1286 N N   . TRP   B 27  ? 0.2408 0.2728 0.2908 -0.0360 0.0018  0.0027  33  TRP   C N   
1287 C CA  . TRP   B 27  ? 0.2450 0.2716 0.2854 -0.0363 -0.0023 0.0064  33  TRP   C CA  
1288 C C   . TRP   B 27  ? 0.2438 0.2676 0.2864 -0.0297 -0.0080 0.0056  33  TRP   C C   
1289 O O   . TRP   B 27  ? 0.2498 0.2754 0.2959 -0.0252 -0.0075 0.0020  33  TRP   C O   
1290 C CB  . TRP   B 27  ? 0.2483 0.2752 0.2786 -0.0385 0.0014  0.0063  33  TRP   C CB  
1291 C CG  . TRP   B 27  ? 0.2632 0.2853 0.2852 -0.0380 -0.0033 0.0096  33  TRP   C CG  
1292 C CD1 . TRP   B 27  ? 0.2862 0.3041 0.3013 -0.0427 -0.0064 0.0147  33  TRP   C CD1 
1293 C CD2 . TRP   B 27  ? 0.2625 0.2838 0.2834 -0.0329 -0.0056 0.0083  33  TRP   C CD2 
1294 N NE1 . TRP   B 27  ? 0.2879 0.3028 0.2990 -0.0403 -0.0108 0.0163  33  TRP   C NE1 
1295 C CE2 . TRP   B 27  ? 0.2811 0.2985 0.2959 -0.0345 -0.0099 0.0123  33  TRP   C CE2 
1296 C CE3 . TRP   B 27  ? 0.2632 0.2867 0.2876 -0.0277 -0.0044 0.0043  33  TRP   C CE3 
1297 C CZ2 . TRP   B 27  ? 0.2867 0.3033 0.3002 -0.0308 -0.0123 0.0121  33  TRP   C CZ2 
1298 C CZ3 . TRP   B 27  ? 0.2785 0.3006 0.3002 -0.0244 -0.0068 0.0045  33  TRP   C CZ3 
1299 C CH2 . TRP   B 27  ? 0.2797 0.2989 0.2967 -0.0259 -0.0103 0.0081  33  TRP   C CH2 
1300 N N   . GLU   B 28  ? 0.2386 0.2576 0.2789 -0.0292 -0.0133 0.0087  34  GLU   C N   
1301 C CA  . GLU   B 28  ? 0.2254 0.2417 0.2667 -0.0232 -0.0176 0.0074  34  GLU   C CA  
1302 C C   . GLU   B 28  ? 0.2245 0.2369 0.2611 -0.0235 -0.0212 0.0108  34  GLU   C C   
1303 O O   . GLU   B 28  ? 0.2172 0.2271 0.2513 -0.0283 -0.0228 0.0149  34  GLU   C O   
1304 C CB  . GLU   B 28  ? 0.2302 0.2447 0.2786 -0.0200 -0.0213 0.0055  34  GLU   C CB  
1305 C CG  . GLU   B 28  ? 0.2520 0.2637 0.3042 -0.0235 -0.0244 0.0083  34  GLU   C CG  
1306 C CD  . GLU   B 28  ? 0.2771 0.2830 0.3275 -0.0234 -0.0295 0.0115  34  GLU   C CD  
1307 O OE1 . GLU   B 28  ? 0.3010 0.3044 0.3519 -0.0282 -0.0313 0.0154  34  GLU   C OE1 
1308 O OE2 . GLU   B 28  ? 0.2479 0.2517 0.2969 -0.0188 -0.0317 0.0102  34  GLU   C OE2 
1309 N N   . ASP   B 29  ? 0.2072 0.2190 0.2431 -0.0188 -0.0226 0.0094  35  ASP   C N   
1310 C CA  . ASP   B 29  ? 0.2133 0.2220 0.2476 -0.0185 -0.0264 0.0122  35  ASP   C CA  
1311 C C   . ASP   B 29  ? 0.2168 0.2246 0.2550 -0.0121 -0.0282 0.0093  35  ASP   C C   
1312 O O   . ASP   B 29  ? 0.2126 0.2228 0.2493 -0.0091 -0.0257 0.0068  35  ASP   C O   
1313 C CB  . ASP   B 29  ? 0.2416 0.2519 0.2696 -0.0212 -0.0246 0.0140  35  ASP   C CB  
1314 C CG  . ASP   B 29  ? 0.2869 0.2943 0.3143 -0.0218 -0.0293 0.0177  35  ASP   C CG  
1315 O OD1 . ASP   B 29  ? 0.3020 0.3074 0.3354 -0.0179 -0.0329 0.0174  35  ASP   C OD1 
1316 O OD2 . ASP   B 29  ? 0.3236 0.3307 0.3449 -0.0261 -0.0295 0.0206  35  ASP   C OD2 
1317 N N   . SER   B 30  ? 0.1989 0.2026 0.2417 -0.0102 -0.0325 0.0095  36  SER   C N   
1318 C CA  A SER   B 30  ? 0.2049 0.2070 0.2509 -0.0045 -0.0337 0.0061  36  SER   C CA  
1319 C CA  B SER   B 30  ? 0.2060 0.2083 0.2519 -0.0044 -0.0336 0.0060  36  SER   C CA  
1320 C C   . SER   B 30  ? 0.2162 0.2200 0.2623 -0.0023 -0.0331 0.0064  36  SER   C C   
1321 O O   . SER   B 30  ? 0.2316 0.2368 0.2777 0.0018  -0.0308 0.0030  36  SER   C O   
1322 C CB  A SER   B 30  ? 0.2128 0.2096 0.2640 -0.0035 -0.0386 0.0062  36  SER   C CB  
1323 C CB  B SER   B 30  ? 0.2180 0.2149 0.2691 -0.0032 -0.0384 0.0059  36  SER   C CB  
1324 O OG  A SER   B 30  ? 0.2324 0.2272 0.2865 0.0020  -0.0394 0.0025  36  SER   C OG  
1325 O OG  B SER   B 30  ? 0.2427 0.2370 0.2963 -0.0054 -0.0423 0.0101  36  SER   C OG  
1326 N N   . SER   B 31  ? 0.2061 0.2098 0.2521 -0.0056 -0.0352 0.0106  37  SER   C N   
1327 C CA  . SER   B 31  ? 0.2114 0.2172 0.2593 -0.0039 -0.0355 0.0113  37  SER   C CA  
1328 C C   . SER   B 31  ? 0.2112 0.2216 0.2545 -0.0036 -0.0304 0.0095  37  SER   C C   
1329 O O   . SER   B 31  ? 0.2195 0.2322 0.2654 -0.0013 -0.0296 0.0089  37  SER   C O   
1330 C CB  . SER   B 31  ? 0.2423 0.2460 0.2907 -0.0079 -0.0402 0.0166  37  SER   C CB  
1331 O OG  . SER   B 31  ? 0.2988 0.3040 0.3391 -0.0131 -0.0385 0.0191  37  SER   C OG  
1332 N N   . ARG   B 32  ? 0.1930 0.2048 0.2307 -0.0060 -0.0272 0.0088  38  ARG   C N   
1333 C CA  . ARG   B 32  ? 0.1941 0.2093 0.2279 -0.0057 -0.0230 0.0071  38  ARG   C CA  
1334 C C   . ARG   B 32  ? 0.1929 0.2087 0.2262 -0.0022 -0.0202 0.0031  38  ARG   C C   
1335 O O   . ARG   B 32  ? 0.1948 0.2126 0.2253 -0.0016 -0.0172 0.0018  38  ARG   C O   
1336 C CB  . ARG   B 32  ? 0.2102 0.2263 0.2383 -0.0107 -0.0212 0.0086  38  ARG   C CB  
1337 C CG  . ARG   B 32  ? 0.2044 0.2193 0.2297 -0.0152 -0.0239 0.0127  38  ARG   C CG  
1338 C CD  . ARG   B 32  ? 0.2116 0.2268 0.2294 -0.0206 -0.0213 0.0135  38  ARG   C CD  
1339 N NE  . ARG   B 32  ? 0.1964 0.2142 0.2112 -0.0201 -0.0172 0.0108  38  ARG   C NE  
1340 C CZ  . ARG   B 32  ? 0.2236 0.2414 0.2315 -0.0243 -0.0154 0.0111  38  ARG   C CZ  
1341 N NH1 . ARG   B 32  ? 0.2117 0.2270 0.2135 -0.0298 -0.0170 0.0142  38  ARG   C NH1 
1342 N NH2 . ARG   B 32  ? 0.2336 0.2531 0.2399 -0.0234 -0.0122 0.0083  38  ARG   C NH2 
1343 N N   . ASP   B 33  ? 0.1927 0.2059 0.2281 -0.0004 -0.0218 0.0015  39  ASP   C N   
1344 C CA  . ASP   B 33  ? 0.1828 0.1953 0.2170 0.0022  -0.0207 -0.0018 39  ASP   C CA  
1345 C C   . ASP   B 33  ? 0.2015 0.2160 0.2339 -0.0001 -0.0186 -0.0021 39  ASP   C C   
1346 O O   . ASP   B 33  ? 0.2068 0.2216 0.2373 0.0018  -0.0172 -0.0041 39  ASP   C O   
1347 C CB  . ASP   B 33  ? 0.1838 0.1963 0.2160 0.0061  -0.0189 -0.0042 39  ASP   C CB  
1348 C CG  . ASP   B 33  ? 0.2060 0.2164 0.2348 0.0082  -0.0187 -0.0072 39  ASP   C CG  
1349 O OD1 . ASP   B 33  ? 0.1896 0.1973 0.2198 0.0085  -0.0214 -0.0083 39  ASP   C OD1 
1350 O OD2 . ASP   B 33  ? 0.2154 0.2266 0.2401 0.0093  -0.0164 -0.0080 39  ASP   C OD2 
1351 N N   . LEU   B 34  ? 0.1947 0.2103 0.2278 -0.0042 -0.0182 -0.0001 40  LEU   C N   
1352 C CA  . LEU   B 34  ? 0.2017 0.2198 0.2347 -0.0062 -0.0154 -0.0011 40  LEU   C CA  
1353 C C   . LEU   B 34  ? 0.2076 0.2258 0.2447 -0.0087 -0.0160 -0.0010 40  LEU   C C   
1354 O O   . LEU   B 34  ? 0.2082 0.2249 0.2461 -0.0113 -0.0178 0.0015  40  LEU   C O   
1355 C CB  . LEU   B 34  ? 0.1972 0.2174 0.2264 -0.0098 -0.0124 0.0002  40  LEU   C CB  
1356 C CG  . LEU   B 34  ? 0.2097 0.2307 0.2356 -0.0084 -0.0111 -0.0002 40  LEU   C CG  
1357 C CD1 . LEU   B 34  ? 0.2059 0.2280 0.2274 -0.0127 -0.0089 0.0010  40  LEU   C CD1 
1358 C CD2 . LEU   B 34  ? 0.2311 0.2525 0.2578 -0.0052 -0.0098 -0.0030 40  LEU   C CD2 
1359 N N   . LEU   B 35  ? 0.1969 0.2172 0.2376 -0.0084 -0.0143 -0.0033 41  LEU   C N   
1360 C CA  . LEU   B 35  ? 0.1984 0.2203 0.2449 -0.0111 -0.0139 -0.0034 41  LEU   C CA  
1361 C C   . LEU   B 35  ? 0.1894 0.2155 0.2389 -0.0122 -0.0095 -0.0056 41  LEU   C C   
1362 O O   . LEU   B 35  ? 0.1872 0.2136 0.2367 -0.0091 -0.0091 -0.0077 41  LEU   C O   
1363 C CB  . LEU   B 35  ? 0.2005 0.2201 0.2521 -0.0085 -0.0183 -0.0047 41  LEU   C CB  
1364 C CG  . LEU   B 35  ? 0.2064 0.2278 0.2661 -0.0115 -0.0186 -0.0046 41  LEU   C CG  
1365 C CD1 . LEU   B 35  ? 0.2124 0.2295 0.2746 -0.0108 -0.0240 -0.0041 41  LEU   C CD1 
1366 C CD2 . LEU   B 35  ? 0.2121 0.2370 0.2790 -0.0103 -0.0175 -0.0075 41  LEU   C CD2 
1367 N N   . VAL   B 36  ? 0.1875 0.2167 0.2398 -0.0166 -0.0059 -0.0052 42  VAL   C N   
1368 C CA  . VAL   B 36  ? 0.1884 0.2220 0.2452 -0.0177 -0.0009 -0.0081 42  VAL   C CA  
1369 C C   . VAL   B 36  ? 0.2006 0.2375 0.2681 -0.0195 -0.0003 -0.0089 42  VAL   C C   
1370 O O   . VAL   B 36  ? 0.1958 0.2323 0.2634 -0.0234 -0.0005 -0.0064 42  VAL   C O   
1371 C CB  . VAL   B 36  ? 0.1900 0.2249 0.2395 -0.0221 0.0046  -0.0077 42  VAL   C CB  
1372 C CG1 . VAL   B 36  ? 0.1890 0.2287 0.2445 -0.0232 0.0107  -0.0118 42  VAL   C CG1 
1373 C CG2 . VAL   B 36  ? 0.1880 0.2200 0.2284 -0.0205 0.0034  -0.0069 42  VAL   C CG2 
1374 N N   . SER   B 37  ? 0.2052 0.2448 0.2824 -0.0168 -0.0002 -0.0122 43  SER   C N   
1375 C CA  . SER   B 37  ? 0.2057 0.2495 0.2960 -0.0183 0.0004  -0.0134 43  SER   C CA  
1376 C C   . SER   B 37  ? 0.2283 0.2783 0.3270 -0.0192 0.0071  -0.0173 43  SER   C C   
1377 O O   . SER   B 37  ? 0.2315 0.2812 0.3264 -0.0173 0.0095  -0.0193 43  SER   C O   
1378 C CB  . SER   B 37  ? 0.2184 0.2600 0.3155 -0.0143 -0.0069 -0.0140 43  SER   C CB  
1379 O OG  . SER   B 37  ? 0.2449 0.2853 0.3427 -0.0096 -0.0090 -0.0162 43  SER   C OG  
1380 N N   . SER   B 38  ? 0.2386 0.2941 0.3494 -0.0221 0.0104  -0.0185 44  SER   C N   
1381 C CA  . SER   B 38  ? 0.2510 0.3130 0.3717 -0.0229 0.0176  -0.0228 44  SER   C CA  
1382 C C   . SER   B 38  ? 0.2658 0.3299 0.4018 -0.0177 0.0136  -0.0260 44  SER   C C   
1383 O O   . SER   B 38  ? 0.2644 0.3269 0.4068 -0.0157 0.0063  -0.0246 44  SER   C O   
1384 C CB  . SER   B 38  ? 0.2684 0.3362 0.3953 -0.0291 0.0242  -0.0227 44  SER   C CB  
1385 O OG  . SER   B 38  ? 0.3054 0.3740 0.4424 -0.0296 0.0192  -0.0207 44  SER   C OG  
1386 N N   . THR   B 39  ? 0.2738 0.3408 0.4157 -0.0158 0.0179  -0.0302 45  THR   C N   
1387 C CA  . THR   B 39  ? 0.3011 0.3698 0.4585 -0.0109 0.0140  -0.0332 45  THR   C CA  
1388 C C   . THR   B 39  ? 0.3292 0.4067 0.5043 -0.0123 0.0220  -0.0382 45  THR   C C   
1389 O O   . THR   B 39  ? 0.3324 0.4132 0.5032 -0.0164 0.0315  -0.0401 45  THR   C O   
1390 C CB  . THR   B 39  ? 0.3220 0.3852 0.4719 -0.0064 0.0112  -0.0341 45  THR   C CB  
1391 O OG1 . THR   B 39  ? 0.3523 0.4173 0.4981 -0.0081 0.0196  -0.0373 45  THR   C OG1 
1392 C CG2 . THR   B 39  ? 0.3268 0.3823 0.4594 -0.0053 0.0053  -0.0298 45  THR   C CG2 
1393 N N   . THR   B 40  ? 0.3399 0.4206 0.5344 -0.0087 0.0181  -0.0406 46  THR   C N   
1394 C CA  . THR   B 40  ? 0.3566 0.4462 0.5713 -0.0089 0.0254  -0.0462 46  THR   C CA  
1395 C C   . THR   B 40  ? 0.3707 0.4587 0.5872 -0.0047 0.0274  -0.0506 46  THR   C C   
1396 O O   . THR   B 40  ? 0.3809 0.4748 0.6062 -0.0057 0.0368  -0.0560 46  THR   C O   
1397 C CB  . THR   B 40  ? 0.3821 0.4766 0.6197 -0.0073 0.0197  -0.0465 46  THR   C CB  
1398 O OG1 . THR   B 40  ? 0.4158 0.5032 0.6530 -0.0022 0.0073  -0.0442 46  THR   C OG1 
1399 C CG2 . THR   B 40  ? 0.3854 0.4825 0.6236 -0.0124 0.0197  -0.0430 46  THR   C CG2 
