data_7I5V
# 
_entry.id   7I5V 
# 
_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   7I5V         pdb_00007i5v 10.2210/pdb7i5v/pdb 
WWPDB D_1001408354 ?            ?                   
# 
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                        7I5V 
_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-[(2-bromo-4,5-difluorophenyl)acetyl]piperidine-3-carboxamide' 361.182   2   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                            65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                  78.133    2   ?         ? ? ? 
5 water       nat water                                                                 18.015    297 ?         ? ? ? 
# 
_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-[(2-bromo-4,5-difluorophenyl)acetyl]piperidine-3-carboxamide' A1B4B 
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 
A1B4B non-polymer         . '(3S)-1-[(2-bromo-4,5-difluorophenyl)acetyl]piperidine-3-carboxamide' ? 'C14 H15 Br F2 N2 O2' 361.182 
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        A1B4B 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B4B 
_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 A1B4B 1   201 201 A1B4B LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 6   DMS   DMS A . 
F 2 A1B4B 1   201 201 A1B4B LIG C . 
G 3 ZN    1   202 1   ZN    ZN  C . 
H 4 DMS   1   203 2   DMS   DMS C . 
I 5 HOH   1   301 5   HOH   HOH A . 
I 5 HOH   2   302 95  HOH   HOH A . 
I 5 HOH   3   303 103 HOH   HOH A . 
I 5 HOH   4   304 251 HOH   HOH A . 
I 5 HOH   5   305 295 HOH   HOH A . 
I 5 HOH   6   306 306 HOH   HOH A . 
I 5 HOH   7   307 152 HOH   HOH A . 
I 5 HOH   8   308 294 HOH   HOH A . 
I 5 HOH   9   309 61  HOH   HOH A . 
I 5 HOH   10  310 148 HOH   HOH A . 
I 5 HOH   11  311 160 HOH   HOH A . 
I 5 HOH   12  312 64  HOH   HOH A . 
I 5 HOH   13  313 66  HOH   HOH A . 
I 5 HOH   14  314 273 HOH   HOH A . 
I 5 HOH   15  315 227 HOH   HOH A . 
I 5 HOH   16  316 84  HOH   HOH A . 
I 5 HOH   17  317 183 HOH   HOH A . 
I 5 HOH   18  318 63  HOH   HOH A . 
I 5 HOH   19  319 93  HOH   HOH A . 
I 5 HOH   20  320 190 HOH   HOH A . 
I 5 HOH   21  321 59  HOH   HOH A . 
I 5 HOH   22  322 23  HOH   HOH A . 
I 5 HOH   23  323 7   HOH   HOH A . 
I 5 HOH   24  324 307 HOH   HOH A . 
I 5 HOH   25  325 312 HOH   HOH A . 
I 5 HOH   26  326 280 HOH   HOH A . 
I 5 HOH   27  327 56  HOH   HOH A . 
I 5 HOH   28  328 116 HOH   HOH A . 
I 5 HOH   29  329 62  HOH   HOH A . 
I 5 HOH   30  330 22  HOH   HOH A . 
I 5 HOH   31  331 13  HOH   HOH A . 
I 5 HOH   32  332 14  HOH   HOH A . 
I 5 HOH   33  333 278 HOH   HOH A . 
I 5 HOH   34  334 239 HOH   HOH A . 
I 5 HOH   35  335 238 HOH   HOH A . 
I 5 HOH   36  336 33  HOH   HOH A . 
I 5 HOH   37  337 301 HOH   HOH A . 
I 5 HOH   38  338 21  HOH   HOH A . 
I 5 HOH   39  339 236 HOH   HOH A . 
I 5 HOH   40  340 48  HOH   HOH A . 
I 5 HOH   41  341 63  HOH   HOH A . 
I 5 HOH   42  342 49  HOH   HOH A . 
I 5 HOH   43  343 248 HOH   HOH A . 
I 5 HOH   44  344 247 HOH   HOH A . 
I 5 HOH   45  345 263 HOH   HOH A . 
I 5 HOH   46  346 241 HOH   HOH A . 
I 5 HOH   47  347 171 HOH   HOH A . 
I 5 HOH   48  348 71  HOH   HOH A . 
I 5 HOH   49  349 287 HOH   HOH A . 
I 5 HOH   50  350 176 HOH   HOH A . 
I 5 HOH   51  351 119 HOH   HOH A . 
I 5 HOH   52  352 269 HOH   HOH A . 
I 5 HOH   53  353 72  HOH   HOH A . 
I 5 HOH   54  354 88  HOH   HOH A . 
I 5 HOH   55  355 275 HOH   HOH A . 
I 5 HOH   56  356 270 HOH   HOH A . 
I 5 HOH   57  357 299 HOH   HOH A . 
I 5 HOH   58  358 128 HOH   HOH A . 
I 5 HOH   59  359 114 HOH   HOH A . 
I 5 HOH   60  360 99  HOH   HOH A . 
I 5 HOH   61  361 111 HOH   HOH A . 
I 5 HOH   62  362 19  HOH   HOH A . 
I 5 HOH   63  363 70  HOH   HOH A . 
I 5 HOH   64  364 149 HOH   HOH A . 
I 5 HOH   65  365 242 HOH   HOH A . 
I 5 HOH   66  366 66  HOH   HOH A . 
I 5 HOH   67  367 10  HOH   HOH A . 
I 5 HOH   68  368 228 HOH   HOH A . 
I 5 HOH   69  369 53  HOH   HOH A . 
I 5 HOH   70  370 296 HOH   HOH A . 
I 5 HOH   71  371 237 HOH   HOH A . 
I 5 HOH   72  372 245 HOH   HOH A . 
I 5 HOH   73  373 75  HOH   HOH A . 
I 5 HOH   74  374 115 HOH   HOH A . 
I 5 HOH   75  375 107 HOH   HOH A . 
I 5 HOH   76  376 115 HOH   HOH A . 
I 5 HOH   77  377 297 HOH   HOH A . 
I 5 HOH   78  378 268 HOH   HOH A . 
I 5 HOH   79  379 102 HOH   HOH A . 
I 5 HOH   80  380 19  HOH   HOH A . 
I 5 HOH   81  381 165 HOH   HOH A . 
I 5 HOH   82  382 26  HOH   HOH A . 
I 5 HOH   83  383 91  HOH   HOH A . 
I 5 HOH   84  384 259 HOH   HOH A . 
I 5 HOH   85  385 23  HOH   HOH A . 
I 5 HOH   86  386 85  HOH   HOH A . 
I 5 HOH   87  387 38  HOH   HOH A . 
I 5 HOH   88  388 256 HOH   HOH A . 
I 5 HOH   89  389 73  HOH   HOH A . 
I 5 HOH   90  390 47  HOH   HOH A . 
I 5 HOH   91  391 150 HOH   HOH A . 
I 5 HOH   92  392 254 HOH   HOH A . 
I 5 HOH   93  393 12  HOH   HOH A . 
I 5 HOH   94  394 113 HOH   HOH A . 
I 5 HOH   95  395 157 HOH   HOH A . 
I 5 HOH   96  396 14  HOH   HOH A . 
I 5 HOH   97  397 92  HOH   HOH A . 
I 5 HOH   98  398 262 HOH   HOH A . 
I 5 HOH   99  399 96  HOH   HOH A . 
I 5 HOH   100 400 101 HOH   HOH A . 
I 5 HOH   101 401 240 HOH   HOH A . 
I 5 HOH   102 402 197 HOH   HOH A . 
I 5 HOH   103 403 85  HOH   HOH A . 
I 5 HOH   104 404 232 HOH   HOH A . 
I 5 HOH   105 405 12  HOH   HOH A . 
I 5 HOH   106 406 304 HOH   HOH A . 
I 5 HOH   107 407 52  HOH   HOH A . 
I 5 HOH   108 408 49  HOH   HOH A . 
I 5 HOH   109 409 290 HOH   HOH A . 
I 5 HOH   110 410 35  HOH   HOH A . 
I 5 HOH   111 411 112 HOH   HOH A . 
I 5 HOH   112 412 40  HOH   HOH A . 
I 5 HOH   113 413 125 HOH   HOH A . 
I 5 HOH   114 414 102 HOH   HOH A . 
I 5 HOH   115 415 142 HOH   HOH A . 
I 5 HOH   116 416 144 HOH   HOH A . 
I 5 HOH   117 417 16  HOH   HOH A . 
I 5 HOH   118 418 151 HOH   HOH A . 
I 5 HOH   119 419 147 HOH   HOH A . 
I 5 HOH   120 420 77  HOH   HOH A . 
I 5 HOH   121 421 101 HOH   HOH A . 
I 5 HOH   122 422 15  HOH   HOH A . 
I 5 HOH   123 423 208 HOH   HOH A . 
I 5 HOH   124 424 100 HOH   HOH A . 
I 5 HOH   125 425 202 HOH   HOH A . 
I 5 HOH   126 426 154 HOH   HOH A . 
I 5 HOH   127 427 177 HOH   HOH A . 
I 5 HOH   128 428 158 HOH   HOH A . 
I 5 HOH   129 429 150 HOH   HOH A . 
I 5 HOH   130 430 136 HOH   HOH A . 
I 5 HOH   131 431 57  HOH   HOH A . 
I 5 HOH   132 432 279 HOH   HOH A . 
I 5 HOH   133 433 172 HOH   HOH A . 
I 5 HOH   134 434 138 HOH   HOH A . 
I 5 HOH   135 435 82  HOH   HOH A . 
I 5 HOH   136 436 24  HOH   HOH A . 
I 5 HOH   137 437 159 HOH   HOH A . 
I 5 HOH   138 438 264 HOH   HOH A . 
I 5 HOH   139 439 129 HOH   HOH A . 
I 5 HOH   140 440 140 HOH   HOH A . 
I 5 HOH   141 441 216 HOH   HOH A . 
I 5 HOH   142 442 132 HOH   HOH A . 
I 5 HOH   143 443 221 HOH   HOH A . 
I 5 HOH   144 444 164 HOH   HOH A . 
I 5 HOH   145 445 277 HOH   HOH A . 
I 5 HOH   146 446 187 HOH   HOH A . 
I 5 HOH   147 447 82  HOH   HOH A . 
I 5 HOH   148 448 181 HOH   HOH A . 
I 5 HOH   149 449 226 HOH   HOH A . 
I 5 HOH   150 450 99  HOH   HOH A . 
I 5 HOH   151 451 206 HOH   HOH A . 
I 5 HOH   152 452 224 HOH   HOH A . 
J 5 HOH   1   301 120 HOH   HOH C . 
J 5 HOH   2   302 313 HOH   HOH C . 
J 5 HOH   3   303 137 HOH   HOH C . 
J 5 HOH   4   304 78  HOH   HOH C . 
J 5 HOH   5   305 174 HOH   HOH C . 
J 5 HOH   6   306 2   HOH   HOH C . 
J 5 HOH   7   307 8   HOH   HOH C . 
J 5 HOH   8   308 51  HOH   HOH C . 
J 5 HOH   9   309 103 HOH   HOH C . 
J 5 HOH   10  310 257 HOH   HOH C . 
J 5 HOH   11  311 33  HOH   HOH C . 
J 5 HOH   12  312 281 HOH   HOH C . 
J 5 HOH   13  313 298 HOH   HOH C . 
J 5 HOH   14  314 230 HOH   HOH C . 
J 5 HOH   15  315 97  HOH   HOH C . 
J 5 HOH   16  316 289 HOH   HOH C . 
J 5 HOH   17  317 111 HOH   HOH C . 
J 5 HOH   18  318 284 HOH   HOH C . 
J 5 HOH   19  319 43  HOH   HOH C . 
J 5 HOH   20  320 50  HOH   HOH C . 
J 5 HOH   21  321 123 HOH   HOH C . 
J 5 HOH   22  322 283 HOH   HOH C . 
J 5 HOH   23  323 311 HOH   HOH C . 
J 5 HOH   24  324 28  HOH   HOH C . 
J 5 HOH   25  325 246 HOH   HOH C . 
J 5 HOH   26  326 70  HOH   HOH C . 
J 5 HOH   27  327 69  HOH   HOH C . 
J 5 HOH   28  328 260 HOH   HOH C . 
J 5 HOH   29  329 286 HOH   HOH C . 
J 5 HOH   30  330 130 HOH   HOH C . 
J 5 HOH   31  331 20  HOH   HOH C . 
J 5 HOH   32  332 122 HOH   HOH C . 
J 5 HOH   33  333 65  HOH   HOH C . 
J 5 HOH   34  334 229 HOH   HOH C . 
J 5 HOH   35  335 109 HOH   HOH C . 
J 5 HOH   36  336 124 HOH   HOH C . 
J 5 HOH   37  337 244 HOH   HOH C . 
J 5 HOH   38  338 39  HOH   HOH C . 
J 5 HOH   39  339 13  HOH   HOH C . 
J 5 HOH   40  340 261 HOH   HOH C . 
J 5 HOH   41  341 255 HOH   HOH C . 
J 5 HOH   42  342 31  HOH   HOH C . 
J 5 HOH   43  343 11  HOH   HOH C . 
J 5 HOH   44  344 274 HOH   HOH C . 
J 5 HOH   45  345 83  HOH   HOH C . 
J 5 HOH   46  346 30  HOH   HOH C . 
J 5 HOH   47  347 204 HOH   HOH C . 
J 5 HOH   48  348 98  HOH   HOH C . 
J 5 HOH   49  349 231 HOH   HOH C . 
J 5 HOH   50  350 80  HOH   HOH C . 
J 5 HOH   51  351 249 HOH   HOH C . 
J 5 HOH   52  352 288 HOH   HOH C . 
J 5 HOH   53  353 91  HOH   HOH C . 
J 5 HOH   54  354 252 HOH   HOH C . 
J 5 HOH   55  355 310 HOH   HOH C . 
J 5 HOH   56  356 29  HOH   HOH C . 
J 5 HOH   57  357 4   HOH   HOH C . 
J 5 HOH   58  358 110 HOH   HOH C . 
J 5 HOH   59  359 155 HOH   HOH C . 
J 5 HOH   60  360 37  HOH   HOH C . 
J 5 HOH   61  361 156 HOH   HOH C . 
J 5 HOH   62  362 67  HOH   HOH C . 
J 5 HOH   63  363 71  HOH   HOH C . 
J 5 HOH   64  364 38  HOH   HOH C . 
J 5 HOH   65  365 250 HOH   HOH C . 
J 5 HOH   66  366 157 HOH   HOH C . 
J 5 HOH   67  367 153 HOH   HOH C . 
J 5 HOH   68  368 1   HOH   HOH C . 
J 5 HOH   69  369 303 HOH   HOH C . 
J 5 HOH   70  370 285 HOH   HOH C . 
J 5 HOH   71  371 16  HOH   HOH C . 
J 5 HOH   72  372 79  HOH   HOH C . 
J 5 HOH   73  373 309 HOH   HOH C . 
J 5 HOH   74  374 205 HOH   HOH C . 
J 5 HOH   75  375 7   HOH   HOH C . 
J 5 HOH   76  376 54  HOH   HOH C . 
J 5 HOH   77  377 271 HOH   HOH C . 
J 5 HOH   78  378 272 HOH   HOH C . 
J 5 HOH   79  379 64  HOH   HOH C . 
J 5 HOH   80  380 108 HOH   HOH C . 
J 5 HOH   81  381 37  HOH   HOH C . 
J 5 HOH   82  382 293 HOH   HOH C . 
J 5 HOH   83  383 11  HOH   HOH C . 
J 5 HOH   84  384 62  HOH   HOH C . 
J 5 HOH   85  385 83  HOH   HOH C . 
J 5 HOH   86  386 89  HOH   HOH C . 
J 5 HOH   87  387 234 HOH   HOH C . 
J 5 HOH   88  388 78  HOH   HOH C . 
J 5 HOH   89  389 41  HOH   HOH C . 
J 5 HOH   90  390 143 HOH   HOH C . 
J 5 HOH   91  391 50  HOH   HOH C . 
J 5 HOH   92  392 3   HOH   HOH C . 
J 5 HOH   93  393 148 HOH   HOH C . 
J 5 HOH   94  394 31  HOH   HOH C . 
J 5 HOH   95  395 54  HOH   HOH C . 
J 5 HOH   96  396 302 HOH   HOH C . 
J 5 HOH   97  397 305 HOH   HOH C . 
J 5 HOH   98  398 135 HOH   HOH C . 
J 5 HOH   99  399 243 HOH   HOH C . 
J 5 HOH   100 400 87  HOH   HOH C . 
J 5 HOH   101 401 45  HOH   HOH C . 
J 5 HOH   102 402 265 HOH   HOH C . 
J 5 HOH   103 403 146 HOH   HOH C . 
J 5 HOH   104 404 233 HOH   HOH C . 
J 5 HOH   105 405 44  HOH   HOH C . 
J 5 HOH   106 406 258 HOH   HOH C . 
J 5 HOH   107 407 52  HOH   HOH C . 
J 5 HOH   108 408 282 HOH   HOH C . 
J 5 HOH   109 409 41  HOH   HOH C . 
J 5 HOH   110 410 300 HOH   HOH C . 
J 5 HOH   111 411 266 HOH   HOH C . 
J 5 HOH   112 412 68  HOH   HOH C . 
J 5 HOH   113 413 235 HOH   HOH C . 
J 5 HOH   114 414 276 HOH   HOH C . 
J 5 HOH   115 415 118 HOH   HOH C . 
J 5 HOH   116 416 47  HOH   HOH C . 
J 5 HOH   117 417 124 HOH   HOH C . 
J 5 HOH   118 418 90  HOH   HOH C . 
J 5 HOH   119 419 145 HOH   HOH C . 
J 5 HOH   120 420 291 HOH   HOH C . 
J 5 HOH   121 421 141 HOH   HOH C . 
J 5 HOH   122 422 292 HOH   HOH C . 
J 5 HOH   123 423 27  HOH   HOH C . 
J 5 HOH   124 424 267 HOH   HOH C . 
J 5 HOH   125 425 139 HOH   HOH C . 
J 5 HOH   126 426 17  HOH   HOH C . 
J 5 HOH   127 427 116 HOH   HOH C . 
J 5 HOH   128 428 185 HOH   HOH C . 
J 5 HOH   129 429 198 HOH   HOH C . 
J 5 HOH   130 430 93  HOH   HOH C . 
J 5 HOH   131 431 151 HOH   HOH C . 
J 5 HOH   132 432 161 HOH   HOH C . 
J 5 HOH   133 433 162 HOH   HOH C . 
J 5 HOH   134 434 199 HOH   HOH C . 
J 5 HOH   135 435 149 HOH   HOH C . 
J 5 HOH   136 436 123 HOH   HOH C . 
J 5 HOH   137 437 222 HOH   HOH C . 
J 5 HOH   138 438 154 HOH   HOH C . 
J 5 HOH   139 439 218 HOH   HOH C . 
J 5 HOH   140 440 163 HOH   HOH C . 
J 5 HOH   141 441 141 HOH   HOH C . 
J 5 HOH   142 442 203 HOH   HOH C . 
J 5 HOH   143 443 207 HOH   HOH C . 
J 5 HOH   144 444 43  HOH   HOH C . 
J 5 HOH   145 445 146 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           7I5V 
_cell.length_a           72.744 
_cell.length_b           61.713 
_cell.length_c           65.445 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.83 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I5V 
_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          7I5V 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.31 
_exptl_crystal.density_percent_sol   46.71 
_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   2025-01-22 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92202 
_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        0.92202 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I5V 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             32.69 
_reflns.d_resolution_high            1.38 
_reflns.number_obs                   58736 
_reflns.percent_possible_obs         98.9 
_reflns.pdbx_Rmerge_I_obs            0.101 
_reflns.pdbx_netI_over_sigmaI        7.4 
_reflns.pdbx_redundancy              6.2 
_reflns.pdbx_Rrim_I_all              0.110 
_reflns.pdbx_Rpim_I_all              0.042 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     365939 
_reflns.pdbx_chi_squared             0.39 
_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                  1.38 
_reflns_shell.d_res_low                   1.40 
_reflns_shell.number_measured_all         11445 
_reflns_shell.number_unique_obs           2723 
_reflns_shell.Rmerge_I_obs                1.579 
_reflns_shell.pdbx_chi_squared            0.11 
_reflns_shell.pdbx_redundancy             4.2 
_reflns_shell.percent_possible_obs        91.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.3 
_reflns_shell.pdbx_Rrim_I_all             1.812 
_reflns_shell.pdbx_Rpim_I_all             0.873 
_reflns_shell.pdbx_CC_half                0.337 
_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                                 7I5V 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     58312 
_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                             20.02 
_refine.ls_d_res_high                            1.380 
_refine.ls_percent_reflns_obs                    98.1 
_refine.ls_R_factor_obs                          0.1929 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1918 
_refine.ls_R_factor_R_free                       0.2139 
_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                  2860 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.957 
_refine.B_iso_mean                               22.46 
_refine.aniso_B[1][1]                            0.30490 
_refine.aniso_B[2][2]                            -2.86180 
_refine.aniso_B[3][3]                            2.55690 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.30370 
_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             0.060 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.061 
_refine.pdbx_overall_SU_R_Blow_DPI               0.063 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.063 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I5V 
_refine_analyze.Luzzati_coordinate_error_obs    0.19 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         52 
_refine_hist.number_atoms_solvent             297 
_refine_hist.number_atoms_total               2497 
_refine_hist.d_res_high                       1.380 
_refine_hist.d_res_low                        20.02 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.011 ? 2.00  2262 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.00  ? 2.00  3081 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  755  '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  412  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2262 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.51  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.58 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  277  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  1963 '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                       1.38 
_refine_ls_shell.d_res_low                        1.39 
_refine_ls_shell.number_reflns_R_work             1109 
_refine_ls_shell.R_factor_R_work                  0.3488 
_refine_ls_shell.percent_reflns_obs               74.84 
_refine_ls_shell.R_factor_R_free                  0.3540 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.97 
_refine_ls_shell.number_reflns_R_free             58 
_refine_ls_shell.number_reflns_all                1167 
_refine_ls_shell.R_factor_all                     0.3490 
# 
_struct.entry_id                  7I5V 
_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-0036446-001 (A71EV2A-x4882)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I5V 
_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 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I5V A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I5V C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,I 
2 1 B,F,G,H,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P6  AA6 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P7  AA7 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P8  AA8 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P9  AA9 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P10 AB1 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 ? ? ? ? ? ? ? 2.318 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.363 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.314 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.089 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 56  C ZN 202 1_555 ? ? ? ? ? ? ? 2.341 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 58  C ZN 202 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 116 C ZN 202 1_555 ? ? ? ? ? ? ? 2.308 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 G ZN . ZN ? ? C HIS 118 C ZN 202 1_555 ? ? ? ? ? ? ? 2.103 ? ? 
# 
_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_555 110.0 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.8 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.3 ? 
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_555 108.7 ? 
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_555 103.1 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 112.9 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.4 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.3 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 116.7 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 107.7 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.0 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.3 ? 
# 
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                   7I5V 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 357 ? ? O A HOH 384 ? ? 2.19 
2 1 O A HOH 337 ? ? O A HOH 344 ? ? 2.19 
# 
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 19.7619 6.7447   18.2929 -0.0258 -0.0477 0.0268 -0.0040 -0.0249 0.0013  0.7055 1.0073 0.5175 
-0.3688 -0.1502 0.0368 -0.0072 -0.0156 0.0691 0.0116 0.0291 0.0452  0.0286  0.0393  -0.0219 
'X-RAY DIFFRACTION' 2 ? refined 15.3128 -23.9521 14.1871 -0.0213 -0.0407 0.0242 0.0023  -0.0318 -0.0046 0.5306 0.9286 0.5009 
0.3635  0.1689  0.0702 -0.0253 0.0247  0.0233 0.0246 0.0456 -0.0588 -0.0071 -0.0153 -0.0203 
# 
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|* }' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       452 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.66 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
A1B4B N1   N  N N 1   
A1B4B C4   C  N N 2   
A1B4B C5   C  N N 3   
A1B4B C6   C  N N 4   
A1B4B C7   C  Y N 5   
A1B4B C8   C  Y N 6   
A1B4B C10  C  Y N 7   
A1B4B C13  C  N N 8   
A1B4B BR   BR N N 9   
A1B4B C12  C  Y N 10  
A1B4B C11  C  Y N 11  
A1B4B F1   F  N N 12  
A1B4B C9   C  Y N 13  
A1B4B F    F  N N 14  
A1B4B O1   O  N N 15  
A1B4B C3   C  N N 16  
A1B4B C2   C  N N 17  
A1B4B C1   C  N S 18  
A1B4B C    C  N N 19  
A1B4B O    O  N N 20  
A1B4B N    N  N N 21  
A1B4B H8   H  N N 22  
A1B4B H7   H  N N 23  
A1B4B H10  H  N N 24  
A1B4B H9   H  N N 25  
A1B4B H11  H  N N 26  
A1B4B H14  H  N N 27  
A1B4B H13  H  N N 28  
A1B4B H12  H  N N 29  
A1B4B H6   H  N N 30  
A1B4B H5   H  N N 31  
A1B4B H4   H  N N 32  
A1B4B H3   H  N N 33  
A1B4B H    H  N N 34  
A1B4B H2   H  N N 35  
A1B4B H1   H  N N 36  
ALA   N    N  N N 37  
ALA   CA   C  N S 38  
ALA   C    C  N N 39  
ALA   O    O  N N 40  
ALA   CB   C  N N 41  
ALA   OXT  O  N N 42  
ALA   H    H  N N 43  
ALA   H2   H  N N 44  
ALA   HA   H  N N 45  
ALA   HB1  H  N N 46  
ALA   HB2  H  N N 47  
ALA   HB3  H  N N 48  
ALA   HXT  H  N N 49  
ARG   N    N  N N 50  
ARG   CA   C  N S 51  
ARG   C    C  N N 52  
ARG   O    O  N N 53  
ARG   CB   C  N N 54  
ARG   CG   C  N N 55  
ARG   CD   C  N N 56  
ARG   NE   N  N N 57  
ARG   CZ   C  N N 58  
ARG   NH1  N  N N 59  
ARG   NH2  N  N N 60  
ARG   OXT  O  N N 61  
ARG   H    H  N N 62  
ARG   H2   H  N N 63  
ARG   HA   H  N N 64  
ARG   HB2  H  N N 65  
ARG   HB3  H  N N 66  
ARG   HG2  H  N N 67  
ARG   HG3  H  N N 68  
ARG   HD2  H  N N 69  
ARG   HD3  H  N N 70  
ARG   HE   H  N N 71  
ARG   HH11 H  N N 72  
ARG   HH12 H  N N 73  
ARG   HH21 H  N N 74  
ARG   HH22 H  N N 75  
ARG   HXT  H  N N 76  
ASN   N    N  N N 77  
ASN   CA   C  N S 78  
ASN   C    C  N N 79  
ASN   O    O  N N 80  
ASN   CB   C  N N 81  
ASN   CG   C  N N 82  
ASN   OD1  O  N N 83  
ASN   ND2  N  N N 84  
ASN   OXT  O  N N 85  
ASN   H    H  N N 86  
ASN   H2   H  N N 87  
ASN   HA   H  N N 88  
ASN   HB2  H  N N 89  
ASN   HB3  H  N N 90  
ASN   HD21 H  N N 91  
ASN   HD22 H  N N 92  
ASN   HXT  H  N N 93  
ASP   N    N  N N 94  
ASP   CA   C  N S 95  
ASP   C    C  N N 96  
ASP   O    O  N N 97  
ASP   CB   C  N N 98  
ASP   CG   C  N N 99  
ASP   OD1  O  N N 100 
ASP   OD2  O  N N 101 
ASP   OXT  O  N N 102 
ASP   H    H  N N 103 
ASP   H2   H  N N 104 
ASP   HA   H  N N 105 
ASP   HB2  H  N N 106 
ASP   HB3  H  N N 107 
ASP   HD2  H  N N 108 
ASP   HXT  H  N N 109 
CYS   N    N  N N 110 
CYS   CA   C  N R 111 
CYS   C    C  N N 112 
CYS   O    O  N N 113 
CYS   CB   C  N N 114 
CYS   SG   S  N N 115 
CYS   OXT  O  N N 116 
CYS   H    H  N N 117 
CYS   H2   H  N N 118 
CYS   HA   H  N N 119 
CYS   HB2  H  N N 120 
CYS   HB3  H  N N 121 
CYS   HG   H  N N 122 
CYS   HXT  H  N N 123 
DMS   S    S  N N 124 
DMS   O    O  N N 125 
DMS   C1   C  N N 126 
DMS   C2   C  N N 127 
DMS   H11  H  N N 128 
DMS   H12  H  N N 129 
DMS   H13  H  N N 130 
DMS   H21  H  N N 131 
DMS   H22  H  N N 132 
DMS   H23  H  N N 133 
GLN   N    N  N N 134 
GLN   CA   C  N S 135 
GLN   C    C  N N 136 
GLN   O    O  N N 137 
GLN   CB   C  N N 138 
GLN   CG   C  N N 139 
GLN   CD   C  N N 140 
GLN   OE1  O  N N 141 
GLN   NE2  N  N N 142 
GLN   OXT  O  N N 143 
GLN   H    H  N N 144 
GLN   H2   H  N N 145 
GLN   HA   H  N N 146 
GLN   HB2  H  N N 147 
GLN   HB3  H  N N 148 
GLN   HG2  H  N N 149 
GLN   HG3  H  N N 150 
GLN   HE21 H  N N 151 
GLN   HE22 H  N N 152 
GLN   HXT  H  N N 153 
GLU   N    N  N N 154 
GLU   CA   C  N S 155 
GLU   C    C  N N 156 
GLU   O    O  N N 157 
GLU   CB   C  N N 158 
GLU   CG   C  N N 159 
GLU   CD   C  N N 160 
GLU   OE1  O  N N 161 
GLU   OE2  O  N N 162 
GLU   OXT  O  N N 163 
GLU   H    H  N N 164 
GLU   H2   H  N N 165 
GLU   HA   H  N N 166 
GLU   HB2  H  N N 167 
GLU   HB3  H  N N 168 
GLU   HG2  H  N N 169 
GLU   HG3  H  N N 170 
GLU   HE2  H  N N 171 
GLU   HXT  H  N N 172 
GLY   N    N  N N 173 
GLY   CA   C  N N 174 
GLY   C    C  N N 175 
GLY   O    O  N N 176 
GLY   OXT  O  N N 177 
GLY   H    H  N N 178 
GLY   H2   H  N N 179 
GLY   HA2  H  N N 180 
GLY   HA3  H  N N 181 
GLY   HXT  H  N N 182 
HIS   N    N  N N 183 
HIS   CA   C  N S 184 
HIS   C    C  N N 185 
HIS   O    O  N N 186 
HIS   CB   C  N N 187 
HIS   CG   C  Y N 188 
HIS   ND1  N  Y N 189 
HIS   CD2  C  Y N 190 
HIS   CE1  C  Y N 191 
HIS   NE2  N  Y N 192 
HIS   OXT  O  N N 193 
HIS   H    H  N N 194 
HIS   H2   H  N N 195 
HIS   HA   H  N N 196 
HIS   HB2  H  N N 197 
HIS   HB3  H  N N 198 
HIS   HD1  H  N N 199 
HIS   HD2  H  N N 200 
HIS   HE1  H  N N 201 
HIS   HE2  H  N N 202 
HIS   HXT  H  N N 203 
HOH   O    O  N N 204 
HOH   H1   H  N N 205 
HOH   H2   H  N N 206 
ILE   N    N  N N 207 
ILE   CA   C  N S 208 
ILE   C    C  N N 209 
ILE   O    O  N N 210 
ILE   CB   C  N S 211 
ILE   CG1  C  N N 212 
ILE   CG2  C  N N 213 
ILE   CD1  C  N N 214 
ILE   OXT  O  N N 215 
ILE   H    H  N N 216 
ILE   H2   H  N N 217 
ILE   HA   H  N N 218 
ILE   HB   H  N N 219 
ILE   HG12 H  N N 220 
ILE   HG13 H  N N 221 
ILE   HG21 H  N N 222 
ILE   HG22 H  N N 223 
ILE   HG23 H  N N 224 
ILE   HD11 H  N N 225 
ILE   HD12 H  N N 226 
ILE   HD13 H  N N 227 
ILE   HXT  H  N N 228 
LEU   N    N  N N 229 
LEU   CA   C  N S 230 
LEU   C    C  N N 231 
LEU   O    O  N N 232 
LEU   CB   C  N N 233 
LEU   CG   C  N N 234 
LEU   CD1  C  N N 235 
LEU   CD2  C  N N 236 
LEU   OXT  O  N N 237 
LEU   H    H  N N 238 
LEU   H2   H  N N 239 
LEU   HA   H  N N 240 
LEU   HB2  H  N N 241 
LEU   HB3  H  N N 242 
LEU   HG   H  N N 243 
LEU   HD11 H  N N 244 
LEU   HD12 H  N N 245 
LEU   HD13 H  N N 246 
LEU   HD21 H  N N 247 
LEU   HD22 H  N N 248 
LEU   HD23 H  N N 249 
LEU   HXT  H  N N 250 
LYS   N    N  N N 251 
LYS   CA   C  N S 252 
LYS   C    C  N N 253 
LYS   O    O  N N 254 
LYS   CB   C  N N 255 
LYS   CG   C  N N 256 
LYS   CD   C  N N 257 
LYS   CE   C  N N 258 
LYS   NZ   N  N N 259 
LYS   OXT  O  N N 260 
LYS   H    H  N N 261 
LYS   H2   H  N N 262 
LYS   HA   H  N N 263 
LYS   HB2  H  N N 264 
LYS   HB3  H  N N 265 
LYS   HG2  H  N N 266 
LYS   HG3  H  N N 267 
LYS   HD2  H  N N 268 
LYS   HD3  H  N N 269 
LYS   HE2  H  N N 270 
LYS   HE3  H  N N 271 
LYS   HZ1  H  N N 272 
LYS   HZ2  H  N N 273 
LYS   HZ3  H  N N 274 
LYS   HXT  H  N N 275 
MET   N    N  N N 276 
MET   CA   C  N S 277 
MET   C    C  N N 278 
MET   O    O  N N 279 
MET   CB   C  N N 280 
MET   CG   C  N N 281 
MET   SD   S  N N 282 
MET   CE   C  N N 283 
MET   OXT  O  N N 284 
MET   H    H  N N 285 
MET   H2   H  N N 286 
MET   HA   H  N N 287 
MET   HB2  H  N N 288 
MET   HB3  H  N N 289 
MET   HG2  H  N N 290 
MET   HG3  H  N N 291 
MET   HE1  H  N N 292 
MET   HE2  H  N N 293 
MET   HE3  H  N N 294 
MET   HXT  H  N N 295 
PHE   N    N  N N 296 
PHE   CA   C  N S 297 
PHE   C    C  N N 298 
PHE   O    O  N N 299 
PHE   CB   C  N N 300 
PHE   CG   C  Y N 301 
PHE   CD1  C  Y N 302 
PHE   CD2  C  Y N 303 
PHE   CE1  C  Y N 304 
PHE   CE2  C  Y N 305 
PHE   CZ   C  Y N 306 
PHE   OXT  O  N N 307 
PHE   H    H  N N 308 
PHE   H2   H  N N 309 
PHE   HA   H  N N 310 
PHE   HB2  H  N N 311 
PHE   HB3  H  N N 312 
PHE   HD1  H  N N 313 
PHE   HD2  H  N N 314 
PHE   HE1  H  N N 315 
PHE   HE2  H  N N 316 
PHE   HZ   H  N N 317 
PHE   HXT  H  N N 318 
PRO   N    N  N N 319 
PRO   CA   C  N S 320 
PRO   C    C  N N 321 
PRO   O    O  N N 322 
PRO   CB   C  N N 323 
PRO   CG   C  N N 324 
PRO   CD   C  N N 325 
PRO   OXT  O  N N 326 
PRO   H    H  N N 327 
PRO   HA   H  N N 328 
PRO   HB2  H  N N 329 
PRO   HB3  H  N N 330 
PRO   HG2  H  N N 331 
PRO   HG3  H  N N 332 
PRO   HD2  H  N N 333 
PRO   HD3  H  N N 334 
PRO   HXT  H  N N 335 
SER   N    N  N N 336 
SER   CA   C  N S 337 
SER   C    C  N N 338 
SER   O    O  N N 339 
SER   CB   C  N N 340 
SER   OG   O  N N 341 
SER   OXT  O  N N 342 
SER   H    H  N N 343 
SER   H2   H  N N 344 
SER   HA   H  N N 345 
SER   HB2  H  N N 346 
SER   HB3  H  N N 347 
SER   HG   H  N N 348 
SER   HXT  H  N N 349 
THR   N    N  N N 350 
THR   CA   C  N S 351 
THR   C    C  N N 352 
THR   O    O  N N 353 
THR   CB   C  N R 354 
THR   OG1  O  N N 355 
THR   CG2  C  N N 356 
THR   OXT  O  N N 357 
THR   H    H  N N 358 
THR   H2   H  N N 359 
THR   HA   H  N N 360 
THR   HB   H  N N 361 
THR   HG1  H  N N 362 
THR   HG21 H  N N 363 
THR   HG22 H  N N 364 
THR   HG23 H  N N 365 
THR   HXT  H  N N 366 
TRP   N    N  N N 367 
TRP   CA   C  N S 368 
TRP   C    C  N N 369 
TRP   O    O  N N 370 
TRP   CB   C  N N 371 
TRP   CG   C  Y N 372 
TRP   CD1  C  Y N 373 
TRP   CD2  C  Y N 374 
TRP   NE1  N  Y N 375 
TRP   CE2  C  Y N 376 
TRP   CE3  C  Y N 377 
TRP   CZ2  C  Y N 378 
TRP   CZ3  C  Y N 379 
TRP   CH2  C  Y N 380 
TRP   OXT  O  N N 381 
TRP   H    H  N N 382 
TRP   H2   H  N N 383 
TRP   HA   H  N N 384 
TRP   HB2  H  N N 385 
TRP   HB3  H  N N 386 
TRP   HD1  H  N N 387 
TRP   HE1  H  N N 388 
TRP   HE3  H  N N 389 
TRP   HZ2  H  N N 390 
TRP   HZ3  H  N N 391 
TRP   HH2  H  N N 392 
TRP   HXT  H  N N 393 
TYR   N    N  N N 394 
TYR   CA   C  N S 395 
TYR   C    C  N N 396 
TYR   O    O  N N 397 
TYR   CB   C  N N 398 
TYR   CG   C  Y N 399 
TYR   CD1  C  Y N 400 
TYR   CD2  C  Y N 401 
TYR   CE1  C  Y N 402 
TYR   CE2  C  Y N 403 
TYR   CZ   C  Y N 404 
TYR   OH   O  N N 405 
TYR   OXT  O  N N 406 
TYR   H    H  N N 407 
TYR   H2   H  N N 408 
TYR   HA   H  N N 409 
TYR   HB2  H  N N 410 
TYR   HB3  H  N N 411 
TYR   HD1  H  N N 412 
TYR   HD2  H  N N 413 
TYR   HE1  H  N N 414 
TYR   HE2  H  N N 415 
TYR   HH   H  N N 416 
TYR   HXT  H  N N 417 
VAL   N    N  N N 418 
VAL   CA   C  N S 419 
VAL   C    C  N N 420 
VAL   O    O  N N 421 
VAL   CB   C  N N 422 
VAL   CG1  C  N N 423 
VAL   CG2  C  N N 424 
VAL   OXT  O  N N 425 
VAL   H    H  N N 426 
VAL   H2   H  N N 427 
VAL   HA   H  N N 428 
VAL   HB   H  N N 429 
VAL   HG11 H  N N 430 
VAL   HG12 H  N N 431 
VAL   HG13 H  N N 432 
VAL   HG21 H  N N 433 
VAL   HG22 H  N N 434 
VAL   HG23 H  N N 435 
VAL   HXT  H  N N 436 
ZN    ZN   ZN N N 437 
# 
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 
A1B4B N   C    sing N N 1   
A1B4B O   C    doub N N 2   
A1B4B C   C1   sing N N 3   
A1B4B C1  C2   sing N N 4   
A1B4B C2  C3   sing N N 5   
A1B4B C3  C4   sing N N 6   
A1B4B C4  N1   sing N N 7   
A1B4B N1  C5   sing N N 8   
A1B4B O1  C5   doub N N 9   
A1B4B C5  C6   sing N N 10  
A1B4B C6  C7   sing N N 11  
A1B4B C7  C8   sing Y N 12  
A1B4B C8  C9   doub Y N 13  
A1B4B F   C9   sing N N 14  
A1B4B C9  C10  sing Y N 15  
A1B4B F1  C10  sing N N 16  
A1B4B C10 C11  doub Y N 17  
A1B4B C11 C12  sing Y N 18  
A1B4B C7  C12  doub Y N 19  
A1B4B C12 BR   sing N N 20  
A1B4B C13 N1   sing N N 21  
A1B4B C1  C13  sing N N 22  
A1B4B C4  H8   sing N N 23  
A1B4B C4  H7   sing N N 24  
A1B4B C6  H10  sing N N 25  
A1B4B C6  H9   sing N N 26  
A1B4B C8  H11  sing N N 27  
A1B4B C13 H14  sing N N 28  
A1B4B C13 H13  sing N N 29  
A1B4B C11 H12  sing N N 30  
A1B4B C3  H6   sing N N 31  
A1B4B C3  H5   sing N N 32  
A1B4B C2  H4   sing N N 33  
A1B4B C2  H3   sing N N 34  
A1B4B C1  H    sing N N 35  
A1B4B N   H2   sing N N 36  
A1B4B N   H1   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                    7I5V 
_atom_sites.fract_transf_matrix[1][1]   0.013747 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000680 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016204 
_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]   0.015299 
_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 
BR 
C  
F  
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   ? 16.477 6.509   8.117  1.00 21.71 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 15.262 6.668   8.921  1.00 21.89 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 15.065 5.499   9.887  1.00 21.47 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 15.651 4.434   9.689  1.00 22.58 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 14.051 6.801   7.997  1.00 24.78 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 13.880 5.591   7.274  1.00 28.80 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 14.258 5.690   10.932 1.00 20.30 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 13.953 4.610   11.864 1.00 19.07 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 13.568 5.118   13.251 1.00 18.38 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 13.895 6.260   13.606 1.00 18.84 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 12.828 4.307   14.029 1.00 17.19 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 12.401 4.739   15.358 1.00 17.61 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 12.326 3.537   16.296 1.00 17.41 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 12.280 2.378   15.830 1.00 17.40 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 10.999 5.383   15.262 1.00 18.68 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 12.300 3.801   17.619 1.00 15.78 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 12.081 2.787   18.635 1.00 15.88 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 10.668 3.007   19.142 1.00 16.28 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 10.314 4.147   19.476 1.00 15.95 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 13.058 2.983   19.822 1.00 15.69 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 14.520 2.903   19.336 1.00 15.11 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 12.823 1.938   20.911 1.00 16.54 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 15.518 3.520   20.414 1.00 16.30 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 9.878  1.925   19.262 1.00 16.17 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 8.518  2.047   19.791 1.00 17.47 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 8.425  1.290   21.096 1.00 18.36 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 8.482  0.072   21.072 1.00 20.63 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 7.504  1.477   18.771 1.00 17.72 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 7.430  2.317   17.524 1.00 19.76 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 6.632  3.451   17.476 1.00 21.52 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 8.217  2.025   16.424 1.00 21.89 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 6.580  4.246   16.338 1.00 23.15 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 8.203  2.828   15.294 1.00 23.37 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 7.361  3.920   15.245 1.00 24.47 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 7.376  4.730   14.139 1.00 27.36 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 8.342  1.981   22.250 1.00 17.13 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 8.330  1.293   23.556 1.00 18.22 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 7.214  1.876   24.385 1.00 19.93 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 7.107  3.095   24.499 1.00 20.42 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 9.714  1.425   24.279 1.00 20.48 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 10.190 2.886   24.321 1.00 21.00 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 9.648  0.855   25.692 1.00 21.40 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 6.293  1.029   24.868 1.00 20.70 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 5.153  1.521   25.632 1.00 21.02 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 4.346  2.505   24.801 1.00 21.48 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 4.127  2.252   23.618 1.00 21.58 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 4.030  3.686   25.365 1.00 21.82 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 3.327  4.699   24.568 1.00 22.25 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 4.288  5.796   24.107 1.00 20.43 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 3.892  6.957   24.009 1.00 19.74 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 2.134  5.293   25.314 1.00 25.69 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 1.017  4.296   25.463 1.00 32.77 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 0.375  3.886   24.482 1.00 35.81 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 0.790  3.878   26.689 1.00 33.48 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 5.537  5.411   23.786 1.00 18.76 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 6.545  6.374   23.326 1.00 17.76 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 7.135  5.948   21.981 1.00 16.56 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 7.236  4.746   21.692 1.00 16.89 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 7.716  6.452   24.337 1.00 17.95 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 7.305  6.982   25.688 1.00 18.05 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 6.680  8.214   25.815 1.00 19.06 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 7.540  6.254   26.841 1.00 19.12 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 6.318  8.720   27.065 1.00 20.48 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 7.190  6.751   28.090 1.00 19.67 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 6.546  7.973   28.196 1.00 21.79 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 6.206  8.491   29.434 1.00 25.34 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 7.529  6.948   21.168 1.00 15.45 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 8.249  6.764   19.921 1.00 16.13 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 9.576  7.570   20.068 1.00 16.76 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 9.521  8.760   20.403 1.00 16.60 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 7.400  7.273   18.732 1.00 17.56 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 8.156  7.543   17.438 1.00 19.05 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 7.227  7.894   16.268 1.00 20.41 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 7.778  8.924   15.378 1.00 21.71 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 8.296  8.697   14.174 1.00 24.79 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 8.386  7.456   13.704 1.00 23.90 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 8.774  9.707   13.447 1.00 23.64 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 10.743 6.911   19.900 1.00 16.04 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 12.046 7.590   20.022 1.00 15.97 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 12.613 7.742   18.620 1.00 16.34 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 12.779 6.739   17.925 1.00 16.23 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 13.044 6.750   20.894 1.00 16.84 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 14.330 7.577   21.163 1.00 15.48 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 12.390 6.276   22.197 1.00 16.50 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 12.966 8.958   18.205 1.00 15.07 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 13.516 9.183   16.872 1.00 15.46 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 14.746 10.100  16.979 1.00 14.85 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 14.945 10.789  18.009 1.00 14.69 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 12.461 9.841   15.948 1.00 17.13 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 11.309 8.888   15.677 1.00 19.99 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 11.953 11.137  16.575 1.00 16.59 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 15.538 10.204  15.877 1.00 14.47 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 16.605 11.214  15.848 1.00 14.01 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 15.898 12.580  15.857 1.00 14.81 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 14.966 12.797  15.058 1.00 14.95 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.388 11.115  14.544 1.00 14.10 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 18.190 9.843   14.467 1.00 17.30 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.718 8.839   13.920 1.00 18.25 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 19.416 9.879   14.997 1.00 15.59 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 16.329 13.497  16.727 1.00 13.67 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 15.668 14.816  16.785 1.00 13.10 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 15.652 15.513  15.393 1.00 14.12 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 14.636 16.132  15.038 1.00 16.48 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 16.343 15.673  17.838 1.00 14.44 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 15.563 16.966  18.180 1.00 16.21 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 16.472 17.826  19.049 1.00 16.41 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 15.860 19.070  19.556 1.00 16.86 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 15.874 20.222  18.896 1.00 18.83 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 16.334 20.278  17.647 1.00 18.27 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 15.388 21.326  19.462 1.00 18.66 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 16.754 15.376  14.616 1.00 13.95 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 16.827 16.066  13.318 1.00 14.49 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 15.888 15.481  12.268 1.00 16.07 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 15.665 16.125  11.233 1.00 18.14 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.291 16.172  12.799 1.00 14.91 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 18.875 14.892  12.288 1.00 15.39 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 19.435 13.945  13.140 1.00 17.29 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 18.974 14.451  11.011 1.00 17.19 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 19.879 12.968  12.354 1.00 17.52 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 19.613 13.222  11.060 1.00 17.66 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 15.301 14.290  12.544 1.00 15.60 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 14.339 13.669  11.604 1.00 15.21 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 12.890 13.670  12.160 1.00 16.92 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 11.984 13.089  11.538 1.00 17.61 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 14.779 12.232  11.301 1.00 14.36 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 16.158 12.111  10.618 1.00 16.14 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 16.526 10.646  10.419 1.00 16.38 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 16.213 12.899  9.301  1.00 16.79 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 12.660 14.321  13.319 1.00 16.12 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 11.308 14.332  13.921 1.00 16.02 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 10.309 15.011  12.958 1.00 17.28 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 10.656 15.986  12.313 1.00 17.01 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 11.347 15.089  15.243 1.00 15.79 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 9.085  14.505  12.912 1.00 18.27 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 8.057  15.053  12.003 1.00 19.48 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 7.234  16.133  12.706 1.00 20.30 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 7.363  16.321  13.921 1.00 19.30 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 7.110  13.884  11.607 1.00 21.49 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 6.432  13.421  12.790 1.00 22.15 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 7.851  12.735  10.944 1.00 21.95 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 6.290  16.799  11.966 1.00 20.98 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 5.392  17.759  12.608 1.00 22.88 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 4.566  17.046  13.698 1.00 20.98 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 4.368  17.607  14.776 1.00 21.57 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 4.411  18.356  11.562 1.00 27.26 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 5.061  19.104  10.440 1.00 36.12 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 5.798  20.261  10.666 1.00 40.35 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 5.012  18.869  9.103  1.00 39.05 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 6.214  20.658  9.471  1.00 41.67 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 5.751  19.858  8.495  1.00 41.22 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 4.136  15.788  13.437 1.00 20.72 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 3.359  15.044  14.427 1.00 20.41 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 4.172  14.723  15.678 1.00 19.39 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 3.637  14.732  16.789 1.00 20.18 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 2.781  13.758  13.842 1.00 22.61 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 1.463  13.988  13.151 1.00 29.06 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 0.602  14.785  13.602 1.00 29.60 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 1.310  13.361  11.996 1.00 30.82 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 5.485  14.395  15.513 1.00 17.37 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 6.325  14.158  16.700 1.00 16.47 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 6.368  15.396  17.594 1.00 16.86 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 6.250  15.288  18.814 1.00 17.77 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 7.765  13.818  16.281 1.00 15.08 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 7.924  12.422  15.737 1.00 20.42 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 7.324  11.487  16.319 1.00 20.81 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 8.639  12.265  14.707 1.00 20.71 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 6.579  16.571  16.980 1.00 16.80 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 6.663  17.816  17.743 1.00 16.78 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 5.302  18.186  18.371 1.00 18.54 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 5.261  18.723  19.478 1.00 18.91 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 7.187  18.944  16.860 1.00 17.20 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 8.690  18.961  16.747 1.00 17.80 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 9.450  18.516  15.702 1.00 18.59 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 9.610  19.475  17.722 1.00 17.31 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 10.792 18.726  15.967 1.00 18.52 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 10.917 19.285  17.214 1.00 18.29 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 9.459  20.014  19.002 1.00 18.44 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 12.064 19.710  17.913 1.00 17.95 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 10.592 20.433  19.688 1.00 19.18 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 11.870 20.248  19.161 1.00 18.03 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 4.193  17.841  17.706 1.00 19.26 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 2.839  18.112  18.268 1.00 20.65 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 2.481  17.182  19.442 1.00 20.90 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 1.513  17.430  20.190 1.00 21.77 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 1.790  17.960  17.178 1.00 21.78 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 3.193  16.064  19.567 1.00 19.16 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 2.969  15.120  20.656 1.00 19.02 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 4.288  14.955  21.486 1.00 17.97 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 4.601  13.878  21.971 1.00 17.56 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 2.535  13.793  20.066 1.00 20.51 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 1.160  13.874  19.424 1.00 24.81 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 0.144  13.894  20.132 1.00 27.00 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 1.105  13.931  18.088 1.00 25.41 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 5.057  16.037  21.618 1.00 17.23 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 6.361  16.029  22.270 1.00 17.85 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 6.314  15.637  23.735 1.00 18.12 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 5.494  16.176  24.484 1.00 19.57 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 6.948  17.426  22.155 1.00 18.12 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 8.324  17.644  22.812 1.00 19.26 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 9.374  16.762  22.123 1.00 19.09 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 8.749  19.117  22.703 1.00 19.72 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 7.202  14.722  24.151 1.00 16.40 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 7.364  14.345  25.561 1.00 17.85 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 8.686  14.939  26.084 1.00 19.30 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 8.751  15.551  27.170 1.00 20.78 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 7.359  12.793  25.710 1.00 19.29 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 7.738  12.370  27.133 1.00 20.26 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 5.976  12.239  25.349 1.00 20.58 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 9.756  14.787  25.287 1.00 18.20 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 11.082 15.256  25.698 1.00 18.59 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 11.964 15.337  24.469 1.00 17.64 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 11.839 14.503  23.569 1.00 17.20 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 11.696 14.213  26.697 1.00 19.23 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 13.170 14.385  27.017 1.00 19.74 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 13.733 15.233  27.930 1.00 21.26 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 14.249 13.646  26.438 1.00 19.05 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 15.113 15.114  27.899 1.00 21.49 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 15.448 14.120  27.016 1.00 19.81 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 14.313 12.629  25.495 1.00 19.10 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 16.696 13.588  26.688 1.00 19.67 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 15.554 12.117  25.150 1.00 19.51 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 16.723 12.591  25.759 1.00 19.05 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 12.842 16.321  24.427 1.00 17.79 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 13.843 16.394  23.348 1.00 17.56 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 15.155 16.962  23.874 1.00 16.76 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 15.150 17.732  24.848 1.00 17.88 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 13.348 17.170  22.114 1.00 18.01 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 12.757 18.551  22.430 1.00 18.54 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 13.754 19.671  22.696 1.00 20.94 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 13.443 20.560  23.529 1.00 23.46 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 14.856 19.659  22.106 1.00 18.87 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 16.277 16.590  23.245 1.00 15.88 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.577 17.096  23.686 1.00 15.40 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 18.471 17.251  22.448 1.00 15.30 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 18.912 