1400 N N   . ALA   B 41  ? 0.3662 0.4461 0.5744 -0.0003 0.0188  -0.0485 47  ALA   C N   
1401 C CA  . ALA   B 41  ? 0.3642 0.4412 0.5736 0.0036  0.0192  -0.0519 47  ALA   C CA  
1402 C C   . ALA   B 41  ? 0.3766 0.4493 0.5650 0.0014  0.0248  -0.0518 47  ALA   C C   
1403 O O   . ALA   B 41  ? 0.3876 0.4563 0.5579 -0.0012 0.0234  -0.0473 47  ALA   C O   
1404 C CB  . ALA   B 41  ? 0.3638 0.4338 0.5745 0.0087  0.0071  -0.0491 47  ALA   C CB  
1405 N N   . GLN   B 42  ? 0.3687 0.4419 0.5603 0.0026  0.0305  -0.0570 48  GLN   C N   
1406 C CA  . GLN   B 42  ? 0.3723 0.4412 0.5456 0.0006  0.0354  -0.0577 48  GLN   C CA  
1407 C C   . GLN   B 42  ? 0.3492 0.4090 0.5093 0.0034  0.0269  -0.0535 48  GLN   C C   
1408 O O   . GLN   B 42  ? 0.3569 0.4134 0.5255 0.0081  0.0204  -0.0537 48  GLN   C O   
1409 C CB  . GLN   B 42  ? 0.4171 0.4889 0.5998 0.0014  0.0436  -0.0655 48  GLN   C CB  
1410 C CG  . GLN   B 42  ? 0.5107 0.5776 0.6747 -0.0011 0.0488  -0.0671 48  GLN   C CG  
1411 C CD  . GLN   B 42  ? 0.6145 0.6841 0.7645 -0.0079 0.0572  -0.0669 48  GLN   C CD  
1412 O OE1 . GLN   B 42  ? 0.6463 0.7222 0.8021 -0.0112 0.0615  -0.0666 48  GLN   C OE1 
1413 N NE2 . GLN   B 42  ? 0.6355 0.6997 0.7665 -0.0106 0.0596  -0.0669 48  GLN   C NE2 
1414 N N   . GLY   B 43  ? 0.3176 0.3735 0.4577 0.0004  0.0272  -0.0498 49  GLY   C N   
1415 C CA  . GLY   B 43  ? 0.3082 0.3563 0.4347 0.0021  0.0208  -0.0457 49  GLY   C CA  
1416 C C   . GLY   B 43  ? 0.3033 0.3482 0.4224 0.0017  0.0247  -0.0487 49  GLY   C C   
1417 O O   . GLY   B 43  ? 0.3113 0.3587 0.4266 -0.0018 0.0328  -0.0522 49  GLY   C O   
1418 N N   . CYS   B 44  ? 0.2880 0.3267 0.4050 0.0050  0.0191  -0.0474 50  CYS   C N   
1419 C CA  . CYS   B 44  ? 0.2926 0.3277 0.4046 0.0047  0.0221  -0.0506 50  CYS   C CA  
1420 C C   . CYS   B 44  ? 0.2864 0.3155 0.3810 0.0032  0.0192  -0.0462 50  CYS   C C   
1421 O O   . CYS   B 44  ? 0.2894 0.3143 0.3807 0.0035  0.0198  -0.0482 50  CYS   C O   
1422 C CB  . CYS   B 44  ? 0.3135 0.3464 0.4403 0.0093  0.0196  -0.0543 50  CYS   C CB  
1423 S SG  . CYS   B 44  ? 0.3981 0.4391 0.5491 0.0113  0.0240  -0.0607 50  CYS   C SG  
1424 N N   . ASP   B 45  ? 0.2641 0.2929 0.3486 0.0017  0.0161  -0.0406 51  ASP   C N   
1425 C CA  . ASP   B 45  ? 0.2722 0.2966 0.3423 0.0002  0.0141  -0.0368 51  ASP   C CA  
1426 C C   . ASP   B 45  ? 0.2776 0.3027 0.3380 -0.0043 0.0199  -0.0387 51  ASP   C C   
1427 O O   . ASP   B 45  ? 0.2728 0.3020 0.3334 -0.0072 0.0251  -0.0409 51  ASP   C O   
1428 C CB  . ASP   B 45  ? 0.2806 0.3047 0.3440 0.0001  0.0096  -0.0310 51  ASP   C CB  
1429 C CG  . ASP   B 45  ? 0.3371 0.3589 0.4059 0.0039  0.0032  -0.0287 51  ASP   C CG  
1430 O OD1 . ASP   B 45  ? 0.3502 0.3691 0.4254 0.0066  0.0006  -0.0300 51  ASP   C OD1 
1431 O OD2 . ASP   B 45  ? 0.3270 0.3494 0.3933 0.0041  0.0003  -0.0257 51  ASP   C OD2 
1432 N N   . THR   B 46  ? 0.2779 0.2988 0.3298 -0.0054 0.0189  -0.0379 52  THR   C N   
1433 C CA  . THR   B 46  ? 0.2806 0.3007 0.3217 -0.0099 0.0228  -0.0392 52  THR   C CA  
1434 C C   . THR   B 46  ? 0.2590 0.2783 0.2898 -0.0118 0.0192  -0.0332 52  THR   C C   
1435 O O   . THR   B 46  ? 0.2622 0.2791 0.2922 -0.0098 0.0146  -0.0296 52  THR   C O   
1436 C CB  . THR   B 46  ? 0.3180 0.3330 0.3574 -0.0096 0.0230  -0.0423 52  THR   C CB  
1437 O OG1 . THR   B 46  ? 0.3460 0.3618 0.3959 -0.0078 0.0269  -0.0488 52  THR   C OG1 
1438 C CG2 . THR   B 46  ? 0.3309 0.3436 0.3568 -0.0146 0.0248  -0.0426 52  THR   C CG2 
1439 N N   . ILE   B 47  ? 0.2390 0.2602 0.2624 -0.0159 0.0215  -0.0320 53  ILE   C N   
1440 C CA  . ILE   B 47  ? 0.2348 0.2553 0.2500 -0.0178 0.0178  -0.0266 53  ILE   C CA  
1441 C C   . ILE   B 47  ? 0.2359 0.2528 0.2418 -0.0209 0.0172  -0.0265 53  ILE   C C   
1442 O O   . ILE   B 47  ? 0.2446 0.2602 0.2455 -0.0241 0.0210  -0.0303 53  ILE   C O   
1443 C CB  . ILE   B 47  ? 0.2464 0.2696 0.2582 -0.0210 0.0192  -0.0246 53  ILE   C CB  
1444 C CG1 . ILE   B 47  ? 0.2614 0.2882 0.2831 -0.0186 0.0200  -0.0252 53  ILE   C CG1 
1445 C CG2 . ILE   B 47  ? 0.2480 0.2702 0.2536 -0.0222 0.0145  -0.0189 53  ILE   C CG2 
1446 C CD1 . ILE   B 47  ? 0.2774 0.3038 0.3053 -0.0137 0.0147  -0.0226 53  ILE   C CD1 
1447 N N   . ALA   B 48  ? 0.2146 0.2300 0.2183 -0.0202 0.0127  -0.0224 54  ALA   C N   
1448 C CA  . ALA   B 48  ? 0.2139 0.2263 0.2099 -0.0234 0.0111  -0.0217 54  ALA   C CA  
1449 C C   . ALA   B 48  ? 0.2124 0.2249 0.1995 -0.0284 0.0110  -0.0198 54  ALA   C C   
1450 O O   . ALA   B 48  ? 0.2064 0.2212 0.1940 -0.0284 0.0098  -0.0166 54  ALA   C O   
1451 C CB  . ALA   B 48  ? 0.2101 0.2220 0.2081 -0.0216 0.0067  -0.0175 54  ALA   C CB  
1452 N N   . ARG   B 49  ? 0.2043 0.2135 0.1826 -0.0327 0.0114  -0.0216 55  ARG   C N   
1453 C CA  . ARG   B 49  ? 0.1993 0.2070 0.1668 -0.0382 0.0101  -0.0193 55  ARG   C CA  
1454 C C   . ARG   B 49  ? 0.2071 0.2114 0.1703 -0.0402 0.0053  -0.0177 55  ARG   C C   
1455 O O   . ARG   B 49  ? 0.2214 0.2217 0.1782 -0.0429 0.0065  -0.0214 55  ARG   C O   
1456 C CB  . ARG   B 49  ? 0.2104 0.2167 0.1700 -0.0422 0.0160  -0.0241 55  ARG   C CB  
1457 C CG  . ARG   B 49  ? 0.2207 0.2311 0.1869 -0.0404 0.0212  -0.0262 55  ARG   C CG  
1458 C CD  . ARG   B 49  ? 0.2362 0.2496 0.2050 -0.0401 0.0187  -0.0208 55  ARG   C CD  
1459 N NE  . ARG   B 49  ? 0.2446 0.2620 0.2208 -0.0386 0.0236  -0.0232 55  ARG   C NE  
1460 C CZ  . ARG   B 49  ? 0.2653 0.2857 0.2480 -0.0367 0.0220  -0.0200 55  ARG   C CZ  
1461 N NH1 . ARG   B 49  ? 0.2171 0.2368 0.1995 -0.0359 0.0160  -0.0145 55  ARG   C NH1 
1462 N NH2 . ARG   B 49  ? 0.2959 0.3199 0.2860 -0.0358 0.0263  -0.0224 55  ARG   C NH2 
1463 N N   . CYS   B 50  ? 0.2062 0.2122 0.1740 -0.0387 0.0001  -0.0124 56  CYS   C N   
1464 C CA  . CYS   B 50  ? 0.2104 0.2147 0.1782 -0.0399 -0.0044 -0.0105 56  CYS   C CA  
1465 C C   . CYS   B 50  ? 0.2277 0.2350 0.2008 -0.0390 -0.0095 -0.0046 56  CYS   C C   
1466 O O   . CYS   B 50  ? 0.2211 0.2313 0.1979 -0.0369 -0.0094 -0.0024 56  CYS   C O   
1467 C CB  . CYS   B 50  ? 0.2090 0.2131 0.1840 -0.0362 -0.0028 -0.0129 56  CYS   C CB  
1468 S SG  . CYS   B 50  ? 0.2265 0.2353 0.2132 -0.0299 -0.0023 -0.0103 56  CYS   C SG  
1469 N N   . ASP   B 51  ? 0.2311 0.2380 0.2065 -0.0402 -0.0138 -0.0024 57  ASP   C N   
1470 C CA  . ASP   B 51  ? 0.2480 0.2586 0.2315 -0.0387 -0.0180 0.0025  57  ASP   C CA  
1471 C C   . ASP   B 51  ? 0.2287 0.2419 0.2216 -0.0355 -0.0172 0.0029  57  ASP   C C   
1472 O O   . ASP   B 51  ? 0.2252 0.2409 0.2246 -0.0358 -0.0206 0.0061  57  ASP   C O   
1473 C CB  . ASP   B 51  ? 0.2687 0.2777 0.2486 -0.0434 -0.0245 0.0058  57  ASP   C CB  
1474 C CG  . ASP   B 51  ? 0.3491 0.3544 0.3249 -0.0473 -0.0272 0.0047  57  ASP   C CG  
1475 O OD1 . ASP   B 51  ? 0.3426 0.3462 0.3180 -0.0464 -0.0237 0.0010  57  ASP   C OD1 
1476 O OD2 . ASP   B 51  ? 0.4192 0.4228 0.3926 -0.0512 -0.0335 0.0076  57  ASP   C OD2 
1477 N N   . CYS   B 52  ? 0.2136 0.2260 0.2076 -0.0327 -0.0129 -0.0001 58  CYS   C N   
1478 C CA  . CYS   B 52  ? 0.1981 0.2119 0.1991 -0.0301 -0.0119 0.0006  58  CYS   C CA  
1479 C C   . CYS   B 52  ? 0.1859 0.2048 0.1947 -0.0273 -0.0122 0.0041  58  CYS   C C   
1480 O O   . CYS   B 52  ? 0.1881 0.2090 0.1975 -0.0254 -0.0118 0.0047  58  CYS   C O   
1481 C CB  . CYS   B 52  ? 0.2066 0.2181 0.2073 -0.0273 -0.0081 -0.0026 58  CYS   C CB  
1482 S SG  . CYS   B 52  ? 0.2507 0.2560 0.2461 -0.0297 -0.0073 -0.0074 58  CYS   C SG  
1483 N N   . GLN   B 53  ? 0.1785 0.1993 0.1934 -0.0272 -0.0127 0.0061  59  GLN   C N   
1484 C CA  . GLN   B 53  ? 0.1799 0.2058 0.2025 -0.0245 -0.0115 0.0086  59  GLN   C CA  
1485 C C   . GLN   B 53  ? 0.1971 0.2228 0.2217 -0.0228 -0.0082 0.0087  59  GLN   C C   
1486 O O   . GLN   B 53  ? 0.1982 0.2280 0.2289 -0.0217 -0.0066 0.0108  59  GLN   C O   
1487 C CB  . GLN   B 53  ? 0.1715 0.2014 0.2015 -0.0264 -0.0150 0.0116  59  GLN   C CB  
1488 C CG  . GLN   B 53  ? 0.1598 0.1907 0.1899 -0.0267 -0.0184 0.0126  59  GLN   C CG  
1489 C CD  . GLN   B 53  ? 0.2317 0.2667 0.2716 -0.0282 -0.0225 0.0157  59  GLN   C CD  
1490 O OE1 . GLN   B 53  ? 0.2444 0.2774 0.2826 -0.0322 -0.0277 0.0169  59  GLN   C OE1 
1491 N NE2 . GLN   B 53  ? 0.2025 0.2430 0.2528 -0.0251 -0.0202 0.0167  59  GLN   C NE2 
1492 N N   . THR   B 54  ? 0.2096 0.2304 0.2293 -0.0230 -0.0072 0.0067  60  THR   C N   
1493 C CA  . THR   B 54  ? 0.2191 0.2381 0.2391 -0.0216 -0.0049 0.0073  60  THR   C CA  
1494 C C   . THR   B 54  ? 0.2220 0.2369 0.2373 -0.0192 -0.0040 0.0045  60  THR   C C   
1495 O O   . THR   B 54  ? 0.2307 0.2433 0.2431 -0.0198 -0.0047 0.0016  60  THR   C O   
1496 C CB  . THR   B 54  ? 0.2705 0.2869 0.2920 -0.0248 -0.0060 0.0085  60  THR   C CB  
1497 O OG1 . THR   B 54  ? 0.3120 0.3233 0.3293 -0.0265 -0.0078 0.0055  60  THR   C OG1 
1498 C CG2 . THR   B 54  ? 0.2703 0.2914 0.2983 -0.0277 -0.0075 0.0112  60  THR   C CG2 
1499 N N   . GLY   B 55  ? 0.2128 0.2268 0.2276 -0.0166 -0.0024 0.0052  61  GLY   C N   
1500 C CA  . GLY   B 55  ? 0.2025 0.2128 0.2147 -0.0141 -0.0023 0.0029  61  GLY   C CA  
1501 C C   . GLY   B 55  ? 0.2002 0.2086 0.2108 -0.0121 -0.0017 0.0047  61  GLY   C C   
1502 O O   . GLY   B 55  ? 0.2047 0.2139 0.2153 -0.0132 -0.0006 0.0076  61  GLY   C O   
1503 N N   . VAL   B 56  ? 0.2034 0.2091 0.2127 -0.0095 -0.0025 0.0031  62  VAL   C N   
1504 C CA  . VAL   B 56  ? 0.2122 0.2145 0.2182 -0.0078 -0.0031 0.0048  62  VAL   C CA  
1505 C C   . VAL   B 56  ? 0.1991 0.2026 0.2044 -0.0049 -0.0034 0.0033  62  VAL   C C   
1506 O O   . VAL   B 56  ? 0.1855 0.1895 0.1937 -0.0039 -0.0042 0.0005  62  VAL   C O   
1507 C CB  . VAL   B 56  ? 0.2303 0.2260 0.2365 -0.0078 -0.0057 0.0047  62  VAL   C CB  
1508 C CG1 . VAL   B 56  ? 0.2427 0.2338 0.2446 -0.0064 -0.0076 0.0071  62  VAL   C CG1 
1509 C CG2 . VAL   B 56  ? 0.2388 0.2325 0.2462 -0.0109 -0.0058 0.0061  62  VAL   C CG2 
1510 N N   . TYR   B 57  ? 0.1938 0.1975 0.1951 -0.0038 -0.0027 0.0048  63  TYR   C N   
1511 C CA  . TYR   B 57  ? 0.1982 0.2019 0.1984 -0.0012 -0.0038 0.0032  63  TYR   C CA  
1512 C C   . TYR   B 57  ? 0.2119 0.2101 0.2065 0.0000  -0.0062 0.0045  63  TYR   C C   