16.255  21.896 1.00 15.16 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 18.187 16.175  24.743 1.00 17.84 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 19.461 16.737  25.371 1.00 23.69 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 20.131 17.596  24.719 1.00 24.38 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 19.779 16.341  26.507 1.00 23.48 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 18.686 18.501  21.985 1.00 16.01 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 19.501 18.765  20.813 0.50 17.08 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 19.504 18.729  20.796 0.50 16.98 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 20.937 18.242  21.002 1.00 17.00 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 21.573 17.790  20.051 1.00 17.44 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 19.501 20.267  20.514 0.50 19.76 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 19.509 20.206  20.401 0.50 19.36 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 20.424 20.608  19.498 0.50 22.10 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 20.211 20.958  21.373 0.50 20.99 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 21.460 18.332  22.249 1.00 16.70 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 22.849 17.873  22.480 1.00 17.53 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 22.984 16.358  22.321 1.00 17.46 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 24.093 15.886  22.159 1.00 18.33 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 23.350 18.297  23.863 1.00 21.51 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 22.783 17.492  24.883 1.00 26.85 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 21.872 15.596  22.374 1.00 14.86 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 21.907 14.130  22.207 1.00 14.43 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 21.348 13.676  20.818 1.00 14.77 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 21.395 12.472  20.500 1.00 14.94 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 21.028 13.447  23.309 1.00 15.42 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 21.629 13.666  24.714 1.00 17.02 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 20.799 12.979  25.787 1.00 18.01 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 20.775 11.508  25.630 1.00 17.33 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 20.569 10.664  26.641 1.00 17.90 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 20.372 11.129  27.882 1.00 18.21 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 20.590 9.347   26.432 1.00 15.88 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 20.786 14.623  20.031 1.00 13.35 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 20.083 14.297  18.788 1.00 13.00 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 18.920 13.325  19.050 1.00 14.12 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 18.639 12.502  18.185 1.00 14.57 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 21.009 13.740  17.692 1.00 13.95 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 20.317 13.509  16.348 1.00 15.56 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 19.496 14.378  15.940 1.00 16.13 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 20.608 12.462  15.706 1.00 14.95 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 18.207 13.483  20.178 1.00 13.23 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.044 12.622  20.455 1.00 13.14 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 15.745 13.410  20.662 1.00 13.39 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 15.754 14.506  21.232 1.00 14.30 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.239 11.781  21.737 1.00 14.01 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 18.265 10.671  21.660 1.00 14.86 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 18.320 9.942   23.038 1.00 15.30 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.900 9.638   20.542 1.00 15.15 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 14.630 12.781  20.288 1.00 12.68 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 13.312 13.343  20.551 1.00 13.54 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 12.400 12.168  20.834 1.00 14.50 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 12.503 11.130  20.159 1.00 15.34 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 12.801 14.181  19.349 1.00 13.46 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 11.408 14.829  19.570 1.00 15.19 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 11.312 16.185  18.842 1.00 15.87 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 10.276 13.913  19.074 1.00 15.84 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 11.548 12.290  21.834 1.00 13.89 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 10.555 11.258  22.195 1.00 14.18 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 9.156  11.894  22.112 1.00 15.28 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 8.926  12.984  22.649 1.00 15.84 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 10.808 10.726  23.629 1.00 15.50 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 9.711  9.709   24.030 1.00 16.11 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 12.190 10.066  23.686 1.00 15.56 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 8.249  11.213  21.403 1.00 15.58 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 6.869  11.685  21.278 1.00 16.45 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 5.920  10.599  21.802 1.00 17.98 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 6.311  9.427   21.956 1.00 17.28 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 6.548  12.018  19.819 1.00 18.22 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 6.723  10.910  18.946 1.00 19.56 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 4.671  10.993  22.095 1.00 19.35 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 3.699  10.019  22.600 1.00 20.30 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 2.924  9.325   21.480 1.00 21.19 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 2.713  9.892   20.409 1.00 21.69 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 2.766  10.681  23.607 1.00 22.20 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 2.117  11.757  22.969 1.00 25.25 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 2.484  8.084   21.727 1.00 22.52 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 1.727  7.327   20.729 1.00 25.26 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 0.412  6.838   21.358 1.00 29.11 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 0.308  6.741   22.586 1.00 30.14 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 2.540  6.105   20.247 1.00 26.49 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 2.644  5.189   21.330 1.00 27.46 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 3.931  6.467   19.783 1.00 25.79 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? -0.561 6.492   20.525 1.00 31.41 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? -1.814 5.927   21.024 1.00 34.22 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? -1.688 4.395   21.114 1.00 35.88 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? -2.258 3.779   22.024 1.00 38.34 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? -2.994 6.378   20.154 1.00 37.29 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? -2.689 6.085   18.785 1.00 39.40 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? -3.278 7.860   20.291 1.00 38.24 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? -0.945 3.776   20.189 1.00 34.29 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? -0.782 2.324   20.188 1.00 33.63 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 0.396  1.876   21.072 1.00 33.20 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 1.354  2.628   21.259 1.00 32.97 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? -0.581 1.830   18.765 1.00 33.59 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 0.335  0.651   21.585 1.00 32.62 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 1.416  0.115   22.422 1.00 33.23 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 2.560  -0.337  21.542 1.00 32.24 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 2.312  -0.979  20.512 1.00 32.13 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 0.909  -1.070  23.243 1.00 37.22 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 1.712  -1.290  24.522 1.00 44.25 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 1.298  -0.289  25.590 1.00 52.59 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 0.157  0.196   25.637 1.00 55.78 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 2.213  0.039   26.491 1.00 54.38 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 3.790  0.022   21.929 1.00 31.02 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 4.992  -0.280  21.174 1.00 30.85 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 5.471  -1.708  21.201 1.00 31.30 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 5.248  -2.405  22.188 1.00 33.01 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 6.261  -2.082  20.145 1.00 28.39 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 6.819  -3.406  19.850 1.00 26.42 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 8.183  -3.703  20.502 1.00 25.35 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 8.534  -4.872  20.648 1.00 24.01 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 6.886  -3.617  18.335 1.00 26.75 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 7.986  -2.465  17.435 1.00 29.41 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 8.936  -2.676  20.908 1.00 24.39 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 10.313 -2.816  21.409 1.00 22.92 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 10.466 -2.831  22.934 1.00 22.73 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 9.567  -2.353  23.642 1.00 23.85 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 11.153 -1.652  20.830 1.00 22.56 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 11.355 -1.706  19.318 1.00 24.84 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 11.858 -2.769  18.820 1.00 24.71 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 11.071 -0.656  18.619 1.00 21.79 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 11.623 -3.372  23.450 1.00 21.30 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 12.058 -3.358  24.851 1.00 21.81 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 13.519 -2.763  24.941 1.00 20.11 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 14.306 -2.918  24.010 1.00 19.80 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 11.872 -4.689  25.558 1.00 25.59 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 12.779 -5.625  25.005 1.00 27.23 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 10.435 -5.230  25.463 1.00 27.14 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 13.841 -2.032  26.034 1.00 18.61 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 15.106 -1.297  26.137 1.00 17.02 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 16.085 -2.027  27.031 1.00 17.20 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 15.708 -2.517  28.105 1.00 18.01 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 14.839 0.107   26.762 1.00 17.06 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 13.714 0.860   26.005 1.00 18.30 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 16.127 0.978   26.758 1.00 17.71 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 14.054 1.147   24.511 1.00 18.69 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.340 -2.122  26.589 1.00 15.08 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 18.380 -2.764  27.390 1.00 15.70 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 18.717 -1.876  28.598 1.00 16.45 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 18.736 -0.654  28.481 1.00 16.66 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 19.641 -2.933  26.532 1.00 14.70 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 19.037 -2.501  29.753 1.00 16.48 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 19.452 -1.752  30.962 1.00 17.16 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 20.725 -2.497  31.394 1.00 18.76 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 20.676 -3.447  32.178 1.00 19.64 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 18.372 -1.818  32.041 1.00 17.83 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.023 -1.265  31.583 1.00 18.26 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.039 0.243   31.276 1.00 19.89 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 15.693 0.697   30.908 1.00 19.11 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 15.436 1.828   30.251 1.00 20.36 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 16.421 2.653   29.921 1.00 17.71 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 14.190 2.153   29.945 1.00 20.05 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 21.841 -2.115  30.796 1.00 18.64 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 23.093 -2.868  30.892 1.00 19.54 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 24.292 -1.968  30.521 1.00 20.00 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 24.119 -0.813  30.129 1.00 20.36 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 23.022 -4.051  29.931 1.00 19.30 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 23.043 -3.543  28.186 1.00 19.74 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 25.514 -2.562  30.566 1.00 21.02 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 26.736 -1.865  30.145 1.00 21.36 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 27.416 -2.606  29.006 1.00 21.59 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 28.637 -2.529  28.869 1.00 22.29 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 27.724 -1.703  31.335 1.00 25.74 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 28.183 -3.006  31.970 1.00 33.17 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 27.721 -4.079  31.538 1.00 32.31 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 29.008 -2.949  32.905 1.00 40.87 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 26.630 -3.279  28.129 1.00 19.77 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 27.222 -3.965  26.970 1.00 18.97 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 27.978 -2.980  26.088 1.00 18.60 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 27.562 -1.821  25.926 1.00 17.86 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 26.139 -4.662  26.150 1.00 18.45 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 25.487 -6.196  26.887 1.00 19.98 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 29.063 -3.451  25.498 1.00 17.03 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 29.858 -2.697  24.526 1.00 16.99 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 30.018 -3.483  23.209 1.00 15.85 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 30.884 -3.165  22.402 1.00 17.07 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 31.237 -2.316  25.060 1.00 19.95 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 31.196 -1.115  25.946 1.00 23.79 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 32.611 -0.754  26.355 1.00 27.74 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 33.019 -0.992  27.505 1.00 28.60 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 33.383 -0.167  25.426 1.00 25.16 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 29.196 -4.537  23.015 1.00 15.45 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 29.092 -5.236  21.738 1.00 15.46 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 27.592 -5.412  21.446 1.00 14.46 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 26.745 -5.521  22.360 1.00 15.92 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 29.833 -6.584  21.719 1.00 17.74 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 29.157 -7.446  22.621 1.00 19.41 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 31.302 -6.468  22.112 1.00 18.44 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 27.278 -5.452  20.154 1.00 13.75 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 25.893 -5.611  19.736 1.00 13.70 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 25.826 -5.707  18.223 1.00 13.81 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 26.851 -5.964  17.569 1.00 14.40 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 24.621 -5.584  17.686 1.00 13.46 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 24.370 -5.690  16.256 1.00 13.98 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 23.508 -4.495  15.869 1.00 13.78 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 22.502 -4.226  16.561 1.00 14.51 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 23.629 -7.019  15.957 1.00 16.17 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 23.195 -7.072  14.482 1.00 16.63 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 24.537 -8.209  16.262 1.00 17.83 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 23.832 -3.809  14.744 1.00 14.76 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 22.989 -2.706  14.295 1.00 13.53 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 22.472 -2.945  12.887 1.00 13.62 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 23.080 -3.686  12.125 1.00 13.91 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 23.720 -1.327  14.349 1.00 13.40 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 24.746 -1.081  13.255 1.00 13.79 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 25.991 -1.700  13.290 1.00 13.86 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 24.490 -0.195  12.213 1.00 14.57 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 26.957 -1.437  12.326 1.00 14.17 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 25.454 0.073   11.238 1.00 15.36 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 26.669 -0.587  11.274 1.00 15.98 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 27.652 -0.357  10.320 1.00 17.30 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 21.369 -2.280  12.547 1.00 12.87 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 20.822 -2.375  11.208 1.00 13.10 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 21.368 -1.206  10.380 1.00 14.31 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 21.240 -0.037  10.796 1.00 13.63 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 19.279 -2.337  11.240 1.00 13.57 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 18.717 -2.455  9.858  1.00 14.45 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 18.888 -3.613  9.123  1.00 15.14 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 18.091 -1.375  9.251  1.00 15.76 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 18.408 -3.718  7.827  1.00 16.92 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.624 -1.458  7.953  1.00 17.21 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.792 -2.627  7.244  1.00 18.25 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.304 -2.727  5.964  1.00 22.33 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 21.910 -1.519  9.184  1.00 14.43 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 22.487 -0.529  8.266  1.00 13.47 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 21.584 -0.474  7.008  1.00 14.50 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 21.692 -1.338  6.127  1.00 14.71 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 23.914 -0.952  7.910  1.00 14.13 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 24.697 0.083   6.631  1.00 16.72 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 20.718 0.557   6.924  1.00 14.63 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 19.782 0.618   5.794  1.00 16.64 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 20.459 0.756   4.433  1.00 16.59 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 19.967 0.191   3.441  1.00 16.19 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 18.738 1.711   6.008  1.00 21.72 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 19.359 2.980   6.058  1.00 28.11 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 21.630 1.435   4.366  1.00 14.48 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 22.363 1.582   3.106  1.00 15.60 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 22.993 0.298   2.585  1.00 15.34 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 23.510 0.298   1.451  1.00 15.57 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 23.428 2.672   3.184  1.00 17.47 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 24.417 2.348   4.148  1.00 17.97 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 22.928 -0.793  3.356  1.00 13.67 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 23.373 -2.101  2.887  1.00 13.88 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 22.228 -3.165  3.048  1.00 15.34 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 22.459 -4.338  2.742  1.00 17.21 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 24.601 -2.570  3.716  1.00 15.35 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 25.864 -1.717  3.458  1.00 17.12 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 26.471 -2.035  2.097  1.00 18.64 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 27.675 -1.230  1.816  1.00 19.67 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 27.653 -0.017  1.270  1.00 20.85 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 26.502 0.543   0.923  1.00 19.62 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 28.793 0.637   1.033  1.00 20.53 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 21.049 -2.762  3.584  1.00 16.09 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 19.933 -3.666  3.920  1.00 18.59 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 20.459 -4.880  4.724  1.00 18.46 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 20.135 -6.048  4.425  1.00 19.97 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 19.204 -4.162  2.665  1.00 21.63 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 18.459 -3.113  1.955  1.00 28.52 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.323 -3.815  1.188  1.00 32.33 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 16.747 -2.890  0.239  1.00 34.24 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.016 -2.877  -1.062 1.00 33.55 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.834 -3.795  -1.594 1.00 32.93 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 16.504 -1.936  -1.837 1.00 31.69 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 21.323 -4.611  5.697  1.00 16.71 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 21.979 -5.714  6.430  1.00 16.67 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 22.264 -5.331  7.854  1.00 15.84 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 22.435 -4.159  8.143  1.00 16.93 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 23.359 -6.037  5.807  1.00 19.09 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 23.328 -7.051  4.658  1.00 28.88 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 24.753 -7.401  4.213  1.00 36.44 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 24.784 -8.576  3.243  1.00 42.57 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 25.366 -8.198  1.927  1.00 46.88 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 22.378 -6.324  8.717  1.00 15.24 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 22.794 -6.117  10.094 1.00 14.86 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 24.288 -6.438  10.218 1.00 15.89 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 24.803 -7.391  9.589  1.00 17.15 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 22.030 -7.044  11.033 1.00 14.29 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 20.548 -6.804  11.070 1.00 16.70 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 19.953 -6.066  12.083 1.00 19.64 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 19.583 -7.287  10.263 1.00 16.54 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 18.653 -6.105  11.838 1.00 18.87 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 18.383 -6.806  10.750 1.00 20.34 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 24.993 -5.664  11.073 1.00 13.71 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 26.433 -5.898  11.265 1.00 13.48 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 26.751 -5.941  12.762 1.00 14.15 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 26.209 -5.154  13.537 1.00 15.10 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 27.265 -4.720  10.682 1.00 14.70 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 27.259 -4.636  9.171  1.00 16.28 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 27.979 -5.547  8.390  1.00 17.64 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 26.584 -3.622  8.519  1.00 16.73 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 27.984 -5.469  6.989  1.00 18.76 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 26.600 -3.517  7.124  1.00 17.69 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 27.297 -4.445  6.361  1.00 19.85 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 27.298 -4.333  4.977  1.00 22.07 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 27.654 -6.825  13.178 1.00 14.14 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 28.105 -6.828  14.583 1.00 14.54 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 29.113 -5.674  14.831 1.00 16.66 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 29.912 -5.338  13.931 1.00 18.20 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 28.819 -8.185  14.723 1.00 15.76 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 29.284 -8.485  13.324 1.00 16.37 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 28.353 -7.843  12.353 1.00 14.28 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 29.111 -5.086  16.060 1.00 15.30 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 29.990 -3.942  16.356 1.00 16.07 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 30.507 -4.013  17.773 1.00 16.14 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 29.848 -4.559  18.655 1.00 16.35 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 29.264 -2.558  16.244 1.00 17.51 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 29.247 -2.046  14.809 1.00 18.77 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 27.846 -2.620  16.808 1.00 18.44 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 31.711 -3.444  17.987 1.00 16.03 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 32.226 -3.171  19.330 1.00 16.66 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 32.118 -1.641  19.423 1.00 15.69 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 32.587 -0.968  18.496 1.00 16.61 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 33.692 -3.572  19.438 1.00 20.86 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 33.719 -4.988  19.395 1.00 26.59 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 31.499 -1.104  20.493 1.00 14.34 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 31.297 0.334   20.563 1.00 14.98 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 31.789 0.919   21.872 1.00 15.43 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 31.840 0.240   22.900 1.00 16.77 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 29.816 0.690   20.281 1.00 14.68 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 28.775 -0.072  21.096 1.00 14.36 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 28.273 -1.296  20.657 1.00 14.93 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 28.289 0.443   22.300 1.00 14.79 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 27.275 -1.969  21.390 1.00 15.01 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 27.308 -0.254  23.050 1.00 15.28 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 26.809 -1.448  22.588 1.00 15.59 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 32.196 2.210   21.829 1.00 14.67 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 32.676 2.883   23.023 1.00 15.55 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 31.531 3.243   23.970 1.00 16.77 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 30.365 3.231   23.570 1.00 17.05 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 33.452 4.143   22.646 1.00 17.59 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 32.615 5.054   21.948 1.00 20.40 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 31.852 3.515   25.266 1.00 16.32 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 30.826 3.903   26.242 1.00 17.17 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 30.264 5.265   25.862 1.00 18.27 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 30.967 6.077   25.258 1.00 18.91 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 31.482 4.002   27.641 1.00 21.21 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 31.812 2.632   28.197 1.00 25.85 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 32.385 2.797   29.612 1.00 30.63 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 32.902 1.488   30.132 1.00 38.28 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 33.532 1.651   31.481 1.00 43.18 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 29.017 5.575   26.283 1.00 18.22 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 28.431 6.884   25.934 1.00 18.17 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 29.301 8.030   26.418 1.00 18.59 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 29.686 8.062   27.599 1.00 19.39 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 27.083 6.900   26.660 1.00 19.30 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 26.782 5.462   26.981 1.00 21.29 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 28.076 4.718   27.039 1.00 19.18 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 29.626 8.958   25.497 1.00 17.04 ? 80  SER   A N   1 
ATOM   582  C  CA  A SER   A 1 74  ? 30.496 10.063  25.873 0.50 18.29 ? 80  SER   A CA  1 
ATOM   583  C  CA  B SER   A 1 74  ? 30.549 10.045  25.815 0.50 18.06 ? 80  SER   A CA  1 
ATOM   584  C  C   . SER   A 1 74  ? 30.213 11.324  25.062 1.00 18.00 ? 80  SER   A C   1 
ATOM   585  O  O   . SER   A 1 74  ? 29.346 11.319  24.179 1.00 17.52 ? 80  SER   A O   1 
ATOM   586  C  CB  A SER   A 1 74  ? 31.964 9.641   25.747 0.50 20.33 ? 80  SER   A CB  1 
ATOM   587  C  CB  B SER   A 1 74  ? 31.982 9.629   25.451 0.50 19.40 ? 80  SER   A CB  1 
ATOM   588  O  OG  A SER   A 1 74  ? 32.329 9.497   24.387 0.50 22.43 ? 80  SER   A OG  1 
ATOM   589  O  OG  B SER   A 1 74  ? 32.323 8.331   25.907 0.50 21.47 ? 80  SER   A OG  1 
ATOM   590  N  N   . LEU   A 1 75  ? 30.955 12.434  25.379 1.00 17.95 ? 81  LEU   A N   1 
ATOM   591  C  CA  . LEU   A 1 75  ? 30.815 13.723  24.698 1.00 19.49 ? 81  LEU   A CA  1 
ATOM   592  C  C   . LEU   A 1 75  ? 31.803 13.691  23.552 1.00 20.73 ? 81  LEU   A C   1 
ATOM   593  O  O   . LEU   A 1 75  ? 33.019 13.614  23.807 1.00 21.14 ? 81  LEU   A O   1 
ATOM   594  C  CB  . LEU   A 1 75  ? 31.275 14.837  25.668 1.00 20.93 ? 81  LEU   A CB  1 
ATOM   595  C  CG  . LEU   A 1 75  ? 30.237 15.649  26.350 1.00 25.50 ? 81  LEU   A CG  1 
ATOM   596  C  CD1 . LEU   A 1 75  ? 30.916 16.693  27.259 1.00 26.76 ? 81  LEU   A CD1 1 
ATOM   597  C  CD2 . LEU   A 1 75  ? 29.281 16.341  25.349 1.00 25.69 ? 81  LEU   A CD2 1 
ATOM   598  N  N   . ILE   A 1 76  ? 31.315 13.790  22.306 1.00 19.50 ? 82  ILE   A N   1 
ATOM   599  C  CA  . ILE   A 1 76  ? 32.138 13.650  21.111 1.00 20.89 ? 82  ILE   A CA  1 
ATOM   600  C  C   . ILE   A 1 76  ? 31.900 14.802  20.175 1.00 20.78 ? 82  ILE   A C   1 
ATOM   601  O  O   . ILE   A 1 76  ? 30.741 15.159  19.947 1.00 21.14 ? 82  ILE   A O   1 
ATOM   602  C  CB  . ILE   A 1 76  ? 31.765 12.291  20.447 1.00 23.47 ? 82  ILE   A CB  1 
ATOM   603  C  CG1 . ILE   A 1 76  ? 32.173 11.141  21.378 1.00 25.82 ? 82  ILE   A CG1 1 
ATOM   604  C  CG2 . ILE   A 1 76  ? 32.381 12.146  19.058 1.00 24.54 ? 82  ILE   A CG2 1 
ATOM   605  C  CD1 . ILE   A 1 76  ? 31.922 9.798   20.914 1.00 28.40 ? 82  ILE   A CD1 1 
ATOM   606  N  N   . PHE   A 1 77  ? 32.977 15.398  19.626 1.00 20.17 ? 83  PHE   A N   1 
ATOM   607  C  CA  . PHE   A 1 77  ? 32.817 16.501  18.691 1.00 20.80 ? 83  PHE   A CA  1 
ATOM   608  C  C   . PHE   A 1 77  ? 32.193 16.010  17.374 1.00 20.99 ? 83  PHE   A C   1 
ATOM   609  O  O   . PHE   A 1 77  ? 32.649 15.008  16.810 1.00 21.78 ? 83  PHE   A O   1 
ATOM   610  C  CB  . PHE   A 1 77  ? 34.192 17.159  18.399 1.00 21.64 ? 83  PHE   A CB  1 
ATOM   611  C  CG  . PHE   A 1 77  ? 34.079 18.345  17.475 1.00 24.38 ? 83  PHE   A CG  1 
ATOM   612  C  CD1 . PHE   A 1 77  ? 34.375 18.224  16.126 1.00 26.17 ? 83  PHE   A CD1 1 
ATOM   613  C  CD2 . PHE   A 1 77  ? 33.613 19.554  17.936 1.00 26.51 ? 83  PHE   A CD2 1 
ATOM   614  C  CE1 . PHE   A 1 77  ? 34.264 19.311  15.272 1.00 27.19 ? 83  PHE   A CE1 1 
ATOM   615  C  CE2 . PHE   A 1 77  ? 33.485 20.637  17.073 1.00 27.96 ? 83  PHE   A CE2 1 
ATOM   616  C  CZ  . PHE   A 1 77  ? 33.840 20.511  15.755 1.00 27.33 ? 83  PHE   A CZ  1 
ATOM   617  N  N   . VAL   A 1 78  ? 31.140 16.720  16.890 1.00 19.90 ? 84  VAL   A N   1 
ATOM   618  C  CA  . VAL   A 1 78  ? 30.489 16.376  15.625 1.00 19.81 ? 84  VAL   A CA  1 
ATOM   619  C  C   . VAL   A 1 78  ? 30.539 17.609  14.734 1.00 21.52 ? 84  VAL   A C   1 
ATOM   620  O  O   . VAL   A 1 78  ? 30.084 18.692  15.145 1.00 22.10 ? 84  VAL   A O   1 
ATOM   621  C  CB  . VAL   A 1 78  ? 29.010 15.933  15.838 1.00 19.71 ? 84  VAL   A CB  1 
ATOM   622  C  CG1 . VAL   A 1 78  ? 28.364 15.584  14.493 1.00 20.64 ? 84  VAL   A CG1 1 
ATOM   623  C  CG2 . VAL   A 1 78  ? 28.934 14.741  16.777 1.00 18.90 ? 84  VAL   A CG2 1 
ATOM   624  N  N   . GLU   A 1 79  ? 31.038 17.440  13.503 1.00 22.32 ? 85  GLU   A N   1 
ATOM   625  C  CA  . GLU   A 1 79  ? 31.199 18.556  12.550 1.00 23.20 ? 85  GLU   A CA  1 
ATOM   626  C  C   . GLU   A 1 79  ? 29.830 19.160  12.178 1.00 23.18 ? 85  GLU   A C   1 
ATOM   627  O  O   . GLU   A 1 79  ? 28.811 18.484  12.316 1.00 22.16 ? 85  GLU   A O   1 
ATOM   628  C  CB  . GLU   A 1 79  ? 31.898 18.018  11.286 1.00 27.49 ? 85  GLU   A CB  1 
ATOM   629  C  CG  . GLU   A 1 79  ? 32.685 19.063  10.516 1.00 39.01 ? 85  GLU   A CG  1 
ATOM   630  C  CD  . GLU   A 1 79  ? 33.361 18.541  9.261  1.00 50.53 ? 85  GLU   A CD  1 
ATOM   631  O  OE1 . GLU   A 1 79  ? 33.696 19.367  8.378  1.00 53.71 ? 85  GLU   A OE1 1 
ATOM   632  O  OE2 . GLU   A 1 79  ? 33.553 17.306  9.159  1.00 53.14 ? 85  GLU   A OE2 1 
ATOM   633  N  N   . ALA   A 1 80  ? 29.807 20.435  11.716 1.00 23.16 ? 86  ALA   A N   1 
ATOM   634  C  CA  . ALA   A 1 80  ? 28.558 21.083  11.328 1.00 23.24 ? 86  ALA   A CA  1 
ATOM   635  C  C   . ALA   A 1 80  ? 27.911 20.335  10.169 1.00 23.26 ? 86  ALA   A C   1 
ATOM   636  O  O   . ALA   A 1 80  ? 28.609 19.773  9.318  1.00 23.55 ? 86  ALA   A O   1 
ATOM   637  C  CB  . ALA   A 1 80  ? 28.822 22.526  10.896 1.00 23.58 ? 86  ALA   A CB  1 
ATOM   638  N  N   . SER   A 1 81  ? 26.579 20.314  10.156 1.00 22.45 ? 87  SER   A N   1 
ATOM   639  C  CA  . SER   A 1 81  ? 25.784 19.725  9.091  1.00 22.33 ? 87  SER   A CA  1 
ATOM   640  C  C   . SER   A 1 81  ? 24.652 20.730  8.775  1.00 23.94 ? 87  SER   A C   1 
ATOM   641  O  O   . SER   A 1 81  ? 24.590 21.803  9.402  1.00 24.43 ? 87  SER   A O   1 
ATOM   642  C  CB  . SER   A 1 81  ? 25.182 18.395  9.573  1.00 22.61 ? 87  SER   A CB  1 
ATOM   643  O  OG  . SER   A 1 81  ? 24.222 18.600  10.599 1.00 22.79 ? 87  SER   A OG  1 
ATOM   644  N  N   . GLU   A 1 82  ? 23.753 20.388  7.826  1.00 24.89 ? 88  GLU   A N   1 
ATOM   645  C  CA  . GLU   A 1 82  ? 22.612 21.269  7.583  1.00 26.43 ? 88  GLU   A CA  1 
ATOM   646  C  C   . GLU   A 1 82  ? 21.626 21.263  8.792  1.00 25.95 ? 88  GLU   A C   1 
ATOM   647  O  O   . GLU   A 1 82  ? 20.794 22.157  8.927  1.00 27.01 ? 88  GLU   A O   1 
ATOM   648  C  CB  . GLU   A 1 82  ? 21.921 20.911  6.257  1.00 31.68 ? 88  GLU   A CB  1 
ATOM   649  C  CG  . GLU   A 1 82  ? 21.298 19.536  6.239  1.00 41.44 ? 88  GLU   A CG  1 
ATOM   650  C  CD  . GLU   A 1 82  ? 21.204 18.947  4.845  1.00 54.91 ? 88  GLU   A CD  1 
ATOM   651  O  OE1 . GLU   A 1 82  ? 20.796 19.678  3.910  1.00 58.22 ? 88  GLU   A OE1 1 
ATOM   652  O  OE2 . GLU   A 1 82  ? 21.552 17.753  4.685  1.00 58.81 ? 88  GLU   A OE2 1 
ATOM   653  N  N   . TYR   A 1 83  ? 21.775 20.282  9.717  1.00 23.44 ? 89  TYR   A N   1 
ATOM   654  C  CA  . TYR   A 1 83  ? 20.888 20.148  10.857 1.00 22.76 ? 89  TYR   A CA  1 
ATOM   655  C  C   . TYR   A 1 83  ? 21.382 20.792  12.142 1.00 21.59 ? 89  TYR   A C   1 
ATOM   656  O  O   . TYR   A 1 83  ? 20.559 21.155  12.976 1.00 22.35 ? 89  TYR   A O   1 
ATOM   657  C  CB  . TYR   A 1 83  ? 20.604 18.666  11.121 1.00 21.96 ? 89  TYR   A CB  1 
ATOM   658  C  CG  . TYR   A 1 83  ? 20.005 17.969  9.922  1.00 22.82 ? 89  TYR   A CG  1 
ATOM   659  C  CD1 . TYR   A 1 83  ? 20.789 17.194  9.081  1.00 23.83 ? 89  TYR   A CD1 1 
ATOM   660  C  CD2 . TYR   A 1 83  ? 18.655 18.080  9.630  1.00 23.26 ? 89  TYR   A CD2 1 
ATOM   661  C  CE1 . TYR   A 1 83  ? 20.227 16.493  8.011  1.00 25.23 ? 89  TYR   A CE1 1 
ATOM   662  C  CE2 . TYR   A 1 83  ? 18.095 17.439  8.526  1.00 24.73 ? 89  TYR   A CE2 1 
ATOM   663  C  CZ  . TYR   A 1 83  ? 18.874 16.614  7.743  1.00 26.26 ? 89  TYR   A CZ  1 
ATOM   664  O  OH  . TYR   A 1 83  ? 18.309 15.974  6.651  1.00 28.75 ? 89  TYR   A OH  1 
ATOM   665  N  N   . TYR   A 1 84  ? 22.697 20.886  12.335 1.00 20.34 ? 90  TYR   A N   1 
ATOM   666  C  CA  . TYR   A 1 84  ? 23.239 21.432  13.586 1.00 20.48 ? 90  TYR   A CA  1 
ATOM   667  C  C   . TYR   A 1 84  ? 24.511 22.185  13.338 1.00 22.47 ? 90  TYR   A C   1 
ATOM   668  O  O   . TYR   A 1 84  ? 25.287 21.803  12.460 1.00 22.20 ? 90  TYR   A O   1 
ATOM   669  C  CB  . TYR   A 1 84  ? 23.640 20.288  14.555 1.00 19.59 ? 90  TYR   A CB  1 
ATOM   670  C  CG  . TYR   A 1 84  ? 22.528 19.402  15.068 1.00 18.06 ? 90  TYR   A CG  1 
ATOM   671  C  CD1 . TYR   A 1 84  ? 21.637 19.858  16.025 1.00 18.37 ? 90  TYR   A CD1 1 
ATOM   672  C  CD2 . TYR   A 1 84  ? 22.379 18.107  14.610 1.00 18.23 ? 90  TYR   A CD2 1 
ATOM   673  C  CE1 . TYR   A 1 84  ? 20.639 19.035  16.536 1.00 16.95 ? 90  TYR   A CE1 1 
ATOM   674  C  CE2 . TYR   A 1 84  ? 21.381 17.270  15.110 1.00 17.15 ? 90  TYR   A CE2 1 
ATOM   675  C  CZ  . TYR   A 1 84  ? 20.519 17.730  16.084 1.00 16.40 ? 90  TYR   A CZ  1 
ATOM   676  O  OH  . TYR   A 1 84  ? 19.502 16.929  16.568 1.00 16.11 ? 90  TYR   A OH  1 
ATOM   677  N  N   . PRO   A 1 85  ? 24.821 23.161  14.195 1.00 23.57 ? 91  PRO   A N   1 
ATOM   678  C  CA  . PRO   A 1 85  ? 26.157 23.779  14.111 1.00 24.55 ? 91  PRO   A CA  1 
ATOM   679  C  C   . PRO   A 1 85  ? 27.197 22.768  14.603 1.00 24.79 ? 91  PRO   A C   1 
ATOM   680  O  O   . PRO   A 1 85  ? 26.863 21.746  15.239 1.00 24.46 ? 91  PRO   A O   1 
ATOM   681  C  CB  . PRO   A 1 85  ? 26.045 24.955  15.089 1.00 25.61 ? 91  PRO   A CB  1 
ATOM   682  C  CG  . PRO   A 1 85  ? 25.054 24.490  16.118 1.00 26.55 ? 91  PRO   A CG  1 
ATOM   683  C  CD  . PRO   A 1 85  ? 24.036 23.684  15.335 1.00 24.02 ? 91  PRO   A CD  1 
ATOM   684  N  N   . ALA   A 1 86  ? 28.504 23.075  14.403 1.00 24.26 ? 92  ALA   A N   1 
ATOM   685  C  CA  . ALA   A 1 86  ? 29.572 22.218  14.940 1.00 24.83 ? 92  ALA   A CA  1 
ATOM   686  C  C   . ALA   A 1 86  ? 29.420 22.239  16.484 1.00 24.47 ? 92  ALA   A C   1 
ATOM   687  O  O   . ALA   A 1 86  ? 29.108 23.307  17.031 1.00 24.70 ? 92  ALA   A O   1 
ATOM   688  C  CB  . ALA   A 1 86  ? 30.931 22.787  14.543 1.00 26.23 ? 92  ALA   A CB  1 
ATOM   689  N  N   . ARG   A 1 87  ? 29.476 21.060  17.145 1.00 23.20 ? 93  ARG   A N   1 
ATOM   690  C  CA  . ARG   A 1 87  ? 29.187 21.028  18.587 1.00 22.06 ? 93  ARG   A CA  1 
ATOM   691  C  C   . ARG   A 1 87  ? 29.630 19.703  19.207 1.00 21.45 ? 93  ARG   A C   1 
ATOM   692  O  O   . ARG   A 1 87  ? 30.003 18.785  18.478 1.00 22.39 ? 93  ARG   A O   1 
ATOM   693  C  CB  . ARG   A 1 87  ? 27.647 21.192  18.789 1.00 22.18 ? 93  ARG   A CB  1 
ATOM   694  C  CG  . ARG   A 1 87  ? 26.879 19.897  18.353 1.00 22.51 ? 93  ARG   A CG  1 
ATOM   695  C  CD  . ARG   A 1 87  ? 25.416 20.109  17.989 1.00 22.17 ? 93  ARG   A CD  1 
ATOM   696  N  NE  . ARG   A 1 87  ? 24.529 18.990  18.382 1.00 20.98 ? 93  ARG   A NE  1 
ATOM   697  C  CZ  . ARG   A 1 87  ? 24.475 17.817  17.749 1.00 19.48 ? 93  ARG   A CZ  1 
ATOM   698  N  NH1 . ARG   A 1 87  ? 23.614 16.875  18.146 1.00 17.98 ? 93  ARG   A NH1 1 
ATOM   699  N  NH2 . ARG   A 1 87  ? 25.322 17.551  16.756 1.00 19.62 ? 93  ARG   A NH2 1 
ATOM   700  N  N   . TYR   A 1 88  ? 29.561 19.584  20.535 1.00 20.72 ? 94  TYR   A N   1 
ATOM   701  C  CA  . TYR   A 1 88  ? 29.787 18.288  21.182 1.00 21.03 ? 94  TYR   A CA  1 
ATOM   702  C  C   . TYR   A 1 88  ? 28.437 17.611  21.362 1.00 19.93 ? 94  TYR   A C   1 
ATOM   703  O  O   . TYR   A 1 88  ? 27.515 18.213  21.911 1.00 20.51 ? 94  TYR   A O   1 
ATOM   704  C  CB  . TYR   A 1 88  ? 30.452 18.433  22.559 1.00 21.96 ? 94  TYR   A CB  1 
ATOM   705  C  CG  . TYR   A 1 88  ? 31.893 18.868  22.429 1.00 23.96 ? 94  TYR   A CG  1 
ATOM   706  C  CD1 . TYR   A 1 88  ? 32.920 17.940  22.392 1.00 25.51 ? 94  TYR   A CD1 1 
ATOM   707  C  CD2 . TYR   A 1 88  ? 32.220 20.203  22.290 1.00 25.78 ? 94  TYR   A CD2 1 
ATOM   708  C  CE1 . TYR   A 1 88  ? 34.250 18.340  22.244 1.00 27.99 ? 94  TYR   A CE1 1 
ATOM   709  C  CE2 . TYR   A 1 88  ? 33.538 20.613  22.114 1.00 27.79 ? 94  TYR   A CE2 1 
ATOM   710  C  CZ  . TYR   A 1 88  ? 34.551 19.679  22.095 1.00 29.48 ? 94  TYR   A CZ  1 
ATOM   711  O  OH  . TYR   A 1 88  ? 35.856 20.122  21.936 1.00 33.13 ? 94  TYR   A OH  1 
ATOM   712  N  N   . GLN   A 1 89  ? 28.307 16.389  20.867 1.00 17.50 ? 95  GLN   A N   1 
ATOM   713  C  CA  . GLN   A 1 89  ? 27.077 15.629  21.059 1.00 16.21 ? 95  GLN   A CA  1 
ATOM   714  C  C   . GLN   A 1 89  ? 27.336 14.695  22.263 1.00 16.85 ? 95  GLN   A C   1 
ATOM   715  O  O   . GLN   A 1 89  ? 28.375 14.008  22.316 1.00 18.77 ? 95  GLN   A O   1 
ATOM   716  C  CB  . GLN   A 1 89  ? 26.720 14.832  19.799 1.00 15.82 ? 95  GLN   A CB  1 
ATOM   717  C  CG  . GLN   A 1 89  ? 25.495 13.920  20.026 1.00 14.54 ? 95  GLN   A CG  1 
ATOM   718  C  CD  . GLN   A 1 89  ? 24.850 13.468  18.741 1.00 16.63 ? 95  GLN   A CD  1 
ATOM   719  O  OE1 . GLN   A 1 89  ? 24.781 14.223  17.756 1.00 17.93 ? 95  GLN   A OE1 1 
ATOM   720  N  NE2 . GLN   A 1 89  ? 24.374 12.213  18.721 1.00 15.09 ? 95  GLN   A NE2 1 
ATOM   721  N  N   . SER   A 1 90  ? 26.416 14.677  23.230 1.00 15.06 ? 96  SER   A N   1 
ATOM   722  C  CA  . SER   A 1 90  ? 26.567 13.862  24.432 1.00 15.19 ? 96  SER   A CA  1 
ATOM   723  C  C   . SER   A 1 90  ? 25.887 12.497  24.281 1.00 16.52 ? 96  SER   A C   1 
ATOM   724  O  O   . SER   A 1 90  ? 25.083 12.304  23.340 1.00 16.30 ? 96  SER   A O   1 
ATOM   725  C  CB  . SER   A 1 90  ? 26.012 14.614  25.635 1.00 18.07 ? 96  SER   A CB  1 
ATOM   726  O  OG  . SER   A 1 90  ? 24.626 14.860  25.481 1.00 20.15 ? 96  SER   A OG  1 
ATOM   727  N  N   . HIS   A 1 91  ? 26.285 11.531  25.143 1.00 16.15 ? 97  HIS   A N   1 
ATOM   728  C  CA  . HIS   A 1 91  ? 25.688 10.189  25.191 1.00 16.25 ? 97  HIS   A CA  1 
ATOM   729  C  C   . HIS   A 1 91  ? 25.849 9.472   23.842 1.00 14.98 ? 97  HIS   A C   1 
ATOM   730  O  O   . HIS   A 1 91  ? 25.010 8.642   23.507 1.00 15.57 ? 97  HIS   A O   1 
ATOM   731  C  CB  . HIS   A 1 91  ? 24.187 10.279  25.598 1.00 18.33 ? 97  HIS   A CB  1 
ATOM   732  C  CG  . HIS   A 1 91  ? 24.005 10.862  26.973 1.00 21.13 ? 97  HIS   A CG  1 
ATOM   733  N  ND1 . HIS   A 1 91  ? 23.904 10.046  28.099 1.00 23.38 ? 97  HIS   A ND1 1 
ATOM   734  C  CD2 . HIS   A 1 91  ? 23.915 12.157  27.365 1.00 21.83 ? 97  HIS   A CD2 1 
ATOM   735  C  CE1 . HIS   A 1 91  ? 23.785 10.877  29.138 1.00 24.05 ? 97  HIS   A CE1 1 
ATOM   736  N  NE2 . HIS   A 1 91  ? 23.780 12.155  28.742 1.00 23.81 ? 97  HIS   A NE2 1 
ATOM   737  N  N   . LEU   A 1 92  ? 26.985 9.728   23.136 1.00 14.09 ? 98  LEU   A N   1 
ATOM   738  C  CA  . LEU   A 1 92  ? 27.228 9.143   21.817 1.00 14.27 ? 98  LEU   A CA  1 
ATOM   739  C  C   . LEU   A 1 92  ? 28.290 8.015   21.940 1.00 15.41 ? 98  LEU   A C   1 
ATOM   740  O  O   . LEU   A 1 92  ? 29.255 8.137   22.711 1.00 15.46 ? 98  LEU   A O   1 
ATOM   741  C  CB  . LEU   A 1 92  ? 27.765 10.258  20.874 1.00 15.34 ? 98  LEU   A CB  1 
ATOM   742  C  CG  . LEU   A 1 92  ? 28.010 9.896   19.390 1.00 17.81 ? 98  LEU   A CG  1 
ATOM   743  C  CD1 . LEU   A 1 92  ? 26.690 9.469   18.658 1.00 18.66 ? 98  LEU   A CD1 1 
ATOM   744  C  CD2 . LEU   A 1 92  ? 28.586 11.142  18.617 1.00 19.61 ? 98  LEU   A CD2 1 
ATOM   745  N  N   . MET   A 1 93  ? 28.060 6.919   21.207 1.00 15.29 ? 99  MET   A N   1 
ATOM   746  C  CA  . MET   A 1 93  ? 28.959 5.758   21.217 1.00 15.44 ? 99  MET   A CA  1 
ATOM   747  C  C   . MET   A 1 93  ? 29.455 5.524   19.819 1.00 15.74 ? 99  MET   A C   1 
ATOM   748  O  O   . MET   A 1 93  ? 28.637 5.477   18.891 1.00 15.99 ? 99  MET   A O   1 
ATOM   749  C  CB  . MET   A 1 93  ? 28.150 4.540   21.663 1.00 16.99 ? 99  MET   A CB  1 
ATOM   750  C  CG  . MET   A 1 93  ? 27.591 4.707   23.083 1.00 18.00 ? 99  MET   A CG  1 
ATOM   751  S  SD  . MET   A 1 93  ? 26.452 3.393   23.636 1.00 19.65 ? 99  MET   A SD  1 
ATOM   752  C  CE  . MET   A 1 93  ? 25.082 3.580   22.426 1.00 21.13 ? 99  MET   A CE  1 
ATOM   753  N  N   . LEU   A 1 94  ? 30.788 5.375   19.619 1.00 14.99 ? 100 LEU   A N   1 
ATOM   754  C  CA  . LEU   A 1 94  ? 31.319 5.167   18.277 1.00 15.95 ? 100 LEU   A CA  1 
ATOM   755  C  C   . LEU   A 1 94  ? 31.745 3.728   18.064 1.00 15.15 ? 100 LEU   A C   1 
ATOM   756  O  O   . LEU   A 1 94  ? 32.212 3.049   18.995 1.00 16.09 ? 100 LEU   A O   1 
ATOM   757  C  CB  . LEU   A 1 94  ? 32.570 6.048   18.024 1.00 17.52 ? 100 LEU   A CB  1 
ATOM   758  C  CG  . LEU   A 1 94  ? 32.349 7.531   18.052 1.00 20.62 ? 100 LEU   A CG  1 
ATOM   759  C  CD1 . LEU   A 1 94  ? 33.641 8.301   17.608 1.00 21.73 ? 100 LEU   A CD1 1 
ATOM   760  C  CD2 . LEU   A 1 94  ? 31.177 7.965   17.157 1.00 20.95 ? 100 LEU   A CD2 1 
ATOM   761  N  N   . ALA   A 1 95  ? 31.674 3.315   16.810 1.00 14.87 ? 101 ALA   A N   1 
ATOM   762  C  CA  . ALA   A 1 95  ? 32.131 1.979   16.442 1.00 15.02 ? 101 ALA   A CA  1 
ATOM   763  C  C   . ALA   A 1 95  ? 32.626 1.994   15.011 1.00 15.30 ? 101 ALA   A C   1 
ATOM   764  O  O   . ALA   A 1 95  ? 32.302 2.911   14.256 1.00 16.37 ? 101 ALA   A O   1 
ATOM   765  C  CB  . ALA   A 1 95  ? 30.953 0.990   16.562 1.00 16.37 ? 101 ALA   A CB  1 
ATOM   766  N  N   . VAL   A 1 96  ? 33.451 1.002   14.643 1.00 14.03 ? 102 VAL   A N   1 
ATOM   767  C  CA  . VAL   A 1 96  ? 33.867 0.857   13.262 1.00 15.10 ? 102 VAL   A CA  1 
ATOM   768  C  C   . VAL   A 1 96  ? 32.774 0.050   12.553 1.00 15.84 ? 102 VAL   A C   1 
ATOM   769  O  O   . VAL   A 1 96  ? 32.443 -1.073  12.938 1.00 15.57 ? 102 VAL   A O   1 
ATOM   770  C  CB  . VAL   A 1 96  ? 35.228 0.122   13.215 1.00 16.88 ? 102 VAL   A CB  1 
ATOM   771  C  CG1 . VAL   A 1 96  ? 35.644 -0.135  11.758 1.00 17.72 ? 102 VAL   A CG1 1 
ATOM   772  C  CG2 . VAL   A 1 96  ? 36.263 0.970   13.932 1.00 17.08 ? 102 VAL   A CG2 1 
ATOM   773  N  N   . GLY   A 1 97  ? 32.258 0.621   11.468 1.00 15.14 ? 103 GLY   A N   1 
ATOM   774  C  CA  . GLY   A 1 97  ? 31.188 0.009   10.706 1.00 16.09 ? 103 GLY   A CA  1 
ATOM   775  C  C   . GLY   A 1 97  ? 30.722 0.993   9.649  1.00 16.94 ? 103 GLY   A C   1 
ATOM   776  O  O   . GLY   A 1 97  ? 30.979 2.204   9.749  1.00 18.37 ? 103 GLY   A O   1 
ATOM   777  N  N   . HIS   A 1 98  ? 30.144 0.467   8.570  1.00 16.19 ? 104 HIS   A N   1 
ATOM   778  C  CA  . HIS   A 1 98  ? 29.643 1.340   7.527  1.00 15.64 ? 104 HIS   A CA  1 
ATOM   779  C  C   . HIS   A 1 98  ? 28.439 2.152   7.939  1.00 15.24 ? 104 HIS   A C   1 
ATOM   780  O  O   . HIS   A 1 98  ? 27.496 1.654   8.552  1.00 15.57 ? 104 HIS   A O   1 
ATOM   781  C  CB  . HIS   A 1 98  ? 29.299 0.533   6.271  1.00 16.40 ? 104 HIS   A CB  1 
ATOM   782  C  CG  . HIS   A 1 98  ? 28.748 1.376   5.152  1.00 16.61 ? 104 HIS   A CG  1 
ATOM   783  N  ND1 . HIS   A 1 98  ? 29.541 2.308   4.510  1.00 17.99 ? 104 HIS   A ND1 1 
ATOM   784  C  CD2 . HIS   A 1 98  ? 27.471 1.484   4.693  1.00 17.01 ? 104 HIS   A CD2 1 
ATOM   785  C  CE1 . HIS   A 1 98  ? 28.753 2.906   3.617  1.00 18.83 ? 104 HIS   A CE1 1 
ATOM   786  N  NE2 . HIS   A 1 98  ? 27.481 2.442   3.703  1.00 17.70 ? 104 HIS   A NE2 1 
ATOM   787  N  N   . SER   A 1 99  ? 28.405 3.377   7.473  1.00 14.74 ? 105 SER   A N   1 
ATOM   788  C  CA  . SER   A 1 99  ? 27.227 4.230   7.576  1.00 15.54 ? 105 SER   A CA  1 
ATOM   789  C  C   . SER   A 1 99  ? 27.379 5.343   6.552  1.00 17.41 ? 105 SER   A C   1 
ATOM   790  O  O   . SER   A 1 99  ? 28.502 5.621   6.078  1.00 17.57 ? 105 SER   A O   1 
ATOM   791  C  CB  . SER   A 1 99  ? 27.013 4.787   8.980  1.00 16.43 ? 105 SER   A CB  1 
ATOM   792  O  OG  . SER   A 1 99  ? 28.020 5.744   9.295  1.00 19.22 ? 105 SER   A OG  1 
ATOM   793  N  N   . GLU   A 1 100 ? 26.247 5.855   6.104  1.00 16.79 ? 106 GLU   A N   1 
ATOM   794  C  CA  . GLU   A 1 100 ? 26.240 6.976   5.182  1.00 18.32 ? 106 GLU   A CA  1 
ATOM   795  C  C   . GLU   A 1 100 ? 24.950 7.764   5.449  1.00 20.59 ? 106 GLU   A C   1 
ATOM   796  O  O   . GLU   A 1 100 ? 24.053 7.303   6.182  1.00 21.30 ? 106 GLU   A O   1 
ATOM   797  C  CB  . GLU   A 1 100 ? 26.398 6.520   3.703  1.00 20.79 ? 106 GLU   A CB  1 
ATOM   798  C  CG  . GLU   A 1 100 ? 25.329 5.568   3.245  1.00 23.83 ? 106 GLU   A CG  1 
ATOM   799  C  CD  . GLU   A 1 100 ? 25.576 5.053   1.831  1.00 23.20 ? 106 GLU   A CD  1 
ATOM   800  O  OE1 . GLU   A 1 100 ? 25.022 5.669   0.890  1.00 24.06 ? 106 GLU   A OE1 1 
ATOM   801  O  OE2 . GLU   A 1 100 ? 26.282 4.025   1.668  1.00 20.15 ? 106 GLU   A OE2 1 
ATOM   802  N  N   . PRO   A 1 101 ? 24.832 9.012   4.924  1.00 22.04 ? 107 PRO   A N   1 
ATOM   803  C  CA  . PRO   A 1 101 ? 23.599 9.768   5.113  1.00 22.84 ? 107 PRO   A CA  1 
ATOM   804  C  C   . PRO   A 1 101 ? 22.407 8.948   4.626  1.00 21.64 ? 107 PRO   A C   1 
ATOM   805  O  O   . PRO   A 1 101 ? 22.435 8.345   3.515  1.00 22.41 ? 107 PRO   A O   1 
ATOM   806  C  CB  . PRO   A 1 101 ? 23.837 11.039  4.277  1.00 24.49 ? 107 PRO   A CB  1 
ATOM   807  C  CG  . PRO   A 1 101 ? 25.320 11.199  4.279  1.00 24.44 ? 107 PRO   A CG  1 
ATOM   808  C  CD  . PRO   A 1 101 ? 25.794 9.766   4.112  1.00 22.11 ? 107 PRO   A CD  1 
ATOM   809  N  N   . GLY   A 1 102 ? 21.420 8.883   5.506  1.00 19.20 ? 108 GLY   A N   1 
ATOM   810  C  CA  . GLY   A 1 102 ? 20.218 8.079   5.347  1.00 18.47 ? 108 GLY   A CA  1 
ATOM   811  C  C   . GLY   A 1 102 ? 20.148 6.950   6.366  1.00 17.37 ? 108 GLY   A C   1 
ATOM   812  O  O   . GLY   A 1 102 ? 19.071 6.382   6.597  1.00 17.54 ? 108 GLY   A O   1 
ATOM   813  N  N   . ASP   A 1 103 ? 21.310 6.566   6.975  1.00 15.88 ? 109 ASP   A N   1 
ATOM   814  C  CA  . ASP   A 1 103 ? 21.317 5.456   7.923  1.00 15.13 ? 109 ASP   A CA  1 
ATOM   815  C  C   . ASP   A 1 103 ? 20.863 5.810   9.344  1.00 15.21 ? 109 ASP   A C   1 
ATOM   816  O  O   . ASP   A 1 103 ? 20.616 4.896   10.154 1.00 16.25 ? 109 ASP   A O   1 
ATOM   817  C  CB  . ASP   A 1 103 ? 22.719 4.823   8.012  1.00 15.65 ? 109 ASP   A CB  1 
ATOM   818  C  CG  . ASP   A 1 103 ? 22.986 3.909   6.829  1.00 17.29 ? 109 ASP   A CG  1 
ATOM   819  O  OD1 . ASP   A 1 103 ? 22.024 3.292   6.336  1.00 18.34 ? 109 ASP   A OD1 1 
ATOM   820  O  OD2 . ASP   A 1 103 ? 24.166 3.846   6.375  1.00 15.97 ? 109 ASP   A OD2 1 