1513 O O   . TYR   B 57  ? 0.2096 0.2048 0.1990 -0.0015 -0.0057 0.0072  63  TYR   C O   
1514 C CB  . TYR   B 57  ? 0.1849 0.1935 0.1855 -0.0005 -0.0016 0.0028  63  TYR   C CB  
1515 C CG  . TYR   B 57  ? 0.2001 0.2087 0.1958 -0.0006 0.0008  0.0044  63  TYR   C CG  
1516 C CD1 . TYR   B 57  ? 0.2134 0.2244 0.2100 -0.0028 0.0038  0.0064  63  TYR   C CD1 
1517 C CD2 . TYR   B 57  ? 0.2170 0.2237 0.2076 0.0013  0.0006  0.0036  63  TYR   C CD2 
1518 C CE1 . TYR   B 57  ? 0.2356 0.2477 0.2287 -0.0030 0.0073  0.0074  63  TYR   C CE1 
1519 C CE2 . TYR   B 57  ? 0.2336 0.2403 0.2189 0.0011  0.0039  0.0043  63  TYR   C CE2 
1520 C CZ  . TYR   B 57  ? 0.2537 0.2635 0.2405 -0.0011 0.0077  0.0061  63  TYR   C CZ  
1521 O OH  . TYR   B 57  ? 0.2685 0.2790 0.2506 -0.0015 0.0121  0.0063  63  TYR   C OH  
1522 N N   . TYR   B 58  ? 0.2168 0.2134 0.2119 0.0022  -0.0090 0.0028  64  TYR   C N   
1523 C CA  . TYR   B 58  ? 0.2173 0.2080 0.2063 0.0031  -0.0125 0.0040  64  TYR   C CA  
1524 C C   . TYR   B 58  ? 0.2200 0.2112 0.2022 0.0037  -0.0110 0.0039  64  TYR   C C   
1525 O O   . TYR   B 58  ? 0.2271 0.2220 0.2125 0.0050  -0.0102 0.0016  64  TYR   C O   
1526 C CB  . TYR   B 58  ? 0.2242 0.2127 0.2186 0.0051  -0.0172 0.0022  64  TYR   C CB  
1527 C CG  . TYR   B 58  ? 0.2543 0.2358 0.2420 0.0057  -0.0222 0.0040  64  TYR   C CG  
1528 C CD1 . TYR   B 58  ? 0.2727 0.2479 0.2550 0.0043  -0.0246 0.0074  64  TYR   C CD1 
1529 C CD2 . TYR   B 58  ? 0.2788 0.2593 0.2648 0.0073  -0.0250 0.0028  64  TYR   C CD2 
1530 C CE1 . TYR   B 58  ? 0.2926 0.2602 0.2669 0.0043  -0.0300 0.0096  64  TYR   C CE1 
1531 C CE2 . TYR   B 58  ? 0.2968 0.2700 0.2751 0.0075  -0.0304 0.0046  64  TYR   C CE2 
1532 C CZ  . TYR   B 58  ? 0.3142 0.2808 0.2863 0.0059  -0.0331 0.0081  64  TYR   C CZ  
1533 O OH  . TYR   B 58  ? 0.3534 0.3119 0.3164 0.0055  -0.0391 0.0104  64  TYR   C OH  
1534 N N   . CYS   B 59  ? 0.2239 0.2108 0.1962 0.0025  -0.0104 0.0062  65  CYS   C N   
1535 C CA  . CYS   B 59  ? 0.2177 0.2038 0.1814 0.0028  -0.0084 0.0056  65  CYS   C CA  
1536 C C   . CYS   B 59  ? 0.2332 0.2112 0.1876 0.0032  -0.0137 0.0063  65  CYS   C C   
1537 O O   . CYS   B 59  ? 0.2439 0.2160 0.1895 0.0011  -0.0151 0.0094  65  CYS   C O   
1538 C CB  . CYS   B 59  ? 0.2193 0.2070 0.1781 0.0004  -0.0027 0.0075  65  CYS   C CB  
1539 S SG  . CYS   B 59  ? 0.2628 0.2497 0.2108 0.0006  0.0015  0.0058  65  CYS   C SG  
1540 N N   . SER   B 60  ? 0.2395 0.2169 0.1957 0.0054  -0.0173 0.0038  66  SER   C N   
1541 C CA  . SER   B 60  ? 0.2794 0.2488 0.2275 0.0056  -0.0237 0.0045  66  SER   C CA  
1542 C C   . SER   B 60  ? 0.2912 0.2550 0.2228 0.0039  -0.0222 0.0054  66  SER   C C   
1543 O O   . SER   B 60  ? 0.3157 0.2712 0.2373 0.0025  -0.0273 0.0080  66  SER   C O   
1544 C CB  . SER   B 60  ? 0.3381 0.3082 0.2926 0.0079  -0.0281 0.0015  66  SER   C CB  
1545 O OG  . SER   B 60  ? 0.4146 0.3883 0.3685 0.0089  -0.0243 -0.0014 66  SER   C OG  
1546 N N   . SER   B 61  ? 0.2849 0.2527 0.2133 0.0037  -0.0151 0.0035  67  SER   C N   
1547 C CA  . SER   B 61  ? 0.2946 0.2576 0.2068 0.0018  -0.0120 0.0036  67  SER   C CA  
1548 C C   . SER   B 61  ? 0.3027 0.2624 0.2059 -0.0019 -0.0094 0.0080  67  SER   C C   
1549 O O   . SER   B 61  ? 0.3142 0.2692 0.2023 -0.0043 -0.0065 0.0087  67  SER   C O   
1550 C CB  . SER   B 61  ? 0.2880 0.2565 0.2013 0.0031  -0.0049 -0.0005 67  SER   C CB  
1551 O OG  . SER   B 61  ? 0.3001 0.2770 0.2238 0.0029  0.0012  0.0000  67  SER   C OG  
1552 N N   . ARG   B 62  ? 0.2908 0.2525 0.2028 -0.0027 -0.0104 0.0110  68  ARG   C N   
1553 C CA  . ARG   B 62  ? 0.2856 0.2434 0.1911 -0.0065 -0.0095 0.0159  68  ARG   C CA  
1554 C C   . ARG   B 62  ? 0.3065 0.2584 0.2160 -0.0066 -0.0180 0.0192  68  ARG   C C   
1555 O O   . ARG   B 62  ? 0.3184 0.2657 0.2233 -0.0097 -0.0189 0.0236  68  ARG   C O   
1556 C CB  . ARG   B 62  ? 0.2777 0.2439 0.1922 -0.0077 -0.0021 0.0163  68  ARG   C CB  
1557 C CG  . ARG   B 62  ? 0.2932 0.2654 0.2056 -0.0078 0.0066  0.0135  68  ARG   C CG  
1558 C CD  . ARG   B 62  ? 0.3484 0.3155 0.2442 -0.0117 0.0109  0.0157  68  ARG   C CD  
1559 N NE  . ARG   B 62  ? 0.4040 0.3774 0.2993 -0.0115 0.0201  0.0122  68  ARG   C NE  
1560 C CZ  . ARG   B 62  ? 0.4434 0.4155 0.3314 -0.0097 0.0220  0.0078  68  ARG   C CZ  
1561 N NH1 . ARG   B 62  ? 0.4497 0.4145 0.3302 -0.0081 0.0148  0.0065  68  ARG   C NH1 
1562 N NH2 . ARG   B 62  ? 0.4571 0.4352 0.3464 -0.0094 0.0309  0.0043  68  ARG   C NH2 
1563 N N   . ARG   B 63  ? 0.3046 0.2572 0.2242 -0.0033 -0.0239 0.0169  69  ARG   C N   
1564 C CA  . ARG   B 63  ? 0.3259 0.2745 0.2534 -0.0024 -0.0314 0.0187  69  ARG   C CA  
1565 C C   . ARG   B 63  ? 0.3361 0.2872 0.2712 -0.0039 -0.0287 0.0206  69  ARG   C C   
1566 O O   . ARG   B 63  ? 0.3531 0.2974 0.2868 -0.0054 -0.0332 0.0243  69  ARG   C O   
1567 C CB  . ARG   B 63  ? 0.3803 0.3174 0.2954 -0.0041 -0.0392 0.0225  69  ARG   C CB  
1568 C CG  . ARG   B 63  ? 0.4554 0.3895 0.3688 -0.0019 -0.0454 0.0202  69  ARG   C CG  
1569 C CD  . ARG   B 63  ? 0.5723 0.4952 0.4792 -0.0029 -0.0559 0.0241  69  ARG   C CD  
1570 N NE  . ARG   B 63  ? 0.6656 0.5832 0.5614 -0.0029 -0.0607 0.0230  69  ARG   C NE  
1571 C CZ  . ARG   B 63  ? 0.7453 0.6536 0.6202 -0.0063 -0.0625 0.0258  69  ARG   C CZ  
1572 N NH1 . ARG   B 63  ? 0.7621 0.6657 0.6252 -0.0103 -0.0596 0.0304  69  ARG   C NH1 
1573 N NH2 . ARG   B 63  ? 0.7653 0.6684 0.6301 -0.0062 -0.0671 0.0240  69  ARG   C NH2 
1574 N N   . LYS   B 64  ? 0.3231 0.2830 0.2653 -0.0037 -0.0216 0.0184  70  LYS   C N   
1575 C CA  . LYS   B 64  ? 0.3260 0.2882 0.2743 -0.0056 -0.0189 0.0201  70  LYS   C CA  
1576 C C   . LYS   B 64  ? 0.2880 0.2591 0.2491 -0.0039 -0.0154 0.0164  70  LYS   C C   
1577 O O   . LYS   B 64  ? 0.2759 0.2525 0.2389 -0.0022 -0.0126 0.0134  70  LYS   C O   
1578 C CB  . LYS   B 64  ? 0.3761 0.3392 0.3155 -0.0093 -0.0126 0.0228  70  LYS   C CB  
1579 C CG  . LYS   B 64  ? 0.5038 0.4580 0.4317 -0.0131 -0.0147 0.0283  70  LYS   C CG  
1580 C CD  . LYS   B 64  ? 0.5871 0.5448 0.5094 -0.0169 -0.0066 0.0302  70  LYS   C CD  
1581 C CE  . LYS   B 64  ? 0.6708 0.6207 0.5837 -0.0218 -0.0076 0.0363  70  LYS   C CE  
1582 N NZ  . LYS   B 64  ? 0.7154 0.6560 0.6106 -0.0237 -0.0105 0.0390  70  LYS   C NZ  
1583 N N   . HIS   B 65  ? 0.2661 0.2380 0.2347 -0.0049 -0.0152 0.0169  71  HIS   C N   
1584 C CA  . HIS   B 65  ? 0.2491 0.2285 0.2273 -0.0045 -0.0118 0.0140  71  HIS   C CA  
1585 C C   . HIS   B 65  ? 0.2553 0.2380 0.2319 -0.0077 -0.0068 0.0163  71  HIS   C C   
1586 O O   . HIS   B 65  ? 0.2831 0.2613 0.2547 -0.0105 -0.0069 0.0200  71  HIS   C O   
1587 C CB  . HIS   B 65  ? 0.2490 0.2267 0.2361 -0.0038 -0.0148 0.0124  71  HIS   C CB  
1588 C CG  . HIS   B 65  ? 0.2543 0.2302 0.2463 -0.0007 -0.0191 0.0098  71  HIS   C CG  
1589 N ND1 . HIS   B 65  ? 0.2954 0.2769 0.2948 0.0011  -0.0177 0.0057  71  HIS   C ND1 
1590 C CD2 . HIS   B 65  ? 0.2644 0.2336 0.2555 0.0005  -0.0248 0.0111  71  HIS   C CD2 
1591 C CE1 . HIS   B 65  ? 0.2727 0.2515 0.2766 0.0035  -0.0220 0.0042  71  HIS   C CE1 
1592 N NE2 . HIS   B 65  ? 0.2751 0.2466 0.2749 0.0034  -0.0268 0.0073  71  HIS   C NE2 
1593 N N   . TYR   B 66  ? 0.2226 0.2130 0.2042 -0.0075 -0.0028 0.0143  72  TYR   C N   
1594 C CA  . TYR   B 66  ? 0.2276 0.2225 0.2108 -0.0102 0.0017  0.0160  72  TYR   C CA  
1595 C C   . TYR   B 66  ? 0.2298 0.2295 0.2221 -0.0108 0.0020  0.0143  72  TYR   C C   
1596 O O   . TYR   B 66  ? 0.2321 0.2352 0.2284 -0.0087 0.0014  0.0113  72  TYR   C O   
1597 C CB  . TYR   B 66  ? 0.2357 0.2355 0.2165 -0.0097 0.0064  0.0154  72  TYR   C CB  
1598 C CG  . TYR   B 66  ? 0.2552 0.2504 0.2247 -0.0102 0.0076  0.0170  72  TYR   C CG  
1599 C CD1 . TYR   B 66  ? 0.2751 0.2680 0.2388 -0.0138 0.0103  0.0207  72  TYR   C CD1 
1600 C CD2 . TYR   B 66  ? 0.2713 0.2642 0.2351 -0.0075 0.0061  0.0148  72  TYR   C CD2 
1601 C CE1 . TYR   B 66  ? 0.3008 0.2887 0.2517 -0.0150 0.0117  0.0223  72  TYR   C CE1 
1602 C CE2 . TYR   B 66  ? 0.2959 0.2837 0.2474 -0.0084 0.0070  0.0161  72  TYR   C CE2 
1603 C CZ  . TYR   B 66  ? 0.3254 0.3106 0.2697 -0.0122 0.0100  0.0198  72  TYR   C CZ  
1604 O OH  . TYR   B 66  ? 0.3683 0.3476 0.2980 -0.0137 0.0109  0.0211  72  TYR   C OH  
1605 N N   . PRO   B 67  ? 0.2371 0.2368 0.2321 -0.0139 0.0026  0.0164  73  PRO   C N   
1606 C CA  . PRO   B 67  ? 0.2395 0.2433 0.2420 -0.0151 0.0024  0.0150  73  PRO   C CA  
1607 C C   . PRO   B 67  ? 0.2318 0.2436 0.2386 -0.0154 0.0058  0.0150  73  PRO   C C   
1608 O O   . PRO   B 67  ? 0.2293 0.2433 0.2353 -0.0166 0.0093  0.0172  73  PRO   C O   
1609 C CB  . PRO   B 67  ? 0.2507 0.2506 0.2542 -0.0185 0.0012  0.0174  73  PRO   C CB  
1610 C CG  . PRO   B 67  ? 0.2694 0.2666 0.2671 -0.0202 0.0030  0.0213  73  PRO   C CG  
1611 C CD  . PRO   B 67  ? 0.2434 0.2388 0.2342 -0.0171 0.0031  0.0205  73  PRO   C CD  
1612 N N   . VAL   B 68  ? 0.2137 0.2295 0.2251 -0.0143 0.0049  0.0127  74  VAL   C N   
1613 C CA  . VAL   B 68  ? 0.2128 0.2357 0.2299 -0.0142 0.0070  0.0129  74  VAL   C CA  
1614 C C   . VAL   B 68  ? 0.2022 0.2279 0.2252 -0.0159 0.0045  0.0123  74  VAL   C C   
1615 O O   . VAL   B 68  ? 0.2075 0.2300 0.2284 -0.0163 0.0017  0.0107  74  VAL   C O   
1616 C CB  . VAL   B 68  ? 0.2267 0.2513 0.2423 -0.0107 0.0081  0.0109  74  VAL   C CB  
1617 C CG1 . VAL   B 68  ? 0.2456 0.2687 0.2554 -0.0096 0.0113  0.0115  74  VAL   C CG1 
1618 C CG2 . VAL   B 68  ? 0.2271 0.2487 0.2402 -0.0088 0.0050  0.0085  74  VAL   C CG2 
1619 N N   . SER   B 69  ? 0.1805 0.2122 0.2109 -0.0170 0.0054  0.0136  75  SER   C N   
1620 C CA  . SER   B 69  ? 0.1837 0.2184 0.2198 -0.0182 0.0021  0.0134  75  SER   C CA  
1621 C C   . SER   B 69  ? 0.1830 0.2203 0.2203 -0.0149 0.0023  0.0120  75  SER   C C   
1622 O O   . SER   B 69  ? 0.1904 0.2296 0.2283 -0.0123 0.0058  0.0116  75  SER   C O   
1623 C CB  . SER   B 69  ? 0.2071 0.2473 0.2529 -0.0207 0.0024  0.0157  75  SER   C CB  
1624 O OG  . SER   B 69  ? 0.2687 0.3063 0.3140 -0.0242 0.0015  0.0171  75  SER   C OG  
1625 N N   . PHE   B 70  ? 0.1691 0.2059 0.2063 -0.0152 -0.0013 0.0112  76  PHE   C N   
1626 C CA  . PHE   B 70  ? 0.1696 0.2079 0.2080 -0.0125 -0.0019 0.0103  76  PHE   C CA  