ATOM   821  N  N   . CYS   A 1 104 ? 20.645 7.109   9.639  1.00 14.79 ? 110 CYS   A N   1 
ATOM   822  C  CA  . CYS   A 1 104 ? 20.192 7.477   11.001 1.00 14.55 ? 110 CYS   A CA  1 
ATOM   823  C  C   . CYS   A 1 104 ? 18.873 6.821   11.327 1.00 15.26 ? 110 CYS   A C   1 
ATOM   824  O  O   . CYS   A 1 104 ? 18.019 6.687   10.448 1.00 16.31 ? 110 CYS   A O   1 
ATOM   825  C  CB  . CYS   A 1 104 ? 20.085 8.984   11.186 1.00 15.38 ? 110 CYS   A CB  1 
ATOM   826  S  SG  . CYS   A 1 104 ? 21.688 9.831   11.167 1.00 18.99 ? 110 CYS   A SG  1 
ATOM   827  N  N   . GLY   A 1 105 ? 18.752 6.385   12.566 1.00 14.55 ? 111 GLY   A N   1 
ATOM   828  C  CA  . GLY   A 1 105 ? 17.522 5.731   13.006 1.00 15.84 ? 111 GLY   A CA  1 
ATOM   829  C  C   . GLY   A 1 105 ? 17.619 4.220   13.038 1.00 15.91 ? 111 GLY   A C   1 
ATOM   830  O  O   . GLY   A 1 105 ? 16.756 3.567   13.644 1.00 15.90 ? 111 GLY   A O   1 
ATOM   831  N  N   . GLY   A 1 106 ? 18.663 3.645   12.427 1.00 14.55 ? 112 GLY   A N   1 
ATOM   832  C  CA  . GLY   A 1 106 ? 18.862 2.184   12.502 1.00 13.97 ? 112 GLY   A CA  1 
ATOM   833  C  C   . GLY   A 1 106 ? 19.115 1.773   13.940 1.00 13.83 ? 112 GLY   A C   1 
ATOM   834  O  O   . GLY   A 1 106 ? 19.844 2.456   14.658 1.00 15.02 ? 112 GLY   A O   1 
ATOM   835  N  N   . ILE   A 1 107 ? 18.461 0.686   14.391 1.00 13.05 ? 113 ILE   A N   1 
ATOM   836  C  CA  . ILE   A 1 107 ? 18.603 0.264   15.780 1.00 12.75 ? 113 ILE   A CA  1 
ATOM   837  C  C   . ILE   A 1 107 ? 19.870 -0.542  16.050 1.00 13.14 ? 113 ILE   A C   1 
ATOM   838  O  O   . ILE   A 1 107 ? 20.201 -1.449  15.267 1.00 13.95 ? 113 ILE   A O   1 
ATOM   839  C  CB  . ILE   A 1 107 ? 17.313 -0.514  16.196 1.00 15.10 ? 113 ILE   A CB  1 
ATOM   840  C  CG1 . ILE   A 1 107 ? 16.159 0.500   16.392 1.00 16.76 ? 113 ILE   A CG1 1 
ATOM   841  C  CG2 . ILE   A 1 107 ? 17.504 -1.361  17.457 1.00 16.57 ? 113 ILE   A CG2 1 
ATOM   842  C  CD1 . ILE   A 1 107 ? 14.759 -0.215  16.643 1.00 19.94 ? 113 ILE   A CD1 1 
ATOM   843  N  N   . LEU   A 1 108 ? 20.484 -0.294  17.216 1.00 12.82 ? 114 LEU   A N   1 
ATOM   844  C  CA  . LEU   A 1 108 ? 21.593 -1.081  17.768 1.00 13.82 ? 114 LEU   A CA  1 
ATOM   845  C  C   . LEU   A 1 108 ? 20.986 -1.887  18.938 1.00 14.73 ? 114 LEU   A C   1 
ATOM   846  O  O   . LEU   A 1 108 ? 20.307 -1.303  19.794 1.00 15.09 ? 114 LEU   A O   1 
ATOM   847  C  CB  . LEU   A 1 108 ? 22.674 -0.118  18.323 1.00 14.86 ? 114 LEU   A CB  1 
ATOM   848  C  CG  . LEU   A 1 108 ? 23.808 -0.791  19.145 1.00 15.41 ? 114 LEU   A CG  1 
ATOM   849  C  CD1 . LEU   A 1 108 ? 24.658 -1.743  18.239 1.00 15.47 ? 114 LEU   A CD1 1 
ATOM   850  C  CD2 . LEU   A 1 108 ? 24.735 0.296   19.757 1.00 16.20 ? 114 LEU   A CD2 1 
ATOM   851  N  N   . ARG   A 1 109 ? 21.198 -3.218  18.957 1.00 14.44 ? 115 ARG   A N   1 
ATOM   852  C  CA  . ARG   A 1 109 ? 20.690 -4.077  20.009 1.00 14.98 ? 115 ARG   A CA  1 
ATOM   853  C  C   . ARG   A 1 109 ? 21.803 -4.940  20.566 1.00 15.60 ? 115 ARG   A C   1 
ATOM   854  O  O   . ARG   A 1 109 ? 22.685 -5.388  19.823 1.00 15.85 ? 115 ARG   A O   1 
ATOM   855  C  CB  . ARG   A 1 109 ? 19.661 -5.087  19.416 1.00 17.47 ? 115 ARG   A CB  1 
ATOM   856  C  CG  . ARG   A 1 109 ? 18.444 -4.494  18.788 1.00 24.09 ? 115 ARG   A CG  1 
ATOM   857  C  CD  . ARG   A 1 109 ? 17.591 -5.624  18.209 1.00 27.88 ? 115 ARG   A CD  1 
ATOM   858  N  NE  . ARG   A 1 109 ? 16.907 -6.262  19.325 1.00 31.78 ? 115 ARG   A NE  1 
ATOM   859  C  CZ  . ARG   A 1 109 ? 15.728 -5.862  19.784 1.00 29.80 ? 115 ARG   A CZ  1 
ATOM   860  N  NH1 . ARG   A 1 109 ? 15.036 -4.946  19.134 1.00 25.44 ? 115 ARG   A NH1 1 
ATOM   861  N  NH2 . ARG   A 1 109 ? 15.227 -6.392  20.882 1.00 26.65 ? 115 ARG   A NH2 1 
ATOM   862  N  N   . CYS   A 1 110 ? 21.693 -5.275  21.854 1.00 15.04 ? 116 CYS   A N   1 
ATOM   863  C  CA  . CYS   A 1 110 ? 22.559 -6.304  22.456 1.00 15.48 ? 116 CYS   A CA  1 
ATOM   864  C  C   . CYS   A 1 110 ? 21.597 -7.456  22.878 1.00 16.80 ? 116 CYS   A C   1 
ATOM   865  O  O   . CYS   A 1 110 ? 20.391 -7.383  22.628 1.00 17.39 ? 116 CYS   A O   1 
ATOM   866  C  CB  . CYS   A 1 110 ? 23.292 -5.740  23.670 1.00 16.22 ? 116 CYS   A CB  1 
ATOM   867  S  SG  . CYS   A 1 110 ? 22.153 -5.235  24.997 1.00 16.08 ? 116 CYS   A SG  1 
ATOM   868  N  N   . GLN   A 1 111 ? 22.097 -8.488  23.589 1.00 17.80 ? 117 GLN   A N   1 
ATOM   869  C  CA  . GLN   A 1 111 ? 21.239 -9.581  24.067 1.00 18.69 ? 117 GLN   A CA  1 
ATOM   870  C  C   . GLN   A 1 111 ? 20.138 -9.113  25.031 1.00 19.01 ? 117 GLN   A C   1 
ATOM   871  O  O   . GLN   A 1 111 ? 19.192 -9.877  25.294 1.00 20.20 ? 117 GLN   A O   1 
ATOM   872  C  CB  . GLN   A 1 111 ? 22.099 -10.674 24.754 1.00 20.98 ? 117 GLN   A CB  1 
ATOM   873  C  CG  . GLN   A 1 111 ? 22.726 -10.178 26.071 1.00 28.70 ? 117 GLN   A CG  1 
ATOM   874  C  CD  . GLN   A 1 111 ? 23.732 -11.157 26.620 1.00 36.44 ? 117 GLN   A CD  1 
ATOM   875  O  OE1 . GLN   A 1 111 ? 24.959 -10.949 26.551 1.00 39.93 ? 117 GLN   A OE1 1 
ATOM   876  N  NE2 . GLN   A 1 111 ? 23.217 -12.227 27.192 1.00 34.91 ? 117 GLN   A NE2 1 
ATOM   877  N  N   . HIS   A 1 112 ? 20.246 -7.895  25.600 1.00 18.31 ? 118 HIS   A N   1 
ATOM   878  C  CA  . HIS   A 1 112 ? 19.259 -7.423  26.584 1.00 18.01 ? 118 HIS   A CA  1 
ATOM   879  C  C   . HIS   A 1 112 ? 18.146 -6.567  26.008 1.00 17.38 ? 118 HIS   A C   1 
ATOM   880  O  O   . HIS   A 1 112 ? 17.161 -6.305  26.719 1.00 17.81 ? 118 HIS   A O   1 
ATOM   881  C  CB  . HIS   A 1 112 ? 19.906 -6.643  27.742 1.00 18.88 ? 118 HIS   A CB  1 
ATOM   882  C  CG  . HIS   A 1 112 ? 21.032 -7.401  28.402 1.00 20.82 ? 118 HIS   A CG  1 
ATOM   883  N  ND1 . HIS   A 1 112 ? 22.360 -7.062  28.174 1.00 21.55 ? 118 HIS   A ND1 1 
ATOM   884  C  CD2 . HIS   A 1 112 ? 20.990 -8.490  29.225 1.00 22.46 ? 118 HIS   A CD2 1 
ATOM   885  C  CE1 . HIS   A 1 112 ? 23.092 -7.943  28.852 1.00 23.16 ? 118 HIS   A CE1 1 
ATOM   886  N  NE2 . HIS   A 1 112 ? 22.314 -8.827  29.502 1.00 23.38 ? 118 HIS   A NE2 1 
ATOM   887  N  N   . GLY   A 1 113 ? 18.308 -6.124  24.759 1.00 15.41 ? 119 GLY   A N   1 
ATOM   888  C  CA  . GLY   A 1 113 ? 17.309 -5.272  24.136 1.00 15.34 ? 119 GLY   A CA  1 
ATOM   889  C  C   . GLY   A 1 113 ? 17.914 -4.137  23.328 1.00 14.66 ? 119 GLY   A C   1 
ATOM   890  O  O   . GLY   A 1 113 ? 19.082 -4.185  22.922 1.00 15.70 ? 119 GLY   A O   1 
ATOM   891  N  N   . VAL   A 1 114 ? 17.112 -3.108  23.111 1.00 14.13 ? 120 VAL   A N   1 
ATOM   892  C  CA  . VAL   A 1 114 ? 17.551 -1.964  22.336 1.00 13.93 ? 120 VAL   A CA  1 
ATOM   893  C  C   . VAL   A 1 114 ? 18.519 -1.104  23.148 1.00 14.27 ? 120 VAL   A C   1 
ATOM   894  O  O   . VAL   A 1 114 ? 18.221 -0.714  24.284 1.00 15.36 ? 120 VAL   A O   1 
ATOM   895  C  CB  . VAL   A 1 114 ? 16.337 -1.104  21.911 1.00 15.49 ? 120 VAL   A CB  1 
ATOM   896  C  CG1 . VAL   A 1 114 ? 16.821 0.166   21.211 1.00 15.94 ? 120 VAL   A CG1 1 
ATOM   897  C  CG2 . VAL   A 1 114 ? 15.442 -1.921  20.967 1.00 15.95 ? 120 VAL   A CG2 1 
ATOM   898  N  N   . VAL   A 1 115 ? 19.666 -0.773  22.531 1.00 13.99 ? 121 VAL   A N   1 
ATOM   899  C  CA  . VAL   A 1 115 ? 20.704 0.042   23.165 1.00 13.92 ? 121 VAL   A CA  1 
ATOM   900  C  C   . VAL   A 1 115 ? 20.635 1.513   22.688 1.00 14.32 ? 121 VAL   A C   1 
ATOM   901  O  O   . VAL   A 1 115 ? 20.861 2.455   23.470 1.00 14.09 ? 121 VAL   A O   1 
ATOM   902  C  CB  . VAL   A 1 115 ? 22.096 -0.537  22.779 1.00 15.92 ? 121 VAL   A CB  1 
ATOM   903  C  CG1 . VAL   A 1 115 ? 23.245 0.397   23.214 1.00 16.64 ? 121 VAL   A CG1 1 
ATOM   904  C  CG2 . VAL   A 1 115 ? 22.293 -1.935  23.364 1.00 15.72 ? 121 VAL   A CG2 1 
ATOM   905  N  N   . GLY   A 1 116 ? 20.383 1.695   21.397 1.00 13.42 ? 122 GLY   A N   1 
ATOM   906  C  CA  . GLY   A 1 116 ? 20.352 3.058   20.853 1.00 14.29 ? 122 GLY   A CA  1 
ATOM   907  C  C   . GLY   A 1 116 ? 20.088 3.103   19.366 1.00 14.05 ? 122 GLY   A C   1 
ATOM   908  O  O   . GLY   A 1 116 ? 19.689 2.092   18.795 1.00 14.05 ? 122 GLY   A O   1 
ATOM   909  N  N   . ILE   A 1 117 ? 20.267 4.294   18.747 1.00 13.13 ? 123 ILE   A N   1 
ATOM   910  C  CA  . ILE   A 1 117 ? 19.983 4.393   17.301 1.00 13.40 ? 123 ILE   A CA  1 
ATOM   911  C  C   . ILE   A 1 117 ? 21.126 5.090   16.592 1.00 13.54 ? 123 ILE   A C   1 
ATOM   912  O  O   . ILE   A 1 117 ? 21.749 5.961   17.176 1.00 13.49 ? 123 ILE   A O   1 
ATOM   913  C  CB  . ILE   A 1 117 ? 18.666 5.180   17.037 1.00 15.41 ? 123 ILE   A CB  1 
ATOM   914  C  CG1 . ILE   A 1 117 ? 18.603 6.490   17.815 1.00 16.83 ? 123 ILE   A CG1 1 
ATOM   915  C  CG2 . ILE   A 1 117 ? 17.450 4.291   17.296 1.00 17.44 ? 123 ILE   A CG2 1 
ATOM   916  C  CD1 . ILE   A 1 117 ? 17.367 7.372   17.274 1.00 18.56 ? 123 ILE   A CD1 1 
ATOM   917  N  N   . VAL   A 1 118 ? 21.358 4.761   15.295 1.00 12.46 ? 124 VAL   A N   1 
ATOM   918  C  CA  . VAL   A 1 118 ? 22.384 5.471   14.502 1.00 11.60 ? 124 VAL   A CA  1 
ATOM   919  C  C   . VAL   A 1 118 ? 22.112 6.982   14.508 1.00 12.12 ? 124 VAL   A C   1 
ATOM   920  O  O   . VAL   A 1 118 ? 20.981 7.382   14.283 1.00 13.07 ? 124 VAL   A O   1 
ATOM   921  C  CB  . VAL   A 1 118 ? 22.450 4.959   13.049 1.00 12.80 ? 124 VAL   A CB  1 
ATOM   922  C  CG1 . VAL   A 1 118 ? 23.490 5.763   12.262 1.00 14.45 ? 124 VAL   A CG1 1 
ATOM   923  C  CG2 . VAL   A 1 118 ? 22.814 3.461   13.016 1.00 13.39 ? 124 VAL   A CG2 1 
ATOM   924  N  N   . SER   A 1 119 ? 23.144 7.792   14.750 1.00 12.37 ? 125 SER   A N   1 
ATOM   925  C  CA  . SER   A 1 119 ? 22.978 9.249   14.802 1.00 12.96 ? 125 SER   A CA  1 
ATOM   926  C  C   . SER   A 1 119 ? 24.083 9.969   14.043 1.00 14.99 ? 125 SER   A C   1 
ATOM   927  O  O   . SER   A 1 119 ? 23.870 11.088  13.602 1.00 16.22 ? 125 SER   A O   1 
ATOM   928  C  CB  . SER   A 1 119 ? 22.979 9.707   16.269 1.00 14.63 ? 125 SER   A CB  1 
ATOM   929  O  OG  . SER   A 1 119 ? 22.894 11.124  16.388 1.00 15.28 ? 125 SER   A OG  1 
ATOM   930  N  N   . THR   A 1 120 ? 25.270 9.345   13.866 1.00 14.53 ? 126 THR   A N   1 
ATOM   931  C  CA  . THR   A 1 120 ? 26.382 10.022  13.150 1.00 15.82 ? 126 THR   A CA  1 
ATOM   932  C  C   . THR   A 1 120 ? 27.197 8.938   12.368 1.00 16.28 ? 126 THR   A C   1 
ATOM   933  O  O   . THR   A 1 120 ? 26.978 7.741   12.558 1.00 15.72 ? 126 THR   A O   1 
ATOM   934  C  CB  . THR   A 1 120 ? 27.378 10.751  14.168 1.00 19.72 ? 126 THR   A CB  1 
ATOM   935  O  OG1 . THR   A 1 120 ? 28.170 9.801   14.873 1.00 21.03 ? 126 THR   A OG1 1 
ATOM   936  C  CG2 . THR   A 1 120 ? 26.725 11.687  15.150 1.00 21.72 ? 126 THR   A CG2 1 
ATOM   937  N  N   . GLY   A 1 121 ? 28.143 9.364   11.550 1.00 16.70 ? 127 GLY   A N   1 
ATOM   938  C  CA  . GLY   A 1 121 ? 29.029 8.423   10.884 1.00 18.53 ? 127 GLY   A CA  1 
ATOM   939  C  C   . GLY   A 1 121 ? 30.035 9.132   10.029 1.00 19.97 ? 127 GLY   A C   1 
ATOM   940  O  O   . GLY   A 1 121 ? 29.999 10.362  9.885  1.00 20.63 ? 127 GLY   A O   1 
ATOM   941  N  N   . GLY   A 1 122 ? 30.903 8.338   9.441  1.00 19.99 ? 128 GLY   A N   1 
ATOM   942  C  CA  . GLY   A 1 122 ? 31.870 8.871   8.500  1.00 22.37 ? 128 GLY   A CA  1 
ATOM   943  C  C   . GLY   A 1 122 ? 33.109 8.042   8.438  1.00 22.93 ? 128 GLY   A C   1 
ATOM   944  O  O   . GLY   A 1 122 ? 33.563 7.576   9.475  1.00 23.57 ? 128 GLY   A O   1 
ATOM   945  N  N   . ASN   A 1 123 ? 33.679 7.906   7.247  1.00 22.60 ? 129 ASN   A N   1 
ATOM   946  C  CA  . ASN   A 1 123 ? 34.948 7.213   6.991  1.00 21.74 ? 129 ASN   A CA  1 
ATOM   947  C  C   . ASN   A 1 123 ? 35.116 5.872   7.699  1.00 20.91 ? 129 ASN   A C   1 
ATOM   948  O  O   . ASN   A 1 123 ? 36.177 5.593   8.270  1.00 21.22 ? 129 ASN   A O   1 
ATOM   949  C  CB  . ASN   A 1 123 ? 36.102 8.161   7.342  1.00 25.67 ? 129 ASN   A CB  1 
ATOM   950  C  CG  . ASN   A 1 123 ? 36.019 9.429   6.543  1.00 32.92 ? 129 ASN   A CG  1 
ATOM   951  O  OD1 . ASN   A 1 123 ? 36.022 9.384   5.311  1.00 36.00 ? 129 ASN   A OD1 1 
ATOM   952  N  ND2 . ASN   A 1 123 ? 35.901 10.577  7.218  1.00 34.50 ? 129 ASN   A ND2 1 
ATOM   953  N  N   . GLY   A 1 124 ? 34.094 5.024   7.611  1.00 18.40 ? 130 GLY   A N   1 
ATOM   954  C  CA  . GLY   A 1 124 ? 34.150 3.702   8.202  1.00 17.56 ? 130 GLY   A CA  1 
ATOM   955  C  C   . GLY   A 1 124 ? 33.811 3.678   9.674  1.00 17.64 ? 130 GLY   A C   1 
ATOM   956  O  O   . GLY   A 1 124 ? 33.970 2.633   10.320 1.00 18.94 ? 130 GLY   A O   1 
ATOM   957  N  N   . LEU   A 1 125 ? 33.266 4.789   10.192 1.00 16.27 ? 131 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 125 ? 32.763 4.833   11.547 1.00 16.08 ? 131 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 125 ? 31.221 4.954   11.529 1.00 15.63 ? 131 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 125 ? 30.619 5.384   10.549 1.00 16.02 ? 131 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 125 ? 33.302 6.057   12.311 1.00 16.53 ? 131 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 125 ? 34.813 6.015   12.558 1.00 20.06 ? 131 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 125 ? 35.325 7.416   12.932 1.00 21.73 ? 131 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 125 ? 35.146 4.972   13.646 1.00 19.66 ? 131 LEU   A CD2 1 
ATOM   965  N  N   . VAL   A 1 126 ? 30.618 4.549   12.627 1.00 14.00 ? 132 VAL   A N   1 
ATOM   966  C  CA  . VAL   A 1 126 ? 29.184 4.725   12.838 1.00 13.84 ? 132 VAL   A CA  1 
ATOM   967  C  C   . VAL   A 1 126 ? 28.992 5.134   14.296 1.00 14.65 ? 132 VAL   A C   1 
ATOM   968  O  O   . VAL   A 1 126 ? 29.623 4.558   15.178 1.00 15.08 ? 132 VAL   A O   1 
ATOM   969  C  CB  . VAL   A 1 126 ? 28.325 3.507   12.445 1.00 14.63 ? 132 VAL   A CB  1 
ATOM   970  C  CG1 . VAL   A 1 126 ? 28.820 2.230   13.137 1.00 15.97 ? 132 VAL   A CG1 1 
ATOM   971  C  CG2 . VAL   A 1 126 ? 26.840 3.759   12.737 1.00 14.45 ? 132 VAL   A CG2 1 
ATOM   972  N  N   . GLY   A 1 127 ? 28.143 6.138   14.556 1.00 14.31 ? 133 GLY   A N   1 
ATOM   973  C  CA  . GLY   A 1 127 ? 27.921 6.598   15.913 1.00 14.33 ? 133 GLY   A CA  1 
ATOM   974  C  C   . GLY   A 1 127 ? 26.469 6.403   16.315 1.00 14.36 ? 133 GLY   A C   1 
ATOM   975  O  O   . GLY   A 1 127 ? 25.569 6.569   15.480 1.00 14.83 ? 133 GLY   A O   1 
ATOM   976  N  N   . PHE   A 1 128 ? 26.239 6.010   17.584 1.00 13.21 ? 134 PHE   A N   1 
ATOM   977  C  CA  . PHE   A 1 128 ? 24.887 5.678   18.059 1.00 13.55 ? 134 PHE   A CA  1 
ATOM   978  C  C   . PHE   A 1 128 ? 24.529 6.547   19.264 1.00 14.28 ? 134 PHE   A C   1 
ATOM   979  O  O   . PHE   A 1 128 ? 25.301 6.646   20.217 1.00 14.55 ? 134 PHE   A O   1 
ATOM   980  C  CB  . PHE   A 1 128 ? 24.826 4.213   18.522 1.00 12.72 ? 134 PHE   A CB  1 
ATOM   981  C  CG  . PHE   A 1 128 ? 25.332 3.212   17.510 1.00 13.40 ? 134 PHE   A CG  1 
ATOM   982  C  CD1 . PHE   A 1 128 ? 24.496 2.727   16.515 1.00 12.96 ? 134 PHE   A CD1 1 
ATOM   983  C  CD2 . PHE   A 1 128 ? 26.641 2.744   17.571 1.00 14.70 ? 134 PHE   A CD2 1 
ATOM   984  C  CE1 . PHE   A 1 128 ? 24.959 1.785   15.599 1.00 13.37 ? 134 PHE   A CE1 1 
ATOM   985  C  CE2 . PHE   A 1 128 ? 27.104 1.796   16.670 1.00 14.86 ? 134 PHE   A CE2 1 
ATOM   986  C  CZ  . PHE   A 1 128 ? 26.264 1.341   15.655 1.00 14.29 ? 134 PHE   A CZ  1 
ATOM   987  N  N   . ALA   A 1 129 ? 23.306 7.082   19.259 1.00 13.09 ? 135 ALA   A N   1 
ATOM   988  C  CA  . ALA   A 1 129 ? 22.788 7.831   20.385 1.00 13.43 ? 135 ALA   A CA  1 
ATOM   989  C  C   . ALA   A 1 129 ? 22.276 6.780   21.403 1.00 12.99 ? 135 ALA   A C   1 
ATOM   990  O  O   . ALA   A 1 129 ? 21.360 6.005   21.076 1.00 13.63 ? 135 ALA   A O   1 
ATOM   991  C  CB  . ALA   A 1 129 ? 21.651 8.735   19.924 1.00 14.14 ? 135 ALA   A CB  1 
ATOM   992  N  N   . ASP   A 1 130 ? 22.844 6.764   22.619 1.00 12.25 ? 136 ASP   A N   1 
ATOM   993  C  CA  . ASP   A 1 130 ? 22.408 5.797   23.656 1.00 13.99 ? 136 ASP   A CA  1 
ATOM   994  C  C   . ASP   A 1 130 ? 21.029 6.155   24.173 1.00 15.08 ? 136 ASP   A C   1 
ATOM   995  O  O   . ASP   A 1 130 ? 20.726 7.348   24.352 1.00 15.22 ? 136 ASP   A O   1 
ATOM   996  C  CB  . ASP   A 1 130 ? 23.378 5.867   24.850 1.00 16.36 ? 136 ASP   A CB  1 
ATOM   997  C  CG  . ASP   A 1 130 ? 23.137 4.811   25.915 1.00 22.36 ? 136 ASP   A CG  1 
ATOM   998  O  OD1 . ASP   A 1 130 ? 22.969 3.650   25.559 1.00 22.41 ? 136 ASP   A OD1 1 
ATOM   999  O  OD2 . ASP   A 1 130 ? 23.083 5.174   27.124 1.00 25.70 ? 136 ASP   A OD2 1 
ATOM   1000 N  N   . VAL   A 1 131 ? 20.214 5.116   24.530 1.00 13.49 ? 137 VAL   A N   1 
ATOM   1001 C  CA  . VAL   A 1 131 ? 18.916 5.365   25.176 1.00 13.87 ? 137 VAL   A CA  1 
ATOM   1002 C  C   . VAL   A 1 131 ? 18.797 4.590   26.511 1.00 15.00 ? 137 VAL   A C   1 
ATOM   1003 O  O   . VAL   A 1 131 ? 17.746 4.644   27.155 1.00 15.90 ? 137 VAL   A O   1 
ATOM   1004 C  CB  . VAL   A 1 131 ? 17.702 5.035   24.283 1.00 15.48 ? 137 VAL   A CB  1 
ATOM   1005 C  CG1 . VAL   A 1 131 ? 17.676 5.928   23.039 1.00 15.79 ? 137 VAL   A CG1 1 
ATOM   1006 C  CG2 . VAL   A 1 131 ? 17.673 3.548   23.910 1.00 14.66 ? 137 VAL   A CG2 1 
ATOM   1007 N  N   . ARG   A 1 132 ? 19.843 3.846   26.912 1.00 14.52 ? 138 ARG   A N   1 
ATOM   1008 C  CA  . ARG   A 1 132 ? 19.751 2.981   28.090 1.00 14.85 ? 138 ARG   A CA  1 
ATOM   1009 C  C   . ARG   A 1 132 ? 19.570 3.708   29.395 1.00 16.82 ? 138 ARG   A C   1 
ATOM   1010 O  O   . ARG   A 1 132 ? 19.067 3.118   30.358 1.00 17.80 ? 138 ARG   A O   1 
ATOM   1011 C  CB  . ARG   A 1 132 ? 20.965 2.027   28.183 1.00 14.91 ? 138 ARG   A CB  1 
ATOM   1012 C  CG  . ARG   A 1 132 ? 21.064 1.080   26.984 1.00 14.44 ? 138 ARG   A CG  1 
ATOM   1013 C  CD  . ARG   A 1 132 ? 22.333 0.279   27.107 1.00 15.42 ? 138 ARG   A CD  1 
ATOM   1014 N  NE  . ARG   A 1 132 ? 23.478 1.118   26.761 1.00 16.78 ? 138 ARG   A NE  1 
ATOM   1015 C  CZ  . ARG   A 1 132 ? 24.725 0.674   26.643 1.00 18.58 ? 138 ARG   A CZ  1 
ATOM   1016 N  NH1 . ARG   A 1 132 ? 25.014 -0.609  26.905 1.00 17.28 ? 138 ARG   A NH1 1 
ATOM   1017 N  NH2 . ARG   A 1 132 ? 25.688 1.496   26.247 1.00 17.83 ? 138 ARG   A NH2 1 
ATOM   1018 N  N   . ASP   A 1 133 ? 19.991 4.991   29.440 1.00 16.53 ? 139 ASP   A N   1 
ATOM   1019 C  CA  . ASP   A 1 133 ? 19.842 5.761   30.671 1.00 17.32 ? 139 ASP   A CA  1 
ATOM   1020 C  C   . ASP   A 1 133 ? 18.437 6.378   30.830 1.00 17.56 ? 139 ASP   A C   1 
ATOM   1021 O  O   . ASP   A 1 133 ? 18.153 6.967   31.868 1.00 18.30 ? 139 ASP   A O   1 
ATOM   1022 C  CB  . ASP   A 1 133 ? 20.908 6.870   30.739 1.00 18.85 ? 139 ASP   A CB  1 
ATOM   1023 C  CG  . ASP   A 1 133 ? 20.766 7.907   29.644 1.00 24.41 ? 139 ASP   A CG  1 
ATOM   1024 O  OD1 . ASP   A 1 133 ? 20.615 7.514   28.477 1.00 24.45 ? 139 ASP   A OD1 1 
ATOM   1025 O  OD2 . ASP   A 1 133 ? 20.806 9.134   29.962 1.00 27.29 ? 139 ASP   A OD2 1 
ATOM   1026 N  N   . LEU   A 1 134 ? 17.585 6.305   29.794 1.00 17.27 ? 140 LEU   A N   1 
ATOM   1027 C  CA  . LEU   A 1 134 ? 16.245 6.925   29.873 1.00 15.84 ? 140 LEU   A CA  1 
ATOM   1028 C  C   . LEU   A 1 134 ? 15.294 5.936   30.545 1.00 16.51 ? 140 LEU   A C   1 
ATOM   1029 O  O   . LEU   A 1 134 ? 14.522 5.226   29.886 1.00 16.94 ? 140 LEU   A O   1 
ATOM   1030 C  CB  . LEU   A 1 134 ? 15.790 7.261   28.441 1.00 15.31 ? 140 LEU   A CB  1 
ATOM   1031 C  CG  . LEU   A 1 134 ? 16.763 8.194   27.657 1.00 17.82 ? 140 LEU   A CG  1 
ATOM   1032 C  CD1 . LEU   A 1 134 ? 16.285 8.403   26.221 1.00 18.07 ? 140 LEU   A CD1 1 
ATOM   1033 C  CD2 . LEU   A 1 134 ? 16.946 9.526   28.377 1.00 18.82 ? 140 LEU   A CD2 1 
ATOM   1034 N  N   . LEU   A 1 135 ? 15.400 5.840   31.882 1.00 16.45 ? 141 LEU   A N   1 
ATOM   1035 C  CA  . LEU   A 1 135 ? 14.637 4.811   32.610 1.00 17.24 ? 141 LEU   A CA  1 
ATOM   1036 C  C   . LEU   A 1 135 ? 13.139 4.972   32.521 1.00 18.53 ? 141 LEU   A C   1 
ATOM   1037 O  O   . LEU   A 1 135 ? 12.398 3.978   32.559 1.00 19.33 ? 141 LEU   A O   1 
ATOM   1038 C  CB  . LEU   A 1 135 ? 15.090 4.738   34.067 1.00 17.19 ? 141 LEU   A CB  1 
ATOM   1039 C  CG  . LEU   A 1 135 ? 16.608 4.737   34.282 1.00 19.40 ? 141 LEU   A CG  1 
ATOM   1040 C  CD1 . LEU   A 1 135 ? 16.909 4.563   35.789 1.00 20.14 ? 141 LEU   A CD1 1 
ATOM   1041 C  CD2 . LEU   A 1 135 ? 17.316 3.627   33.444 1.00 19.65 ? 141 LEU   A CD2 1 
ATOM   1042 N  N   . TRP   A 1 136 ? 12.692 6.231   32.352 1.00 18.64 ? 142 TRP   A N   1 
ATOM   1043 C  CA  . TRP   A 1 136 ? 11.276 6.538   32.275 1.00 19.48 ? 142 TRP   A CA  1 
ATOM   1044 C  C   . TRP   A 1 136 ? 10.586 5.962   31.021 1.00 20.85 ? 142 TRP   A C   1 
ATOM   1045 O  O   . TRP   A 1 136 ? 9.350  5.931   30.976 1.00 22.95 ? 142 TRP   A O   1 
ATOM   1046 C  CB  . TRP   A 1 136 ? 11.075 8.060   32.366 1.00 19.31 ? 142 TRP   A CB  1 
ATOM   1047 C  CG  . TRP   A 1 136 ? 11.903 8.865   31.398 1.00 18.69 ? 142 TRP   A CG  1 
ATOM   1048 C  CD1 . TRP   A 1 136 ? 13.140 9.410   31.604 1.00 19.16 ? 142 TRP   A CD1 1 
ATOM   1049 C  CD2 . TRP   A 1 136 ? 11.519 9.229   30.074 1.00 19.35 ? 142 TRP   A CD2 1 
ATOM   1050 N  NE1 . TRP   A 1 136 ? 13.532 10.127  30.496 1.00 19.46 ? 142 TRP   A NE1 1 
ATOM   1051 C  CE2 . TRP   A 1 136 ? 12.569 10.001  29.523 1.00 19.65 ? 142 TRP   A CE2 1 
ATOM   1052 C  CE3 . TRP   A 1 136 ? 10.371 9.001   29.308 1.00 20.34 ? 142 TRP   A CE3 1 
ATOM   1053 C  CZ2 . TRP   A 1 136 ? 12.506 10.543  28.236 1.00 20.04 ? 142 TRP   A CZ2 1 
ATOM   1054 C  CZ3 . TRP   A 1 136 ? 10.305 9.551   28.035 1.00 20.03 ? 142 TRP   A CZ3 1 
ATOM   1055 C  CH2 . TRP   A 1 136 ? 11.355 10.337  27.528 1.00 20.30 ? 142 TRP   A CH2 1 
ATOM   1056 N  N   . LEU   A 1 137 ? 11.356 5.494   30.010 1.00 20.23 ? 143 LEU   A N   1 
ATOM   1057 C  CA  . LEU   A 1 137 ? 10.718 4.933   28.801 1.00 21.36 ? 143 LEU   A CA  1 
ATOM   1058 C  C   . LEU   A 1 137 ? 9.891  3.676   29.130 1.00 25.69 ? 143 LEU   A C   1 
ATOM   1059 O  O   . LEU   A 1 137 ? 8.958  3.355   28.387 1.00 25.63 ? 143 LEU   A O   1 
ATOM   1060 C  CB  . LEU   A 1 137 ? 11.772 4.531   27.765 1.00 19.70 ? 143 LEU   A CB  1 
ATOM   1061 C  CG  . LEU   A 1 137 ? 12.444 5.682   27.013 1.00 18.74 ? 143 LEU   A CG  1 
ATOM   1062 C  CD1 . LEU   A 1 137 ? 13.548 5.147   26.088 1.00 19.60 ? 143 LEU   A CD1 1 
ATOM   1063 C  CD2 . LEU   A 1 137 ? 11.420 6.460   26.136 1.00 18.79 ? 143 LEU   A CD2 1 
ATOM   1064 N  N   . ASP   A 1 138 ? 10.299 2.946   30.208 1.00 28.95 ? 144 ASP   A N   1 
ATOM   1065 C  CA  . ASP   A 1 138 ? 9.752  1.690   30.722 1.00 34.12 ? 144 ASP   A CA  1 
ATOM   1066 C  C   . ASP   A 1 138 ? 8.530  1.834   31.576 1.00 38.77 ? 144 ASP   A C   1 
ATOM   1067 O  O   . ASP   A 1 138 ? 7.999  0.802   31.980 1.00 40.16 ? 144 ASP   A O   1 
ATOM   1068 C  CB  . ASP   A 1 138 ? 10.790 1.029   31.652 1.00 37.35 ? 144 ASP   A CB  1 
ATOM   1069 C  CG  . ASP   A 1 138 ? 11.918 0.340   30.974 1.00 44.86 ? 144 ASP   A CG  1 
ATOM   1070 O  OD1 . ASP   A 1 138 ? 11.763 -0.017  29.797 1.00 45.82 ? 144 ASP   A OD1 1 
ATOM   1071 O  OD2 . ASP   A 1 138 ? 12.966 0.136   31.632 1.00 49.75 ? 144 ASP   A OD2 1 
ATOM   1072 N  N   . GLU   A 1 139 ? 8.147  3.052   31.971 1.00 41.62 ? 145 GLU   A N   1 
ATOM   1073 C  CA  . GLU   A 1 139 ? 6.974  3.231   32.824 1.00 45.15 ? 145 GLU   A CA  1 
ATOM   1074 C  C   . GLU   A 1 139 ? 5.936  4.146   32.182 1.00 46.88 ? 145 GLU   A C   1 
ATOM   1075 O  O   . GLU   A 1 139 ? 6.293  5.062   31.439 1.00 48.05 ? 145 GLU   A O   1 
ATOM   1076 C  CB  . GLU   A 1 139 ? 7.382  3.748   34.216 1.00 49.24 ? 145 GLU   A CB  1 
ATOM   1077 C  CG  . GLU   A 1 139 ? 8.245  4.993   34.169 1.00 57.44 ? 145 GLU   A CG  1 
ATOM   1078 C  CD  . GLU   A 1 139 ? 9.309  5.030   35.247 1.00 67.54 ? 145 GLU   A CD  1 
ATOM   1079 O  OE1 . GLU   A 1 139 ? 9.364  6.036   35.992 1.00 69.98 ? 145 GLU   A OE1 1 
ATOM   1080 O  OE2 . GLU   A 1 139 ? 10.089 4.053   35.344 1.00 70.31 ? 145 GLU   A OE2 1 
ATOM   1081 N  N   . SER   B 1 1   ? 19.553 -24.664 24.001 1.00 27.62 ? 7   SER   C N   1 
ATOM   1082 C  CA  . SER   B 1 1   ? 20.669 -24.515 23.056 1.00 27.95 ? 7   SER   C CA  1 
ATOM   1083 C  C   . SER   B 1 1   ? 20.687 -25.681 22.043 1.00 26.47 ? 7   SER   C C   1 
ATOM   1084 O  O   . SER   B 1 1   ? 20.052 -26.714 22.276 1.00 26.54 ? 7   SER   C O   1 
ATOM   1085 C  CB  . SER   B 1 1   ? 21.995 -24.470 23.819 1.00 31.39 ? 7   SER   C CB  1 
ATOM   1086 O  OG  . SER   B 1 1   ? 22.227 -25.721 24.457 1.00 35.78 ? 7   SER   C OG  1 
ATOM   1087 N  N   . GLY   B 1 2   ? 21.427 -25.517 20.947 1.00 23.95 ? 8   GLY   C N   1 
ATOM   1088 C  CA  . GLY   B 1 2   ? 21.567 -26.559 19.934 1.00 22.61 ? 8   GLY   C CA  1 
ATOM   1089 C  C   . GLY   B 1 2   ? 21.875 -26.009 18.554 1.00 21.20 ? 8   GLY   C C   1 
ATOM   1090 O  O   . GLY   B 1 2   ? 21.561 -24.850 18.266 1.00 22.21 ? 8   GLY   C O   1 
ATOM   1091 N  N   . ALA   B 1 3   ? 22.529 -26.797 17.697 1.00 19.44 ? 9   ALA   C N   1 
ATOM   1092 C  CA  . ALA   B 1 3   ? 22.868 -26.341 16.336 1.00 19.08 ? 9   ALA   C CA  1 
ATOM   1093 C  C   . ALA   B 1 3   ? 22.828 -27.507 15.345 1.00 18.65 ? 9   ALA   C C   1 
ATOM   1094 O  O   . ALA   B 1 3   ? 22.895 -28.682 15.741 1.00 19.77 ? 9   ALA   C O   1 
ATOM   1095 C  CB  . ALA   B 1 3   ? 24.287 -25.733 16.327 1.00 20.12 ? 9   ALA   C CB  1 
ATOM   1096 N  N   . ILE   B 1 4   ? 22.732 -27.180 14.047 1.00 17.96 ? 10  ILE   C N   1 
ATOM   1097 C  CA  . ILE   B 1 4   ? 22.827 -28.153 12.967 1.00 17.06 ? 10  ILE   C CA  1 
ATOM   1098 C  C   . ILE   B 1 4   ? 24.189 -27.940 12.307 1.00 17.99 ? 10  ILE   C C   1 
ATOM   1099 O  O   . ILE   B 1 4   ? 24.554 -26.810 11.996 1.00 17.55 ? 10  ILE   C O   1 
ATOM   1100 C  CB  . ILE   B 1 4   ? 21.713 -27.893 11.934 1.00 17.19 ? 10  ILE   C CB  1 
ATOM   1101 C  CG1 . ILE   B 1 4   ? 20.325 -27.983 12.586 1.00 18.22 ? 10  ILE   C CG1 1 
ATOM   1102 C  CG2 . ILE   B 1 4   ? 21.840 -28.887 10.762 1.00 16.90 ? 10  ILE   C CG2 1 
ATOM   1103 C  CD1 . ILE   B 1 4   ? 19.225 -27.277 11.654 1.00 19.94 ? 10  ILE   C CD1 1 
ATOM   1104 N  N   . TYR   B 1 5   ? 24.944 -29.028 12.057 1.00 19.31 ? 11  TYR   C N   1 
ATOM   1105 C  CA  . TYR   B 1 5   ? 26.256 -28.939 11.423 1.00 19.73 ? 11  TYR   C CA  1 
ATOM   1106 C  C   . TYR   B 1 5   ? 26.164 -29.659 10.094 1.00 20.44 ? 11  TYR   C C   1 
ATOM   1107 O  O   . TYR   B 1 5   ? 26.008 -30.889 10.083 1.00 20.76 ? 11  TYR   C O   1 
ATOM   1108 C  CB  . TYR   B 1 5   ? 27.318 -29.608 12.331 1.00 19.76 ? 11  TYR   C CB  1 
ATOM   1109 C  CG  . TYR   B 1 5   ? 27.530 -28.821 13.607 1.00 19.63 ? 11  TYR   C CG  1 
ATOM   1110 C  CD1 . TYR   B 1 5   ? 28.357 -27.702 13.630 1.00 20.47 ? 11  TYR   C CD1 1 
ATOM   1111 C  CD2 . TYR   B 1 5   ? 26.825 -29.125 14.760 1.00 21.24 ? 11  TYR   C CD2 1 
ATOM   1112 C  CE1 . TYR   B 1 5   ? 28.504 -26.934 14.784 1.00 22.24 ? 11  TYR   C CE1 1 
ATOM   1113 C  CE2 . TYR   B 1 5   ? 26.961 -28.360 15.915 1.00 22.76 ? 11  TYR   C CE2 1 
ATOM   1114 C  CZ  . TYR   B 1 5   ? 27.836 -27.292 15.935 1.00 23.76 ? 11  TYR   C CZ  1 
ATOM   1115 O  OH  . TYR   B 1 5   ? 27.933 -26.515 17.062 1.00 26.57 ? 11  TYR   C OH  1 
ATOM   1116 N  N   . VAL   B 1 6   ? 26.259 -28.937 8.972  1.00 20.27 ? 12  VAL   C N   1 
ATOM   1117 C  CA  . VAL   B 1 6   ? 26.132 -29.567 7.655  1.00 21.50 ? 12  VAL   C CA  1 
ATOM   1118 C  C   . VAL   B 1 6   ? 27.198 -28.966 6.755  1.00 22.86 ? 12  VAL   C C   1 
ATOM   1119 O  O   . VAL   B 1 6   ? 27.323 -27.751 6.679  1.00 22.13 ? 12  VAL   C O   1 
ATOM   1120 C  CB  . VAL   B 1 6   ? 24.694 -29.393 7.067  1.00 22.85 ? 12  VAL   C CB  1 
ATOM   1121 C  CG1 . VAL   B 1 6   ? 24.238 -27.938 7.141  1.00 22.51 ? 12  VAL   C CG1 1 
ATOM   1122 C  CG2 . VAL   B 1 6   ? 24.616 -29.931 5.647  1.00 25.02 ? 12  VAL   C CG2 1 
ATOM   1123 N  N   . GLY   B 1 7   ? 28.064 -29.800 6.163  1.00 24.05 ? 13  GLY   C N   1 
ATOM   1124 C  CA  . GLY   B 1 7   ? 29.145 -29.295 5.311  1.00 24.72 ? 13  GLY   C CA  1 
ATOM   1125 C  C   . GLY   B 1 7   ? 30.046 -28.372 6.117  1.00 26.22 ? 13  GLY   C C   1 
ATOM   1126 O  O   . GLY   B 1 7   ? 30.344 -28.682 7.277  1.00 27.42 ? 13  GLY   C O   1 
ATOM   1127 N  N   . ASN   B 1 8   ? 30.358 -27.176 5.596  1.00 25.61 ? 14  ASN   C N   1 
ATOM   1128 C  CA  . ASN   B 1 8   ? 31.140 -26.214 6.378  1.00 25.84 ? 14  ASN   C CA  1 
ATOM   1129 C  C   . ASN   B 1 8   ? 30.242 -25.113 6.952  1.00 23.46 ? 14  ASN   C C   1 
ATOM   1130 O  O   . ASN   B 1 8   ? 30.674 -23.961 7.066  1.00 23.31 ? 14  ASN   C O   1 
ATOM   1131 C  CB  . ASN   B 1 8   ? 32.277 -25.617 5.567  1.00 28.89 ? 14  ASN   C CB  1 
ATOM   1132 C  CG  . ASN   B 1 8   ? 33.355 -26.626 5.279  1.00 36.64 ? 14  ASN   C CG  1 
ATOM   1133 O  OD1 . ASN   B 1 8   ? 34.058 -27.108 6.189  1.00 38.82 ? 14  ASN   C OD1 1 
ATOM   1134 N  ND2 . ASN   B 1 8   ? 33.481 -26.985 4.017  1.00 38.43 ? 14  ASN   C ND2 1 
ATOM   1135 N  N   . TYR   B 1 9   ? 29.014 -25.481 7.354  1.00 21.36 ? 15  TYR   C N   1 
ATOM   1136 C  CA  . TYR   B 1 9   ? 28.070 -24.532 7.935  1.00 20.41 ? 15  TYR   C CA  1 
ATOM   1137 C  C   . TYR   B 1 9   ? 27.593 -24.991 9.309  1.00 19.61 ? 15  TYR   C C   1 
ATOM   1138 O  O   . TYR   B 1 9   ? 27.453 -26.203 9.568  1.00 20.31 ? 15  TYR   C O   1 
ATOM   1139 C  CB  . TYR   B 1 9   ? 26.806 -24.416 7.041  1.00 20.42 ? 15  TYR   C CB  1 
ATOM   1140 C  CG  . TYR   B 1 9   ? 27.083 -23.856 5.665  1.00 21.44 ? 15  TYR   C CG  1 
ATOM   1141 C  CD1 . TYR   B 1 9   ? 27.751 -22.650 5.507  1.00 23.20 ? 15  TYR   C CD1 1 
ATOM   1142 C  CD2 . TYR   B 1 9   ? 26.713 -24.553 4.522  1.00 22.83 ? 15  TYR   C CD2 1 
ATOM   1143 C  CE1 . TYR   B 1 9   ? 28.023 -22.138 4.248  1.00 24.66 ? 15  TYR   C CE1 1 
ATOM   1144 C  CE2 . TYR   B 1 9   ? 26.958 -24.041 3.254  1.00 24.07 ? 15  TYR   C CE2 1 
ATOM   1145 C  CZ  . TYR   B 1 9   ? 27.614 -22.831 3.122  1.00 26.21 ? 15  TYR   C CZ  1 
ATOM   1146 O  OH  . TYR   B 1 9   ? 27.844 -22.293 1.874  1.00 29.32 ? 15  TYR   C OH  1 
ATOM   1147 N  N   . ARG   B 1 10  ? 27.309 -23.997 10.182 1.00 17.10 ? 16  ARG   C N   1 
ATOM   1148 C  CA  . ARG   B 1 10  ? 26.684 -24.221 11.486 1.00 16.90 ? 16  ARG   C CA  1 
ATOM   1149 C  C   . ARG   B 1 10  ? 25.384 -23.387 11.502 1.00 17.23 ? 16  ARG   C C   1 
ATOM   1150 O  O   . ARG   B 1 10  ? 25.447 -22.188 11.227 1.00 16.87 ? 16  ARG   C O   1 
ATOM   1151 C  CB  . ARG   B 1 10  ? 27.628 -23.807 12.628 1.00 17.09 ? 16  ARG   C CB  1 
ATOM   1152 C  CG  . ARG   B 1 10  ? 26.991 -23.542 13.993 1.00 19.72 ? 16  ARG   C CG  1 
ATOM   1153 C  CD  . ARG   B 1 10  ? 28.063 -23.244 15.079 1.00 20.53 ? 16  ARG   C CD  1 
ATOM   1154 N  NE  . ARG   B 1 10  ? 27.655 -22.222 16.056 1.00 24.06 ? 16  ARG   C NE  1 
ATOM   1155 C  CZ  . ARG   B 1 10  ? 27.206 -22.480 17.285 1.00 27.49 ? 16  ARG   C CZ  1 
ATOM   1156 N  NH1 . ARG   B 1 10  ? 27.061 -23.738 17.698 1.00 26.31 ? 16  ARG   C NH1 1 
ATOM   1157 N  NH2 . ARG   B 1 10  ? 26.848 -21.481 18.095 1.00 26.19 ? 16  ARG   C NH2 1 
ATOM   1158 N  N   . VAL   B 1 11  ? 24.211 -24.027 11.737 1.00 16.54 ? 17  VAL   C N   1 
ATOM   1159 C  CA  . VAL   B 1 11  ? 22.914 -23.315 11.770 1.00 16.82 ? 17  VAL   C CA  1 
ATOM   1160 C  C   . VAL   B 1 11  ? 22.470 -23.207 13.221 1.00 17.26 ? 17  VAL   C C   1 
ATOM   1161 O  O   . VAL   B 1 11  ? 22.334 -24.230 13.890 1.00 17.36 ? 17  VAL   C O   1 
ATOM   1162 C  CB  . VAL   B 1 11  ? 21.810 -24.098 10.974 1.00 17.33 ? 17  VAL   C CB  1 
ATOM   1163 C  CG1 . VAL   B 1 11  ? 20.539 -23.235 10.837 1.00 17.17 ? 17  VAL   C CG1 1 
ATOM   1164 C  CG2 . VAL   B 1 11  ? 22.327 -24.516 9.603  1.00 17.69 ? 17  VAL   C CG2 1 
ATOM   1165 N  N   . VAL   B 1 12  ? 22.190 -22.002 13.708 1.00 15.44 ? 18  VAL   C N   1 
ATOM   1166 C  CA  . VAL   B 1 12  ? 21.772 -21.810 15.093 1.00 16.20 ? 18  VAL   C CA  1 
ATOM   1167 C  C   . VAL   B 1 12  ? 20.578 -20.849 15.124 1.00 15.68 ? 18  VAL   C C   1 
ATOM   1168 O  O   . VAL   B 1 12  ? 20.322 -20.124 14.144 1.00 15.17 ? 18  VAL   C O   1 
ATOM   1169 C  CB  . VAL   B 1 12  ? 22.941 -21.201 15.931 1.00 18.10 ? 18  VAL   C CB  1 
ATOM   1170 C  CG1 . VAL   B 1 12  ? 24.065 -22.206 16.073 1.00 20.58 ? 18  VAL   C CG1 1 
ATOM   1171 C  CG2 . VAL   B 1 12  ? 23.450 -19.903 15.308 1.00 17.47 ? 18  VAL   C CG2 1 
ATOM   1172 N  N   . ASN   B 1 13  ? 19.882 -20.777 16.280 1.00 15.20 ? 19  ASN   C N   1 
ATOM   1173 C  CA  . ASN   B 1 13  ? 18.862 -19.728 16.461 1.00 14.97 ? 19  ASN   C CA  1 
ATOM   1174 C  C   . ASN   B 1 13  ? 19.613 -18.383 16.415 1.00 15.27 ? 19  ASN   C C   1 
ATOM   1175 O  O   . ASN   B 1 13  ? 20.628 -18.224 17.120 1.00 15.47 ? 19  ASN   C O   1 
ATOM   1176 C  CB  . ASN   B 1 13  ? 18.212 -19.826 17.834 1.00 15.60 ? 19  ASN   C CB  1 
ATOM   1177 C  CG  . ASN   B 1 13  ? 17.354 -21.070 17.990 1.00 17.40 ? 19  ASN   C CG  1 
ATOM   1178 O  OD1 . ASN   B 1 13  ? 17.833 -22.120 18.449 1.00 17.57 ? 19  ASN   C OD1 1 
ATOM   1179 N  ND2 . ASN   B 1 13  ? 16.095 -20.969 17.601 1.00 15.43 ? 19  ASN   C ND2 1 
ATOM   1180 N  N   . ARG   B 1 14  ? 19.135 -17.433 15.600 1.00 14.51 ? 20  ARG   C N   1 
ATOM   1181 C  CA  . ARG   B 1 14  ? 19.836 -16.127 15.514 1.00 14.04 ? 20  ARG   C CA  1 
ATOM   1182 C  C   . ARG   B 1 14  ? 19.992 -15.459 16.908 1.00 14.94 ? 20  ARG   C C   1 
ATOM   1183 O  O   . ARG   B 1 14  ? 21.046 -14.867 17.188 1.00 15.42 ? 20  ARG   C O   1 
ATOM   1184 C  CB  . ARG   B 1 14  ? 19.082 -15.203 14.555 1.00 15.19 ? 20  ARG   C CB  1 
ATOM   1185 C  CG  . ARG   B 1 14  ? 19.853 -13.921 14.158 1.00 16.47 ? 20  ARG   C CG  1 
ATOM   1186 C  CD  . ARG   B 1 14  ? 18.896 -13.029 13.385 1.00 17.02 ? 20  ARG   C CD  1 
ATOM   1187 N  NE  . ARG   B 1 14  ? 19.481 -11.770 12.858 1.00 16.91 ? 20  ARG   C NE  1 
ATOM   1188 C  CZ  . ARG   B 1 14  ? 19.529 -10.634 13.539 1.00 18.04 ? 20  ARG   C CZ  1 
ATOM   1189 N  NH1 . ARG   B 1 14  ? 19.199 -10.607 14.828 1.00 17.88 ? 20  ARG   C NH1 1 
ATOM   1190 N  NH2 . ARG   B 1 14  ? 20.005 -9.531  12.965 1.00 18.25 ? 20  ARG   C NH2 1 
ATOM   1191 N  N   . HIS   B 1 15  ? 18.959 -15.578 17.780 1.00 14.30 ? 21  HIS   C N   1 
ATOM   1192 C  CA  . HIS   B 1 15  ? 19.046 -14.924 19.097 1.00 14.51 ? 21  HIS   C CA  1 
ATOM   1193 C  C   . HIS   B 1 15  ? 20.057 -15.573 20.045 1.00 15.60 ? 21  HIS   C C   1 
ATOM   1194 O  O   . HIS   B 1 15  ? 20.422 -14.958 21.060 1.00 17.03 ? 21  HIS   C O   1 
ATOM   1195 C  CB  . HIS   B 1 15  ? 17.669 -14.785 19.746 1.00 14.47 ? 21  HIS   C CB  1 
ATOM   1196 C  CG  . HIS   B 1 15  ? 17.078 -16.044 20.302 1.00 16.35 ? 21  HIS   C CG  1 
ATOM   1197 N  ND1 . HIS   B 1 15  ? 16.399 -16.955 19.496 1.00 16.72 ? 21  HIS   C ND1 1 
ATOM   1198 C  CD2 . HIS   B 1 15  ? 17.053 -16.481 21.585 1.00 17.31 ? 21  HIS   C CD2 1 
ATOM   1199 C  CE1 . HIS   B 1 15  ? 15.999 -17.927 20.309 1.00 17.22 ? 21  HIS   C CE1 1 
ATOM   1200 N  NE2 . HIS   B 1 15  ? 16.351 -17.673 21.584 1.00 18.47 ? 21  HIS   C NE2 1 
ATOM   1201 N  N   . LEU   B 1 16  ? 20.554 -16.767 19.712 1.00 15.75 ? 22  LEU   C N   1 
ATOM   1202 C  CA  . LEU   B 1 16  ? 21.563 -17.439 20.553 1.00 16.26 ? 22  LEU   C CA  1 
ATOM   1203 C  C   . LEU   B 1 16  ? 22.958 -17.464 19.868 1.00 17.97 ? 22  LEU   C C   1 
ATOM   1204 O  O   . LEU   B 1 16  ? 23.870 -18.104 20.379 1.00 18.70 ? 22  LEU   C O   1 
ATOM   1205 C  CB  . LEU   B 1 16  ? 21.125 -18.889 20.843 1.00 16.44 ? 22  LEU   C CB  1 
ATOM   1206 C  CG  . LEU   B 1 16  ? 19.788 -18.982 21.629 1.00 17.77 ? 22  LEU   C CG  1 
ATOM   1207 C  CD1 . LEU   B 1 16  ? 19.411 -20.457 21.849 1.00 19.11 ? 22  LEU   C CD1 1 
ATOM   1208 C  CD2 . LEU   B 1 16  ? 19.862 -18.204 23.015 1.00 19.07 ? 22  LEU   C CD2 1 
ATOM   1209 N  N   . ALA   B 1 17  ? 23.117 -16.790 18.707 1.00 16.97 ? 23  ALA   C N   1 
ATOM   1210 C  CA  . ALA   B 1 17  ? 24.410 -16.780 17.992 1.00 18.11 ? 23  ALA   C CA  1 
ATOM   1211 C  C   . ALA   B 1 17  ? 25.483 -16.139 18.875 1.00 18.15 ? 23  ALA   C C   1 
ATOM   1212 O  O   . ALA   B 1 17  ? 25.206 -15.177 19.582 1.00 18.35 ? 23  ALA   C O   1 
ATOM   1213 C  CB  . ALA   B 1 17  ? 24.279 -15.985 16.696 1.00 18.27 ? 23  ALA   C CB  1 
ATOM   1214 N  N   . THR   B 1 18  ? 26.707 -16.666 18.815 1.00 17.90 ? 24  THR   C N   1 
ATOM   1215 C  CA  . THR   B 1 18  ? 27.822 -16.157 19.623 1.00 18.58 ? 24  THR   C CA  1 
ATOM   1216 C  C   . THR   B 1 18  ? 28.592 -15.052 18.879 1.00 18.82 ? 24  THR   C C   1 
ATOM   1217 O  O   . THR   B 1 18  ? 28.369 -14.839 17.683 1.00 17.80 ? 24  THR   C O   1 
ATOM   1218 C  CB  . THR   B 1 18  ? 28.775 -17.346 19.896 1.00 19.84 ? 24  THR   C CB  1 
ATOM   1219 O  OG1 . THR   B 1 18  ? 29.323 -17.782 18.646 1.00 20.95 ? 24  THR   C OG1 1 
ATOM   1220 C  CG2 . THR   B 1 18  ? 28.077 -18.500 20.597 1.00 19.72 ? 24  THR   C CG2 1 
ATOM   1221 N  N   . HIS   B 1 19  ? 29.598 -14.420 19.549 1.00 19.03 ? 25  HIS   C N   1 
ATOM   1222 C  CA  . HIS   B 1 19  ? 30.453 -13.458 18.848 1.00 19.88 ? 25  HIS   C CA  1 
ATOM   1223 C  C   . HIS   B 1 19  ? 31.166 -14.157 17.668 1.00 19.47 ? 25  HIS   C C   1 
ATOM   1224 O  O   . HIS   B 1 19  ? 31.296 -13.564 16.594 1.00 20.19 ? 25  HIS   C O   1 
ATOM   1225 C  CB  . HIS   B 1 19  ? 31.523 -12.907 19.819 1.00 23.47 ? 25  HIS   C CB  1 
ATOM   1226 C  CG  . HIS   B 1 19  ? 30.978 -12.121 20.970 1.00 30.89 ? 25  HIS   C CG  1 
ATOM   1227 N  ND1 . HIS   B 1 19  ? 30.306 -10.916 20.779 1.00 34.49 ? 25  HIS   C ND1 1 
ATOM   1228 C  CD2 . HIS   B 1 19  ? 31.098 -12.343 22.302 1.00 33.71 ? 25  HIS   C CD2 1 
ATOM   1229 C  CE1 . HIS   B 1 19  ? 30.017 -10.464 21.991 1.00 35.12 ? 25  HIS   C CE1 1 
ATOM   1230 N  NE2 . HIS   B 1 19  ? 30.456 -11.298 22.939 1.00 35.22 ? 25  HIS   C NE2 1 
ATOM   1231 N  N   . ASN   B 1 20  ? 31.581 -15.424 17.852 1.00 19.15 ? 26  ASN   C N   1 
ATOM   1232 C  CA  . ASN   B 1 20  ? 32.276 -16.151 16.776 1.00 19.40 ? 26  ASN   C CA  1 
ATOM   1233 C  C   . ASN   B 1 20  ? 31.338 -16.408 15.594 1.00 19.05 ? 26  ASN   C C   1 
ATOM   1234 O  O   . ASN   B 1 20  ? 31.769 -16.370 14.436 1.00 19.57 ? 26  ASN   C O   1 
ATOM   1235 C  CB  . ASN   B 1 20  ? 32.820 -17.496 17.280 1.00 23.14 ? 26  ASN   C CB  1 
ATOM   1236 C  CG  . ASN   B 1 20  ? 33.667 -18.202 16.241 1.00 31.37 ? 26  ASN   C CG  1 
ATOM   1237 O  OD1 . ASN   B 1 20  ? 34.695 -17.674 15.809 1.00 33.66 ? 26  ASN   C OD1 1 
ATOM   1238 N  ND2 . ASN   B 1 20  ? 33.261 -19.411 15.819 1.00 33.43 ? 26  ASN   C ND2 1 
ATOM   1239 N  N   . ASP   B 1 21  ? 30.037 -16.727 15.871 1.00 18.33 ? 27  ASP   C N   1 
ATOM   1240 C  CA  . ASP   B 1 21  ? 29.092 -16.929 14.755 1.00 18.25 ? 27  ASP   C CA  1 
ATOM   1241 C  C   . ASP   B 1 21  ? 28.974 -15.645 13.909 1.00 18.98 ? 27  ASP   C C   1 
ATOM   1242 O  O   . ASP   B 1 21  ? 28.986 -15.701 12.684 1.00 19.79 ? 27  ASP   C O   1 
ATOM   1243 C  CB  . ASP   B 1 21  ? 27.691 -17.270 15.299 1.00 17.64 ? 27  ASP   C CB  1 
ATOM   1244 C  CG  . ASP   B 1 21  ? 27.567 -18.690 15.827 1.00 21.14 ? 27  ASP   C CG  1 
ATOM   1245 O  OD1 . ASP   B 1 21  ? 28.103 -19.614 15.174 1.00 21.88 ? 27  ASP   C OD1 1 
ATOM   1246 O  OD2 . ASP   B 1 21  ? 26.948 -18.872 16.911 1.00 21.05 ? 27  ASP   C OD2 1 
ATOM   1247 N  N   . TRP   B 1 22  ? 28.855 -14.493 14.579 1.00 18.80 ? 28  TRP   C N   1 
ATOM   1248 C  CA  . TRP   B 1 22  ? 28.725 -13.220 13.874 1.00 19.00 ? 28  TRP   C CA  1 
ATOM   1249 C  C   . TRP   B 1 22  ? 30.029 -12.829 13.139 1.00 19.72 ? 28  TRP   C C   1 
ATOM   1250 O  O   . TRP   B 1 22  ? 29.964 -12.234 12.063 1.00 20.76 ? 28  TRP   C O   1 
ATOM   1251 C  CB  . TRP   B 1 22  ? 28.297 -12.112 14.855 1.00 19.30 ? 28  TRP   C CB  1 
ATOM   1252 C  CG  . TRP   B 1 22  ? 26.814 -12.075 15.084 1.00 17.88 ? 28  TRP   C CG  1 
ATOM   1253 C  CD1 . TRP   B 1 22  ? 26.122 -12.540 16.165 1.00 18.17 ? 28  TRP   C CD1 1 
ATOM   1254 C  CD2 . TRP   B 1 22  ? 25.845 -11.497 14.194 1.00 17.30 ? 28  TRP   C CD2 1 
ATOM   1255 N  NE1 . TRP   B 1 22  ? 24.770 -12.291 16.004 1.00 18.70 ? 28  TRP   C NE1 1 
ATOM   1256 C  CE2 . TRP   B 1 22  ? 24.575 -11.668 14.786 1.00 17.84 ? 28  TRP   C CE2 1 
ATOM   1257 C  CE3 . TRP   B 1 22  ? 25.926 -10.911 12.924 1.00 18.46 ? 28  TRP   C CE3 1 
ATOM   1258 C  CZ2 . TRP   B 1 22  ? 23.404 -11.204 14.180 1.00 18.35 ? 28  TRP   C CZ2 1 
ATOM   1259 C  CZ3 . TRP   B 1 22  ? 24.762 -10.466 12.316 1.00 19.15 ? 28  TRP   C CZ3 1 
ATOM   1260 C  CH2 . TRP   B 1 22  ? 23.521 -10.629 12.937 1.00 18.44 ? 28  TRP   C CH2 1 
ATOM   1261 N  N   . ALA   B 1 23  ? 31.178 -13.229 13.676 1.00 18.87 ? 29  ALA   C N   1 
ATOM   1262 C  CA  . ALA   B 1 23  ? 32.471 -12.925 13.024 1.00 20.62 ? 29  ALA   C CA  1 
ATOM   1263 C  C   . ALA   B 1 23  ? 32.715 -13.813 11.780 1.00 21.77 ? 29  ALA   C C   1 
ATOM   1264 O  O   . ALA   B 1 23  ? 33.631 -13.536 10.994 1.00 22.50 ? 29  ALA   C O   1 
ATOM   1265 C  CB  . ALA   B 1 23  ? 33.616 -13.144 14.018 1.00 20.26 ? 29  ALA   C CB  1 
ATOM   1266 N  N   . ASN   B 1 24  ? 31.987 -14.944 11.676 1.00 19.58 ? 30  ASN   C N   1 
ATOM   1267 C  CA  . ASN   B 1 24  ? 32.122 -15.882 10.556 1.00 19.35 ? 30  ASN   C CA  1 
ATOM   1268 C  C   . ASN   B 1 24  ? 30.741 -16.043 9.856  1.00 20.28 ? 30  ASN   C C   1 
ATOM   1269 O  O   . ASN   B 1 24  ? 30.368 -17.117 9.433  1.00 20.30 ? 30  ASN   C O   1 
ATOM   1270 C  CB  . ASN   B 1 24  ? 32.617 -17.227 11.093 1.00 19.67 ? 30  ASN   C CB  1 
ATOM   1271 C  CG  . ASN   B 1 24  ? 34.054 -17.118 11.596 1.00 24.74 ? 30  ASN   C CG  1 
ATOM   1272 O  OD1 . ASN   B 1 24  ? 35.013 -17.045 10.801 1.00 25.38 ? 30  ASN   C OD1 1 
ATOM   1273 N  ND2 . ASN   B 1 24  ? 34.228 -17.046 12.922 1.00 24.76 ? 30  ASN   C ND2 1 
ATOM   1274 N  N   . LEU   B 1 25  ? 30.000 -14.955 9.779  1.00 20.19 ? 31  LEU   C N   1 
ATOM   1275 C  CA  . LEU   B 1 25  ? 28.647 -14.934 9.245  1.00 20.04 ? 31  LEU   C CA  1 
ATOM   1276 C  C   . LEU   B 1 25  ? 28.550 -15.304 7.777  1.00 20.23 ? 31  LEU   C C   1 
ATOM   1277 O  O   . LEU   B 1 25  ? 29.275 -14.742 6.955  1.00 22.19 ? 31  LEU   C O   1 
ATOM   1278 C  CB  . LEU   B 1 25  ? 28.107 -13.512 9.434  1.00 20.09 ? 31  LEU   C CB  1 
ATOM   1279 C  CG  . LEU   B 1 25  ? 26.673 -13.267 8.944  1.00 21.01 ? 31  LEU   C CG  1 
ATOM   1280 C  CD1 . LEU   B 1 25  ? 25.683 -14.161 9.722  1.00 20.05 ? 31  LEU   C CD1 1 
ATOM   1281 C  CD2 . LEU   B 1 25  ? 26.298 -11.810 9.162  1.00 21.19 ? 31  LEU   C CD2 1 
ATOM   1282 N  N   . VAL   B 1 26  ? 27.605 -16.205 7.427  1.00 18.05 ? 32  VAL   C N   1 
ATOM   1283 C  CA  . VAL   B 1 26  ? 27.307 -16.559 6.040  1.00 18.66 ? 32  VAL   C CA  1 
ATOM   1284 C  C   . VAL   B 1 26  ? 25.967 -15.918 5.645  1.00 20.19 ? 32  VAL   C C   1 
ATOM   1285 O  O   . VAL   B 1 26  ? 25.839 -15.292 4.581  1.00 21.52 ? 32  VAL   C O   1 
ATOM   1286 C  CB  . VAL   B 1 26  ? 27.259 -18.099 5.856  1.00 19.39 ? 32  VAL   C CB  1 
ATOM   1287 C  CG1 . VAL   B 1 26  ? 26.728 -18.487 4.463  1.00 19.49 ? 32  VAL   C CG1 1 
ATOM   1288 C  CG2 . VAL   B 1 26  ? 28.655 -18.702 6.114  1.00 19.75 ? 32  VAL   C CG2 1 
ATOM   1289 N  N   . TRP   B 1 27  ? 24.965 -16.051 6.526  1.00 19.25 ? 33  TRP   C N   1 
ATOM   1290 C  CA  . TRP   B 1 27  ? 23.616 -15.543 6.255  1.00 18.76 ? 33  TRP   C CA  1 
ATOM   1291 C  C   . TRP   B 1 27  ? 22.858 -15.475 7.552  1.00 18.23 ? 33  TRP   C C   1 
ATOM   1292 O  O   . TRP   B 1 27  ? 23.051 -16.320 8.421  1.00 17.93 ? 33  TRP   C O   1 
ATOM   1293 C  CB  . TRP   B 1 27  ? 22.896 -16.547 5.291  1.00 19.39 ? 33  TRP   C CB  1 
ATOM   1294 C  CG  . TRP   B 1 27  ? 21.410 -16.340 5.098  1.00 20.06 ? 33  TRP   C CG  1 
ATOM   1295 C  CD1 . TRP   B 1 27  ? 20.796 -15.462 4.246  1.00 22.06 ? 33  TRP   C CD1 1 
ATOM   1296 C  CD2 . TRP   B 1 27  ? 20.352 -17.076 5.746  1.00 19.88 ? 33  TRP   C CD2 1 
ATOM   1297 N  NE1 . TRP   B 1 27  ? 19.419 -15.570 4.372  1.00 22.14 ? 33  TRP   C NE1 1 
ATOM   1298 C  CE2 . TRP   B 1 27  ? 19.125 -16.554 5.284  1.00 21.22 ? 33  TRP   C CE2 1 
ATOM   1299 C  CE3 . TRP   B 1 27  ? 20.328 -18.107 6.699  1.00 20.17 ? 33  TRP   C CE3 1 
ATOM   1300 C  CZ2 . TRP   B 1 27  ? 17.882 -17.078 5.696  1.00 20.95 ? 33  TRP   C CZ2 1 
ATOM   1301 C  CZ3 . TRP   B 1 27  ? 19.102 -18.604 7.123  1.00 20.19 ? 33  TRP   C CZ3 1 
ATOM   1302 C  CH2 . TRP   B 1 27  ? 17.897 -18.095 6.623  1.00 19.81 ? 33  TRP   C CH2 1 
ATOM   1303 N  N   . GLU   B 1 28  ? 22.008 -14.471 7.701  1.00 17.71 ? 34  GLU   C N   1 
ATOM   1304 C  CA  . GLU   B 1 28  ? 21.109 -14.412 8.852  1.00 17.96 ? 34  GLU   C CA  1 
ATOM   1305 C  C   . GLU   B 1 28  ? 19.769 -13.798 8.441  1.00 17.81 ? 34  GLU   C C   1 
ATOM   1306 O  O   . GLU   B 1 28  ? 19.711 -13.001 7.486  1.00 17.17 ? 34  GLU   C O   1 
ATOM   1307 C  CB  . GLU   B 1 28  ? 21.713 -13.672 10.056 1.00 17.84 ? 34  GLU   C CB  1 
ATOM   1308 C  CG  . GLU   B 1 28  ? 22.309 -12.303 9.739  1.00 18.55 ? 34  GLU   C CG  1 
ATOM   1309 C  CD  . GLU   B 1 28  ? 21.326 -11.156 9.587  1.00 23.71 ? 34  GLU   C CD  1 
ATOM   1310 O  OE1 . GLU   B 1 28  ? 21.624 -10.224 8.803  1.00 26.10 ? 34  GLU   C OE1 1 
ATOM   1311 O  OE2 . GLU   B 1 28  ? 20.267 -11.168 10.264 1.00 21.34 ? 34  GLU   C OE2 1 
ATOM   1312 N  N   . ASP   B 1 29  ? 18.694 -14.180 9.144  1.00 16.91 ? 35  ASP   C N   1 
ATOM   1313 C  CA  . ASP   B 1 29  ? 17.374 -13.616 8.832  1.00 16.47 ? 35  ASP   C CA  1 
ATOM   1314 C  C   . ASP   B 1 29  ? 16.606 -13.465 10.157 1.00 16.15 ? 35  ASP   C C   1 
ATOM   1315 O  O   . ASP   B 1 29  ? 16.176 -14.455 10.740 1.00 16.13 ? 35  ASP   C O   1 
ATOM   1316 C  CB  . ASP   B 1 29  ? 16.638 -14.513 7.839  1.00 17.35 ? 35  ASP   C CB  1 
ATOM   1317 C  CG  . ASP   B 1 29  ? 15.340 -13.927 7.346  1.00 22.64 ? 35  ASP   C CG  1 
ATOM   1318 O  OD1 . ASP   B 1 29  ? 14.749 -13.098 8.068  1.00 24.93 ? 35  ASP   C OD1 1 
ATOM   1319 O  OD2 . ASP   B 1 29  ? 14.905 -14.300 6.226  1.00 22.65 ? 35  ASP   C OD2 1 
ATOM   1320 N  N   . SER   B 1 30  ? 16.450 -12.210 10.647 1.00 15.66 ? 36  SER   C N   1 
ATOM   1321 C  CA  A SER   B 1 30  ? 15.760 -11.951 11.893 0.50 16.24 ? 36  SER   C CA  1 
ATOM   1322 C  CA  B SER   B 1 30  ? 15.757 -11.983 11.910 0.50 15.85 ? 36  SER   C CA  1 
ATOM   1323 C  C   . SER   B 1 30  ? 14.300 -12.432 11.834 1.00 16.90 ? 36  SER   C C   1 
ATOM   1324 O  O   . SER   B 1 30  ? 13.773 -12.897 12.832 1.00 17.54 ? 36  SER   C O   1 
ATOM   1325 C  CB  A SER   B 1 30  ? 15.830 -10.457 12.215 0.50 18.85 ? 36  SER   C CB  1 
ATOM   1326 C  CB  B SER   B 1 30  ? 15.824 -10.511 12.321 0.50 17.38 ? 36  SER   C CB  1 
ATOM   1327 O  OG  A SER   B 1 30  ? 15.007 -10.108 13.307 0.50 22.14 ? 36  SER   C OG  1 
ATOM   1328 O  OG  B SER   B 1 30  ? 15.062 -9.733  11.414 0.50 18.80 ? 36  SER   C OG  1 
ATOM   1329 N  N   . SER   B 1 31  ? 13.666 -12.306 10.659 1.00 16.16 ? 37  SER   C N   1 
ATOM   1330 C  CA  . SER   B 1 31  ? 12.259 -12.723 10.542 1.00 16.49 ? 37  SER   C CA  1 
ATOM   1331 C  C   . SER   B 1 31  ? 12.097 -14.234 10.722 1.00 16.63 ? 37  SER   C C   1 
ATOM   1332 O  O   . SER   B 1 31  ? 10.980 -14.669 11.028 1.00 18.01 ? 37  SER   C O   1 
ATOM   1333 C  CB  . SER   B 1 31  ? 11.657 -12.276 9.211  1.00 20.00 ? 37  SER   C CB  1 
ATOM   1334 O  OG  . SER   B 1 31  ? 12.090 -13.103 8.137  1.00 23.72 ? 37  SER   C OG  1 
ATOM   1335 N  N   . ARG   B 1 32  ? 13.160 -15.020 10.540 1.00 13.70 ? 38  ARG   C N   1 
ATOM   1336 C  CA  . ARG   B 1 32  ? 13.100 -16.495 10.695 1.00 13.41 ? 38  ARG   C CA  1 
ATOM   1337 C  C   . ARG   B 1 32  ? 13.761 -16.981 12.010 1.00 14.23 ? 38  ARG   C C   1 
ATOM   1338 O  O   . ARG   B 1 32  ? 13.714 -18.187 12.319 1.00 14.37 ? 38  ARG   C O   1 
ATOM   1339 C  CB  . ARG   B 1 32  ? 13.828 -17.190 9.508  1.00 15.27 ? 38  ARG   C CB  1 
ATOM   1340 C  CG  . ARG   B 1 32  ? 13.112 -16.922 8.180  1.00 15.72 ? 38  ARG   C CG  1 
ATOM   1341 C  CD  . ARG   B 1 32  ? 13.820 -17.592 7.000  1.00 15.55 ? 38  ARG   C CD  1 
ATOM   1342 N  NE  . ARG   B 1 32  ? 13.814 -19.051 7.117  1.00 15.18 ? 38  ARG   C NE  1 
ATOM   1343 C  CZ  . ARG   B 1 32  ? 13.862 -19.876 6.072  1.00 16.66 ? 38  ARG   C CZ  1 
ATOM   1344 N  NH1 . ARG   B 1 32  ? 13.929 -19.388 4.827  1.00 17.41 ? 38  ARG   C NH1 1 
ATOM   1345 N  NH2 . ARG   B 1 32  ? 13.784 -21.195 6.254  1.00 17.24 ? 38  ARG   C NH2 1 
ATOM   1346 N  N   . ASP   B 1 33  ? 14.454 -16.090 12.723 1.00 14.31 ? 39  ASP   C N   1 
ATOM   1347 C  CA  . ASP   B 1 33  ? 15.255 -16.459 13.900 1.00 13.42 ? 39  ASP   C CA  1 
ATOM   1348 C  C   . ASP   B 1 33  ? 16.342 -17.458 13.515 1.00 14.05 ? 39  ASP   C C   1 
ATOM   1349 O  O   . ASP   B 1 33  ? 16.697 -18.313 14.331 1.00 14.63 ? 39  ASP   C O   1 
ATOM   1350 C  CB  . ASP   B 1 33  ? 14.411 -17.005 15.091 1.00 14.80 ? 39  ASP   C CB  1 
ATOM   1351 C  CG  . ASP   B 1 33  ? 15.226 -17.288 16.366 1.00 15.45 ? 39  ASP   C CG  1 
ATOM   1352 O  OD1 . ASP   B 1 33  ? 16.134 -16.456 16.710 1.00 15.96 ? 39  ASP   C OD1 1 
ATOM   1353 O  OD2 . ASP   B 1 33  ? 14.982 -18.343 17.029 1.00 14.76 ? 39  ASP   C OD2 1 
ATOM   1354 N  N   . LEU   B 1 34  ? 16.949 -17.294 12.320 1.00 13.53 ? 40  LEU   C N   1 
ATOM   1355 C  CA  . LEU   B 1 34  ? 18.069 -18.174 11.942 1.00 13.61 ? 40  LEU   C CA  1 
ATOM   1356 C  C   . LEU   B 1 34  ? 19.358 -17.414 11.637 1.00 14.59 ? 40  LEU   C C   1 
ATOM   1357 O  O   . LEU   B 1 34  ? 19.327 -16.324 11.062 1.00 15.57 ? 40  LEU   C O   1 
ATOM   1358 C  CB  . LEU   B 1 34  ? 17.736 -18.970 10.671 1.00 13.72 ? 40  LEU   C CB  1 
ATOM   1359 C  CG  . LEU   B 1 34  ? 16.656 -20.052 10.822 1.00 15.38 ? 40  LEU   C CG  1 
ATOM   1360 C  CD1 . LEU   B 1 34  ? 16.443 -20.736 9.438  1.00 15.52 ? 40  LEU   C CD1 1 
ATOM   1361 C  CD2 . LEU   B 1 34  ? 17.079 -21.104 11.865 1.00 16.57 ? 40  LEU   C CD2 1 
ATOM   1362 N  N   . LEU   B 1 35  ? 20.491 -18.085 11.885 1.00 13.62 ? 41  LEU   C N   1 
ATOM   1363 C  CA  . LEU   B 1 35  ? 21.791 -17.531 11.525 1.00 14.14 ? 41  LEU   C CA  1 
ATOM   1364 C  C   . LEU   B 1 35  ? 22.660 -18.718 11.139 1.00 14.80 ? 41  LEU   C C   1 
ATOM   1365 O  O   . LEU   B 1 35  ? 22.573 -19.777 11.781 1.00 15.59 ? 41  LEU   C O   1 
ATOM   1366 C  CB  . LEU   B 1 35  ? 22.418 -16.735 12.688 1.00 14.66 ? 41  LEU   C CB  1 
ATOM   1367 C  CG  . LEU   B 1 35  ? 23.793 -16.084 12.383 1.00 15.91 ? 41  LEU   C CG  1 
ATOM   1368 C  CD1 . LEU   B 1 35  ? 23.971 -14.738 13.144 1.00 16.77 ? 41  LEU   C CD1 1 
ATOM   1369 C  CD2 . LEU   B 1 35  ? 24.961 -17.042 12.781 1.00 17.92 ? 41  LEU   C CD2 1 
ATOM   1370 N  N   . VAL   B 1 36  ? 23.445 -18.576 10.080 1.00 14.14 ? 42  VAL   C N   1 
ATOM   1371 C  CA  . VAL   B 1 36  ? 24.370 -19.612 9.604  1.00 14.70 ? 42  VAL   C CA  1 
ATOM   1372 C  C   . VAL   B 1 36  ? 25.770 -19.002 9.595  1.00 16.59 ? 42  VAL   C C   1 
ATOM   1373 O  O   . VAL   B 1 36  ? 25.985 -17.915 9.040  1.00 16.17 ? 42  VAL   C O   1 
ATOM   1374 C  CB  . VAL   B 1 36  ? 23.964 -20.099 8.190  1.00 15.20 ? 42  VAL   C CB  1 
ATOM   1375 C  CG1 . VAL   B 1 36  ? 24.978 -21.119 7.647  1.00 17.13 ? 42  VAL   C CG1 1 
ATOM   1376 C  CG2 . VAL   B 1 36  ? 22.554 -20.712 8.244  1.00 15.49 ? 42  VAL   C CG2 1 
ATOM   1377 N  N   . SER   B 1 37  ? 26.714 -19.713 10.216 1.00 17.25 ? 43  SER   C N   1 
ATOM   1378 C  CA  . SER   B 1 37  ? 28.116 -19.283 10.226 1.00 17.22 ? 43  SER   C CA  1 
ATOM   1379 C  C   . SER   B 1 37  ? 28.988 -20.387 9.603  1.00 18.09 ? 43  SER   C C   1 
ATOM   1380 O  O   . SER   B 1 37  ? 28.544 -21.539 9.430  1.00 18.34 ? 43  SER   C O   1 
ATOM   1381 C  CB  . SER   B 1 37  ? 28.565 -18.988 11.652 1.00 17.88 ? 43  SER   C CB  1 
ATOM   1382 O  OG  . SER   B 1 37  ? 28.424 -20.126 12.498 1.00 20.04 ? 43  SER   C OG  1 
ATOM   1383 N  N   . SER   B 1 38  ? 30.220 -20.009 9.219  1.00 19.03 ? 44  SER   C N   1 
ATOM   1384 C  CA  . SER   B 1 38  ? 31.103 -20.984 8.584  1.00 21.63 ? 44  SER   C CA  1 
ATOM   1385 C  C   . SER   B 1 38  ? 31.964 -21.724 9.616  1.00 23.89 ? 44  SER   C C   1 
ATOM   1386 O  O   . SER   B 1 38  ? 32.280 -21.183 10.679 1.00 25.06 ? 44  SER   C O   1 
ATOM   1387 C  CB  . SER   B 1 38  ? 31.982 -20.298 7.547  1.00 24.14 ? 44  SER   C CB  1 
ATOM   1388 O  OG  . SER   B 1 38  ? 32.736 -19.284 8.173  1.00 27.90 ? 44  SER   C OG  1 
ATOM   1389 N  N   . THR   B 1 39  ? 32.306 -22.988 9.313  1.00 25.41 ? 45  THR   C N   1 
ATOM   1390 C  CA  . THR   B 1 39  ? 33.125 -23.817 10.211 1.00 28.24 ? 45  THR   C CA  1 