1627 C C   . PHE   B 70  ? 0.1816 0.2217 0.2247 -0.0142 -0.0064 0.0115  76  PHE   C C   
1628 O O   . PHE   B 70  ? 0.1909 0.2296 0.2328 -0.0176 -0.0094 0.0124  76  PHE   C O   
1629 C CB  . PHE   B 70  ? 0.1530 0.1868 0.1834 -0.0106 -0.0015 0.0082  76  PHE   C CB  
1630 C CG  . PHE   B 70  ? 0.1626 0.1922 0.1871 -0.0126 -0.0033 0.0070  76  PHE   C CG  
1631 C CD1 . PHE   B 70  ? 0.1753 0.2014 0.1961 -0.0134 -0.0023 0.0063  76  PHE   C CD1 
1632 C CD2 . PHE   B 70  ? 0.1642 0.1930 0.1868 -0.0139 -0.0058 0.0065  76  PHE   C CD2 
1633 C CE1 . PHE   B 70  ? 0.1861 0.2084 0.2026 -0.0148 -0.0034 0.0043  76  PHE   C CE1 
1634 C CE2 . PHE   B 70  ? 0.1706 0.1959 0.1876 -0.0159 -0.0063 0.0047  76  PHE   C CE2 
1635 C CZ  . PHE   B 70  ? 0.1830 0.2053 0.1975 -0.0160 -0.0048 0.0032  76  PHE   C CZ  
1636 N N   . SER   B 71  ? 0.1839 0.2263 0.2319 -0.0119 -0.0072 0.0116  77  SER   C N   
1637 C CA  . SER   B 71  ? 0.1944 0.2381 0.2478 -0.0135 -0.0124 0.0135  77  SER   C CA  
1638 C C   . SER   B 71  ? 0.2143 0.2533 0.2592 -0.0157 -0.0162 0.0136  77  SER   C C   
1639 O O   . SER   B 71  ? 0.2143 0.2498 0.2506 -0.0156 -0.0141 0.0117  77  SER   C O   
1640 C CB  . SER   B 71  ? 0.1871 0.2349 0.2507 -0.0101 -0.0123 0.0135  77  SER   C CB  
1641 O OG  . SER   B 71  ? 0.2056 0.2509 0.2652 -0.0073 -0.0115 0.0118  77  SER   C OG  
1642 N N   . LYS   B 72  ? 0.2090 0.2478 0.2566 -0.0180 -0.0218 0.0159  78  LYS   C N   
1643 C CA  . LYS   B 72  ? 0.2211 0.2553 0.2598 -0.0208 -0.0252 0.0165  78  LYS   C CA  
1644 C C   . LYS   B 72  ? 0.2291 0.2626 0.2683 -0.0179 -0.0248 0.0162  78  LYS   C C   
1645 O O   . LYS   B 72  ? 0.2383 0.2748 0.2869 -0.0144 -0.0247 0.0164  78  LYS   C O   
1646 C CB  . LYS   B 72  ? 0.2627 0.2962 0.3034 -0.0246 -0.0323 0.0199  78  LYS   C CB  
1647 C CG  . LYS   B 72  ? 0.3247 0.3578 0.3638 -0.0283 -0.0337 0.0202  78  LYS   C CG  
1648 C CD  . LYS   B 72  ? 0.4276 0.4576 0.4638 -0.0331 -0.0416 0.0233  78  LYS   C CD  
1649 C CE  . LYS   B 72  ? 0.5388 0.5668 0.5709 -0.0374 -0.0437 0.0232  78  LYS   C CE  
1650 N NZ  . LYS   B 72  ? 0.6196 0.6415 0.6355 -0.0406 -0.0415 0.0203  78  LYS   C NZ  
1651 N N   . PRO   B 73  ? 0.2292 0.2588 0.2590 -0.0194 -0.0243 0.0154  79  PRO   C N   
1652 C CA  . PRO   B 73  ? 0.2299 0.2585 0.2605 -0.0172 -0.0244 0.0152  79  PRO   C CA  
1653 C C   . PRO   B 73  ? 0.2398 0.2686 0.2779 -0.0169 -0.0299 0.0183  79  PRO   C C   
1654 O O   . PRO   B 73  ? 0.2387 0.2659 0.2759 -0.0206 -0.0353 0.0215  79  PRO   C O   
1655 C CB  . PRO   B 73  ? 0.2472 0.2720 0.2671 -0.0206 -0.0236 0.0146  79  PRO   C CB  
1656 C CG  . PRO   B 73  ? 0.2619 0.2860 0.2756 -0.0228 -0.0210 0.0128  79  PRO   C CG  
1657 C CD  . PRO   B 73  ? 0.2291 0.2552 0.2479 -0.0234 -0.0235 0.0143  79  PRO   C CD  
1658 N N   . SER   B 74  ? 0.2440 0.2745 0.2903 -0.0124 -0.0290 0.0173  80  SER   C N   
1659 C CA  . SER   B 74  ? 0.2508 0.2816 0.3070 -0.0112 -0.0343 0.0197  80  SER   C CA  
1660 C C   . SER   B 74  ? 0.2401 0.2702 0.3012 -0.0069 -0.0333 0.0179  80  SER   C C   
1661 O O   . SER   B 74  ? 0.2325 0.2618 0.2885 -0.0051 -0.0287 0.0148  80  SER   C O   
1662 C CB  . SER   B 74  ? 0.2954 0.3311 0.3629 -0.0101 -0.0352 0.0203  80  SER   C CB  
1663 O OG  . SER   B 74  ? 0.3420 0.3819 0.4152 -0.0056 -0.0290 0.0168  80  SER   C OG  
1664 N N   . LEU   B 75  ? 0.2286 0.2579 0.2992 -0.0056 -0.0386 0.0198  81  LEU   C N   
1665 C CA  . LEU   B 75  ? 0.2463 0.2739 0.3229 -0.0017 -0.0391 0.0182  81  LEU   C CA  
1666 C C   . LEU   B 75  ? 0.2446 0.2771 0.3322 0.0036  -0.0348 0.0144  81  LEU   C C   
1667 O O   . LEU   B 75  ? 0.2390 0.2753 0.3378 0.0043  -0.0368 0.0155  81  LEU   C O   
1668 C CB  . LEU   B 75  ? 0.2611 0.2852 0.3442 -0.0031 -0.0476 0.0225  81  LEU   C CB  
1669 C CG  . LEU   B 75  ? 0.3187 0.3362 0.3971 -0.0051 -0.0519 0.0249  81  LEU   C CG  
1670 C CD1 . LEU   B 75  ? 0.3411 0.3559 0.4316 -0.0038 -0.0598 0.0279  81  LEU   C CD1 
1671 C CD2 . LEU   B 75  ? 0.3201 0.3361 0.3940 -0.0029 -0.0472 0.0212  81  LEU   C CD2 
1672 N N   . ILE   B 76  ? 0.2371 0.2698 0.3214 0.0068  -0.0288 0.0100  82  ILE   C N   
1673 C CA  . ILE   B 76  ? 0.2416 0.2785 0.3330 0.0113  -0.0232 0.0059  82  ILE   C CA  
1674 C C   . ILE   B 76  ? 0.2462 0.2803 0.3397 0.0156  -0.0217 0.0018  82  ILE   C C   
1675 O O   . ILE   B 76  ? 0.2418 0.2714 0.3261 0.0152  -0.0218 0.0009  82  ILE   C O   
1676 C CB  . ILE   B 76  ? 0.2663 0.3054 0.3485 0.0102  -0.0170 0.0044  82  ILE   C CB  
1677 C CG1 . ILE   B 76  ? 0.2916 0.3338 0.3746 0.0064  -0.0183 0.0077  82  ILE   C CG1 
1678 C CG2 . ILE   B 76  ? 0.2827 0.3244 0.3669 0.0140  -0.0101 0.0000  82  ILE   C CG2 
1679 C CD1 . ILE   B 76  ? 0.3268 0.3691 0.3996 0.0042  -0.0144 0.0074  82  ILE   C CD1 
1680 N N   . PHE   B 77  ? 0.2418 0.2786 0.3476 0.0198  -0.0200 -0.0012 83  PHE   C N   
1681 C CA  . PHE   B 77  ? 0.2640 0.2975 0.3715 0.0241  -0.0184 -0.0060 83  PHE   C CA  
1682 C C   . PHE   B 77  ? 0.2685 0.3009 0.3637 0.0251  -0.0116 -0.0102 83  PHE   C C   
1683 O O   . PHE   B 77  ? 0.2722 0.3086 0.3644 0.0247  -0.0059 -0.0112 83  PHE   C O   
1684 C CB  . PHE   B 77  ? 0.2701 0.3071 0.3948 0.0285  -0.0175 -0.0090 83  PHE   C CB  
1685 C CG  . PHE   B 77  ? 0.2823 0.3150 0.4092 0.0330  -0.0161 -0.0146 83  PHE   C CG  
1686 C CD1 . PHE   B 77  ? 0.2993 0.3337 0.4240 0.0363  -0.0078 -0.0209 83  PHE   C CD1 
1687 C CD2 . PHE   B 77  ? 0.2989 0.3251 0.4281 0.0335  -0.0230 -0.0135 83  PHE   C CD2 
1688 C CE1 . PHE   B 77  ? 0.3159 0.3454 0.4410 0.0402  -0.0066 -0.0267 83  PHE   C CE1 
1689 C CE2 . PHE   B 77  ? 0.3150 0.3364 0.4459 0.0375  -0.0221 -0.0190 83  PHE   C CE2 
1690 C CZ  . PHE   B 77  ? 0.3114 0.3343 0.4399 0.0409  -0.0140 -0.0258 83  PHE   C CZ  
1691 N N   . VAL   B 78  ? 0.2649 0.2912 0.3526 0.0257  -0.0130 -0.0120 84  VAL   C N   
1692 C CA  . VAL   B 78  ? 0.2597 0.2834 0.3353 0.0265  -0.0084 -0.0158 84  VAL   C CA  
1693 C C   . VAL   B 78  ? 0.2804 0.2995 0.3580 0.0305  -0.0083 -0.0211 84  VAL   C C   
1694 O O   . VAL   B 78  ? 0.2877 0.3023 0.3692 0.0309  -0.0139 -0.0205 84  VAL   C O   
1695 C CB  . VAL   B 78  ? 0.2532 0.2736 0.3172 0.0231  -0.0109 -0.0132 84  VAL   C CB  
1696 C CG1 . VAL   B 78  ? 0.2654 0.2826 0.3177 0.0240  -0.0074 -0.0168 84  VAL   C CG1 
1697 C CG2 . VAL   B 78  ? 0.2447 0.2687 0.3065 0.0191  -0.0112 -0.0086 84  VAL   C CG2 
1698 N N   . GLU   B 79  ? 0.2938 0.3130 0.3673 0.0331  -0.0021 -0.0263 85  GLU   C N   
1699 C CA  . GLU   B 79  ? 0.3161 0.3306 0.3895 0.0368  -0.0007 -0.0326 85  GLU   C CA  
1700 C C   . GLU   B 79  ? 0.3234 0.3302 0.3873 0.0360  -0.0053 -0.0332 85  GLU   C C   
1701 O O   . GLU   B 79  ? 0.3336 0.3394 0.3878 0.0328  -0.0068 -0.0300 85  GLU   C O   
1702 C CB  . GLU   B 79  ? 0.3825 0.3985 0.4482 0.0382  0.0080  -0.0375 85  GLU   C CB  
1703 C CG  . GLU   B 79  ? 0.4825 0.5069 0.5575 0.0385  0.0138  -0.0372 85  GLU   C CG  
1704 C CD  . GLU   B 79  ? 0.5924 0.6197 0.6841 0.0428  0.0160  -0.0416 85  GLU   C CD  
1705 O OE1 . GLU   B 79  ? 0.6047 0.6398 0.7074 0.0432  0.0202  -0.0411 85  GLU   C OE1 
1706 O OE2 . GLU   B 79  ? 0.6327 0.6546 0.7276 0.0459  0.0133  -0.0456 85  GLU   C OE2 
1707 N N   . ALA   B 80  ? 0.3232 0.3244 0.3903 0.0390  -0.0073 -0.0376 86  ALA   C N   
1708 C CA  . ALA   B 80  ? 0.3246 0.3182 0.3837 0.0382  -0.0121 -0.0386 86  ALA   C CA  
1709 C C   . ALA   B 80  ? 0.3268 0.3180 0.3696 0.0371  -0.0090 -0.0407 86  ALA   C C   
1710 O O   . ALA   B 80  ? 0.3328 0.3262 0.3697 0.0379  -0.0025 -0.0434 86  ALA   C O   
1711 C CB  . ALA   B 80  ? 0.3246 0.3121 0.3897 0.0420  -0.0141 -0.0442 86  ALA   C CB  
1712 N N   . SER   B 81  ? 0.3188 0.3056 0.3548 0.0347  -0.0139 -0.0390 87  SER   C N   
1713 C CA  . SER   B 81  ? 0.3156 0.2988 0.3370 0.0335  -0.0133 -0.0404 87  SER   C CA  
1714 C C   . SER   B 81  ? 0.3334 0.3095 0.3534 0.0330  -0.0201 -0.0416 87  SER   C C   
1715 O O   . SER   B 81  ? 0.3439 0.3182 0.3737 0.0336  -0.0241 -0.0411 87  SER   C O   
1716 C CB  . SER   B 81  ? 0.3163 0.3042 0.3337 0.0301  -0.0127 -0.0350 87  SER   C CB  
1717 O OG  . SER   B 81  ? 0.3029 0.2919 0.3260 0.0276  -0.0178 -0.0303 87  SER   C OG  
1718 N N   . GLU   B 82  ? 0.3373 0.3086 0.3456 0.0318  -0.0220 -0.0428 88  GLU   C N   
1719 C CA  . GLU   B 82  ? 0.3461 0.3112 0.3545 0.0309  -0.0290 -0.0436 88  GLU   C CA  
1720 C C   . GLU   B 82  ? 0.3386 0.3070 0.3561 0.0278  -0.0334 -0.0376 88  GLU   C C   
1721 O O   . GLU   B 82  ? 0.3456 0.3101 0.3679 0.0269  -0.0388 -0.0374 88  GLU   C O   
1722 C CB  . GLU   B 82  ? 0.3925 0.3519 0.3872 0.0300  -0.0311 -0.0459 88  GLU   C CB  
1723 C CG  . GLU   B 82  ? 0.4760 0.4290 0.4603 0.0326  -0.0283 -0.0529 88  GLU   C CG  
1724 C CD  . GLU   B 82  ? 0.6117 0.5580 0.5798 0.0312  -0.0307 -0.0549 88  GLU   C CD  
1725 O OE1 . GLU   B 82  ? 0.6076 0.5535 0.5751 0.0287  -0.0363 -0.0512 88  GLU   C OE1 
1726 O OE2 . GLU   B 82  ? 0.6731 0.6145 0.6291 0.0326  -0.0271 -0.0603 88  GLU   C OE2 
1727 N N   . TYR   B 83  ? 0.3212 0.2966 0.3409 0.0259  -0.0308 -0.0328 89  TYR   C N   
1728 C CA  . TYR   B 83  ? 0.3114 0.2906 0.3378 0.0226  -0.0333 -0.0275 89  TYR   C CA  
1729 C C   . TYR   B 83  ? 0.3074 0.2890 0.3438 0.0219  -0.0339 -0.0244 89  TYR   C C   
1730 O O   . TYR   B 83  ? 0.3274 0.3096 0.3686 0.0188  -0.0371 -0.0207 89  TYR   C O   
1731 C CB  . TYR   B 83  ? 0.3117 0.2963 0.3342 0.0208  -0.0301 -0.0245 89  TYR   C CB  
1732 C CG  . TYR   B 83  ? 0.3299 0.3116 0.3426 0.0210  -0.0305 -0.0265 89  TYR   C CG  
1733 C CD1 . TYR   B 83  ? 0.3470 0.3260 0.3595 0.0195  -0.0354 -0.0262 89  TYR   C CD1 
1734 C CD2 . TYR   B 83  ? 0.3475 0.3289 0.3515 0.0225  -0.0264 -0.0283 89  TYR   C CD2 
1735 C CE1 . TYR   B 83  ? 0.3694 0.3449 0.3732 0.0196  -0.0371 -0.0277 89  TYR   C CE1 
1736 C CE2 . TYR   B 83  ? 0.3728 0.3507 0.3667 0.0222  -0.0275 -0.0293 89  TYR   C CE2 
1737 C CZ  . TYR   B 83  ? 0.3905 0.3652 0.3844 0.0208  -0.0333 -0.0289 89  TYR   C CZ  
1738 O OH  . TYR   B 83  ? 0.4287 0.3993 0.4131 0.0204  -0.0358 -0.0293 89  TYR   C OH  
1739 N N   . TYR   B 84  ? 0.2794 0.2629 0.3191 0.0244  -0.0309 -0.0255 90  TYR   C N   
1740 C CA  . TYR   B 84  ? 0.2796 0.2651 0.3291 0.0237  -0.0325 -0.0221 90  TYR   C CA  