ATOM   1391 C  C   . THR   B 1 39  ? 34.346 -24.344 9.458  1.00 30.95 ? 45  THR   C C   1 
ATOM   1392 O  O   . THR   B 1 39  ? 34.334 -24.393 8.224  1.00 31.32 ? 45  THR   C O   1 
ATOM   1393 C  CB  . THR   B 1 39  ? 32.296 -25.035 10.689 1.00 29.72 ? 45  THR   C CB  1 
ATOM   1394 O  OG1 . THR   B 1 39  ? 32.064 -25.901 9.582  1.00 31.47 ? 45  THR   C OG1 1 
ATOM   1395 C  CG2 . THR   B 1 39  ? 30.966 -24.639 11.281 1.00 29.45 ? 45  THR   C CG2 1 
ATOM   1396 N  N   . THR   B 1 40  ? 35.372 -24.786 10.188 1.00 33.00 ? 46  THR   C N   1 
ATOM   1397 C  CA  . THR   B 1 40  ? 36.537 -25.399 9.554  1.00 35.38 ? 46  THR   C CA  1 
ATOM   1398 C  C   . THR   B 1 40  ? 36.315 -26.910 9.407  1.00 37.22 ? 46  THR   C C   1 
ATOM   1399 O  O   . THR   B 1 40  ? 36.768 -27.503 8.422  1.00 39.05 ? 46  THR   C O   1 
ATOM   1400 C  CB  . THR   B 1 40  ? 37.818 -25.061 10.322 1.00 37.22 ? 46  THR   C CB  1 
ATOM   1401 O  OG1 . THR   B 1 40  ? 37.612 -25.373 11.701 1.00 39.41 ? 46  THR   C OG1 1 
ATOM   1402 C  CG2 . THR   B 1 40  ? 38.201 -23.593 10.185 1.00 37.35 ? 46  THR   C CG2 1 
ATOM   1403 N  N   . ALA   B 1 41  ? 35.623 -27.542 10.375 1.00 36.70 ? 47  ALA   C N   1 
ATOM   1404 C  CA  . ALA   B 1 41  ? 35.382 -28.984 10.333 1.00 36.76 ? 47  ALA   C CA  1 
ATOM   1405 C  C   . ALA   B 1 41  ? 34.150 -29.344 9.513  1.00 36.91 ? 47  ALA   C C   1 
ATOM   1406 O  O   . ALA   B 1 41  ? 33.214 -28.550 9.416  1.00 37.22 ? 47  ALA   C O   1 
ATOM   1407 C  CB  . ALA   B 1 41  ? 35.243 -29.536 11.740 1.00 37.04 ? 47  ALA   C CB  1 
ATOM   1408 N  N   . GLN   B 1 42  ? 34.140 -30.548 8.944  1.00 36.58 ? 48  GLN   C N   1 
ATOM   1409 C  CA  . GLN   B 1 42  ? 33.021 -31.003 8.125  1.00 36.65 ? 48  GLN   C CA  1 
ATOM   1410 C  C   . GLN   B 1 42  ? 31.892 -31.517 9.016  1.00 34.66 ? 48  GLN   C C   1 
ATOM   1411 O  O   . GLN   B 1 42  ? 32.125 -32.325 9.899  1.00 35.54 ? 48  GLN   C O   1 
ATOM   1412 C  CB  . GLN   B 1 42  ? 33.479 -32.124 7.183  1.00 40.73 ? 48  GLN   C CB  1 
ATOM   1413 C  CG  . GLN   B 1 42  ? 32.611 -32.243 5.932  1.00 48.12 ? 48  GLN   C CG  1 
ATOM   1414 C  CD  . GLN   B 1 42  ? 32.958 -31.180 4.922  1.00 56.68 ? 48  GLN   C CD  1 
ATOM   1415 O  OE1 . GLN   B 1 42  ? 34.105 -30.714 4.839  1.00 59.73 ? 48  GLN   C OE1 1 
ATOM   1416 N  NE2 . GLN   B 1 42  ? 31.984 -30.788 4.118  1.00 57.91 ? 48  GLN   C NE2 1 
ATOM   1417 N  N   . GLY   B 1 43  ? 30.683 -31.029 8.792  1.00 31.30 ? 49  GLY   C N   1 
ATOM   1418 C  CA  . GLY   B 1 43  ? 29.511 -31.445 9.564  1.00 29.64 ? 49  GLY   C CA  1 
ATOM   1419 C  C   . GLY   B 1 43  ? 28.811 -32.571 8.822  1.00 27.53 ? 49  GLY   C C   1 
ATOM   1420 O  O   . GLY   B 1 43  ? 28.809 -32.586 7.574  1.00 27.84 ? 49  GLY   C O   1 
ATOM   1421 N  N   . CYS   B 1 44  ? 28.225 -33.509 9.546  1.00 25.67 ? 50  CYS   C N   1 
ATOM   1422 C  CA  . CYS   B 1 44  ? 27.628 -34.666 8.908  1.00 25.33 ? 50  CYS   C CA  1 
ATOM   1423 C  C   . CYS   B 1 44  ? 26.106 -34.759 9.031  1.00 23.86 ? 50  CYS   C C   1 
ATOM   1424 O  O   . CYS   B 1 44  ? 25.575 -35.845 8.777  1.00 24.45 ? 50  CYS   C O   1 
ATOM   1425 C  CB  . CYS   B 1 44  ? 28.301 -35.944 9.401  1.00 27.91 ? 50  CYS   C CB  1 
ATOM   1426 S  SG  . CYS   B 1 44  ? 30.085 -35.995 9.093  1.00 34.48 ? 50  CYS   C SG  1 
ATOM   1427 N  N   . ASP   B 1 45  ? 25.392 -33.662 9.404  1.00 21.04 ? 51  ASP   C N   1 
ATOM   1428 C  CA  . ASP   B 1 45  ? 23.925 -33.767 9.511  1.00 20.92 ? 51  ASP   C CA  1 
ATOM   1429 C  C   . ASP   B 1 45  ? 23.303 -33.807 8.111  1.00 21.87 ? 51  ASP   C C   1 
ATOM   1430 O  O   . ASP   B 1 45  ? 23.771 -33.100 7.224  1.00 23.18 ? 51  ASP   C O   1 
ATOM   1431 C  CB  . ASP   B 1 45  ? 23.303 -32.593 10.325 1.00 21.91 ? 51  ASP   C CB  1 
ATOM   1432 C  CG  . ASP   B 1 45  ? 23.621 -32.633 11.816 1.00 28.52 ? 51  ASP   C CG  1 
ATOM   1433 O  OD1 . ASP   B 1 45  ? 23.941 -33.728 12.333 1.00 29.68 ? 51  ASP   C OD1 1 
ATOM   1434 O  OD2 . ASP   B 1 45  ? 23.568 -31.571 12.466 1.00 28.78 ? 51  ASP   C OD2 1 
ATOM   1435 N  N   . THR   B 1 46  ? 22.286 -34.636 7.902  1.00 20.47 ? 52  THR   C N   1 
ATOM   1436 C  CA  . THR   B 1 46  ? 21.581 -34.682 6.616  1.00 21.63 ? 52  THR   C CA  1 
ATOM   1437 C  C   . THR   B 1 46  ? 20.357 -33.796 6.756  1.00 19.95 ? 52  THR   C C   1 
ATOM   1438 O  O   . THR   B 1 46  ? 19.611 -33.990 7.699  1.00 20.37 ? 52  THR   C O   1 
ATOM   1439 C  CB  . THR   B 1 46  ? 21.110 -36.113 6.326  1.00 26.62 ? 52  THR   C CB  1 
ATOM   1440 O  OG1 . THR   B 1 46  ? 22.292 -36.921 6.108  1.00 30.67 ? 52  THR   C OG1 1 
ATOM   1441 C  CG2 . THR   B 1 46  ? 20.190 -36.189 5.093  1.00 27.82 ? 52  THR   C CG2 1 
ATOM   1442 N  N   . ILE   B 1 47  ? 20.140 -32.865 5.820  1.00 18.56 ? 53  ILE   C N   1 
ATOM   1443 C  CA  . ILE   B 1 47  ? 18.965 -32.006 5.882  1.00 17.54 ? 53  ILE   C CA  1 
ATOM   1444 C  C   . ILE   B 1 47  ? 17.852 -32.664 5.083  1.00 17.22 ? 53  ILE   C C   1 
ATOM   1445 O  O   . ILE   B 1 47  ? 18.088 -33.140 3.948  1.00 17.44 ? 53  ILE   C O   1 
ATOM   1446 C  CB  . ILE   B 1 47  ? 19.238 -30.607 5.282  1.00 19.00 ? 53  ILE   C CB  1 
ATOM   1447 C  CG1 . ILE   B 1 47  ? 20.491 -29.942 5.911  1.00 21.52 ? 53  ILE   C CG1 1 
ATOM   1448 C  CG2 . ILE   B 1 47  ? 17.991 -29.670 5.428  1.00 19.31 ? 53  ILE   C CG2 1 
ATOM   1449 C  CD1 . ILE   B 1 47  ? 20.335 -29.683 7.407  1.00 22.97 ? 53  ILE   C CD1 1 
ATOM   1450 N  N   . ALA   B 1 48  ? 16.650 -32.698 5.653  1.00 15.63 ? 54  ALA   C N   1 
ATOM   1451 C  CA  . ALA   B 1 48  ? 15.503 -33.255 4.935  1.00 15.01 ? 54  ALA   C CA  1 
ATOM   1452 C  C   . ALA   B 1 48  ? 15.080 -32.333 3.792  1.00 14.22 ? 54  ALA   C C   1 
ATOM   1453 O  O   . ALA   B 1 48  ? 15.118 -31.115 3.943  1.00 14.18 ? 54  ALA   C O   1 
ATOM   1454 C  CB  . ALA   B 1 48  ? 14.329 -33.382 5.904  1.00 14.33 ? 54  ALA   C CB  1 
ATOM   1455 N  N   . ARG   B 1 49  ? 14.622 -32.911 2.657  1.00 13.72 ? 55  ARG   C N   1 
ATOM   1456 C  CA  . ARG   B 1 49  ? 14.154 -32.141 1.475  1.00 14.29 ? 55  ARG   C CA  1 
ATOM   1457 C  C   . ARG   B 1 49  ? 12.808 -32.815 1.157  1.00 14.53 ? 55  ARG   C C   1 
ATOM   1458 O  O   . ARG   B 1 49  ? 12.746 -33.783 0.389  1.00 15.21 ? 55  ARG   C O   1 
ATOM   1459 C  CB  . ARG   B 1 49  ? 15.138 -32.257 0.314  1.00 15.07 ? 55  ARG   C CB  1 
ATOM   1460 C  CG  . ARG   B 1 49  ? 16.539 -31.765 0.687  1.00 16.07 ? 55  ARG   C CG  1 
ATOM   1461 C  CD  . ARG   B 1 49  ? 16.599 -30.254 0.999  1.00 17.44 ? 55  ARG   C CD  1 
ATOM   1462 N  NE  . ARG   B 1 49  ? 17.996 -29.842 1.258  1.00 19.77 ? 55  ARG   C NE  1 
ATOM   1463 C  CZ  . ARG   B 1 49  ? 18.343 -28.744 1.921  1.00 20.97 ? 55  ARG   C CZ  1 
ATOM   1464 N  NH1 . ARG   B 1 49  ? 17.414 -27.907 2.360  1.00 18.15 ? 55  ARG   C NH1 1 
ATOM   1465 N  NH2 . ARG   B 1 49  ? 19.634 -28.457 2.127  1.00 19.47 ? 55  ARG   C NH2 1 
ATOM   1466 N  N   . CYS   B 1 50  ? 11.754 -32.313 1.800  1.00 13.91 ? 56  CYS   C N   1 
ATOM   1467 C  CA  . CYS   B 1 50  ? 10.459 -32.963 1.818  1.00 14.68 ? 56  CYS   C CA  1 
ATOM   1468 C  C   . CYS   B 1 50  ? 9.341  -32.032 2.316  1.00 15.35 ? 56  CYS   C C   1 
ATOM   1469 O  O   . CYS   B 1 50  ? 9.603  -30.909 2.743  1.00 14.90 ? 56  CYS   C O   1 
ATOM   1470 C  CB  . CYS   B 1 50  ? 10.569 -34.173 2.739  1.00 14.66 ? 56  CYS   C CB  1 
ATOM   1471 S  SG  . CYS   B 1 50  ? 10.723 -33.708 4.498  1.00 15.55 ? 56  CYS   C SG  1 
ATOM   1472 N  N   . ASP   B 1 51  ? 8.094  -32.564 2.353  1.00 15.29 ? 57  ASP   C N   1 
ATOM   1473 C  CA  . ASP   B 1 51  ? 6.944  -31.863 2.936  1.00 16.19 ? 57  ASP   C CA  1 
ATOM   1474 C  C   . ASP   B 1 51  ? 6.342  -32.650 4.105  1.00 16.94 ? 57  ASP   C C   1 
ATOM   1475 O  O   . ASP   B 1 51  ? 5.139  -32.563 4.383  1.00 17.40 ? 57  ASP   C O   1 
ATOM   1476 C  CB  . ASP   B 1 51  ? 5.873  -31.562 1.871  1.00 18.24 ? 57  ASP   C CB  1 
ATOM   1477 C  CG  . ASP   B 1 51  ? 5.253  -32.771 1.231  1.00 24.85 ? 57  ASP   C CG  1 
ATOM   1478 O  OD1 . ASP   B 1 51  ? 5.624  -33.910 1.604  1.00 24.74 ? 57  ASP   C OD1 1 
ATOM   1479 O  OD2 . ASP   B 1 51  ? 4.384  -32.589 0.337  1.00 30.19 ? 57  ASP   C OD2 1 
ATOM   1480 N  N   . CYS   B 1 52  ? 7.181  -33.405 4.849  1.00 15.01 ? 58  CYS   C N   1 
ATOM   1481 C  CA  . CYS   B 1 52  ? 6.694  -34.164 6.017  1.00 14.27 ? 58  CYS   C CA  1 
ATOM   1482 C  C   . CYS   B 1 52  ? 6.012  -33.244 7.005  1.00 14.12 ? 58  CYS   C C   1 
ATOM   1483 O  O   . CYS   B 1 52  ? 6.438  -32.086 7.185  1.00 13.81 ? 58  CYS   C O   1 
ATOM   1484 C  CB  . CYS   B 1 52  ? 7.844  -34.872 6.726  1.00 14.47 ? 58  CYS   C CB  1 
ATOM   1485 S  SG  . CYS   B 1 52  ? 8.365  -36.386 5.898  1.00 16.42 ? 58  CYS   C SG  1 
ATOM   1486 N  N   . GLN   B 1 53  ? 5.013  -33.789 7.679  1.00 13.34 ? 59  GLN   C N   1 
ATOM   1487 C  CA  . GLN   B 1 53  ? 4.325  -33.122 8.778  1.00 13.81 ? 59  GLN   C CA  1 
ATOM   1488 C  C   . GLN   B 1 53  ? 4.306  -33.986 10.044 1.00 14.81 ? 59  GLN   C C   1 
ATOM   1489 O  O   . GLN   B 1 53  ? 3.510  -33.739 10.955 1.00 14.71 ? 59  GLN   C O   1 
ATOM   1490 C  CB  . GLN   B 1 53  ? 2.890  -32.698 8.408  1.00 15.06 ? 59  GLN   C CB  1 
ATOM   1491 C  CG  . GLN   B 1 53  ? 2.869  -31.377 7.595  1.00 15.74 ? 59  GLN   C CG  1 
ATOM   1492 C  CD  . GLN   B 1 53  ? 1.442  -31.025 7.277  1.00 18.80 ? 59  GLN   C CD  1 
ATOM   1493 O  OE1 . GLN   B 1 53  ? 0.967  -31.255 6.120  1.00 18.70 ? 59  GLN   C OE1 1 
ATOM   1494 N  NE2 . GLN   B 1 53  ? 0.738  -30.517 8.302  1.00 16.12 ? 59  GLN   C NE2 1 
ATOM   1495 N  N   . THR   B 1 54  ? 5.155  -35.034 10.097 1.00 14.84 ? 60  THR   C N   1 
ATOM   1496 C  CA  . THR   B 1 54  ? 5.327  -35.816 11.322 1.00 15.42 ? 60  THR   C CA  1 
ATOM   1497 C  C   . THR   B 1 54  ? 6.838  -36.006 11.521 1.00 15.17 ? 60  THR   C C   1 
ATOM   1498 O  O   . THR   B 1 54  ? 7.607  -36.122 10.548 1.00 15.86 ? 60  THR   C O   1 
ATOM   1499 C  CB  . THR   B 1 54  ? 4.622  -37.179 11.282 1.00 21.21 ? 60  THR   C CB  1 
ATOM   1500 O  OG1 . THR   B 1 54  ? 5.233  -37.975 10.260 1.00 24.52 ? 60  THR   C OG1 1 
ATOM   1501 C  CG2 . THR   B 1 54  ? 3.137  -37.077 10.972 1.00 23.41 ? 60  THR   C CG2 1 
ATOM   1502 N  N   . GLY   B 1 55  ? 7.251  -36.040 12.791 1.00 14.18 ? 61  GLY   C N   1 
ATOM   1503 C  CA  . GLY   B 1 55  ? 8.680  -36.177 13.097 1.00 14.13 ? 61  GLY   C CA  1 
ATOM   1504 C  C   . GLY   B 1 55  ? 8.900  -36.304 14.598 1.00 12.63 ? 61  GLY   C C   1 
ATOM   1505 O  O   . GLY   B 1 55  ? 7.949  -36.583 15.330 1.00 14.70 ? 61  GLY   C O   1 
ATOM   1506 N  N   . VAL   B 1 56  ? 10.139 -36.186 15.025 1.00 12.32 ? 62  VAL   C N   1 
ATOM   1507 C  CA  . VAL   B 1 56  ? 10.510 -36.351 16.436 1.00 13.05 ? 62  VAL   C CA  1 
ATOM   1508 C  C   . VAL   B 1 56  ? 11.422 -35.170 16.798 1.00 13.46 ? 62  VAL   C C   1 
ATOM   1509 O  O   . VAL   B 1 56  ? 12.378 -34.894 16.044 1.00 14.02 ? 62  VAL   C O   1 
ATOM   1510 C  CB  . VAL   B 1 56  ? 11.292 -37.676 16.645 1.00 14.20 ? 62  VAL   C CB  1 
ATOM   1511 C  CG1 . VAL   B 1 56  ? 11.840 -37.776 18.097 1.00 15.95 ? 62  VAL   C CG1 1 
ATOM   1512 C  CG2 . VAL   B 1 56  ? 10.417 -38.874 16.324 1.00 15.01 ? 62  VAL   C CG2 1 
ATOM   1513 N  N   . TYR   B 1 57  ? 11.177 -34.496 17.965 1.00 14.61 ? 63  TYR   C N   1 
ATOM   1514 C  CA  . TYR   B 1 57  ? 12.088 -33.425 18.375 1.00 13.81 ? 63  TYR   C CA  1 
ATOM   1515 C  C   . TYR   B 1 57  ? 12.691 -33.690 19.746 1.00 14.04 ? 63  TYR   C C   1 
ATOM   1516 O  O   . TYR   B 1 57  ? 12.125 -34.435 20.538 1.00 14.18 ? 63  TYR   C O   1 
ATOM   1517 C  CB  . TYR   B 1 57  ? 11.400 -32.012 18.392 1.00 14.11 ? 63  TYR   C CB  1 
ATOM   1518 C  CG  . TYR   B 1 57  ? 10.459 -31.770 19.559 1.00 15.28 ? 63  TYR   C CG  1 
ATOM   1519 C  CD1 . TYR   B 1 57  ? 9.209  -32.365 19.601 1.00 15.71 ? 63  TYR   C CD1 1 
ATOM   1520 C  CD2 . TYR   B 1 57  ? 10.808 -30.911 20.598 1.00 15.11 ? 63  TYR   C CD2 1 
ATOM   1521 C  CE1 . TYR   B 1 57  ? 8.305  -32.080 20.620 1.00 17.28 ? 63  TYR   C CE1 1 
ATOM   1522 C  CE2 . TYR   B 1 57  ? 9.925  -30.645 21.641 1.00 16.22 ? 63  TYR   C CE2 1 
ATOM   1523 C  CZ  . TYR   B 1 57  ? 8.688  -31.256 21.666 1.00 17.82 ? 63  TYR   C CZ  1 
ATOM   1524 O  OH  . TYR   B 1 57  ? 7.794  -30.969 22.679 1.00 18.68 ? 63  TYR   C OH  1 
ATOM   1525 N  N   . TYR   B 1 58  ? 13.845 -33.079 20.000 1.00 13.84 ? 64  TYR   C N   1 
ATOM   1526 C  CA  . TYR   B 1 58  ? 14.491 -33.198 21.285 1.00 13.95 ? 64  TYR   C CA  1 
ATOM   1527 C  C   . TYR   B 1 58  ? 14.040 -32.048 22.176 1.00 14.51 ? 64  TYR   C C   1 
ATOM   1528 O  O   . TYR   B 1 58  ? 14.179 -30.882 21.806 1.00 13.98 ? 64  TYR   C O   1 
ATOM   1529 C  CB  . TYR   B 1 58  ? 16.023 -33.206 21.145 1.00 15.07 ? 64  TYR   C CB  1 
ATOM   1530 C  CG  . TYR   B 1 58  ? 16.663 -33.358 22.511 1.00 16.64 ? 64  TYR   C CG  1 
ATOM   1531 C  CD1 . TYR   B 1 58  ? 16.540 -34.543 23.228 1.00 17.45 ? 64  TYR   C CD1 1 
ATOM   1532 C  CD2 . TYR   B 1 58  ? 17.363 -32.311 23.092 1.00 18.62 ? 64  TYR   C CD2 1 
ATOM   1533 C  CE1 . TYR   B 1 58  ? 17.105 -34.688 24.501 1.00 18.63 ? 64  TYR   C CE1 1 
ATOM   1534 C  CE2 . TYR   B 1 58  ? 17.923 -32.438 24.360 1.00 19.01 ? 64  TYR   C CE2 1 
ATOM   1535 C  CZ  . TYR   B 1 58  ? 17.784 -33.623 25.060 1.00 20.13 ? 64  TYR   C CZ  1 
ATOM   1536 O  OH  . TYR   B 1 58  ? 18.354 -33.737 26.319 1.00 23.21 ? 64  TYR   C OH  1 
ATOM   1537 N  N   . CYS   B 1 59  ? 13.575 -32.389 23.399 1.00 14.94 ? 65  CYS   C N   1 
ATOM   1538 C  CA  . CYS   B 1 59  ? 13.094 -31.412 24.388 1.00 14.63 ? 65  CYS   C CA  1 
ATOM   1539 C  C   . CYS   B 1 59  ? 14.076 -31.411 25.601 1.00 16.48 ? 65  CYS   C C   1 
ATOM   1540 O  O   . CYS   B 1 59  ? 13.998 -32.306 26.454 1.00 18.14 ? 65  CYS   C O   1 
ATOM   1541 C  CB  . CYS   B 1 59  ? 11.677 -31.780 24.813 1.00 14.81 ? 65  CYS   C CB  1 
ATOM   1542 S  SG  . CYS   B 1 59  ? 11.029 -30.743 26.160 1.00 18.92 ? 65  CYS   C SG  1 
ATOM   1543 N  N   . SER   B 1 60  ? 14.992 -30.417 25.668 1.00 16.46 ? 66  SER   C N   1 
ATOM   1544 C  CA  . SER   B 1 60  ? 15.986 -30.416 26.742 1.00 19.26 ? 66  SER   C CA  1 
ATOM   1545 C  C   . SER   B 1 60  ? 15.390 -30.287 28.121 1.00 19.41 ? 66  SER   C C   1 
ATOM   1546 O  O   . SER   B 1 60  ? 15.909 -30.904 29.060 1.00 19.90 ? 66  SER   C O   1 
ATOM   1547 C  CB  . SER   B 1 60  ? 17.072 -29.369 26.510 1.00 24.34 ? 66  SER   C CB  1 
ATOM   1548 O  OG  . SER   B 1 60  ? 16.524 -28.077 26.498 1.00 32.48 ? 66  SER   C OG  1 
ATOM   1549 N  N   . SER   B 1 61  ? 14.262 -29.567 28.274 1.00 18.43 ? 67  SER   C N   1 
ATOM   1550 C  CA  . SER   B 1 61  ? 13.627 -29.429 29.596 1.00 18.85 ? 67  SER   C CA  1 
ATOM   1551 C  C   . SER   B 1 61  ? 12.978 -30.716 30.129 1.00 18.81 ? 67  SER   C C   1 
ATOM   1552 O  O   . SER   B 1 61  ? 12.558 -30.773 31.310 1.00 18.91 ? 67  SER   C O   1 
ATOM   1553 C  CB  . SER   B 1 61  ? 12.619 -28.286 29.608 1.00 18.72 ? 67  SER   C CB  1 
ATOM   1554 O  OG  . SER   B 1 61  ? 11.551 -28.544 28.722 1.00 19.13 ? 67  SER   C OG  1 
ATOM   1555 N  N   . ARG   B 1 62  ? 12.918 -31.770 29.290 1.00 16.43 ? 68  ARG   C N   1 
ATOM   1556 C  CA  . ARG   B 1 62  ? 12.445 -33.075 29.748 1.00 16.17 ? 68  ARG   C CA  1 
ATOM   1557 C  C   . ARG   B 1 62  ? 13.545 -34.173 29.506 1.00 17.89 ? 68  ARG   C C   1 
ATOM   1558 O  O   . ARG   B 1 62  ? 13.321 -35.335 29.839 1.00 20.32 ? 68  ARG   C O   1 
ATOM   1559 C  CB  . ARG   B 1 62  ? 11.162 -33.473 28.988 1.00 18.38 ? 68  ARG   C CB  1 
ATOM   1560 C  CG  . ARG   B 1 62  ? 9.968  -32.561 29.316 1.00 19.21 ? 68  ARG   C CG  1 
ATOM   1561 C  CD  . ARG   B 1 62  ? 9.422  -32.890 30.698 1.00 21.29 ? 68  ARG   C CD  1 
ATOM   1562 N  NE  . ARG   B 1 62  ? 8.275  -32.055 31.058 1.00 22.85 ? 68  ARG   C NE  1 
ATOM   1563 C  CZ  . ARG   B 1 62  ? 8.363  -30.876 31.657 1.00 26.87 ? 68  ARG   C CZ  1 
ATOM   1564 N  NH1 . ARG   B 1 62  ? 9.553  -30.367 31.974 1.00 27.13 ? 68  ARG   C NH1 1 
ATOM   1565 N  NH2 . ARG   B 1 62  ? 7.260  -30.201 31.968 1.00 27.77 ? 68  ARG   C NH2 1 
ATOM   1566 N  N   . ARG   B 1 63  ? 14.719 -33.802 28.917 1.00 18.13 ? 69  ARG   C N   1 
ATOM   1567 C  CA  . ARG   B 1 63  ? 15.808 -34.721 28.516 1.00 19.77 ? 69  ARG   C CA  1 
ATOM   1568 C  C   . ARG   B 1 63  ? 15.225 -35.876 27.728 1.00 21.10 ? 69  ARG   C C   1 
ATOM   1569 O  O   . ARG   B 1 63  ? 15.535 -37.041 27.989 1.00 23.69 ? 69  ARG   C O   1 
ATOM   1570 C  CB  . ARG   B 1 63  ? 16.640 -35.218 29.733 1.00 23.22 ? 69  ARG   C CB  1 
ATOM   1571 C  CG  . ARG   B 1 63  ? 17.278 -34.130 30.558 1.00 29.67 ? 69  ARG   C CG  1 
ATOM   1572 C  CD  . ARG   B 1 63  ? 18.652 -33.627 30.151 1.00 38.08 ? 69  ARG   C CD  1 
ATOM   1573 N  NE  . ARG   B 1 63  ? 19.056 -32.503 30.999 1.00 44.09 ? 69  ARG   C NE  1 
ATOM   1574 C  CZ  . ARG   B 1 63  ? 18.975 -31.224 30.647 1.00 48.21 ? 69  ARG   C CZ  1 
ATOM   1575 N  NH1 . ARG   B 1 63  ? 18.576 -30.888 29.431 1.00 48.20 ? 69  ARG   C NH1 1 
ATOM   1576 N  NH2 . ARG   B 1 63  ? 19.368 -30.274 31.484 1.00 49.67 ? 69  ARG   C NH2 1 
ATOM   1577 N  N   . LYS   B 1 64  ? 14.282 -35.562 26.802 1.00 19.44 ? 70  LYS   C N   1 
ATOM   1578 C  CA  . LYS   B 1 64  ? 13.573 -36.631 26.096 1.00 19.33 ? 70  LYS   C CA  1 
ATOM   1579 C  C   . LYS   B 1 64  ? 13.221 -36.210 24.690 1.00 17.19 ? 70  LYS   C C   1 
ATOM   1580 O  O   . LYS   B 1 64  ? 13.047 -35.026 24.435 1.00 16.59 ? 70  LYS   C O   1 
ATOM   1581 C  CB  . LYS   B 1 64  ? 12.191 -36.924 26.790 1.00 23.36 ? 70  LYS   C CB  1 
ATOM   1582 C  CG  . LYS   B 1 64  ? 12.250 -37.953 27.915 1.00 34.22 ? 70  LYS   C CG  1 
ATOM   1583 C  CD  . LYS   B 1 64  ? 10.835 -38.272 28.408 1.00 42.94 ? 70  LYS   C CD  1 
ATOM   1584 C  CE  . LYS   B 1 64  ? 10.834 -39.447 29.380 1.00 48.68 ? 70  LYS   C CE  1 
ATOM   1585 N  NZ  . LYS   B 1 64  ? 10.252 -39.086 30.708 1.00 50.62 ? 70  LYS   C NZ  1 
ATOM   1586 N  N   . HIS   B 1 65  ? 13.011 -37.190 23.827 1.00 16.46 ? 71  HIS   C N   1 
ATOM   1587 C  CA  . HIS   B 1 65  ? 12.516 -36.934 22.473 1.00 15.65 ? 71  HIS   C CA  1 
ATOM   1588 C  C   . HIS   B 1 65  ? 11.019 -37.205 22.448 1.00 17.46 ? 71  HIS   C C   1 
ATOM   1589 O  O   . HIS   B 1 65  ? 10.535 -38.161 23.105 1.00 19.63 ? 71  HIS   C O   1 
ATOM   1590 C  CB  . HIS   B 1 65  ? 13.202 -37.869 21.469 1.00 16.36 ? 71  HIS   C CB  1 
ATOM   1591 C  CG  . HIS   B 1 65  ? 14.679 -37.639 21.330 1.00 17.86 ? 71  HIS   C CG  1 
ATOM   1592 N  ND1 . HIS   B 1 65  ? 15.211 -36.883 20.294 1.00 20.30 ? 71  HIS   C ND1 1 
ATOM   1593 C  CD2 . HIS   B 1 65  ? 15.699 -38.135 22.068 1.00 17.79 ? 71  HIS   C CD2 1 
ATOM   1594 C  CE1 . HIS   B 1 65  ? 16.526 -36.926 20.462 1.00 19.58 ? 71  HIS   C CE1 1 
ATOM   1595 N  NE2 . HIS   B 1 65  ? 16.857 -37.643 21.519 1.00 20.31 ? 71  HIS   C NE2 1 
ATOM   1596 N  N   . TYR   B 1 66  ? 10.272 -36.412 21.645 1.00 14.45 ? 72  TYR   C N   1 
ATOM   1597 C  CA  . TYR   B 1 66  ? 8.824  -36.618 21.525 1.00 14.28 ? 72  TYR   C CA  1 
ATOM   1598 C  C   . TYR   B 1 66  ? 8.419  -36.684 20.069 1.00 14.16 ? 72  TYR   C C   1 
ATOM   1599 O  O   . TYR   B 1 66  ? 8.862  -35.850 19.264 1.00 14.92 ? 72  TYR   C O   1 
ATOM   1600 C  CB  . TYR   B 1 66  ? 8.032  -35.439 22.148 1.00 15.03 ? 72  TYR   C CB  1 
ATOM   1601 C  CG  . TYR   B 1 66  ? 8.120  -35.351 23.664 1.00 17.79 ? 72  TYR   C CG  1 
ATOM   1602 C  CD1 . TYR   B 1 66  ? 7.405  -36.228 24.474 1.00 19.13 ? 72  TYR   C CD1 1 
ATOM   1603 C  CD2 . TYR   B 1 66  ? 8.876  -34.361 24.283 1.00 18.86 ? 72  TYR   C CD2 1 
ATOM   1604 C  CE1 . TYR   B 1 66  ? 7.489  -36.151 25.862 1.00 20.71 ? 72  TYR   C CE1 1 
ATOM   1605 C  CE2 . TYR   B 1 66  ? 8.957  -34.275 25.663 1.00 20.32 ? 72  TYR   C CE2 1 
ATOM   1606 C  CZ  . TYR   B 1 66  ? 8.254  -35.163 26.446 1.00 22.52 ? 72  TYR   C CZ  1 
ATOM   1607 O  OH  . TYR   B 1 66  ? 8.326  -35.067 27.821 1.00 24.68 ? 72  TYR   C OH  1 
ATOM   1608 N  N   . PRO   B 1 67  ? 7.571  -37.673 19.717 1.00 14.12 ? 73  PRO   C N   1 
ATOM   1609 C  CA  . PRO   B 1 67  ? 7.028  -37.723 18.357 1.00 14.61 ? 73  PRO   C CA  1 
ATOM   1610 C  C   . PRO   B 1 67  ? 5.887  -36.689 18.242 1.00 15.90 ? 73  PRO   C C   1 
ATOM   1611 O  O   . PRO   B 1 67  ? 5.062  -36.607 19.176 1.00 16.92 ? 73  PRO   C O   1 
ATOM   1612 C  CB  . PRO   B 1 67  ? 6.486  -39.160 18.254 1.00 15.35 ? 73  PRO   C CB  1 
ATOM   1613 C  CG  . PRO   B 1 67  ? 6.156  -39.540 19.644 1.00 16.17 ? 73  PRO   C CG  1 
ATOM   1614 C  CD  . PRO   B 1 67  ? 7.038  -38.762 20.578 1.00 14.26 ? 73  PRO   C CD  1 
ATOM   1615 N  N   . VAL   B 1 68  ? 5.825  -35.926 17.134 1.00 15.11 ? 74  VAL   C N   1 
ATOM   1616 C  CA  . VAL   B 1 68  ? 4.760  -34.915 16.970 1.00 16.15 ? 74  VAL   C CA  1 
ATOM   1617 C  C   . VAL   B 1 68  ? 4.300  -34.796 15.525 1.00 15.83 ? 74  VAL   C C   1 
ATOM   1618 O  O   . VAL   B 1 68  ? 5.064  -35.094 14.624 1.00 16.45 ? 74  VAL   C O   1 
ATOM   1619 C  CB  . VAL   B 1 68  ? 5.193  -33.498 17.428 1.00 18.50 ? 74  VAL   C CB  1 
ATOM   1620 C  CG1 . VAL   B 1 68  ? 5.351  -33.415 18.955 1.00 19.78 ? 74  VAL   C CG1 1 
ATOM   1621 C  CG2 . VAL   B 1 68  ? 6.447  -33.008 16.691 1.00 19.46 ? 74  VAL   C CG2 1 
ATOM   1622 N  N   . SER   B 1 69  ? 3.069  -34.300 15.320 1.00 15.09 ? 75  SER   C N   1 
ATOM   1623 C  CA  . SER   B 1 69  ? 2.613  -33.827 14.013 1.00 15.61 ? 75  SER   C CA  1 
ATOM   1624 C  C   . SER   B 1 69  ? 2.886  -32.293 14.048 1.00 15.13 ? 75  SER   C C   1 
ATOM   1625 O  O   . SER   B 1 69  ? 2.778  -31.662 15.119 1.00 16.20 ? 75  SER   C O   1 
ATOM   1626 C  CB  . SER   B 1 69  ? 1.094  -34.028 13.869 1.00 19.12 ? 75  SER   C CB  1 
ATOM   1627 O  OG  . SER   B 1 69  ? 0.797  -35.409 13.763 1.00 23.90 ? 75  SER   C OG  1 
ATOM   1628 N  N   . PHE   B 1 70  ? 3.222  -31.677 12.901 1.00 13.68 ? 76  PHE   C N   1 
ATOM   1629 C  CA  . PHE   B 1 70  ? 3.498  -30.229 12.881 1.00 14.13 ? 76  PHE   C CA  1 
ATOM   1630 C  C   . PHE   B 1 70  ? 2.911  -29.590 11.629 1.00 13.71 ? 76  PHE   C C   1 
ATOM   1631 O  O   . PHE   B 1 70  ? 2.671  -30.273 10.640 1.00 14.94 ? 76  PHE   C O   1 
ATOM   1632 C  CB  . PHE   B 1 70  ? 4.996  -29.905 13.053 1.00 14.22 ? 76  PHE   C CB  1 
ATOM   1633 C  CG  . PHE   B 1 70  ? 5.921  -30.655 12.114 1.00 13.42 ? 76  PHE   C CG  1 
ATOM   1634 C  CD1 . PHE   B 1 70  ? 6.415  -31.899 12.447 1.00 13.65 ? 76  PHE   C CD1 1 
ATOM   1635 C  CD2 . PHE   B 1 70  ? 6.318  -30.089 10.913 1.00 14.31 ? 76  PHE   C CD2 1 
ATOM   1636 C  CE1 . PHE   B 1 70  ? 7.306  -32.580 11.585 1.00 13.57 ? 76  PHE   C CE1 1 
ATOM   1637 C  CE2 . PHE   B 1 70  ? 7.196  -30.747 10.058 1.00 13.83 ? 76  PHE   C CE2 1 
ATOM   1638 C  CZ  . PHE   B 1 70  ? 7.688  -31.995 10.389 1.00 13.70 ? 76  PHE   C CZ  1 
ATOM   1639 N  N   . SER   B 1 71  ? 2.678  -28.286 11.676 1.00 13.13 ? 77  SER   C N   1 
ATOM   1640 C  CA  . SER   B 1 71  ? 2.016  -27.595 10.571 1.00 14.13 ? 77  SER   C CA  1 
ATOM   1641 C  C   . SER   B 1 71  ? 2.985  -27.289 9.427  1.00 15.74 ? 77  SER   C C   1 
ATOM   1642 O  O   . SER   B 1 71  ? 4.162  -27.666 9.466  1.00 16.59 ? 77  SER   C O   1 
ATOM   1643 C  CB  . SER   B 1 71  ? 1.418  -26.296 11.116 1.00 14.63 ? 77  SER   C CB  1 
ATOM   1644 O  OG  . SER   B 1 71  ? 2.429  -25.366 11.499 1.00 16.85 ? 77  SER   C OG  1 
ATOM   1645 N  N   . LYS   B 1 72  ? 2.455  -26.697 8.336  1.00 14.97 ? 78  LYS   C N   1 
ATOM   1646 C  CA  . LYS   B 1 72  ? 3.325  -26.288 7.247  1.00 16.51 ? 78  LYS   C CA  1 
ATOM   1647 C  C   . LYS   B 1 72  ? 4.017  -24.951 7.610  1.00 17.13 ? 78  LYS   C C   1 
ATOM   1648 O  O   . LYS   B 1 72  ? 3.437  -24.130 8.343  1.00 19.04 ? 78  LYS   C O   1 
ATOM   1649 C  CB  . LYS   B 1 72  ? 2.466  -26.104 5.998  1.00 18.71 ? 78  LYS   C CB  1 
ATOM   1650 C  CG  . LYS   B 1 72  ? 1.829  -27.431 5.591  1.00 22.20 ? 78  LYS   C CG  1 
ATOM   1651 C  CD  . LYS   B 1 72  ? 1.120  -27.249 4.239  1.00 28.97 ? 78  LYS   C CD  1 
ATOM   1652 C  CE  . LYS   B 1 72  ? 0.425  -28.500 3.789  1.00 36.39 ? 78  LYS   C CE  1 
ATOM   1653 N  NZ  . LYS   B 1 72  ? -0.414 -28.209 2.602  1.00 41.15 ? 78  LYS   C NZ  1 
ATOM   1654 N  N   . PRO   B 1 73  ? 5.218  -24.667 7.062  1.00 16.89 ? 79  PRO   C N   1 
ATOM   1655 C  CA  . PRO   B 1 73  ? 5.895  -23.394 7.392  1.00 17.71 ? 79  PRO   C CA  1 
ATOM   1656 C  C   . PRO   B 1 73  ? 5.046  -22.182 7.047  1.00 19.13 ? 79  PRO   C C   1 
ATOM   1657 O  O   . PRO   B 1 73  ? 4.490  -22.092 5.939  1.00 20.31 ? 79  PRO   C O   1 
ATOM   1658 C  CB  . PRO   B 1 73  ? 7.175  -23.403 6.551  1.00 19.29 ? 79  PRO   C CB  1 
ATOM   1659 C  CG  . PRO   B 1 73  ? 7.379  -24.827 6.142  1.00 20.05 ? 79  PRO   C CG  1 
ATOM   1660 C  CD  . PRO   B 1 73  ? 6.026  -25.520 6.169  1.00 17.48 ? 79  PRO   C CD  1 
ATOM   1661 N  N   . SER   B 1 74  ? 4.929  -21.260 8.003  1.00 18.72 ? 80  SER   C N   1 
ATOM   1662 C  CA  . SER   B 1 74  ? 4.069  -20.100 7.788  1.00 20.13 ? 80  SER   C CA  1 
ATOM   1663 C  C   . SER   B 1 74  ? 4.432  -18.919 8.663  1.00 19.14 ? 80  SER   C C   1 
ATOM   1664 O  O   . SER   B 1 74  ? 5.394  -18.985 9.434  1.00 17.44 ? 80  SER   C O   1 
ATOM   1665 C  CB  . SER   B 1 74  ? 2.618  -20.508 8.011  1.00 24.43 ? 80  SER   C CB  1 
ATOM   1666 O  OG  . SER   B 1 74  ? 2.382  -20.767 9.389  1.00 27.89 ? 80  SER   C OG  1 
ATOM   1667 N  N   . LEU   B 1 75  ? 3.721  -17.785 8.465  1.00 18.65 ? 81  LEU   C N   1 
ATOM   1668 C  CA  . LEU   B 1 75  ? 3.944  -16.545 9.199  1.00 19.62 ? 81  LEU   C CA  1 
ATOM   1669 C  C   . LEU   B 1 75  ? 3.088  -16.596 10.451 1.00 20.44 ? 81  LEU   C C   1 
ATOM   1670 O  O   . LEU   B 1 75  ? 1.839  -16.656 10.340 1.00 22.05 ? 81  LEU   C O   1 
ATOM   1671 C  CB  . LEU   B 1 75  ? 3.407  -15.395 8.329  1.00 21.25 ? 81  LEU   C CB  1 
ATOM   1672 C  CG  . LEU   B 1 75  ? 4.404  -14.637 7.503  1.00 25.71 ? 81  LEU   C CG  1 
ATOM   1673 C  CD1 . LEU   B 1 75  ? 3.659  -13.573 6.638  1.00 28.61 ? 81  LEU   C CD1 1 
ATOM   1674 C  CD2 . LEU   B 1 75  ? 5.459  -13.957 8.388  1.00 26.44 ? 81  LEU   C CD2 1 
ATOM   1675 N  N   . ILE   B 1 76  ? 3.711  -16.527 11.637 1.00 18.66 ? 82  ILE   C N   1 
ATOM   1676 C  CA  . ILE   B 1 76  ? 3.027  -16.654 12.923 1.00 20.15 ? 82  ILE   C CA  1 
ATOM   1677 C  C   . ILE   B 1 76  ? 3.419  -15.536 13.879 1.00 20.80 ? 82  ILE   C C   1 
ATOM   1678 O  O   . ILE   B 1 76  ? 4.597  -15.232 13.991 1.00 19.02 ? 82  ILE   C O   1 
ATOM   1679 C  CB  . ILE   B 1 76  ? 3.392  -18.045 13.496 1.00 23.32 ? 82  ILE   C CB  1 
ATOM   1680 C  CG1 . ILE   B 1 76  ? 2.848  -19.161 12.545 1.00 26.43 ? 82  ILE   C CG1 1 
ATOM   1681 C  CG2 . ILE   B 1 76  ? 2.932  -18.208 14.970 1.00 24.96 ? 82  ILE   C CG2 1 
ATOM   1682 C  CD1 . ILE   B 1 76  ? 3.103  -20.530 12.913 1.00 30.02 ? 82  ILE   C CD1 1 
ATOM   1683 N  N   . PHE   B 1 77  ? 2.436  -14.897 14.548 1.00 21.39 ? 83  PHE   C N   1 
ATOM   1684 C  CA  . PHE   B 1 77  ? 2.734  -13.808 15.472 1.00 22.32 ? 83  PHE   C CA  1 
ATOM   1685 C  C   . PHE   B 1 77  ? 3.482  -14.314 16.714 1.00 22.00 ? 83  PHE   C C   1 
ATOM   1686 O  O   . PHE   B 1 77  ? 3.095  -15.320 17.318 1.00 22.14 ? 83  PHE   C O   1 
ATOM   1687 C  CB  . PHE   B 1 77  ? 1.431  -13.085 15.907 1.00 23.69 ? 83  PHE   C CB  1 
ATOM   1688 C  CG  . PHE   B 1 77  ? 1.683  -11.889 16.801 1.00 25.47 ? 83  PHE   C CG  1 
ATOM   1689 C  CD1 . PHE   B 1 77  ? 1.504  -11.977 18.165 1.00 27.66 ? 83  PHE   C CD1 1 
ATOM   1690 C  CD2 . PHE   B 1 77  ? 2.171  -10.704 16.283 1.00 27.61 ? 83  PHE   C CD2 1 
ATOM   1691 C  CE1 . PHE   B 1 77  ? 1.754  -10.881 18.990 1.00 28.79 ? 83  PHE   C CE1 1 
ATOM   1692 C  CE2 . PHE   B 1 77  ? 2.440  -9.610  17.117 1.00 29.21 ? 83  PHE   C CE2 1 
ATOM   1693 C  CZ  . PHE   B 1 77  ? 2.224  -9.711  18.462 1.00 29.08 ? 83  PHE   C CZ  1 
ATOM   1694 N  N   . VAL   B 1 78  ? 4.575  -13.621 17.085 1.00 21.57 ? 84  VAL   C N   1 
ATOM   1695 C  CA  . VAL   B 1 78  ? 5.378  -13.964 18.270 1.00 20.17 ? 84  VAL   C CA  1 
ATOM   1696 C  C   . VAL   B 1 78  ? 5.495  -12.714 19.144 1.00 21.27 ? 84  VAL   C C   1 
ATOM   1697 O  O   . VAL   B 1 78  ? 5.914  -11.660 18.666 1.00 20.50 ? 84  VAL   C O   1 
ATOM   1698 C  CB  . VAL   B 1 78  ? 6.789  -14.475 17.861 1.00 19.61 ? 84  VAL   C CB  1 
ATOM   1699 C  CG1 . VAL   B 1 78  ? 7.597  -14.895 19.103 1.00 19.00 ? 84  VAL   C CG1 1 
ATOM   1700 C  CG2 . VAL   B 1 78  ? 6.669  -15.658 16.898 1.00 18.99 ? 84  VAL   C CG2 1 
ATOM   1701 N  N   . GLU   B 1 79  ? 5.186  -12.846 20.440 1.00 23.08 ? 85  GLU   C N   1 
ATOM   1702 C  CA  . GLU   B 1 79  ? 5.244  -11.749 21.411 1.00 24.51 ? 85  GLU   C CA  1 
ATOM   1703 C  C   . GLU   B 1 79  ? 6.661  -11.191 21.553 1.00 23.23 ? 85  GLU   C C   1 
ATOM   1704 O  O   . GLU   B 1 79  ? 7.627  -11.929 21.324 1.00 22.92 ? 85  GLU   C O   1 
ATOM   1705 C  CB  . GLU   B 1 79  ? 4.828  -12.284 22.791 1.00 29.16 ? 85  GLU   C CB  1 
ATOM   1706 C  CG  . GLU   B 1 79  ? 3.476  -12.967 22.825 1.00 37.71 ? 85  GLU   C CG  1 
ATOM   1707 C  CD  . GLU   B 1 79  ? 2.285  -12.031 22.868 1.00 46.70 ? 85  GLU   C CD  1 
ATOM   1708 O  OE1 . GLU   B 1 79  ? 1.143  -12.545 22.900 1.00 48.93 ? 85  GLU   C OE1 1 
ATOM   1709 O  OE2 . GLU   B 1 79  ? 2.483  -10.794 22.850 1.00 47.74 ? 85  GLU   C OE2 1 
ATOM   1710 N  N   . ALA   B 1 80  ? 6.790  -9.932  22.000 1.00 22.21 ? 86  ALA   C N   1 
ATOM   1711 C  CA  . ALA   B 1 80  ? 8.099  -9.314  22.217 1.00 21.52 ? 86  ALA   C CA  1 
ATOM   1712 C  C   . ALA   B 1 80  ? 8.859  -10.092 23.294 1.00 20.95 ? 86  ALA   C C   1 
ATOM   1713 O  O   . ALA   B 1 80  ? 8.271  -10.675 24.215 1.00 21.06 ? 86  ALA   C O   1 
ATOM   1714 C  CB  . ALA   B 1 80  ? 7.939  -7.855  22.687 1.00 21.36 ? 86  ALA   C CB  1 
ATOM   1715 N  N   . SER   B 1 81  ? 10.175 -10.111 23.155 1.00 19.37 ? 87  SER   C N   1 
ATOM   1716 C  CA  . SER   B 1 81  ? 11.075 -10.711 24.129 1.00 18.57 ? 87  SER   C CA  1 
ATOM   1717 C  C   . SER   B 1 81  ? 12.267 -9.727  24.239 1.00 20.64 ? 87  SER   C C   1 
ATOM   1718 O  O   . SER   B 1 81  ? 12.276 -8.677  23.550 1.00 22.03 ? 87  SER   C O   1 
ATOM   1719 C  CB  . SER   B 1 81  ? 11.560 -12.092 23.647 1.00 17.97 ? 87  SER   C CB  1 
ATOM   1720 O  OG  . SER   B 1 81  ? 12.311 -11.964 22.450 1.00 19.11 ? 87  SER   C OG  1 
ATOM   1721 N  N   . GLU   B 1 82  ? 13.249 -10.032 25.087 1.00 21.01 ? 88  GLU   C N   1 
ATOM   1722 C  CA  . GLU   B 1 82  ? 14.444 -9.170  25.125 1.00 22.33 ? 88  GLU   C CA  1 
ATOM   1723 C  C   . GLU   B 1 82  ? 15.263 -9.281  23.801 1.00 22.65 ? 88  GLU   C C   1 
ATOM   1724 O  O   . GLU   B 1 82  ? 16.034 -8.362  23.480 1.00 22.93 ? 88  GLU   C O   1 
ATOM   1725 C  CB  . GLU   B 1 82  ? 15.295 -9.451  26.364 1.00 26.48 ? 88  GLU   C CB  1 
ATOM   1726 C  CG  . GLU   B 1 82  ? 15.889 -10.842 26.372 1.00 34.54 ? 88  GLU   C CG  1 
ATOM   1727 C  CD  . GLU   B 1 82  ? 16.125 -11.364 27.781 1.00 48.88 ? 88  GLU   C CD  1 
ATOM   1728 O  OE1 . GLU   B 1 82  ? 16.731 -10.619 28.590 1.00 52.78 ? 88  GLU   C OE1 1 
ATOM   1729 O  OE2 . GLU   B 1 82  ? 15.713 -12.513 28.075 1.00 52.24 ? 88  GLU   C OE2 1 
ATOM   1730 N  N   . TYR   B 1 83  ? 14.985 -10.319 22.974 1.00 21.60 ? 89  TYR   C N   1 
ATOM   1731 C  CA  . TYR   B 1 83  ? 15.693 -10.569 21.736 1.00 21.67 ? 89  TYR   C CA  1 
ATOM   1732 C  C   . TYR   B 1 83  ? 15.061 -9.930  20.499 1.00 22.14 ? 89  TYR   C C   1 
ATOM   1733 O  O   . TYR   B 1 83  ? 15.780 -9.684  19.527 1.00 23.91 ? 89  TYR   C O   1 
ATOM   1734 C  CB  . TYR   B 1 83  ? 15.779 -12.091 21.511 1.00 20.72 ? 89  TYR   C CB  1 
ATOM   1735 C  CG  . TYR   B 1 83  ? 16.426 -12.809 22.662 1.00 21.51 ? 89  TYR   C CG  1 
ATOM   1736 C  CD1 . TYR   B 1 83  ? 17.802 -12.752 22.859 1.00 23.02 ? 89  TYR   C CD1 1 
ATOM   1737 C  CD2 . TYR   B 1 83  ? 15.675 -13.573 23.536 1.00 22.35 ? 89  TYR   C CD2 1 
ATOM   1738 C  CE1 . TYR   B 1 83  ? 18.406 -13.416 23.919 1.00 24.52 ? 89  TYR   C CE1 1 
ATOM   1739 C  CE2 . TYR   B 1 83  ? 16.273 -14.274 24.581 1.00 24.71 ? 89  TYR   C CE2 1 
ATOM   1740 C  CZ  . TYR   B 1 83  ? 17.645 -14.202 24.762 1.00 26.28 ? 89  TYR   C CZ  1 
ATOM   1741 O  OH  . TYR   B 1 83  ? 18.246 -14.888 25.800 1.00 29.74 ? 89  TYR   C OH  1 
ATOM   1742 N  N   . TYR   B 1 84  ? 13.737 -9.723  20.492 1.00 20.19 ? 90  TYR   C N   1 
ATOM   1743 C  CA  . TYR   B 1 84  ? 13.053 -9.234  19.300 1.00 20.03 ? 90  TYR   C CA  1 
ATOM   1744 C  C   . TYR   B 1 84  ? 11.888 -8.382  19.688 1.00 21.69 ? 90  TYR   C C   1 
ATOM   1745 O  O   . TYR   B 1 84  ? 11.194 -8.686  20.674 1.00 21.40 ? 90  TYR   C O   1 
ATOM   1746 C  CB  . TYR   B 1 84  ? 12.432 -10.403 18.476 1.00 18.69 ? 90  TYR   C CB  1 
ATOM   1747 C  CG  . TYR   B 1 84  ? 13.423 -11.334 17.846 1.00 17.87 ? 90  TYR   C CG  1 
ATOM   1748 C  CD1 . TYR   B 1 84  ? 13.611 -12.615 18.342 1.00 17.65 ? 90  TYR   C CD1 1 
ATOM   1749 C  CD2 . TYR   B 1 84  ? 14.147 -10.953 16.726 1.00 17.03 ? 90  TYR   C CD2 1 
ATOM   1750 C  CE1 . TYR   B 1 84  ? 14.514 -13.480 17.768 1.00 17.20 ? 90  TYR   C CE1 1 
ATOM   1751 C  CE2 . TYR   B 1 84  ? 15.040 -11.822 16.127 1.00 16.35 ? 90  TYR   C CE2 1 
ATOM   1752 C  CZ  . TYR   B 1 84  ? 15.215 -13.087 16.647 1.00 16.77 ? 90  TYR   C CZ  1 
ATOM   1753 O  OH  . TYR   B 1 84  ? 16.135 -13.920 16.080 1.00 16.60 ? 90  TYR   C OH  1 
ATOM   1754 N  N   . PRO   B 1 85  ? 11.520 -7.413  18.838 1.00 22.74 ? 91  PRO   C N   1 
ATOM   1755 C  CA  . PRO   B 1 85  ? 10.249 -6.752  19.055 1.00 22.37 ? 91  PRO   C CA  1 
ATOM   1756 C  C   . PRO   B 1 85  ? 9.087  -7.737  18.775 1.00 22.54 ? 91  PRO   C C   1 
ATOM   1757 O  O   . PRO   B 1 85  ? 9.277  -8.757  18.112 1.00 22.05 ? 91  PRO   C O   1 
ATOM   1758 C  CB  . PRO   B 1 85  ? 10.259 -5.634  17.992 1.00 23.53 ? 91  PRO   C CB  1 
ATOM   1759 C  CG  . PRO   B 1 85  ? 11.114 -6.159  16.927 1.00 24.13 ? 91  PRO   C CG  1 
ATOM   1760 C  CD  . PRO   B 1 85  ? 12.163 -6.992  17.575 1.00 22.35 ? 91  PRO   C CD  1 
ATOM   1761 N  N   . ALA   B 1 86  ? 7.851  -7.396  19.150 1.00 22.83 ? 92  ALA   C N   1 
ATOM   1762 C  CA  . ALA   B 1 86  ? 6.659  -8.178  18.782 1.00 23.61 ? 92  ALA   C CA  1 
ATOM   1763 C  C   . ALA   B 1 86  ? 6.592  -8.160  17.224 1.00 23.29 ? 92  ALA   C C   1 
ATOM   1764 O  O   . ALA   B 1 86  ? 6.912  -7.109  16.630 1.00 23.03 ? 92  ALA   C O   1 
ATOM   1765 C  CB  . ALA   B 1 86  ? 5.395  -7.523  19.359 1.00 23.94 ? 92  ALA   C CB  1 
ATOM   1766 N  N   . ARG   B 1 87  ? 6.384  -9.332  16.579 1.00 22.38 ? 93  ARG   C N   1 
ATOM   1767 C  CA  . ARG   B 1 87  ? 6.485  -9.374  15.116 1.00 21.54 ? 93  ARG   C CA  1 
ATOM   1768 C  C   . ARG   B 1 87  ? 5.919  -10.693 14.571 1.00 21.42 ? 93  ARG   C C   1 
ATOM   1769 O  O   . ARG   B 1 87  ? 5.635  -11.616 15.338 1.00 21.78 ? 93  ARG   C O   1 
ATOM   1770 C  CB  . ARG   B 1 87  ? 7.991  -9.297  14.731 1.00 21.77 ? 93  ARG   C CB  1 
ATOM   1771 C  CG  . ARG   B 1 87  ? 8.752  -10.632 15.092 1.00 18.15 ? 93  ARG   C CG  1 
ATOM   1772 C  CD  . ARG   B 1 87  ? 10.249 -10.476 15.250 1.00 19.23 ? 93  ARG   C CD  1 
ATOM   1773 N  NE  . ARG   B 1 87  ? 11.041 -11.617 14.785 1.00 18.46 ? 93  ARG   C NE  1 
ATOM   1774 C  CZ  . ARG   B 1 87  ? 11.122 -12.792 15.407 1.00 20.54 ? 93  ARG   C CZ  1 
ATOM   1775 N  NH1 . ARG   B 1 87  ? 11.892 -13.754 14.919 1.00 17.90 ? 93  ARG   C NH1 1 
ATOM   1776 N  NH2 . ARG   B 1 87  ? 10.396 -13.029 16.500 1.00 20.14 ? 93  ARG   C NH2 1 
ATOM   1777 N  N   . TYR   B 1 88  ? 5.828  -10.813 13.236 1.00 20.95 ? 94  TYR   C N   1 
ATOM   1778 C  CA  . TYR   B 1 88  ? 5.473  -12.096 12.631 1.00 21.37 ? 94  TYR   C CA  1 
ATOM   1779 C  C   . TYR   B 1 88  ? 6.778  -12.802 12.282 1.00 19.00 ? 94  TYR   C C   1 
ATOM   1780 O  O   . TYR   B 1 88  ? 7.639  -12.212 11.617 1.00 19.26 ? 94  TYR   C O   1 
ATOM   1781 C  CB  . TYR   B 1 88  ? 4.669  -11.912 11.336 1.00 23.40 ? 94  TYR   C CB  1 
ATOM   1782 C  CG  . TYR   B 1 88  ? 3.271  -11.446 11.625 1.00 26.82 ? 94  TYR   C CG  1 
ATOM   1783 C  CD1 . TYR   B 1 88  ? 2.239  -12.354 11.794 1.00 28.97 ? 94  TYR   C CD1 1 
ATOM   1784 C  CD2 . TYR   B 1 88  ? 2.994  -10.101 11.809 1.00 29.87 ? 94  TYR   C CD2 1 
ATOM   1785 C  CE1 . TYR   B 1 88  ? 0.947  -11.929 12.090 1.00 31.86 ? 94  TYR   C CE1 1 
ATOM   1786 C  CE2 . TYR   B 1 88  ? 1.709  -9.666  12.121 1.00 31.96 ? 94  TYR   C CE2 1 
ATOM   1787 C  CZ  . TYR   B 1 88  ? 0.696  -10.587 12.278 1.00 33.79 ? 94  TYR   C CZ  1 
ATOM   1788 O  OH  . TYR   B 1 88  ? -0.575 -10.168 12.587 1.00 38.21 ? 94  TYR   C OH  1 
ATOM   1789 N  N   . GLN   B 1 89  ? 6.936  -14.036 12.759 1.00 15.91 ? 95  GLN   C N   1 
ATOM   1790 C  CA  . GLN   B 1 89  ? 8.112  -14.824 12.397 1.00 14.94 ? 95  GLN   C CA  1 
ATOM   1791 C  C   . GLN   B 1 89  ? 7.692  -15.717 11.222 1.00 16.14 ? 95  GLN   C C   1 
ATOM   1792 O  O   . GLN   B 1 89  ? 6.640  -16.382 11.283 1.00 17.81 ? 95  GLN   C O   1 
ATOM   1793 C  CB  . GLN   B 1 89  ? 8.579  -15.660 13.605 1.00 15.19 ? 95  GLN   C CB  1 
ATOM   1794 C  CG  . GLN   B 1 89  ? 9.737  -16.620 13.217 1.00 14.74 ? 95  GLN   C CG  1 
ATOM   1795 C  CD  . GLN   B 1 89  ? 10.507 -17.100 14.429 1.00 16.04 ? 95  GLN   C CD  1 
ATOM   1796 O  OE1 . GLN   B 1 89  ? 10.694 -16.366 15.409 1.00 16.72 ? 95  GLN   C OE1 1 
ATOM   1797 N  NE2 . GLN   B 1 89  ? 10.946 -18.371 14.372 1.00 14.49 ? 95  GLN   C NE2 1 
ATOM   1798 N  N   . SER   B 1 90  ? 8.517  -15.756 10.169 1.00 15.29 ? 96  SER   C N   1 
ATOM   1799 C  CA  . SER   B 1 90  ? 8.212  -16.524 8.961  1.00 14.57 ? 96  SER   C CA  1 
ATOM   1800 C  C   . SER   B 1 90  ? 8.854  -17.921 9.004  1.00 15.12 ? 96  SER   C C   1 
ATOM   1801 O  O   . SER   B 1 90  ? 9.746  -18.179 9.847  1.00 15.83 ? 96  SER   C O   1 
ATOM   1802 C  CB  . SER   B 1 90  ? 8.671  -15.768 7.706  1.00 17.42 ? 96  SER   C CB  1 
ATOM   1803 O  OG  . SER   B 1 90  ? 10.077 -15.573 7.750  1.00 19.37 ? 96  SER   C OG  1 
ATOM   1804 N  N   . HIS   B 1 91  ? 8.342  -18.834 8.127  1.00 15.07 ? 97  HIS   C N   1 
ATOM   1805 C  CA  . HIS   B 1 91  ? 8.876  -20.192 7.972  1.00 14.83 ? 97  HIS   C CA  1 
ATOM   1806 C  C   . HIS   B 1 91  ? 8.811  -20.959 9.309  1.00 15.82 ? 97  HIS   C C   1 
ATOM   1807 O  O   . HIS   B 1 91  ? 9.666  -21.811 9.555  1.00 16.40 ? 97  HIS   C O   1 
ATOM   1808 C  CB  . HIS   B 1 91  ? 10.329 -20.139 7.449  1.00 15.21 ? 97  HIS   C CB  1 
ATOM   1809 C  CG  . HIS   B 1 91  ? 10.418 -19.521 6.078  1.00 16.90 ? 97  HIS   C CG  1 
ATOM   1810 N  ND1 . HIS   B 1 91  ? 10.381 -20.302 4.922  1.00 20.32 ? 97  HIS   C ND1 1 
ATOM   1811 C  CD2 . HIS   B 1 91  ? 10.495 -18.213 5.719  1.00 19.31 ? 97  HIS   C CD2 1 
ATOM   1812 C  CE1 . HIS   B 1 91  ? 10.452 -19.446 3.904  1.00 20.87 ? 97  HIS   C CE1 1 
ATOM   1813 N  NE2 . HIS   B 1 91  ? 10.529 -18.178 4.331  1.00 20.28 ? 97  HIS   C NE2 1 
ATOM   1814 N  N   . LEU   B 1 92  ? 7.761  -20.673 10.133 1.00 15.43 ? 98  LEU   C N   1 
ATOM   1815 C  CA  . LEU   B 1 92  ? 7.609  -21.303 11.453 1.00 14.75 ? 98  LEU   C CA  1 
ATOM   1816 C  C   . LEU   B 1 92  ? 6.522  -22.409 11.395 1.00 15.46 ? 98  LEU   C C   1 
ATOM   1817 O  O   . LEU   B 1 92  ? 5.496  -22.251 10.725 1.00 15.38 ? 98  LEU   C O   1 
ATOM   1818 C  CB  . LEU   B 1 92  ? 7.237  -20.211 12.510 1.00 15.14 ? 98  LEU   C CB  1 
ATOM   1819 C  CG  . LEU   B 1 92  ? 7.147  -20.607 13.976 1.00 18.04 ? 98  LEU   C CG  1 
ATOM   1820 C  CD1 . LEU   B 1 92  ? 8.536  -21.031 14.518 1.00 18.29 ? 98  LEU   C CD1 1 
ATOM   1821 C  CD2 . LEU   B 1 92  ? 6.727  -19.391 14.820 1.00 19.03 ? 98  LEU   C CD2 1 
ATOM   1822 N  N   . MET   B 1 93  ? 6.780  -23.538 12.078 1.00 14.30 ? 99  MET   C N   1 
ATOM   1823 C  CA  . MET   B 1 93  ? 5.827  -24.674 12.100 1.00 14.95 ? 99  MET   C CA  1 
ATOM   1824 C  C   . MET   B 1 93  ? 5.454  -24.938 13.531 1.00 15.50 ? 99  MET   C C   1 
ATOM   1825 O  O   . MET   B 1 93  ? 6.354  -24.978 14.377 1.00 16.13 ? 99  MET   C O   1 
ATOM   1826 C  CB  . MET   B 1 93  ? 6.529  -25.923 11.535 1.00 14.90 ? 99  MET   C CB  1 
ATOM   1827 C  CG  . MET   B 1 93  ? 6.920  -25.699 10.104 1.00 17.75 ? 99  MET   C CG  1 
ATOM   1828 S  SD  . MET   B 1 93  ? 7.963  -26.992 9.434  1.00 20.01 ? 99  MET   C SD  1 
ATOM   1829 C  CE  . MET   B 1 93  ? 9.486  -26.882 10.543 1.00 19.60 ? 99  MET   C CE  1 
ATOM   1830 N  N   . LEU   B 1 94  ? 4.151  -25.153 13.831 1.00 14.50 ? 100 LEU   C N   1 
ATOM   1831 C  CA  . LEU   B 1 94  ? 3.732  -25.400 15.210 1.00 13.55 ? 100 LEU   C CA  1 
ATOM   1832 C  C   . LEU   B 1 94  ? 3.351  -26.852 15.421 1.00 13.62 ? 100 LEU   C C   1 
ATOM   1833 O  O   . LEU   B 1 94  ? 2.818  -27.507 14.514 1.00 14.05 ? 100 LEU   C O   1 
ATOM   1834 C  CB  . LEU   B 1 94  ? 2.513  -24.513 15.604 1.00 15.53 ? 100 LEU   C CB  1 
ATOM   1835 C  CG  . LEU   B 1 94  ? 2.736  -23.018 15.535 1.00 18.34 ? 100 LEU   C CG  1 
ATOM   1836 C  CD1 . LEU   B 1 94  ? 1.442  -22.267 16.017 1.00 19.49 ? 100 LEU   C CD1 1 
ATOM   1837 C  CD2 . LEU   B 1 94  ? 3.961  -22.597 16.409 1.00 19.52 ? 100 LEU   C CD2 1 
ATOM   1838 N  N   . ALA   B 1 95  ? 3.580  -27.342 16.658 1.00 13.16 ? 101 ALA   C N   1 
ATOM   1839 C  CA  . ALA   B 1 95  ? 3.133  -28.663 17.060 1.00 14.47 ? 101 ALA   C CA  1 
ATOM   1840 C  C   . ALA   B 1 95  ? 2.552  -28.538 18.494 1.00 15.32 ? 101 ALA   C C   1 
ATOM   1841 O  O   . ALA   B 1 95  ? 2.897  -27.606 19.239 1.00 16.43 ? 101 ALA   C O   1 
ATOM   1842 C  CB  . ALA   B 1 95  ? 4.299  -29.648 17.098 1.00 14.41 ? 101 ALA   C CB  1 
ATOM   1843 N  N   . VAL   B 1 96  ? 1.694  -29.494 18.910 1.00 15.32 ? 102 VAL   C N   1 
ATOM   1844 C  CA  . VAL   B 1 96  ? 1.223  -29.573 20.283 1.00 16.39 ? 102 VAL   C CA  1 
ATOM   1845 C  C   . VAL   B 1 96  ? 2.297  -30.343 21.049 1.00 18.25 ? 102 VAL   C C   1 
ATOM   1846 O  O   . VAL   B 1 96  ? 2.587  -31.487 20.712 1.00 19.45 ? 102 VAL   C O   1 
ATOM   1847 C  CB  . VAL   B 1 96  ? -0.148 -30.301 20.323 1.00 18.72 ? 102 VAL   C CB  1 
ATOM   1848 C  CG1 . VAL   B 1 96  ? -0.634 -30.425 21.762 1.00 19.90 ? 102 VAL   C CG1 1 
ATOM   1849 C  CG2 . VAL   B 1 96  ? -1.159 -29.515 19.465 1.00 19.21 ? 102 VAL   C CG2 1 
ATOM   1850 N  N   . GLY   B 1 97  ? 2.947  -29.674 21.985 1.00 17.90 ? 103 GLY   C N   1 
ATOM   1851 C  CA  . GLY   B 1 97  ? 4.021  -30.314 22.738 1.00 19.45 ? 103 GLY   C CA  1 
ATOM   1852 C  C   . GLY   B 1 97  ? 4.654  -29.358 23.706 1.00 20.10 ? 103 GLY   C C   1 
ATOM   1853 O  O   . GLY   B 1 97  ? 4.437  -28.127 23.650 1.00 20.32 ? 103 GLY   C O   1 
ATOM   1854 N  N   . HIS   B 1 98  ? 5.442  -29.933 24.617 1.00 19.29 ? 104 HIS   C N   1 
ATOM   1855 C  CA  . HIS   B 1 98  ? 6.080  -29.127 25.632 1.00 19.47 ? 104 HIS   C CA  1 
ATOM   1856 C  C   . HIS   B 1 98  ? 7.315  -28.409 25.155 1.00 19.21 ? 104 HIS   C C   1 
ATOM   1857 O  O   . HIS   B 1 98  ? 8.145  -28.983 24.460 1.00 18.90 ? 104 HIS   C O   1 
ATOM   1858 C  CB  . HIS   B 1 98  ? 6.445  -30.014 26.848 1.00 19.70 ? 104 HIS   C CB  1 
ATOM   1859 C  CG  . HIS   B 1 98  ? 7.121  -29.248 27.940 1.00 20.84 ? 104 HIS   C CG  1 
ATOM   1860 N  ND1 . HIS   B 1 98  ? 6.429  -28.282 28.682 1.00 23.78 ? 104 HIS   C ND1 1 
ATOM   1861 C  CD2 . HIS   B 1 98  ? 8.430  -29.235 28.314 1.00 21.68 ? 104 HIS   C CD2 1 
ATOM   1862 C  CE1 . HIS   B 1 98  ? 7.325  -27.775 29.535 1.00 25.00 ? 104 HIS   C CE1 1 
ATOM   1863 N  NE2 . HIS   B 1 98  ? 8.551  -28.309 29.335 1.00 24.13 ? 104 HIS   C NE2 1 
ATOM   1864 N  N   . SER   B 1 99  ? 7.480  -27.171 25.626 1.00 18.85 ? 105 SER   C N   1 
ATOM   1865 C  CA  . SER   B 1 99  ? 8.693  -26.396 25.448 1.00 20.08 ? 105 SER   C CA  1 
ATOM   1866 C  C   . SER   B 1 99  ? 8.766  -25.331 26.535 1.00 22.25 ? 105 SER   C C   1 
ATOM   1867 O  O   . SER   B 1 99  ? 7.752  -24.891 27.087 1.00 23.84 ? 105 SER   C O   1 
ATOM   1868 C  CB  . SER   B 1 99  ? 8.831  -25.804 24.045 1.00 21.42 ? 105 SER   C CB  1 
ATOM   1869 O  OG  . SER   B 1 99  ? 7.870  -24.784 23.828 1.00 25.03 ? 105 SER   C OG  1 
ATOM   1870 N  N   . GLU   B 1 100 ? 9.974  -24.958 26.861 1.00 22.19 ? 106 GLU   C N   1 
ATOM   1871 C  CA  . GLU   B 1 100 ? 10.234 -23.925 27.846 1.00 23.98 ? 106 GLU   C CA  1 
ATOM   1872 C  C   . GLU   B 1 100 ? 11.369 -23.086 27.351 1.00 25.00 ? 106 GLU   C C   1 
ATOM   1873 O  O   . GLU   B 1 100 ? 12.189 -23.567 26.560 1.00 25.14 ? 106 GLU   C O   1 
ATOM   1874 C  CB  . GLU   B 1 100 ? 10.748 -24.617 29.119 1.00 26.70 ? 106 GLU   C CB  1 
ATOM   1875 C  CG  . GLU   B 1 100 ? 9.670  -25.022 30.063 1.00 32.81 ? 106 GLU   C CG  1 
ATOM   1876 C  CD  . GLU   B 1 100 ? 10.292 -25.889 31.135 1.00 33.66 ? 106 GLU   C CD  1 
ATOM   1877 O  OE1 . GLU   B 1 100 ? 11.350 -25.511 31.684 1.00 36.11 ? 106 GLU   C OE1 1 
ATOM   1878 O  OE2 . GLU   B 1 100 ? 9.732  -26.967 31.404 1.00 33.24 ? 106 GLU   C OE2 1 
ATOM   1879 N  N   . PRO   B 1 101 ? 11.546 -21.852 27.899 1.00 26.75 ? 107 PRO   C N   1 
ATOM   1880 C  CA  . PRO   B 1 101 ? 12.791 -21.133 27.639 1.00 28.37 ? 107 PRO   C CA  1 
ATOM   1881 C  C   . PRO   B 1 101 ? 13.994 -22.029 28.102 1.00 28.21 ? 107 PRO   C C   1 
ATOM   1882 O  O   . PRO   B 1 101 ? 14.040 -22.576 29.232 1.00 30.66 ? 107 PRO   C O   1 
ATOM   1883 C  CB  . PRO   B 1 101 ? 12.654 -19.875 28.522 1.00 29.98 ? 107 PRO   C CB  1 
ATOM   1884 C  CG  . PRO   B 1 101 ? 11.157 -19.713 28.723 1.00 30.49 ? 107 PRO   C CG  1 
ATOM   1885 C  CD  . PRO   B 1 101 ? 10.694 -21.144 28.873 1.00 27.81 ? 107 PRO   C CD  1 
ATOM   1886 N  N   . GLY   B 1 102 ? 14.907 -22.246 27.186 1.00 24.70 ? 108 GLY   C N   1 
ATOM   1887 C  CA  . GLY   B 1 102 ? 16.022 -23.162 27.340 1.00 22.55 ? 108 GLY   C CA  1 
ATOM   1888 C  C   . GLY   B 1 102 ? 15.963 -24.273 26.293 1.00 21.27 ? 108 GLY   C C   1 
ATOM   1889 O  O   . GLY   B 1 102 ? 16.988 -24.901 25.971 1.00 20.95 ? 108 GLY   C O   1 
ATOM   1890 N  N   . ASP   B 1 103 ? 14.754 -24.487 25.711 1.00 18.98 ? 109 ASP   C N   1 
ATOM   1891 C  CA  . ASP   B 1 103 ? 14.563 -25.534 24.701 1.00 18.60 ? 109 ASP   C CA  1 
ATOM   1892 C  C   . ASP   B 1 103 ? 14.937 -25.134 23.284 1.00 17.74 ? 109 ASP   C C   1 
ATOM   1893 O  O   . ASP   B 1 103 ? 15.063 -26.034 22.420 1.00 17.45 ? 109 ASP   C O   1 
ATOM   1894 C  CB  . ASP   B 1 103 ? 13.114 -26.088 24.729 1.00 18.02 ? 109 ASP   C CB  1 
ATOM   1895 C  CG  . ASP   B 1 103 ? 12.890 -27.001 25.932 1.00 19.94 ? 109 ASP   C CG  1 
ATOM   1896 O  OD1 . ASP   B 1 103 ? 13.854 -27.658 26.363 1.00 20.35 ? 109 ASP   C OD1 1 
ATOM   1897 O  OD2 . ASP   B 1 103 ? 11.761 -27.033 26.452 1.00 20.31 ? 109 ASP   C OD2 1 
ATOM   1898 N  N   . CYS   B 1 104 ? 15.171 -23.826 23.011 1.00 16.78 ? 110 CYS   C N   1 
ATOM   1899 C  CA  . CYS   B 1 104 ? 15.541 -23.419 21.626 1.00 16.94 ? 110 CYS   C CA  1 
ATOM   1900 C  C   . CYS   B 1 104 ? 16.795 -24.130 21.170 1.00 17.23 ? 110 CYS   C C   1 
ATOM   1901 O  O   . CYS   B 1 104 ? 17.725 -24.297 21.959 1.00 17.55 ? 110 CYS   C O   1 
ATOM   1902 C  CB  . CYS   B 1 104 ? 15.694 -21.907 21.477 1.00 17.21 ? 110 CYS   C CB  1 
ATOM   1903 S  SG  . CYS   B 1 104 ? 14.123 -21.007 21.629 1.00 21.97 ? 110 CYS   C SG  1 
ATOM   1904 N  N   . GLY   B 1 105 ? 16.792 -24.558 19.916 1.00 15.79 ? 111 GLY   C N   1 
ATOM   1905 C  CA  . GLY   B 1 105 ? 17.952 -25.242 19.379 1.00 16.94 ? 111 GLY   C CA  1 
ATOM   1906 C  C   . GLY   B 1 105 ? 17.801 -26.746 19.308 1.00 17.18 ? 111 GLY   C C   1 
ATOM   1907 O  O   . GLY   B 1 105 ? 18.575 -27.417 18.614 1.00 18.24 ? 111 GLY   C O   1 
ATOM   1908 N  N   . GLY   B 1 106 ? 16.771 -27.283 19.976 1.00 15.23 ? 112 GLY   C N   1 
ATOM   1909 C  CA  . GLY   B 1 106 ? 16.506 -28.724 19.895 1.00 14.26 ? 112 GLY   C CA  1 
ATOM   1910 C  C   . GLY   B 1 106 ? 16.116 -29.072 18.467 1.00 14.59 ? 112 GLY   C C   1 
ATOM   1911 O  O   . GLY   B 1 106 ? 15.361 -28.333 17.839 1.00 14.77 ? 112 GLY   C O   1 
ATOM   1912 N  N   . ILE   B 1 107 ? 16.663 -30.178 17.961 1.00 13.73 ? 113 ILE   C N   1 
ATOM   1913 C  CA  . ILE   B 1 107 ? 16.410 -30.541 16.563 1.00 14.32 ? 113 ILE   C CA  1 
ATOM   1914 C  C   . ILE   B 1 107 ? 15.109 -31.304 16.385 1.00 14.07 ? 113 ILE   C C   1 
ATOM   1915 O  O   . ILE   B 1 107 ? 14.789 -32.205 17.195 1.00 15.12 ? 113 ILE   C O   1 
ATOM   1916 C  CB  . ILE   B 1 107 ? 17.641 -31.308 15.987 1.00 17.79 ? 113 ILE   C CB  1 
ATOM   1917 C  CG1 . ILE   B 1 107 ? 18.832 -30.319 15.757 1.00 20.28 ? 113 ILE   C CG1 1 
ATOM   1918 C  CG2 . ILE   B 1 107 ? 17.324 -32.104 14.702 1.00 19.00 ? 113 ILE   C CG2 1 
ATOM   1919 C  CD1 . ILE   B 1 107 ? 20.161 -31.091 15.285 1.00 23.77 ? 113 ILE   C CD1 1 
ATOM   1920 N  N   . LEU   B 1 108 ? 14.404 -30.994 15.280 1.00 13.40 ? 114 LEU   C N   1 
ATOM   1921 C  CA  . LEU   B 1 108 ? 13.219 -31.746 14.816 1.00 14.04 ? 114 LEU   C CA  1 
ATOM   1922 C  C   . LEU   B 1 108 ? 13.701 -32.543 13.577 1.00 14.69 ? 114 LEU   C C   1 
ATOM   1923 O  O   . LEU   B 1 108 ? 14.307 -31.960 12.663 1.00 14.49 ? 114 LEU   C O   1 
ATOM   1924 C  CB  . LEU   B 1 108 ? 12.119 -30.748 14.379 1.00 13.84 ? 114 LEU   C CB  1 
ATOM   1925 C  CG  . LEU   B 1 108 ? 10.923 -31.364 13.661 1.00 15.30 ? 114 LEU   C CG  1 
ATOM   1926 C  CD1 . LEU   B 1 108 ? 10.127 -32.343 14.612 1.00 15.81 ? 114 LEU   C CD1 1 
ATOM   1927 C  CD2 . LEU   B 1 108 ? 9.976  -30.223 13.130 1.00 15.80 ? 114 LEU   C CD2 1 
ATOM   1928 N  N   . ARG   B 1 109 ? 13.453 -33.864 13.553 1.00 13.65 ? 115 ARG   C N   1 
ATOM   1929 C  CA  . ARG   B 1 109 ? 13.855 -34.718 12.438 1.00 14.49 ? 115 ARG   C CA  1 
ATOM   1930 C  C   . ARG   B 1 109 ? 12.668 -35.523 11.954 1.00 15.68 ? 115 ARG   C C   1 
ATOM   1931 O  O   . ARG   B 1 109 ? 11.846 -35.973 12.758 1.00 15.89 ? 115 ARG   C O   1 
ATOM   1932 C  CB  . ARG   B 1 109 ? 14.884 -35.771 12.917 1.00 17.44 ? 115 ARG   C CB  1 
ATOM   1933 C  CG  . ARG   B 1 109 ? 16.163 -35.228 13.469 1.00 23.40 ? 115 ARG   C CG  1 
ATOM   1934 C  CD  . ARG   B 1 109 ? 17.043 -36.390 13.962 1.00 29.38 ? 115 ARG   C CD  1 
ATOM   1935 N  NE  . ARG   B 1 109 ? 17.567 -37.067 12.778 1.00 36.35 ? 115 ARG   C NE  1 
ATOM   1936 C  CZ  . ARG   B 1 109 ? 18.705 -36.727 12.180 1.00 40.88 ? 115 ARG   C CZ  1 
ATOM   1937 N  NH1 . ARG   B 1 109 ? 19.525 -35.844 12.747 1.00 43.02 ? 115 ARG   C NH1 1 
ATOM   1938 N  NH2 . ARG   B 1 109 ? 19.060 -37.307 11.049 1.00 41.89 ? 115 ARG   C NH2 1 
ATOM   1939 N  N   . CYS   B 1 110 ? 12.635 -35.789 10.661 1.00 15.02 ? 116 CYS   C N   1 
ATOM   1940 C  CA  . CYS   B 1 110 ? 11.656 -36.728 10.084 1.00 15.92 ? 116 CYS   C CA  1 
ATOM   1941 C  C   . CYS   B 1 110 ? 12.457 -37.936 9.537  1.00 17.30 ? 116 CYS   C C   1 
ATOM   1942 O  O   . CYS   B 1 110 ? 13.688 -38.007 9.693  1.00 16.56 ? 116 CYS   C O   1 
ATOM   1943 C  CB  . CYS   B 1 110 ? 10.851 -36.059 8.968  1.00 15.60 ? 116 CYS   C CB  1 
ATOM   1944 S  SG  . CYS   B 1 110 ? 11.874 -35.544 7.552  1.00 14.80 ? 116 CYS   C SG  1 
ATOM   1945 N  N   . GLN   B 1 111 ? 11.761 -38.850 8.806  1.00 19.01 ? 117 GLN   C N   1 
ATOM   1946 C  CA  . GLN   B 1 111 ? 12.453 -39.988 8.209  1.00 19.41 ? 117 GLN   C CA  1 
ATOM   1947 C  C   . GLN   B 1 111 ? 13.542 -39.566 7.185  1.00 19.94 ? 117 GLN   C C   1 
ATOM   1948 O  O   . GLN   B 1 111 ? 14.405 -40.381 6.828  1.00 21.76 ? 117 GLN   C O   1 
ATOM   1949 C  CB  . GLN   B 1 111 ? 11.441 -40.933 7.542  1.00 21.57 ? 117 GLN   C CB  1 
ATOM   1950 C  CG  . GLN   B 1 111 ? 10.742 -40.311 6.322  1.00 24.57 ? 117 GLN   C CG  1 
ATOM   1951 C  CD  . GLN   B 1 111 ? 9.740  -41.280 5.727  1.00 33.58 ? 117 GLN   C CD  1 
ATOM   1952 O  OE1 . GLN   B 1 111 ? 8.530  -41.043 5.783  1.00 35.14 ? 117 GLN   C OE1 1 
ATOM   1953 N  NE2 . GLN   B 1 111 ? 10.222 -42.369 5.124  1.00 35.69 ? 117 GLN   C NE2 1 
ATOM   1954 N  N   . HIS   B 1 112 ? 13.513 -38.308 6.701  1.00 17.65 ? 118 HIS   C N   1 
ATOM   1955 C  CA  . HIS   B 1 112 ? 14.468 -37.864 5.676  1.00 18.07 ? 118 HIS   C CA  1 
ATOM   1956 C  C   . HIS   B 1 112 ? 15.670 -37.103 6.213  1.00 18.99 ? 118 HIS   C C   1 
ATOM   1957 O  O   . HIS   B 1 112 ? 16.599 -36.846 5.453  1.00 20.85 ? 118 HIS   C O   1 
ATOM   1958 C  CB  . HIS   B 1 112 ? 13.779 -36.987 4.610  1.00 17.56 ? 118 HIS   C CB  1 
ATOM   1959 C  CG  . HIS   B 1 112 ? 12.583 -37.653 3.991  1.00 17.56 ? 118 HIS   C CG  1 
ATOM   1960 N  ND1 . HIS   B 1 112 ? 11.299 -37.248 4.310  1.00 17.65 ? 118 HIS   C ND1 1 
ATOM   1961 C  CD2 . HIS   B 1 112 ? 12.519 -38.659 3.087  1.00 19.00 ? 118 HIS   C CD2 1 
ATOM   1962 C  CE1 . HIS   B 1 112 ? 10.473 -38.031 3.625  1.00 19.26 ? 118 HIS   C CE1 1 
ATOM   1963 N  NE2 . HIS   B 1 112 ? 11.148 -38.906 2.859  1.00 20.13 ? 118 HIS   C NE2 1 
ATOM   1964 N  N   . GLY   B 1 113 ? 15.652 -36.740 7.490  1.00 17.93 ? 119 GLY   C N   1 
ATOM   1965 C  CA  . GLY   B 1 113 ? 16.752 -35.955 8.047  1.00 17.22 ? 119 GLY   C CA  1 
ATOM   1966 C  C   . GLY   B 1 113 ? 16.294 -34.799 8.916  1.00 15.34 ? 119 GLY   C C   1 
ATOM   1967 O  O   . GLY   B 1 113 ? 15.173 -34.799 9.430  1.00 15.08 ? 119 GLY   C O   1 
ATOM   1968 N  N   . VAL   B 1 114 ? 17.149 -33.805 9.062  1.00 14.26 ? 120 VAL   C N   1 
ATOM   1969 C  CA  . VAL   B 1 114 ? 16.832 -32.644 9.885  1.00 14.63 ? 120 VAL   C CA  1 
ATOM   1970 C  C   . VAL   B 1 114 ? 15.828 -31.731 9.201  1.00 14.81 ? 120 VAL   C C   1 
ATOM   1971 O  O   . VAL   B 1 114 ? 16.034 -31.316 8.049  1.00 15.24 ? 120 VAL   C O   1 
ATOM   1972 C  CB  . VAL   B 1 114 ? 18.125 -31.857 10.195 1.00 16.21 ? 120 VAL   C CB  1 
ATOM   1973 C  CG1 . VAL   B 1 114 ? 17.773 -30.577 10.959 1.00 16.64 ? 120 VAL   C CG1 1 
ATOM   1974 C  CG2 . VAL   B 1 114 ? 19.079 -32.747 11.024 1.00 17.02 ? 120 VAL   C CG2 1 
ATOM   1975 N  N   . VAL   B 1 115 ? 14.760 -31.359 9.918  1.00 13.87 ? 121 VAL   C N   1 
ATOM   1976 C  CA  . VAL   B 1 115 ? 13.703 -30.501 9.397  1.00 13.25 ? 121 VAL   C CA  1 
ATOM   1977 C  C   . VAL   B 1 115 ? 13.866 -29.052 9.891  1.00 14.37 ? 121 VAL   C C   1 
ATOM   1978 O  O   . VAL   B 1 115 ? 13.602 -28.098 9.146  1.00 14.10 ? 121 VAL   C O   1 
ATOM   1979 C  CB  . VAL   B 1 115 ? 12.312 -31.036 9.898  1.00 13.92 ? 121 VAL   C CB  1 
ATOM   1980 C  CG1 . VAL   B 1 115 ? 11.178 -30.052 9.574  1.00 14.94 ? 121 VAL   C CG1 1 
ATOM   1981 C  CG2 . VAL   B 1 115 ? 12.032 -32.396 9.304  1.00 14.24 ? 121 VAL   C CG2 1 
ATOM   1982 N  N   . GLY   B 1 116 ? 14.250 -28.910 11.157 1.00 14.11 ? 122 GLY   C N   1 
ATOM   1983 C  CA  . GLY   B 1 116 ? 14.365 -27.569 11.720 1.00 15.11 ? 122 GLY   C CA  1 
ATOM   1984 C  C   . GLY   B 1 116 ? 14.741 -27.576 13.178 1.00 14.49 ? 122 GLY   C C   1 
ATOM   1985 O  O   . GLY   B 1 116 ? 15.153 -28.617 13.690 1.00 14.75 ? 122 GLY   C O   1 
ATOM   1986 N  N   . ILE   B 1 117 ? 14.668 -26.399 13.832 1.00 13.93 ? 123 ILE   C N   1 
ATOM   1987 C  CA  . ILE   B 1 117 ? 15.072 -26.333 15.237 1.00 14.10 ? 123 ILE   C CA  1 
ATOM   1988 C  C   . ILE   B 1 117 ? 14.030 -25.607 16.070 1.00 13.80 ? 123 ILE   C C   1 
ATOM   1989 O  O   . ILE   B 1 117 ? 13.407 -24.670 15.580 1.00 14.32 ? 123 ILE   C O   1 
ATOM   1990 C  CB  . ILE   B 1 117 ? 16.430 -25.615 15.392 1.00 16.13 ? 123 ILE   C CB  1 
ATOM   1991 C  CG1 . ILE   B 1 117 ? 16.458 -24.287 14.646 1.00 16.62 ? 123 ILE   C CG1 1 
ATOM   1992 C  CG2 . ILE   B 1 117 ? 17.607 -26.534 15.003 1.00 17.89 ? 123 ILE   C CG2 1 
ATOM   1993 C  CD1 . ILE   B 1 117 ? 17.805 -23.456 15.015 1.00 19.51 ? 123 ILE   C CD1 1 
ATOM   1994 N  N   . VAL   B 1 118 ? 13.893 -25.965 17.385 1.00 13.17 ? 124 VAL   C N   1 
ATOM   1995 C  CA  . VAL   B 1 118 ? 12.943 -25.241 18.252 1.00 13.15 ? 124 VAL   C CA  1 
ATOM   1996 C  C   . VAL   B 1 118 ? 13.300 -23.744 18.277 1.00 13.06 ? 124 VAL   C C   1 
ATOM   1997 O  O   . VAL   B 1 118 ? 14.485 -23.402 18.425 1.00 14.09 ? 124 VAL   C O   1 
ATOM   1998 C  CB  . VAL   B 1 118 ? 12.974 -25.792 19.696 1.00 13.85 ? 124 VAL   C CB  1 
ATOM   1999 C  CG1 . VAL   B 1 118 ? 12.082 -24.947 20.596 1.00 15.00 ? 124 VAL   C CG1 1 
ATOM   2000 C  CG2 . VAL   B 1 118 ? 12.569 -27.269 19.738 1.00 14.26 ? 124 VAL   C CG2 1 
ATOM   2001 N  N   . SER   B 1 119 ? 12.289 -22.872 18.116 1.00 13.59 ? 125 SER   C N   1 
ATOM   2002 C  CA  . SER   B 1 119 ? 12.518 -21.434 18.075 1.00 13.84 ? 125 SER   C CA  1 
ATOM   2003 C  C   . SER   B 1 119 ? 11.527 -20.666 18.949 1.00 15.26 ? 125 SER   C C   1 
ATOM   2004 O  O   . SER   B 1 119 ? 11.860 -19.581 19.427 1.00 16.46 ? 125 SER   C O   1 
ATOM   2005 C  CB  . SER   B 1 119 ? 12.416 -20.946 16.620 1.00 15.44 ? 125 SER   C CB  1 
ATOM   2006 O  OG  . SER   B 1 119 ? 12.564 -19.524 16.548 1.00 16.00 ? 125 SER   C OG  1 
ATOM   2007 N  N   . THR   B 1 120 ? 10.337 -21.209 19.201 1.00 15.52 ? 126 THR   C N   1 
ATOM   2008 C  CA  . THR   B 1 120 ? 9.320  -20.512 20.016 1.00 17.03 ? 126 THR   C CA  1 
ATOM   2009 C  C   . THR   B 1 120 ? 8.500  -21.538 20.816 1.00 17.37 ? 126 THR   C C   1 
ATOM   2010 O  O   . THR   B 1 120 ? 8.566  -22.753 20.560 1.00 15.90 ? 126 THR   C O   1 
ATOM   2011 C  CB  . THR   B 1 120 ? 8.289  -19.726 19.093 1.00 19.75 ? 126 THR   C CB  1 
ATOM   2012 O  OG1 . THR   B 1 120 ? 7.408  -20.642 18.427 1.00 21.72 ? 126 THR   C OG1 1 
ATOM   2013 C  CG2 . THR   B 1 120 ? 8.910  -18.804 18.106 1.00 20.36 ? 126 THR   C CG2 1 
ATOM   2014 N  N   . GLY   B 1 121 ? 7.739  -21.053 21.782 1.00 18.20 ? 127 GLY   C N   1 
ATOM   2015 C  CA  . GLY   B 1 121 ? 6.826  -21.920 22.517 1.00 19.99 ? 127 GLY   C CA  1 
ATOM   2016 C  C   . GLY   B 1 121 ? 5.858  -21.131 23.355 1.00 21.21 ? 127 GLY   C C   1 
ATOM   2017 O  O   . GLY   B 1 121 ? 6.016  -19.925 23.530 1.00 20.46 ? 127 GLY   C O   1 
ATOM   2018 N  N   . GLY   B 1 122 ? 4.862  -21.826 23.892 1.00 22.58 ? 128 GLY   C N   1 
ATOM   2019 C  CA  . GLY   B 1 122 ? 3.887  -21.208 24.785 1.00 23.86 ? 128 GLY   C CA  1 
ATOM   2020 C  C   . GLY   B 1 122 ? 2.536  -21.880 24.645 1.00 24.64 ? 128 GLY   C C   1 
ATOM   2021 O  O   . GLY   B 1 122 ? 2.228  -22.429 23.582 1.00 23.63 ? 128 GLY   C O   1 
ATOM   2022 N  N   . ASN   B 1 123 ? 1.710  -21.841 25.713 1.00 25.51 ? 129 ASN   C N   1 
ATOM   2023 C  CA  . ASN   B 1 123 ? 0.364  -22.436 25.734 1.00 26.11 ? 129 ASN   C CA  1 
ATOM   2024 C  C   . ASN   B 1 123 ? 0.292  -23.885 25.249 1.00 26.01 ? 129 ASN   C C   1 
ATOM   2025 O  O   . ASN   B 1 123 ? -0.677 -24.264 24.565 1.00 26.89 ? 129 ASN   C O   1 
ATOM   2026 C  CB  . ASN   B 1 123 ? -0.603 -21.566 24.937 1.00 29.07 ? 129 ASN   C CB  1 
ATOM   2027 C  CG  . ASN   B 1 123 ? -0.718 -20.182 25.494 1.00 35.04 ? 129 ASN   C CG  1 
ATOM   2028 O  OD1 . ASN   B 1 123 ? -0.956 -19.991 26.676 1.00 37.48 ? 129 ASN   C OD1 1 
ATOM   2029 N  ND2 . ASN   B 1 123 ? -0.530 -19.191 24.648 1.00 38.44 ? 129 ASN   C ND2 1 
ATOM   2030 N  N   . GLY   B 1 124 ? 1.306  -24.692 25.569 1.00 24.37 ? 130 GLY   C N   1 
ATOM   2031 C  CA  . GLY   B 1 124 ? 1.316  -26.080 25.126 1.00 22.79 ? 130 GLY   C CA  1 
ATOM   2032 C  C   . GLY   B 1 124 ? 1.584  -26.291 23.640 1.00 20.18 ? 130 GLY   C C   1 
ATOM   2033 O  O   . GLY   B 1 124 ? 1.347  -27.384 23.129 1.00 21.10 ? 130 GLY   C O   1 
ATOM   2034 N  N   . LEU   B 1 125 ? 2.149  -25.286 22.948 1.00 17.87 ? 131 LEU   C N   1 
ATOM   2035 C  CA  . LEU   B 1 125 ? 2.535  -25.384 21.556 1.00 18.60 ? 131 LEU   C CA  1 
ATOM   2036 C  C   . LEU   B 1 125 ? 4.057  -25.139 21.478 1.00 18.74 ? 131 LEU   C C   1 
ATOM   2037 O  O   . LEU   B 1 125 ? 4.611  -24.395 22.294 1.00 21.02 ? 131 LEU   C O   1 
ATOM   2038 C  CB  . LEU   B 1 125 ? 1.812  -24.314 20.721 1.00 19.99 ? 131 LEU   C CB  1 
ATOM   2039 C  CG  . LEU   B 1 125 ? 0.263  -24.437 20.778 1.00 22.66 ? 131 LEU   C CG  1 
ATOM   2040 C  CD1 . LEU   B 1 125 ? -0.399 -23.118 20.411 1.00 24.15 ? 131 LEU   C CD1 1 
ATOM   2041 C  CD2 . LEU   B 1 125 ? -0.218 -25.526 19.809 1.00 22.60 ? 131 LEU   C CD2 1 
ATOM   2042 N  N   . VAL   B 1 126 ? 4.722  -25.821 20.549 1.00 14.78 ? 132 VAL   C N   1 
ATOM   2043 C  CA  . VAL   B 1 126 ? 6.148  -25.630 20.294 1.00 15.54 ? 132 VAL   C CA  1 
ATOM   2044 C  C   . VAL   B 1 126 ? 6.274  -25.196 18.842 1.00 15.36 ? 132 VAL   C C   1 
ATOM   2045 O  O   . VAL   B 1 126 ? 5.615  -25.773 17.937 1.00 16.04 ? 132 VAL   C O   1 
ATOM   2046 C  CB  . VAL   B 1 126 ? 6.991  -26.876 20.623 1.00 17.45 ? 132 VAL   C CB  1 
ATOM   2047 C  CG1 . VAL   B 1 126 ? 6.453  -28.144 19.972 1.00 19.53 ? 132 VAL   C CG1 1 
ATOM   2048 C  CG2 . VAL   B 1 126 ? 8.495  -26.655 20.288 1.00 17.21 ? 132 VAL   C CG2 1 
ATOM   2049 N  N   . GLY   B 1 127 ? 7.149  -24.196 18.594 1.00 14.51 ? 133 GLY   C N   1 
ATOM   2050 C  CA  . GLY   B 1 127 ? 7.360  -23.727 17.230 1.00 14.70 ? 133 GLY   C CA  1 
ATOM   2051 C  C   . GLY   B 1 127 ? 8.766  -24.039 16.730 1.00 14.79 ? 133 GLY   C C   1 
ATOM   2052 O  O   . GLY   B 1 127 ? 9.730  -23.924 17.489 1.00 14.73 ? 133 GLY   C O   1 
ATOM   2053 N  N   . PHE   B 1 128 ? 8.874  -24.516 15.489 1.00 13.88 ? 134 PHE   C N   1 
ATOM   2054 C  CA  . PHE   B 1 128 ? 10.176 -24.894 14.922 1.00 14.06 ? 134 PHE   C CA  1 
ATOM   2055 C  C   . PHE   B 1 128 ? 10.461 -24.028 13.703 1.00 13.94 ? 134 PHE   C C   1 
ATOM   2056 O  O   . PHE   B 1 128 ? 9.607  -23.882 12.820 1.00 14.25 ? 134 PHE   C O   1 
ATOM   2057 C  CB  . PHE   B 1 128 ? 10.136 -26.347 14.418 1.00 14.18 ? 134 PHE   C CB  1 
ATOM   2058 C  CG  . PHE   B 1 128 ? 9.682  -27.338 15.469 1.00 14.16 ? 134 PHE   C CG  1 
ATOM   2059 C  CD1 . PHE   B 1 128 ? 10.581 -27.876 16.374 1.00 13.79 ? 134 PHE   C CD1 1 
ATOM   2060 C  CD2 . PHE   B 1 128 ? 8.361  -27.772 15.514 1.00 15.41 ? 134 PHE   C CD2 1 
ATOM   2061 C  CE1 . PHE   B 1 128 ? 10.158 -28.811 17.318 1.00 14.46 ? 134 PHE   C CE1 1 
ATOM   2062 C  CE2 . PHE   B 1 128 ? 7.944  -28.717 16.441 1.00 15.47 ? 134 PHE   C CE2 1 
ATOM   2063 C  CZ  . PHE   B 1 128 ? 8.847  -29.215 17.361 1.00 15.49 ? 134 PHE   C CZ  1 
ATOM   2064 N  N   . ALA   B 1 129 ? 11.710 -23.523 13.622 1.00 12.88 ? 135 ALA   C N   1 
ATOM   2065 C  CA  . ALA   B 1 129 ? 12.139 -22.766 12.452 1.00 12.80 ? 135 ALA   C CA  1 
ATOM   2066 C  C   . ALA   B 1 129 ? 12.520 -23.790 11.390 1.00 12.99 ? 135 ALA   C C   1 
ATOM   2067 O  O   . ALA   B 1 129 ? 13.442 -24.590 11.609 1.00 12.64 ? 135 ALA   C O   1 
ATOM   2068 C  CB  . ALA   B 1 129 ? 13.357 -21.907 12.817 1.00 13.68 ? 135 ALA   C CB  1 
ATOM   2069 N  N   . ASP   B 1 130 ? 11.838 -23.752 10.221 1.00 13.30 ? 136 ASP   C N   1 
ATOM   2070 C  CA  . ASP   B 1 130 ? 12.132 -24.719 9.151  1.00 14.32 ? 136 ASP   C CA  1 
ATOM   2071 C  C   . ASP   B 1 130 ? 13.480 -24.413 8.498  1.00 14.74 ? 136 ASP   C C   1 
ATOM   2072 O  O   . ASP   B 1 130 ? 13.812 -23.234 8.308  1.00 15.08 ? 136 ASP   C O   1 
ATOM   2073 C  CB  . ASP   B 1 130 ? 11.047 -24.558 8.040  1.00 14.86 ? 136 ASP   C CB  1 
ATOM   2074 C  CG  . ASP   B 1 130 ? 11.141 -25.602 6.942  1.00 21.92 ? 136 ASP   C CG  1 
ATOM   2075 O  OD1 . ASP   B 1 130 ? 11.300 -26.771 7.267  1.00 21.35 ? 136 ASP   C OD1 1 
ATOM   2076 O  OD2 . ASP   B 1 130 ? 11.089 -25.225 5.754  1.00 24.78 ? 136 ASP   C OD2 1 
ATOM   2077 N  N   . VAL   B 1 131 ? 14.219 -25.466 8.070  1.00 14.07 ? 137 VAL   C N   1 
ATOM   2078 C  CA  . VAL   B 1 131 ? 15.454 -25.242 7.294  1.00 13.86 ? 137 VAL   C CA  1 
ATOM   2079 C  C   . VAL   B 1 131 ? 15.415 -26.003 5.940  1.00 14.86 ? 137 VAL   C C   1 
ATOM   2080 O  O   . VAL   B 1 131 ? 16.389 -25.971 5.197  1.00 15.81 ? 137 VAL   C O   1 
ATOM   2081 C  CB  . VAL   B 1 131 ? 16.750 -25.628 8.059  1.00 15.44 ? 137 VAL   C CB  1 
ATOM   2082 C  CG1 . VAL   B 1 131 ? 16.940 -24.753 9.305  1.00 15.45 ? 137 VAL   C CG1 1 
ATOM   2083 C  CG2 . VAL   B 1 131 ? 16.781 -27.116 8.409  1.00 15.12 ? 137 VAL   C CG2 1 
ATOM   2084 N  N   . ARG   B 1 132 ? 14.305 -26.692 5.630  1.00 14.19 ? 138 ARG   C N   1 
ATOM   2085 C  CA  . ARG   B 1 132 ? 14.236 -27.546 4.453  1.00 13.13 ? 138 ARG   C CA  1 
ATOM   2086 C  C   . ARG   B 1 132 ? 14.324 -26.786 3.133  1.00 14.86 ? 138 ARG   C C   1 
ATOM   2087 O  O   . ARG   B 1 132 ? 14.694 -27.382 2.115  1.00 16.67 ? 138 ARG   C O   1 
ATOM   2088 C  CB  . ARG   B 1 132 ? 12.983 -28.421 4.485  1.00 12.89 ? 138 ARG   C CB  1 
ATOM   2089 C  CG  . ARG   B 1 132 ? 12.970 -29.372 5.660  1.00 13.26 ? 138 ARG   C CG  1 
ATOM   2090 C  CD  . ARG   B 1 132 ? 11.654 -30.125 5.676  1.00 13.12 ? 138 ARG   C CD  1 
ATOM   2091 N  NE  . ARG   B 1 132 ? 10.570 -29.226 6.103  1.00 13.12 ? 138 ARG   C NE  1 
ATOM   2092 C  CZ  . ARG   B 1 132 ? 9.323  -29.615 6.319  1.00 15.28 ? 138 ARG   C CZ  1 
ATOM   2093 N  NH1 . ARG   B 1 132 ? 8.952  -30.869 6.061  1.00 15.63 ? 138 ARG   C NH1 1 
ATOM   2094 N  NH2 . ARG   B 1 132 ? 8.422  -28.756 6.795  1.00 14.32 ? 138 ARG   C NH2 1 
ATOM   2095 N  N   . ASP   B 1 133 ? 13.945 -25.508 3.131  1.00 14.88 ? 139 ASP   C N   1 
ATOM   2096 C  CA  . ASP   B 1 133 ? 14.013 -24.709 1.913  1.00 15.80 ? 139 ASP   C CA  1 
ATOM   2097 C  C   . ASP   B 1 133 ? 15.414 -24.130 1.660  1.00 16.40 ? 139 ASP   C C   1 
ATOM   2098 O  O   . ASP   B 1 133 ? 15.635 -23.552 0.581  1.00 18.06 ? 139 ASP   C O   1 
ATOM   2099 C  CB  . ASP   B 1 133 ? 12.987 -23.570 1.954  1.00 18.26 ? 139 ASP   C CB  1 
ATOM   2100 C  CG  . ASP   B 1 133 ? 13.263 -22.554 3.044  1.00 22.34 ? 139 ASP   C CG  1 
ATOM   2101 O  OD1 . ASP   B 1 133 ? 13.504 -22.980 4.204  1.00 22.18 ? 139 ASP   C OD1 1 
ATOM   2102 O  OD2 . ASP   B 1 133 ? 13.246 -21.317 2.736  1.00 23.05 ? 139 ASP   C OD2 1 
ATOM   2103 N  N   . LEU   B 1 134 ? 16.360 -24.251 2.620  1.00 15.52 ? 140 LEU   C N   1 
ATOM   2104 C  CA  . LEU   B 1 134 ? 17.703 -23.676 2.431  1.00 15.79 ? 140 LEU   C CA  1 
ATOM   2105 C  C   . LEU   B 1 134 ? 18.558 -24.659 1.654  1.00 16.86 ? 140 LEU   C C   1 
ATOM   2106 O  O   . LEU   B 1 134 ? 19.407 -25.388 2.219  1.00 17.78 ? 140 LEU   C O   1 
ATOM   2107 C  CB  . LEU   B 1 134 ? 18.319 -23.370 3.828  1.00 15.90 ? 140 LEU   C CB  1 
ATOM   2108 C  CG  . LEU   B 1 134 ? 17.453 -22.440 4.693  1.00 17.80 ? 140 LEU   C CG  1 
ATOM   2109 C  CD1 . LEU   B 1 134 ? 18.100 -22.260 6.081  1.00 18.39 ? 140 LEU   C CD1 1 
ATOM   2110 C  CD2 . LEU   B 1 134 ? 17.223 -21.083 4.010  1.00 17.86 ? 140 LEU   C CD2 1 
ATOM   2111 N  N   . LEU   B 1 135 ? 18.309 -24.728 0.337  1.00 16.43 ? 141 LEU   C N   1 
ATOM   2112 C  CA  . LEU   B 1 135 ? 18.973 -25.760 -0.479 1.00 17.41 ? 141 LEU   C CA  1 
ATOM   2113 C  C   . LEU   B 1 135 ? 20.464 -25.593 -0.546 1.00 18.66 ? 141 LEU   C C   1 
ATOM   2114 O  O   . LEU   B 1 135 ? 21.180 -26.582 -0.701 1.00 20.62 ? 141 LEU   C O   1 
ATOM   2115 C  CB  . LEU   B 1 135 ? 18.373 -25.853 -1.894 1.00 17.91 ? 141 LEU   C CB  1 
ATOM   2116 C  CG  . LEU   B 1 135 ? 16.849 -25.813 -1.967 1.00 18.97 ? 141 LEU   C CG  1 
ATOM   2117 C  CD1 . LEU   B 1 135 ? 16.385 -26.049 -3.385 1.00 19.79 ? 141 LEU   C CD1 1 
ATOM   2118 C  CD2 . LEU   B 1 135 ? 16.200 -26.886 -1.065 1.00 18.60 ? 141 LEU   C CD2 1 
ATOM   2119 N  N   . TRP   B 1 136 ? 20.938 -24.346 -0.414 1.00 18.74 ? 142 TRP   C N   1 
ATOM   2120 C  CA  . TRP   B 1 136 ? 22.369 -24.042 -0.497 1.00 19.76 ? 142 TRP   C CA  1 
ATOM   2121 C  C   . TRP   B 1 136 ? 23.196 -24.650 0.664  1.00 21.98 ? 142 TRP   C C   1 
ATOM   2122 O  O   . TRP   B 1 136 ? 24.422 -24.703 0.565  1.00 22.88 ? 142 TRP   C O   1 
ATOM   2123 C  CB  . TRP   B 1 136 ? 22.560 -22.516 -0.564 1.00 20.07 ? 142 TRP   C CB  1 
ATOM   2124 C  CG  . TRP   B 1 136 ? 21.886 -21.746 0.529  1.00 20.43 ? 142 TRP   C CG  1 
ATOM   2125 C  CD1 . TRP   B 1 136 ? 20.645 -21.176 0.505  1.00 21.25 ? 142 TRP   C CD1 1 
ATOM   2126 C  CD2 . TRP   B 1 136 ? 22.453 -21.430 1.813  1.00 19.94 ? 142 TRP   C CD2 1 
ATOM   2127 N  NE1 . TRP   B 1 136 ? 20.413 -20.511 1.694  1.00 21.37 ? 142 TRP   C NE1 1 
ATOM   2128 C  CE2 . TRP   B 1 136 ? 21.511 -20.658 2.507  1.00 20.59 ? 142 TRP   C CE2 1 
ATOM   2129 C  CE3 . TRP   B 1 136 ? 23.696 -21.700 2.425  1.00 20.70 ? 142 TRP   C CE3 1 
ATOM   2130 C  CZ2 . TRP   B 1 136 ? 21.749 -20.196 3.806  1.00 21.34 ? 142 TRP   C CZ2 1 
ATOM   2131 C  CZ3 . TRP   B 1 136 ? 23.951 -21.176 3.689  1.00 21.69 ? 142 TRP   C CZ3 1 
ATOM   2132 C  CH2 . TRP   B 1 136 ? 22.992 -20.417 4.351  1.00 21.53 ? 142 TRP   C CH2 1 
ATOM   2133 N  N   . LEU   B 1 137 ? 22.543 -25.142 1.735  1.00 21.71 ? 143 LEU   C N   1 
ATOM   2134 C  CA  . LEU   B 1 137 ? 23.299 -25.753 2.850  1.00 22.79 ? 143 LEU   C CA  1 
ATOM   2135 C  C   . LEU   B 1 137 ? 24.058 -27.007 2.383  1.00 27.67 ? 143 LEU   C C   1 
ATOM   2136 O  O   . LEU   B 1 137 ? 25.072 -27.354 2.994  1.00 28.67 ? 143 LEU   C O   1 
ATOM   2137 C  CB  . LEU   B 1 137 ? 22.349 -26.173 3.993  1.00 20.90 ? 143 LEU   C CB  1 
ATOM   2138 C  CG  . LEU   B 1 137 ? 21.778 -25.043 4.859  1.00 20.35 ? 143 LEU   C CG  1 
ATOM   2139 C  CD1 . LEU   B 1 137 ? 20.756 -25.606 5.863  1.00 20.00 ? 143 LEU   C CD1 1 
ATOM   2140 C  CD2 . LEU   B 1 137 ? 22.913 -24.298 5.640  1.00 20.29 ? 143 LEU   C CD2 1 
ATOM   2141 N  N   . ASP   B 1 138 ? 23.504 -27.700 1.354  1.00 30.44 ? 144 ASP   C N   1 
ATOM   2142 C  CA  . ASP   B 1 138 ? 23.956 -28.951 0.736  1.00 35.07 ? 144 ASP   C CA  1 
ATOM   2143 C  C   . ASP   B 1 138 ? 25.083 -28.800 -0.248 1.00 38.36 ? 144 ASP   C C   1 
ATOM   2144 O  O   . ASP   B 1 138 ? 25.547 -29.820 -0.743 1.00 39.49 ? 144 ASP   C O   1 
ATOM   2145 C  CB  . ASP   B 1 138 ? 22.803 -29.581 -0.066 1.00 38.00 ? 144 ASP   C CB  1 
ATOM   2146 C  CG  . ASP   B 1 138 ? 21.736 -30.264 0.738  1.00 42.65 ? 144 ASP   C CG  1 
ATOM   2147 O  OD1 . ASP   B 1 138 ? 22.010 -30.634 1.892  1.00 43.29 ? 144 ASP   C OD1 1 
ATOM   2148 O  OD2 . ASP   B 1 138 ? 20.613 -30.443 0.200  1.00 47.11 ? 144 ASP   C OD2 1 
ATOM   2149 N  N   . GLU   B 1 139 ? 25.435 -27.574 -0.652 1.00 39.92 ? 145 GLU   C N   1 
ATOM   2150 C  CA  . GLU   B 1 139 ? 26.509 -27.382 -1.632 1.00 42.13 ? 145 GLU   C CA  1 
ATOM   2151 C  C   . GLU   B 1 139 ? 27.629 -26.496 -1.095 1.00 42.93 ? 145 GLU   C C   1 
ATOM   2152 O  O   . GLU   B 1 139 ? 27.380 -25.615 -0.270 1.00 43.56 ? 145 GLU   C O   1 
ATOM   2153 C  CB  . GLU   B 1 139 ? 25.950 -26.821 -2.944 1.00 45.94 ? 145 GLU   C CB  1 
ATOM   2154 C  CG  . GLU   B 1 139 ? 25.128 -25.562 -2.767 1.00 52.73 ? 145 GLU   C CG  1 
ATOM   2155 C  CD  . GLU   B 1 139 ? 23.948 -25.482 -3.716 1.00 61.79 ? 145 GLU   C CD  1 
ATOM   2156 O  OE1 . GLU   B 1 139 ? 23.818 -24.456 -4.424 1.00 62.93 ? 145 GLU   C OE1 1 
ATOM   2157 O  OE2 . GLU   B 1 139 ? 23.153 -26.450 -3.750 1.00 64.65 ? 145 GLU   C OE2 1 
HETATM 2158 N  N1  . A1B4B C 2 .   ? 25.235 13.834  10.494 1.00 18.95 ? 201 A1B4B A N1  1 
HETATM 2159 C  C4  . A1B4B C 2 .   ? 24.181 14.520  9.730  1.00 18.51 ? 201 A1B4B A C4  1 
HETATM 2160 C  C5  . A1B4B C 2 .   ? 25.988 12.814  10.026 1.00 20.05 ? 201 A1B4B A C5  1 
HETATM 2161 C  C6  . A1B4B C 2 .   ? 25.630 12.306  8.641  1.00 22.88 ? 201 A1B4B A C6  1 
HETATM 2162 C  C7  . A1B4B C 2 .   ? 26.567 11.228  8.156  1.00 25.99 ? 201 A1B4B A C7  1 
HETATM 2163 C  C8  . A1B4B C 2 .   ? 27.654 11.590  7.360  1.00 26.87 ? 201 A1B4B A C8  1 
HETATM 2164 C  C10 . A1B4B C 2 .   ? 28.295 9.307   7.164  1.00 28.13 ? 201 A1B4B A C10 1 
HETATM 2165 C  C13 . A1B4B C 2 .   ? 25.404 14.294  11.876 1.00 18.22 ? 201 A1B4B A C13 1 
HETATM 2166 BR BR  . A1B4B C 2 .   ? 24.898 9.298   9.468  1.00 34.54 ? 201 A1B4B A BR  1 
HETATM 2167 C  C12 . A1B4B C 2 .   ? 26.377 9.876   8.419  1.00 28.84 ? 201 A1B4B A C12 1 
HETATM 2168 C  C11 . A1B4B C 2 .   ? 27.229 8.907   7.930  1.00 28.24 ? 201 A1B4B A C11 1 
HETATM 2169 F  F1  . A1B4B C 2 .   ? 29.186 8.397   6.704  1.00 29.52 ? 201 A1B4B A F1  1 
HETATM 2170 C  C9  . A1B4B C 2 .   ? 28.499 10.625  6.879  1.00 27.92 ? 201 A1B4B A C9  1 
HETATM 2171 F  F   . A1B4B C 2 .   ? 29.578 10.974  6.141  1.00 29.01 ? 201 A1B4B A F   1 
HETATM 2172 O  O1  . A1B4B C 2 .   ? 26.871 12.307  10.688 1.00 18.81 ? 201 A1B4B A O1  1 
HETATM 2173 C  C3  . A1B4B C 2 .   ? 22.849 14.446  10.456 1.00 18.40 ? 201 A1B4B A C3  1 
HETATM 2174 C  C2  . A1B4B C 2 .   ? 22.996 14.947  11.897 1.00 18.79 ? 201 A1B4B A C2  1 
HETATM 2175 C  C1  . A1B4B C 2 .   ? 24.082 14.139  12.633 1.00 18.14 ? 201 A1B4B A C1  1 
HETATM 2176 C  C   . A1B4B C 2 .   ? 24.261 14.608  14.066 1.00 18.32 ? 201 A1B4B A C   1 
HETATM 2177 O  O   . A1B4B C 2 .   ? 24.721 15.725  14.318 1.00 18.64 ? 201 A1B4B A O   1 
HETATM 2178 N  N   . A1B4B C 2 .   ? 23.963 13.718  15.003 1.00 17.73 ? 201 A1B4B A N   1 
HETATM 2179 ZN ZN  . ZN    D 3 .   ? 23.220 -5.543  27.027 1.00 19.26 2 202 ZN    A ZN  1 
HETATM 2180 S  S   . DMS   E 4 .   ? 15.260 -0.312  12.273 1.00 50.14 ? 203 DMS   A S   1 
HETATM 2181 O  O   . DMS   E 4 .   ? 16.604 -0.630  12.761 1.00 48.23 ? 203 DMS   A O   1 
HETATM 2182 C  C1  . DMS   E 4 .   ? 15.276 0.406   10.605 1.00 50.28 ? 203 DMS   A C1  1 
HETATM 2183 C  C2  . DMS   E 4 .   ? 14.554 1.150   13.123 1.00 49.65 ? 203 DMS   A C2  1 
HETATM 2184 N  N1  . A1B4B F 2 .   ? 10.868 -16.811 22.661 1.00 17.79 ? 201 A1B4B C N1  1 
HETATM 2185 C  C4  . A1B4B F 2 .   ? 11.973 -16.131 23.362 1.00 17.82 ? 201 A1B4B C C4  1 
HETATM 2186 C  C5  . A1B4B F 2 .   ? 10.101 -17.812 23.161 1.00 20.14 ? 201 A1B4B C C5  1 
HETATM 2187 C  C6  . A1B4B F 2 .   ? 10.515 -18.370 24.510 1.00 23.44 ? 201 A1B4B C C6  1 
HETATM 2188 C  C7  . A1B4B F 2 .   ? 9.551  -19.421 25.022 1.00 27.53 ? 201 A1B4B C C7  1 
HETATM 2189 C  C8  . A1B4B F 2 .   ? 8.560  -19.049 25.931 1.00 28.41 ? 201 A1B4B C C8  1 
HETATM 2190 C  C10 . A1B4B F 2 .   ? 7.785  -21.291 26.071 1.00 30.41 ? 201 A1B4B C C10 1 
HETATM 2191 C  C13 . A1B4B F 2 .   ? 10.627 -16.326 21.300 1.00 15.64 ? 201 A1B4B C C13 1 
HETATM 2192 BR BR  . A1B4B F 2 .   ? 10.987 -21.395 23.518 1.00 36.22 ? 201 A1B4B C BR  1 
HETATM 2193 C  C12 . A1B4B F 2 .   ? 9.632  -20.771 24.691 1.00 30.73 ? 201 A1B4B C C12 1 
HETATM 2194 C  C11 . A1B4B F 2 .   ? 8.765  -21.715 25.216 1.00 30.37 ? 201 A1B4B C C11 1 
HETATM 2195 F  F1  . A1B4B F 2 .   ? 6.808  -22.143 26.461 1.00 30.78 ? 201 A1B4B C F1  1 
HETATM 2196 C  C9  . A1B4B F 2 .   ? 7.693  -19.991 26.434 1.00 30.19 ? 201 A1B4B C C9  1 
HETATM 2197 F  F   . A1B4B F 2 .   ? 6.664  -19.614 27.228 1.00 32.05 ? 201 A1B4B C F   1 
HETATM 2198 O  O1  . A1B4B F 2 .   ? 9.136  -18.266 22.551 1.00 18.70 ? 201 A1B4B C O1  1 
HETATM 2199 C  C3  . A1B4B F 2 .   ? 13.267 -16.243 22.558 1.00 16.71 ? 201 A1B4B C C3  1 
HETATM 2200 C  C2  . A1B4B F 2 .   ? 13.054 -15.744 21.126 1.00 15.81 ? 201 A1B4B C C2  1 
HETATM 2201 C  C1  . A1B4B F 2 .   ? 11.894 -16.515 20.456 1.00 15.66 ? 201 A1B4B C C1  1 
HETATM 2202 C  C   . A1B4B F 2 .   ? 11.624 -16.007 19.050 1.00 16.31 ? 201 A1B4B C C   1 
HETATM 2203 O  O   . A1B4B F 2 .   ? 11.202 -14.854 18.860 1.00 15.44 ? 201 A1B4B C O   1 
HETATM 2204 N  N   . A1B4B F 2 .   ? 11.787 -16.898 18.080 1.00 16.67 ? 201 A1B4B C N   1 
HETATM 2205 ZN ZN  . ZN    G 3 .   ? 10.619 -35.756 5.627  1.00 16.10 2 202 ZN    C ZN  1 
HETATM 2206 S  S   . DMS   H 4 .   ? 14.211 -10.612 7.087  1.00 87.45 ? 203 DMS   C S   1 
HETATM 2207 O  O   . DMS   H 4 .   ? 14.327 -9.935  8.427  1.00 87.22 ? 203 DMS   C O   1 
HETATM 2208 C  C1  . DMS   H 4 .   ? 12.726 -9.980  6.252  1.00 87.45 ? 203 DMS   C C1  1 
HETATM 2209 C  C2  . DMS   H 4 .   ? 15.411 -9.838  5.965  1.00 87.50 ? 203 DMS   C C2  1 
HETATM 2210 O  O   . HOH   I 5 .   ? 7.140  7.251   31.653 1.00 35.07 ? 301 HOH   A O   1 
HETATM 2211 O  O   . HOH   I 5 .   ? 14.849 22.271  24.522 1.00 23.02 ? 302 HOH   A O   1 
HETATM 2212 O  O   . HOH   I 5 .   ? 22.480 6.815   1.575  1.00 34.88 ? 303 HOH   A O   1 
HETATM 2213 O  O   . HOH   I 5 .   ? 23.822 7.306   28.185 1.00 24.75 ? 304 HOH   A O   1 
HETATM 2214 O  O   . HOH   I 5 .   ? 6.803  -2.031  24.142 1.00 35.52 ? 305 HOH   A O   1 
HETATM 2215 O  O   . HOH   I 5 .   ? 31.773 7.180   23.118 1.00 39.61 ? 306 HOH   A O   1 
HETATM 2216 O  O   . HOH   I 5 .   ? 14.472 -5.517  26.919 1.00 30.56 ? 307 HOH   A O   1 
HETATM 2217 O  O   . HOH   I 5 .   ? 6.147  -4.535  23.309 1.00 47.67 ? 308 HOH   A O   1 
HETATM 2218 O  O   . HOH   I 5 .   ? 11.678 -1.812  27.948 1.00 26.28 ? 309 HOH   A O   1 
HETATM 2219 O  O   . HOH   I 5 .   ? 12.897 -4.610  20.537 1.00 38.32 ? 310 HOH   A O   1 
HETATM 2220 O  O   . HOH   I 5 .   ? 37.198 7.443   4.069  1.00 41.57 ? 311 HOH   A O   1 
HETATM 2221 O  O   . HOH   I 5 .   ? 24.950 24.036  10.713 1.00 43.32 ? 312 HOH   A O   1 
HETATM 2222 O  O   . HOH   I 5 .   ? 20.932 10.294  32.315 1.00 35.71 ? 313 HOH   A O   1 
HETATM 2223 O  O   . HOH   I 5 .   ? -1.842 15.600  20.397 1.00 28.75 ? 314 HOH   A O   1 
HETATM 2224 O  O   . HOH   I 5 .   ? 15.079 8.617   13.416 1.00 16.11 ? 315 HOH   A O   1 
HETATM 2225 O  O   . HOH   I 5 .   ? 11.198 21.370  24.670 1.00 28.42 ? 316 HOH   A O   1 
HETATM 2226 O  O   . HOH   I 5 .   ? 31.069 -2.040  29.795 1.00 43.29 ? 317 HOH   A O   1 
HETATM 2227 O  O   . HOH   I 5 .   ? 19.010 -11.582 27.314 1.00 35.19 ? 318 HOH   A O   1 
HETATM 2228 O  O   . HOH   I 5 .   ? 17.168 20.715  22.893 1.00 23.33 ? 319 HOH   A O   1 
HETATM 2229 O  O   . HOH   I 5 .   ? 35.032 13.913  16.319 1.00 32.82 ? 320 HOH   A O   1 
HETATM 2230 O  O   . HOH   I 5 .   ? 28.312 -6.309  3.494  1.00 27.18 ? 321 HOH   A O   1 
HETATM 2231 O  O   . HOH   I 5 .   ? 29.997 6.969   4.316  1.00 33.11 ? 322 HOH   A O   1 
HETATM 2232 O  O   . HOH   I 5 .   ? 24.126 3.900   29.245 1.00 26.04 ? 323 HOH   A O   1 
HETATM 2233 O  O   . HOH   I 5 .   ? 18.677 13.307  6.484  1.00 42.61 ? 324 HOH   A O   1 
HETATM 2234 O  O   . HOH   I 5 .   ? 6.316  3.157   28.930 1.00 44.82 ? 325 HOH   A O   1 
HETATM 2235 O  O   . HOH   I 5 .   ? 29.157 13.505  11.512 1.00 34.33 ? 326 HOH   A O   1 
HETATM 2236 O  O   . HOH   I 5 .   ? 32.180 2.711   5.031  1.00 28.82 ? 327 HOH   A O   1 
HETATM 2237 O  O   . HOH   I 5 .   ? 15.987 -0.557  4.979  1.00 33.55 ? 328 HOH   A O   1 
HETATM 2238 O  O   . HOH   I 5 .   ? 31.220 12.703  9.214  1.00 40.57 ? 329 HOH   A O   1 
HETATM 2239 O  O   . HOH   I 5 .   ? 6.980  15.538  29.246 1.00 41.90 ? 330 HOH   A O   1 
HETATM 2240 O  O   . HOH   I 5 .   ? 34.557 -0.874  16.610 1.00 15.53 ? 331 HOH   A O   1 
HETATM 2241 O  O   . HOH   I 5 .   ? 25.656 17.825  12.788 1.00 19.24 ? 332 HOH   A O   1 
HETATM 2242 O  O   . HOH   I 5 .   ? 22.348 -5.953  0.540  1.00 41.17 ? 333 HOH   A O   1 
HETATM 2243 O  O   . HOH   I 5 .   ? 27.203 19.040  15.007 1.00 20.52 ? 334 HOH   A O   1 
HETATM 2244 O  O   . HOH   I 5 .   ? 23.625 10.959  21.437 1.00 15.71 ? 335 HOH   A O   1 
HETATM 2245 O  O   . HOH   I 5 .   ? 5.086  11.027  12.672 1.00 39.23 ? 336 HOH   A O   1 
HETATM 2246 O  O   . HOH   I 5 .   ? 12.471 17.895  13.124 1.00 37.14 ? 337 HOH   A O   1 
HETATM 2247 O  O   . HOH   I 5 .   ? 23.039 20.803  20.375 1.00 24.88 ? 338 HOH   A O   1 
HETATM 2248 O  O   . HOH   I 5 .   ? 23.652 1.774   -0.892 1.00 17.39 ? 339 HOH   A O   1 
HETATM 2249 O  O   . HOH   I 5 .   ? 11.164 -0.163  15.863 1.00 24.39 ? 340 HOH   A O   1 
HETATM 2250 O  O   . HOH   I 5 .   ? 11.334 10.829  10.057 1.00 54.67 ? 341 HOH   A O   1 
HETATM 2251 O  O   . HOH   I 5 .   ? 20.439 2.239   9.346  1.00 16.58 ? 342 HOH   A O   1 
HETATM 2252 O  O   . HOH   I 5 .   ? 30.981 5.282   7.786  1.00 23.87 ? 343 HOH   A O   1 
HETATM 2253 O  O   . HOH   I 5 .   ? 13.647 18.727  14.771 1.00 32.24 ? 344 HOH   A O   1 
HETATM 2254 O  O   . HOH   I 5 .   ? 4.144  20.017  21.692 1.00 31.26 ? 345 HOH   A O   1 
HETATM 2255 O  O   . HOH   I 5 .   ? 25.141 4.081   -1.413 1.00 24.35 ? 346 HOH   A O   1 
HETATM 2256 O  O   . HOH   I 5 .   ? 16.514 18.618  27.131 1.00 44.26 ? 347 HOH   A O   1 
HETATM 2257 O  O   . HOH   I 5 .   ? 5.064  3.098   21.033 1.00 23.18 ? 348 HOH   A O   1 
HETATM 2258 O  O   . HOH   I 5 .   ? 16.742 -7.186  29.350 1.00 33.95 ? 349 HOH   A O   1 
HETATM 2259 O  O   . HOH   I 5 .   ? 35.081 14.905  25.236 1.00 44.18 ? 350 HOH   A O   1 
HETATM 2260 O  O   . HOH   I 5 .   ? 16.975 4.648   5.848  1.00 27.99 ? 351 HOH   A O   1 
HETATM 2261 O  O   . HOH   I 5 .   ? 24.247 8.346   1.351  1.00 29.03 ? 352 HOH   A O   1 
HETATM 2262 O  O   . HOH   I 5 .   ? 4.118  10.239  17.983 1.00 38.32 ? 353 HOH   A O   1 
HETATM 2263 O  O   . HOH   I 5 .   ? 24.424 14.392  30.362 1.00 54.57 ? 354 HOH   A O   1 
HETATM 2264 O  O   . HOH   I 5 .   ? 4.287  4.083   28.170 1.00 38.84 ? 355 HOH   A O   1 
HETATM 2265 O  O   . HOH   I 5 .   ? 21.938 -5.449  33.763 1.00 31.85 ? 356 HOH   A O   1 
HETATM 2266 O  O   . HOH   I 5 .   ? 25.032 -8.742  24.750 1.00 35.08 ? 357 HOH   A O   1 
HETATM 2267 O  O   . HOH   I 5 .   ? 29.790 25.871  15.987 1.00 40.69 ? 358 HOH   A O   1 
HETATM 2268 O  O   . HOH   I 5 .   ? 11.796 13.121  8.693  1.00 46.90 ? 359 HOH   A O   1 
HETATM 2269 O  O   . HOH   I 5 .   ? 34.871 -6.450  21.559 1.00 42.39 ? 360 HOH   A O   1 
HETATM 2270 O  O   . HOH   I 5 .   ? 2.821  8.543   26.129 1.00 31.63 ? 361 HOH   A O   1 
HETATM 2271 O  O   . HOH   I 5 .   ? 20.113 12.025  8.515  1.00 22.47 ? 362 HOH   A O   1 
HETATM 2272 O  O   . HOH   I 5 .   ? 28.136 3.085   -0.300 1.00 26.93 ? 363 HOH   A O   1 
HETATM 2273 O  O   . HOH   I 5 .   ? 34.567 3.563   26.178 1.00 30.20 ? 364 HOH   A O   1 
HETATM 2274 O  O   . HOH   I 5 .   ? 29.806 -2.368  8.320  1.00 28.58 ? 365 HOH   A O   1 
HETATM 2275 O  O   . HOH   I 5 .   ? 17.504 2.284   9.286  1.00 23.20 ? 366 HOH   A O   1 
HETATM 2276 O  O   . HOH   I 5 .   ? 25.603 1.634   29.925 1.00 25.70 ? 367 HOH   A O   1 
HETATM 2277 O  O   . HOH   I 5 .   ? 21.673 9.871   23.360 1.00 14.99 ? 368 HOH   A O   1 
HETATM 2278 O  O   . HOH   I 5 .   ? 17.283 18.503  15.597 1.00 16.74 ? 369 HOH   A O   1 
HETATM 2279 O  O   . HOH   I 5 .   ? 20.002 -5.132  15.472 1.00 27.00 ? 370 HOH   A O   1 
HETATM 2280 O  O   . HOH   I 5 .   ? 28.455 0.788   26.740 1.00 21.17 ? 371 HOH   A O   1 
HETATM 2281 O  O   . HOH   I 5 .   ? 30.286 -5.945  26.242 1.00 32.63 ? 372 HOH   A O   1 
HETATM 2282 O  O   . HOH   I 5 .   ? 35.639 14.527  20.309 1.00 26.77 ? 373 HOH   A O   1 
HETATM 2283 O  O   . HOH   I 5 .   ? 3.574  18.181  23.706 1.00 38.74 ? 374 HOH   A O   1 
HETATM 2284 O  O   . HOH   I 5 .   ? 28.171 16.274  10.555 1.00 33.50 ? 375 HOH   A O   1 
HETATM 2285 O  O   . HOH   I 5 .   ? 16.854 9.049   6.765  1.00 23.73 ? 376 HOH   A O   1 
HETATM 2286 O  O   . HOH   I 5 .   ? 16.186 -3.361  13.671 1.00 43.03 ? 377 HOH   A O   1 
HETATM 2287 O  O   . HOH   I 5 .   ? 19.469 -5.988  32.919 1.00 42.79 ? 378 HOH   A O   1 
HETATM 2288 O  O   . HOH   I 5 .   ? 4.155  20.448  15.425 1.00 40.89 ? 379 HOH   A O   1 
HETATM 2289 O  O   . HOH   I 5 .   ? 32.281 8.771   4.825  1.00 34.61 ? 380 HOH   A O   1 
HETATM 2290 O  O   . HOH   I 5 .   ? 20.530 20.474  24.344 1.00 36.18 ? 381 HOH   A O   1 
HETATM 2291 O  O   . HOH   I 5 .   ? 33.033 -2.767  15.256 1.00 22.14 ? 382 HOH   A O   1 
HETATM 2292 O  O   . HOH   I 5 .   ? 31.931 14.736  12.800 1.00 29.50 ? 383 HOH   A O   1 
HETATM 2293 O  O   . HOH   I 5 .   ? 25.813 -8.273  22.763 1.00 41.16 ? 384 HOH   A O   1 
HETATM 2294 O  O   . HOH   I 5 .   ? 30.602 -3.173  12.024 1.00 25.99 ? 385 HOH   A O   1 
HETATM 2295 O  O   . HOH   I 5 .   ? 9.014  3.994   11.813 1.00 38.71 ? 386 HOH   A O   1 
HETATM 2296 O  O   . HOH   I 5 .   ? 12.155 -2.671  15.898 1.00 36.03 ? 387 HOH   A O   1 
HETATM 2297 O  O   . HOH   I 5 .   ? 17.134 0.581   2.702  1.00 31.29 ? 388 HOH   A O   1 
HETATM 2298 O  O   . HOH   I 5 .   ? 29.991 6.285   29.955 1.00 37.67 ? 389 HOH   A O   1 
HETATM 2299 O  O   . HOH   I 5 .   ? 15.846 11.955  30.847 1.00 36.39 ? 390 HOH   A O   1 
HETATM 2300 O  O   . HOH   I 5 .   ? 26.966 19.177  24.669 1.00 43.10 ? 391 HOH   A O   1 
HETATM 2301 O  O   . HOH   I 5 .   ? 27.983 11.923  27.552 1.00 23.43 ? 392 HOH   A O   1 
HETATM 2302 O  O   . HOH   I 5 .   ? 18.167 -5.231  30.568 1.00 30.50 ? 393 HOH   A O   1 
HETATM 2303 O  O   . HOH   I 5 .   ? 17.840 16.653  28.752 1.00 46.24 ? 394 HOH   A O   1 
HETATM 2304 O  O   . HOH   I 5 .   ? 25.142 -5.196  32.538 1.00 43.85 ? 395 HOH   A O   1 
HETATM 2305 O  O   . HOH   I 5 .   ? 17.840 20.022  13.484 1.00 23.67 ? 396 HOH   A O   1 
HETATM 2306 O  O   . HOH   I 5 .   ? 28.936 22.026  22.145 1.00 31.88 ? 397 HOH   A O   1 
HETATM 2307 O  O   . HOH   I 5 .   ? 24.082 17.808  6.283  1.00 40.62 ? 398 HOH   A O   1 
HETATM 2308 O  O   . HOH   I 5 .   ? 20.087 13.865  29.066 1.00 31.13 ? 399 HOH   A O   1 
HETATM 2309 O  O   . HOH   I 5 .   ? 20.329 23.457  14.878 1.00 51.85 ? 400 HOH   A O   1 
HETATM 2310 O  O   . HOH   I 5 .   ? 18.319 -3.735  14.751 1.00 33.95 ? 401 HOH   A O   1 
HETATM 2311 O  O   . HOH   I 5 .   ? 29.417 25.726  13.303 1.00 32.74 ? 402 HOH   A O   1 
HETATM 2312 O  O   . HOH   I 5 .   ? 32.810 12.184  27.744 1.00 33.32 ? 403 HOH   A O   1 
HETATM 2313 O  O   . HOH   I 5 .   ? 13.394 8.577   11.113 1.00 20.85 ? 404 HOH   A O   1 
HETATM 2314 O  O   . HOH   I 5 .   ? 12.370 18.486  26.507 1.00 31.13 ? 405 HOH   A O   1 
HETATM 2315 O  O   . HOH   I 5 .   ? 25.563 20.529  22.186 1.00 43.26 ? 406 HOH   A O   1 
HETATM 2316 O  O   . HOH   I 5 .   ? 29.993 -2.317  3.459  1.00 42.85 ? 407 HOH   A O   1 
HETATM 2317 O  O   . HOH   I 5 .   ? 32.227 22.242  11.321 1.00 34.73 ? 408 HOH   A O   1 
HETATM 2318 O  O   . HOH   I 5 .   ? 19.745 9.563   7.961  1.00 26.82 ? 409 HOH   A O   1 
HETATM 2319 O  O   . HOH   I 5 .   ? 3.878  14.749  10.556 1.00 27.01 ? 410 HOH   A O   1 
HETATM 2320 O  O   . HOH   I 5 .   ? 6.638  16.210  8.965  1.00 34.64 ? 411 HOH   A O   1 
HETATM 2321 O  O   . HOH   I 5 .   ? 3.471  2.432   18.986 1.00 32.55 ? 412 HOH   A O   1 
HETATM 2322 O  O   . HOH   I 5 .   ? 4.599  10.545  15.104 1.00 46.11 ? 413 HOH   A O   1 
HETATM 2323 O  O   . HOH   I 5 .   ? 11.232 2.173   12.386 1.00 30.64 ? 414 HOH   A O   1 
HETATM 2324 O  O   . HOH   I 5 .   ? 16.925 7.370   4.526  1.00 38.70 ? 415 HOH   A O   1 
HETATM 2325 O  O   . HOH   I 5 .   ? 14.496 -4.034  16.168 1.00 33.90 ? 416 HOH   A O   1 
HETATM 2326 O  O   . HOH   I 5 .   ? 15.287 23.246  16.956 1.00 27.62 ? 417 HOH   A O   1 
HETATM 2327 O  O   . HOH   I 5 .   ? 0.941  17.506  23.343 1.00 52.38 ? 418 HOH   A O   1 
HETATM 2328 O  O   . HOH   I 5 .   ? 26.606 -6.590  29.849 1.00 37.06 ? 419 HOH   A O   1 
HETATM 2329 O  O   . HOH   I 5 .   ? 32.875 5.319   4.612  1.00 49.42 ? 420 HOH   A O   1 
HETATM 2330 O  O   . HOH   I 5 .   ? 22.287 -8.656  19.479 1.00 38.79 ? 421 HOH   A O   1 
HETATM 2331 O  O   . HOH   I 5 .   ? 15.988 8.418   33.910 1.00 36.93 ? 422 HOH   A O   1 
HETATM 2332 O  O   . HOH   I 5 .   ? 19.703 -9.828  20.462 1.00 35.96 ? 423 HOH   A O   1 
HETATM 2333 O  O   . HOH   I 5 .   ? 31.713 -7.336  17.825 1.00 47.73 ? 424 HOH   A O   1 
HETATM 2334 O  O   . HOH   I 5 .   ? 2.464  14.435  25.129 1.00 52.10 ? 425 HOH   A O   1 
HETATM 2335 O  O   . HOH   I 5 .   ? 8.884  18.088  9.117  1.00 57.11 ? 426 HOH   A O   1 
HETATM 2336 O  O   . HOH   I 5 .   ? 26.506 22.048  6.089  1.00 55.50 ? 427 HOH   A O   1 
HETATM 2337 O  O   . HOH   I 5 .   ? 22.323 11.960  7.389  1.00 47.88 ? 428 HOH   A O   1 
HETATM 2338 O  O   . HOH   I 5 .   ? 33.122 0.563   6.106  1.00 32.51 ? 429 HOH   A O   1 
HETATM 2339 O  O   . HOH   I 5 .   ? 13.913 21.610  14.922 1.00 29.37 ? 430 HOH   A O   1 
HETATM 2340 O  O   . HOH   I 5 .   ? 18.150 13.059  30.452 1.00 55.83 ? 431 HOH   A O   1 
HETATM 2341 O  O   . HOH   I 5 .   ? 30.924 -3.053  5.813  1.00 37.80 ? 432 HOH   A O   1 
HETATM 2342 O  O   . HOH   I 5 .   ? 2.057  21.293  8.748  1.00 50.47 ? 433 HOH   A O   1 
HETATM 2343 O  O   . HOH   I 5 .   ? 33.809 -2.306  9.239  1.00 27.76 ? 434 HOH   A O   1 
HETATM 2344 O  O   . HOH   I 5 .   ? 1.922  16.289  9.321  1.00 45.02 ? 435 HOH   A O   1 
HETATM 2345 O  O   . HOH   I 5 .   ? 2.229  21.085  12.365 1.00 44.48 ? 436 HOH   A O   1 
HETATM 2346 O  O   . HOH   I 5 .   ? 32.355 11.391  5.443  1.00 49.52 ? 437 HOH   A O   1 
HETATM 2347 O  O   . HOH   I 5 .   ? 28.227 1.624   29.440 1.00 34.47 ? 438 HOH   A O   1 
HETATM 2348 O  O   . HOH   I 5 .   ? 8.843  -2.754  27.715 1.00 48.20 ? 439 HOH   A O   1 
HETATM 2349 O  O   . HOH   I 5 .   ? 23.244 14.271  6.288  1.00 52.96 ? 440 HOH   A O   1 
HETATM 2350 O  O   . HOH   I 5 .   ? -4.913 5.864   15.172 1.00 57.97 ? 441 HOH   A O   1 
HETATM 2351 O  O   . HOH   I 5 .   ? 9.419  21.822  12.462 1.00 35.36 ? 442 HOH   A O   1 
HETATM 2352 O  O   . HOH   I 5 .   ? 34.995 11.596  15.320 1.00 47.15 ? 443 HOH   A O   1 
HETATM 2353 O  O   . HOH   I 5 .   ? 16.213 20.503  11.477 1.00 40.87 ? 444 HOH   A O   1 
HETATM 2354 O  O   . HOH   I 5 .   ? 13.027 10.028  8.471  1.00 37.05 ? 445 HOH   A O   1 
HETATM 2355 O  O   . HOH   I 5 .   ? 2.786  3.961   17.047 1.00 38.41 ? 446 HOH   A O   1 
HETATM 2356 O  O   . HOH   I 5 .   ? 31.431 -3.932  9.663  1.00 28.50 ? 447 HOH   A O   1 
HETATM 2357 O  O   . HOH   I 5 .   ? 6.646  19.354  28.197 1.00 62.73 ? 448 HOH   A O   1 
HETATM 2358 O  O   . HOH   I 5 .   ? 4.698  1.046   14.744 1.00 57.78 ? 449 HOH   A O   1 
HETATM 2359 O  O   . HOH   I 5 .   ? 25.908 14.803  5.972  1.00 48.71 ? 450 HOH   A O   1 
HETATM 2360 O  O   . HOH   I 5 .   ? 29.503 20.747  25.310 1.00 54.76 ? 451 HOH   A O   1 
HETATM 2361 O  O   . HOH   I 5 .   ? 0.515  18.097  28.472 1.00 60.51 ? 452 HOH   A O   1 
HETATM 2362 O  O   . HOH   J 5 .   ? 20.299 -8.480  7.741  1.00 28.03 ? 301 HOH   C O   1 
HETATM 2363 O  O   . HOH   J 5 .   ? 2.652  -23.083 10.447 1.00 34.48 ? 302 HOH   C O   1 
HETATM 2364 O  O   . HOH   J 5 .   ? 30.765 -10.707 10.261 1.00 44.29 ? 303 HOH   C O   1 
HETATM 2365 O  O   . HOH   J 5 .   ? 6.522  -23.682 28.928 1.00 50.86 ? 304 HOH   C O   1 
HETATM 2366 O  O   . HOH   J 5 .   ? 35.714 -15.348 15.799 1.00 37.37 ? 305 HOH   C O   1 
HETATM 2367 O  O   . HOH   J 5 .   ? 23.697 -31.321 14.993 1.00 29.44 ? 306 HOH   C O   1 
HETATM 2368 O  O   . HOH   J 5 .   ? 10.217 -23.019 4.807  1.00 26.29 ? 307 HOH   C O   1 
HETATM 2369 O  O   . HOH   J 5 .   ? 26.507 -23.193 -0.309 1.00 41.88 ? 308 HOH   C O   1 
HETATM 2370 O  O   . HOH   J 5 .   ? 10.539 -27.581 33.780 1.00 36.40 ? 309 HOH   C O   1 
HETATM 2371 O  O   . HOH   J 5 .   ? 23.880 -9.288  7.847  1.00 24.13 ? 310 HOH   C O   1 
HETATM 2372 O  O   . HOH   J 5 .   ? 17.063 -37.753 3.029  1.00 36.16 ? 311 HOH   C O   1 
HETATM 2373 O  O   . HOH   J 5 .   ? 4.396  -36.216 21.696 1.00 33.73 ? 312 HOH   C O   1 
HETATM 2374 O  O   . HOH   J 5 .   ? 27.558 -27.783 2.173  1.00 41.29 ? 313 HOH   C O   1 
HETATM 2375 O  O   . HOH   J 5 .   ? 20.512 -22.433 18.645 1.00 16.57 ? 314 HOH   C O   1 
HETATM 2376 O  O   . HOH   J 5 .   ? 5.142  -25.391 24.706 1.00 36.63 ? 315 HOH   C O   1 
HETATM 2377 O  O   . HOH   J 5 .   ? 15.783 -22.030 -1.599 1.00 40.82 ? 316 HOH   C O   1 
HETATM 2378 O  O   . HOH   J 5 .   ? 34.371 -11.006 10.557 1.00 46.36 ? 317 HOH   C O   1 
HETATM 2379 O  O   . HOH   J 5 .   ? 12.048 -20.532 0.479  1.00 33.30 ? 318 HOH   C O   1 
HETATM 2380 O  O   . HOH   J 5 .   ? 10.591 -12.758 20.558 1.00 18.34 ? 319 HOH   C O   1 
HETATM 2381 O  O   . HOH   J 5 .   ? 9.868  -26.285 3.616  1.00 20.80 ? 320 HOH   C O   1 
HETATM 2382 O  O   . HOH   J 5 .   ? 22.139 -32.593 3.724  1.00 29.49 ? 321 HOH   C O   1 
HETATM 2383 O  O   . HOH   J 5 .   ? 4.958  -31.107 -1.828 1.00 36.49 ? 322 HOH   C O   1 
HETATM 2384 O  O   . HOH   J 5 .   ? 24.733 -20.650 20.427 1.00 41.02 ? 323 HOH   C O   1 
HETATM 2385 O  O   . HOH   J 5 .   ? 12.355 -29.480 33.671 1.00 22.13 ? 324 HOH   C O   1 
HETATM 2386 O  O   . HOH   J 5 .   ? 22.145 -12.396 17.212 1.00 27.13 ? 325 HOH   C O   1 
HETATM 2387 O  O   . HOH   J 5 .   ? 5.401  -17.701 24.964 1.00 36.48 ? 326 HOH   C O   1 
HETATM 2388 O  O   . HOH   J 5 .   ? 22.870 -36.226 12.295 1.00 46.70 ? 327 HOH   C O   1 
HETATM 2389 O  O   . HOH   J 5 .   ? 33.079 -16.934 6.845  1.00 50.22 ? 328 HOH   C O   1 
HETATM 2390 O  O   . HOH   J 5 .   ? 11.530 -14.153 5.689  1.00 61.77 ? 329 HOH   C O   1 
HETATM 2391 O  O   . HOH   J 5 .   ? 0.827  -16.710 17.926 1.00 29.47 ? 330 HOH   C O   1 
HETATM 2392 O  O   . HOH   J 5 .   ? 8.368  -28.484 3.012  1.00 22.13 ? 331 HOH   C O   1 
HETATM 2393 O  O   . HOH   J 5 .   ? 17.923 -10.033 9.417  1.00 22.83 ? 332 HOH   C O   1 
HETATM 2394 O  O   . HOH   J 5 .   ? 30.895 -21.286 13.041 1.00 32.95 ? 333 HOH   C O   1 
HETATM 2395 O  O   . HOH   J 5 .   ? 0.890  -31.688 17.105 1.00 16.35 ? 334 HOH   C O   1 
HETATM 2396 O  O   . HOH   J 5 .   ? 17.852 -7.654  21.550 1.00 21.91 ? 335 HOH   C O   1 
HETATM 2397 O  O   . HOH   J 5 .   ? 3.769  -23.539 3.715  1.00 29.14 ? 336 HOH   C O   1 
HETATM 2398 O  O   . HOH   J 5 .   ? 29.492 -28.027 9.896  1.00 27.62 ? 337 HOH   C O   1 
HETATM 2399 O  O   . HOH   J 5 .   ? 11.377 -19.602 11.552 1.00 16.35 ? 338 HOH   C O   1 
HETATM 2400 O  O   . HOH   J 5 .   ? 4.178  -8.622  22.789 1.00 33.90 ? 339 HOH   C O   1 
HETATM 2401 O  O   . HOH   J 5 .   ? 18.169 -12.047 5.408  1.00 35.58 ? 340 HOH   C O   1 
HETATM 2402 O  O   . HOH   J 5 .   ? 18.269 -28.689 23.004 1.00 25.48 ? 341 HOH   C O   1 
HETATM 2403 O  O   . HOH   J 5 .   ? 10.202 -40.617 0.904  1.00 46.88 ? 342 HOH   C O   1 
HETATM 2404 O  O   . HOH   J 5 .   ? 11.251 -35.932 -0.520 1.00 34.67 ? 343 HOH   C O   1 
HETATM 2405 O  O   . HOH   J 5 .   ? 2.704  -31.351 3.831  1.00 33.56 ? 344 HOH   C O   1 
HETATM 2406 O  O   . HOH   J 5 .   ? 7.917  -5.517  14.590 1.00 35.22 ? 345 HOH   C O   1 
HETATM 2407 O  O   . HOH   J 5 .   ? 8.857  -11.474 18.504 1.00 17.92 ? 346 HOH   C O   1 
HETATM 2408 O  O   . HOH   J 5 .   ? 21.557 -36.702 9.962  1.00 32.34 ? 347 HOH   C O   1 
HETATM 2409 O  O   . HOH   J 5 .   ? 27.695 -15.139 2.503  1.00 44.72 ? 348 HOH   C O   1 
HETATM 2410 O  O   . HOH   J 5 .   ? 15.366 -28.716 23.130 1.00 18.91 ? 349 HOH   C O   1 
HETATM 2411 O  O   . HOH   J 5 .   ? 7.021  -37.042 29.301 1.00 34.47 ? 350 HOH   C O   1 
HETATM 2412 O  O   . HOH   J 5 .   ? 23.567 -12.939 19.223 1.00 35.33 ? 351 HOH   C O   1 
HETATM 2413 O  O   . HOH   J 5 .   ? 6.927  -16.545 22.596 1.00 33.25 ? 352 HOH   C O   1 
HETATM 2414 O  O   . HOH   J 5 .   ? 16.274 -38.759 10.473 1.00 55.28 ? 353 HOH   C O   1 
HETATM 2415 O  O   . HOH   J 5 .   ? 12.664 -6.253  22.194 1.00 25.80 ? 354 HOH   C O   1 
HETATM 2416 O  O   . HOH   J 5 .   ? 17.492 -17.574 26.087 1.00 42.40 ? 355 HOH   C O   1 
HETATM 2417 O  O   . HOH   J 5 .   ? 1.131  -29.602 24.844 1.00 34.52 ? 356 HOH   C O   1 
HETATM 2418 O  O   . HOH   J 5 .   ? 13.058 -20.760 9.418  1.00 15.91 ? 357 HOH   C O   1 
HETATM 2419 O  O   . HOH   J 5 .   ? 31.350 -10.760 16.307 1.00 29.50 ? 358 HOH   C O   1 
HETATM 2420 O  O   . HOH   J 5 .   ? 13.141 -12.278 26.937 1.00 35.21 ? 359 HOH   C O   1 
HETATM 2421 O  O   . HOH   J 5 .   ? 18.471 -12.419 16.867 1.00 18.39 ? 360 HOH   C O   1 
HETATM 2422 O  O   . HOH   J 5 .   ? 15.831 -21.374 24.664 1.00 37.55 ? 361 HOH   C O   1 
HETATM 2423 O  O   . HOH   J 5 .   ? 16.007 -18.824 24.156 1.00 23.80 ? 362 HOH   C O   1 
HETATM 2424 O  O   . HOH   J 5 .   ? 19.910 -31.454 26.973 1.00 31.96 ? 363 HOH   C O   1 
HETATM 2425 O  O   . HOH   J 5 .   ? 30.609 -20.313 18.913 1.00 32.71 ? 364 HOH   C O   1 
HETATM 2426 O  O   . HOH   J 5 .   ? 14.911 -35.794 17.003 1.00 23.99 ? 365 HOH   C O   1 
HETATM 2427 O  O   . HOH   J 5 .   ? 19.357 -27.028 25.601 1.00 44.13 ? 366 HOH   C O   1 
HETATM 2428 O  O   . HOH   J 5 .   ? 0.346  -15.287 22.644 1.00 49.64 ? 367 HOH   C O   1 
HETATM 2429 O  O   . HOH   J 5 .   ? 8.030  -35.087 0.571  1.00 21.44 ? 368 HOH   C O   1 
HETATM 2430 O  O   . HOH   J 5 .   ? 26.531 -27.289 19.451 1.00 46.00 ? 369 HOH   C O   1 
HETATM 2431 O  O   . HOH   J 5 .   ? 7.161  -39.028 7.317  1.00 37.27 ? 370 HOH   C O   1 
HETATM 2432 O  O   . HOH   J 5 .   ? 9.547  -10.160 10.949 1.00 37.90 ? 371 HOH   C O   1 
HETATM 2433 O  O   . HOH   J 5 .   ? 19.610 -22.196 25.489 1.00 38.63 ? 372 HOH   C O   1 
HETATM 2434 O  O   . HOH   J 5 .   ? 29.655 -26.539 2.868  1.00 44.08 ? 373 HOH   C O   1 
HETATM 2435 O  O   . HOH   J 5 .   ? 4.662  -30.801 30.853 1.00 62.96 ? 374 HOH   C O   1 
HETATM 2436 O  O   . HOH   J 5 .   ? 3.807  -36.337 7.038  1.00 26.07 ? 375 HOH   C O   1 
HETATM 2437 O  O   . HOH   J 5 .   ? 5.868  -33.015 29.771 1.00 54.09 ? 376 HOH   C O   1 
HETATM 2438 O  O   . HOH   J 5 .   ? 4.010  -24.294 26.534 1.00 33.36 ? 377 HOH   C O   1 
HETATM 2439 O  O   . HOH   J 5 .   ? 18.325 -10.995 19.062 1.00 30.33 ? 378 HOH   C O   1 
HETATM 2440 O  O   . HOH   J 5 .   ? 26.155 -33.116 5.564  1.00 48.96 ? 379 HOH   C O   1 
HETATM 2441 O  O   . HOH   J 5 .   ? 28.767 -33.344 12.402 1.00 38.94 ? 380 HOH   C O   1 
HETATM 2442 O  O   . HOH   J 5 .   ? -0.311 -15.814 14.188 1.00 29.83 ? 381 HOH   C O   1 
HETATM 2443 O  O   . HOH   J 5 .   ? 26.446 -33.246 13.768 1.00 35.95 ? 382 HOH   C O   1 
HETATM 2444 O  O   . HOH   J 5 .   ? 5.765  -32.845 24.648 1.00 25.27 ? 383 HOH   C O   1 
HETATM 2445 O  O   . HOH   J 5 .   ? 6.568  -18.358 5.838  1.00 22.23 ? 384 HOH   C O   1 
HETATM 2446 O  O   . HOH   J 5 .   ? 14.244 -16.683 3.726  1.00 31.33 ? 385 HOH   C O   1 
HETATM 2447 O  O   . HOH   J 5 .   ? -2.201 -30.527 8.496  1.00 20.52 ? 386 HOH   C O   1 
HETATM 2448 O  O   . HOH   J 5 .   ? 5.565  -29.273 7.322  1.00 16.93 ? 387 HOH   C O   1 
HETATM 2449 O  O   . HOH   J 5 .   ? 0.974  -33.957 20.578 1.00 40.28 ? 388 HOH   C O   1 
HETATM 2450 O  O   . HOH   J 5 .   ? 22.412 -12.261 5.781  1.00 28.97 ? 389 HOH   C O   1 
HETATM 2451 O  O   . HOH   J 5 .   ? 18.840 -31.565 19.413 1.00 23.04 ? 390 HOH   C O   1 
HETATM 2452 O  O   . HOH   J 5 .   ? 1.975  -17.688 6.063  1.00 37.60 ? 391 HOH   C O   1 
HETATM 2453 O  O   . HOH   J 5 .   ? 12.094 -9.897  12.588 1.00 29.14 ? 392 HOH   C O   1 
HETATM 2454 O  O   . HOH   J 5 .   ? 8.339  -39.673 24.456 1.00 45.44 ? 393 HOH   C O   1 
HETATM 2455 O  O   . HOH   J 5 .   ? 19.496 -7.542  15.139 1.00 27.02 ? 394 HOH   C O   1 
HETATM 2456 O  O   . HOH   J 5 .   ? 6.260  -8.362  11.577 1.00 35.13 ? 395 HOH   C O   1 
HETATM 2457 O  O   . HOH   J 5 .   ? 16.584 -7.904  14.587 1.00 41.26 ? 396 HOH   C O   1 
HETATM 2458 O  O   . HOH   J 5 .   ? 22.040 -14.825 23.583 1.00 42.06 ? 397 HOH   C O   1 
HETATM 2459 O  O   . HOH   J 5 .   ? 28.326 -9.805  18.806 1.00 55.84 ? 398 HOH   C O   1 
HETATM 2460 O  O   . HOH   J 5 .   ? 15.297 -35.700 1.755  1.00 24.32 ? 399 HOH   C O   1 
HETATM 2461 O  O   . HOH   J 5 .   ? 8.778  -38.724 9.561  1.00 28.71 ? 400 HOH   C O   1 
HETATM 2462 O  O   . HOH   J 5 .   ? 31.431 -22.104 4.804  1.00 38.93 ? 401 HOH   C O   1 
HETATM 2463 O  O   . HOH   J 5 .   ? 8.210  -14.301 23.118 1.00 29.19 ? 402 HOH   C O   1 
HETATM 2464 O  O   . HOH   J 5 .   ? 21.253 -12.033 21.363 1.00 38.18 ? 403 HOH   C O   1 
HETATM 2465 O  O   . HOH   J 5 .   ? 1.477  -34.305 17.946 1.00 25.37 ? 404 HOH   C O   1 
HETATM 2466 O  O   . HOH   J 5 .   ? 24.206 -29.081 18.904 1.00 32.49 ? 405 HOH   C O   1 
HETATM 2467 O  O   . HOH   J 5 .   ? 16.802 -8.568  16.844 1.00 40.92 ? 406 HOH   C O   1 
HETATM 2468 O  O   . HOH   J 5 .   ? 31.250 -28.757 11.791 1.00 33.25 ? 407 HOH   C O   1 
HETATM 2469 O  O   . HOH   J 5 .   ? 2.481  -20.428 21.235 1.00 56.46 ? 408 HOH   C O   1 
HETATM 2470 O  O   . HOH   J 5 .   ? 4.665  -15.733 21.435 1.00 39.18 ? 409 HOH   C O   1 
HETATM 2471 O  O   . HOH   J 5 .   ? 2.740  -20.385 28.264 1.00 43.14 ? 410 HOH   C O   1 
HETATM 2472 O  O   . HOH   J 5 .   ? 32.231 -16.680 20.630 1.00 23.97 ? 411 HOH   C O   1 
HETATM 2473 O  O   . HOH   J 5 .   ? 29.224 -14.858 22.628 1.00 36.79 ? 412 HOH   C O   1 
HETATM 2474 O  O   . HOH   J 5 .   ? 22.441 -22.509 20.680 1.00 22.52 ? 413 HOH   C O   1 
HETATM 2475 O  O   . HOH   J 5 .   ? 24.919 -23.956 20.050 1.00 40.62 ? 414 HOH   C O   1 
HETATM 2476 O  O   . HOH   J 5 .   ? -0.039 -19.331 21.489 1.00 39.92 ? 415 HOH   C O   1 
HETATM 2477 O  O   . HOH   J 5 .   ? 12.124 -39.152 13.039 1.00 35.72 ? 416 HOH   C O   1 
HETATM 2478 O  O   . HOH   J 5 .   ? 17.829 -18.571 1.590  1.00 43.74 ? 417 HOH   C O   1 
HETATM 2479 O  O   . HOH   J 5 .   ? -0.493 -35.795 16.721 1.00 43.80 ? 418 HOH   C O   1 
HETATM 2480 O  O   . HOH   J 5 .   ? 6.999  -36.532 2.958  1.00 28.86 ? 419 HOH   C O   1 
HETATM 2481 O  O   . HOH   J 5 .   ? 4.332  -20.479 19.511 1.00 41.18 ? 420 HOH   C O   1 
HETATM 2482 O  O   . HOH   J 5 .   ? 18.809 -22.322 -2.136 1.00 32.88 ? 421 HOH   C O   1 
HETATM 2483 O  O   . HOH   J 5 .   ? 20.661 -9.376  17.653 1.00 40.33 ? 422 HOH   C O   1 
HETATM 2484 O  O   . HOH   J 5 .   ? 8.767  -8.197  26.541 1.00 41.23 ? 423 HOH   C O   1 
HETATM 2485 O  O   . HOH   J 5 .   ? 17.133 -34.609 17.994 1.00 46.74 ? 424 HOH   C O   1 
HETATM 2486 O  O   . HOH   J 5 .   ? 0.384  -34.973 10.041 1.00 55.49 ? 425 HOH   C O   1 
HETATM 2487 O  O   . HOH   J 5 .   ? 24.404 -15.687 23.069 1.00 54.00 ? 426 HOH   C O   1 
HETATM 2488 O  O   . HOH   J 5 .   ? 5.323  -28.870 4.673  1.00 41.26 ? 427 HOH   C O   1 
HETATM 2489 O  O   . HOH   J 5 .   ? 30.614 -31.286 13.327 1.00 47.19 ? 428 HOH   C O   1 
HETATM 2490 O  O   . HOH   J 5 .   ? 2.584  -29.079 27.354 1.00 42.98 ? 429 HOH   C O   1 
HETATM 2491 O  O   . HOH   J 5 .   ? 8.695  -23.965 2.712  1.00 36.66 ? 430 HOH   C O   1 
HETATM 2492 O  O   . HOH   J 5 .   ? 34.532 -11.329 17.665 1.00 42.16 ? 431 HOH   C O   1 
HETATM 2493 O  O   . HOH   J 5 .   ? 2.524  -17.206 22.789 1.00 53.38 ? 432 HOH   C O   1 
HETATM 2494 O  O   . HOH   J 5 .   ? 9.717  -14.222 25.947 1.00 50.01 ? 433 HOH   C O   1 
HETATM 2495 O  O   . HOH   J 5 .   ? 32.956 -9.242  11.852 1.00 38.76 ? 434 HOH   C O   1 
HETATM 2496 O  O   . HOH   J 5 .   ? 33.030 -9.402  14.342 1.00 35.04 ? 435 HOH   C O   1 
HETATM 2497 O  O   . HOH   J 5 .   ? 32.116 -27.325 13.787 1.00 44.65 ? 436 HOH   C O   1 
HETATM 2498 O  O   . HOH   J 5 .   ? 31.876 -36.127 12.324 1.00 43.00 ? 437 HOH   C O   1 
HETATM 2499 O  O   . HOH   J 5 .   ? 13.701 -17.114 26.394 1.00 43.06 ? 438 HOH   C O   1 
HETATM 2500 O  O   . HOH   J 5 .   ? 5.421  -39.723 23.439 1.00 34.79 ? 439 HOH   C O   1 
HETATM 2501 O  O   . HOH   J 5 .   ? 10.401 -16.267 27.387 1.00 48.91 ? 440 HOH   C O   1 
HETATM 2502 O  O   . HOH   J 5 .   ? 29.837 -8.577  8.953  1.00 43.48 ? 441 HOH   C O   1 
HETATM 2503 O  O   . HOH   J 5 .   ? 30.678 -30.576 15.951 1.00 60.46 ? 442 HOH   C O   1 
HETATM 2504 O  O   . HOH   J 5 .   ? 35.343 -9.577  8.330  1.00 64.72 ? 443 HOH   C O   1 
HETATM 2505 O  O   . HOH   J 5 .   ? 31.610 -26.597 -2.989 1.00 66.53 ? 444 HOH   C O   1 
HETATM 2506 O  O   . HOH   J 5 .   ? 35.620 -10.282 15.586 1.00 34.80 ? 445 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   ? 0.2749 0.2422 0.3079 -0.0002 -0.0429 0.0121  7   SER   A N   
2    C  CA  . SER   A 1   ? 0.2731 0.2427 0.3158 -0.0019 -0.0444 0.0115  7   SER   A CA  
3    C  C   . SER   A 1   ? 0.2666 0.2365 0.3126 -0.0038 -0.0441 0.0088  7   SER   A C   
4    O  O   . SER   A 1   ? 0.2833 0.2510 0.3235 -0.0036 -0.0442 0.0071  7   SER   A O   
5    C  CB  . SER   A 1   ? 0.3094 0.2791 0.3528 -0.0008 -0.0499 0.0119  7   SER   A CB  
6    O  OG  . SER   A 1   ? 0.3629 0.3306 0.4006 -0.0004 -0.0539 0.0094  7   SER   A OG  
7    N  N   . GLY   A 2   ? 0.2481 0.2201 0.3030 -0.0054 -0.0431 0.0085  8   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.2315 0.2032 0.2897 -0.0070 -0.0420 0.0067  8   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.2197 0.1934 0.2852 -0.0079 -0.0383 0.0072  8   GLY   A C   
10   O  O   . GLY   A 2   ? 0.2247 0.1996 0.2914 -0.0073 -0.0362 0.0082  8   GLY   A O   
11   N  N   . ALA   A 3   ? 0.2030 0.1765 0.2735 -0.0093 -0.0373 0.0064  9   ALA   A N   
12   C  CA  . ALA   A 3   ? 0.2060 0.1808 0.2823 -0.0096 -0.0332 0.0070  9   ALA   A CA  
13   C  C   . ALA   A 3   ? 0.2042 0.1769 0.2804 -0.0102 -0.0304 0.0065  9   ALA   A C   
14   O  O   . ALA   A 3   ? 0.2054 0.1758 0.2800 -0.0111 -0.0321 0.0056  9   ALA   A O   
15   C  CB  . ALA   A 3   ? 0.2151 0.1929 0.3018 -0.0101 -0.0343 0.0079  9   ALA   A CB  
16   N  N   . ILE   A 4   ? 0.1833 0.1560 0.2604 -0.0096 -0.0258 0.0069  10  ILE   A N   
17   C  CA  . ILE   A 4   ? 0.1853 0.1556 0.2623 -0.0097 -0.0221 0.0073  10  ILE   A CA  
18   C  C   . ILE   A 4   ? 0.1863 0.1584 0.2738 -0.0107 -0.0196 0.0085  10  ILE   A C   
19   O  O   . ILE   A 4   ? 0.1802 0.1547 0.2712 -0.0099 -0.0184 0.0088  10  ILE   A O   
20   C  CB  . ILE   A 4   ? 0.1860 0.1550 0.2552 -0.0074 -0.0186 0.0072  10  ILE   A CB  
21   C  CG1 . ILE   A 4   ? 0.1816 0.1502 0.2424 -0.0063 -0.0210 0.0060  10  ILE   A CG1 
22   C  CG2 . ILE   A 4   ? 0.1985 0.1641 0.2659 -0.0066 -0.0143 0.0083  10  ILE   A CG2 
23   C  CD1 . ILE   A 4   ? 0.1983 0.1675 0.2535 -0.0040 -0.0191 0.0051  10  ILE   A CD1 
24   N  N   . TYR   A 5   ? 0.1836 0.1542 0.2766 -0.0123 -0.0183 0.0091  11  TYR   A N   
25   C  CA  . TYR   A 5   ? 0.1954 0.1682 0.3003 -0.0134 -0.0151 0.0104  11  TYR   A CA  