1741 C C   . TYR   B 84  ? 0.2984 0.2823 0.3545 0.0278  -0.0317 -0.0257 90  TYR   C C   
1742 O O   . TYR   B 84  ? 0.2933 0.2780 0.3462 0.0309  -0.0269 -0.0302 90  TYR   C O   
1743 C CB  . TYR   B 84  ? 0.2667 0.2592 0.3167 0.0217  -0.0293 -0.0180 90  TYR   C CB  
1744 C CG  . TYR   B 84  ? 0.2608 0.2559 0.3062 0.0177  -0.0294 -0.0144 90  TYR   C CG  
1745 C CD1 . TYR   B 84  ? 0.2582 0.2559 0.2966 0.0175  -0.0258 -0.0150 90  TYR   C CD1 
1746 C CD2 . TYR   B 84  ? 0.2652 0.2599 0.3137 0.0139  -0.0328 -0.0103 90  TYR   C CD2 
1747 C CE1 . TYR   B 84  ? 0.2547 0.2547 0.2907 0.0143  -0.0256 -0.0123 90  TYR   C CE1 
1748 C CE2 . TYR   B 84  ? 0.2703 0.2679 0.3155 0.0104  -0.0318 -0.0078 90  TYR   C CE2 
1749 C CZ  . TYR   B 84  ? 0.2675 0.2680 0.3073 0.0109  -0.0282 -0.0090 90  TYR   C CZ  
1750 O OH  . TYR   B 84  ? 0.2740 0.2771 0.3122 0.0078  -0.0272 -0.0072 90  TYR   C OH  
1751 N N   . PRO   B 85  ? 0.3036 0.2858 0.3697 0.0276  -0.0360 -0.0234 91  PRO   C N   
1752 C CA  . PRO   B 85  ? 0.3038 0.2858 0.3793 0.0317  -0.0353 -0.0263 91  PRO   C CA  
1753 C C   . PRO   B 85  ? 0.2987 0.2885 0.3774 0.0321  -0.0309 -0.0245 91  PRO   C C   
1754 O O   . PRO   B 85  ? 0.2890 0.2831 0.3635 0.0285  -0.0301 -0.0199 91  PRO   C O   
1755 C CB  . PRO   B 85  ? 0.3153 0.2934 0.4004 0.0303  -0.0425 -0.0223 91  PRO   C CB  
1756 C CG  . PRO   B 85  ? 0.3164 0.2965 0.3972 0.0246  -0.0448 -0.0155 91  PRO   C CG  
1757 C CD  . PRO   B 85  ? 0.2997 0.2807 0.3694 0.0233  -0.0415 -0.0174 91  PRO   C CD  
1758 N N   . ALA   B 86  ? 0.2992 0.2909 0.3871 0.0361  -0.0283 -0.0279 92  ALA   C N   
1759 C CA  . ALA   B 86  ? 0.2969 0.2963 0.3911 0.0362  -0.0251 -0.0258 92  ALA   C CA  
1760 C C   . ALA   B 86  ? 0.2888 0.2891 0.3886 0.0324  -0.0315 -0.0182 92  ALA   C C   
1761 O O   . ALA   B 86  ? 0.2849 0.2800 0.3903 0.0320  -0.0380 -0.0162 92  ALA   C O   
1762 C CB  . ALA   B 86  ? 0.2923 0.2935 0.3991 0.0413  -0.0221 -0.0309 92  ALA   C CB  
1763 N N   . ARG   B 87  ? 0.2816 0.2872 0.3774 0.0290  -0.0300 -0.0139 93  ARG   C N   
1764 C CA  . ARG   B 87  ? 0.2626 0.2681 0.3598 0.0245  -0.0359 -0.0069 93  ARG   C CA  
1765 C C   . ARG   B 87  ? 0.2650 0.2770 0.3603 0.0220  -0.0333 -0.0039 93  ARG   C C   
1766 O O   . ARG   B 87  ? 0.2753 0.2916 0.3675 0.0234  -0.0270 -0.0069 93  ARG   C O   
1767 C CB  . ARG   B 87  ? 0.2567 0.2579 0.3434 0.0205  -0.0382 -0.0046 93  ARG   C CB  
1768 C CG  . ARG   B 87  ? 0.2513 0.2557 0.3261 0.0184  -0.0330 -0.0050 93  ARG   C CG  
1769 C CD  . ARG   B 87  ? 0.2574 0.2580 0.3244 0.0168  -0.0335 -0.0059 93  ARG   C CD  
1770 N NE  . ARG   B 87  ? 0.2622 0.2655 0.3211 0.0130  -0.0315 -0.0035 93  ARG   C NE  
1771 C CZ  . ARG   B 87  ? 0.2744 0.2810 0.3275 0.0135  -0.0267 -0.0052 93  ARG   C CZ  
1772 N NH1 . ARG   B 87  ? 0.2417 0.2501 0.2890 0.0103  -0.0254 -0.0033 93  ARG   C NH1 
1773 N NH2 . ARG   B 87  ? 0.2811 0.2891 0.3345 0.0172  -0.0231 -0.0089 93  ARG   C NH2 
1774 N N   . TYR   B 88  ? 0.2629 0.2749 0.3587 0.0178  -0.0382 0.0020  94  TYR   C N   
1775 C CA  . TYR   B 88  ? 0.2706 0.2875 0.3625 0.0147  -0.0364 0.0049  94  TYR   C CA  
1776 C C   . TYR   B 88  ? 0.2540 0.2695 0.3321 0.0106  -0.0349 0.0063  94  TYR   C C   
1777 O O   . TYR   B 88  ? 0.2688 0.2801 0.3430 0.0074  -0.0387 0.0091  94  TYR   C O   
1778 C CB  . TYR   B 88  ? 0.2886 0.3055 0.3872 0.0119  -0.0432 0.0104  94  TYR   C CB  
1779 C CG  . TYR   B 88  ? 0.3215 0.3415 0.4363 0.0160  -0.0445 0.0091  94  TYR   C CG  
1780 C CD1 . TYR   B 88  ? 0.3381 0.3648 0.4584 0.0166  -0.0414 0.0086  94  TYR   C CD1 
1781 C CD2 . TYR   B 88  ? 0.3470 0.3635 0.4729 0.0195  -0.0486 0.0079  94  TYR   C CD2 
1782 C CE1 . TYR   B 88  ? 0.3571 0.3878 0.4945 0.0204  -0.0422 0.0072  94  TYR   C CE1 
1783 C CE2 . TYR   B 88  ? 0.3616 0.3815 0.5046 0.0238  -0.0494 0.0060  94  TYR   C CE2 
1784 C CZ  . TYR   B 88  ? 0.3758 0.4033 0.5250 0.0242  -0.0460 0.0056  94  TYR   C CZ  
1785 O OH  . TYR   B 88  ? 0.4232 0.4554 0.5912 0.0283  -0.0461 0.0036  94  TYR   C OH  
1786 N N   . GLN   B 89  ? 0.2204 0.2395 0.2920 0.0104  -0.0293 0.0045  95  GLN   C N   
1787 C CA  . GLN   B 89  ? 0.2190 0.2373 0.2796 0.0069  -0.0277 0.0054  95  GLN   C CA  
1788 C C   . GLN   B 89  ? 0.2193 0.2397 0.2774 0.0025  -0.0290 0.0093  95  GLN   C C   
1789 O O   . GLN   B 89  ? 0.2288 0.2529 0.2911 0.0031  -0.0281 0.0096  95  GLN   C O   
1790 C CB  . GLN   B 89  ? 0.2340 0.2538 0.2889 0.0090  -0.0219 0.0014  95  GLN   C CB  
1791 C CG  . GLN   B 89  ? 0.2580 0.2776 0.3040 0.0058  -0.0204 0.0022  95  GLN   C CG  
1792 C CD  . GLN   B 89  ? 0.2435 0.2623 0.2843 0.0079  -0.0170 -0.0013 95  GLN   C CD  
1793 O OE1 . GLN   B 89  ? 0.2386 0.2551 0.2800 0.0109  -0.0169 -0.0041 95  GLN   C OE1 
1794 N NE2 . GLN   B 89  ? 0.2198 0.2399 0.2550 0.0062  -0.0146 -0.0010 95  GLN   C NE2 
1795 N N   . SER   B 90  ? 0.2034 0.2213 0.2546 -0.0021 -0.0310 0.0122  96  SER   C N   
1796 C CA  . SER   B 90  ? 0.1977 0.2164 0.2445 -0.0067 -0.0325 0.0155  96  SER   C CA  
1797 C C   . SER   B 90  ? 0.1988 0.2195 0.2375 -0.0083 -0.0274 0.0137  96  SER   C C   
1798 O O   . SER   B 90  ? 0.2010 0.2217 0.2372 -0.0065 -0.0237 0.0107  96  SER   C O   
1799 C CB  . SER   B 90  ? 0.2045 0.2189 0.2473 -0.0116 -0.0373 0.0198  96  SER   C CB  
1800 O OG  . SER   B 90  ? 0.2160 0.2286 0.2530 -0.0131 -0.0349 0.0187  96  SER   C OG  
1801 N N   . HIS   B 91  ? 0.1909 0.2124 0.2258 -0.0118 -0.0280 0.0155  97  HIS   C N   
1802 C CA  . HIS   B 91  ? 0.1971 0.2196 0.2247 -0.0137 -0.0239 0.0138  97  HIS   C CA  
1803 C C   . HIS   B 91  ? 0.2086 0.2339 0.2387 -0.0096 -0.0194 0.0104  97  HIS   C C   
1804 O O   . HIS   B 91  ? 0.2092 0.2342 0.2348 -0.0095 -0.0160 0.0081  97  HIS   C O   
1805 C CB  . HIS   B 91  ? 0.2022 0.2225 0.2224 -0.0167 -0.0220 0.0132  97  HIS   C CB  
1806 C CG  . HIS   B 91  ? 0.2236 0.2407 0.2387 -0.0219 -0.0256 0.0168  97  HIS   C CG  
1807 N ND1 . HIS   B 91  ? 0.2526 0.2685 0.2592 -0.0270 -0.0255 0.0178  97  HIS   C ND1 
1808 C CD2 . HIS   B 91  ? 0.2353 0.2497 0.2522 -0.0230 -0.0296 0.0197  97  HIS   C CD2 
1809 C CE1 . HIS   B 91  ? 0.2615 0.2738 0.2637 -0.0313 -0.0293 0.0216  97  HIS   C CE1 
1810 N NE2 . HIS   B 91  ? 0.2488 0.2601 0.2575 -0.0291 -0.0321 0.0231  97  HIS   C NE2 
1811 N N   . LEU   B 92  ? 0.1888 0.2164 0.2266 -0.0061 -0.0196 0.0101  98  LEU   C N   
1812 C CA  . LEU   B 92  ? 0.1863 0.2157 0.2250 -0.0027 -0.0152 0.0072  98  LEU   C CA  
1813 C C   . LEU   B 92  ? 0.1872 0.2197 0.2280 -0.0037 -0.0139 0.0080  98  LEU   C C   
1814 O O   . LEU   B 92  ? 0.1930 0.2272 0.2393 -0.0050 -0.0170 0.0103  98  LEU   C O   
1815 C CB  . LEU   B 92  ? 0.1801 0.2101 0.2255 0.0015  -0.0150 0.0056  98  LEU   C CB  
1816 C CG  . LEU   B 92  ? 0.2058 0.2367 0.2503 0.0048  -0.0102 0.0025  98  LEU   C CG  
1817 C CD1 . LEU   B 92  ? 0.2039 0.2318 0.2401 0.0050  -0.0087 0.0007  98  LEU   C CD1 
1818 C CD2 . LEU   B 92  ? 0.2412 0.2723 0.2921 0.0087  -0.0099 0.0004  98  LEU   C CD2 
1819 N N   . MET   B 93  ? 0.1833 0.2162 0.2203 -0.0033 -0.0102 0.0065  99  MET   C N   
1820 C CA  . MET   B 93  ? 0.1846 0.2200 0.2237 -0.0046 -0.0088 0.0074  99  MET   C CA  
1821 C C   . MET   B 93  ? 0.1933 0.2304 0.2338 -0.0018 -0.0044 0.0058  99  MET   C C   
1822 O O   . MET   B 93  ? 0.2033 0.2379 0.2382 -0.0001 -0.0024 0.0039  99  MET   C O   
1823 C CB  . MET   B 93  ? 0.1989 0.2321 0.2310 -0.0077 -0.0085 0.0073  99  MET   C CB  
1824 C CG  . MET   B 93  ? 0.2225 0.2534 0.2504 -0.0109 -0.0116 0.0082  99  MET   C CG  
1825 S SD  . MET   B 93  ? 0.2585 0.2863 0.2780 -0.0137 -0.0099 0.0063  99  MET   C SD  
1826 C CE  . MET   B 93  ? 0.1775 0.2039 0.1951 -0.0104 -0.0070 0.0036  99  MET   C CE  
1827 N N   . LEU   B 94  ? 0.1805 0.2217 0.2282 -0.0016 -0.0031 0.0066  100 LEU   C N   
1828 C CA  . LEU   B 94  ? 0.1866 0.2297 0.2351 0.0004  0.0021  0.0051  100 LEU   C CA  
1829 C C   . LEU   B 94  ? 0.1874 0.2313 0.2339 -0.0020 0.0045  0.0064  100 LEU   C C   
1830 O O   . LEU   B 94  ? 0.1846 0.2296 0.2338 -0.0050 0.0021  0.0084  100 LEU   C O   
1831 C CB  . LEU   B 94  ? 0.1948 0.2428 0.2547 0.0027  0.0035  0.0045  100 LEU   C CB  
1832 C CG  . LEU   B 94  ? 0.2134 0.2604 0.2772 0.0058  0.0014  0.0028  100 LEU   C CG  
1833 C CD1 . LEU   B 94  ? 0.2200 0.2723 0.2968 0.0085  0.0037  0.0014  100 LEU   C CD1 
1834 C CD2 . LEU   B 94  ? 0.2376 0.2798 0.2916 0.0079  0.0031  0.0001  100 LEU   C CD2 
1835 N N   . ALA   B 95  ? 0.1795 0.2221 0.2205 -0.0012 0.0088  0.0055  101 ALA   C N   
1836 C CA  . ALA   B 95  ? 0.1866 0.2291 0.2251 -0.0036 0.0115  0.0070  101 ALA   C CA  
1837 C C   . ALA   B 95  ? 0.1977 0.2421 0.2355 -0.0023 0.0175  0.0060  101 ALA   C C   
1838 O O   . ALA   B 95  ? 0.2003 0.2439 0.2360 0.0007  0.0191  0.0035  101 ALA   C O   
1839 C CB  . ALA   B 95  ? 0.1917 0.2281 0.2204 -0.0046 0.0099  0.0072  101 ALA   C CB  
1840 N N   . VAL   B 96  ? 0.1983 0.2447 0.2372 -0.0048 0.0209  0.0079  102 VAL   C N   
1841 C CA  . VAL   B 96  ? 0.2073 0.2549 0.2431 -0.0048 0.0274  0.0073  102 VAL   C CA  
1842 C C   . VAL   B 96  ? 0.2371 0.2768 0.2583 -0.0055 0.0269  0.0080  102 VAL   C C   
1843 O O   . VAL   B 96  ? 0.2486 0.2850 0.2664 -0.0082 0.0246  0.0105  102 VAL   C O   
1844 C CB  . VAL   B 96  ? 0.2088 0.2622 0.2532 -0.0079 0.0312  0.0096  102 VAL   C CB  
1845 C CG1 . VAL   B 96  ? 0.2096 0.2638 0.2487 -0.0089 0.0389  0.0093  102 VAL   C CG1 
1846 C CG2 . VAL   B 96  ? 0.1975 0.2588 0.2585 -0.0070 0.0302  0.0091  102 VAL   C CG2 
1847 N N   . GLY   B 97  ? 0.2538 0.2900 0.2667 -0.0031 0.0282  0.0056  103 GLY   C N   
1848 C CA  . GLY   B 97  ? 0.2778 0.3060 0.2770 -0.0037 0.0266  0.0064  103 GLY   C CA  
1849 C C   . GLY   B 97  ? 0.2920 0.3164 0.2825 -0.0011 0.0274  0.0034  103 GLY   C C   
1850 O O   . GLY   B 97  ? 0.3027 0.3301 0.2982 0.0017  0.0286  0.0002  103 GLY   C O   
1851 N N   . HIS   B 98  ? 0.2872 0.3041 0.2647 -0.0020 0.0258  0.0045  104 HIS   C N   
1852 C CA  . HIS   B 98  ? 0.2857 0.2977 0.2531 -0.0001 0.0257  0.0017  104 HIS   C CA  
1853 C C   . HIS   B 98  ? 0.2714 0.2805 0.2399 0.0027  0.0193  -0.0001 104 HIS   C C   
1854 O O   . HIS   B 98  ? 0.2612 0.2682 0.2317 0.0023  0.0142  0.0016  104 HIS   C O   
1855 C CB  . HIS   B 98  ? 0.3024 0.3067 0.2542 -0.0028 0.0258  0.0041  104 HIS   C CB  
1856 C CG  . HIS   B 98  ? 0.3069 0.3052 0.2464 -0.0013 0.0253  0.0012  104 HIS   C CG  
1857 N ND1 . HIS   B 98  ? 0.3301 0.3305 0.2664 -0.0004 0.0317  -0.0025 104 HIS   C ND1 
1858 C CD2 . HIS   B 98  ? 0.3099 0.3005 0.2409 -0.0005 0.0187  0.0012  104 HIS   C CD2 
1859 C CE1 . HIS   B 98  ? 0.3430 0.3360 0.2670 0.0006  0.0288  -0.0047 104 HIS   C CE1 
1860 N NE2 . HIS   B 98  ? 0.3336 0.3205 0.2541 0.0004  0.0206  -0.0022 104 HIS   C NE2 
1861 N N   . SER   B 99  ? 0.2564 0.2649 0.2236 0.0054  0.0198  -0.0039 105 SER   C N   
1862 C CA  . SER   B 99  ? 0.2574 0.2626 0.2248 0.0076  0.0139  -0.0056 105 SER   C CA  
1863 C C   . SER   B 99  ? 0.2694 0.2715 0.2307 0.0098  0.0148  -0.0097 105 SER   C C   
1864 O O   . SER   B 99  ? 0.2865 0.2914 0.2485 0.0106  0.0205  -0.0123 105 SER   C O   
1865 C CB  . SER   B 99  ? 0.2750 0.2852 0.2555 0.0086  0.0114  -0.0056 105 SER   C CB  
1866 O OG  . SER   B 99  ? 0.3204 0.3358 0.3088 0.0101  0.0146  -0.0076 105 SER   C OG  
1867 N N   . GLU   B 100 ? 0.2675 0.2635 0.2227 0.0106  0.0093  -0.0106 106 GLU   C N   
1868 C CA  . GLU   B 100 ? 0.2785 0.2698 0.2270 0.0124  0.0083  -0.0146 106 GLU   C CA  
1869 C C   . GLU   B 100 ? 0.2769 0.2678 0.2331 0.0142  0.0019  -0.0155 106 GLU   C C   
1870 O O   . GLU   B 100 ? 0.2693 0.2621 0.2323 0.0135  -0.0015 -0.0128 106 GLU   C O   
1871 C CB  . GLU   B 100 ? 0.3118 0.2946 0.2433 0.0107  0.0065  -0.0140 106 GLU   C CB  
1872 C CG  . GLU   B 100 ? 0.3821 0.3649 0.3044 0.0084  0.0138  -0.0134 106 GLU   C CG  
1873 C CD  . GLU   B 100 ? 0.4748 0.4485 0.3786 0.0056  0.0119  -0.0114 106 GLU   C CD  
1874 O OE1 . GLU   B 100 ? 0.5223 0.4886 0.4181 0.0060  0.0052  -0.0122 106 GLU   C OE1 
1875 O OE2 . GLU   B 100 ? 0.4656 0.4395 0.3631 0.0025  0.0167  -0.0087 106 GLU   C OE2 
1876 N N   . PRO   B 101 ? 0.2790 0.2672 0.2344 0.0163  0.0004  -0.0193 107 PRO   C N   
1877 C CA  . PRO   B 101 ? 0.2803 0.2685 0.2440 0.0174  -0.0053 -0.0198 107 PRO   C CA  
1878 C C   . PRO   B 101 ? 0.2883 0.2739 0.2518 0.0161  -0.0115 -0.0172 107 PRO   C C   
1879 O O   . PRO   B 101 ? 0.2758 0.2650 0.2497 0.0159  -0.0137 -0.0158 107 PRO   C O   
1880 C CB  . PRO   B 101 ? 0.2956 0.2789 0.2547 0.0193  -0.0063 -0.0245 107 PRO   C CB  
1881 C CG  . PRO   B 101 ? 0.2973 0.2822 0.2529 0.0201  0.0012  -0.0271 107 PRO   C CG  
1882 C CD  . PRO   B 101 ? 0.2813 0.2667 0.2293 0.0176  0.0044  -0.0238 107 PRO   C CD  
1883 N N   . GLY   B 102 ? 0.2922 0.2717 0.2446 0.0151  -0.0140 -0.0164 108 GLY   C N   
1884 C CA  . GLY   B 102 ? 0.2883 0.2651 0.2417 0.0142  -0.0204 -0.0141 108 GLY   C CA  
1885 C C   . GLY   B 102 ? 0.2689 0.2500 0.2295 0.0130  -0.0194 -0.0107 108 GLY   C C   
1886 O O   . GLY   B 102 ? 0.2669 0.2470 0.2320 0.0127  -0.0240 -0.0092 108 GLY   C O   
1887 N N   . ASP   B 103 ? 0.2481 0.2340 0.2107 0.0124  -0.0135 -0.0097 109 ASP   C N   
1888 C CA  . ASP   B 103 ? 0.2289 0.2188 0.1982 0.0111  -0.0123 -0.0070 109 ASP   C CA  
1889 C C   . ASP   B 103 ? 0.2200 0.2154 0.2017 0.0115  -0.0127 -0.0074 109 ASP   C C   
1890 O O   . ASP   B 103 ? 0.2178 0.2157 0.2049 0.0104  -0.0125 -0.0059 109 ASP   C O   
1891 C CB  . ASP   B 103 ? 0.2364 0.2293 0.2037 0.0098  -0.0062 -0.0056 109 ASP   C CB  
1892 C CG  . ASP   B 103 ? 0.2624 0.2499 0.2174 0.0082  -0.0055 -0.0038 109 ASP   C CG  
1893 O OD1 . ASP   B 103 ? 0.2589 0.2406 0.2088 0.0077  -0.0105 -0.0024 109 ASP   C OD1 
1894 O OD2 . ASP   B 103 ? 0.2780 0.2671 0.2287 0.0074  0.0001  -0.0039 109 ASP   C OD2 
1895 N N   . CYS   B 104 ? 0.2174 0.2141 0.2030 0.0126  -0.0133 -0.0096 110 CYS   C N   
1896 C CA  . CYS   B 104 ? 0.2199 0.2212 0.2158 0.0122  -0.0137 -0.0096 110 CYS   C CA  
1897 C C   . CYS   B 104 ? 0.2086 0.2099 0.2092 0.0115  -0.0167 -0.0090 110 CYS   C C   
1898 O O   . CYS   B 104 ? 0.2101 0.2074 0.2086 0.0121  -0.0206 -0.0095 110 CYS   C O   
1899 C CB  . CYS   B 104 ? 0.2217 0.2227 0.2202 0.0134  -0.0150 -0.0115 110 CYS   C CB  
1900 S SG  . CYS   B 104 ? 0.2471 0.2502 0.2457 0.0145  -0.0108 -0.0126 110 CYS   C SG  
1901 N N   . GLY   B 105 ? 0.2022 0.2076 0.2091 0.0100  -0.0149 -0.0082 111 GLY   C N   
1902 C CA  . GLY   B 105 ? 0.2100 0.2161 0.2226 0.0094  -0.0165 -0.0084 111 GLY   C CA  
1903 C C   . GLY   B 105 ? 0.2257 0.2311 0.2374 0.0089  -0.0156 -0.0074 111 GLY   C C   
1904 O O   . GLY   B 105 ? 0.2263 0.2331 0.2441 0.0083  -0.0156 -0.0081 111 GLY   C O   
1905 N N   . GLY   B 106 ? 0.2172 0.2204 0.2218 0.0088  -0.0144 -0.0059 112 GLY   C N   
1906 C CA  . GLY   B 106 ? 0.2177 0.2196 0.2212 0.0079  -0.0136 -0.0045 112 GLY   C CA  
1907 C C   . GLY   B 106 ? 0.2136 0.2199 0.2221 0.0062  -0.0105 -0.0047 112 GLY   C C   
1908 O O   . GLY   B 106 ? 0.2156 0.2254 0.2248 0.0053  -0.0082 -0.0046 112 GLY   C O   
1909 N N   . ILE   B 107 ? 0.2021 0.2078 0.2145 0.0056  -0.0108 -0.0052 113 ILE   C N   
1910 C CA  . ILE   B 107 ? 0.2029 0.2118 0.2188 0.0037  -0.0080 -0.0062 113 ILE   C CA  
1911 C C   . ILE   B 107 ? 0.1929 0.2017 0.2054 0.0020  -0.0062 -0.0043 113 ILE   C C   
1912 O O   . ILE   B 107 ? 0.2073 0.2127 0.2166 0.0020  -0.0070 -0.0027 113 ILE   C O   
1913 C CB  . ILE   B 107 ? 0.2381 0.2466 0.2607 0.0040  -0.0086 -0.0087 113 ILE   C CB  
1914 C CG1 . ILE   B 107 ? 0.2665 0.2779 0.2946 0.0045  -0.0087 -0.0107 113 ILE   C CG1 
1915 C CG2 . ILE   B 107 ? 0.2495 0.2588 0.2733 0.0020  -0.0058 -0.0100 113 ILE   C CG2 
1916 C CD1 . ILE   B 107 ? 0.3073 0.3189 0.3442 0.0054  -0.0091 -0.0136 113 ILE   C CD1 
1917 N N   . LEU   B 108 ? 0.1673 0.1795 0.1804 0.0000  -0.0041 -0.0044 114 LEU   C N   
1918 C CA  . LEU   B 108 ? 0.1725 0.1852 0.1843 -0.0022 -0.0028 -0.0030 114 LEU   C CA  
1919 C C   . LEU   B 108 ? 0.1852 0.1975 0.1989 -0.0040 -0.0022 -0.0052 114 LEU   C C   
1920 O O   . LEU   B 108 ? 0.1748 0.1890 0.1899 -0.0047 -0.0014 -0.0071 114 LEU   C O   
1921 C CB  . LEU   B 108 ? 0.1704 0.1870 0.1822 -0.0033 -0.0020 -0.0016 114 LEU   C CB  
1922 C CG  . LEU   B 108 ? 0.1877 0.2056 0.1999 -0.0060 -0.0014 -0.0002 114 LEU   C CG  
1923 C CD1 . LEU   B 108 ? 0.1779 0.1944 0.1891 -0.0064 -0.0007 0.0018  114 LEU   C CD1 
1924 C CD2 . LEU   B 108 ? 0.2034 0.2251 0.2176 -0.0069 -0.0017 0.0011  114 LEU   C CD2 
1925 N N   . ARG   B 109 ? 0.1953 0.2046 0.2088 -0.0049 -0.0025 -0.0051 115 ARG   C N   
1926 C CA  . ARG   B 109 ? 0.2068 0.2147 0.2217 -0.0065 -0.0016 -0.0081 115 ARG   C CA  
1927 C C   . ARG   B 109 ? 0.2044 0.2112 0.2172 -0.0093 -0.0017 -0.0070 115 ARG   C C   
1928 O O   . ARG   B 109 ? 0.2080 0.2136 0.2201 -0.0095 -0.0026 -0.0041 115 ARG   C O   
1929 C CB  . ARG   B 109 ? 0.2388 0.2428 0.2575 -0.0045 -0.0027 -0.0101 115 ARG   C CB  
1930 C CG  . ARG   B 109 ? 0.3211 0.3252 0.3434 -0.0015 -0.0039 -0.0109 115 ARG   C CG  
1931 C CD  . ARG   B 109 ? 0.3851 0.3848 0.4125 0.0004  -0.0061 -0.0124 115 ARG   C CD  
1932 N NE  . ARG   B 109 ? 0.4525 0.4523 0.4843 -0.0003 -0.0037 -0.0170 115 ARG   C NE  
1933 C CZ  . ARG   B 109 ? 0.4833 0.4858 0.5214 0.0007  -0.0018 -0.0208 115 ARG   C CZ  
1934 N NH1 . ARG   B 109 ? 0.4775 0.4822 0.5194 0.0027  -0.0032 -0.0204 115 ARG   C NH1 
1935 N NH2 . ARG   B 109 ? 0.4876 0.4905 0.5285 -0.0004 0.0016  -0.0255 115 ARG   C NH2 
1936 N N   . CYS   B 110 ? 0.2082 0.2149 0.2198 -0.0118 -0.0007 -0.0095 116 CYS   C N   
1937 C CA  . CYS   B 110 ? 0.2214 0.2259 0.2312 -0.0148 -0.0015 -0.0092 116 CYS   C CA  
1938 C C   . CYS   B 110 ? 0.2350 0.2349 0.2457 -0.0149 -0.0008 -0.0137 116 CYS   C C   
1939 O O   . CYS   B 110 ? 0.2228 0.2221 0.2371 -0.0124 0.0003  -0.0166 116 CYS   C O   
1940 C CB  . CYS   B 110 ? 0.2170 0.2242 0.2233 -0.0181 -0.0017 -0.0085 116 CYS   C CB  
1941 S SG  . CYS   B 110 ? 0.2095 0.2170 0.2119 -0.0198 0.0005  -0.0126 116 CYS   C SG  
1942 N N   . GLN   B 111 ? 0.2540 0.2509 0.2627 -0.0179 -0.0015 -0.0147 117 GLN   C N   
1943 C CA  . GLN   B 111 ? 0.2773 0.2693 0.2870 -0.0180 -0.0007 -0.0197 117 GLN   C CA  
1944 C C   . GLN   B 111 ? 0.2835 0.2768 0.2919 -0.0181 0.0029  -0.0250 117 GLN   C C   
1945 O O   . GLN   B 111 ? 0.3035 0.2937 0.3148 -0.0171 0.0048  -0.0301 117 GLN   C O   
1946 C CB  . GLN   B 111 ? 0.3210 0.3091 0.3276 -0.0217 -0.0025 -0.0199 117 GLN   C CB  
1947 C CG  . GLN   B 111 ? 0.3760 0.3660 0.3757 -0.0258 -0.0026 -0.0201 117 GLN   C CG  
1948 C CD  . GLN   B 111 ? 0.4666 0.4527 0.4637 -0.0296 -0.0054 -0.0199 117 GLN   C CD  
1949 O OE1 . GLN   B 111 ? 0.4848 0.4732 0.4812 -0.0321 -0.0082 -0.0157 117 GLN   C OE1 
1950 N NE2 . GLN   B 111 ? 0.4849 0.4648 0.4815 -0.0302 -0.0051 -0.0247 117 GLN   C NE2 
1951 N N   . HIS   B 112 ? 0.2614 0.2592 0.2659 -0.0194 0.0042  -0.0238 118 HIS   C N   
1952 C CA  . HIS   B 112 ? 0.2484 0.2476 0.2503 -0.0207 0.0082  -0.0281 118 HIS   C CA  
1953 C C   . HIS   B 112 ? 0.2588 0.2618 0.2668 -0.0175 0.0103  -0.0288 118 HIS   C C   
1954 O O   . HIS   B 112 ? 0.2722 0.2768 0.2799 -0.0184 0.0143  -0.0326 118 HIS   C O   
1955 C CB  . HIS   B 112 ? 0.2444 0.2451 0.2374 -0.0251 0.0078  -0.0262 118 HIS   C CB  
1956 C CG  . HIS   B 112 ? 0.2572 0.2543 0.2442 -0.0288 0.0049  -0.0255 118 HIS   C CG  
1957 N ND1 . HIS   B 112 ? 0.2511 0.2497 0.2378 -0.0300 0.0007  -0.0200 118 HIS   C ND1 
1958 C CD2 . HIS   B 112 ? 0.2786 0.2707 0.2606 -0.0316 0.0056  -0.0299 118 HIS   C CD2 
1959 C CE1 . HIS   B 112 ? 0.2718 0.2666 0.2540 -0.0335 -0.0016 -0.0207 118 HIS   C CE1 
1960 N NE2 . HIS   B 112 ? 0.2879 0.2782 0.2663 -0.0347 0.0010  -0.0266 118 HIS   C NE2 
1961 N N   . GLY   B 113 ? 0.2391 0.2436 0.2521 -0.0142 0.0077  -0.0250 119 GLY   C N   
1962 C CA  . GLY   B 113 ? 0.2220 0.2296 0.2408 -0.0113 0.0085  -0.0253 119 GLY   C CA  
1963 C C   . GLY   B 113 ? 0.2049 0.2152 0.2226 -0.0104 0.0060  -0.0203 119 GLY   C C   
1964 O O   . GLY   B 113 ? 0.2072 0.2169 0.2218 -0.0109 0.0037  -0.0166 119 GLY   C O   
1965 N N   . VAL   B 114 ? 0.1872 0.2006 0.2080 -0.0092 0.0068  -0.0205 120 VAL   C N   
1966 C CA  . VAL   B 114 ? 0.1988 0.2141 0.2190 -0.0080 0.0045  -0.0166 120 VAL   C CA  
1967 C C   . VAL   B 114 ? 0.2111 0.2281 0.2254 -0.0109 0.0042  -0.0139 120 VAL   C C   