26   C  C   . TYR   A 5   ? 0.2084 0.1776 0.3115 -0.0127 -0.0083 0.0121  11  TYR   A C   
27   O  O   . TYR   A 5   ? 0.2387 0.2042 0.3411 -0.0138 -0.0076 0.0125  11  TYR   A O   
28   C  CB  . TYR   A 5   ? 0.1942 0.1690 0.3101 -0.0163 -0.0193 0.0096  11  TYR   A CB  
29   C  CG  . TYR   A 5   ? 0.2183 0.1968 0.3356 -0.0162 -0.0259 0.0084  11  TYR   A CG  
30   C  CD1 . TYR   A 5   ? 0.2363 0.2195 0.3620 -0.0156 -0.0264 0.0092  11  TYR   A CD1 
31   C  CD2 . TYR   A 5   ? 0.2486 0.2253 0.3577 -0.0161 -0.0313 0.0068  11  TYR   A CD2 
32   C  CE1 . TYR   A 5   ? 0.2560 0.2418 0.3818 -0.0148 -0.0322 0.0087  11  TYR   A CE1 
33   C  CE2 . TYR   A 5   ? 0.2668 0.2460 0.3751 -0.0153 -0.0367 0.0063  11  TYR   A CE2 
34   C  CZ  . TYR   A 5   ? 0.2765 0.2602 0.3932 -0.0146 -0.0373 0.0074  11  TYR   A CZ  
35   O  OH  . TYR   A 5   ? 0.3131 0.2985 0.4279 -0.0132 -0.0425 0.0075  11  TYR   A OH  
36   N  N   . VAL   A 6   ? 0.1935 0.1628 0.2947 -0.0104 -0.0031 0.0132  12  VAL   A N   
37   C  CA  . VAL   A 6   ? 0.2102 0.1752 0.3068 -0.0087 0.0039  0.0152  12  VAL   A CA  
38   C  C   . VAL   A 6   ? 0.2286 0.1955 0.3333 -0.0080 0.0097  0.0169  12  VAL   A C   
39   O  O   . VAL   A 6   ? 0.2335 0.2034 0.3391 -0.0067 0.0094  0.0159  12  VAL   A O   
40   C  CB  . VAL   A 6   ? 0.2451 0.2070 0.3260 -0.0052 0.0044  0.0145  12  VAL   A CB  
41   C  CG1 . VAL   A 6   ? 0.2517 0.2167 0.3294 -0.0036 0.0022  0.0124  12  VAL   A CG1 
42   C  CG2 . VAL   A 6   ? 0.2604 0.2177 0.3350 -0.0024 0.0116  0.0169  12  VAL   A CG2 
43   N  N   . GLY   A 7   ? 0.2362 0.2017 0.3488 -0.0092 0.0153  0.0194  13  GLY   A N   
44   C  CA  . GLY   A 7   ? 0.2365 0.2041 0.3582 -0.0085 0.0218  0.0213  13  GLY   A CA  
45   C  C   . GLY   A 7   ? 0.2355 0.2101 0.3704 -0.0101 0.0177  0.0199  13  GLY   A C   
46   O  O   . GLY   A 7   ? 0.2333 0.2109 0.3759 -0.0131 0.0112  0.0186  13  GLY   A O   
47   N  N   . ASN   A 8   ? 0.2388 0.2156 0.3745 -0.0075 0.0206  0.0198  14  ASN   A N   
48   C  CA  . ASN   A 8   ? 0.2383 0.2213 0.3857 -0.0083 0.0165  0.0187  14  ASN   A CA  
49   C  C   . ASN   A 8   ? 0.2185 0.2014 0.3563 -0.0067 0.0110  0.0163  14  ASN   A C   
50   O  O   . ASN   A 8   ? 0.2072 0.1930 0.3499 -0.0053 0.0105  0.0157  14  ASN   A O   
51   C  CB  . ASN   A 8   ? 0.2771 0.2632 0.4357 -0.0068 0.0233  0.0204  14  ASN   A CB  
52   C  CG  . ASN   A 8   ? 0.3612 0.3493 0.5345 -0.0093 0.0279  0.0228  14  ASN   A CG  
53   O  OD1 . ASN   A 8   ? 0.3937 0.3863 0.5807 -0.0128 0.0229  0.0224  14  ASN   A OD1 
54   N  ND2 . ASN   A 8   ? 0.3725 0.3568 0.5429 -0.0075 0.0374  0.0254  14  ASN   A ND2 
55   N  N   . TYR   A 9   ? 0.2026 0.1823 0.3280 -0.0069 0.0070  0.0149  15  TYR   A N   
56   C  CA  . TYR   A 9   ? 0.1927 0.1722 0.3098 -0.0057 0.0023  0.0128  15  TYR   A CA  
57   C  C   . TYR   A 9   ? 0.1780 0.1580 0.2933 -0.0079 -0.0049 0.0119  15  TYR   A C   
58   O  O   . TYR   A 9   ? 0.1829 0.1614 0.2975 -0.0095 -0.0059 0.0122  15  TYR   A O   
59   C  CB  . TYR   A 9   ? 0.2016 0.1766 0.3039 -0.0032 0.0048  0.0116  15  TYR   A CB  
60   C  CG  . TYR   A 9   ? 0.2040 0.1774 0.3043 -0.0002 0.0115  0.0118  15  TYR   A CG  
61   C  CD1 . TYR   A 9   ? 0.2141 0.1895 0.3206 0.0010  0.0129  0.0111  15  TYR   A CD1 
62   C  CD2 . TYR   A 9   ? 0.2220 0.1912 0.3135 0.0019  0.0168  0.0127  15  TYR   A CD2 
63   C  CE1 . TYR   A 9   ? 0.2338 0.2071 0.3373 0.0042  0.0194  0.0109  15  TYR   A CE1 
64   C  CE2 . TYR   A 9   ? 0.2309 0.1980 0.3185 0.0053  0.0231  0.0127  15  TYR   A CE2 
65   C  CZ  . TYR   A 9   ? 0.2549 0.2242 0.3489 0.0064  0.0246  0.0117  15  TYR   A CZ  
66   O  OH  . TYR   A 9   ? 0.3024 0.2690 0.3915 0.0102  0.0311  0.0113  15  TYR   A OH  
67   N  N   . ARG   A 10  ? 0.1637 0.1453 0.2780 -0.0075 -0.0094 0.0109  16  ARG   A N   
68   C  CA  . ARG   A 10  ? 0.1738 0.1553 0.2838 -0.0086 -0.0156 0.0102  16  ARG   A CA  
69   C  C   . ARG   A 10  ? 0.1858 0.1654 0.2857 -0.0071 -0.0159 0.0089  16  ARG   A C   
70   O  O   . ARG   A 10  ? 0.1832 0.1632 0.2845 -0.0058 -0.0146 0.0086  16  ARG   A O   
71   C  CB  . ARG   A 10  ? 0.1876 0.1729 0.3068 -0.0093 -0.0204 0.0108  16  ARG   A CB  
72   C  CG  . ARG   A 10  ? 0.2087 0.1935 0.3218 -0.0092 -0.0261 0.0104  16  ARG   A CG  
73   C  CD  . ARG   A 10  ? 0.2221 0.2104 0.3430 -0.0092 -0.0313 0.0111  16  ARG   A CD  
74   N  NE  . ARG   A 10  ? 0.2404 0.2281 0.3563 -0.0076 -0.0343 0.0119  16  ARG   A NE  
75   C  CZ  . ARG   A 10  ? 0.2821 0.2686 0.3913 -0.0073 -0.0390 0.0119  16  ARG   A CZ  
76   N  NH1 . ARG   A 10  ? 0.2721 0.2578 0.3783 -0.0087 -0.0418 0.0105  16  ARG   A NH1 
77   N  NH2 . ARG   A 10  ? 0.2694 0.2548 0.3742 -0.0056 -0.0405 0.0134  16  ARG   A NH2 
78   N  N   . VAL   A 11  ? 0.1805 0.1579 0.2711 -0.0072 -0.0174 0.0081  17  VAL   A N   
79   C  CA  . VAL   A 11  ? 0.1824 0.1589 0.2654 -0.0062 -0.0179 0.0067  17  VAL   A CA  
80   C  C   . VAL   A 11  ? 0.1874 0.1645 0.2688 -0.0070 -0.0223 0.0069  17  VAL   A C   
81   O  O   . VAL   A 11  ? 0.1872 0.1636 0.2660 -0.0077 -0.0246 0.0071  17  VAL   A O   
82   C  CB  . VAL   A 11  ? 0.1972 0.1714 0.2712 -0.0051 -0.0161 0.0056  17  VAL   A CB  
83   C  CG1 . VAL   A 11  ? 0.1817 0.1561 0.2503 -0.0041 -0.0169 0.0036  17  VAL   A CG1 
84   C  CG2 . VAL   A 11  ? 0.1935 0.1661 0.2673 -0.0040 -0.0114 0.0061  17  VAL   A CG2 
85   N  N   . VAL   A 12  ? 0.1710 0.1485 0.2530 -0.0066 -0.0232 0.0070  18  VAL   A N   
86   C  CA  . VAL   A 12  ? 0.1767 0.1543 0.2563 -0.0068 -0.0264 0.0079  18  VAL   A CA  
87   C  C   . VAL   A 12  ? 0.1703 0.1473 0.2468 -0.0065 -0.0253 0.0071  18  VAL   A C   
88   O  O   . VAL   A 12  ? 0.1679 0.1446 0.2457 -0.0062 -0.0229 0.0056  18  VAL   A O   
89   C  CB  . VAL   A 12  ? 0.1955 0.1742 0.2812 -0.0066 -0.0288 0.0099  18  VAL   A CB  
90   C  CG1 . VAL   A 12  ? 0.2298 0.2099 0.3200 -0.0072 -0.0309 0.0101  18  VAL   A CG1 
91   C  CG2 . VAL   A 12  ? 0.1866 0.1655 0.2783 -0.0058 -0.0263 0.0101  18  VAL   A CG2 
92   N  N   . ASN   A 13  ? 0.1667 0.1433 0.2398 -0.0066 -0.0269 0.0081  19  ASN   A N   
93   C  CA  . ASN   A 13  ? 0.1611 0.1373 0.2339 -0.0067 -0.0255 0.0079  19  ASN   A CA  
94   C  C   . ASN   A 13  ? 0.1694 0.1448 0.2484 -0.0065 -0.0246 0.0089  19  ASN   A C   
95   O  O   . ASN   A 13  ? 0.1707 0.1457 0.2518 -0.0058 -0.0262 0.0114  19  ASN   A O   
96   C  CB  . ASN   A 13  ? 0.1637 0.1395 0.2324 -0.0065 -0.0264 0.0097  19  ASN   A CB  
97   C  CG  . ASN   A 13  ? 0.2060 0.1824 0.2688 -0.0063 -0.0270 0.0085  19  ASN   A CG  
98   O  OD1 . ASN   A 13  ? 0.2195 0.1951 0.2788 -0.0059 -0.0290 0.0089  19  ASN   A OD1 
99   N  ND2 . ASN   A 13  ? 0.1842 0.1619 0.2463 -0.0065 -0.0254 0.0069  19  ASN   A ND2 
100  N  N   . ARG   A 14  ? 0.1543 0.1289 0.2361 -0.0069 -0.0224 0.0070  20  ARG   A N   
101  C  CA  . ARG   A 14  ? 0.1457 0.1185 0.2334 -0.0064 -0.0211 0.0078  20  ARG   A CA  
102  C  C   . ARG   A 14  ? 0.1589 0.1301 0.2475 -0.0060 -0.0218 0.0116  20  ARG   A C   
103  O  O   . ARG   A 14  ? 0.1878 0.1580 0.2803 -0.0047 -0.0222 0.0138  20  ARG   A O   
104  C  CB  . ARG   A 14  ? 0.1624 0.1340 0.2522 -0.0071 -0.0190 0.0044  20  ARG   A CB  
105  C  CG  . ARG   A 14  ? 0.1837 0.1526 0.2796 -0.0064 -0.0173 0.0043  20  ARG   A CG  
106  C  CD  . ARG   A 14  ? 0.1863 0.1534 0.2838 -0.0074 -0.0158 0.0003  20  ARG   A CD  
107  N  NE  . ARG   A 14  ? 0.1915 0.1550 0.2943 -0.0066 -0.0138 -0.0009 20  ARG   A NE  
108  C  CZ  . ARG   A 14  ? 0.2158 0.1758 0.3237 -0.0069 -0.0127 0.0011  20  ARG   A CZ  
109  N  NH1 . ARG   A 14  ? 0.2088 0.1687 0.3167 -0.0076 -0.0131 0.0051  20  ARG   A NH1 
110  N  NH2 . ARG   A 14  ? 0.2134 0.1696 0.3259 -0.0061 -0.0107 -0.0006 20  ARG   A NH2 
111  N  N   . HIS   A 15  ? 0.1582 0.1291 0.2429 -0.0066 -0.0217 0.0127  21  HIS   A N   
112  C  CA  . HIS   A 15  ? 0.1661 0.1345 0.2501 -0.0056 -0.0215 0.0168  21  HIS   A CA  
113  C  C   . HIS   A 15  ? 0.1873 0.1560 0.2674 -0.0037 -0.0248 0.0197  21  HIS   A C   
114  O  O   . HIS   A 15  ? 0.2147 0.1810 0.2935 -0.0019 -0.0251 0.0235  21  HIS   A O   
115  C  CB  . HIS   A 15  ? 0.1723 0.1402 0.2539 -0.0066 -0.0193 0.0175  21  HIS   A CB  
116  C  CG  . HIS   A 15  ? 0.1801 0.1500 0.2546 -0.0064 -0.0206 0.0173  21  HIS   A CG  
117  N  ND1 . HIS   A 15  ? 0.2036 0.1765 0.2769 -0.0073 -0.0211 0.0137  21  HIS   A ND1 
118  C  CD2 . HIS   A 15  ? 0.2055 0.1743 0.2733 -0.0048 -0.0213 0.0204  21  HIS   A CD2 
119  C  CE1 . HIS   A 15  ? 0.2085 0.1819 0.2753 -0.0064 -0.0219 0.0146  21  HIS   A CE1 
120  N  NE2 . HIS   A 15  ? 0.2123 0.1833 0.2753 -0.0049 -0.0221 0.0184  21  HIS   A NE2 
121  N  N   . LEU   A 16  ? 0.1810 0.1523 0.2595 -0.0038 -0.0274 0.0179  22  LEU   A N   
122  C  CA  . LEU   A 16  ? 0.1766 0.1485 0.2527 -0.0022 -0.0315 0.0196  22  LEU   A CA  
123  C  C   . LEU   A 16  ? 0.1950 0.1691 0.2787 -0.0019 -0.0331 0.0190  22  LEU   A C   
124  O  O   . LEU   A 16  ? 0.2031 0.1788 0.2872 -0.0011 -0.0371 0.0195  22  LEU   A O   
125  C  CB  . LEU   A 16  ? 0.1677 0.1406 0.2372 -0.0027 -0.0333 0.0180  22  LEU   A CB  
126  C  CG  . LEU   A 16  ? 0.1934 0.1646 0.2554 -0.0025 -0.0316 0.0188  22  LEU   A CG  
127  C  CD1 . LEU   A 16  ? 0.1983 0.1700 0.2542 -0.0026 -0.0333 0.0168  22  LEU   A CD1 
128  C  CD2 . LEU   A 16  ? 0.2039 0.1723 0.2619 -0.0003 -0.0318 0.0228  22  LEU   A CD2 
129  N  N   . ALA   A 17  ? 0.1828 0.1571 0.2728 -0.0025 -0.0300 0.0176  23  ALA   A N   
130  C  CA  . ALA   A 17  ? 0.1781 0.1547 0.2759 -0.0020 -0.0304 0.0171  23  ALA   A CA  
131  C  C   . ALA   A 17  ? 0.1925 0.1695 0.2945 0.0003  -0.0334 0.0203  23  ALA   A C   
132  O  O   . ALA   A 17  ? 0.1906 0.1648 0.2908 0.0017  -0.0330 0.0228  23  ALA   A O   
133  C  CB  . ALA   A 17  ? 0.1740 0.1496 0.2762 -0.0023 -0.0261 0.0152  23  ALA   A CB  
134  N  N   . THR   A 18  ? 0.2018 0.1825 0.3100 0.0008  -0.0361 0.0202  24  THR   A N   
135  C  CA  . THR   A 18  ? 0.2150 0.1972 0.3279 0.0035  -0.0400 0.0229  24  THR   A CA  
136  C  C   . THR   A 18  ? 0.2220 0.2047 0.3447 0.0050  -0.0373 0.0237  24  THR   A C   
137  O  O   . THR   A 18  ? 0.2085 0.1907 0.3341 0.0039  -0.0325 0.0216  24  THR   A O   
138  C  CB  . THR   A 18  ? 0.2377 0.2244 0.3543 0.0029  -0.0451 0.0218  24  THR   A CB  
139  O  OG1 . THR   A 18  ? 0.2421 0.2319 0.3677 0.0012  -0.0422 0.0197  24  THR   A OG1 
140  C  CG2 . THR   A 18  ? 0.2472 0.2327 0.3541 0.0016  -0.0478 0.0204  24  THR   A CG2 
141  N  N   . HIS   A 19  ? 0.2282 0.2124 0.3563 0.0081  -0.0405 0.0264  25  HIS   A N   
142  C  CA  . HIS   A 19  ? 0.2486 0.2337 0.3872 0.0100  -0.0379 0.0271  25  HIS   A CA  
143  C  C   . HIS   A 19  ? 0.2198 0.2098 0.3676 0.0084  -0.0358 0.0245  25  HIS   A C   
144  O  O   . HIS   A 19  ? 0.2259 0.2150 0.3786 0.0087  -0.0306 0.0234  25  HIS   A O   
145  C  CB  . HIS   A 19  ? 0.3016 0.2888 0.4452 0.0140  -0.0429 0.0306  25  HIS   A CB  
146  C  CG  . HIS   A 19  ? 0.4187 0.4007 0.5531 0.0165  -0.0445 0.0343  25  HIS   A CG  
147  N  ND1 . HIS   A 19  ? 0.4754 0.4509 0.6070 0.0171  -0.0395 0.0359  25  HIS   A ND1 
148  C  CD2 . HIS   A 19  ? 0.4580 0.4400 0.5856 0.0188  -0.0504 0.0367  25  HIS   A CD2 
149  C  CE1 . HIS   A 19  ? 0.4960 0.4677 0.6195 0.0195  -0.0417 0.0397  25  HIS   A CE1 
150  N  NE2 . HIS   A 19  ? 0.4903 0.4656 0.6102 0.0210  -0.0483 0.0404  25  HIS   A NE2 
151  N  N   . ASN   A 20  ? 0.2143 0.2088 0.3641 0.0067  -0.0395 0.0232  26  ASN   A N   
152  C  CA  . ASN   A 20  ? 0.2059 0.2046 0.3649 0.0050  -0.0368 0.0213  26  ASN   A CA  
153  C  C   . ASN   A 20  ? 0.1961 0.1914 0.3493 0.0029  -0.0304 0.0190  26  ASN   A C   
154  O  O   . ASN   A 20  ? 0.2036 0.2001 0.3631 0.0029  -0.0254 0.0181  26  ASN   A O   
155  C  CB  . ASN   A 20  ? 0.2309 0.2342 0.3938 0.0032  -0.0420 0.0203  26  ASN   A CB  
156  C  CG  . ASN   A 20  ? 0.3064 0.3159 0.4818 0.0053  -0.0472 0.0216  26  ASN   A CG  
157  O  OD1 . ASN   A 20  ? 0.3087 0.3210 0.4950 0.0074  -0.0448 0.0228  26  ASN   A OD1 
158  N  ND2 . ASN   A 20  ? 0.3287 0.3401 0.5021 0.0052  -0.0548 0.0212  26  ASN   A ND2 
159  N  N   . ASP   A 21  ? 0.1760 0.1672 0.3169 0.0014  -0.0306 0.0181  27  ASP   A N   
160  C  CA  . ASP   A 21  ? 0.1675 0.1557 0.3025 0.0000  -0.0254 0.0158  27  ASP   A CA  
161  C  C   . ASP   A 21  ? 0.1728 0.1583 0.3094 0.0016  -0.0206 0.0152  27  ASP   A C   
162  O  O   . ASP   A 21  ? 0.1843 0.1693 0.3215 0.0017  -0.0159 0.0134  27  ASP   A O   
163  C  CB  . ASP   A 21  ? 0.1551 0.1399 0.2781 -0.0014 -0.0267 0.0151  27  ASP   A CB  
164  C  CG  . ASP   A 21  ? 0.2235 0.2096 0.3427 -0.0031 -0.0300 0.0146  27  ASP   A CG  
165  O  OD1 . ASP   A 21  ? 0.2264 0.2145 0.3498 -0.0043 -0.0289 0.0137  27  ASP   A OD1 
166  O  OD2 . ASP   A 21  ? 0.2301 0.2147 0.3421 -0.0031 -0.0334 0.0152  27  ASP   A OD2 
167  N  N   . TRP   A 22  ? 0.1729 0.1559 0.3094 0.0032  -0.0217 0.0167  28  TRP   A N   
168  C  CA  . TRP   A 22  ? 0.1734 0.1528 0.3115 0.0048  -0.0174 0.0158  28  TRP   A CA  
169  C  C   . TRP   A 22  ? 0.1911 0.1731 0.3401 0.0070  -0.0146 0.0161  28  TRP   A C   
170  O  O   . TRP   A 22  ? 0.1964 0.1760 0.3460 0.0080  -0.0097 0.0140  28  TRP   A O   
171  C  CB  . TRP   A 22  ? 0.1807 0.1561 0.3169 0.0059  -0.0189 0.0179  28  TRP   A CB  
172  C  CG  . TRP   A 22  ? 0.1926 0.1643 0.3196 0.0038  -0.0186 0.0166  28  TRP   A CG  
173  C  CD1 . TRP   A 22  ? 0.2048 0.1762 0.3255 0.0027  -0.0217 0.0183  28  TRP   A CD1 
174  C  CD2 . TRP   A 22  ? 0.1886 0.1565 0.3125 0.0026  -0.0151 0.0132  28  TRP   A CD2 
175  N  NE1 . TRP   A 22  ? 0.2067 0.1750 0.3218 0.0009  -0.0198 0.0165  28  TRP   A NE1 
176  C  CE2 . TRP   A 22  ? 0.2038 0.1702 0.3211 0.0006  -0.0162 0.0131  28  TRP   A CE2 
177  C  CE3 . TRP   A 22  ? 0.2029 0.1688 0.3288 0.0033  -0.0112 0.0099  28  TRP   A CE3 
178  C  CZ2 . TRP   A 22  ? 0.2014 0.1649 0.3158 -0.0010 -0.0141 0.0097  28  TRP   A CZ2 
179  C  CZ3 . TRP   A 22  ? 0.2150 0.1773 0.3364 0.0019  -0.0095 0.0062  28  TRP   A CZ3 
180  C  CH2 . TRP   A 22  ? 0.2024 0.1640 0.3189 -0.0004 -0.0112 0.0060  28  TRP   A CH2 
181  N  N   . ALA   A 23  ? 0.1956 0.1829 0.3533 0.0079  -0.0178 0.0184  29  ALA   A N   
182  C  CA  . ALA   A 23  ? 0.2077 0.1989 0.3780 0.0101  -0.0149 0.0189  29  ALA   A CA  
183  C  C   . ALA   A 23  ? 0.2095 0.2028 0.3817 0.0088  -0.0101 0.0170  29  ALA   A C   
184  O  O   . ALA   A 23  ? 0.2168 0.2123 0.3982 0.0106  -0.0056 0.0171  29  ALA   A O   
185  C  CB  . ALA   A 23  ? 0.2168 0.2139 0.3969 0.0113  -0.0205 0.0216  29  ALA   A CB  
186  N  N   . ASN   A 24  ? 0.1903 0.1830 0.3546 0.0059  -0.0108 0.0158  30  ASN   A N   
187  C  CA  . ASN   A 24  ? 0.1882 0.1817 0.3527 0.0048  -0.0059 0.0146  30  ASN   A CA  
188  C  C   . ASN   A 24  ? 0.1816 0.1694 0.3316 0.0041  -0.0033 0.0120  30  ASN   A C   
189  O  O   . ASN   A 24  ? 0.1782 0.1657 0.3232 0.0026  -0.0018 0.0114  30  ASN   A O   
190  C  CB  . ASN   A 24  ? 0.2041 0.2021 0.3732 0.0023  -0.0094 0.0156  30  ASN   A CB  
191  C  CG  . ASN   A 24  ? 0.2511 0.2556 0.4360 0.0030  -0.0121 0.0174  30  ASN   A CG  
192  O  OD1 . ASN   A 24  ? 0.2740 0.2820 0.4700 0.0039  -0.0073 0.0179  30  ASN   A OD1 
193  N  ND2 . ASN   A 24  ? 0.2575 0.2643 0.4438 0.0029  -0.0196 0.0183  30  ASN   A ND2 
194  N  N   . LEU   A 25  ? 0.1757 0.1592 0.3199 0.0052  -0.0030 0.0105  31  LEU   A N   
195  C  CA  . LEU   A 25  ? 0.1891 0.1680 0.3211 0.0046  -0.0019 0.0076  31  LEU   A CA  
196  C  C   . LEU   A 25  ? 0.1947 0.1718 0.3219 0.0058  0.0037  0.0056  31  LEU   A C   
197  O  O   . LEU   A 25  ? 0.2117 0.1884 0.3434 0.0082  0.0084  0.0052  31  LEU   A O   
198  C  CB  . LEU   A 25  ? 0.1946 0.1693 0.3248 0.0055  -0.0023 0.0063  31  LEU   A CB  
199  C  CG  . LEU   A 25  ? 0.2138 0.1842 0.3337 0.0048  -0.0019 0.0025  31  LEU   A CG  
200  C  CD1 . LEU   A 25  ? 0.2134 0.1850 0.3270 0.0022  -0.0059 0.0030  31  LEU   A CD1 
201  C  CD2 . LEU   A 25  ? 0.2207 0.1867 0.3418 0.0054  -0.0018 0.0010  31  LEU   A CD2 
202  N  N   . VAL   A 26  ? 0.1767 0.1525 0.2941 0.0047  0.0034  0.0043  32  VAL   A N   
203  C  CA  . VAL   A 26  ? 0.1986 0.1716 0.3081 0.0065  0.0083  0.0023  32  VAL   A CA  
204  C  C   . VAL   A 26  ? 0.2218 0.1908 0.3207 0.0070  0.0069  -0.0017 32  VAL   A C   
205  O  O   . VAL   A 26  ? 0.2433 0.2089 0.3372 0.0096  0.0102  -0.0047 32  VAL   A O   
206  C  CB  . VAL   A 26  ? 0.2174 0.1917 0.3239 0.0053  0.0090  0.0042  32  VAL   A CB  
207  C  CG1 . VAL   A 26  ? 0.2347 0.2052 0.3300 0.0077  0.0136  0.0025  32  VAL   A CG1 
208  C  CG2 . VAL   A 26  ? 0.2283 0.2066 0.3472 0.0045  0.0109  0.0075  32  VAL   A CG2 
209  N  N   . TRP   A 27  ? 0.2088 0.1782 0.3044 0.0047  0.0019  -0.0021 33  TRP   A N   
210  C  CA  . TRP   A 27  ? 0.2173 0.1841 0.3050 0.0047  0.0000  -0.0060 33  TRP   A CA  
211  C  C   . TRP   A 27  ? 0.2044 0.1725 0.2935 0.0020  -0.0048 -0.0052 33  TRP   A C   
212  O  O   . TRP   A 27  ? 0.1973 0.1680 0.2881 0.0005  -0.0069 -0.0021 33  TRP   A O   
213  C  CB  . TRP   A 27  ? 0.2293 0.1952 0.3061 0.0060  0.0009  -0.0075 33  TRP   A CB  
214  C  CG  . TRP   A 27  ? 0.2387 0.2036 0.3078 0.0058  -0.0025 -0.0115 33  TRP   A CG  
215  C  CD1 . TRP   A 27  ? 0.2605 0.2225 0.3248 0.0074  -0.0026 -0.0164 33  TRP   A CD1 
216  C  CD2 . TRP   A 27  ? 0.2303 0.1973 0.2963 0.0041  -0.0064 -0.0111 33  TRP   A CD2 
217  N  NE1 . TRP   A 27  ? 0.2644 0.2275 0.3245 0.0064  -0.0068 -0.0192 33  TRP   A NE1 
218  C  CE2 . TRP   A 27  ? 0.2419 0.2081 0.3028 0.0045  -0.0088 -0.0157 33  TRP   A CE2 
219  C  CE3 . TRP   A 27  ? 0.2296 0.1990 0.2970 0.0023  -0.0081 -0.0077 33  TRP   A CE3 
220  C  CZ2 . TRP   A 27  ? 0.2403 0.2088 0.2982 0.0034  -0.0126 -0.0166 33  TRP   A CZ2 
221  C  CZ3 . TRP   A 27  ? 0.2358 0.2066 0.2990 0.0014  -0.0115 -0.0085 33  TRP   A CZ3 
222  C  CH2 . TRP   A 27  ? 0.2314 0.2021 0.2905 0.0020  -0.0135 -0.0127 33  TRP   A CH2 
223  N  N   . GLU   A 28  ? 0.2071 0.1733 0.2957 0.0014  -0.0064 -0.0079 34  GLU   A N   
224  C  CA  . GLU   A 28  ? 0.2035 0.1707 0.2929 -0.0011 -0.0099 -0.0071 34  GLU   A CA  
225  C  C   . GLU   A 28  ? 0.1949 0.1607 0.2811 -0.0017 -0.0112 -0.0116 34  GLU   A C   
226  O  O   . GLU   A 28  ? 0.2104 0.1733 0.2957 -0.0005 -0.0099 -0.0155 34  GLU   A O   
227  C  CB  . GLU   A 28  ? 0.2067 0.1737 0.3038 -0.0018 -0.0107 -0.0037 34  GLU   A CB  
228  C  CG  . GLU   A 28  ? 0.2128 0.1763 0.3154 -0.0006 -0.0084 -0.0047 34  GLU   A CG  
229  C  CD  . GLU   A 28  ? 0.2443 0.2042 0.3473 -0.0015 -0.0084 -0.0083 34  GLU   A CD  
230  O  OE1 . GLU   A 28  ? 0.2769 0.2332 0.3813 -0.0001 -0.0062 -0.0114 34  GLU   A OE1 
231  O  OE2 . GLU   A 28  ? 0.2181 0.1785 0.3203 -0.0037 -0.0105 -0.0083 34  GLU   A OE2 
232  N  N   . ASP   A 29  ? 0.1836 0.1514 0.2685 -0.0036 -0.0139 -0.0114 35  ASP   A N   
233  C  CA  . ASP   A 29  ? 0.1778 0.1455 0.2619 -0.0046 -0.0156 -0.0158 35  ASP   A CA  
234  C  C   . ASP   A 29  ? 0.1746 0.1439 0.2630 -0.0072 -0.0171 -0.0136 35  ASP   A C   
235  O  O   . ASP   A 29  ? 0.1729 0.1450 0.2583 -0.0075 -0.0183 -0.0115 35  ASP   A O   
236  C  CB  . ASP   A 29  ? 0.2109 0.1802 0.2867 -0.0030 -0.0169 -0.0189 35  ASP   A CB  
237  C  CG  . ASP   A 29  ? 0.2848 0.2546 0.3605 -0.0037 -0.0195 -0.0245 35  ASP   A CG  
238  O  OD1 . ASP   A 29  ? 0.2911 0.2609 0.3742 -0.0063 -0.0203 -0.0252 35  ASP   A OD1 
239  O  OD2 . ASP   A 29  ? 0.2846 0.2545 0.3530 -0.0014 -0.0207 -0.0282 35  ASP   A OD2 
240  N  N   . SER   A 30  ? 0.1822 0.1489 0.2774 -0.0088 -0.0163 -0.0137 36  SER   A N   
241  C  CA  A SER   A 30  ? 0.1940 0.1614 0.2934 -0.0110 -0.0164 -0.0111 36  SER   A CA  
242  C  CA  B SER   A 30  ? 0.1927 0.1603 0.2920 -0.0109 -0.0165 -0.0110 36  SER   A CA  
243  C  C   . SER   A 30  ? 0.1920 0.1633 0.2904 -0.0123 -0.0184 -0.0138 36  SER   A C   
244  O  O   . SER   A 30  ? 0.1968 0.1704 0.2955 -0.0132 -0.0184 -0.0109 36  SER   A O   
245  C  CB  A SER   A 30  ? 0.2269 0.1899 0.3341 -0.0123 -0.0145 -0.0111 36  SER   A CB  
246  C  CB  B SER   A 30  ? 0.2219 0.1850 0.3289 -0.0123 -0.0145 -0.0106 36  SER   A CB  
247  O  OG  A SER   A 30  ? 0.2550 0.2181 0.3665 -0.0144 -0.0138 -0.0086 36  SER   A OG  
248  O  OG  B SER   A 30  ? 0.2418 0.2037 0.3522 -0.0135 -0.0150 -0.0166 36  SER   A OG  
249  N  N   . SER   A 31  ? 0.1884 0.1605 0.2855 -0.0119 -0.0200 -0.0197 37  SER   A N   
250  C  CA  . SER   A 31  ? 0.1973 0.1740 0.2948 -0.0129 -0.0225 -0.0227 37  SER   A CA  
251  C  C   . SER   A 31  ? 0.1976 0.1780 0.2877 -0.0111 -0.0237 -0.0204 37  SER   A C   
252  O  O   . SER   A 31  ? 0.2069 0.1914 0.2980 -0.0116 -0.0253 -0.0212 37  SER   A O   
253  C  CB  . SER   A 31  ? 0.2479 0.2247 0.3449 -0.0124 -0.0251 -0.0299 37  SER   A CB  
254  O  OG  . SER   A 31  ? 0.3189 0.2955 0.4057 -0.0089 -0.0260 -0.0313 37  SER   A OG  
255  N  N   . ARG   A 32  ? 0.1674 0.1462 0.2510 -0.0090 -0.0228 -0.0176 38  ARG   A N   
256  C  CA  . ARG   A 32  ? 0.1634 0.1446 0.2404 -0.0075 -0.0235 -0.0153 38  ARG   A CA  
257  C  C   . ARG   A 32  ? 0.1678 0.1484 0.2450 -0.0081 -0.0224 -0.0098 38  ARG   A C   
258  O  O   . ARG   A 32  ? 0.1712 0.1530 0.2435 -0.0072 -0.0230 -0.0080 38  ARG   A O   
259  C  CB  . ARG   A 32  ? 0.1789 0.1584 0.2485 -0.0048 -0.0231 -0.0161 38  ARG   A CB  
260  C  CG  . ARG   A 32  ? 0.2004 0.1802 0.2662 -0.0030 -0.0248 -0.0215 38  ARG   A CG  
261  C  CD  . ARG   A 32  ? 0.2166 0.1941 0.2737 0.0002  -0.0234 -0.0216 38  ARG   A CD  
262  N  NE  . ARG   A 32  ? 0.2096 0.1880 0.2609 0.0017  -0.0232 -0.0183 38  ARG   A NE  
263  C  CZ  . ARG   A 32  ? 0.2203 0.1972 0.2628 0.0049  -0.0225 -0.0185 38  ARG   A CZ  
264  N  NH1 . ARG   A 32  ? 0.2266 0.2013 0.2639 0.0074  -0.0220 -0.0218 38  ARG   A NH1 
265  N  NH2 . ARG   A 32  ? 0.1961 0.1732 0.2343 0.0060  -0.0221 -0.0154 38  ARG   A NH2 
266  N  N   . ASP   A 33  ? 0.1489 0.1272 0.2312 -0.0093 -0.0209 -0.0074 39  ASP   A N   
267  C  CA  . ASP   A 33  ? 0.1450 0.1223 0.2265 -0.0092 -0.0205 -0.0026 39  ASP   A CA  
268  C  C   . ASP   A 33  ? 0.1606 0.1376 0.2381 -0.0077 -0.0209 -0.0014 39  ASP   A C   
269  O  O   . ASP   A 33  ? 0.1672 0.1445 0.2421 -0.0075 -0.0218 0.0013  39  ASP   A O   
270  C  CB  . ASP   A 33  ? 0.1570 0.1361 0.2369 -0.0097 -0.0208 -0.0004 39  ASP   A CB  
271  C  CG  . ASP   A 33  ? 0.1787 0.1562 0.2564 -0.0092 -0.0209 0.0041  39  ASP   A CG  
272  O  OD1 . ASP   A 33  ? 0.1857 0.1608 0.2666 -0.0091 -0.0203 0.0062  39  ASP   A OD1 
273  O  OD2 . ASP   A 33  ? 0.1723 0.1507 0.2450 -0.0085 -0.0218 0.0053  39  ASP   A OD2 
274  N  N   . LEU   A 34  ? 0.1498 0.1257 0.2273 -0.0068 -0.0200 -0.0034 40  LEU   A N   
275  C  CA  . LEU   A 34  ? 0.1493 0.1249 0.2249 -0.0056 -0.0194 -0.0019 40  LEU   A CA  
276  C  C   . LEU   A 34  ? 0.1512 0.1254 0.2321 -0.0050 -0.0177 -0.0011 40  LEU   A C   
277  O  O   . LEU   A 34  ? 0.1625 0.1350 0.2460 -0.0048 -0.0163 -0.0031 40  LEU   A O   
278  C  CB  . LEU   A 34  ? 0.1622 0.1380 0.2320 -0.0041 -0.0187 -0.0042 40  LEU   A CB  
279  C  CG  . LEU   A 34  ? 0.1744 0.1516 0.2385 -0.0038 -0.0203 -0.0045 40  LEU   A CG  
280  C  CD1 . LEU   A 34  ? 0.1824 0.1588 0.2400 -0.0014 -0.0193 -0.0063 40  LEU   A CD1 
281  C  CD2 . LEU   A 34  ? 0.1783 0.1556 0.2418 -0.0044 -0.0212 -0.0013 40  LEU   A CD2 
282  N  N   . LEU   A 35  ? 0.1414 0.1162 0.2243 -0.0048 -0.0177 0.0015  41  LEU   A N   
283  C  CA  . LEU   A 35  ? 0.1504 0.1248 0.2393 -0.0039 -0.0158 0.0024  41  LEU   A CA  
284  C  C   . LEU   A 35  ? 0.1619 0.1376 0.2513 -0.0036 -0.0149 0.0037  41  LEU   A C   
285  O  O   . LEU   A 35  ? 0.1728 0.1496 0.2604 -0.0046 -0.0171 0.0049  41  LEU   A O   
286  C  CB  . LEU   A 35  ? 0.1474 0.1219 0.2422 -0.0041 -0.0175 0.0052  41  LEU   A CB  
287  C  CG  . LEU   A 35  ? 0.1666 0.1414 0.2692 -0.0027 -0.0158 0.0063  41  LEU   A CG  
288  C  CD1 . LEU   A 35  ? 0.1743 0.1473 0.2814 -0.0020 -0.0163 0.0078  41  LEU   A CD1 
289  C  CD2 . LEU   A 35  ? 0.1724 0.1503 0.2794 -0.0027 -0.0173 0.0086  41  LEU   A CD2 
290  N  N   . VAL   A 36  ? 0.1535 0.1289 0.2455 -0.0023 -0.0114 0.0032  42  VAL   A N   
291  C  CA  . VAL   A 36  ? 0.1559 0.1323 0.2505 -0.0022 -0.0093 0.0048  42  VAL   A CA  
292  C  C   . VAL   A 36  ? 0.1658 0.1440 0.2709 -0.0015 -0.0076 0.0063  42  VAL   A C   
293  O  O   . VAL   A 36  ? 0.1726 0.1497 0.2797 0.0001  -0.0052 0.0052  42  VAL   A O   
294  C  CB  . VAL   A 36  ? 0.1758 0.1500 0.2632 -0.0005 -0.0053 0.0033  42  VAL   A CB  
295  C  CG1 . VAL   A 36  ? 0.1820 0.1567 0.2734 -0.0004 -0.0018 0.0056  42  VAL   A CG1 
296  C  CG2 . VAL   A 36  ? 0.1801 0.1532 0.2579 -0.0007 -0.0075 0.0019  42  VAL   A CG2 
297  N  N   . SER   A 37  ? 0.1661 0.1473 0.2785 -0.0027 -0.0092 0.0085  43  SER   A N   
298  C  CA  . SER   A 37  ? 0.1722 0.1564 0.2965 -0.0020 -0.0081 0.0100  43  SER   A CA  
299  C  C   . SER   A 37  ? 0.1889 0.1750 0.3193 -0.0027 -0.0049 0.0112  43  SER   A C   
300  O  O   . SER   A 37  ? 0.1821 0.1668 0.3076 -0.0040 -0.0047 0.0112  43  SER   A O   
301  C  CB  . SER   A 37  ? 0.1918 0.1786 0.3217 -0.0026 -0.0139 0.0116  43  SER   A CB  
302  O  OG  . SER   A 37  ? 0.2091 0.1970 0.3372 -0.0046 -0.0182 0.0119  43  SER   A OG  
303  N  N   . SER   A 38  ? 0.2014 0.1905 0.3433 -0.0017 -0.0019 0.0123  44  SER   A N   
304  C  CA  . SER   A 38  ? 0.2100 0.2013 0.3600 -0.0026 0.0021  0.0138  44  SER   A CA  
305  C  C   . SER   A 38  ? 0.2159 0.2120 0.3774 -0.0051 -0.0030 0.0148  44  SER   A C   
306  O  O   . SER   A 38  ? 0.2198 0.2187 0.3857 -0.0051 -0.0088 0.0149  44  SER   A O   
307  C  CB  . SER   A 38  ? 0.2314 0.2237 0.3885 -0.0001 0.0090  0.0144  44  SER   A CB  
308  O  OG  . SER   A 38  ? 0.2657 0.2614 0.4324 0.0011  0.0065  0.0148  44  SER   A OG  
309  N  N   . THR   A 39  ? 0.2309 0.2276 0.3970 -0.0073 -0.0009 0.0156  45  THR   A N   
310  C  CA  . THR   A 39  ? 0.2603 0.2613 0.4381 -0.0101 -0.0060 0.0157  45  THR   A CA  
311  C  C   . THR   A 39  ? 0.3024 0.3073 0.4963 -0.0111 -0.0004 0.0173  45  THR   A C   
312  O  O   . THR   A 39  ? 0.3169 0.3193 0.5090 -0.0099 0.0081  0.0186  45  THR   A O   
313  C  CB  . THR   A 39  ? 0.2799 0.2774 0.4491 -0.0126 -0.0094 0.0147  45  THR   A CB  
314  O  OG1 . THR   A 39  ? 0.2945 0.2881 0.4607 -0.0131 -0.0025 0.0157  45  THR   A OG1 
315  C  CG2 . THR   A 39  ? 0.2776 0.2711 0.4310 -0.0115 -0.0133 0.0134  45  THR   A CG2 
316  N  N   . THR   A 40  ? 0.3245 0.3353 0.5338 -0.0133 -0.0050 0.0171  46  THR   A N   
317  C  CA  . THR   A 40  ? 0.3526 0.3679 0.5799 -0.0150 0.0000  0.0185  46  THR   A CA  
318  C  C   . THR   A 40  ? 0.3746 0.3866 0.6021 -0.0187 0.0012  0.0184  46  THR   A C   
319  O  O   . THR   A 40  ? 0.4034 0.4149 0.6385 -0.0197 0.0093  0.0204  46  THR   A O   
320  C  CB  . THR   A 40  ? 0.3822 0.4064 0.6284 -0.0153 -0.0057 0.0182  46  THR   A CB  
321  O  OG1 . THR   A 40  ? 0.4094 0.4345 0.6530 -0.0169 -0.0165 0.0159  46  THR   A OG1 
322  C  CG2 . THR   A 40  ? 0.3927 0.4196 0.6408 -0.0111 -0.0047 0.0190  46  THR   A CG2 
323  N  N   . ALA   A 41  ? 0.3581 0.3674 0.5772 -0.0206 -0.0062 0.0163  47  ALA   A N   
324  C  CA  . ALA   A 41  ? 0.3512 0.3564 0.5701 -0.0240 -0.0056 0.0158  47  ALA   A CA  
325  C  C   . ALA   A 41  ? 0.3548 0.3514 0.5552 -0.0225 0.0001  0.0169  47  ALA   A C   
326  O  O   . ALA   A 41  ? 0.3578 0.3517 0.5432 -0.0195 -0.0002 0.0167  47  ALA   A O   
327  C  CB  . ALA   A 41  ? 0.3507 0.3566 0.5692 -0.0262 -0.0163 0.0126  47  ALA   A CB  
328  N  N   . GLN   A 42  ? 0.3484 0.3407 0.5503 -0.0247 0.0049  0.0181  48  GLN   A N   
329  C  CA  . GLN   A 42  ? 0.3647 0.3486 0.5492 -0.0229 0.0100  0.0195  48  GLN   A CA  
330  C  C   . GLN   A 42  ? 0.3577 0.3378 0.5293 -0.0233 0.0027  0.0170  48  GLN   A C   
331  O  O   . GLN   A 42  ? 0.3539 0.3349 0.5321 -0.0264 -0.0036 0.0147  48  GLN   A O   
332  C  CB  . GLN   A 42  ? 0.4144 0.3944 0.6055 -0.0247 0.0182  0.0223  48  GLN   A CB  
333  C  CG  . GLN   A 42  ? 0.5114 0.4839 0.6859 -0.0210 0.0263  0.0251  48  GLN   A CG  
334  C  CD  . GLN   A 42  ? 0.6165 0.5910 0.7905 -0.0174 0.0335  0.0272  48  GLN   A CD  
335  O  OE1 . GLN   A 42  ? 0.6497 0.6302 0.8396 -0.0182 0.0360  0.0280  48  GLN   A OE1 
336  N  NE2 . GLN   A 42  ? 0.6469 0.6164 0.8028 -0.0131 0.0370  0.0280  48  GLN   A NE2 
337  N  N   . GLY   A 43  ? 0.3495 0.3256 0.5034 -0.0200 0.0032  0.0170  49  GLY   A N   
338  C  CA  . GLY   A 43  ? 0.3528 0.3256 0.4938 -0.0197 -0.0028 0.0148  49  GLY   A CA  
339  C  C   . GLY   A 43  ? 0.3623 0.3287 0.4984 -0.0210 -0.0018 0.0149  49  GLY   A C   
340  O  O   . GLY   A 43  ? 0.3850 0.3474 0.5218 -0.0208 0.0053  0.0176  49  GLY   A O   
341  N  N   . CYS   A 44  ? 0.3285 0.2931 0.4573 -0.0214 -0.0086 0.0123  50  CYS   A N   
342  C  CA  . CYS   A 44  ? 0.3073 0.2656 0.4309 -0.0225 -0.0095 0.0115  50  CYS   A CA  
343  C  C   . CYS   A 44  ? 0.3011 0.2539 0.4081 -0.0190 -0.0067 0.0126  50  CYS   A C   
344  O  O   . CYS   A 44  ? 0.2875 0.2341 0.3907 -0.0191 -0.0049 0.0131  50  CYS   A O   
345  C  CB  . CYS   A 44  ? 0.3108 0.2701 0.4354 -0.0243 -0.0183 0.0077  50  CYS   A CB  
346  S  SG  . CYS   A 44  ? 0.3478 0.3100 0.4597 -0.0214 -0.0245 0.0060  50  CYS   A SG  
347  N  N   . ASP   A 45  ? 0.2913 0.2463 0.3892 -0.0158 -0.0064 0.0129  51  ASP   A N   
348  C  CA  . ASP   A 45  ? 0.2788 0.2303 0.3618 -0.0123 -0.0054 0.0131  51  ASP   A CA  
349  C  C   . ASP   A 45  ? 0.2793 0.2280 0.3562 -0.0092 0.0016  0.0160  51  ASP   A C   
350  O  O   . ASP   A 45  ? 0.2908 0.2413 0.3740 -0.0093 0.0061  0.0176  51  ASP   A O   
351  C  CB  . ASP   A 45  ? 0.2748 0.2306 0.3519 -0.0109 -0.0102 0.0111  51  ASP   A CB  
352  C  CG  . ASP   A 45  ? 0.3029 0.2600 0.3808 -0.0125 -0.0169 0.0086  51  ASP   A CG  
353  O  OD1 . ASP   A 45  ? 0.3041 0.2571 0.3776 -0.0127 -0.0185 0.0077  51  ASP   A OD1 
354  O  OD2 . ASP   A 45  ? 0.2615 0.2234 0.3432 -0.0131 -0.0204 0.0077  51  ASP   A OD2 
355  N  N   . THR   A 46  ? 0.2669 0.2113 0.3311 -0.0059 0.0025  0.0165  52  THR   A N   
356  C  CA  . THR   A 46  ? 0.2776 0.2192 0.3321 -0.0017 0.0077  0.0187  52  THR   A CA  
357  C  C   . THR   A 46  ? 0.2592 0.2028 0.3020 0.0017  0.0038  0.0165  52  THR   A C   
358  O  O   . THR   A 46  ? 0.2555 0.2002 0.2966 0.0011  -0.0011 0.0145  52  THR   A O   
359  C  CB  . THR   A 46  ? 0.3287 0.2629 0.3807 -0.0006 0.0134  0.0222  52  THR   A CB  
360  O  OG1 . THR   A 46  ? 0.3527 0.2831 0.3989 0.0000  0.0103  0.0214  52  THR   A OG1 
361  C  CG2 . THR   A 46  ? 0.3442 0.2769 0.4101 -0.0046 0.0175  0.0241  52  THR   A CG2 
362  N  N   . ILE   A 47  ? 0.2423 0.1868 0.2782 0.0051  0.0059  0.0166  53  ILE   A N   
363  C  CA  . ILE   A 47  ? 0.2238 0.1714 0.2516 0.0077  0.0018  0.0139  53  ILE   A CA  
364  C  C   . ILE   A 47  ? 0.2313 0.1752 0.2470 0.0124  0.0028  0.0149  53  ILE   A C   
365  O  O   . ILE   A 47  ? 0.2450 0.1842 0.2553 0.0152  0.0080  0.0177  53  ILE   A O   
366  C  CB  . ILE   A 47  ? 0.2229 0.1741 0.2513 0.0085  0.0026  0.0123  53  ILE   A CB  
367  C  CG1 . ILE   A 47  ? 0.2332 0.1878 0.2741 0.0045  0.0023  0.0119  53  ILE   A CG1 
368  C  CG2 . ILE   A 47  ? 0.2317 0.1866 0.2545 0.0101  -0.0023 0.0087  53  ILE   A CG2 
369  C  CD1 . ILE   A 47  ? 0.2352 0.1934 0.2816 0.0014  -0.0037 0.0101  53  ILE   A CD1 
370  N  N   . ALA   A 48  ? 0.2052 0.1511 0.2165 0.0136  -0.0019 0.0129  54  ALA   A N   
371  C  CA  . ALA   A 48  ? 0.2177 0.1610 0.2177 0.0186  -0.0020 0.0135  54  ALA   A CA  
372  C  C   . ALA   A 48  ? 0.2290 0.1743 0.2218 0.0224  -0.0020 0.0120  54  ALA   A C   
373  O  O   . ALA   A 48  ? 0.2288 0.1789 0.2253 0.0208  -0.0043 0.0090  54  ALA   A O   
374  C  CB  . ALA   A 48  ? 0.2041 0.1507 0.2036 0.0189  -0.0073 0.0113  54  ALA   A CB  
375  N  N   . ARG   A 49  ? 0.2346 0.1755 0.2161 0.0277  0.0003  0.0140  55  ARG   A N   
376  C  CA  . ARG   A 49  ? 0.2459 0.1880 0.2180 0.0322  -0.0004 0.0121  55  ARG   A CA  
377  C  C   . ARG   A 49  ? 0.2698 0.2112 0.2319 0.0375  -0.0036 0.0122  55  ARG   A C   
378  O  O   . ARG   A 49  ? 0.2862 0.2214 0.2388 0.0420  -0.0001 0.0159  55  ARG   A O   
379  C  CB  . ARG   A 49  ? 0.2580 0.1946 0.2249 0.0344  0.0066  0.0152  55  ARG   A CB  
380  C  CG  . ARG   A 49  ? 0.2593 0.1967 0.2379 0.0294  0.0104  0.0158  55  ARG   A CG  
381  C  CD  . ARG   A 49  ? 0.2758 0.2194 0.2604 0.0270  0.0067  0.0111  55  ARG   A CD  
382  N  NE  . ARG   A 49  ? 0.2621 0.2062 0.2576 0.0230  0.0106  0.0122  55  ARG   A NE  
383  C  CZ  . ARG   A 49  ? 0.2734 0.2224 0.2780 0.0196  0.0080  0.0093  55  ARG   A CZ  
384  N  NH1 . ARG   A 49  ? 0.2385 0.1917 0.2426 0.0193  0.0021  0.0052  55  ARG   A NH1 
385  N  NH2 . ARG   A 49  ? 0.2658 0.2153 0.2805 0.0167  0.0114  0.0107  55  ARG   A NH2 
386  N  N   . CYS   A 50  ? 0.2651 0.2128 0.2304 0.0369  -0.0099 0.0085  56  CYS   A N   
387  C  CA  . CYS   A 50  ? 0.2781 0.2267 0.2377 0.0411  -0.0135 0.0084  56  CYS   A CA  
388  C  C   . CYS   A 50  ? 0.2794 0.2369 0.2437 0.0405  -0.0204 0.0031  56  CYS   A C   
389  O  O   . CYS   A 50  ? 0.2799 0.2420 0.2518 0.0365  -0.0219 -0.0001 56  CYS   A O   
390  C  CB  . CYS   A 50  ? 0.2749 0.2199 0.2385 0.0394  -0.0118 0.0115  56  CYS   A CB  
391  S  SG  . CYS   A 50  ? 0.2739 0.2244 0.2517 0.0323  -0.0145 0.0089  56  CYS   A SG  
392  N  N   . ASP   A 51  ? 0.2925 0.2526 0.2537 0.0444  -0.0243 0.0026  57  ASP   A N   
393  C  CA  . ASP   A 51  ? 0.2916 0.2607 0.2593 0.0438  -0.0304 -0.0020 57  ASP   A CA  
394  C  C   . ASP   A 51  ? 0.2919 0.2628 0.2656 0.0427  -0.0311 -0.0010 57  ASP   A C   
395  O  O   . ASP   A 51  ? 0.2976 0.2751 0.2744 0.0446  -0.0355 -0.0034 57  ASP   A O   
396  C  CB  . ASP   A 51  ? 0.3486 0.3212 0.3083 0.0500  -0.0354 -0.0048 57  ASP   A CB  
397  C  CG  . ASP   A 51  ? 0.4476 0.4160 0.3965 0.0569  -0.0353 -0.0014 57  ASP   A CG  
398  O  OD1 . ASP   A 51  ? 0.4393 0.4012 0.3869 0.0568  -0.0307 0.0034  57  ASP   A OD1 
399  O  OD2 . ASP   A 51  ? 0.5465 0.5180 0.4884 0.0627  -0.0400 -0.0035 57  ASP   A OD2 
400  N  N   . CYS   A 52  ? 0.2697 0.2353 0.2462 0.0395  -0.0270 0.0023  58  CYS   A N   
401  C  CA  . CYS   A 52  ? 0.2577 0.2242 0.2390 0.0386  -0.0274 0.0028  58  CYS   A CA  
402  C  C   . CYS   A 52  ? 0.2468 0.2219 0.2380 0.0353  -0.0306 -0.0008 58  CYS   A C   
403  O  O   . CYS   A 52  ? 0.2347 0.2127 0.2312 0.0313  -0.0310 -0.0028 58  CYS   A O   
404  C  CB  . CYS   A 52  ? 0.2529 0.2123 0.2360 0.0351  -0.0231 0.0058  58  CYS   A CB  
405  S  SG  . CYS   A 52  ? 0.2791 0.2273 0.2529 0.0388  -0.0184 0.0108  58  CYS   A SG  
406  N  N   . GLN   A 53  ? 0.2248 0.2035 0.2187 0.0371  -0.0324 -0.0013 59  GLN   A N   
407  C  CA  . GLN   A 53  ? 0.2185 0.2048 0.2222 0.0343  -0.0342 -0.0038 59  GLN   A CA  
408  C  C   . GLN   A 53  ? 0.2041 0.1882 0.2099 0.0334  -0.0320 -0.0022 59  GLN   A C   
409  O  O   . GLN   A 53  ? 0.2155 0.2053 0.2278 0.0326  -0.0327 -0.0036 59  GLN   A O   
410  C  CB  . GLN   A 53  ? 0.2518 0.2469 0.2590 0.0374  -0.0386 -0.0069 59  GLN   A CB  
411  C  CG  . GLN   A 53  ? 0.2986 0.2978 0.3075 0.0364  -0.0415 -0.0102 59  GLN   A CG  
412  C  CD  . GLN   A 53  ? 0.3435 0.3523 0.3580 0.0391  -0.0466 -0.0139 59  GLN   A CD  
413  O  OE1 . GLN   A 53  ? 0.3561 0.3660 0.3644 0.0441  -0.0502 -0.0152 59  GLN   A OE1 
414  N  NE2 . GLN   A 53  ? 0.3046 0.3203 0.3311 0.0360  -0.0470 -0.0156 59  GLN   A NE2 
415  N  N   . THR   A 54  ? 0.2040 0.1792 0.2040 0.0337  -0.0291 0.0006  60  THR   A N   
416  C  CA  . THR   A 54  ? 0.2049 0.1764 0.2059 0.0323  -0.0271 0.0015  60  THR   A CA  
417  C  C   . THR   A 54  ? 0.1952 0.1593 0.1948 0.0284  -0.0247 0.0030  60  THR   A C   
418  O  O   . THR   A 54  ? 0.2162 0.1761 0.2125 0.0284  -0.0235 0.0044  60  THR   A O   
419  C  CB  . THR   A 54  ? 0.2365 0.2047 0.2329 0.0373  -0.0265 0.0028  60  THR   A CB  
420  O  OG1 . THR   A 54  ? 0.2627 0.2229 0.2519 0.0396  -0.0249 0.0053  60  THR   A OG1 
421  C  CG2 . THR   A 54  ? 0.2419 0.2182 0.2407 0.0417  -0.0292 0.0014  60  THR   A CG2 
422  N  N   . GLY   A 55  ? 0.1860 0.1484 0.1881 0.0253  -0.0241 0.0026  61  GLY   A N   
423  C  CA  . GLY   A 55  ? 0.1872 0.1437 0.1897 0.0215  -0.0228 0.0034  61  GLY   A CA  
424  C  C   . GLY   A 55  ? 0.1885 0.1438 0.1923 0.0194  -0.0231 0.0023  61  GLY   A C   
425  O  O   . GLY   A 55  ? 0.1957 0.1529 0.1986 0.0216  -0.0233 0.0015  61  GLY   A O   
426  N  N   . VAL   A 56  ? 0.1846 0.1366 0.1903 0.0156  -0.0232 0.0023  62  VAL   A N   
427  C  CA  . VAL   A 56  ? 0.1919 0.1419 0.1975 0.0138  -0.0242 0.0010  62  VAL   A CA  
428  C  C   . VAL   A 56  ? 0.1866 0.1399 0.1969 0.0100  -0.0254 0.0009  62  VAL   A C   
429  O  O   . VAL   A 56  ? 0.1951 0.1477 0.2086 0.0079  -0.0252 0.0017  62  VAL   A O   
430  C  CB  . VAL   A 56  ? 0.2233 0.1646 0.2264 0.0133  -0.0239 0.0008  62  VAL   A CB  
431  C  CG1 . VAL   A 56  ? 0.2302 0.1691 0.2325 0.0113  -0.0259 -0.0012 62  VAL   A CG1 
432  C  CG2 . VAL   A 56  ? 0.2473 0.1846 0.2454 0.0176  -0.0223 0.0012  62  VAL   A CG2 
433  N  N   . TYR   A 57  ? 0.1980 0.1541 0.2085 0.0093  -0.0264 0.0002  63  TYR   A N   
434  C  CA  . TYR   A 57  ? 0.1804 0.1387 0.1948 0.0063  -0.0277 0.0004  63  TYR   A CA  
435  C  C   . TYR   A 57  ? 0.1837 0.1386 0.1952 0.0054  -0.0296 -0.0004 63  TYR   A C   
436  O  O   . TYR   A 57  ? 0.1901 0.1422 0.1961 0.0074  -0.0295 -0.0014 63  TYR   A O   
437  C  CB  . TYR   A 57  ? 0.1755 0.1405 0.1933 0.0062  -0.0271 0.0009  63  TYR   A CB  
438  C  CG  . TYR   A 57  ? 0.1805 0.1474 0.1961 0.0076  -0.0263 0.0009  63  TYR   A CG  
439  C  CD1 . TYR   A 57  ? 0.1816 0.1498 0.1951 0.0105  -0.0248 0.0005  63  TYR   A CD1 
440  C  CD2 . TYR   A 57  ? 0.1900 0.1577 0.2058 0.0063  -0.0265 0.0017  63  TYR   A CD2 
441  C  CE1 . TYR   A 57  ? 0.1851 0.1556 0.1976 0.0120  -0.0231 0.0008  63  TYR   A CE1 
442  C  CE2 . TYR   A 57  ? 0.2003 0.1695 0.2139 0.0079  -0.0247 0.0023  63  TYR   A CE2 
443  C  CZ  . TYR   A 57  ? 0.2082 0.1788 0.2202 0.0106  -0.0228 0.0018  63  TYR   A CZ  
444  O  OH  . TYR   A 57  ? 0.2249 0.1972 0.2353 0.0124  -0.0200 0.0026  63  TYR   A OH  
445  N  N   . TYR   A 58  ? 0.1728 0.1282 0.1878 0.0029  -0.0315 -0.0002 64  TYR   A N   
446  C  CA  . TYR   A 58  ? 0.1778 0.1305 0.1895 0.0024  -0.0343 -0.0012 64  TYR   A CA  
447  C  C   . TYR   A 58  ? 0.1925 0.1487 0.2025 0.0033  -0.0340 0.0000  64  TYR   A C   
448  O  O   . TYR   A 58  ? 0.1808 0.1412 0.1960 0.0021  -0.0332 0.0016  64  TYR   A O   
449  C  CB  . TYR   A 58  ? 0.1822 0.1339 0.1995 -0.0005 -0.0371 -0.0016 64  TYR   A CB  
450  C  CG  . TYR   A 58  ? 0.1954 0.1446 0.2090 -0.0005 -0.0412 -0.0032 64  TYR   A CG  
451  C  CD1 . TYR   A 58  ? 0.2082 0.1518 0.2154 0.0006  -0.0428 -0.0058 64  TYR   A CD1 
452  C  CD2 . TYR   A 58  ? 0.2105 0.1625 0.2260 -0.0011 -0.0435 -0.0022 64  TYR   A CD2 
453  C  CE1 . TYR   A 58  ? 0.2331 0.1742 0.2354 0.0011  -0.0471 -0.0078 64  TYR   A CE1 
454  C  CE2 . TYR   A 58  ? 0.2312 0.1810 0.2418 -0.0004 -0.0478 -0.0036 64  TYR   A CE2 
455  C  CZ  . TYR   A 58  ? 0.2485 0.1929 0.2520 0.0007  -0.0497 -0.0066 64  TYR   A CZ  
456  O  OH  . TYR   A 58  ? 0.3031 0.2449 0.3005 0.0018  -0.0546 -0.0087 64  TYR   A OH  
457  N  N   . CYS   A 59  ? 0.1974 0.1512 0.1997 0.0054  -0.0342 -0.0006 65  CYS   A N   
458  C  CA  . CYS   A 59  ? 0.1856 0.1415 0.1848 0.0068  -0.0329 0.0012  65  CYS   A CA  
459  C  C   . CYS   A 59  ? 0.2016 0.1540 0.1952 0.0071  -0.0367 0.0006  65  CYS   A C   
460  O  O   . CYS   A 59  ? 0.2087 0.1565 0.1939 0.0091  -0.0380 -0.0014 65  CYS   A O   
461  C  CB  . CYS   A 59  ? 0.1955 0.1516 0.1898 0.0098  -0.0293 0.0012  65  CYS   A CB  
462  S  SG  . CYS   A 59  ? 0.2295 0.1869 0.2190 0.0119  -0.0262 0.0038  65  CYS   A SG  
463  N  N   . SER   A 60  ? 0.2013 0.1558 0.1990 0.0056  -0.0386 0.0022  66  SER   A N   
464  C  CA  . SER   A 60  ? 0.2293 0.1810 0.2220 0.0063  -0.0432 0.0016  66  SER   A CA  
465  C  C   . SER   A 60  ? 0.2335 0.1824 0.2144 0.0100  -0.0423 0.0025  66  SER   A C   
466  O  O   . SER   A 60  ? 0.2326 0.1773 0.2053 0.0117  -0.0464 0.0003  66  SER   A O   
467  C  CB  . SER   A 60  ? 0.2901 0.2450 0.2903 0.0046  -0.0453 0.0035  66  SER   A CB  
468  O  OG  . SER   A 60  ? 0.3696 0.3272 0.3713 0.0051  -0.0415 0.0069  66  SER   A OG  
469  N  N   . SER   A 61  ? 0.2064 0.1574 0.1863 0.0114  -0.0368 0.0053  67  SER   A N   
470  C  CA  . SER   A 61  ? 0.2253 0.1735 0.1940 0.0152  -0.0344 0.0068  67  SER   A CA  
471  C  C   . SER   A 61  ? 0.2265 0.1704 0.1859 0.0179  -0.0338 0.0039  67  SER   A C   
472  O  O   . SER   A 61  ? 0.2342 0.1749 0.1825 0.0216  -0.0318 0.0047  67  SER   A O   
473  C  CB  . SER   A 61  ? 0.2465 0.1984 0.2188 0.0156  -0.0280 0.0109  67  SER   A CB  
474  O  OG  . SER   A 61  ? 0.2494 0.2049 0.2286 0.0145  -0.0243 0.0101  67  SER   A OG  
475  N  N   . ARG   A 62  ? 0.2044 0.1476 0.1675 0.0164  -0.0351 0.0006  68  ARG   A N   
476  C  CA  . ARG   A 62  ? 0.2116 0.1496 0.1662 0.0189  -0.0351 -0.0026 68  ARG   A CA  
477  C  C   . ARG   A 62  ? 0.2313 0.1649 0.1865 0.0170  -0.0412 -0.0070 68  ARG   A C   
478  O  O   . ARG   A 62  ? 0.2589 0.1871 0.2080 0.0186  -0.0418 -0.0104 68  ARG   A O   
479  C  CB  . ARG   A 62  ? 0.2279 0.1684 0.1870 0.0195  -0.0299 -0.0023 68  ARG   A CB  
480  C  CG  . ARG   A 62  ? 0.2487 0.1936 0.2082 0.0215  -0.0237 0.0012  68  ARG   A CG  
481  C  CD  . ARG   A 62  ? 0.2738 0.2142 0.2202 0.0261  -0.0211 0.0011  68  ARG   A CD  
482  N  NE  . ARG   A 62  ? 0.2849 0.2295 0.2329 0.0279  -0.0141 0.0049  68  ARG   A NE  
483  C  CZ  . ARG   A 62  ? 0.2996 0.2457 0.2471 0.0280  -0.0119 0.0087  68  ARG   A CZ  
484  N  NH1 . ARG   A 62  ? 0.2857 0.2296 0.2303 0.0268  -0.0165 0.0093  68  ARG   A NH1 
485  N  NH2 . ARG   A 62  ? 0.2933 0.2430 0.2437 0.0293  -0.0049 0.0122  68  ARG   A NH2 
486  N  N   . ARG   A 63  ? 0.2371 0.1730 0.2010 0.0134  -0.0451 -0.0069 69  ARG   A N   
487  C  CA  . ARG   A 63  ? 0.2683 0.2013 0.2368 0.0107  -0.0501 -0.0105 69  ARG   A CA  
488  C  C   . ARG   A 63  ? 0.2669 0.1970 0.2374 0.0103  -0.0475 -0.0122 69  ARG   A C   
489  O  O   . ARG   A 63  ? 0.2891 0.2131 0.2565 0.0103  -0.0501 -0.0161 69  ARG   A O   
490  C  CB  . ARG   A 63  ? 0.3114 0.2392 0.2713 0.0121  -0.0562 -0.0143 69  ARG   A CB  
491  C  CG  . ARG   A 63  ? 0.3984 0.3286 0.3568 0.0126  -0.0601 -0.0127 69  ARG   A CG  
492  C  CD  . ARG   A 63  ? 0.4489 0.3750 0.4045 0.0122  -0.0683 -0.0178 69  ARG   A CD  
493  N  NE  . ARG   A 63  ? 0.4744 0.4020 0.4248 0.0143  -0.0727 -0.0165 69  ARG   A NE  
494  C  CZ  . ARG   A 63  ? 0.4723 0.3955 0.4071 0.0189  -0.0748 -0.0176 69  ARG   A CZ  
495  N  NH1 . ARG   A 63  ? 0.4703 0.3874 0.3935 0.0217  -0.0729 -0.0204 69  ARG   A NH1 
496  N  NH2 . ARG   A 63  ? 0.4498 0.3745 0.3797 0.0214  -0.0784 -0.0155 69  ARG   A NH2 
497  N  N   . LYS   A 64  ? 0.2419 0.1759 0.2171 0.0104  -0.0424 -0.0095 70  LYS   A N   
498  C  CA  . LYS   A 64  ? 0.2420 0.1734 0.2179 0.0112  -0.0397 -0.0106 70  LYS   A CA  
499  C  C   . LYS   A 64  ? 0.2269 0.1634 0.2116 0.0098  -0.0366 -0.0079 70  LYS   A C   
500  O  O   . LYS   A 64  ? 0.2374 0.1798 0.2261 0.0092  -0.0353 -0.0053 70  LYS   A O   
501  C  CB  . LYS   A 64  ? 0.2761 0.2061 0.2433 0.0156  -0.0360 -0.0107 70  LYS   A CB  
502  C  CG  . LYS   A 64  ? 0.4063 0.3283 0.3627 0.0181  -0.0380 -0.0145 70  LYS   A CG  
503  C  CD  . LYS   A 64  ? 0.5048 0.4258 0.4539 0.0227  -0.0331 -0.0143 70  LYS   A CD  
504  C  CE  . LYS   A 64  ? 0.5891 0.5011 0.5273 0.0256  -0.0346 -0.0187 70  LYS   A CE  
505  N  NZ  . LYS   A 64  ? 0.6480 0.5588 0.5745 0.0298  -0.0327 -0.0186 70  LYS   A NZ  
506  N  N   . HIS   A 65  ? 0.2195 0.1531 0.2062 0.0099  -0.0353 -0.0085 71  HIS   A N   
507  C  CA  . HIS   A 65  ? 0.2115 0.1491 0.2041 0.0097  -0.0324 -0.0062 71  HIS   A CA  
508  C  C   . HIS   A 65  ? 0.2252 0.1642 0.2143 0.0136  -0.0291 -0.0057 71  HIS   A C   
509  O  O   . HIS   A 65  ? 0.2449 0.1789 0.2277 0.0163  -0.0285 -0.0074 71  HIS   A O   
510  C  CB  . HIS   A 65  ? 0.2044 0.1376 0.2009 0.0081  -0.0325 -0.0065 71  HIS   A CB  
511  C  CG  . HIS   A 65  ? 0.2330 0.1658 0.2357 0.0041  -0.0352 -0.0069 71  HIS   A CG  
512  N  ND1 . HIS   A 65  ? 0.2664 0.2034 0.2764 0.0020  -0.0342 -0.0047 71  HIS   A ND1 
513  C  CD2 . HIS   A 65  ? 0.2324 0.1608 0.2353 0.0021  -0.0389 -0.0095 71  HIS   A CD2 
514  C  CE1 . HIS   A 65  ? 0.2553 0.1910 0.2706 -0.0011 -0.0369 -0.0057 71  HIS   A CE1 
515  N  NE2 . HIS   A 65  ? 0.2767 0.2077 0.2885 -0.0013 -0.0401 -0.0087 71  HIS   A NE2 
516  N  N   . TYR   A 66  ? 0.1938 0.1395 0.1875 0.0141  -0.0270 -0.0036 72  TYR   A N   
517  C  CA  . TYR   A 66  ? 0.1903 0.1390 0.1829 0.0178  -0.0243 -0.0032 72  TYR   A CA  
518  C  C   . TYR   A 66  ? 0.1963 0.1481 0.1934 0.0184  -0.0236 -0.0020 72  TYR   A C   
519  O  O   . TYR   A 66  ? 0.2056 0.1606 0.2074 0.0161  -0.0244 -0.0011 72  TYR   A O   
520  C  CB  . TYR   A 66  ? 0.2029 0.1584 0.1974 0.0182  -0.0226 -0.0021 72  TYR   A CB  
521  C  CG  . TYR   A 66  ? 0.2260 0.1786 0.2140 0.0190  -0.0223 -0.0026 72  TYR   A CG  
522  C  CD1 . TYR   A 66  ? 0.2468 0.1956 0.2279 0.0227  -0.0205 -0.0039 72  TYR   A CD1 
523  C  CD2 . TYR   A 66  ? 0.2314 0.1850 0.2194 0.0168  -0.0235 -0.0017 72  TYR   A CD2 
524  C  CE1 . TYR   A 66  ? 0.2647 0.2103 0.2379 0.0241  -0.0199 -0.0044 72  TYR   A CE1 
525  C  CE2 . TYR   A 66  ? 0.2471 0.1976 0.2274 0.0183  -0.0232 -0.0019 72  TYR   A CE2 
526  C  CZ  . TYR   A 66  ? 0.2784 0.2250 0.2508 0.0220  -0.0214 -0.0033 72  TYR   A CZ  
527  O  OH  . TYR   A 66  ? 0.3108 0.2538 0.2738 0.0241  -0.0209 -0.0036 72  TYR   A OH  
528  N  N   . PRO   A 67  ? 0.1971 0.1480 0.1922 0.0222  -0.0222 -0.0020 73  PRO   A N   
529  C  CA  . PRO   A 67  ? 0.1999 0.1544 0.1980 0.0239  -0.0220 -0.0009 73  PRO   A CA  
530  C  C   . PRO   A 67  ? 0.2216 0.1861 0.2254 0.0243  -0.0219 -0.0007 73  PRO   A C   
531  O  O   . PRO   A 67  ? 0.2395 0.2075 0.2445 0.0251  -0.0206 -0.0011 73  PRO   A O   
532  C  CB  . PRO   A 67  ? 0.2184 0.1684 0.2121 0.0284  -0.0208 -0.0009 73  PRO   A CB  
533  C  CG  . PRO   A 67  ? 0.2279 0.1760 0.2182 0.0297  -0.0197 -0.0024 73  PRO   A CG  
534  C  CD  . PRO   A 67  ? 0.2021 0.1488 0.1917 0.0257  -0.0208 -0.0032 73  PRO   A CD  
535  N  N   . VAL   A 68  ? 0.2016 0.1704 0.2091 0.0239  -0.0230 -0.0004 74  VAL   A N   
536  C  CA  . VAL   A 68  ? 0.2061 0.1841 0.2204 0.0237  -0.0235 -0.0010 74  VAL   A CA  
537  C  C   . VAL   A 68  ? 0.2054 0.1870 0.2208 0.0263  -0.0252 -0.0013 74  VAL   A C   
538  O  O   . VAL   A 68  ? 0.2111 0.1880 0.2220 0.0272  -0.0257 -0.0005 74  VAL   A O   
539  C  CB  . VAL   A 68  ? 0.2220 0.2024 0.2407 0.0191  -0.0241 -0.0010 74  VAL   A CB  
540  C  CG1 . VAL   A 68  ? 0.2378 0.2182 0.2572 0.0173  -0.0226 -0.0006 74  VAL   A CG1 
541  C  CG2 . VAL   A 68  ? 0.2365 0.2116 0.2527 0.0169  -0.0249 -0.0005 74  VAL   A CG2 
542  N  N   . SER   A 69  ? 0.1991 0.1893 0.2207 0.0278  -0.0261 -0.0025 75  SER   A N   
543  C  CA  . SER   A 69  ? 0.2046 0.1999 0.2284 0.0299  -0.0289 -0.0037 75  SER   A CA  
544  C  C   . SER   A 69  ? 0.1881 0.1889 0.2192 0.0257  -0.0299 -0.0053 75  SER   A C   
545  O  O   . SER   A 69  ? 0.1963 0.2011 0.2339 0.0235  -0.0284 -0.0055 75  SER   A O   
546  C  CB  . SER   A 69  ? 0.2542 0.2562 0.2820 0.0343  -0.0298 -0.0045 75  SER   A CB  
547  O  OG  . SER   A 69  ? 0.3314 0.3271 0.3517 0.0384  -0.0287 -0.0029 75  SER   A OG  
548  N  N   . PHE   A 70  ? 0.1716 0.1718 0.2013 0.0248  -0.0318 -0.0062 76  PHE   A N   
549  C  CA  . PHE   A 70  ? 0.1763 0.1802 0.2126 0.0208  -0.0325 -0.0079 76  PHE   A CA  
550  C  C   . PHE   A 70  ? 0.1796 0.1886 0.2181 0.0222  -0.0361 -0.0109 76  PHE   A C   
551  O  O   . PHE   A 70  ? 0.1992 0.2069 0.2311 0.0262  -0.0381 -0.0111 76  PHE   A O   
552  C  CB  . PHE   A 70  ? 0.1756 0.1731 0.2089 0.0173  -0.0307 -0.0064 76  PHE   A CB  
553  C  CG  . PHE   A 70  ? 0.1766 0.1674 0.2016 0.0187  -0.0305 -0.0051 76  PHE   A CG  
554  C  CD1 . PHE   A 70  ? 0.1880 0.1722 0.2072 0.0198  -0.0287 -0.0028 76  PHE   A CD1 
555  C  CD2 . PHE   A 70  ? 0.1828 0.1732 0.2059 0.0189  -0.0315 -0.0062 76  PHE   A CD2 
556  C  CE1 . PHE   A 70  ? 0.1931 0.1708 0.2063 0.0206  -0.0276 -0.0012 76  PHE   A CE1 
557  C  CE2 . PHE   A 70  ? 0.1937 0.1776 0.2094 0.0204  -0.0301 -0.0044 76  PHE   A CE2 
558  C  CZ  . PHE   A 70  ? 0.2011 0.1788 0.2126 0.0210  -0.0280 -0.0017 76  PHE   A CZ  
559  N  N   . SER   A 71  ? 0.1649 0.1797 0.2128 0.0191  -0.0372 -0.0135 77  SER   A N   
560  C  CA  . SER   A 71  ? 0.1735 0.1932 0.2242 0.0200  -0.0414 -0.0174 77  SER   A CA  
561  C  C   . SER   A 71  ? 0.1932 0.2074 0.2366 0.0197  -0.0419 -0.0180 77  SER   A C   
562  O  O   . SER   A 71  ? 0.2001 0.2079 0.2398 0.0175  -0.0388 -0.0154 77  SER   A O   
563  C  CB  . SER   A 71  ? 0.1925 0.2193 0.2567 0.0163  -0.0421 -0.0202 77  SER   A CB  
564  O  OG  . SER   A 71  ? 0.2284 0.2515 0.2953 0.0116  -0.0389 -0.0189 77  SER   A OG  
565  N  N   . LYS   A 72  ? 0.1876 0.2042 0.2285 0.0223  -0.0460 -0.0215 78  LYS   A N   
566  C  CA  . LYS   A 72  ? 0.2025 0.2139 0.2359 0.0226  -0.0461 -0.0223 78  LYS   A CA  
567  C  C   . LYS   A 72  ? 0.2142 0.2251 0.2548 0.0174  -0.0447 -0.0238 78  LYS   A C   
568  O  O   . LYS   A 72  ? 0.2169 0.2330 0.2686 0.0142  -0.0454 -0.0257 78  LYS   A O   
569  C  CB  . LYS   A 72  ? 0.2542 0.2688 0.2831 0.0270  -0.0514 -0.0265 78  LYS   A CB  
570  C  CG  . LYS   A 72  ? 0.3167 0.3299 0.3357 0.0332  -0.0524 -0.0243 78  LYS   A CG  
571  C  CD  . LYS   A 72  ? 0.3782 0.3944 0.3913 0.0381  -0.0583 -0.0285 78  LYS   A CD  
572  C  CE  . LYS   A 72  ? 0.4784 0.4939 0.4824 0.0449  -0.0599 -0.0262 78  LYS   A CE  
573  N  NZ  . LYS   A 72  ? 0.5414 0.5604 0.5391 0.0504  -0.0665 -0.0304 78  LYS   A NZ  
574  N  N   . PRO   A 73  ? 0.2176 0.2223 0.2525 0.0166  -0.0425 -0.0230 79  PRO   A N   
575  C  CA  . PRO   A 73  ? 0.2150 0.2188 0.2568 0.0122  -0.0411 -0.0243 79  PRO   A CA  
576  C  C   . PRO   A 73  ? 0.2160 0.2249 0.2654 0.0109  -0.0449 -0.0299 79  PRO   A C   
577  O  O   . PRO   A 73  ? 0.2272 0.2376 0.2719 0.0141  -0.0488 -0.0338 79  PRO   A O   
578  C  CB  . PRO   A 73  ? 0.2342 0.2313 0.2677 0.0132  -0.0387 -0.0232 79  PRO   A CB  
579  C  CG  . PRO   A 73  ? 0.2639 0.2575 0.2874 0.0169  -0.0373 -0.0196 79  PRO   A CG  
580  C  CD  . PRO   A 73  ? 0.2360 0.2342 0.2588 0.0200  -0.0406 -0.0205 79  PRO   A CD  
581  N  N   . SER   A 74  ? 0.1916 0.2031 0.2528 0.0064  -0.0438 -0.0303 80  SER   A N   
582  C  CA  A SER   A 74  ? 0.2026 0.2190 0.2735 0.0045  -0.0472 -0.0358 80  SER   A CA  
583  C  CA  B SER   A 74  ? 0.1994 0.2161 0.2708 0.0044  -0.0471 -0.0357 80  SER   A CA  
584  C  C   . SER   A 74  ? 0.1960 0.2109 0.2772 -0.0006 -0.0442 -0.0355 80  SER   A C   
585  O  O   . SER   A 74  ? 0.1917 0.2022 0.2717 -0.0022 -0.0399 -0.0308 80  SER   A O   
586  C  CB  A SER   A 74  ? 0.2233 0.2479 0.3011 0.0055  -0.0503 -0.0375 80  SER   A CB  
587  C  CB  B SER   A 74  ? 0.2110 0.2358 0.2903 0.0049  -0.0494 -0.0366 80  SER   A CB  
588  O  OG  A SER   A 74  ? 0.2467 0.2734 0.3321 0.0031  -0.0466 -0.0336 80  SER   A OG  
589  O  OG  B SER   A 74  ? 0.2396 0.2658 0.3103 0.0099  -0.0514 -0.0355 80  SER   A OG  
590  N  N   . LEU   A 75  ? 0.1907 0.2090 0.2823 -0.0032 -0.0468 -0.0407 81  LEU   A N   
591  C  CA  . LEU   A 75  ? 0.2072 0.2237 0.3097 -0.0080 -0.0440 -0.0406 81  LEU   A CA  
592  C  C   . LEU   A 75  ? 0.2175 0.2392 0.3311 -0.0104 -0.0418 -0.0381 81  LEU   A C   
593  O  O   . LEU   A 75  ? 0.2176 0.2466 0.3392 -0.0104 -0.0450 -0.0415 81  LEU   A O   
594  C  CB  . LEU   A 75  ? 0.2227 0.2405 0.3319 -0.0095 -0.0481 -0.0482 81  LEU   A CB  
595  C  CG  . LEU   A 75  ? 0.2847 0.2954 0.3888 -0.0095 -0.0477 -0.0506 81  LEU   A CG  
596  C  CD1 . LEU   A 75  ? 0.2976 0.3100 0.4091 -0.0110 -0.0525 -0.0590 81  LEU   A CD1 
597  C  CD2 . LEU   A 75  ? 0.2881 0.2927 0.3954 -0.0125 -0.0418 -0.0456 81  LEU   A CD2 
598  N  N   . ILE   A 76  ? 0.2027 0.2209 0.3174 -0.0123 -0.0365 -0.0323 82  ILE   A N   
599  C  CA  . ILE   A 76  ? 0.2165 0.2384 0.3389 -0.0138 -0.0332 -0.0287 82  ILE   A CA  
600  C  C   . ILE   A 76  ? 0.2136 0.2318 0.3440 -0.0177 -0.0285 -0.0259 82  ILE   A C   
601  O  O   . ILE   A 76  ? 0.2224 0.2338 0.3470 -0.0179 -0.0266 -0.0234 82  ILE   A O   
602  C  CB  . ILE   A 76  ? 0.2532 0.2737 0.3648 -0.0107 -0.0314 -0.0236 82  ILE   A CB  