1968 O O   . VAL   B 114 ? 0.2241 0.2422 0.2353 -0.0140 0.0062  -0.0150 120 VAL   C O   
1969 C CB  . VAL   B 114 ? 0.2123 0.2300 0.2384 -0.0061 0.0049  -0.0178 120 VAL   C CB  
1970 C CG1 . VAL   B 114 ? 0.2214 0.2403 0.2461 -0.0051 0.0024  -0.0144 120 VAL   C CG1 
1971 C CG2 . VAL   B 114 ? 0.2259 0.2417 0.2594 -0.0028 0.0035  -0.0199 120 VAL   C CG2 
1972 N N   . VAL   B 115 ? 0.1945 0.2117 0.2074 -0.0101 0.0018  -0.0103 121 VAL   C N   
1973 C CA  . VAL   B 115 ? 0.1893 0.2081 0.1991 -0.0123 0.0006  -0.0074 121 VAL   C CA  
1974 C C   . VAL   B 115 ? 0.1906 0.2113 0.2021 -0.0108 -0.0005 -0.0058 121 VAL   C C   
1975 O O   . VAL   B 115 ? 0.1828 0.2045 0.1925 -0.0130 -0.0012 -0.0045 121 VAL   C O   
1976 C CB  . VAL   B 115 ? 0.1948 0.2132 0.2043 -0.0123 -0.0010 -0.0049 121 VAL   C CB  
1977 C CG1 . VAL   B 115 ? 0.2069 0.2275 0.2160 -0.0138 -0.0029 -0.0020 121 VAL   C CG1 
1978 C CG2 . VAL   B 115 ? 0.2032 0.2190 0.2108 -0.0144 -0.0006 -0.0063 121 VAL   C CG2 
1979 N N   . GLY   B 116 ? 0.1889 0.2093 0.2032 -0.0074 -0.0011 -0.0059 122 GLY   C N   
1980 C CA  . GLY   B 116 ? 0.1913 0.2126 0.2071 -0.0057 -0.0024 -0.0048 122 GLY   C CA  
1981 C C   . GLY   B 116 ? 0.1819 0.2018 0.1989 -0.0022 -0.0034 -0.0052 122 GLY   C C   
1982 O O   . GLY   B 116 ? 0.1796 0.1975 0.1966 -0.0012 -0.0034 -0.0061 122 GLY   C O   
1983 N N   . ILE   B 117 ? 0.1776 0.1976 0.1950 -0.0006 -0.0048 -0.0046 123 ILE   C N   
1984 C CA  . ILE   B 117 ? 0.1908 0.2084 0.2073 0.0023  -0.0061 -0.0051 123 ILE   C CA  
1985 C C   . ILE   B 117 ? 0.1975 0.2150 0.2119 0.0038  -0.0061 -0.0043 123 ILE   C C   
1986 O O   . ILE   B 117 ? 0.2017 0.2210 0.2179 0.0034  -0.0061 -0.0036 123 ILE   C O   
1987 C CB  . ILE   B 117 ? 0.2025 0.2194 0.2220 0.0032  -0.0079 -0.0067 123 ILE   C CB  
1988 C CG1 . ILE   B 117 ? 0.2103 0.2289 0.2320 0.0021  -0.0084 -0.0063 123 ILE   C CG1 
1989 C CG2 . ILE   B 117 ? 0.2156 0.2327 0.2389 0.0026  -0.0075 -0.0083 123 ILE   C CG2 
1990 C CD1 . ILE   B 117 ? 0.2174 0.2351 0.2427 0.0029  -0.0106 -0.0076 123 ILE   C CD1 
1991 N N   . VAL   B 118 ? 0.1906 0.2055 0.2010 0.0056  -0.0062 -0.0044 124 VAL   C N   
1992 C CA  . VAL   B 118 ? 0.1894 0.2040 0.1972 0.0070  -0.0050 -0.0045 124 VAL   C CA  
1993 C C   . VAL   B 118 ? 0.1908 0.2051 0.2008 0.0084  -0.0067 -0.0059 124 VAL   C C   
1994 O O   . VAL   B 118 ? 0.1864 0.1987 0.1968 0.0089  -0.0093 -0.0069 124 VAL   C O   
1995 C CB  . VAL   B 118 ? 0.1899 0.2006 0.1907 0.0080  -0.0048 -0.0046 124 VAL   C CB  
1996 C CG1 . VAL   B 118 ? 0.2068 0.2173 0.2042 0.0095  -0.0026 -0.0056 124 VAL   C CG1 
1997 C CG2 . VAL   B 118 ? 0.1970 0.2074 0.1958 0.0064  -0.0034 -0.0026 124 VAL   C CG2 
1998 N N   . SER   B 119 ? 0.1979 0.2144 0.2108 0.0090  -0.0057 -0.0059 125 SER   C N   
1999 C CA  . SER   B 119 ? 0.1966 0.2123 0.2125 0.0102  -0.0076 -0.0071 125 SER   C CA  
2000 C C   . SER   B 119 ? 0.2296 0.2450 0.2456 0.0126  -0.0057 -0.0088 125 SER   C C   
2001 O O   . SER   B 119 ? 0.2455 0.2581 0.2612 0.0145  -0.0072 -0.0110 125 SER   C O   
2002 C CB  . SER   B 119 ? 0.2041 0.2221 0.2256 0.0082  -0.0091 -0.0052 125 SER   C CB  
2003 O OG  . SER   B 119 ? 0.2145 0.2310 0.2394 0.0091  -0.0115 -0.0058 125 SER   C OG  
2004 N N   . THR   B 120 ? 0.2286 0.2472 0.2460 0.0125  -0.0024 -0.0081 126 THR   C N   
2005 C CA  . THR   B 120 ? 0.2268 0.2464 0.2460 0.0149  0.0006  -0.0103 126 THR   C CA  
2006 C C   . THR   B 120 ? 0.2521 0.2727 0.2662 0.0144  0.0055  -0.0103 126 THR   C C   
2007 O O   . THR   B 120 ? 0.2408 0.2614 0.2514 0.0123  0.0057  -0.0080 126 THR   C O   
2008 C CB  . THR   B 120 ? 0.2288 0.2524 0.2589 0.0152  0.0000  -0.0094 126 THR   C CB  
2009 O OG1 . THR   B 120 ? 0.2312 0.2593 0.2649 0.0131  0.0014  -0.0067 126 THR   C OG1 
2010 C CG2 . THR   B 120 ? 0.2188 0.2409 0.2528 0.0145  -0.0050 -0.0082 126 THR   C CG2 
2011 N N   . GLY   B 121 ? 0.2730 0.2945 0.2871 0.0163  0.0096  -0.0129 127 GLY   C N   
2012 C CA  . GLY   B 121 ? 0.3008 0.3236 0.3102 0.0153  0.0151  -0.0127 127 GLY   C CA  
2013 C C   . GLY   B 121 ? 0.3246 0.3480 0.3332 0.0174  0.0205  -0.0167 127 GLY   C C   
2014 O O   . GLY   B 121 ? 0.3064 0.3289 0.3191 0.0201  0.0198  -0.0200 127 GLY   C O   
2015 N N   . GLY   B 122 ? 0.3649 0.3890 0.3672 0.0158  0.0261  -0.0165 128 GLY   C N   
2016 C CA  . GLY   B 122 ? 0.3840 0.4095 0.3848 0.0171  0.0333  -0.0204 128 GLY   C CA  
2017 C C   . GLY   B 122 ? 0.3910 0.4253 0.4047 0.0164  0.0386  -0.0195 128 GLY   C C   
2018 O O   . GLY   B 122 ? 0.3843 0.4229 0.4089 0.0155  0.0353  -0.0162 128 GLY   C O   
2019 N N   . ASN   B 123 ? 0.3934 0.4303 0.4062 0.0166  0.0470  -0.0225 129 ASN   C N   
2020 C CA  . ASN   B 123 ? 0.3855 0.4318 0.4127 0.0158  0.0525  -0.0218 129 ASN   C CA  
2021 C C   . ASN   B 123 ? 0.3403 0.3892 0.3681 0.0115  0.0515  -0.0158 129 ASN   C C   
2022 O O   . ASN   B 123 ? 0.3243 0.3806 0.3669 0.0107  0.0522  -0.0139 129 ASN   C O   
2023 C CB  . ASN   B 123 ? 0.4222 0.4741 0.4692 0.0191  0.0496  -0.0231 129 ASN   C CB  
2024 C CG  . ASN   B 123 ? 0.4731 0.5285 0.5294 0.0229  0.0555  -0.0292 129 ASN   C CG  
2025 O OD1 . ASN   B 123 ? 0.5058 0.5585 0.5519 0.0235  0.0621  -0.0337 129 ASN   C OD1 
2026 N ND2 . ASN   B 123 ? 0.4705 0.5315 0.5464 0.0254  0.0529  -0.0296 129 ASN   C ND2 
2027 N N   . GLY   B 124 ? 0.3157 0.3579 0.3282 0.0088  0.0493  -0.0130 130 GLY   C N   
2028 C CA  . GLY   B 124 ? 0.2928 0.3359 0.3049 0.0048  0.0479  -0.0077 130 GLY   C CA  
2029 C C   . GLY   B 124 ? 0.2672 0.3114 0.2880 0.0047  0.0403  -0.0048 130 GLY   C C   
2030 O O   . GLY   B 124 ? 0.2723 0.3183 0.2963 0.0016  0.0392  -0.0011 130 GLY   C O   
2031 N N   . LEU   B 125 ? 0.2477 0.2901 0.2714 0.0076  0.0350  -0.0065 131 LEU   C N   
2032 C CA  . LEU   B 125 ? 0.2417 0.2842 0.2710 0.0070  0.0281  -0.0040 131 LEU   C CA  
2033 C C   . LEU   B 125 ? 0.2477 0.2830 0.2670 0.0076  0.0228  -0.0042 131 LEU   C C   
2034 O O   . LEU   B 125 ? 0.2753 0.3059 0.2858 0.0093  0.0233  -0.0066 131 LEU   C O   
2035 C CB  . LEU   B 125 ? 0.2500 0.2972 0.2935 0.0093  0.0259  -0.0052 131 LEU   C CB  
2036 C CG  . LEU   B 125 ? 0.2832 0.3385 0.3407 0.0095  0.0305  -0.0057 131 LEU   C CG  
2037 C CD1 . LEU   B 125 ? 0.2938 0.3520 0.3646 0.0128  0.0279  -0.0076 131 LEU   C CD1 
2038 C CD2 . LEU   B 125 ? 0.2840 0.3432 0.3471 0.0057  0.0296  -0.0016 131 LEU   C CD2 
2039 N N   . VAL   B 126 ? 0.2111 0.2455 0.2318 0.0060  0.0180  -0.0017 132 VAL   C N   
2040 C CA  . VAL   B 126 ? 0.2155 0.2446 0.2301 0.0066  0.0134  -0.0021 132 VAL   C CA  
2041 C C   . VAL   B 126 ? 0.2142 0.2455 0.2366 0.0061  0.0092  -0.0012 132 VAL   C C   
2042 O O   . VAL   B 126 ? 0.1998 0.2346 0.2281 0.0041  0.0087  0.0009  132 VAL   C O   
2043 C CB  . VAL   B 126 ? 0.2347 0.2592 0.2405 0.0046  0.0123  -0.0003 132 VAL   C CB  
2044 C CG1 . VAL   B 126 ? 0.2423 0.2690 0.2514 0.0016  0.0128  0.0025  132 VAL   C CG1 
2045 C CG2 . VAL   B 126 ? 0.2387 0.2588 0.2413 0.0053  0.0075  -0.0010 132 VAL   C CG2 
2046 N N   . GLY   B 127 ? 0.2013 0.2302 0.2232 0.0077  0.0061  -0.0026 133 GLY   C N   
2047 C CA  . GLY   B 127 ? 0.1945 0.2244 0.2217 0.0067  0.0022  -0.0014 133 GLY   C CA  
2048 C C   . GLY   B 127 ? 0.1974 0.2239 0.2198 0.0056  -0.0005 -0.0013 133 GLY   C C   
2049 O O   . GLY   B 127 ? 0.1919 0.2150 0.2096 0.0070  -0.0010 -0.0029 133 GLY   C O   
2050 N N   . PHE   B 128 ? 0.1940 0.2214 0.2178 0.0029  -0.0023 0.0003  134 PHE   C N   
2051 C CA  . PHE   B 128 ? 0.1851 0.2102 0.2056 0.0015  -0.0037 0.0000  134 PHE   C CA  
2052 C C   . PHE   B 128 ? 0.1805 0.2060 0.2031 -0.0002 -0.0062 0.0008  134 PHE   C C   
2053 O O   . PHE   B 128 ? 0.1690 0.1962 0.1944 -0.0020 -0.0075 0.0026  134 PHE   C O   
2054 C CB  . PHE   B 128 ? 0.1770 0.2019 0.1954 -0.0009 -0.0029 0.0006  134 PHE   C CB  
2055 C CG  . PHE   B 128 ? 0.1808 0.2049 0.1969 -0.0002 -0.0008 0.0009  134 PHE   C CG  
2056 C CD1 . PHE   B 128 ? 0.1882 0.2089 0.2000 0.0010  -0.0007 0.0000  134 PHE   C CD1 
2057 C CD2 . PHE   B 128 ? 0.1761 0.2029 0.1949 -0.0013 0.0006  0.0025  134 PHE   C CD2 
2058 C CE1 . PHE   B 128 ? 0.1875 0.2066 0.1960 0.0010  0.0008  0.0010  134 PHE   C CE1 
2059 C CE2 . PHE   B 128 ? 0.1884 0.2145 0.2048 -0.0014 0.0030  0.0032  134 PHE   C CE2 
2060 C CZ  . PHE   B 128 ? 0.1888 0.2106 0.1992 -0.0004 0.0030  0.0026  134 PHE   C CZ  
2061 N N   . ALA   B 129 ? 0.1749 0.1985 0.1964 0.0000  -0.0072 -0.0003 135 ALA   C N   
2062 C CA  . ALA   B 129 ? 0.1746 0.1981 0.1970 -0.0024 -0.0090 0.0007  135 ALA   C CA  
2063 C C   . ALA   B 129 ? 0.1828 0.2065 0.2019 -0.0059 -0.0078 0.0008  135 ALA   C C   
2064 O O   . ALA   B 129 ? 0.1709 0.1941 0.1889 -0.0056 -0.0061 -0.0012 135 ALA   C O   
2065 C CB  . ALA   B 129 ? 0.1713 0.1931 0.1943 -0.0013 -0.0099 -0.0007 135 ALA   C CB  
2066 N N   . ASP   B 130 ? 0.1832 0.2074 0.2011 -0.0090 -0.0090 0.0028  136 ASP   C N   
2067 C CA  . ASP   B 130 ? 0.1888 0.2126 0.2022 -0.0127 -0.0078 0.0023  136 ASP   C CA  
2068 C C   . ASP   B 130 ? 0.1957 0.2187 0.2069 -0.0148 -0.0063 0.0011  136 ASP   C C   
2069 O O   . ASP   B 130 ? 0.1901 0.2128 0.2024 -0.0154 -0.0078 0.0024  136 ASP   C O   
2070 C CB  . ASP   B 130 ? 0.2139 0.2374 0.2253 -0.0161 -0.0105 0.0051  136 ASP   C CB  
2071 C CG  . ASP   B 130 ? 0.2680 0.2902 0.2731 -0.0202 -0.0094 0.0043  136 ASP   C CG  
2072 O OD1 . ASP   B 130 ? 0.2374 0.2595 0.2421 -0.0194 -0.0071 0.0020  136 ASP   C OD1 
2073 O OD2 . ASP   B 130 ? 0.2944 0.3149 0.2943 -0.0244 -0.0111 0.0059  136 ASP   C OD2 
2074 N N   . VAL   B 131 ? 0.1951 0.2180 0.2040 -0.0162 -0.0032 -0.0015 137 VAL   C N   
2075 C CA  . VAL   B 131 ? 0.1962 0.2193 0.2037 -0.0188 -0.0005 -0.0032 137 VAL   C CA  
2076 C C   . VAL   B 131 ? 0.2163 0.2384 0.2169 -0.0233 0.0018  -0.0044 137 VAL   C C   
2077 O O   . VAL   B 131 ? 0.2305 0.2530 0.2290 -0.0262 0.0052  -0.0062 137 VAL   C O   
2078 C CB  . VAL   B 131 ? 0.2006 0.2249 0.2138 -0.0159 0.0018  -0.0064 137 VAL   C CB  
2079 C CG1 . VAL   B 131 ? 0.2049 0.2292 0.2229 -0.0120 -0.0010 -0.0055 137 VAL   C CG1 
2080 C CG2 . VAL   B 131 ? 0.1876 0.2113 0.2015 -0.0143 0.0034  -0.0092 137 VAL   C CG2 