603  C  CG1 . ILE   A 76  ? 0.2840 0.3082 0.3889 -0.0066 -0.0357 -0.0261 82  ILE   A CG1 
604  C  CG2 . ILE   A 76  ? 0.2644 0.2868 0.3811 -0.0117 -0.0268 -0.0192 82  ILE   A CG2 
605  C  CD1 . ILE   A 76  ? 0.3204 0.3430 0.4156 -0.0034 -0.0344 -0.0222 82  ILE   A CD1 
606  N  N   . PHE   A 77  ? 0.1999 0.2224 0.3440 -0.0206 -0.0263 -0.0261 83  PHE   A N   
607  C  CA  . PHE   A 77  ? 0.2069 0.2251 0.3585 -0.0241 -0.0210 -0.0226 83  PHE   A CA  
608  C  C   . PHE   A 77  ? 0.2137 0.2275 0.3565 -0.0225 -0.0161 -0.0151 83  PHE   A C   
609  O  O   . PHE   A 77  ? 0.2238 0.2409 0.3628 -0.0204 -0.0150 -0.0126 83  PHE   A O   
610  C  CB  . PHE   A 77  ? 0.2096 0.2338 0.3789 -0.0276 -0.0190 -0.0241 83  PHE   A CB  
611  C  CG  . PHE   A 77  ? 0.2433 0.2623 0.4208 -0.0311 -0.0128 -0.0202 83  PHE   A CG  
612  C  CD1 . PHE   A 77  ? 0.2658 0.2842 0.4442 -0.0311 -0.0062 -0.0134 83  PHE   A CD1 
613  C  CD2 . PHE   A 77  ? 0.2704 0.2841 0.4530 -0.0339 -0.0132 -0.0228 83  PHE   A CD2 
614  C  CE1 . PHE   A 77  ? 0.2785 0.2912 0.4633 -0.0337 0.0000  -0.0090 83  PHE   A CE1 
615  C  CE2 . PHE   A 77  ? 0.2882 0.2961 0.4780 -0.0367 -0.0071 -0.0186 83  PHE   A CE2 
616  C  CZ  . PHE   A 77  ? 0.2800 0.2876 0.4709 -0.0366 -0.0005 -0.0115 83  PHE   A CZ  
617  N  N   . VAL   A 78  ? 0.2035 0.2097 0.3428 -0.0233 -0.0135 -0.0117 84  VAL   A N   
618  C  CA  . VAL   A 78  ? 0.2067 0.2084 0.3374 -0.0216 -0.0097 -0.0049 84  VAL   A CA  
619  C  C   . VAL   A 78  ? 0.2274 0.2249 0.3655 -0.0240 -0.0043 -0.0010 84  VAL   A C   
620  O  O   . VAL   A 78  ? 0.2344 0.2277 0.3775 -0.0260 -0.0043 -0.0025 84  VAL   A O   
621  C  CB  . VAL   A 78  ? 0.2114 0.2081 0.3296 -0.0192 -0.0121 -0.0039 84  VAL   A CB  
622  C  CG1 . VAL   A 78  ? 0.2272 0.2197 0.3371 -0.0174 -0.0092 0.0024  84  VAL   A CG1 
623  C  CG2 . VAL   A 78  ? 0.2023 0.2022 0.3134 -0.0168 -0.0166 -0.0074 84  VAL   A CG2 
624  N  N   . GLU   A 79  ? 0.2376 0.2351 0.3754 -0.0234 0.0007  0.0042  85  GLU   A N   
625  C  CA  . GLU   A 79  ? 0.2481 0.2410 0.3922 -0.0253 0.0069  0.0091  85  GLU   A CA  
626  C  C   . GLU   A 79  ? 0.2533 0.2377 0.3898 -0.0241 0.0073  0.0127  85  GLU   A C   
627  O  O   . GLU   A 79  ? 0.2446 0.2274 0.3698 -0.0215 0.0035  0.0126  85  GLU   A O   
628  C  CB  . GLU   A 79  ? 0.3030 0.2972 0.4443 -0.0235 0.0123  0.0145  85  GLU   A CB  
629  C  CG  . GLU   A 79  ? 0.4457 0.4383 0.5983 -0.0260 0.0198  0.0185  85  GLU   A CG  
630  C  CD  . GLU   A 79  ? 0.5926 0.5860 0.7412 -0.0237 0.0260  0.0241  85  GLU   A CD  
631  O  OE1 . GLU   A 79  ? 0.6328 0.6222 0.7858 -0.0245 0.0334  0.0296  85  GLU   A OE1 
632  O  OE2 . GLU   A 79  ? 0.6270 0.6244 0.7676 -0.0208 0.0240  0.0232  85  GLU   A OE2 
633  N  N   . ALA   A 80  ? 0.2525 0.2315 0.3960 -0.0260 0.0119  0.0159  86  ALA   A N   
634  C  CA  . ALA   A 80  ? 0.2583 0.2293 0.3955 -0.0244 0.0123  0.0197  86  ALA   A CA  
635  C  C   . ALA   A 80  ? 0.2642 0.2327 0.3868 -0.0201 0.0129  0.0255  86  ALA   A C   
636  O  O   . ALA   A 80  ? 0.2684 0.2388 0.3876 -0.0189 0.0161  0.0286  86  ALA   A O   
637  C  CB  . ALA   A 80  ? 0.2611 0.2263 0.4085 -0.0268 0.0181  0.0230  86  ALA   A CB  
638  N  N   . SER   A 81  ? 0.2580 0.2226 0.3723 -0.0178 0.0096  0.0265  87  SER   A N   
639  C  CA  . SER   A 81  ? 0.2620 0.2237 0.3628 -0.0137 0.0089  0.0314  87  SER   A CA  
640  C  C   . SER   A 81  ? 0.2851 0.2399 0.3847 -0.0122 0.0091  0.0350  87  SER   A C   
641  O  O   . SER   A 81  ? 0.2889 0.2412 0.3981 -0.0145 0.0103  0.0336  87  SER   A O   
642  C  CB  . SER   A 81  ? 0.2668 0.2325 0.3596 -0.0121 0.0029  0.0277  87  SER   A CB  
643  O  OG  . SER   A 81  ? 0.2685 0.2339 0.3636 -0.0127 -0.0011 0.0242  87  SER   A OG  
644  N  N   . GLU   A 82  ? 0.3020 0.2538 0.3901 -0.0082 0.0075  0.0394  88  GLU   A N   
645  C  CA  . GLU   A 82  ? 0.3235 0.2698 0.4108 -0.0062 0.0067  0.0426  88  GLU   A CA  
646  C  C   . GLU   A 82  ? 0.3154 0.2636 0.4069 -0.0071 0.0018  0.0375  88  GLU   A C   
647  O  O   . GLU   A 82  ? 0.3291 0.2733 0.4239 -0.0062 0.0017  0.0388  88  GLU   A O   
648  C  CB  . GLU   A 82  ? 0.3955 0.3387 0.4695 -0.0013 0.0054  0.0481  88  GLU   A CB  
649  C  CG  . GLU   A 82  ? 0.5207 0.4681 0.5859 0.0004  -0.0008 0.0452  88  GLU   A CG  
650  C  CD  . GLU   A 82  ? 0.6966 0.6418 0.7480 0.0046  -0.0014 0.0494  88  GLU   A CD  
651  O  OE1 . GLU   A 82  ? 0.7420 0.6818 0.7883 0.0080  -0.0001 0.0551  88  GLU   A OE1 
652  O  OE2 . GLU   A 82  ? 0.7469 0.6954 0.7920 0.0050  -0.0033 0.0470  88  GLU   A OE2 
653  N  N   . TYR   A 83  ? 0.2816 0.2356 0.3734 -0.0086 -0.0016 0.0317  89  TYR   A N   
654  C  CA  . TYR   A 83  ? 0.2715 0.2273 0.3660 -0.0090 -0.0054 0.0273  89  TYR   A CA  
655  C  C   . TYR   A 83  ? 0.2532 0.2098 0.3574 -0.0122 -0.0045 0.0221  89  TYR   A C   
656  O  O   . TYR   A 83  ? 0.2622 0.2178 0.3692 -0.0120 -0.0061 0.0195  89  TYR   A O   
657  C  CB  . TYR   A 83  ? 0.2620 0.2227 0.3498 -0.0083 -0.0096 0.0245  89  TYR   A CB  
658  C  CG  . TYR   A 83  ? 0.2763 0.2362 0.3545 -0.0052 -0.0117 0.0284  89  TYR   A CG  
659  C  CD1 . TYR   A 83  ? 0.2911 0.2520 0.3624 -0.0044 -0.0109 0.0299  89  TYR   A CD1 
660  C  CD2 . TYR   A 83  ? 0.2831 0.2415 0.3594 -0.0028 -0.0148 0.0302  89  TYR   A CD2 
661  C  CE1 . TYR   A 83  ? 0.3125 0.2723 0.3737 -0.0013 -0.0135 0.0325  89  TYR   A CE1 
662  C  CE2 . TYR   A 83  ? 0.3047 0.2627 0.3722 0.0001  -0.0178 0.0330  89  TYR   A CE2 
663  C  CZ  . TYR   A 83  ? 0.3266 0.2850 0.3860 0.0009  -0.0174 0.0338  89  TYR   A CZ  
664  O  OH  . TYR   A 83  ? 0.3618 0.3192 0.4115 0.0040  -0.0208 0.0359  89  TYR   A OH  
665  N  N   . TYR   A 84  ? 0.2350 0.1935 0.3443 -0.0149 -0.0022 0.0201  90  TYR   A N   
666  C  CA  . TYR   A 84  ? 0.2334 0.1931 0.3518 -0.0179 -0.0024 0.0141  90  TYR   A CA  
667  C  C   . TYR   A 84  ? 0.2556 0.2148 0.3832 -0.0209 0.0017  0.0143  90  TYR   A C   
668  O  O   . TYR   A 84  ? 0.2521 0.2130 0.3784 -0.0209 0.0043  0.0176  90  TYR   A O   
669  C  CB  . TYR   A 84  ? 0.2209 0.1870 0.3366 -0.0183 -0.0061 0.0086  90  TYR   A CB  
670  C  CG  . TYR   A 84  ? 0.2036 0.1710 0.3116 -0.0159 -0.0097 0.0074  90  TYR   A CG  
671  C  CD1 . TYR   A 84  ? 0.2076 0.1731 0.3172 -0.0155 -0.0109 0.0045  90  TYR   A CD1 
672  C  CD2 . TYR   A 84  ? 0.2075 0.1777 0.3073 -0.0142 -0.0116 0.0089  90  TYR   A CD2 
673  C  CE1 . TYR   A 84  ? 0.1911 0.1579 0.2949 -0.0135 -0.0134 0.0036  90  TYR   A CE1 
674  C  CE2 . TYR   A 84  ? 0.1953 0.1665 0.2897 -0.0125 -0.0145 0.0078  90  TYR   A CE2 
675  C  CZ  . TYR   A 84  ? 0.1855 0.1553 0.2823 -0.0122 -0.0152 0.0053  90  TYR   A CZ  
676  O  OH  . TYR   A 84  ? 0.1829 0.1536 0.2755 -0.0106 -0.0171 0.0047  90  TYR   A OH  
677  N  N   . PRO   A 85  ? 0.2668 0.2243 0.4044 -0.0237 0.0022  0.0100  91  PRO   A N   
678  C  CA  . PRO   A 85  ? 0.2751 0.2335 0.4242 -0.0274 0.0056  0.0089  91  PRO   A CA  
679  C  C   . PRO   A 85  ? 0.2750 0.2420 0.4250 -0.0285 0.0029  0.0045  91  PRO   A C   
680  O  O   . PRO   A 85  ? 0.2719 0.2430 0.4142 -0.0266 -0.0016 0.0014  91  PRO   A O   
681  C  CB  . PRO   A 85  ? 0.2867 0.2410 0.4452 -0.0298 0.0051  0.0037  91  PRO   A CB  
682  C  CG  . PRO   A 85  ? 0.3008 0.2560 0.4519 -0.0275 0.0002  -0.0007 91  PRO   A CG  
683  C  CD  . PRO   A 85  ? 0.2727 0.2278 0.4121 -0.0236 -0.0003 0.0051  91  PRO   A CD  
684  N  N   . ALA   A 86  ? 0.2636 0.2336 0.4245 -0.0316 0.0058  0.0038  92  ALA   A N   
685  C  CA  . ALA   A 86  ? 0.2668 0.2456 0.4309 -0.0325 0.0030  -0.0008 92  ALA   A CA  
686  C  C   . ALA   A 86  ? 0.2611 0.2421 0.4265 -0.0331 -0.0032 -0.0093 92  ALA   A C   
687  O  O   . ALA   A 86  ? 0.2636 0.2398 0.4349 -0.0349 -0.0033 -0.0123 92  ALA   A O   
688  C  CB  . ALA   A 86  ? 0.2788 0.2603 0.4577 -0.0362 0.0074  -0.0005 92  ALA   A CB  
689  N  N   . ARG   A 87  ? 0.2457 0.2323 0.4035 -0.0308 -0.0079 -0.0125 93  ARG   A N   
690  C  CA  . ARG   A 87  ? 0.2317 0.2193 0.3874 -0.0303 -0.0134 -0.0197 93  ARG   A CA  
691  C  C   . ARG   A 87  ? 0.2237 0.2183 0.3729 -0.0279 -0.0179 -0.0226 93  ARG   A C   
692  O  O   . ARG   A 87  ? 0.2356 0.2338 0.3814 -0.0265 -0.0166 -0.0188 93  ARG   A O   
693  C  CB  . ARG   A 87  ? 0.2386 0.2195 0.3847 -0.0279 -0.0136 -0.0182 93  ARG   A CB  
694  C  CG  . ARG   A 87  ? 0.2469 0.2287 0.3797 -0.0242 -0.0142 -0.0138 93  ARG   A CG  
695  C  CD  . ARG   A 87  ? 0.2467 0.2226 0.3731 -0.0223 -0.0129 -0.0098 93  ARG   A CD  
696  N  NE  . ARG   A 87  ? 0.2349 0.2119 0.3505 -0.0192 -0.0154 -0.0096 93  ARG   A NE  
697  C  CZ  . ARG   A 87  ? 0.2174 0.1967 0.3259 -0.0175 -0.0158 -0.0063 93  ARG   A CZ  
698  N  NH1 . ARG   A 87  ? 0.2010 0.1806 0.3014 -0.0152 -0.0178 -0.0063 93  ARG   A NH1 
699  N  NH2 . ARG   A 87  ? 0.2180 0.1995 0.3280 -0.0181 -0.0140 -0.0033 93  ARG   A NH2 
700  N  N   . TYR   A 88  ? 0.2149 0.2110 0.3613 -0.0268 -0.0229 -0.0291 94  TYR   A N   
701  C  CA  . TYR   A 88  ? 0.2200 0.2213 0.3578 -0.0236 -0.0270 -0.0311 94  TYR   A CA  
702  C  C   . TYR   A 88  ? 0.2122 0.2091 0.3359 -0.0202 -0.0269 -0.0284 94  TYR   A C   
703  O  O   . TYR   A 88  ? 0.2222 0.2140 0.3432 -0.0198 -0.0270 -0.0299 94  TYR   A O   
704  C  CB  . TYR   A 88  ? 0.2296 0.2348 0.3700 -0.0234 -0.0327 -0.0394 94  TYR   A CB  
705  C  CG  . TYR   A 88  ? 0.2476 0.2593 0.4033 -0.0266 -0.0337 -0.0426 94  TYR   A CG  
706  C  CD1 . TYR   A 88  ? 0.2638 0.2837 0.4216 -0.0253 -0.0358 -0.0430 94  TYR   A CD1 
707  C  CD2 . TYR   A 88  ? 0.2670 0.2764 0.4363 -0.0310 -0.0320 -0.0449 94  TYR   A CD2 
708  C  CE1 . TYR   A 88  ? 0.2875 0.3144 0.4614 -0.0284 -0.0364 -0.0458 94  TYR   A CE1 
709  C  CE2 . TYR   A 88  ? 0.2849 0.3005 0.4705 -0.0345 -0.0323 -0.0475 94  TYR   A CE2 
710  C  CZ  . TYR   A 88  ? 0.3024 0.3273 0.4906 -0.0332 -0.0346 -0.0481 94  TYR   A CZ  
711  O  OH  . TYR   A 88  ? 0.3401 0.3720 0.5466 -0.0368 -0.0347 -0.0509 94  TYR   A OH  
712  N  N   . GLN   A 89  ? 0.1835 0.1822 0.2993 -0.0178 -0.0265 -0.0245 95  GLN   A N   
713  C  CA  . GLN   A 89  ? 0.1722 0.1674 0.2763 -0.0150 -0.0266 -0.0221 95  GLN   A CA  
714  C  C   . GLN   A 89  ? 0.1817 0.1799 0.2786 -0.0120 -0.0305 -0.0260 95  GLN   A C   
715  O  O   . GLN   A 89  ? 0.2040 0.2075 0.3017 -0.0111 -0.0324 -0.0271 95  GLN   A O   
716  C  CB  . GLN   A 89  ? 0.1691 0.1634 0.2686 -0.0142 -0.0240 -0.0158 95  GLN   A CB  
717  C  CG  . GLN   A 89  ? 0.1574 0.1488 0.2464 -0.0116 -0.0245 -0.0139 95  GLN   A CG  
718  C  CD  . GLN   A 89  ? 0.1857 0.1748 0.2714 -0.0113 -0.0225 -0.0084 95  GLN   A CD  
719  O  OE1 . GLN   A 89  ? 0.2015 0.1887 0.2912 -0.0127 -0.0202 -0.0054 95  GLN   A OE1 
720  N  NE2 . GLN   A 89  ? 0.1689 0.1577 0.2467 -0.0092 -0.0233 -0.0069 95  GLN   A NE2 
721  N  N   . SER   A 90  ? 0.1627 0.1573 0.2524 -0.0100 -0.0314 -0.0278 96  SER   A N   
722  C  CA  . SER   A 90  ? 0.1667 0.1628 0.2478 -0.0065 -0.0345 -0.0309 96  SER   A CA  
723  C  C   . SER   A 90  ? 0.1873 0.1819 0.2586 -0.0038 -0.0332 -0.0265 96  SER   A C   
724  O  O   . SER   A 90  ? 0.1854 0.1775 0.2565 -0.0047 -0.0302 -0.0218 96  SER   A O   
725  C  CB  . SER   A 90  ? 0.2054 0.1979 0.2834 -0.0054 -0.0356 -0.0355 96  SER   A CB  
726  O  OG  . SER   A 90  ? 0.2345 0.2215 0.3096 -0.0053 -0.0320 -0.0325 96  SER   A OG  
727  N  N   . HIS   A 91  ? 0.1845 0.1809 0.2481 -0.0003 -0.0356 -0.0281 97  HIS   A N   
728  C  CA  . HIS   A 91  ? 0.1896 0.1839 0.2439 0.0025  -0.0342 -0.0243 97  HIS   A CA  
729  C  C   . HIS   A 91  ? 0.1725 0.1677 0.2290 0.0012  -0.0326 -0.0198 97  HIS   A C   
730  O  O   . HIS   A 91  ? 0.1827 0.1747 0.2343 0.0020  -0.0306 -0.0162 97  HIS   A O   
731  C  CB  . HIS   A 91  ? 0.2196 0.2081 0.2688 0.0031  -0.0312 -0.0225 97  HIS   A CB  
732  C  CG  . HIS   A 91  ? 0.2572 0.2439 0.3018 0.0053  -0.0322 -0.0269 97  HIS   A CG  
733  N  ND1 . HIS   A 91  ? 0.2898 0.2749 0.3234 0.0097  -0.0326 -0.0275 97  HIS   A ND1 
734  C  CD2 . HIS   A 91  ? 0.2650 0.2506 0.3138 0.0040  -0.0327 -0.0308 97  HIS   A CD2 
735  C  CE1 . HIS   A 91  ? 0.2999 0.2833 0.3305 0.0111  -0.0336 -0.0320 97  HIS   A CE1 
736  N  NE2 . HIS   A 91  ? 0.2937 0.2773 0.3336 0.0077  -0.0338 -0.0344 97  HIS   A NE2 
737  N  N   . LEU   A 92  ? 0.1572 0.1571 0.2211 -0.0004 -0.0335 -0.0204 98  LEU   A N   
738  C  CA  . LEU   A 92  ? 0.1587 0.1593 0.2242 -0.0012 -0.0316 -0.0165 98  LEU   A CA  
739  C  C   . LEU   A 92  ? 0.1726 0.1772 0.2356 0.0016  -0.0333 -0.0169 98  LEU   A C   
740  O  O   . LEU   A 92  ? 0.1709 0.1801 0.2364 0.0029  -0.0363 -0.0205 98  LEU   A O   
741  C  CB  . LEU   A 92  ? 0.1682 0.1708 0.2440 -0.0046 -0.0301 -0.0162 98  LEU   A CB  
742  C  CG  . LEU   A 92  ? 0.1990 0.2017 0.2760 -0.0054 -0.0273 -0.0119 98  LEU   A CG  
743  C  CD1 . LEU   A 92  ? 0.2139 0.2110 0.2842 -0.0052 -0.0257 -0.0080 98  LEU   A CD1 
744  C  CD2 . LEU   A 92  ? 0.2178 0.2220 0.3052 -0.0085 -0.0251 -0.0114 98  LEU   A CD2 
745  N  N   . MET   A 93  ? 0.1736 0.1760 0.2314 0.0029  -0.0317 -0.0133 99  MET   A N   
746  C  CA  . MET   A 93  ? 0.1756 0.1805 0.2304 0.0060  -0.0327 -0.0131 99  MET   A CA  
747  C  C   . MET   A 93  ? 0.1779 0.1840 0.2360 0.0050  -0.0304 -0.0106 99  MET   A C   
748  O  O   . MET   A 93  ? 0.1834 0.1851 0.2391 0.0036  -0.0282 -0.0078 99  MET   A O   
749  C  CB  . MET   A 93  ? 0.2005 0.2001 0.2451 0.0087  -0.0324 -0.0112 99  MET   A CB  
750  C  CG  . MET   A 93  ? 0.2156 0.2132 0.2552 0.0103  -0.0337 -0.0130 99  MET   A CG  
751  S  SD  . MET   A 93  ? 0.2426 0.2328 0.2712 0.0130  -0.0316 -0.0098 99  MET   A SD  
752  C  CE  . MET   A 93  ? 0.2618 0.2477 0.2935 0.0089  -0.0286 -0.0068 99  MET   A CE  
753  N  N   . LEU   A 94  ? 0.1647 0.1768 0.2282 0.0061  -0.0308 -0.0117 100 LEU   A N   
754  C  CA  . LEU   A 94  ? 0.1756 0.1886 0.2417 0.0057  -0.0277 -0.0092 100 LEU   A CA  
755  C  C   . LEU   A 94  ? 0.1677 0.1802 0.2277 0.0095  -0.0275 -0.0081 100 LEU   A C   
756  O  O   . LEU   A 94  ? 0.1796 0.1942 0.2375 0.0127  -0.0301 -0.0097 100 LEU   A O   
757  C  CB  . LEU   A 94  ? 0.1889 0.2093 0.2674 0.0041  -0.0270 -0.0107 100 LEU   A CB  
758  C  CG  . LEU   A 94  ? 0.2255 0.2462 0.3119 0.0000  -0.0264 -0.0117 100 LEU   A CG  
759  C  CD1 . LEU   A 94  ? 0.2325 0.2602 0.3328 -0.0020 -0.0245 -0.0125 100 LEU   A CD1 
760  C  CD2 . LEU   A 94  ? 0.2334 0.2472 0.3155 -0.0020 -0.0235 -0.0082 100 LEU   A CD2 
761  N  N   . ALA   A 95  ? 0.1660 0.1757 0.2233 0.0096  -0.0245 -0.0054 101 ALA   A N   
762  C  CA  . ALA   A 95  ? 0.1702 0.1786 0.2220 0.0133  -0.0237 -0.0045 101 ALA   A CA  
763  C  C   . ALA   A 95  ? 0.1733 0.1819 0.2262 0.0133  -0.0198 -0.0026 101 ALA   A C   
764  O  O   . ALA   A 95  ? 0.1864 0.1940 0.2415 0.0105  -0.0177 -0.0012 101 ALA   A O   
765  C  CB  . ALA   A 95  ? 0.1935 0.1937 0.2347 0.0143  -0.0244 -0.0034 101 ALA   A CB  
766  N  N   . VAL   A 96  ? 0.1575 0.1671 0.2085 0.0168  -0.0185 -0.0023 102 VAL   A N   
767  C  CA  . VAL   A 96  ? 0.1718 0.1805 0.2215 0.0177  -0.0142 -0.0004 102 VAL   A CA  
768  C  C   . VAL   A 96  ? 0.1884 0.1875 0.2257 0.0183  -0.0141 0.0007  102 VAL   A C   
769  O  O   . VAL   A 96  ? 0.1886 0.1834 0.2195 0.0205  -0.0159 0.0000  102 VAL   A O   
770  C  CB  . VAL   A 96  ? 0.1913 0.2053 0.2448 0.0217  -0.0126 -0.0010 102 VAL   A CB  
771  C  CG1 . VAL   A 96  ? 0.2037 0.2157 0.2539 0.0233  -0.0073 0.0011  102 VAL   A CG1 
772  C  CG2 . VAL   A 96  ? 0.1857 0.2100 0.2532 0.0206  -0.0135 -0.0026 102 VAL   A CG2 
773  N  N   . GLY   A 97  ? 0.1817 0.1774 0.2160 0.0165  -0.0121 0.0024  103 GLY   A N   
774  C  CA  . GLY   A 97  ? 0.2001 0.1875 0.2237 0.0168  -0.0129 0.0029  103 GLY   A CA  
775  C  C   . GLY   A 97  ? 0.2120 0.1975 0.2341 0.0149  -0.0112 0.0050  103 GLY   A C   
776  O  O   . GLY   A 97  ? 0.2261 0.2159 0.2559 0.0127  -0.0097 0.0062  103 GLY   A O   
777  N  N   . HIS   A 98  ? 0.2081 0.1871 0.2200 0.0163  -0.0111 0.0055  104 HIS   A N   
778  C  CA  . HIS   A 98  ? 0.2031 0.1796 0.2115 0.0154  -0.0100 0.0078  104 HIS   A CA  
779  C  C   . HIS   A 98  ? 0.1975 0.1731 0.2086 0.0121  -0.0133 0.0082  104 HIS   A C   
780  O  O   . HIS   A 98  ? 0.2028 0.1759 0.2128 0.0109  -0.0172 0.0065  104 HIS   A O   
781  C  CB  . HIS   A 98  ? 0.2193 0.1888 0.2148 0.0183  -0.0100 0.0075  104 HIS   A CB  
782  C  CG  . HIS   A 98  ? 0.2250 0.1914 0.2147 0.0183  -0.0094 0.0100  104 HIS   A CG  
783  N  ND1 . HIS   A 98  ? 0.2411 0.2098 0.2326 0.0191  -0.0040 0.0133  104 HIS   A ND1 
784  C  CD2 . HIS   A 98  ? 0.2337 0.1953 0.2174 0.0175  -0.0136 0.0099  104 HIS   A CD2 
785  C  CE1 . HIS   A 98  ? 0.2556 0.2200 0.2400 0.0194  -0.0049 0.0154  104 HIS   A CE1 
786  N  NE2 . HIS   A 98  ? 0.2441 0.2045 0.2238 0.0186  -0.0111 0.0132  104 HIS   A NE2 
787  N  N   . SER   A 99  ? 0.1899 0.1665 0.2037 0.0108  -0.0113 0.0107  105 SER   A N   
788  C  CA  . SER   A 99  ? 0.2001 0.1749 0.2153 0.0084  -0.0139 0.0117  105 SER   A CA  
789  C  C   . SER   A 99  ? 0.2244 0.1983 0.2386 0.0087  -0.0105 0.0154  105 SER   A C   
790  O  O   . SER   A 99  ? 0.2253 0.2012 0.2411 0.0099  -0.0055 0.0172  105 SER   A O   
791  C  CB  . SER   A 99  ? 0.2068 0.1855 0.2321 0.0054  -0.0156 0.0103  105 SER   A CB  
792  O  OG  . SER   A 99  ? 0.2374 0.2211 0.2718 0.0043  -0.0122 0.0111  105 SER   A OG  
793  N  N   . GLU   A 100 ? 0.2190 0.1893 0.2297 0.0083  -0.0131 0.0168  106 GLU   A N   
794  C  CA  . GLU   A 100 ? 0.2396 0.2080 0.2485 0.0090  -0.0101 0.0209  106 GLU   A CA  
795  C  C   . GLU   A 100 ? 0.2679 0.2349 0.2796 0.0073  -0.0138 0.0216  106 GLU   A C   
796  O  O   . GLU   A 100 ? 0.2761 0.2435 0.2899 0.0059  -0.0185 0.0189  106 GLU   A O   
797  C  CB  . GLU   A 100 ? 0.2771 0.2406 0.2723 0.0131  -0.0085 0.0228  106 GLU   A CB  
798  C  CG  . GLU   A 100 ? 0.3205 0.2796 0.3055 0.0148  -0.0145 0.0204  106 GLU   A CG  
799  C  CD  . GLU   A 100 ? 0.3191 0.2731 0.2893 0.0193  -0.0133 0.0213  106 GLU   A CD  
800  O  OE1 . GLU   A 100 ? 0.3337 0.2840 0.2963 0.0213  -0.0140 0.0241  106 GLU   A OE1 
801  O  OE2 . GLU   A 100 ? 0.2823 0.2355 0.2478 0.0211  -0.0117 0.0191  106 GLU   A OE2 
802  N  N   . PRO   A 101 ? 0.2863 0.2517 0.2994 0.0074  -0.0114 0.0256  107 PRO   A N   
803  C  CA  . PRO   A 101 ? 0.2960 0.2600 0.3117 0.0064  -0.0148 0.0265  107 PRO   A CA  
804  C  C   . PRO   A 101 ? 0.2846 0.2458 0.2919 0.0082  -0.0209 0.0250  107 PRO   A C   
805  O  O   . PRO   A 101 ? 0.2993 0.2571 0.2950 0.0114  -0.0218 0.0256  107 PRO   A O   
806  C  CB  . PRO   A 101 ? 0.3180 0.2792 0.3331 0.0076  -0.0104 0.0318  107 PRO   A CB  
807  C  CG  . PRO   A 101 ? 0.3154 0.2788 0.3346 0.0070  -0.0039 0.0327  107 PRO   A CG  
808  C  CD  . PRO   A 101 ? 0.2877 0.2522 0.3000 0.0087  -0.0049 0.0298  107 PRO   A CD  
809  N  N   . GLY   A 102 ? 0.2510 0.2139 0.2647 0.0061  -0.0250 0.0227  108 GLY   A N   
810  C  CA  . GLY   A 102 ? 0.2433 0.2050 0.2535 0.0066  -0.0311 0.0205  108 GLY   A CA  
811  C  C   . GLY   A 102 ? 0.2275 0.1911 0.2414 0.0045  -0.0327 0.0163  108 GLY   A C   
812  O  O   . GLY   A 102 ? 0.2291 0.1926 0.2447 0.0037  -0.0370 0.0143  108 GLY   A O   
813  N  N   . ASP   A 103 ? 0.2074 0.1730 0.2231 0.0039  -0.0291 0.0151  109 ASP   A N   
814  C  CA  . ASP   A 103 ? 0.1969 0.1635 0.2146 0.0027  -0.0303 0.0118  109 ASP   A CA  
815  C  C   . ASP   A 103 ? 0.1938 0.1632 0.2209 0.0002  -0.0303 0.0107  109 ASP   A C   
816  O  O   . ASP   A 103 ? 0.2065 0.1761 0.2349 -0.0005 -0.0314 0.0085  109 ASP   A O   
817  C  CB  . ASP   A 103 ? 0.2039 0.1715 0.2192 0.0038  -0.0269 0.0109  109 ASP   A CB  
818  C  CG  . ASP   A 103 ? 0.2295 0.1933 0.2341 0.0066  -0.0274 0.0105  109 ASP   A CG  
819  O  OD1 . ASP   A 103 ? 0.2456 0.2060 0.2453 0.0070  -0.0316 0.0091  109 ASP   A OD1 
820  O  OD2 . ASP   A 103 ? 0.2136 0.1779 0.2151 0.0084  -0.0235 0.0114  109 ASP   A OD2 
821  N  N   . CYS   A 104 ? 0.1859 0.1569 0.2193 -0.0009 -0.0291 0.0124  110 CYS   A N   
822  C  CA  . CYS   A 104 ? 0.1796 0.1527 0.2207 -0.0028 -0.0290 0.0110  110 CYS   A CA  
823  C  C   . CYS   A 104 ? 0.1884 0.1606 0.2309 -0.0034 -0.0321 0.0099  110 CYS   A C   
824  O  O   . CYS   A 104 ? 0.2028 0.1735 0.2433 -0.0028 -0.0350 0.0107  110 CYS   A O   
825  C  CB  . CYS   A 104 ? 0.1878 0.1616 0.2351 -0.0036 -0.0273 0.0126  110 CYS   A CB  
826  S  SG  . CYS   A 104 ? 0.2319 0.2075 0.2819 -0.0041 -0.0230 0.0133  110 CYS   A SG  
827  N  N   . GLY   A 105 ? 0.1779 0.1512 0.2236 -0.0043 -0.0313 0.0081  111 GLY   A N   
828  C  CA  . GLY   A 105 ? 0.1935 0.1661 0.2421 -0.0051 -0.0331 0.0073  111 GLY   A CA  
829  C  C   . GLY   A 105 ? 0.1965 0.1670 0.2409 -0.0049 -0.0339 0.0058  111 GLY   A C   
830  O  O   . GLY   A 105 ? 0.1956 0.1652 0.2432 -0.0059 -0.0342 0.0052  111 GLY   A O   
831  N  N   . GLY   A 106 ? 0.1820 0.1512 0.2197 -0.0036 -0.0337 0.0054  112 GLY   A N   
832  C  CA  . GLY   A 106 ? 0.1770 0.1434 0.2105 -0.0030 -0.0340 0.0039  112 GLY   A CA  
833  C  C   . GLY   A 106 ? 0.1743 0.1412 0.2098 -0.0030 -0.0316 0.0034  112 GLY   A C   
834  O  O   . GLY   A 106 ? 0.1882 0.1579 0.2248 -0.0025 -0.0297 0.0035  112 GLY   A O   
835  N  N   . ILE   A 107 ? 0.1654 0.1293 0.2013 -0.0035 -0.0317 0.0028  113 ILE   A N   
836  C  CA  . ILE   A 107 ? 0.1616 0.1250 0.1979 -0.0029 -0.0291 0.0029  113 ILE   A CA  
837  C  C   . ILE   A 107 ? 0.1690 0.1312 0.1992 -0.0004 -0.0279 0.0024  113 ILE   A C   
838  O  O   . ILE   A 107 ? 0.1815 0.1407 0.2076 0.0004  -0.0288 0.0018  113 ILE   A O   
839  C  CB  . ILE   A 107 ? 0.1909 0.1512 0.2314 -0.0045 -0.0286 0.0033  113 ILE   A CB  
840  C  CG1 . ILE   A 107 ? 0.2085 0.1716 0.2567 -0.0063 -0.0287 0.0040  113 ILE   A CG1 
841  C  CG2 . ILE   A 107 ? 0.2112 0.1688 0.2495 -0.0032 -0.0253 0.0040  113 ILE   A CG2 
842  C  CD1 . ILE   A 107 ? 0.2470 0.2082 0.3022 -0.0084 -0.0282 0.0044  113 ILE   A CD1 
843  N  N   . LEU   A 108 ? 0.1644 0.1286 0.1940 0.0011  -0.0261 0.0026  114 LEU   A N   
844  C  CA  . LEU   A 108 ? 0.1790 0.1426 0.2036 0.0040  -0.0252 0.0023  114 LEU   A CA  
845  C  C   . LEU   A 108 ? 0.1923 0.1520 0.2154 0.0049  -0.0232 0.0034  114 LEU   A C   
846  O  O   . LEU   A 108 ? 0.1957 0.1562 0.2213 0.0042  -0.0219 0.0039  114 LEU   A O   
847  C  CB  . LEU   A 108 ? 0.1900 0.1592 0.2155 0.0053  -0.0253 0.0014  114 LEU   A CB  
848  C  CG  . LEU   A 108 ? 0.1981 0.1681 0.2194 0.0089  -0.0251 0.0009  114 LEU   A CG  
849  C  CD1 . LEU   A 108 ? 0.2003 0.1691 0.2185 0.0108  -0.0253 0.0009  114 LEU   A CD1 
850  C  CD2 . LEU   A 108 ? 0.2051 0.1814 0.2292 0.0096  -0.0261 -0.0007 114 LEU   A CD2 
851  N  N   . ARG   A 109 ? 0.1916 0.1464 0.2106 0.0066  -0.0224 0.0039  115 ARG   A N   
852  C  CA  . ARG   A 109 ? 0.2007 0.1507 0.2177 0.0078  -0.0197 0.0056  115 ARG   A CA  
853  C  C   . ARG   A 109 ? 0.2114 0.1595 0.2217 0.0121  -0.0190 0.0062  115 ARG   A C   
854  O  O   . ARG   A 109 ? 0.2154 0.1635 0.2234 0.0135  -0.0204 0.0052  115 ARG   A O   
855  C  CB  . ARG   A 109 ? 0.2334 0.1772 0.2530 0.0053  -0.0191 0.0061  115 ARG   A CB  
856  C  CG  . ARG   A 109 ? 0.3143 0.2596 0.3414 0.0013  -0.0204 0.0055  115 ARG   A CG  
857  C  CD  . ARG   A 109 ? 0.3633 0.3027 0.3934 -0.0009 -0.0206 0.0052  115 ARG   A CD  
858  N  NE  . ARG   A 109 ? 0.4133 0.3487 0.4456 -0.0010 -0.0163 0.0076  115 ARG   A NE  
859  C  CZ  . ARG   A 109 ? 0.3853 0.3219 0.4252 -0.0034 -0.0144 0.0087  115 ARG   A CZ  
860  N  NH1 . ARG   A 109 ? 0.3262 0.2676 0.3728 -0.0060 -0.0171 0.0075  115 ARG   A NH1 
861  N  NH2 . ARG   A 109 ? 0.3464 0.2792 0.3871 -0.0028 -0.0093 0.0115  115 ARG   A NH2 
862  N  N   . CYS   A 110 ? 0.2064 0.1520 0.2130 0.0146  -0.0165 0.0080  116 CYS   A N   
863  C  CA  . CYS   A 110 ? 0.2155 0.1576 0.2149 0.0193  -0.0156 0.0093  116 CYS   A CA  
864  C  C   . CYS   A 110 ? 0.2357 0.1689 0.2339 0.0191  -0.0117 0.0122  116 CYS   A C   
865  O  O   . CYS   A 110 ? 0.2417 0.1730 0.2459 0.0151  -0.0102 0.0126  116 CYS   A O   
866  C  CB  . CYS   A 110 ? 0.2251 0.1713 0.2199 0.0232  -0.0162 0.0092  116 CYS   A CB  
867  S  SG  . CYS   A 110 ? 0.2245 0.1687 0.2178 0.0231  -0.0128 0.0111  116 CYS   A SG  
868  N  N   . GLN   A 111 ? 0.2524 0.1803 0.2438 0.0236  -0.0096 0.0145  117 GLN   A N   
869  C  CA  . GLN   A 111 ? 0.2671 0.1857 0.2575 0.0235  -0.0050 0.0179  117 GLN   A CA  
870  C  C   . GLN   A 111 ? 0.2708 0.1886 0.2628 0.0223  -0.0011 0.0201  117 GLN   A C   
871  O  O   . GLN   A 111 ? 0.2875 0.1982 0.2819 0.0208  0.0035  0.0229  117 GLN   A O   
872  C  CB  . GLN   A 111 ? 0.3009 0.2138 0.2824 0.0296  -0.0033 0.0205  117 GLN   A CB  
873  C  CG  . GLN   A 111 ? 0.4003 0.3165 0.3737 0.0350  -0.0035 0.0218  117 GLN   A CG  
874  C  CD  . GLN   A 111 ? 0.5026 0.4147 0.4671 0.0417  -0.0033 0.0240  117 GLN   A CD  
875  O  OE1 . GLN   A 111 ? 0.5456 0.4637 0.5077 0.0453  -0.0075 0.0220  117 GLN   A OE1 
876  N  NE2 . GLN   A 111 ? 0.4880 0.3902 0.4484 0.0437  0.0018  0.0283  117 GLN   A NE2 
877  N  N   . HIS   A 112 ? 0.2601 0.1846 0.2511 0.0230  -0.0023 0.0190  118 HIS   A N   
878  C  CA  . HIS   A 112 ? 0.2565 0.1800 0.2477 0.0226  0.0018  0.0210  118 HIS   A CA  
879  C  C   . HIS   A 112 ? 0.2438 0.1710 0.2456 0.0171  0.0018  0.0195  118 HIS   A C   
880  O  O   . HIS   A 112 ? 0.2489 0.1748 0.2529 0.0164  0.0062  0.0215  118 HIS   A O   
881  C  CB  . HIS   A 112 ? 0.2692 0.1963 0.2517 0.0274  0.0011  0.0206  118 HIS   A CB  
882  C  CG  . HIS   A 112 ? 0.2984 0.2228 0.2700 0.0337  0.0003  0.0219  118 HIS   A CG  
883  N  ND1 . HIS   A 112 ? 0.3062 0.2368 0.2756 0.0362  -0.0054 0.0188  118 HIS   A ND1 
884  C  CD2 . HIS   A 112 ? 0.3245 0.2408 0.2880 0.0382  0.0045  0.0263  118 HIS   A CD2 
885  C  CE1 . HIS   A 112 ? 0.3310 0.2578 0.2911 0.0421  -0.0051 0.0211  118 HIS   A CE1 
886  N  NE2 . HIS   A 112 ? 0.3384 0.2560 0.2938 0.0437  0.0009  0.0258  118 HIS   A NE2 
887  N  N   . GLY   A 113 ? 0.2152 0.1471 0.2233 0.0136  -0.0028 0.0164  119 GLY   A N   
888  C  CA  . GLY   A 113 ? 0.2098 0.1455 0.2276 0.0090  -0.0037 0.0150  119 GLY   A CA  
889  C  C   . GLY   A 113 ? 0.1981 0.1410 0.2178 0.0078  -0.0087 0.0117  119 GLY   A C   
890  O  O   . GLY   A 113 ? 0.2121 0.1568 0.2276 0.0096  -0.0117 0.0102  119 GLY   A O   
891  N  N   . VAL   A 114 ? 0.1877 0.1345 0.2144 0.0050  -0.0091 0.0109  120 VAL   A N   
892  C  CA  . VAL   A 114 ? 0.1825 0.1352 0.2117 0.0037  -0.0131 0.0084  120 VAL   A CA  
893  C  C   . VAL   A 114 ? 0.1874 0.1436 0.2114 0.0066  -0.0138 0.0071  120 VAL   A C   
894  O  O   . VAL   A 114 ? 0.2021 0.1579 0.2238 0.0083  -0.0113 0.0076  120 VAL   A O   
895  C  CB  . VAL   A 114 ? 0.1983 0.1536 0.2366 0.0004  -0.0133 0.0083  120 VAL   A CB  
896  C  CG1 . VAL   A 114 ? 0.2017 0.1622 0.2418 -0.0004 -0.0167 0.0063  120 VAL   A CG1 
897  C  CG2 . VAL   A 114 ? 0.2029 0.1557 0.2474 -0.0027 -0.0142 0.0086  120 VAL   A CG2 
898  N  N   . VAL   A 115 ? 0.1830 0.1428 0.2057 0.0071  -0.0172 0.0052  121 VAL   A N   
899  C  CA  . VAL   A 115 ? 0.1817 0.1457 0.2014 0.0094  -0.0187 0.0032  121 VAL   A CA  
900  C  C   . VAL   A 115 ? 0.1831 0.1517 0.2091 0.0068  -0.0204 0.0014  121 VAL   A C   
901  O  O   . VAL   A 115 ? 0.1796 0.1505 0.2054 0.0076  -0.0206 -0.0004 121 VAL   A O   
902  C  CB  . VAL   A 115 ? 0.2077 0.1733 0.2240 0.0116  -0.0210 0.0024  121 VAL   A CB  
903  C  CG1 . VAL   A 115 ? 0.2148 0.1862 0.2312 0.0130  -0.0235 -0.0003 121 VAL   A CG1 
904  C  CG2 . VAL   A 115 ? 0.2090 0.1696 0.2185 0.0149  -0.0195 0.0042  121 VAL   A CG2 
905  N  N   . GLY   A 116 ? 0.1699 0.1393 0.2007 0.0041  -0.0216 0.0017  122 GLY   A N   
906  C  CA  . GLY   A 116 ? 0.1780 0.1508 0.2142 0.0020  -0.0228 0.0006  122 GLY   A CA  
907  C  C   . GLY   A 116 ? 0.1738 0.1467 0.2132 -0.0002 -0.0242 0.0016  122 GLY   A C   
908  O  O   . GLY   A 116 ? 0.1753 0.1453 0.2132 -0.0004 -0.0244 0.0025  122 GLY   A O   
909  N  N   . ILE   A 117 ? 0.1600 0.1355 0.2034 -0.0015 -0.0250 0.0012  123 ILE   A N   
910  C  CA  . ILE   A 117 ? 0.1631 0.1381 0.2078 -0.0028 -0.0263 0.0025  123 ILE   A CA  
911  C  C   . ILE   A 117 ? 0.1640 0.1415 0.2089 -0.0027 -0.0265 0.0023  123 ILE   A C   
912  O  O   . ILE   A 117 ? 0.1615 0.1417 0.2094 -0.0029 -0.0258 0.0012  123 ILE   A O   
913  C  CB  . ILE   A 117 ? 0.1869 0.1616 0.2369 -0.0044 -0.0266 0.0035  123 ILE   A CB  
914  C  CG1 . ILE   A 117 ? 0.2029 0.1794 0.2571 -0.0047 -0.0253 0.0029  123 ILE   A CG1 
915  C  CG2 . ILE   A 117 ? 0.2130 0.1855 0.2644 -0.0050 -0.0265 0.0041  123 ILE   A CG2 
916  C  CD1 . ILE   A 117 ? 0.2230 0.1993 0.2831 -0.0059 -0.0258 0.0044  123 ILE   A CD1 
917  N  N   . VAL   A 118 ? 0.1516 0.1281 0.1938 -0.0026 -0.0272 0.0034  124 VAL   A N   
918  C  CA  . VAL   A 118 ? 0.1397 0.1184 0.1826 -0.0024 -0.0262 0.0040  124 VAL   A CA  
919  C  C   . VAL   A 118 ? 0.1440 0.1238 0.1927 -0.0039 -0.0255 0.0048  124 VAL   A C   
920  O  O   . VAL   A 118 ? 0.1561 0.1342 0.2063 -0.0046 -0.0264 0.0059  124 VAL   A O   
921  C  CB  . VAL   A 118 ? 0.1575 0.1339 0.1951 -0.0015 -0.0267 0.0054  124 VAL   A CB  
922  C  CG1 . VAL   A 118 ? 0.1775 0.1557 0.2159 -0.0012 -0.0245 0.0068  124 VAL   A CG1 
923  C  CG2 . VAL   A 118 ? 0.1675 0.1420 0.1994 0.0002  -0.0272 0.0043  124 VAL   A CG2 
924  N  N   . SER   A 119 ? 0.1448 0.1275 0.1976 -0.0044 -0.0240 0.0041  125 SER   A N   
925  C  CA  . SER   A 119 ? 0.1502 0.1331 0.2092 -0.0060 -0.0229 0.0046  125 SER   A CA  
926  C  C   . SER   A 119 ? 0.1743 0.1587 0.2365 -0.0065 -0.0205 0.0059  125 SER   A C   
927  O  O   . SER   A 119 ? 0.1892 0.1721 0.2551 -0.0075 -0.0191 0.0076  125 SER   A O   
928  C  CB  . SER   A 119 ? 0.1695 0.1539 0.2325 -0.0065 -0.0232 0.0015  125 SER   A CB  
929  O  OG  . SER   A 119 ? 0.1758 0.1598 0.2451 -0.0081 -0.0221 0.0013  125 SER   A OG  
930  N  N   . THR   A 120 ? 0.1680 0.1551 0.2292 -0.0056 -0.0196 0.0052  126 THR   A N   
931  C  CA  . THR   A 120 ? 0.1821 0.1712 0.2480 -0.0063 -0.0164 0.0067  126 THR   A CA  
932  C  C   . THR   A 120 ? 0.1892 0.1793 0.2499 -0.0041 -0.0152 0.0076  126 THR   A C   
933  O  O   . THR   A 120 ? 0.1845 0.1738 0.2389 -0.0024 -0.0172 0.0065  126 THR   A O   
934  C  CB  . THR   A 120 ? 0.2265 0.2204 0.3025 -0.0081 -0.0161 0.0034  126 THR   A CB  
935  O  OG1 . THR   A 120 ? 0.2419 0.2399 0.3173 -0.0066 -0.0178 0.0006  126 THR   A OG1 
936  C  CG2 . THR   A 120 ? 0.2507 0.2434 0.3311 -0.0098 -0.0176 0.0012  126 THR   A CG2 
937  N  N   . GLY   A 121 ? 0.1931 0.1847 0.2568 -0.0041 -0.0114 0.0096  127 GLY   A N   
938  C  CA  . GLY   A 121 ? 0.2171 0.2101 0.2768 -0.0017 -0.0095 0.0102  127 GLY   A CA  
939  C  C   . GLY   A 121 ? 0.2330 0.2277 0.2978 -0.0020 -0.0041 0.0129  127 GLY   A C   
940  O  O   . GLY   A 121 ? 0.2395 0.2336 0.3107 -0.0042 -0.0019 0.0147  127 GLY   A O   
941  N  N   . GLY   A 122 ? 0.2337 0.2301 0.2956 0.0004  -0.0016 0.0135  128 GLY   A N   
942  C  CA  . GLY   A 122 ? 0.2621 0.2598 0.3280 0.0007  0.0046  0.0167  128 GLY   A CA  
943  C  C   . GLY   A 122 ? 0.2666 0.2695 0.3352 0.0028  0.0070  0.0157  128 GLY   A C   
944  O  O   . GLY   A 122 ? 0.2710 0.2792 0.3454 0.0026  0.0038  0.0120  128 GLY   A O   
945  N  N   . ASN   A 123 ? 0.2642 0.2658 0.3288 0.0052  0.0127  0.0190  129 ASN   A N   
946  C  CA  . ASN   A 123 ? 0.2506 0.2571 0.3185 0.0076  0.0165  0.0188  129 ASN   A CA  
947  C  C   . ASN   A 123 ? 0.2402 0.2491 0.3051 0.0100  0.0121  0.0149  129 ASN   A C   
948  O  O   . ASN   A 123 ? 0.2383 0.2547 0.3132 0.0105  0.0126  0.0129  129 ASN   A O   
949  C  CB  . ASN   A 123 ? 0.2915 0.3060 0.3778 0.0048  0.0205  0.0190  129 ASN   A CB  
950  C  CG  . ASN   A 123 ? 0.3836 0.3947 0.4727 0.0028  0.0262  0.0236  129 ASN   A CG  
951  O  OD1 . ASN   A 123 ? 0.4272 0.4334 0.5071 0.0054  0.0317  0.0279  129 ASN   A OD1 
952  N  ND2 . ASN   A 123 ? 0.3991 0.4118 0.5000 -0.0016 0.0250  0.0227  129 ASN   A ND2 
953  N  N   . GLY   A 124 ? 0.2150 0.2174 0.2666 0.0117  0.0081  0.0140  130 GLY   A N   
954  C  CA  . GLY   A 124 ? 0.2057 0.2083 0.2531 0.0142  0.0044  0.0109  130 GLY   A CA  
955  C  C   . GLY   A 124 ? 0.2040 0.2094 0.2568 0.0122  -0.0012 0.0077  130 GLY   A C   
956  O  O   . GLY   A 124 ? 0.2210 0.2271 0.2715 0.0144  -0.0040 0.0055  130 GLY   A O   
957  N  N   . LEU   A 125 ? 0.1845 0.1906 0.2430 0.0085  -0.0029 0.0076  131 LEU   A N   
958  C  CA  . LEU   A 125 ? 0.1808 0.1881 0.2420 0.0070  -0.0080 0.0047  131 LEU   A CA  
959  C  C   . LEU   A 125 ? 0.1800 0.1803 0.2334 0.0056  -0.0107 0.0053  131 LEU   A C   
960  O  O   . LEU   A 125 ? 0.1880 0.1839 0.2368 0.0051  -0.0091 0.0079  131 LEU   A O   
961  C  CB  . LEU   A 125 ? 0.1800 0.1934 0.2547 0.0038  -0.0083 0.0032  131 LEU   A CB  
962  C  CG  . LEU   A 125 ? 0.2180 0.2401 0.3039 0.0046  -0.0068 0.0017  131 LEU   A CG  
963  C  CD1 . LEU   A 125 ? 0.2327 0.2599 0.3331 0.0007  -0.0061 0.0006  131 LEU   A CD1 
964  C  CD2 . LEU   A 125 ? 0.2124 0.2377 0.2969 0.0075  -0.0113 -0.0015 131 LEU   A CD2 
965  N  N   . VAL   A 126 ? 0.1601 0.1597 0.2120 0.0054  -0.0147 0.0031  132 VAL   A N   
966  C  CA  . VAL   A 126 ? 0.1613 0.1557 0.2087 0.0039  -0.0172 0.0033  132 VAL   A CA  
967  C  C   . VAL   A 126 ? 0.1690 0.1660 0.2215 0.0026  -0.0198 0.0008  132 VAL   A C   
968  O  O   . VAL   A 126 ? 0.1731 0.1732 0.2265 0.0043  -0.0213 -0.0013 132 VAL   A O   
969  C  CB  . VAL   A 126 ? 0.1767 0.1652 0.2140 0.0056  -0.0187 0.0036  132 VAL   A CB  
970  C  CG1 . VAL   A 126 ? 0.1944 0.1833 0.2290 0.0082  -0.0198 0.0019  132 VAL   A CG1 
971  C  CG2 . VAL   A 126 ? 0.1763 0.1608 0.2119 0.0037  -0.0211 0.0038  132 VAL   A CG2 
972  N  N   . GLY   A 127 ? 0.1645 0.1599 0.2196 0.0001  -0.0204 0.0010  133 GLY   A N   
973  C  CA  . GLY   A 127 ? 0.1629 0.1599 0.2215 -0.0007 -0.0226 -0.0017 133 GLY   A CA  
974  C  C   . GLY   A 127 ? 0.1665 0.1587 0.2203 -0.0010 -0.0240 -0.0013 133 GLY   A C   
975  O  O   . GLY   A 127 ? 0.1743 0.1630 0.2261 -0.0019 -0.0234 0.0010  133 GLY   A O   
976  N  N   . PHE   A 128 ? 0.1526 0.1449 0.2046 0.0000  -0.0257 -0.0033 134 PHE   A N   
977  C  CA  . PHE   A 128 ? 0.1597 0.1476 0.2076 0.0000  -0.0261 -0.0027 134 PHE   A CA  
978  C  C   . PHE   A 128 ? 0.1678 0.1563 0.2183 -0.0006 -0.0266 -0.0048 134 PHE   A C   
979  O  O   . PHE   A 128 ? 0.1701 0.1615 0.2211 0.0007  -0.0278 -0.0074 134 PHE   A O   
980  C  CB  . PHE   A 128 ? 0.1521 0.1378 0.1934 0.0025  -0.0266 -0.0025 134 PHE   A CB  
981  C  CG  . PHE   A 128 ? 0.1622 0.1469 0.2000 0.0037  -0.0262 -0.0013 134 PHE   A CG  
982  C  CD1 . PHE   A 128 ? 0.1590 0.1395 0.1940 0.0029  -0.0260 0.0003  134 PHE   A CD1 
983  C  CD2 . PHE   A 128 ? 0.1777 0.1656 0.2153 0.0059  -0.0263 -0.0022 134 PHE   A CD2 
984  C  CE1 . PHE   A 128 ? 0.1663 0.1450 0.1969 0.0044  -0.0257 0.0008  134 PHE   A CE1 
985  C  CE2 . PHE   A 128 ? 0.1813 0.1678 0.2153 0.0075  -0.0255 -0.0013 134 PHE   A CE2 
986  C  CZ  . PHE   A 128 ? 0.1772 0.1587 0.2072 0.0068  -0.0251 0.0002  134 PHE   A CZ  
987  N  N   . ALA   A 129 ? 0.1534 0.1390 0.2050 -0.0019 -0.0259 -0.0038 135 ALA   A N   
988  C  CA  . ALA   A 129 ? 0.1574 0.1425 0.2105 -0.0020 -0.0257 -0.0057 135 ALA   A CA  
989  C  C   . ALA   A 129 ? 0.1547 0.1375 0.2012 0.0004  -0.0254 -0.0057 135 ALA   A C   
990  O  O   . ALA   A 129 ? 0.1644 0.1444 0.2091 0.0003  -0.0244 -0.0033 135 ALA   A O   
991  C  CB  . ALA   A 129 ? 0.1656 0.1486 0.2229 -0.0038 -0.0246 -0.0042 135 ALA   A CB  
992  N  N   . ASP   A 130 ? 0.1461 0.1301 0.1894 0.0025  -0.0262 -0.0083 136 ASP   A N   
993  C  CA  . ASP   A 130 ? 0.1716 0.1527 0.2074 0.0054  -0.0252 -0.0077 136 ASP   A CA  
994  C  C   . ASP   A 130 ? 0.1864 0.1642 0.2224 0.0050  -0.0226 -0.0068 136 ASP   A C   
995  O  O   . ASP   A 130 ? 0.1867 0.1649 0.2267 0.0038  -0.0224 -0.0085 136 ASP   A O   
996  C  CB  . ASP   A 130 ? 0.2024 0.1856 0.2337 0.0084  -0.0273 -0.0110 136 ASP   A CB  
997  C  CG  . ASP   A 130 ? 0.2827 0.2625 0.3044 0.0124  -0.0262 -0.0099 136 ASP   A CG  
998  O  OD1 . ASP   A 130 ? 0.2851 0.2624 0.3039 0.0131  -0.0249 -0.0069 136 ASP   A OD1 
999  O  OD2 . ASP   A 130 ? 0.3270 0.3059 0.3436 0.0149  -0.0264 -0.0121 136 ASP   A OD2 
1000 N  N   . VAL   A 131 ? 0.1690 0.1430 0.2007 0.0063  -0.0201 -0.0043 137 VAL   A N   
1001 C  CA  . VAL   A 131 ? 0.1744 0.1457 0.2068 0.0064  -0.0167 -0.0032 137 VAL   A CA  
1002 C  C   . VAL   A 131 ? 0.1929 0.1608 0.2163 0.0102  -0.0141 -0.0026 137 VAL   A C   
1003 O  O   . VAL   A 131 ? 0.2053 0.1705 0.2283 0.0109  -0.0102 -0.0013 137 VAL   A O   
1004 C  CB  . VAL   A 131 ? 0.1931 0.1631 0.2318 0.0038  -0.0151 -0.0002 137 VAL   A CB  
1005 C  CG1 . VAL   A 131 ? 0.1938 0.1665 0.2398 0.0009  -0.0174 -0.0005 137 VAL   A CG1 
1006 C  CG2 . VAL   A 131 ? 0.1844 0.1520 0.2205 0.0039  -0.0147 0.0021  137 VAL   A CG2 
1007 N  N   . ARG   A 132 ? 0.1892 0.1571 0.2054 0.0130  -0.0159 -0.0031 138 ARG   A N   
1008 C  CA  . ARG   A 132 ? 0.1980 0.1619 0.2044 0.0173  -0.0133 -0.0015 138 ARG   A CA  
1009 C  C   . ARG   A 132 ? 0.2254 0.1881 0.2256 0.0203  -0.0120 -0.0036 138 ARG   A C   
1010 O  O   . ARG   A 132 ? 0.2420 0.2001 0.2343 0.0237  -0.0081 -0.0014 138 ARG   A O   
1011 C  CB  . ARG   A 132 ? 0.2007 0.1650 0.2008 0.0203  -0.0160 -0.0015 138 ARG   A CB  
1012 C  CG  . ARG   A 132 ? 0.1936 0.1572 0.1977 0.0181  -0.0163 0.0008  138 ARG   A CG  
1013 C  CD  . ARG   A 132 ? 0.2075 0.1721 0.2061 0.0215  -0.0190 0.0005  138 ARG   A CD  
1014 N  NE  . ARG   A 132 ? 0.2214 0.1926 0.2238 0.0210  -0.0235 -0.0032 138 ARG   A NE  
1015 C  CZ  . ARG   A 132 ? 0.2435 0.2178 0.2445 0.0233  -0.0266 -0.0042 138 ARG   A CZ  
1016 N  NH1 . ARG   A 132 ? 0.2304 0.2013 0.2249 0.0270  -0.0258 -0.0018 138 ARG   A NH1 
1017 N  NH2 . ARG   A 132 ? 0.2298 0.2107 0.2370 0.0221  -0.0301 -0.0074 138 ARG   A NH2 
1018 N  N   . ASP   A 133 ? 0.2195 0.1857 0.2229 0.0193  -0.0151 -0.0079 139 ASP   A N   
1019 C  CA  . ASP   A 133 ? 0.2322 0.1968 0.2291 0.0224  -0.0143 -0.0109 139 ASP   A CA  
1020 C  C   . ASP   A 133 ? 0.2348 0.1967 0.2356 0.0212  -0.0092 -0.0097 139 ASP   A C   
1021 O  O   . ASP   A 133 ? 0.2470 0.2066 0.2417 0.0240  -0.0075 -0.0119 139 ASP   A O   
1022 C  CB  . ASP   A 133 ? 0.2494 0.2182 0.2485 0.0219  -0.0199 -0.0167 139 ASP   A CB  
1023 C  CG  . ASP   A 133 ? 0.3147 0.2864 0.3265 0.0167  -0.0208 -0.0178 139 ASP   A CG  
1024 O  OD1 . ASP   A 133 ? 0.3124 0.2854 0.3310 0.0137  -0.0204 -0.0147 139 ASP   A OD1 
1025 O  OD2 . ASP   A 133 ? 0.3501 0.3222 0.3646 0.0161  -0.0219 -0.0219 139 ASP   A OD2 
1026 N  N   . LEU   A 134 ? 0.2275 0.1900 0.2384 0.0172  -0.0073 -0.0067 140 LEU   A N   
1027 C  CA  . LEU   A 134 ? 0.2080 0.1691 0.2247 0.0161  -0.0028 -0.0056 140 LEU   A CA  
1028 C  C   . LEU   A 134 ? 0.2193 0.1762 0.2319 0.0182  0.0034  -0.0014 140 LEU   A C   
1029 O  O   . LEU   A 134 ? 0.2224 0.1791 0.2421 0.0157  0.0057  0.0023  140 LEU   A O   
1030 C  CB  . LEU   A 134 ? 0.1960 0.1601 0.2255 0.0113  -0.0042 -0.0042 140 LEU   A CB  
1031 C  CG  . LEU   A 134 ? 0.2252 0.1928 0.2591 0.0091  -0.0094 -0.0074 140 LEU   A CG  
1032 C  CD1 . LEU   A 134 ? 0.2243 0.1939 0.2684 0.0052  -0.0105 -0.0052 140 LEU   A CD1 
1033 C  CD2 . LEU   A 134 ? 0.2382 0.2054 0.2713 0.0101  -0.0099 -0.0117 140 LEU   A CD2 
1034 N  N   . LEU   A 135 ? 0.2236 0.1770 0.2244 0.0231  0.0061  -0.0021 141 LEU   A N   
1035 C  CA  . LEU   A 135 ? 0.2371 0.1857 0.2324 0.0258  0.0128  0.0026  141 LEU   A CA  
1036 C  C   . LEU   A 135 ? 0.2504 0.1983 0.2553 0.0239  0.0192  0.0055  141 LEU   A C   
1037 O  O   . LEU   A 135 ? 0.2605 0.2059 0.2679 0.0235  0.0244  0.0101  141 LEU   A O   
1038 C  CB  . LEU   A 135 ? 0.2433 0.1877 0.2220 0.0322  0.0144  0.0014  141 LEU   A CB  
1039 C  CG  . LEU   A 135 ? 0.2737 0.2199 0.2436 0.0346  0.0072  -0.0025 141 LEU   A CG  
1040 C  CD1 . LEU   A 135 ? 0.2905 0.2320 0.2425 0.0418  0.0088  -0.0032 141 LEU   A CD1 
1041 C  CD2 . LEU   A 135 ? 0.2755 0.2232 0.2479 0.0329  0.0039  -0.0001 141 LEU   A CD2 
1042 N  N   . TRP   A 136 ? 0.2488 0.1991 0.2605 0.0226  0.0188  0.0028  142 TRP   A N   
1043 C  CA  . TRP   A 136 ? 0.2557 0.2065 0.2779 0.0213  0.0245  0.0051  142 TRP   A CA  
1044 C  C   . TRP   A 136 ? 0.2672 0.2211 0.3040 0.0162  0.0238  0.0083  142 TRP   A C   
1045 O  O   . TRP   A 136 ? 0.2902 0.2449 0.3370 0.0151  0.0288  0.0109  142 TRP   A O   
1046 C  CB  . TRP   A 136 ? 0.2520 0.2042 0.2775 0.0215  0.0237  0.0011  142 TRP   A CB  
1047 C  CG  . TRP   A 136 ? 0.2413 0.1970 0.2716 0.0184  0.0160  -0.0024 142 TRP   A CG  
1048 C  CD1 . TRP   A 136 ? 0.2496 0.2055 0.2728 0.0194  0.0108  -0.0070 142 TRP   A CD1 
1049 C  CD2 . TRP   A 136 ? 0.2438 0.2036 0.2879 0.0140  0.0132  -0.0015 142 TRP   A CD2 
1050 N  NE1 . TRP   A 136 ? 0.2494 0.2087 0.2815 0.0156  0.0058  -0.0086 142 TRP   A NE1 
1051 C  CE2 . TRP   A 136 ? 0.2471 0.2085 0.2910 0.0126  0.0071  -0.0050 142 TRP   A CE2 
1052 C  CE3 . TRP   A 136 ? 0.2513 0.2134 0.3080 0.0114  0.0152  0.0020  142 TRP   A CE3 
1053 C  CZ2 . TRP   A 136 ? 0.2475 0.2120 0.3018 0.0090  0.0036  -0.0046 142 TRP   A CZ2 
1054 C  CZ3 . TRP   A 136 ? 0.2429 0.2086 0.3095 0.0081  0.0107  0.0019  142 TRP   A CZ3 
1055 C  CH2 . TRP   A 136 ? 0.2467 0.2131 0.3114 0.0072  0.0053  -0.0011 142 TRP   A CH2 
1056 N  N   . LEU   A 137 ? 0.2580 0.2140 0.2966 0.0134  0.0178  0.0079  143 LEU   A N   
1057 C  CA  . LEU   A 137 ? 0.2672 0.2258 0.3184 0.0090  0.0164  0.0103  143 LEU   A CA  
1058 C  C   . LEU   A 137 ? 0.3223 0.2779 0.3761 0.0088  0.0222  0.0145  143 LEU   A C   
1059 O  O   . LEU   A 137 ? 0.3164 0.2742 0.3831 0.0053  0.0226  0.0163  143 LEU   A O   
1060 C  CB  . LEU   A 137 ? 0.2463 0.2062 0.2960 0.0069  0.0096  0.0091  143 LEU   A CB  
1061 C  CG  . LEU   A 137 ? 0.2322 0.1957 0.2840 0.0056  0.0039  0.0058  143 LEU   A CG  
1062 C  CD1 . LEU   A 137 ? 0.2437 0.2082 0.2928 0.0042  -0.0014 0.0051  143 LEU   A CD1 
1063 C  CD2 . LEU   A 137 ? 0.2275 0.1943 0.2921 0.0029  0.0032  0.0063  143 LEU   A CD2 
1064 N  N   . ASP   A 138 ? 0.3693 0.3198 0.4109 0.0125  0.0262  0.0161  144 ASP   A N   
1065 C  CA  . ASP   A 138 ? 0.4365 0.3824 0.4775 0.0132  0.0326  0.0206  144 ASP   A CA  
1066 C  C   . ASP   A 138 ? 0.4945 0.4390 0.5397 0.0146  0.0414  0.0235  144 ASP   A C   
1067 O  O   . ASP   A 138 ? 0.5130 0.4535 0.5592 0.0149  0.0477  0.0277  144 ASP   A O   
1068 C  CB  . ASP   A 138 ? 0.4850 0.4255 0.5087 0.0180  0.0334  0.0214  144 ASP   A CB  
1069 C  CG  . ASP   A 138 ? 0.5816 0.5219 0.6011 0.0172  0.0271  0.0204  144 ASP   A CG  
1070 O  OD1 . ASP   A 138 ? 0.5896 0.5322 0.6193 0.0128  0.0237  0.0202  144 ASP   A OD1 
1071 O  OD2 . ASP   A 138 ? 0.6488 0.5867 0.6546 0.0215  0.0255  0.0196  144 ASP   A OD2 
1072 N  N   . GLU   A 139 ? 0.5295 0.4762 0.5758 0.0161  0.0428  0.0214  145 GLU   A N   
1073 C  CA  . GLU   A 139 ? 0.5732 0.5187 0.6235 0.0181  0.0520  0.0241  145 GLU   A CA  
1074 C  C   . GLU   A 139 ? 0.5874 0.5390 0.6547 0.0152  0.0518  0.0231  145 GLU   A C   
1075 O  O   . GLU   A 139 ? 0.6000 0.5554 0.6701 0.0137  0.0449  0.0194  145 GLU   A O   
1076 C  CB  . GLU   A 139 ? 0.6325 0.5733 0.6652 0.0245  0.0561  0.0229  145 GLU   A CB  
1077 C  CG  . GLU   A 139 ? 0.7379 0.6806 0.7638 0.0259  0.0491  0.0170  145 GLU   A CG  
1078 C  CD  . GLU   A 139 ? 0.8743 0.8122 0.8797 0.0315  0.0482  0.0148  145 GLU   A CD  
1079 O  OE1 . GLU   A 139 ? 0.9081 0.8448 0.9060 0.0351  0.0490  0.0113  145 GLU   A OE1 
1080 O  OE2 . GLU   A 139 ? 0.9131 0.8484 0.9098 0.0326  0.0463  0.0164  145 GLU   A OE2 
1081 N  N   . SER   B 1   ? 0.3593 0.3073 0.3829 0.0040  -0.0562 -0.0086 7   SER   C N   
1082 C  CA  . SER   B 1   ? 0.3583 0.3105 0.3931 0.0050  -0.0572 -0.0093 7   SER   C CA  
1083 C  C   . SER   B 1   ? 0.3362 0.2923 0.3772 0.0057  -0.0558 -0.0090 7   SER   C C   
1084 O  O   . SER   B 1   ? 0.3392 0.2934 0.3758 0.0054  -0.0558 -0.0079 7   SER   C O   
1085 C  CB  . SER   B 1   ? 0.4019 0.3512 0.4395 0.0046  -0.0633 -0.0097 7   SER   C CB  
1086 O  OG  . SER   B 1   ? 0.4595 0.4050 0.4949 0.0044  -0.0676 -0.0084 7   SER   C OG  
1087 N  N   . GLY   B 2   ? 0.2994 0.2605 0.3501 0.0062  -0.0544 -0.0101 8   GLY   C N   
1088 C  CA  . GLY   B 2   ? 0.2793 0.2438 0.3359 0.0067  -0.0526 -0.0106 8   GLY   C CA  
1089 C  C   . GLY   B 2   ? 0.2572 0.2275 0.3207 0.0064  -0.0485 -0.0118 8   GLY   C C   
1090 O  O   . GLY   B 2   ? 0.2702 0.2417 0.3320 0.0057  -0.0463 -0.0116 8   GLY   C O   
1091 N  N   . ALA   B 3   ? 0.2314 0.2049 0.3025 0.0068  -0.0473 -0.0133 9   ALA   C N   
1092 C  CA  . ALA   B 3   ? 0.2233 0.2021 0.2997 0.0057  -0.0428 -0.0147 9   ALA   C CA  
1093 C  C   . ALA   B 3   ? 0.2161 0.1970 0.2955 0.0057  -0.0400 -0.0162 9   ALA   C C   
1094 O  O   . ALA   B 3   ? 0.2307 0.2092 0.3111 0.0071  -0.0423 -0.0166 9   ALA   C O   
1095 C  CB  . ALA   B 3   ? 0.2323 0.2139 0.3182 0.0055  -0.0440 -0.0164 9   ALA   C CB  
1096 N  N   . ILE   B 4   ? 0.2060 0.1905 0.2860 0.0040  -0.0352 -0.0171 10  ILE   C N   
1097 C  CA  . ILE   B 4   ? 0.1931 0.1797 0.2756 0.0034  -0.0318 -0.0193 10  ILE   C CA  
1098 C  C   . ILE   B 4   ? 0.2000 0.1912 0.2926 0.0028  -0.0293 -0.0224 10  ILE   C C   
1099 O  O   . ILE   B 4   ? 0.1932 0.1868 0.2868 0.0010  -0.0278 -0.0220 10  ILE   C O   
1100 C  CB  . ILE   B 4   ? 0.1972 0.1843 0.2717 0.0011  -0.0281 -0.0180 10  ILE   C CB  
1101 C  CG1 . ILE   B 4   ? 0.2142 0.1979 0.2803 0.0015  -0.0302 -0.0150 10  ILE   C CG1 
1102 C  CG2 . ILE   B 4   ? 0.1925 0.1811 0.2684 -0.0001 -0.0244 -0.0207 10  ILE   C CG2 
1103 C  CD1 . ILE   B 4   ? 0.2376 0.2225 0.2973 -0.0007 -0.0277 -0.0130 10  ILE   C CD1 
1104 N  N   . TYR   B 5   ? 0.2135 0.2060 0.3142 0.0042  -0.0286 -0.0256 11  TYR   C N   
1105 C  CA  . TYR   B 5   ? 0.2132 0.2112 0.3254 0.0037  -0.0255 -0.0292 11  TYR   C CA  
1106 C  C   . TYR   B 5   ? 0.2217 0.2215 0.3333 0.0022  -0.0196 -0.0323 11  TYR   C C   
1107 O  O   . TYR   B 5   ? 0.2262 0.2236 0.3389 0.0040  -0.0200 -0.0340 11  TYR   C O   
1108 C  CB  . TYR   B 5   ? 0.2095 0.2077 0.3336 0.0070  -0.0301 -0.0309 11  TYR   C CB  
1109 C  CG  . TYR   B 5   ? 0.2086 0.2047 0.3325 0.0078  -0.0362 -0.0280 11  TYR   C CG  
1110 C  CD1 . TYR   B 5   ? 0.2160 0.2160 0.3456 0.0063  -0.0359 -0.0283 11  TYR   C CD1 
1111 C  CD2 . TYR   B 5   ? 0.2336 0.2236 0.3500 0.0092  -0.0417 -0.0250 11  TYR   C CD2 
1112 C  CE1 . TYR   B 5   ? 0.2398 0.2373 0.3680 0.0066  -0.0415 -0.0259 11  TYR   C CE1 
1113 C  CE2 . TYR   B 5   ? 0.2545 0.2419 0.3686 0.0093  -0.0468 -0.0227 11  TYR   C CE2 
1114 C  CZ  . TYR   B 5   ? 0.2639 0.2549 0.3842 0.0082  -0.0469 -0.0233 11  TYR   C CZ  
1115 O  OH  . TYR   B 5   ? 0.3015 0.2893 0.4186 0.0080  -0.0520 -0.0213 11  TYR   C OH  
1116 N  N   . VAL   B 6   ? 0.2193 0.2224 0.3286 -0.0014 -0.0141 -0.0332 12  VAL   C N   
1117 C  CA  . VAL   B 6   ? 0.2354 0.2395 0.3418 -0.0037 -0.0081 -0.0362 12  VAL   C CA  
1118 C  C   . VAL   B 6   ? 0.2486 0.2585 0.3614 -0.0067 -0.0022 -0.0393 12  VAL   C C   
1119 O  O   . VAL   B 6   ? 0.2396 0.2510 0.3503 -0.0093 -0.0019 -0.0371 12  VAL   C O   
1120 C  CB  . VAL   B 6   ? 0.2587 0.2591 0.3503 -0.0064 -0.0074 -0.0330 12  VAL   C CB  
1121 C  CG1 . VAL   B 6   ? 0.2566 0.2569 0.3419 -0.0086 -0.0087 -0.0288 12  VAL   C CG1 
1122 C  CG2 . VAL   B 6   ? 0.2875 0.2885 0.3747 -0.0097 -0.0014 -0.0362 12  VAL   C CG2 
1123 N  N   . GLY   B 7   ? 0.2596 0.2729 0.3814 -0.0063 0.0023  -0.0448 13  GLY   C N   
1124 C  CA  . GLY   B 7   ? 0.2636 0.2833 0.3926 -0.0095 0.0088  -0.0484 13  GLY   C CA  
1125 C  C   . GLY   B 7   ? 0.2777 0.3014 0.4170 -0.0087 0.0058  -0.0471 13  GLY   C C   
1126 O  O   . GLY   B 7   ? 0.2905 0.3134 0.4378 -0.0044 -0.0004 -0.0464 13  GLY   C O   
1127 N  N   . ASN   B 8   ? 0.2698 0.2964 0.4069 -0.0132 0.0089  -0.0460 14  ASN   C N   
1128 C  CA  . ASN   B 8   ? 0.2688 0.2984 0.4146 -0.0130 0.0055  -0.0444 14  ASN   C CA  
1129 C  C   . ASN   B 8   ? 0.2444 0.2686 0.3785 -0.0139 0.0004  -0.0383 14  ASN   C C   
1130 O  O   . ASN   B 8   ? 0.2415 0.2672 0.3771 -0.0164 -0.0001 -0.0366 14  ASN   C O   
1131 C  CB  . ASN   B 8   ? 0.3022 0.3391 0.4563 -0.0172 0.0121  -0.0475 14  ASN   C CB  
1132 C  CG  . ASN   B 8   ? 0.3929 0.4362 0.5630 -0.0153 0.0166  -0.0540 14  ASN   C CG  
1133 O  OD1 . ASN   B 8   ? 0.4148 0.4607 0.5995 -0.0107 0.0121  -0.0556 14  ASN   C OD1 
1134 N  ND2 . ASN   B 8   ? 0.4156 0.4615 0.5832 -0.0188 0.0252  -0.0580 14  ASN   C ND2 
1135 N  N   . TYR   B 9   ? 0.2233 0.2413 0.3469 -0.0117 -0.0034 -0.0354 15  TYR   C N   
1136 C  CA  . TYR   B 9   ? 0.2163 0.2294 0.3298 -0.0119 -0.0080 -0.0303 15  TYR   C CA  
1137 C  C   . TYR   B 9   ? 0.2076 0.2166 0.3209 -0.0073 -0.0148 -0.0286 15  TYR   C C   
1138 O  O   . TYR   B 9   ? 0.2162 0.2241 0.3315 -0.0044 -0.0159 -0.0301 15  TYR   C O   
1139 C  CB  . TYR   B 9   ? 0.2225 0.2318 0.3217 -0.0146 -0.0058 -0.0279 15  TYR   C CB  
1140 C  CG  . TYR   B 9   ? 0.2359 0.2474 0.3313 -0.0201 0.0002  -0.0286 15  TYR   C CG  
1141 C  CD1 . TYR   B 9   ? 0.2569 0.2702 0.3545 -0.0234 0.0012  -0.0275 15  TYR   C CD1 
1142 C  CD2 . TYR   B 9   ? 0.2557 0.2670 0.3447 -0.0226 0.0050  -0.0303 15  TYR   C CD2 
1143 C  CE1 . TYR   B 9   ? 0.2765 0.2912 0.3695 -0.0292 0.0069  -0.0278 15  TYR   C CE1 
1144 C  CE2 . TYR   B 9   ? 0.2729 0.2853 0.3564 -0.0285 0.0106  -0.0308 15  TYR   C CE2 
1145 C  CZ  . TYR   B 9   ? 0.2988 0.3130 0.3842 -0.0319 0.0116  -0.0294 15  TYR   C CZ  
1146 O  OH  . TYR   B 9   ? 0.3402 0.3550 0.4190 -0.0384 0.0170  -0.0294 15  TYR   C OH  
1147 N  N   . ARG   B 10  ? 0.1780 0.1840 0.2878 -0.0069 -0.0192 -0.0253 16  ARG   C N   
1148 C  CA  . ARG   B 10  ? 0.1782 0.1794 0.2844 -0.0035 -0.0251 -0.0232 16  ARG   C CA  
1149 C  C   . ARG   B 10  ? 0.1878 0.1847 0.2819 -0.0045 -0.0258 -0.0195 16  ARG   C C   
1150 O  O   . ARG   B 10  ? 0.1840 0.1808 0.2763 -0.0068 -0.0251 -0.0181 16  ARG   C O   
1151 C  CB  . ARG   B 10  ? 0.1780 0.1795 0.2920 -0.0021 -0.0300 -0.0233 16  ARG   C CB  
1152 C  CG  . ARG   B 10  ? 0.2154 0.2110 0.3228 -0.0001 -0.0359 -0.0207 16  ARG   C CG  
1153 C  CD  . ARG   B 10  ? 0.2231 0.2186 0.3382 0.0008  -0.0412 -0.0212 16  ARG   C CD  
1154 N  NE  . ARG   B 10  ? 0.2720 0.2625 0.3797 0.0005  -0.0450 -0.0190 16  ARG   C NE  
1155 C  CZ  . ARG   B 10  ? 0.3193 0.3043 0.4210 0.0023  -0.0498 -0.0177 16  ARG   C CZ  
1156 N  NH1 . ARG   B 10  ? 0.3049 0.2884 0.4066 0.0044  -0.0520 -0.0179 16  ARG   C NH1 
1157 N  NH2 . ARG   B 10  ? 0.3067 0.2870 0.4014 0.0018  -0.0523 -0.0164 16  ARG   C NH2 
1158 N  N   . VAL   B 11  ? 0.1828 0.1764 0.2694 -0.0029 -0.0269 -0.0181 17  VAL   C N   
1159 C  CA  . VAL   B 11  ? 0.1906 0.1809 0.2676 -0.0034 -0.0275 -0.0149 17  VAL   C CA  
1160 C  C   . VAL   B 11  ? 0.1983 0.1848 0.2727 -0.0007 -0.0320 -0.0136 17  VAL   C C   
1161 O  O   . VAL   B 11  ? 0.2001 0.1852 0.2744 0.0012  -0.0339 -0.0141 17  VAL   C O   
1162 C  CB  . VAL   B 11  ? 0.1992 0.1892 0.2700 -0.0040 -0.0253 -0.0142 17  VAL   C CB  
1163 C  CG1 . VAL   B 11  ? 0.2004 0.1882 0.2635 -0.0046 -0.0259 -0.0109 17  VAL   C CG1 
1164 C  CG2 . VAL   B 11  ? 0.2022 0.1954 0.2747 -0.0067 -0.0207 -0.0163 17  VAL   C CG2 
1165 N  N   . VAL   B 12  ? 0.1770 0.1611 0.2484 -0.0008 -0.0335 -0.0120 18  VAL   C N   
1166 C  CA  . VAL   B 12  ? 0.1892 0.1693 0.2570 0.0012  -0.0370 -0.0114 18  VAL   C CA  
1167 C  C   . VAL   B 12  ? 0.1856 0.1632 0.2470 0.0013  -0.0365 -0.0094 18  VAL   C C   
1168 O  O   . VAL   B 12  ? 0.1790 0.1576 0.2399 -0.0003 -0.0345 -0.0083 18  VAL   C O   
1169 C  CB  . VAL   B 12  ? 0.2122 0.1911 0.2846 0.0012  -0.0402 -0.0124 18  VAL   C CB  
1170 C  CG1 . VAL   B 12  ? 0.2400 0.2215 0.3203 0.0018  -0.0417 -0.0143 18  VAL   C CG1 
1171 C  CG2 . VAL   B 12  ? 0.2030 0.1829 0.2779 -0.0010 -0.0390 -0.0122 18  VAL   C CG2 
1172 N  N   . ASN   B 13  ? 0.1822 0.1563 0.2389 0.0030  -0.0383 -0.0091 19  ASN   C N   
1173 C  CA  . ASN   B 13  ? 0.1814 0.1533 0.2340 0.0036  -0.0378 -0.0080 19  ASN   C CA  
1174 C  C   . ASN   B 13  ? 0.1851 0.1551 0.2399 0.0026  -0.0388 -0.0082 19  ASN   C C   
1175 O  O   . ASN   B 13  ? 0.1874 0.1561 0.2444 0.0024  -0.0411 -0.0095 19  ASN   C O   
1176 C  CB  . ASN   B 13  ? 0.1923 0.1607 0.2397 0.0052  -0.0391 -0.0085 19  ASN   C CB  
1177 C  CG  . ASN   B 13  ? 0.2157 0.1852 0.2601 0.0057  -0.0381 -0.0080 19  ASN   C CG  
1178 O  OD1 . ASN   B 13  ? 0.2182 0.1872 0.2623 0.0056  -0.0396 -0.0085 19  ASN   C OD1 
1179 N  ND2 . ASN   B 13  ? 0.1909 0.1619 0.2336 0.0061  -0.0359 -0.0069 19  ASN   C ND2 