2081 N N   . ARG   B 132 ? 0.2074 0.2280 0.2043 -0.0244 0.0002  -0.0036 138 ARG   C N   
2082 C CA  . ARG   B 132 ? 0.2054 0.2240 0.1947 -0.0286 0.0019  -0.0053 138 ARG   C CA  
2083 C C   . ARG   B 132 ? 0.2107 0.2276 0.1916 -0.0342 0.0016  -0.0035 138 ARG   C C   
2084 O O   . ARG   B 132 ? 0.2412 0.2563 0.2145 -0.0382 0.0047  -0.0060 138 ARG   C O   
2085 C CB  . ARG   B 132 ? 0.1824 0.1996 0.1705 -0.0287 -0.0008 -0.0043 138 ARG   C CB  
2086 C CG  . ARG   B 132 ? 0.1458 0.1636 0.1400 -0.0245 0.0002  -0.0062 138 ARG   C CG  
2087 C CD  . ARG   B 132 ? 0.1922 0.2089 0.1857 -0.0253 -0.0026 -0.0045 138 ARG   C CD  
2088 N NE  . ARG   B 132 ? 0.1991 0.2180 0.1966 -0.0240 -0.0062 -0.0004 138 ARG   C NE  
2089 C CZ  . ARG   B 132 ? 0.2127 0.2322 0.2129 -0.0242 -0.0087 0.0017  138 ARG   C CZ  
2090 N NH1 . ARG   B 132 ? 0.1919 0.2096 0.1902 -0.0259 -0.0087 0.0005  138 ARG   C NH1 
2091 N NH2 . ARG   B 132 ? 0.2049 0.2271 0.2107 -0.0225 -0.0111 0.0047  138 ARG   C NH2 
2092 N N   . ASP   B 133 ? 0.1971 0.2139 0.1786 -0.0349 -0.0023 0.0009  139 ASP   C N   
2093 C CA  . ASP   B 133 ? 0.2136 0.2279 0.1865 -0.0407 -0.0035 0.0037  139 ASP   C CA  
2094 C C   . ASP   B 133 ? 0.2297 0.2450 0.2018 -0.0426 0.0011  0.0023  139 ASP   C C   
2095 O O   . ASP   B 133 ? 0.2567 0.2696 0.2197 -0.0485 0.0016  0.0042  139 ASP   C O   
2096 C CB  . ASP   B 133 ? 0.2401 0.2530 0.2148 -0.0408 -0.0104 0.0093  139 ASP   C CB  
2097 C CG  . ASP   B 133 ? 0.2855 0.3006 0.2701 -0.0362 -0.0113 0.0102  139 ASP   C CG  
2098 O OD1 . ASP   B 133 ? 0.2770 0.2948 0.2688 -0.0312 -0.0090 0.0072  139 ASP   C OD1 
2099 O OD2 . ASP   B 133 ? 0.2994 0.3127 0.2840 -0.0379 -0.0148 0.0139  139 ASP   C OD2 
2100 N N   . LEU   B 134 ? 0.2159 0.2346 0.1973 -0.0383 0.0044  -0.0007 140 LEU   C N   
2101 C CA  . LEU   B 134 ? 0.2329 0.2537 0.2167 -0.0398 0.0087  -0.0021 140 LEU   C CA  
2102 C C   . LEU   B 134 ? 0.2416 0.2634 0.2219 -0.0425 0.0158  -0.0071 140 LEU   C C   
2103 O O   . LEU   B 134 ? 0.2516 0.2765 0.2403 -0.0391 0.0197  -0.0116 140 LEU   C O   
2104 C CB  . LEU   B 134 ? 0.2376 0.2613 0.2337 -0.0341 0.0080  -0.0030 140 LEU   C CB  
2105 C CG  . LEU   B 134 ? 0.2534 0.2759 0.2531 -0.0310 0.0017  0.0009  140 LEU   C CG  
2106 C CD1 . LEU   B 134 ? 0.2581 0.2825 0.2677 -0.0256 0.0012  -0.0008 140 LEU   C CD1 
2107 C CD2 . LEU   B 134 ? 0.2702 0.2903 0.2660 -0.0351 -0.0013 0.0055  140 LEU   C CD2 
2108 N N   . LEU   B 135 ? 0.2395 0.2583 0.2072 -0.0488 0.0174  -0.0067 141 LEU   C N   
2109 C CA  . LEU   B 135 ? 0.2533 0.2723 0.2156 -0.0517 0.0246  -0.0123 141 LEU   C CA  
2110 C C   . LEU   B 135 ? 0.2741 0.2977 0.2433 -0.0522 0.0319  -0.0159 141 LEU   C C   
2111 O O   . LEU   B 135 ? 0.2963 0.3219 0.2689 -0.0512 0.0381  -0.0221 141 LEU   C O   
2112 C CB  . LEU   B 135 ? 0.2531 0.2670 0.1981 -0.0591 0.0245  -0.0108 141 LEU   C CB  
2113 C CG  . LEU   B 135 ? 0.2560 0.2654 0.1946 -0.0597 0.0163  -0.0064 141 LEU   C CG  
2114 C CD1 . LEU   B 135 ? 0.2768 0.2805 0.1973 -0.0674 0.0162  -0.0058 141 LEU   C CD1 
2115 C CD2 . LEU   B 135 ? 0.2678 0.2780 0.2143 -0.0537 0.0139  -0.0087 141 LEU   C CD2 
2116 N N   . TRP   B 136 ? 0.2781 0.3033 0.2505 -0.0538 0.0312  -0.0122 142 TRP   C N   
2117 C CA  . TRP   B 136 ? 0.2844 0.3146 0.2650 -0.0548 0.0377  -0.0149 142 TRP   C CA  
2118 C C   . TRP   B 136 ? 0.2857 0.3207 0.2834 -0.0478 0.0389  -0.0193 142 TRP   C C   
2119 O O   . TRP   B 136 ? 0.2802 0.3200 0.2869 -0.0481 0.0448  -0.0229 142 TRP   C O   
2120 C CB  . TRP   B 136 ? 0.2868 0.3168 0.2675 -0.0580 0.0351  -0.0092 142 TRP   C CB  
2121 C CG  . TRP   B 136 ? 0.2813 0.3097 0.2681 -0.0533 0.0262  -0.0046 142 TRP   C CG  
2122 C CD1 . TRP   B 136 ? 0.2881 0.3116 0.2678 -0.0538 0.0190  0.0006  142 TRP   C CD1 
2123 C CD2 . TRP   B 136 ? 0.2654 0.2969 0.2667 -0.0475 0.0239  -0.0052 142 TRP   C CD2 
2124 N NE1 . TRP   B 136 ? 0.2853 0.3091 0.2746 -0.0485 0.0132  0.0027  142 TRP   C NE1 
2125 C CE2 . TRP   B 136 ? 0.2737 0.3018 0.2750 -0.0448 0.0160  -0.0007 142 TRP   C CE2 
2126 C CE3 . TRP   B 136 ? 0.2633 0.2999 0.2779 -0.0446 0.0274  -0.0091 142 TRP   C CE3 
2127 C CZ2 . TRP   B 136 ? 0.2707 0.2999 0.2827 -0.0395 0.0120  -0.0005 142 TRP   C CZ2 
2128 C CZ3 . TRP   B 136 ? 0.2639 0.3013 0.2892 -0.0396 0.0224  -0.0082 142 TRP   C CZ3 
2129 C CH2 . TRP   B 136 ? 0.2654 0.2988 0.2884 -0.0371 0.0150  -0.0042 142 TRP   C CH2 
2130 N N   . LEU   B 137 ? 0.2819 0.3156 0.2845 -0.0417 0.0331  -0.0188 143 LEU   C N   
2131 C CA  . LEU   B 137 ? 0.2888 0.3257 0.3059 -0.0354 0.0331  -0.0224 143 LEU   C CA  
2132 C C   . LEU   B 137 ? 0.3277 0.3668 0.3487 -0.0352 0.0401  -0.0293 143 LEU   C C   
2133 O O   . LEU   B 137 ? 0.3235 0.3665 0.3584 -0.0316 0.0420  -0.0328 143 LEU   C O   
2134 C CB  . LEU   B 137 ? 0.2703 0.3044 0.2886 -0.0301 0.0264  -0.0206 143 LEU   C CB  
2135 C CG  . LEU   B 137 ? 0.2665 0.2995 0.2863 -0.0281 0.0199  -0.0155 143 LEU   C CG  
2136 C CD1 . LEU   B 137 ? 0.2565 0.2869 0.2758 -0.0236 0.0149  -0.0143 143 LEU   C CD1 
2137 C CD2 . LEU   B 137 ? 0.2658 0.3021 0.2972 -0.0260 0.0196  -0.0161 143 LEU   C CD2 
2138 N N   . ASP   B 138 ? 0.3645 0.4006 0.3738 -0.0387 0.0434  -0.0314 144 ASP   C N   
2139 C CA  . ASP   B 138 ? 0.4146 0.4514 0.4255 -0.0388 0.0501  -0.0386 144 ASP   C CA  
2140 C C   . ASP   B 138 ? 0.4610 0.5018 0.4725 -0.0434 0.0596  -0.0428 144 ASP   C C   
2141 O O   . ASP   B 138 ? 0.4721 0.5133 0.4841 -0.0438 0.0661  -0.0495 144 ASP   C O   
2142 C CB  . ASP   B 138 ? 0.4445 0.4754 0.4407 -0.0413 0.0493  -0.0393 144 ASP   C CB  
2143 C CG  . ASP   B 138 ? 0.5097 0.5373 0.5075 -0.0366 0.0423  -0.0375 144 ASP   C CG  
2144 O OD1 . ASP   B 138 ? 0.5266 0.5560 0.5374 -0.0308 0.0401  -0.0384 144 ASP   C OD1 
2145 O OD2 . ASP   B 138 ? 0.5533 0.5764 0.5394 -0.0390 0.0388  -0.0351 144 ASP   C OD2 
2146 N N   . GLU   B 139 ? 0.4863 0.5296 0.4969 -0.0473 0.0608  -0.0392 145 GLU   C N   
2147 C CA  . GLU   B 139 ? 0.5219 0.5695 0.5330 -0.0525 0.0705  -0.0427 145 GLU   C CA  
2148 C C   . GLU   B 139 ? 0.5414 0.5946 0.5659 -0.0522 0.0702  -0.0400 145 GLU   C C   
2149 O O   . GLU   B 139 ? 0.5555 0.6146 0.5881 -0.0547 0.0784  -0.0436 145 GLU   C O   
2150 C CB  . GLU   B 139 ? 0.5704 0.6133 0.5598 -0.0610 0.0731  -0.0402 145 GLU   C CB  
2151 C CG  . GLU   B 139 ? 0.6493 0.6885 0.6300 -0.0638 0.0652  -0.0312 145 GLU   C CG  
2152 C CD  . GLU   B 139 ? 0.7750 0.8067 0.7340 -0.0696 0.0624  -0.0278 145 GLU   C CD  
2153 O OE1 . GLU   B 139 ? 0.8078 0.8368 0.7562 -0.0757 0.0607  -0.0219 145 GLU   C OE1 
2154 O OE2 . GLU   B 139 ? 0.8123 0.8405 0.7651 -0.0682 0.0614  -0.0308 145 GLU   C OE2 
2155 N N1  . A1B2E C .   ? 0.3163 0.3168 0.3421 -0.0143 0.0298  0.0197  201 A1B2E A N1  
2156 C C4  . A1B2E C .   ? 0.3138 0.3087 0.3293 -0.0110 0.0277  0.0235  201 A1B2E A C4  
2157 C C5  . A1B2E C .   ? 0.3382 0.3406 0.3663 -0.0154 0.0364  0.0214  201 A1B2E A C5  
2158 C C6  . A1B2E C .   ? 0.3617 0.3675 0.3807 -0.0123 0.0362  0.0213  201 A1B2E A C6  
2159 C C7  . A1B2E C .   ? 0.3682 0.3799 0.3760 -0.0079 0.0324  0.0176  201 A1B2E A C7  
2160 C C8  . A1B2E C .   ? 0.3616 0.3756 0.3629 -0.0053 0.0282  0.0146  201 A1B2E A C8  
2161 C C10 . A1B2E C .   ? 0.3578 0.3696 0.3643 -0.0070 0.0197  0.0116  201 A1B2E A C10 
2162 C C13 . A1B2E C .   ? 0.2965 0.3012 0.3326 -0.0167 0.0265  0.0138  201 A1B2E A C13 
2163 O O1  . A1B2E C .   ? 0.3289 0.3200 0.3345 -0.0081 0.0302  0.0280  201 A1B2E A O1  
2164 C C3  . A1B2E C .   ? 0.3083 0.3015 0.3248 -0.0104 0.0222  0.0219  201 A1B2E A C3  
2165 C C2  . A1B2E C .   ? 0.2970 0.2923 0.3250 -0.0136 0.0214  0.0175  201 A1B2E A C2  
2166 C C1  . A1B2E C .   ? 0.2921 0.2948 0.3251 -0.0150 0.0209  0.0124  201 A1B2E A C1  
2167 C C   . A1B2E C .   ? 0.2800 0.2849 0.3221 -0.0168 0.0188  0.0072  201 A1B2E A C   
2168 O O   . A1B2E C .   ? 0.2739 0.2769 0.3247 -0.0194 0.0210  0.0063  201 A1B2E A O   
2169 N N   . A1B2E C .   ? 0.2710 0.2789 0.3107 -0.0149 0.0146  0.0036  201 A1B2E A N   
2170 C C12 . A1B2E C .   ? 0.3599 0.3694 0.3737 -0.0101 0.0298  0.0172  201 A1B2E A C12 
2171 O O2  . A1B2E C .   ? 0.3860 0.3960 0.3947 -0.0085 0.0400  0.0218  201 A1B2E A O2  
2172 N N2  . A1B2E C .   ? 0.3798 0.3857 0.3960 -0.0115 0.0425  0.0243  201 A1B2E A N2  
2173 C C11 . A1B2E C .   ? 0.3583 0.3681 0.3708 -0.0094 0.0232  0.0141  201 A1B2E A C11 
2174 C C9  . A1B2E C .   ? 0.3614 0.3751 0.3625 -0.0051 0.0218  0.0116  201 A1B2E A C9  
2180 N N1  . A1B2E F .   ? 0.3317 0.3331 0.3399 0.0233  -0.0050 -0.0239 201 A1B2E C N1  
2181 C C4  . A1B2E F .   ? 0.3342 0.3302 0.3349 0.0228  -0.0087 -0.0248 201 A1B2E C C4  
2182 C C5  . A1B2E F .   ? 0.3479 0.3502 0.3540 0.0251  0.0008  -0.0271 201 A1B2E C C5  
2183 C C6  . A1B2E F .   ? 0.3694 0.3727 0.3666 0.0236  0.0052  -0.0260 201 A1B2E C C6  
2184 C C7  . A1B2E F .   ? 0.3727 0.3784 0.3604 0.0198  0.0096  -0.0216 201 A1B2E C C7  
2185 C C8  . A1B2E F .   ? 0.3679 0.3742 0.3512 0.0172  0.0101  -0.0179 201 A1B2E C C8  
2186 C C10 . A1B2E F .   ? 0.3592 0.3661 0.3529 0.0165  0.0010  -0.0149 201 A1B2E C C10 
2187 C C13 . A1B2E F .   ? 0.3047 0.3108 0.3236 0.0221  -0.0065 -0.0203 201 A1B2E C C13 
2188 O O1  . A1B2E F .   ? 0.3499 0.3412 0.3403 0.0235  -0.0078 -0.0275 201 A1B2E C O1  
2189 C C3  . A1B2E F .   ? 0.3139 0.3096 0.3192 0.0210  -0.0141 -0.0222 201 A1B2E C C3  
2190 C C2  . A1B2E F .   ? 0.2965 0.2963 0.3128 0.0202  -0.0150 -0.0196 201 A1B2E C C2  
2191 C C1  . A1B2E F .   ? 0.2937 0.2992 0.3132 0.0195  -0.0111 -0.0173 201 A1B2E C C1  
2192 C C   . A1B2E F .   ? 0.2785 0.2870 0.3072 0.0180  -0.0132 -0.0142 201 A1B2E C C   
2193 O O   . A1B2E F .   ? 0.2683 0.2758 0.3034 0.0194  -0.0150 -0.0150 201 A1B2E C O   
2194 N N   . A1B2E F .   ? 0.2588 0.2703 0.2877 0.0151  -0.0132 -0.0109 201 A1B2E C N   
2195 C C12 . A1B2E F .   ? 0.3652 0.3706 0.3605 0.0207  0.0045  -0.0214 201 A1B2E C C12 
2196 O O2  . A1B2E F .   ? 0.3817 0.3860 0.3662 0.0218  0.0139  -0.0260 201 A1B2E C O2  
2197 N N2  . A1B2E F .   ? 0.3809 0.3835 0.3719 0.0244  0.0107  -0.0291 201 A1B2E C N2  
2198 C C11 . A1B2E F .   ? 0.3566 0.3627 0.3543 0.0188  0.0003  -0.0179 201 A1B2E C C11 
2199 C C9  . A1B2E F .   ? 0.3645 0.3712 0.3513 0.0158  0.0054  -0.0147 201 A1B2E C C9  
# 