1180 N  N   . ARG   B 14  ? 0.1756 0.1454 0.2303 0.0019  -0.0376 -0.0067 20  ARG   C N   
1181 C  CA  . ARG   B 14  ? 0.1699 0.1372 0.2264 0.0005  -0.0387 -0.0066 20  ARG   C CA  
1182 C  C   . ARG   B 14  ? 0.1836 0.1459 0.2381 0.0019  -0.0412 -0.0082 20  ARG   C C   
1183 O  O   . ARG   B 14  ? 0.1894 0.1502 0.2464 0.0005  -0.0431 -0.0091 20  ARG   C O   
1184 C  CB  . ARG   B 14  ? 0.1852 0.1514 0.2406 -0.0003 -0.0378 -0.0043 20  ARG   C CB  
1185 C  CG  . ARG   B 14  ? 0.2017 0.1652 0.2589 -0.0026 -0.0388 -0.0036 20  ARG   C CG  
1186 C  CD  . ARG   B 14  ? 0.2103 0.1712 0.2654 -0.0028 -0.0389 -0.0009 20  ARG   C CD  
1187 N  NE  . ARG   B 14  ? 0.2098 0.1671 0.2657 -0.0055 -0.0400 0.0006  20  ARG   C NE  
1188 C  CZ  . ARG   B 14  ? 0.2259 0.1775 0.2818 -0.0046 -0.0422 0.0001  20  ARG   C CZ  
1189 N  NH1 . ARG   B 14  ? 0.2250 0.1742 0.2801 -0.0013 -0.0431 -0.0024 20  ARG   C NH1 
1190 N  NH2 . ARG   B 14  ? 0.2297 0.1776 0.2860 -0.0075 -0.0434 0.0019  20  ARG   C NH2 
1191 N  N   . HIS   B 15  ? 0.1778 0.1379 0.2277 0.0043  -0.0411 -0.0088 21  HIS   C N   
1192 C  CA  . HIS   B 15  ? 0.1835 0.1381 0.2298 0.0052  -0.0430 -0.0107 21  HIS   C CA  
1193 C  C   . HIS   B 15  ? 0.1979 0.1515 0.2434 0.0044  -0.0457 -0.0122 21  HIS   C C   
1194 O  O   . HIS   B 15  ? 0.2186 0.1673 0.2610 0.0043  -0.0481 -0.0137 21  HIS   C O   
1195 C  CB  . HIS   B 15  ? 0.1851 0.1377 0.2268 0.0075  -0.0412 -0.0115 21  HIS   C CB  
1196 C  CG  . HIS   B 15  ? 0.2095 0.1640 0.2477 0.0082  -0.0401 -0.0117 21  HIS   C CG  
1197 N  ND1 . HIS   B 15  ? 0.2121 0.1715 0.2519 0.0083  -0.0382 -0.0100 21  HIS   C ND1 
1198 C  CD2 . HIS   B 15  ? 0.2247 0.1761 0.2570 0.0083  -0.0409 -0.0133 21  HIS   C CD2 
1199 C  CE1 . HIS   B 15  ? 0.2198 0.1791 0.2554 0.0086  -0.0378 -0.0106 21  HIS   C CE1 
1200 N  NE2 . HIS   B 15  ? 0.2390 0.1934 0.2695 0.0085  -0.0393 -0.0125 21  HIS   C NE2 
1201 N  N   . LEU   B 16  ? 0.1973 0.1551 0.2459 0.0039  -0.0460 -0.0117 22  LEU   C N   
1202 C  CA  . LEU   B 16  ? 0.2039 0.1608 0.2532 0.0034  -0.0495 -0.0127 22  LEU   C CA  
1203 C  C   . LEU   B 16  ? 0.2213 0.1820 0.2796 0.0018  -0.0508 -0.0128 22  LEU   C C   
1204 O  O   . LEU   B 16  ? 0.2292 0.1905 0.2909 0.0016  -0.0540 -0.0135 22  LEU   C O   
1205 C  CB  . LEU   B 16  ? 0.2066 0.1647 0.2534 0.0043  -0.0494 -0.0122 22  LEU   C CB  
1206 C  CG  . LEU   B 16  ? 0.2274 0.1823 0.2654 0.0054  -0.0479 -0.0122 22  LEU   C CG  
1207 C  CD1 . LEU   B 16  ? 0.2450 0.2008 0.2805 0.0056  -0.0479 -0.0114 22  LEU   C CD1 
1208 C  CD2 . LEU   B 16  ? 0.2484 0.1967 0.2794 0.0050  -0.0502 -0.0138 22  LEU   C CD2 
1209 N  N   . ALA   B 17  ? 0.2062 0.1697 0.2688 0.0005  -0.0482 -0.0121 23  ALA   C N   
1210 C  CA  . ALA   B 17  ? 0.2163 0.1843 0.2877 -0.0016 -0.0482 -0.0126 23  ALA   C CA  
1211 C  C   . ALA   B 17  ? 0.2166 0.1822 0.2909 -0.0027 -0.0525 -0.0136 23  ALA   C C   
1212 O  O   . ALA   B 17  ? 0.2228 0.1828 0.2918 -0.0028 -0.0543 -0.0138 23  ALA   C O   
1213 C  CB  . ALA   B 17  ? 0.2171 0.1870 0.2899 -0.0037 -0.0448 -0.0113 23  ALA   C CB  
1214 N  N   . THR   B 18  ? 0.2090 0.1788 0.2922 -0.0036 -0.0542 -0.0146 24  THR   C N   
1215 C  CA  . THR   B 18  ? 0.2167 0.1851 0.3043 -0.0050 -0.0590 -0.0155 24  THR   C CA  
1216 C  C   . THR   B 18  ? 0.2169 0.1876 0.3106 -0.0082 -0.0576 -0.0155 24  THR   C C   
1217 O  O   . THR   B 18  ? 0.2025 0.1763 0.2974 -0.0095 -0.0529 -0.0148 24  THR   C O   
1218 C  CB  . THR   B 18  ? 0.2283 0.2010 0.3246 -0.0041 -0.0619 -0.0165 24  THR   C CB  
1219 O  OG1 . THR   B 18  ? 0.2365 0.2168 0.3427 -0.0049 -0.0576 -0.0172 24  THR   C OG1 
1220 C  CG2 . THR   B 18  ? 0.2298 0.1996 0.3199 -0.0015 -0.0636 -0.0161 24  THR   C CG2 
1221 N  N   . HIS   B 19  ? 0.2185 0.1879 0.3165 -0.0100 -0.0620 -0.0163 25  HIS   C N   
1222 C  CA  . HIS   B 19  ? 0.2261 0.1983 0.3312 -0.0136 -0.0608 -0.0163 25  HIS   C CA  
1223 C  C   . HIS   B 19  ? 0.2139 0.1956 0.3301 -0.0149 -0.0564 -0.0169 25  HIS   C C   
1224 O  O   . HIS   B 19  ? 0.2216 0.2058 0.3396 -0.0178 -0.0521 -0.0162 25  HIS   C O   
1225 C  CB  . HIS   B 19  ? 0.2706 0.2410 0.3802 -0.0155 -0.0668 -0.0172 25  HIS   C CB  
1226 C  CG  . HIS   B 19  ? 0.3715 0.3321 0.4701 -0.0151 -0.0709 -0.0172 25  HIS   C CG  
1227 N  ND1 . HIS   B 19  ? 0.4216 0.3762 0.5128 -0.0160 -0.0691 -0.0167 25  HIS   C ND1 
1228 C  CD2 . HIS   B 19  ? 0.4104 0.3661 0.5045 -0.0142 -0.0767 -0.0180 25  HIS   C CD2 
1229 C  CE1 . HIS   B 19  ? 0.4351 0.3816 0.5179 -0.0154 -0.0732 -0.0177 25  HIS   C CE1 
1230 N  NE2 . HIS   B 19  ? 0.4361 0.3828 0.5193 -0.0146 -0.0777 -0.0184 25  HIS   C NE2 
1231 N  N   . ASN   B 20  ? 0.2061 0.1924 0.3290 -0.0127 -0.0574 -0.0181 26  ASN   C N   
1232 C  CA  . ASN   B 20  ? 0.2026 0.1978 0.3367 -0.0135 -0.0529 -0.0196 26  ASN   C CA  
1233 C  C   . ASN   B 20  ? 0.2000 0.1961 0.3277 -0.0136 -0.0463 -0.0189 26  ASN   C C   
1234 O  O   . ASN   B 20  ? 0.2030 0.2047 0.3359 -0.0163 -0.0410 -0.0196 26  ASN   C O   
1235 C  CB  . ASN   B 20  ? 0.2459 0.2447 0.3885 -0.0104 -0.0558 -0.0212 26  ASN   C CB  
1236 C  CG  . ASN   B 20  ? 0.3425 0.3508 0.4987 -0.0111 -0.0511 -0.0236 26  ASN   C CG  
1237 O  OD1 . ASN   B 20  ? 0.3661 0.3801 0.5329 -0.0141 -0.0495 -0.0248 26  ASN   C OD1 
1238 N  ND2 . ASN   B 20  ? 0.3679 0.3779 0.5242 -0.0084 -0.0483 -0.0246 26  ASN   C ND2 
1239 N  N   . ASP   B 21  ? 0.1965 0.1872 0.3128 -0.0109 -0.0465 -0.0175 27  ASP   C N   
1240 C  CA  . ASP   B 21  ? 0.1974 0.1887 0.3075 -0.0113 -0.0411 -0.0166 27  ASP   C CA  
1241 C  C   . ASP   B 21  ? 0.2083 0.1982 0.3149 -0.0151 -0.0384 -0.0149 27  ASP   C C   
1242 O  O   . ASP   B 21  ? 0.2173 0.2105 0.3242 -0.0176 -0.0335 -0.0147 27  ASP   C O   
1243 C  CB  . ASP   B 21  ? 0.1951 0.1808 0.2942 -0.0082 -0.0424 -0.0152 27  ASP   C CB  
1244 C  CG  . ASP   B 21  ? 0.2388 0.2254 0.3391 -0.0051 -0.0439 -0.0162 27  ASP   C CG  
1245 O  OD1 . ASP   B 21  ? 0.2440 0.2358 0.3514 -0.0050 -0.0415 -0.0178 27  ASP   C OD1 
1246 O  OD2 . ASP   B 21  ? 0.2415 0.2230 0.3353 -0.0029 -0.0475 -0.0155 27  ASP   C OD2 
1247 N  N   . TRP   B 22  ? 0.2091 0.1933 0.3118 -0.0156 -0.0418 -0.0136 28  TRP   C N   
1248 C  CA  . TRP   B 22  ? 0.2138 0.1952 0.3130 -0.0191 -0.0402 -0.0117 28  TRP   C CA  
1249 C  C   . TRP   B 22  ? 0.2181 0.2050 0.3263 -0.0239 -0.0378 -0.0124 28  TRP   C C   
1250 O  O   . TRP   B 22  ? 0.2321 0.2190 0.3377 -0.0277 -0.0342 -0.0108 28  TRP   C O   
1251 C  CB  . TRP   B 22  ? 0.2222 0.1954 0.3156 -0.0183 -0.0446 -0.0108 28  TRP   C CB  
1252 C  CG  . TRP   B 22  ? 0.2093 0.1771 0.2930 -0.0150 -0.0447 -0.0095 28  TRP   C CG  
1253 C  CD1 . TRP   B 22  ? 0.2155 0.1802 0.2946 -0.0112 -0.0470 -0.0104 28  TRP   C CD1 
1254 C  CD2 . TRP   B 22  ? 0.2048 0.1698 0.2826 -0.0157 -0.0426 -0.0070 28  TRP   C CD2 
1255 N  NE1 . TRP   B 22  ? 0.2258 0.1869 0.2978 -0.0093 -0.0459 -0.0090 28  TRP   C NE1 
1256 C  CE2 . TRP   B 22  ? 0.2151 0.1763 0.2866 -0.0117 -0.0435 -0.0068 28  TRP   C CE2 
1257 C  CE3 . TRP   B 22  ? 0.2196 0.1851 0.2969 -0.0195 -0.0400 -0.0048 28  TRP   C CE3 
1258 C  CZ2 . TRP   B 22  ? 0.2241 0.1824 0.2906 -0.0111 -0.0425 -0.0045 28  TRP   C CZ2 
1259 C  CZ3 . TRP   B 22  ? 0.2317 0.1933 0.3024 -0.0191 -0.0395 -0.0022 28  TRP   C CZ3 
1260 C  CH2 . TRP   B 22  ? 0.2254 0.1837 0.2916 -0.0147 -0.0409 -0.0021 28  TRP   C CH2 
1261 N  N   . ALA   B 23  ? 0.2022 0.1939 0.3210 -0.0239 -0.0396 -0.0147 29  ALA   C N   
1262 C  CA  . ALA   B 23  ? 0.2185 0.2168 0.3480 -0.0284 -0.0369 -0.0159 29  ALA   C CA  
1263 C  C   . ALA   B 23  ? 0.2291 0.2351 0.3630 -0.0299 -0.0300 -0.0174 29  ALA   C C   
1264 O  O   . ALA   B 23  ? 0.2341 0.2458 0.3751 -0.0344 -0.0259 -0.0184 29  ALA   C O   
1265 C  CB  . ALA   B 23  ? 0.2089 0.2108 0.3501 -0.0277 -0.0415 -0.0180 29  ALA   C CB  
1266 N  N   . ASN   B 24  ? 0.2024 0.2087 0.3327 -0.0262 -0.0288 -0.0181 30  ASN   C N   
1267 C  CA  . ASN   B 24  ? 0.1966 0.2090 0.3297 -0.0271 -0.0224 -0.0201 30  ASN   C CA  
1268 C  C   . ASN   B 24  ? 0.2144 0.2221 0.3339 -0.0268 -0.0201 -0.0179 30  ASN   C C   
1269 O  O   . ASN   B 24  ? 0.2144 0.2241 0.3327 -0.0251 -0.0175 -0.0193 30  ASN   C O   
1270 C  CB  . ASN   B 24  ? 0.1957 0.2129 0.3389 -0.0229 -0.0236 -0.0234 30  ASN   C CB  
1271 C  CG  . ASN   B 24  ? 0.2527 0.2759 0.4115 -0.0237 -0.0256 -0.0256 30  ASN   C CG  
1272 O  OD1 . ASN   B 24  ? 0.2550 0.2855 0.4236 -0.0272 -0.0206 -0.0278 30  ASN   C OD1 
1273 N  ND2 . ASN   B 24  ? 0.2532 0.2733 0.4144 -0.0209 -0.0331 -0.0251 30  ASN   C ND2 
1274 N  N   . LEU   B 25  ? 0.2187 0.2199 0.3285 -0.0283 -0.0218 -0.0144 31  LEU   C N   
1275 C  CA  . LEU   B 25  ? 0.2224 0.2187 0.3202 -0.0278 -0.0211 -0.0118 31  LEU   C CA  
1276 C  C   . LEU   B 25  ? 0.2252 0.2242 0.3192 -0.0317 -0.0152 -0.0118 31  LEU   C C   
1277 O  O   . LEU   B 25  ? 0.2488 0.2500 0.3441 -0.0369 -0.0116 -0.0118 31  LEU   C O   
1278 C  CB  . LEU   B 25  ? 0.2278 0.2168 0.3187 -0.0291 -0.0243 -0.0083 31  LEU   C CB  
1279 C  CG  . LEU   B 25  ? 0.2450 0.2285 0.3249 -0.0285 -0.0248 -0.0050 31  LEU   C CG  
1280 C  CD1 . LEU   B 25  ? 0.2339 0.2164 0.3114 -0.0229 -0.0270 -0.0057 31  LEU   C CD1 
1281 C  CD2 . LEU   B 25  ? 0.2512 0.2274 0.3266 -0.0295 -0.0283 -0.0020 31  LEU   C CD2 
1282 N  N   . VAL   B 26  ? 0.1998 0.1982 0.2877 -0.0296 -0.0141 -0.0118 32  VAL   C N   
1283 C  CA  . VAL   B 26  ? 0.2095 0.2088 0.2909 -0.0334 -0.0092 -0.0115 32  VAL   C CA  
1284 C  C   . VAL   B 26  ? 0.2351 0.2277 0.3045 -0.0341 -0.0116 -0.0070 32  VAL   C C   
1285 O  O   . VAL   B 26  ? 0.2550 0.2454 0.3174 -0.0392 -0.0097 -0.0045 32  VAL   C O   
1286 C  CB  . VAL   B 26  ? 0.2165 0.2198 0.3005 -0.0309 -0.0064 -0.0151 32  VAL   C CB  
1287 C  CG1 . VAL   B 26  ? 0.2211 0.2239 0.2957 -0.0348 -0.0019 -0.0147 32  VAL   C CG1 
1288 C  CG2 . VAL   B 26  ? 0.2141 0.2244 0.3117 -0.0304 -0.0038 -0.0197 32  VAL   C CG2 
1289 N  N   . TRP   B 27  ? 0.2250 0.2142 0.2922 -0.0291 -0.0161 -0.0057 33  TRP   C N   
1290 C  CA  . TRP   B 27  ? 0.2236 0.2073 0.2818 -0.0288 -0.0188 -0.0017 33  TRP   C CA  
1291 C  C   . TRP   B 27  ? 0.2175 0.1984 0.2767 -0.0232 -0.0233 -0.0013 33  TRP   C C   
1292 O  O   . TRP   B 27  ? 0.2114 0.1948 0.2752 -0.0197 -0.0238 -0.0040 33  TRP   C O   
1293 C  CB  . TRP   B 27  ? 0.2333 0.2182 0.2853 -0.0299 -0.0164 -0.0017 33  TRP   C CB  
1294 C  CG  . TRP   B 27  ? 0.2457 0.2263 0.2902 -0.0287 -0.0197 0.0020  33  TRP   C CG  
1295 C  CD1 . TRP   B 27  ? 0.2749 0.2511 0.3122 -0.0320 -0.0213 0.0061  33  TRP   C CD1 
1296 C  CD2 . TRP   B 27  ? 0.2435 0.2240 0.2877 -0.0240 -0.0220 0.0019  33  TRP   C CD2 
1297 N  NE1 . TRP   B 27  ? 0.2778 0.2517 0.3119 -0.0292 -0.0248 0.0085  33  TRP   C NE1 
1298 C  CE2 . TRP   B 27  ? 0.2637 0.2406 0.3020 -0.0244 -0.0248 0.0058  33  TRP   C CE2 
1299 C  CE3 . TRP   B 27  ? 0.2449 0.2280 0.2936 -0.0198 -0.0221 -0.0010 33  TRP   C CE3 
1300 C  CZ2 . TRP   B 27  ? 0.2605 0.2374 0.2980 -0.0209 -0.0271 0.0066  33  TRP   C CZ2 
1301 C  CZ3 . TRP   B 27  ? 0.2462 0.2284 0.2926 -0.0166 -0.0243 0.0001  33  TRP   C CZ3 
1302 C  CH2 . TRP   B 27  ? 0.2439 0.2236 0.2853 -0.0172 -0.0265 0.0036  33  TRP   C CH2 
1303 N  N   . GLU   B 28  ? 0.2141 0.1897 0.2692 -0.0225 -0.0266 0.0018  34  GLU   C N   
1304 C  CA  . GLU   B 28  ? 0.2181 0.1911 0.2733 -0.0174 -0.0300 0.0019  34  GLU   C CA  
1305 C  C   . GLU   B 28  ? 0.2192 0.1882 0.2692 -0.0168 -0.0322 0.0054  34  GLU   C C   
1306 O  O   . GLU   B 28  ? 0.2133 0.1794 0.2598 -0.0204 -0.0327 0.0084  34  GLU   C O   
1307 C  CB  . GLU   B 28  ? 0.2159 0.1866 0.2752 -0.0156 -0.0324 0.0005  34  GLU   C CB  
1308 C  CG  . GLU   B 28  ? 0.2261 0.1931 0.2856 -0.0189 -0.0334 0.0022  34  GLU   C CG  
1309 C  CD  . GLU   B 28  ? 0.2951 0.2555 0.3503 -0.0184 -0.0362 0.0055  34  GLU   C CD  
1310 O  OE1 . GLU   B 28  ? 0.3271 0.2842 0.3803 -0.0225 -0.0366 0.0080  34  GLU   C OE1 
1311 O  OE2 . GLU   B 28  ? 0.2661 0.2244 0.3203 -0.0141 -0.0381 0.0054  34  GLU   C OE2 
1312 N  N   . ASP   B 29  ? 0.2080 0.1768 0.2578 -0.0125 -0.0337 0.0053  35  ASP   C N   
1313 C  CA  . ASP   B 29  ? 0.2043 0.1700 0.2514 -0.0114 -0.0361 0.0083  35  ASP   C CA  
1314 C  C   . ASP   B 29  ? 0.1998 0.1643 0.2494 -0.0062 -0.0377 0.0069  35  ASP   C C   
1315 O  O   . ASP   B 29  ? 0.1985 0.1660 0.2485 -0.0039 -0.0367 0.0052  35  ASP   C O   
1316 C  CB  . ASP   B 29  ? 0.2157 0.1842 0.2593 -0.0129 -0.0352 0.0098  35  ASP   C CB  
1317 C  CG  . ASP   B 29  ? 0.2842 0.2500 0.3259 -0.0123 -0.0384 0.0135  35  ASP   C CG  
1318 O  OD1 . ASP   B 29  ? 0.3131 0.2761 0.3579 -0.0089 -0.0407 0.0140  35  ASP   C OD1 
1319 O  OD2 . ASP   B 29  ? 0.2855 0.2520 0.3230 -0.0153 -0.0386 0.0158  35  ASP   C OD2 
1320 N  N   . SER   B 30  ? 0.1950 0.1544 0.2458 -0.0048 -0.0399 0.0075  36  SER   C N   
1321 C  CA  A SER   B 30  ? 0.2023 0.1599 0.2550 -0.0003 -0.0407 0.0056  36  SER   C CA  
1322 C  CA  B SER   B 30  ? 0.1973 0.1550 0.2500 -0.0002 -0.0407 0.0055  36  SER   C CA  
1323 C  C   . SER   B 30  ? 0.2096 0.1697 0.2629 0.0024  -0.0407 0.0065  36  SER   C C   
1324 O  O   . SER   B 30  ? 0.2169 0.1785 0.2711 0.0054  -0.0396 0.0042  36  SER   C O   
1325 C  CB  A SER   B 30  ? 0.2371 0.1882 0.2910 0.0005  -0.0430 0.0059  36  SER   C CB  
1326 C  CB  B SER   B 30  ? 0.2184 0.1697 0.2723 0.0008  -0.0429 0.0056  36  SER   C CB  
1327 O  OG  A SER   B 30  ? 0.2789 0.2278 0.3343 0.0049  -0.0433 0.0038  36  SER   C OG  
1328 O  OG  B SER   B 30  ? 0.2372 0.1856 0.2914 0.0003  -0.0451 0.0092  36  SER   C OG  
1329 N  N   . SER   B 31  ? 0.2003 0.1608 0.2530 0.0008  -0.0420 0.0099  37  SER   C N   
1330 C  CA  . SER   B 31  ? 0.2029 0.1662 0.2574 0.0030  -0.0426 0.0111  37  SER   C CA  
1331 C  C   . SER   B 31  ? 0.2033 0.1722 0.2565 0.0029  -0.0401 0.0095  37  SER   C C   
1332 O  O   . SER   B 31  ? 0.2190 0.1909 0.2745 0.0052  -0.0399 0.0094  37  SER   C O   
1333 C  CB  . SER   B 31  ? 0.2480 0.2100 0.3018 0.0009  -0.0456 0.0155  37  SER   C CB  
1334 O  OG  . SER   B 31  ? 0.2961 0.2604 0.3448 -0.0036 -0.0447 0.0170  37  SER   C OG  
1335 N  N   . ARG   B 32  ? 0.1666 0.1370 0.2169 0.0004  -0.0382 0.0082  38  ARG   C N   
1336 C  CA  . ARG   B 32  ? 0.1619 0.1366 0.2110 0.0002  -0.0362 0.0067  38  ARG   C CA  
1337 C  C   . ARG   B 32  ? 0.1721 0.1469 0.2217 0.0020  -0.0348 0.0033  38  ARG   C C   
1338 O  O   . ARG   B 32  ? 0.1733 0.1506 0.2220 0.0022  -0.0336 0.0020  38  ARG   C O   
1339 C  CB  . ARG   B 32  ? 0.1860 0.1623 0.2320 -0.0039 -0.0350 0.0072  38  ARG   C CB  
1340 C  CG  . ARG   B 32  ? 0.1927 0.1687 0.2360 -0.0065 -0.0366 0.0108  38  ARG   C CG  
1341 C  CD  . ARG   B 32  ? 0.1918 0.1687 0.2305 -0.0111 -0.0347 0.0108  38  ARG   C CD  
1342 N  NE  . ARG   B 32  ? 0.1861 0.1664 0.2242 -0.0110 -0.0325 0.0084  38  ARG   C NE  
1343 C  CZ  . ARG   B 32  ? 0.2059 0.1874 0.2397 -0.0144 -0.0311 0.0084  38  ARG   C CZ  
1344 N  NH1 . ARG   B 32  ? 0.2178 0.1973 0.2465 -0.0186 -0.0316 0.0107  38  ARG   C NH1 
1345 N  NH2 . ARG   B 32  ? 0.2126 0.1963 0.2462 -0.0138 -0.0295 0.0062  38  ARG   C NH2 
1346 N  N   . ASP   B 33  ? 0.1739 0.1453 0.2245 0.0029  -0.0355 0.0020  39  ASP   C N   
1347 C  CA  . ASP   B 33  ? 0.1630 0.1335 0.2133 0.0039  -0.0352 -0.0009 39  ASP   C CA  
1348 C  C   . ASP   B 33  ? 0.1700 0.1431 0.2208 0.0017  -0.0344 -0.0018 39  ASP   C C   
1349 O  O   . ASP   B 33  ? 0.1772 0.1508 0.2277 0.0026  -0.0344 -0.0036 39  ASP   C O   
1350 C  CB  . ASP   B 33  ? 0.1809 0.1517 0.2298 0.0065  -0.0346 -0.0024 39  ASP   C CB  
1351 C  CG  . ASP   B 33  ? 0.1905 0.1590 0.2375 0.0071  -0.0352 -0.0050 39  ASP   C CG  
1352 O  OD1 . ASP   B 33  ? 0.1979 0.1631 0.2455 0.0067  -0.0366 -0.0059 39  ASP   C OD1 
1353 O  OD2 . ASP   B 33  ? 0.1822 0.1517 0.2268 0.0075  -0.0347 -0.0058 39  ASP   C OD2 
1354 N  N   . LEU   B 34  ? 0.1628 0.1370 0.2142 -0.0012 -0.0337 -0.0007 40  LEU   C N   
1355 C  CA  . LEU   B 34  ? 0.1622 0.1393 0.2155 -0.0031 -0.0322 -0.0023 40  LEU   C CA  
1356 C  C   . LEU   B 34  ? 0.1738 0.1505 0.2301 -0.0055 -0.0320 -0.0029 40  LEU   C C   
1357 O  O   . LEU   B 34  ? 0.1873 0.1618 0.2425 -0.0073 -0.0324 -0.0010 40  LEU   C O   
1358 C  CB  . LEU   B 34  ? 0.1635 0.1433 0.2147 -0.0053 -0.0302 -0.0015 40  LEU   C CB  
1359 C  CG  . LEU   B 34  ? 0.1847 0.1658 0.2337 -0.0038 -0.0301 -0.0013 40  LEU   C CG  
1360 C  CD1 . LEU   B 34  ? 0.1868 0.1699 0.2331 -0.0068 -0.0283 -0.0006 40  LEU   C CD1 
1361 C  CD2 . LEU   B 34  ? 0.1991 0.1807 0.2499 -0.0019 -0.0303 -0.0037 40  LEU   C CD2 
1362 N  N   . LEU   B 35  ? 0.1593 0.1384 0.2198 -0.0058 -0.0314 -0.0053 41  LEU   C N   
1363 C  CA  . LEU   B 35  ? 0.1640 0.1443 0.2290 -0.0085 -0.0306 -0.0061 41  LEU   C CA  
1364 C  C   . LEU   B 35  ? 0.1691 0.1542 0.2389 -0.0092 -0.0283 -0.0087 41  LEU   C C   
1365 O  O   . LEU   B 35  ? 0.1785 0.1643 0.2496 -0.0066 -0.0292 -0.0101 41  LEU   C O   
1366 C  CB  . LEU   B 35  ? 0.1706 0.1482 0.2383 -0.0074 -0.0337 -0.0070 41  LEU   C CB  
1367 C  CG  . LEU   B 35  ? 0.1839 0.1632 0.2574 -0.0105 -0.0332 -0.0078 41  LEU   C CG  
1368 C  CD1 . LEU   B 35  ? 0.1967 0.1710 0.2696 -0.0106 -0.0364 -0.0072 41  LEU   C CD1 
1369 C  CD2 . LEU   B 35  ? 0.2053 0.1890 0.2867 -0.0100 -0.0333 -0.0107 41  LEU   C CD2 
1370 N  N   . VAL   B 36  ? 0.1590 0.1470 0.2313 -0.0128 -0.0251 -0.0093 42  VAL   C N   
1371 C  CA  . VAL   B 36  ? 0.1624 0.1554 0.2407 -0.0136 -0.0219 -0.0124 42  VAL   C CA  
1372 C  C   . VAL   B 36  ? 0.1827 0.1786 0.2691 -0.0158 -0.0211 -0.0140 42  VAL   C C   
1373 O  O   . VAL   B 36  ? 0.1783 0.1734 0.2629 -0.0193 -0.0200 -0.0124 42  VAL   C O   
1374 C  CB  . VAL   B 36  ? 0.1700 0.1644 0.2433 -0.0166 -0.0176 -0.0124 42  VAL   C CB  
1375 C  CG1 . VAL   B 36  ? 0.1905 0.1900 0.2706 -0.0175 -0.0134 -0.0165 42  VAL   C CG1 
1376 C  CG2 . VAL   B 36  ? 0.1769 0.1687 0.2431 -0.0145 -0.0191 -0.0107 42  VAL   C CG2 
1377 N  N   . SER   B 37  ? 0.1868 0.1861 0.2825 -0.0139 -0.0219 -0.0169 43  SER   C N   
1378 C  CA  . SER   B 37  ? 0.1816 0.1851 0.2875 -0.0159 -0.0212 -0.0188 43  SER   C CA  
1379 C  C   . SER   B 37  ? 0.1874 0.1974 0.3025 -0.0161 -0.0169 -0.0228 43  SER   C C   
1380 O  O   . SER   B 37  ? 0.1910 0.2011 0.3047 -0.0139 -0.0159 -0.0241 43  SER   C O   
1381 C  CB  . SER   B 37  ? 0.1890 0.1908 0.2996 -0.0133 -0.0270 -0.0188 43  SER   C CB  
1382 O  OG  . SER   B 37  ? 0.2159 0.2170 0.3285 -0.0092 -0.0301 -0.0199 43  SER   C OG  
1383 N  N   . SER   B 38  ? 0.1944 0.2098 0.3191 -0.0190 -0.0142 -0.0248 44  SER   C N   
1384 C  CA  . SER   B 38  ? 0.2215 0.2438 0.3565 -0.0192 -0.0093 -0.0293 44  SER   C CA  
1385 C  C   . SER   B 38  ? 0.2445 0.2699 0.3933 -0.0150 -0.0135 -0.0318 44  SER   C C   
1386 O  O   . SER   B 38  ? 0.2587 0.2825 0.4108 -0.0137 -0.0193 -0.0303 44  SER   C O   
1387 C  CB  . SER   B 38  ? 0.2502 0.2777 0.3894 -0.0248 -0.0032 -0.0307 44  SER   C CB  
1388 O  OG  . SER   B 38  ? 0.2953 0.3239 0.4410 -0.0262 -0.0064 -0.0296 44  SER   C OG  
1389 N  N   . THR   B 39  ? 0.2601 0.2890 0.4163 -0.0127 -0.0109 -0.0355 45  THR   C N   
1390 C  CA  . THR   B 39  ? 0.2904 0.3219 0.4606 -0.0085 -0.0153 -0.0379 45  THR   C CA  
1391 C  C   . THR   B 39  ? 0.3165 0.3569 0.5027 -0.0092 -0.0096 -0.0432 45  THR   C C   
1392 O  O   . THR   B 39  ? 0.3210 0.3644 0.5047 -0.0125 -0.0016 -0.0454 45  THR   C O   
1393 C  CB  . THR   B 39  ? 0.3126 0.3390 0.4777 -0.0041 -0.0186 -0.0375 45  THR   C CB  
1394 O  OG1 . THR   B 39  ? 0.3347 0.3627 0.4984 -0.0046 -0.0121 -0.0405 45  THR   C OG1 
1395 C  CG2 . THR   B 39  ? 0.3172 0.3356 0.4663 -0.0036 -0.0226 -0.0329 45  THR   C CG2 
1396 N  N   . THR   B 40  ? 0.3355 0.3801 0.5382 -0.0061 -0.0135 -0.0453 46  THR   C N   
1397 C  CA  . THR   B 40  ? 0.3566 0.4103 0.5772 -0.0059 -0.0082 -0.0510 46  THR   C CA  
1398 C  C   . THR   B 40  ? 0.3794 0.4317 0.6031 -0.0015 -0.0075 -0.0541 46  THR   C C   
1399 O  O   . THR   B 40  ? 0.3983 0.4560 0.6295 -0.0021 0.0002  -0.0593 46  THR   C O   
1400 C  CB  . THR   B 40  ? 0.3718 0.4316 0.6109 -0.0050 -0.0130 -0.0518 46  THR   C CB  
1401 O  OG1 . THR   B 40  ? 0.4017 0.4555 0.6403 -0.0008 -0.0235 -0.0488 46  THR   C OG1 
1402 C  CG2 . THR   B 40  ? 0.3730 0.4354 0.6109 -0.0104 -0.0117 -0.0498 46  THR   C CG2 
1403 N  N   . ALA   B 41  ? 0.3773 0.4222 0.5951 0.0026  -0.0151 -0.0513 47  ALA   C N   
1404 C  CA  . ALA   B 41  ? 0.3782 0.4204 0.5984 0.0068  -0.0154 -0.0538 47  ALA   C CA  
1405 C  C   . ALA   B 41  ? 0.3874 0.4244 0.5905 0.0052  -0.0105 -0.0534 47  ALA   C C   
1406 O  O   . ALA   B 41  ? 0.3980 0.4309 0.5852 0.0023  -0.0104 -0.0493 47  ALA   C O   
1407 C  CB  . ALA   B 41  ? 0.3832 0.4194 0.6047 0.0113  -0.0260 -0.0508 47  ALA   C CB  
1408 N  N   . GLN   B 42  ? 0.3821 0.4190 0.5888 0.0072  -0.0070 -0.0575 48  GLN   C N   
1409 C  CA  . GLN   B 42  ? 0.3898 0.4217 0.5810 0.0056  -0.0026 -0.0575 48  GLN   C CA  
1410 C  C   . GLN   B 42  ? 0.3714 0.3943 0.5512 0.0081  -0.0099 -0.0530 48  GLN   C C   
1411 O  O   . GLN   B 42  ? 0.3810 0.4012 0.5681 0.0124  -0.0160 -0.0530 48  GLN   C O   
1412 C  CB  . GLN   B 42  ? 0.4378 0.4725 0.6373 0.0066  0.0041  -0.0643 48  GLN   C CB  
1413 C  CG  . GLN   B 42  ? 0.5374 0.5695 0.7214 0.0025  0.0114  -0.0654 48  GLN   C CG  
1414 C  CD  . GLN   B 42  ? 0.6451 0.6827 0.8259 -0.0035 0.0191  -0.0664 48  GLN   C CD  
1415 O  OE1 . GLN   B 42  ? 0.6766 0.7218 0.8711 -0.0043 0.0220  -0.0691 48  GLN   C OE1 
1416 N  NE2 . GLN   B 42  ? 0.6679 0.7017 0.8308 -0.0080 0.0223  -0.0642 48  GLN   C NE2 
1417 N  N   . GLY   B 43  ? 0.3361 0.3545 0.4985 0.0053  -0.0094 -0.0492 49  GLY   C N   
1418 C  CA  . GLY   B 43  ? 0.3216 0.3322 0.4725 0.0070  -0.0152 -0.0450 49  GLY   C CA  
1419 C  C   . GLY   B 43  ? 0.2981 0.3052 0.4428 0.0070  -0.0120 -0.0471 49  GLY   C C   
1420 O  O   . GLY   B 43  ? 0.3021 0.3116 0.4441 0.0041  -0.0047 -0.0502 49  GLY   C O   
1421 N  N   . CYS   B 44  ? 0.2776 0.2786 0.4193 0.0098  -0.0171 -0.0455 50  CYS   C N   
1422 C  CA  . CYS   B 44  ? 0.2762 0.2732 0.4131 0.0099  -0.0147 -0.0476 50  CYS   C CA  
1423 C  C   . CYS   B 44  ? 0.2649 0.2560 0.3855 0.0082  -0.0167 -0.0433 50  CYS   C C   
1424 O  O   . CYS   B 44  ? 0.2751 0.2618 0.3921 0.0086  -0.0166 -0.0444 50  CYS   C O   
1425 C  CB  . CYS   B 44  ? 0.3056 0.3003 0.4546 0.0144  -0.0181 -0.0506 50  CYS   C CB  
1426 S  SG  . CYS   B 44  ? 0.3788 0.3815 0.5499 0.0167  -0.0150 -0.0568 50  CYS   C SG  
1427 N  N   . ASP   B 45  ? 0.2322 0.2233 0.3438 0.0063  -0.0185 -0.0385 51  ASP   C N   
1428 C  CA  . ASP   B 45  ? 0.2368 0.2233 0.3348 0.0048  -0.0201 -0.0347 51  ASP   C CA  
1429 C  C   . ASP   B 45  ? 0.2512 0.2384 0.3412 0.0011  -0.0144 -0.0361 51  ASP   C C   
1430 O  O   . ASP   B 45  ? 0.2662 0.2575 0.3570 -0.0014 -0.0097 -0.0378 51  ASP   C O   
1431 C  CB  . ASP   B 45  ? 0.2516 0.2378 0.3431 0.0041  -0.0234 -0.0297 51  ASP   C CB  
1432 C  CG  . ASP   B 45  ? 0.3350 0.3186 0.4301 0.0070  -0.0297 -0.0277 51  ASP   C CG  
1433 O  OD1 . ASP   B 45  ? 0.3492 0.3295 0.4489 0.0094  -0.0329 -0.0286 51  ASP   C OD1 
1434 O  OD2 . ASP   B 45  ? 0.3388 0.3229 0.4318 0.0067  -0.0317 -0.0251 51  ASP   C OD2 
1435 N  N   . THR   B 46  ? 0.2375 0.2204 0.3197 0.0003  -0.0150 -0.0353 52  THR   C N   
1436 C  CA  . THR   B 46  ? 0.2553 0.2380 0.3284 -0.0037 -0.0107 -0.0361 52  THR   C CA  
1437 C  C   . THR   B 46  ? 0.2375 0.2199 0.3007 -0.0058 -0.0128 -0.0307 52  THR   C C   
1438 O  O   . THR   B 46  ? 0.2444 0.2243 0.3051 -0.0043 -0.0171 -0.0275 52  THR   C O   
1439 C  CB  . THR   B 46  ? 0.3211 0.2989 0.3914 -0.0036 -0.0108 -0.0382 52  THR   C CB  
1440 O  OG1 . THR   B 46  ? 0.3688 0.3469 0.4496 -0.0013 -0.0084 -0.0438 52  THR   C OG1 
1441 C  CG2 . THR   B 46  ? 0.3404 0.3171 0.3994 -0.0082 -0.0076 -0.0383 52  THR   C CG2 
1442 N  N   . ILE   B 47  ? 0.2209 0.2058 0.2787 -0.0093 -0.0098 -0.0299 53  ILE   C N   
1443 C  CA  . ILE   B 47  ? 0.2107 0.1953 0.2605 -0.0110 -0.0121 -0.0249 53  ILE   C CA  
1444 C  C   . ILE   B 47  ? 0.2104 0.1925 0.2514 -0.0139 -0.0118 -0.0243 53  ILE   C C   
1445 O  O   . ILE   B 47  ? 0.2144 0.1959 0.2521 -0.0167 -0.0081 -0.0274 53  ILE   C O   
1446 C  CB  . ILE   B 47  ? 0.2288 0.2163 0.2768 -0.0135 -0.0101 -0.0235 53  ILE   C CB  
1447 C  CG1 . ILE   B 47  ? 0.2567 0.2471 0.3141 -0.0115 -0.0099 -0.0247 53  ILE   C CG1 
1448 C  CG2 . ILE   B 47  ? 0.2351 0.2220 0.2765 -0.0145 -0.0133 -0.0182 53  ILE   C CG2 
1449 C  CD1 . ILE   B 47  ? 0.2742 0.2635 0.3350 -0.0077 -0.0148 -0.0222 53  ILE   C CD1 
1450 N  N   . ALA   B 48  ? 0.1920 0.1728 0.2290 -0.0135 -0.0155 -0.0204 54  ALA   C N   
1451 C  CA  . ALA   B 48  ? 0.1874 0.1663 0.2166 -0.0165 -0.0160 -0.0193 54  ALA   C CA  
1452 C  C   . ALA   B 48  ? 0.1792 0.1595 0.2017 -0.0206 -0.0149 -0.0175 54  ALA   C C   
1453 O  O   . ALA   B 48  ? 0.1777 0.1601 0.2011 -0.0203 -0.0156 -0.0149 54  ALA   C O   
1454 C  CB  . ALA   B 48  ? 0.1794 0.1578 0.2075 -0.0152 -0.0200 -0.0154 54  ALA   C CB  
1455 N  N   . ARG   B 49  ? 0.1760 0.1542 0.1911 -0.0245 -0.0137 -0.0185 55  ARG   C N   
1456 C  CA  . ARG   B 49  ? 0.1859 0.1643 0.1929 -0.0292 -0.0134 -0.0164 55  ARG   C CA  
1457 C  C   . ARG   B 49  ? 0.1916 0.1680 0.1925 -0.0315 -0.0165 -0.0143 55  ARG   C C   
1458 O  O   . ARG   B 49  ? 0.2030 0.1764 0.1986 -0.0343 -0.0151 -0.0171 55  ARG   C O   
1459 C  CB  . ARG   B 49  ? 0.1974 0.1748 0.2005 -0.0327 -0.0082 -0.0206 55  ARG   C CB  
1460 C  CG  . ARG   B 49  ? 0.2065 0.1865 0.2177 -0.0303 -0.0047 -0.0233 55  ARG   C CG  
1461 C  CD  . ARG   B 49  ? 0.2225 0.2050 0.2353 -0.0300 -0.0064 -0.0192 55  ARG   C CD  
1462 N  NE  . ARG   B 49  ? 0.2484 0.2336 0.2690 -0.0286 -0.0030 -0.0221 55  ARG   C NE  
1463 C  CZ  . ARG   B 49  ? 0.2613 0.2485 0.2868 -0.0268 -0.0045 -0.0197 55  ARG   C CZ  
1464 N  NH1 . ARG   B 49  ? 0.2265 0.2131 0.2499 -0.0260 -0.0090 -0.0148 55  ARG   C NH1 
1465 N  NH2 . ARG   B 49  ? 0.2390 0.2289 0.2721 -0.0259 -0.0015 -0.0226 55  ARG   C NH2 
1466 N  N   . CYS   B 50  ? 0.1824 0.1608 0.1851 -0.0301 -0.0207 -0.0097 56  CYS   C N   
1467 C  CA  . CYS   B 50  ? 0.1933 0.1711 0.1935 -0.0315 -0.0241 -0.0075 56  CYS   C CA  
1468 C  C   . CYS   B 50  ? 0.1996 0.1810 0.2027 -0.0304 -0.0281 -0.0023 56  CYS   C C   
1469 O  O   . CYS   B 50  ? 0.1920 0.1754 0.1988 -0.0281 -0.0283 -0.0007 56  CYS   C O   
1470 C  CB  . CYS   B 50  ? 0.1921 0.1684 0.1964 -0.0288 -0.0238 -0.0098 56  CYS   C CB  
1471 S  SG  . CYS   B 50  ? 0.1995 0.1784 0.2128 -0.0232 -0.0250 -0.0081 56  CYS   C SG  
1472 N  N   . ASP   B 51  ? 0.1988 0.1809 0.2011 -0.0317 -0.0311 -0.0001 57  ASP   C N   
1473 C  CA  . ASP   B 51  ? 0.2072 0.1935 0.2144 -0.0303 -0.0345 0.0041  57  ASP   C CA  
1474 C  C   . ASP   B 51  ? 0.2146 0.2023 0.2266 -0.0282 -0.0349 0.0042  57  ASP   C C   
1475 O  O   . ASP   B 51  ? 0.2182 0.2094 0.2333 -0.0285 -0.0374 0.0071  57  ASP   C O   
1476 C  CB  . ASP   B 51  ? 0.2342 0.2213 0.2375 -0.0343 -0.0384 0.0075  57  ASP   C CB  
1477 C  CG  . ASP   B 51  ? 0.3203 0.3054 0.3183 -0.0384 -0.0397 0.0068  57  ASP   C CG  
1478 O  OD1 . ASP   B 51  ? 0.3200 0.3026 0.3174 -0.0380 -0.0375 0.0035  57  ASP   C OD1 
1479 O  OD2 . ASP   B 51  ? 0.3890 0.3745 0.3834 -0.0421 -0.0435 0.0096  57  ASP   C OD2 
1480 N  N   . CYS   B 52  ? 0.1907 0.1758 0.2037 -0.0260 -0.0325 0.0011  58  CYS   C N   
1481 C  CA  . CYS   B 52  ? 0.1803 0.1657 0.1964 -0.0245 -0.0329 0.0015  58  CYS   C CA  
1482 C  C   . CYS   B 52  ? 0.1750 0.1649 0.1966 -0.0220 -0.0337 0.0042  58  CYS   C C   
1483 O  O   . CYS   B 52  ? 0.1698 0.1612 0.1939 -0.0197 -0.0332 0.0046  58  CYS   C O   
1484 C  CB  . CYS   B 52  ? 0.1838 0.1652 0.2007 -0.0222 -0.0311 -0.0017 58  CYS   C CB  
1485 S  SG  . CYS   B 52  ? 0.2121 0.1876 0.2243 -0.0247 -0.0302 -0.0055 58  CYS   C SG  
1486 N  N   . GLN   B 53  ? 0.1639 0.1557 0.1874 -0.0226 -0.0345 0.0057  59  GLN   C N   
1487 C  CA  . GLN   B 53  ? 0.1667 0.1627 0.1955 -0.0203 -0.0342 0.0074  59  GLN   C CA  
1488 C  C   . GLN   B 53  ? 0.1800 0.1742 0.2084 -0.0198 -0.0330 0.0068  59  GLN   C C   
1489 O  O   . GLN   B 53  ? 0.1766 0.1742 0.2081 -0.0192 -0.0323 0.0081  59  GLN   C O   
1490 C  CB  . GLN   B 53  ? 0.1791 0.1810 0.2121 -0.0218 -0.0361 0.0103  59  GLN   C CB  
1491 C  CG  . GLN   B 53  ? 0.1864 0.1903 0.2214 -0.0210 -0.0376 0.0118  59  GLN   C CG  
1492 C  CD  . GLN   B 53  ? 0.2213 0.2311 0.2620 -0.0222 -0.0403 0.0147  59  GLN   C CD  
1493 O  OE1 . GLN   B 53  ? 0.2207 0.2306 0.2591 -0.0256 -0.0434 0.0163  59  GLN   C OE1 
1494 N  NE2 . GLN   B 53  ? 0.1833 0.1979 0.2313 -0.0196 -0.0391 0.0153  59  GLN   C NE2 
1495 N  N   . THR   B 54  ? 0.1837 0.1721 0.2081 -0.0203 -0.0329 0.0048  60  THR   C N   
1496 C  CA  . THR   B 54  ? 0.1926 0.1776 0.2157 -0.0199 -0.0325 0.0046  60  THR   C CA  
1497 C  C   . THR   B 54  ? 0.1916 0.1713 0.2135 -0.0175 -0.0325 0.0020  60  THR   C C   
1498 O  O   . THR   B 54  ? 0.2011 0.1789 0.2225 -0.0174 -0.0323 0.0000  60  THR   C O   
1499 C  CB  . THR   B 54  ? 0.2676 0.2503 0.2879 -0.0234 -0.0335 0.0052  60  THR   C CB  
1500 O  OG1 . THR   B 54  ? 0.3121 0.2901 0.3295 -0.0247 -0.0344 0.0031  60  THR   C OG1 
1501 C  CG2 . THR   B 54  ? 0.2927 0.2814 0.3155 -0.0262 -0.0339 0.0076  60  THR   C CG2 
1502 N  N   . GLY   B 55  ? 0.1800 0.1572 0.2016 -0.0157 -0.0326 0.0022  61  GLY   C N   
1503 C  CA  . GLY   B 55  ? 0.1807 0.1533 0.2027 -0.0132 -0.0332 0.0001  61  GLY   C CA  
1504 C  C   . GLY   B 55  ? 0.1635 0.1329 0.1837 -0.0122 -0.0343 0.0010  61  GLY   C C   
1505 O  O   . GLY   B 55  ? 0.1904 0.1601 0.2078 -0.0140 -0.0341 0.0030  61  GLY   C O   
1506 N  N   . VAL   B 56  ? 0.1601 0.1262 0.1816 -0.0097 -0.0356 -0.0004 62  VAL   C N   
1507 C  CA  . VAL   B 56  ? 0.1718 0.1334 0.1905 -0.0090 -0.0376 0.0005  62  VAL   C CA  
1508 C  C   . VAL   B 56  ? 0.1756 0.1386 0.1971 -0.0062 -0.0377 -0.0005 62  VAL   C C   
1509 O  O   . VAL   B 56  ? 0.1808 0.1447 0.2070 -0.0044 -0.0376 -0.0026 62  VAL   C O   
1510 C  CB  . VAL   B 56  ? 0.1890 0.1434 0.2072 -0.0089 -0.0408 -0.0001 62  VAL   C CB  
1511 C  CG1 . VAL   B 56  ? 0.2140 0.1630 0.2290 -0.0083 -0.0440 0.0013  62  VAL   C CG1 
1512 C  CG2 . VAL   B 56  ? 0.2011 0.1531 0.2162 -0.0120 -0.0410 0.0010  62  VAL   C CG2 
1513 N  N   . TYR   B 57  ? 0.1914 0.1541 0.2096 -0.0060 -0.0377 0.0006  63  TYR   C N   
1514 C  CA  . TYR   B 57  ? 0.1805 0.1434 0.2008 -0.0036 -0.0384 -0.0004 63  TYR   C CA  
1515 C  C   . TYR   B 57  ? 0.1869 0.1437 0.2028 -0.0035 -0.0417 0.0002  63  TYR   C C   
1516 O  O   . TYR   B 57  ? 0.1920 0.1450 0.2017 -0.0057 -0.0426 0.0020  63  TYR   C O   
1517 C  CB  . TYR   B 57  ? 0.1824 0.1504 0.2032 -0.0031 -0.0355 -0.0004 63  TYR   C CB  
1518 C  CG  . TYR   B 57  ? 0.1993 0.1668 0.2146 -0.0043 -0.0341 0.0007  63  TYR   C CG  
1519 C  CD1 . TYR   B 57  ? 0.2048 0.1742 0.2180 -0.0067 -0.0322 0.0021  63  TYR   C CD1 
1520 C  CD2 . TYR   B 57  ? 0.1987 0.1641 0.2111 -0.0033 -0.0344 0.0001  63  TYR   C CD2 
1521 C  CE1 . TYR   B 57  ? 0.2259 0.1959 0.2347 -0.0080 -0.0299 0.0027  63  TYR   C CE1 
1522 C  CE2 . TYR   B 57  ? 0.2147 0.1798 0.2217 -0.0047 -0.0322 0.0005  63  TYR   C CE2 
1523 C  CZ  . TYR   B 57  ? 0.2348 0.2024 0.2401 -0.0071 -0.0297 0.0017  63  TYR   C CZ  
1524 O  OH  . TYR   B 57  ? 0.2470 0.2151 0.2476 -0.0086 -0.0266 0.0016  63  TYR   C OH  
1525 N  N   . TYR   B 58  ? 0.1838 0.1395 0.2026 -0.0015 -0.0438 -0.0010 64  TYR   C N   
1526 C  CA  . TYR   B 58  ? 0.1885 0.1383 0.2031 -0.0016 -0.0477 -0.0002 64  TYR   C CA  
1527 C  C   . TYR   B 58  ? 0.1973 0.1476 0.2066 -0.0020 -0.0461 -0.0001 64  TYR   C C   
1528 O  O   . TYR   B 58  ? 0.1880 0.1422 0.2011 -0.0005 -0.0442 -0.0015 64  TYR   C O   
1529 C  CB  . TYR   B 58  ? 0.2009 0.1493 0.2225 0.0008  -0.0515 -0.0017 64  TYR   C CB  
1530 C  CG  . TYR   B 58  ? 0.2245 0.1662 0.2415 0.0004  -0.0567 -0.0004 64  TYR   C CG  
1531 C  CD1 . TYR   B 58  ? 0.2390 0.1739 0.2503 -0.0013 -0.0604 0.0017  64  TYR   C CD1 
1532 C  CD2 . TYR   B 58  ? 0.2496 0.1911 0.2669 0.0012  -0.0584 -0.0011 64  TYR   C CD2 
1533 C  CE1 . TYR   B 58  ? 0.2581 0.1860 0.2637 -0.0022 -0.0660 0.0034  64  TYR   C CE1 
1534 C  CE2 . TYR   B 58  ? 0.2585 0.1934 0.2703 0.0003  -0.0638 0.0002  64  TYR   C CE2 
1535 C  CZ  . TYR   B 58  ? 0.2771 0.2051 0.2828 -0.0014 -0.0677 0.0025  64  TYR   C CZ  
1536 O  OH  . TYR   B 58  ? 0.3207 0.2413 0.3198 -0.0028 -0.0738 0.0043  64  TYR   C OH  
1537 N  N   . CYS   B 59  ? 0.2074 0.1528 0.2075 -0.0043 -0.0471 0.0015  65  CYS   C N   
1538 C  CA  . CYS   B 59  ? 0.2059 0.1507 0.1994 -0.0053 -0.0452 0.0011  65  CYS   C CA  
1539 C  C   . CYS   B 59  ? 0.2339 0.1711 0.2212 -0.0060 -0.0504 0.0016  65  CYS   C C   
1540 O  O   . CYS   B 59  ? 0.2597 0.1906 0.2389 -0.0086 -0.0532 0.0036  65  CYS   C O   
1541 C  CB  . CYS   B 59  ? 0.2100 0.1556 0.1970 -0.0082 -0.0412 0.0022  65  CYS   C CB  
1542 S  SG  . CYS   B 59  ? 0.2657 0.2098 0.2434 -0.0098 -0.0379 0.0011  65  CYS   C SG  
1543 N  N   . SER   B 60  ? 0.2323 0.1698 0.2231 -0.0040 -0.0521 0.0000  66  SER   C N   
1544 C  CA  . SER   B 60  ? 0.2719 0.2023 0.2577 -0.0048 -0.0580 0.0005  66  SER   C CA  
1545 C  C   . SER   B 60  ? 0.2804 0.2049 0.2522 -0.0081 -0.0577 0.0012  66  SER   C C   
1546 O  O   . SER   B 60  ? 0.2916 0.2085 0.2560 -0.0102 -0.0632 0.0031  66  SER   C O   
1547 C  CB  . SER   B 60  ? 0.3332 0.2654 0.3260 -0.0025 -0.0599 -0.0014 66  SER   C CB  
1548 O  OG  . SER   B 60  ? 0.4358 0.3711 0.4274 -0.0021 -0.0554 -0.0032 66  SER   C OG  
1549 N  N   . SER   B 61  ? 0.2682 0.1959 0.2360 -0.0089 -0.0513 -0.0002 67  SER   C N   
1550 C  CA  . SER   B 61  ? 0.2800 0.2024 0.2339 -0.0125 -0.0497 -0.0001 67  SER   C CA  
1551 C  C   . SER   B 61  ? 0.2838 0.2021 0.2289 -0.0164 -0.0499 0.0027  67  SER   C C   
1552 O  O   . SER   B 61  ? 0.2914 0.2040 0.2231 -0.0204 -0.0491 0.0031  67  SER   C O   
1553 C  CB  . SER   B 61  ? 0.2767 0.2042 0.2305 -0.0119 -0.0424 -0.0030 67  SER   C CB  
1554 O  OG  . SER   B 61  ? 0.2772 0.2120 0.2376 -0.0111 -0.0373 -0.0029 67  SER   C OG  
1555 N  N   . ARG   B 62  ? 0.2508 0.1711 0.2024 -0.0158 -0.0511 0.0045  68  ARG   C N   
1556 C  CA  . ARG   B 62  ? 0.2518 0.1671 0.1955 -0.0196 -0.0525 0.0076  68  ARG   C CA  
1557 C  C   . ARG   B 62  ? 0.2741 0.1839 0.2217 -0.0187 -0.0605 0.0099  68  ARG   C C   
1558 O  O   . ARG   B 62  ? 0.3086 0.2129 0.2505 -0.0216 -0.0631 0.0128  68  ARG   C O   
1559 C  CB  . ARG   B 62  ? 0.2761 0.1983 0.2239 -0.0203 -0.0464 0.0077  68  ARG   C CB  
1560 C  CG  . ARG   B 62  ? 0.2858 0.2134 0.2307 -0.0214 -0.0386 0.0055  68  ARG   C CG  
1561 C  CD  . ARG   B 62  ? 0.3194 0.2406 0.2490 -0.0268 -0.0372 0.0066  68  ARG   C CD  
1562 N  NE  . ARG   B 62  ? 0.3379 0.2647 0.2655 -0.0279 -0.0291 0.0039  68  ARG   C NE  
1563 C  CZ  . ARG   B 62  ? 0.3902 0.3165 0.3144 -0.0270 -0.0266 0.0008  68  ARG   C CZ  
1564 N  NH1 . ARG   B 62  ? 0.3961 0.3168 0.3180 -0.0254 -0.0320 0.0003  68  ARG   C NH1 
1565 N  NH2 . ARG   B 62  ? 0.4001 0.3315 0.3236 -0.0279 -0.0187 -0.0020 68  ARG   C NH2 
1566 N  N   . ARG   B 63  ? 0.2731 0.1847 0.2312 -0.0146 -0.0642 0.0086  69  ARG   C N   
1567 C  CA  . ARG   B 63  ? 0.2924 0.2008 0.2581 -0.0126 -0.0709 0.0098  69  ARG   C CA  
1568 C  C   . ARG   B 63  ? 0.3077 0.2173 0.2769 -0.0129 -0.0694 0.0108  69  ARG   C C   
1569 O  O   . ARG   B 63  ? 0.3434 0.2461 0.3107 -0.0140 -0.0746 0.0132  69  ARG   C O   
1570 C  CB  . ARG   B 63  ? 0.3423 0.2402 0.2999 -0.0147 -0.0794 0.0124  69  ARG   C CB  
1571 C  CG  . ARG   B 63  ? 0.4261 0.3218 0.3793 -0.0149 -0.0818 0.0114  69  ARG   C CG  
1572 C  CD  . ARG   B 63  ? 0.5277 0.4259 0.4934 -0.0110 -0.0864 0.0098  69  ARG   C CD  
1573 N  NE  . ARG   B 63  ? 0.6066 0.5025 0.5661 -0.0121 -0.0880 0.0088  69  ARG   C NE  
1574 C  CZ  . ARG   B 63  ? 0.6556 0.5575 0.6187 -0.0106 -0.0832 0.0057  69  ARG   C CZ  
1575 N  NH1 . ARG   B 63  ? 0.6491 0.5599 0.6225 -0.0078 -0.0769 0.0036  69  ARG   C NH1 
1576 N  NH2 . ARG   B 63  ? 0.6774 0.5758 0.6341 -0.0119 -0.0852 0.0047  69  ARG   C NH2 
1577 N  N   . LYS   B 64  ? 0.2825 0.2002 0.2560 -0.0123 -0.0625 0.0092  70  LYS   C N   
1578 C  CA  . LYS   B 64  ? 0.2802 0.1988 0.2556 -0.0134 -0.0608 0.0102  70  LYS   C CA  
1579 C  C   . LYS   B 64  ? 0.2466 0.1744 0.2321 -0.0110 -0.0558 0.0078  70  LYS   C C   
1580 O  O   . LYS   B 64  ? 0.2361 0.1699 0.2243 -0.0095 -0.0521 0.0060  70  LYS   C O   
1581 C  CB  . LYS   B 64  ? 0.3353 0.2526 0.2995 -0.0182 -0.0570 0.0122  70  LYS   C CB  
1582 C  CG  . LYS   B 64  ? 0.4802 0.3870 0.4330 -0.0223 -0.0619 0.0157  70  LYS   C CG  
1583 C  CD  . LYS   B 64  ? 0.5937 0.5008 0.5371 -0.0274 -0.0569 0.0173  70  LYS   C CD  
1584 C  CE  . LYS   B 64  ? 0.6740 0.5700 0.6056 -0.0322 -0.0618 0.0213  70  LYS   C CE  
1585 N  NZ  . LYS   B 64  ? 0.7046 0.5971 0.6215 -0.0373 -0.0593 0.0225  70  LYS   C NZ  
1586 N  N   . HIS   B 65  ? 0.2359 0.1640 0.2254 -0.0110 -0.0557 0.0080  71  HIS   C N   
1587 C  CA  . HIS   B 65  ? 0.2206 0.1566 0.2175 -0.0098 -0.0512 0.0061  71  HIS   C CA  
1588 C  C   . HIS   B 65  ? 0.2442 0.1828 0.2364 -0.0132 -0.0471 0.0075  71  HIS   C C   
1589 O  O   . HIS   B 65  ? 0.2757 0.2090 0.2610 -0.0165 -0.0485 0.0099  71  HIS   C O   
1590 C  CB  . HIS   B 65  ? 0.2277 0.1622 0.2318 -0.0081 -0.0533 0.0049  71  HIS   C CB  
1591 C  CG  . HIS   B 65  ? 0.2445 0.1781 0.2561 -0.0046 -0.0566 0.0030  71  HIS   C CG  
1592 N  ND1 . HIS   B 65  ? 0.2705 0.2104 0.2905 -0.0020 -0.0540 0.0002  71  HIS   C ND1 
1593 C  CD2 . HIS   B 65  ? 0.2455 0.1725 0.2577 -0.0035 -0.0625 0.0037  71  HIS   C CD2 
1594 C  CE1 . HIS   B 65  ? 0.2600 0.1979 0.2861 0.0004  -0.0578 -0.0010 71  HIS   C CE1 
1595 N  NE2 . HIS   B 65  ? 0.2731 0.2034 0.2952 -0.0002 -0.0632 0.0011  71  HIS   C NE2 
1596 N  N   . TYR   B 66  ? 0.2018 0.1487 0.1985 -0.0125 -0.0425 0.0063  72  TYR   C N   
1597 C  CA  . TYR   B 66  ? 0.1990 0.1499 0.1936 -0.0155 -0.0387 0.0075  72  TYR   C CA  
1598 C  C   . TYR   B 66  ? 0.1933 0.1499 0.1949 -0.0149 -0.0370 0.0065  72  TYR   C C   
1599 O  O   . TYR   B 66  ? 0.1996 0.1602 0.2069 -0.0122 -0.0362 0.0048  72  TYR   C O   
1600 C  CB  . TYR   B 66  ? 0.2074 0.1633 0.2004 -0.0158 -0.0345 0.0071  72  TYR   C CB  
1601 C  CG  . TYR   B 66  ? 0.2473 0.1978 0.2310 -0.0176 -0.0350 0.0079  72  TYR   C CG  
1602 C  CD1 . TYR   B 66  ? 0.2682 0.2150 0.2438 -0.0221 -0.0345 0.0101  72  TYR   C CD1 
1603 C  CD2 . TYR   B 66  ? 0.2619 0.2107 0.2441 -0.0155 -0.0358 0.0065  72  TYR   C CD2 
1604 C  CE1 . TYR   B 66  ? 0.2935 0.2346 0.2589 -0.0245 -0.0349 0.0109  72  TYR   C CE1 
1605 C  CE2 . TYR   B 66  ? 0.2855 0.2286 0.2578 -0.0177 -0.0365 0.0071  72  TYR   C CE2 
1606 C  CZ  . TYR   B 66  ? 0.3177 0.2569 0.2811 -0.0223 -0.0358 0.0093  72  TYR   C CZ  
1607 O  OH  . TYR   B 66  ? 0.3510 0.2840 0.3028 -0.0252 -0.0363 0.0100  72  TYR   C OH  
1608 N  N   . PRO   B 67  ? 0.1933 0.1498 0.1936 -0.0180 -0.0366 0.0078  73  PRO   C N   
1609 C  CA  . PRO   B 67  ? 0.1960 0.1577 0.2015 -0.0183 -0.0352 0.0071  73  PRO   C CA  
1610 C  C   . PRO   B 67  ? 0.2084 0.1788 0.2170 -0.0186 -0.0314 0.0075  73  PRO   C C   
1611 O  O   . PRO   B 67  ? 0.2218 0.1936 0.2275 -0.0206 -0.0294 0.0086  73  PRO   C O   
1612 C  CB  . PRO   B 67  ? 0.2077 0.1654 0.2100 -0.0219 -0.0365 0.0086  73  PRO   C CB  
1613 C  CG  . PRO   B 67  ? 0.2219 0.1754 0.2173 -0.0245 -0.0368 0.0107  73  PRO   C CG  
1614 C  CD  . PRO   B 67  ? 0.1991 0.1502 0.1923 -0.0220 -0.0376 0.0102  73  PRO   C CD  
1615 N  N   . VAL   B 68  ? 0.1947 0.1704 0.2090 -0.0168 -0.0306 0.0065  74  VAL   C N   
1616 C  CA  . VAL   B 68  ? 0.2037 0.1873 0.2224 -0.0166 -0.0279 0.0069  74  VAL   C CA  
1617 C  C   . VAL   B 68  ? 0.1967 0.1847 0.2200 -0.0171 -0.0284 0.0071  74  VAL   C C   
1618 O  O   . VAL   B 68  ? 0.2056 0.1909 0.2286 -0.0167 -0.0300 0.0061  74  VAL   C O   
1619 C  CB  . VAL   B 68  ? 0.2323 0.2176 0.2529 -0.0132 -0.0267 0.0057  74  VAL   C CB  
1620 C  CG1 . VAL   B 68  ? 0.2516 0.2333 0.2668 -0.0134 -0.0257 0.0056  74  VAL   C CG1 
1621 C  CG2 . VAL   B 68  ? 0.2445 0.2278 0.2669 -0.0105 -0.0285 0.0043  74  VAL   C CG2 
1622 N  N   . SER   B 69  ? 0.1834 0.1784 0.2114 -0.0180 -0.0269 0.0082  75  SER   C N   
1623 C  CA  . SER   B 69  ? 0.1869 0.1866 0.2197 -0.0180 -0.0280 0.0088  75  SER   C CA  
1624 C  C   . SER   B 69  ? 0.1787 0.1810 0.2154 -0.0143 -0.0273 0.0082  75  SER   C C   
1625 O  O   . SER   B 69  ? 0.1916 0.1948 0.2292 -0.0126 -0.0251 0.0076  75  SER   C O   
1626 C  CB  . SER   B 69  ? 0.2277 0.2339 0.2650 -0.0207 -0.0275 0.0105  75  SER   C CB  
1627 O  OG  . SER   B 69  ? 0.2903 0.2939 0.3240 -0.0245 -0.0285 0.0113  75  SER   C OG  
1628 N  N   . PHE   B 70  ? 0.1595 0.1625 0.1980 -0.0135 -0.0289 0.0083  76  PHE   C N   
1629 C  CA  . PHE   B 70  ? 0.1634 0.1679 0.2055 -0.0103 -0.0287 0.0080  76  PHE   C CA  
1630 C  C   . PHE   B 70  ? 0.1556 0.1638 0.2017 -0.0109 -0.0308 0.0097  76  PHE   C C   
1631 O  O   . PHE   B 70  ? 0.1717 0.1798 0.2160 -0.0137 -0.0327 0.0107  76  PHE   C O   
1632 C  CB  . PHE   B 70  ? 0.1675 0.1668 0.2061 -0.0084 -0.0287 0.0062  76  PHE   C CB  
1633 C  CG  . PHE   B 70  ? 0.1598 0.1553 0.1948 -0.0099 -0.0300 0.0054  76  PHE   C CG  
1634 C  CD1 . PHE   B 70  ? 0.1654 0.1568 0.1966 -0.0110 -0.0300 0.0043  76  PHE   C CD1 
1635 C  CD2 . PHE   B 70  ? 0.1709 0.1666 0.2061 -0.0103 -0.0309 0.0055  76  PHE   C CD2 
1636 C  CE1 . PHE   B 70  ? 0.1663 0.1542 0.1952 -0.0120 -0.0307 0.0028  76  PHE   C CE1 
1637 C  CE2 . PHE   B 70  ? 0.1672 0.1595 0.1989 -0.0118 -0.0310 0.0041  76  PHE   C CE2 
1638 C  CZ  . PHE   B 70  ? 0.1675 0.1563 0.1967 -0.0124 -0.0307 0.0024  76  PHE   C CZ  
1639 N  N   . SER   B 71  ? 0.1457 0.1564 0.1969 -0.0083 -0.0309 0.0102  77  SER   C N   
1640 C  CA  . SER   B 71  ? 0.1559 0.1697 0.2114 -0.0087 -0.0338 0.0125  77  SER   C CA  
1641 C  C   . SER   B 71  ? 0.1793 0.1888 0.2299 -0.0097 -0.0358 0.0128  77  SER   C C   
1642 O  O   . SER   B 71  ? 0.1934 0.1985 0.2385 -0.0100 -0.0346 0.0110  77  SER   C O   
1643 C  CB  . SER   B 71  ? 0.1585 0.1757 0.2218 -0.0052 -0.0333 0.0127  77  SER   C CB  
1644 O  OG  . SER   B 71  ? 0.1885 0.2017 0.2501 -0.0025 -0.0324 0.0113  77  SER   C OG  
1645 N  N   . LYS   B 72  ? 0.1684 0.1795 0.2210 -0.0109 -0.0391 0.0154  78  LYS   C N   
1646 C  CA  . LYS   B 72  ? 0.1912 0.1980 0.2382 -0.0125 -0.0407 0.0159  78  LYS   C CA  
1647 C  C   . LYS   B 72  ? 0.1990 0.2039 0.2481 -0.0093 -0.0402 0.0156  78  LYS   C C   
1648 O  O   . LYS   B 72  ? 0.2201 0.2274 0.2759 -0.0061 -0.0401 0.0159  78  LYS   C O   
1649 C  CB  . LYS   B 72  ? 0.2185 0.2268 0.2658 -0.0153 -0.0451 0.0192  78  LYS   C CB  
1650 C  CG  . LYS   B 72  ? 0.2630 0.2727 0.3077 -0.0190 -0.0459 0.0194  78  LYS   C CG  
1651 C  CD  . LYS   B 72  ? 0.3493 0.3592 0.3922 -0.0226 -0.0510 0.0227  78  LYS   C CD  
1652 C  CE  . LYS   B 72  ? 0.4437 0.4548 0.4842 -0.0265 -0.0525 0.0230  78  LYS   C CE  
1653 N  NZ  . LYS   B 72  ? 0.5039 0.5158 0.5439 -0.0299 -0.0583 0.0267  78  LYS   C NZ  
1654 N  N   . PRO   B 73  ? 0.1992 0.1997 0.2427 -0.0104 -0.0397 0.0149  79  PRO   C N   
1655 C  CA  . PRO   B 73  ? 0.2098 0.2081 0.2551 -0.0080 -0.0395 0.0147  79  PRO   C CA  
1656 C  C   . PRO   B 73  ? 0.2258 0.2250 0.2762 -0.0068 -0.0429 0.0178  79  PRO   C C   
1657 O  O   . PRO   B 73  ? 0.2411 0.2404 0.2902 -0.0095 -0.0464 0.0208  79  PRO   C O   
1658 C  CB  . PRO   B 73  ? 0.2333 0.2276 0.2720 -0.0107 -0.0386 0.0140  79  PRO   C CB  
1659 C  CG  . PRO   B 73  ? 0.2446 0.2388 0.2785 -0.0134 -0.0372 0.0123  79  PRO   C CG  
1660 C  CD  . PRO   B 73  ? 0.2102 0.2078 0.2462 -0.0140 -0.0389 0.0138  79  PRO   C CD  
1661 N  N   . SER   B 74  ? 0.2186 0.2180 0.2748 -0.0028 -0.0422 0.0170  80  SER   C N   
1662 C  CA  . SER   B 74  ? 0.2339 0.2341 0.2968 -0.0009 -0.0455 0.0196  80  SER   C CA  
1663 C  C   . SER   B 74  ? 0.2209 0.2187 0.2877 0.0030  -0.0444 0.0181  80  SER   C C   
1664 O  O   . SER   B 74  ? 0.2012 0.1966 0.2647 0.0037  -0.0413 0.0152  80  SER   C O   
1665 C  CB  . SER   B 74  ? 0.2839 0.2902 0.3543 0.0001  -0.0464 0.0204  80  SER   C CB  
1666 O  OG  . SER   B 74  ? 0.3254 0.3345 0.3996 0.0031  -0.0422 0.0172  80  SER   C OG  
1667 N  N   . LEU   B 75  ? 0.2125 0.2100 0.2860 0.0051  -0.0476 0.0202  81  LEU   C N   
1668 C  CA  . LEU   B 75  ? 0.2245 0.2188 0.3022 0.0089  -0.0472 0.0188  81  LEU   C CA  
1669 C  C   . LEU   B 75  ? 0.2308 0.2295 0.3161 0.0129  -0.0440 0.0158  81  LEU   C C   
1670 O  O   . LEU   B 75  ? 0.2468 0.2506 0.3403 0.0141  -0.0453 0.0169  81  LEU   C O   
1671 C  CB  . LEU   B 75  ? 0.2444 0.2362 0.3268 0.0094  -0.0526 0.0227  81  LEU   C CB  
1672 C  CG  . LEU   B 75  ? 0.3054 0.2903 0.3811 0.0067  -0.0552 0.0250  81  LEU   C CG  
1673 C  CD1 . LEU   B 75  ? 0.3415 0.3236 0.4221 0.0071  -0.0616 0.0296  81  LEU   C CD1 
1674 C  CD2 . LEU   B 75  ? 0.3167 0.2971 0.3907 0.0085  -0.0523 0.0219  81  LEU   C CD2 
1675 N  N   . ILE   B 76  ? 0.2097 0.2065 0.2928 0.0146  -0.0400 0.0120  82  ILE   C N   
1676 C  CA  . ILE   B 76  ? 0.2259 0.2262 0.3136 0.0175  -0.0359 0.0085  82  ILE   C CA  
1677 C  C   . ILE   B 76  ? 0.2353 0.2310 0.3241 0.0208  -0.0342 0.0054  82  ILE   C C   
1678 O  O   . ILE   B 76  ? 0.2167 0.2068 0.2991 0.0199  -0.0344 0.0048  82  ILE   C O   
1679 C  CB  . ILE   B 76  ? 0.2678 0.2697 0.3485 0.0151  -0.0325 0.0068  82  ILE   C CB  
1680 C  CG1 . ILE   B 76  ? 0.3058 0.3121 0.3861 0.0119  -0.0343 0.0096  82  ILE   C CG1 
1681 C  CG2 . ILE   B 76  ? 0.2875 0.2914 0.3696 0.0171  -0.0277 0.0030  82  ILE   C CG2 
1682 C  CD1 . ILE   B 76  ? 0.3530 0.3604 0.4273 0.0094  -0.0319 0.0085  82  ILE   C CD1 
1683 N  N   . PHE   B 77  ? 0.2391 0.2371 0.3365 0.0246  -0.0324 0.0033  83  PHE   C N   
1684 C  CA  . PHE   B 77  ? 0.2522 0.2453 0.3506 0.0277  -0.0306 -0.0002 83  PHE   C CA  
1685 C  C   . PHE   B 77  ? 0.2519 0.2426 0.3413 0.0267  -0.0262 -0.0040 83  PHE   C C   
1686 O  O   . PHE   B 77  ? 0.2530 0.2479 0.3403 0.0256  -0.0228 -0.0054 83  PHE   C O   
1687 C  CB  . PHE   B 77  ? 0.2643 0.2610 0.3750 0.0322  -0.0290 -0.0022 83  PHE   C CB  
1688 C  CG  . PHE   B 77  ? 0.2884 0.2791 0.4002 0.0356  -0.0271 -0.0063 83  PHE   C CG  
1689 C  CD1 . PHE   B 77  ? 0.3167 0.3078 0.4266 0.0369  -0.0211 -0.0116 83  PHE   C CD1 
1690 C  CD2 . PHE   B 77  ? 0.3173 0.3011 0.4305 0.0370  -0.0313 -0.0049 83  PHE   C CD2 
1691 C  CE1 . PHE   B 77  ? 0.3330 0.3179 0.4429 0.0397  -0.0192 -0.0158 83  PHE   C CE1 
1692 C  CE2 . PHE   B 77  ? 0.3396 0.3170 0.4533 0.0399  -0.0297 -0.0089 83  PHE   C CE2 
1693 C  CZ  . PHE   B 77  ? 0.3382 0.3163 0.4503 0.0414  -0.0236 -0.0145 83  PHE   C CZ  
1694 N  N   . VAL   B 78  ? 0.2507 0.2342 0.3345 0.0268  -0.0268 -0.0055 84  VAL   C N   
1695 C  CA  . VAL   B 78  ? 0.2370 0.2171 0.3121 0.0258  -0.0238 -0.0089 84  VAL   C CA  
1696 C  C   . VAL   B 78  ? 0.2526 0.2270 0.3283 0.0286  -0.0226 -0.0127 84  VAL   C C   
1697 O  O   . VAL   B 78  ? 0.2438 0.2133 0.3217 0.0296  -0.0257 -0.0117 84  VAL   C O   
1698 C  CB  . VAL   B 78  ? 0.2337 0.2106 0.3008 0.0224  -0.0263 -0.0071 84  VAL   C CB  
1699 C  CG1 . VAL   B 78  ? 0.2299 0.2034 0.2886 0.0212  -0.0244 -0.0101 84  VAL   C CG1 
1700 C  CG2 . VAL   B 78  ? 0.2244 0.2063 0.2910 0.0197  -0.0275 -0.0037 84  VAL   C CG2 
1701 N  N   . GLU   B 79  ? 0.2767 0.2508 0.3493 0.0293  -0.0180 -0.0170 85  GLU   C N   
1702 C  CA  . GLU   B 79  ? 0.2971 0.2653 0.3689 0.0317  -0.0159 -0.0215 85  GLU   C CA  
1703 C  C   . GLU   B 79  ? 0.2861 0.2460 0.3505 0.0302  -0.0190 -0.0217 85  GLU   C C   
1704 O  O   . GLU   B 79  ? 0.2844 0.2439 0.3425 0.0270  -0.0213 -0.0195 85  GLU   C O   
1705 C  CB  . GLU   B 79  ? 0.3576 0.3267 0.4236 0.0311  -0.0101 -0.0259 85  GLU   C CB  
1706 C  CG  . GLU   B 79  ? 0.4608 0.4386 0.5333 0.0317  -0.0061 -0.0261 85  GLU   C CG  
1707 C  CD  . GLU   B 79  ? 0.5696 0.5504 0.6545 0.0361  -0.0033 -0.0289 85  GLU   C CD  
1708 O  OE1 . GLU   B 79  ? 0.5927 0.5816 0.6847 0.0366  0.0001  -0.0293 85  GLU   C OE1 
1709 O  OE2 . GLU   B 79  ? 0.5835 0.5587 0.6719 0.0391  -0.0048 -0.0307 85  GLU   C OE2 
1710 N  N   . ALA   B 80  ? 0.2749 0.2284 0.3404 0.0324  -0.0191 -0.0247 86  ALA   C N   
1711 C  CA  . ALA   B 80  ? 0.2711 0.2165 0.3300 0.0308  -0.0221 -0.0253 86  ALA   C CA  
1712 C  C   . ALA   B 80  ? 0.2683 0.2117 0.3159 0.0278  -0.0208 -0.0274 86  ALA   C C   
1713 O  O   . ALA   B 80  ? 0.2704 0.2157 0.3139 0.0276  -0.0166 -0.0301 86  ALA   C O   
1714 C  CB  . ALA   B 80  ? 0.2706 0.2089 0.3322 0.0338  -0.0217 -0.0290 86  ALA   C CB  
1715 N  N   . SER   B 81  ? 0.2513 0.1909 0.2939 0.0251  -0.0246 -0.0258 87  SER   C N   
1716 C  CA  . SER   B 81  ? 0.2455 0.1820 0.2781 0.0221  -0.0250 -0.0273 87  SER   C CA  
1717 C  C   . SER   B 81  ? 0.2750 0.2039 0.3052 0.0210  -0.0289 -0.0280 87  SER   C C   
1718 O  O   . SER   B 81  ? 0.2914 0.2180 0.3276 0.0224  -0.0305 -0.0272 87  SER   C O   
1719 C  CB  . SER   B 81  ? 0.2368 0.1784 0.2677 0.0195  -0.0266 -0.0237 87  SER   C CB  
1720 O  OG  . SER   B 81  ? 0.2492 0.1921 0.2849 0.0186  -0.0302 -0.0202 87  SER   C OG  
1721 N  N   . GLU   B 82  ? 0.2838 0.2088 0.3058 0.0183  -0.0307 -0.0293 88  GLU   C N   
1722 C  CA  . GLU   B 82  ? 0.3029 0.2217 0.3237 0.0167  -0.0348 -0.0296 88  GLU   C CA  
1723 C  C   . GLU   B 82  ? 0.3036 0.2261 0.3310 0.0152  -0.0382 -0.0251 88  GLU   C C   
1724 O  O   . GLU   B 82  ? 0.3078 0.2261 0.3372 0.0142  -0.0411 -0.0247 88  GLU   C O   
1725 C  CB  . GLU   B 82  ? 0.3606 0.2743 0.3714 0.0139  -0.0368 -0.0319 88  GLU   C CB  
1726 C  CG  . GLU   B 82  ? 0.4619 0.3800 0.4704 0.0116  -0.0386 -0.0292 88  GLU   C CG  
1727 C  CD  . GLU   B 82  ? 0.6488 0.5624 0.6459 0.0094  -0.0392 -0.0315 88  GLU   C CD  
1728 O  OE1 . GLU   B 82  ? 0.7028 0.6089 0.6938 0.0080  -0.0415 -0.0342 88  GLU   C OE1 
1729 O  OE2 . GLU   B 82  ? 0.6915 0.6084 0.6850 0.0087  -0.0378 -0.0305 88  GLU   C OE2 
1730 N  N   . TYR   B 83  ? 0.2865 0.2165 0.3175 0.0151  -0.0374 -0.0219 89  TYR   C N   
1731 C  CA  . TYR   B 83  ? 0.2845 0.2184 0.3206 0.0133  -0.0396 -0.0181 89  TYR   C CA  
1732 C  C   . TYR   B 83  ? 0.2877 0.2232 0.3303 0.0145  -0.0393 -0.0155 89  TYR   C C   
1733 O  O   . TYR   B 83  ? 0.3090 0.2451 0.3545 0.0124  -0.0413 -0.0129 89  TYR   C O   
1734 C  CB  . TYR   B 83  ? 0.2705 0.2107 0.3060 0.0122  -0.0390 -0.0164 89  TYR   C CB  
1735 C  CG  . TYR   B 83  ? 0.2832 0.2215 0.3125 0.0108  -0.0403 -0.0182 89  TYR   C CG  
1736 C  CD1 . TYR   B 83  ? 0.3032 0.2394 0.3323 0.0086  -0.0439 -0.0182 89  TYR   C CD1 
1737 C  CD2 . TYR   B 83  ? 0.2957 0.2342 0.3194 0.0114  -0.0381 -0.0195 89  TYR   C CD2 
1738 C  CE1 . TYR   B 83  ? 0.3247 0.2586 0.3482 0.0072  -0.0462 -0.0194 89  TYR   C CE1 
1739 C  CE2 . TYR   B 83  ? 0.3288 0.2646 0.3456 0.0096  -0.0400 -0.0205 89  TYR   C CE2 
1740 C  CZ  . TYR   B 83  ? 0.3494 0.2828 0.3663 0.0077  -0.0444 -0.0203 89  TYR   C CZ  
1741 O  OH  . TYR   B 83  ? 0.3965 0.3267 0.4068 0.0059  -0.0474 -0.0209 89  TYR   C OH  
1742 N  N   . TYR   B 84  ? 0.2619 0.1984 0.3069 0.0175  -0.0370 -0.0161 90  TYR   C N   
1743 C  CA  . TYR   B 84  ? 0.2571 0.1954 0.3085 0.0186  -0.0376 -0.0130 90  TYR   C CA  
1744 C  C   . TYR   B 84  ? 0.2777 0.2135 0.3327 0.0225  -0.0361 -0.0152 90  TYR   C C   
1745 O  O   . TYR   B 84  ? 0.2743 0.2111 0.3276 0.0244  -0.0328 -0.0185 90  TYR   C O   
1746 C  CB  . TYR   B 84  ? 0.2369 0.1830 0.2904 0.0182  -0.0365 -0.0102 90  TYR   C CB  
1747 C  CG  . TYR   B 84  ? 0.2260 0.1755 0.2776 0.0148  -0.0375 -0.0081 90  TYR   C CG  
1748 C  CD1 . TYR   B 84  ? 0.2231 0.1761 0.2713 0.0140  -0.0361 -0.0089 90  TYR   C CD1 
1749 C  CD2 . TYR   B 84  ? 0.2149 0.1639 0.2681 0.0123  -0.0395 -0.0052 90  TYR   C CD2 
1750 C  CE1 . TYR   B 84  ? 0.2167 0.1726 0.2644 0.0113  -0.0369 -0.0075 90  TYR   C CE1 
1751 C  CE2 . TYR   B 84  ? 0.2055 0.1580 0.2576 0.0093  -0.0396 -0.0039 90  TYR   C CE2 
1752 C  CZ  . TYR   B 84  ? 0.2103 0.1664 0.2604 0.0091  -0.0383 -0.0053 90  TYR   C CZ  
1753 O  OH  . TYR   B 84  ? 0.2070 0.1663 0.2573 0.0066  -0.0383 -0.0045 90  TYR   C OH  
1754 N  N   . PRO   B 85  ? 0.2900 0.2234 0.3507 0.0237  -0.0383 -0.0130 91  PRO   C N   
1755 C  CA  . PRO   B 85  ? 0.2836 0.2162 0.3503 0.0280  -0.0369 -0.0147 91  PRO   C CA  
1756 C  C   . PRO   B 85  ? 0.2814 0.2227 0.3522 0.0294  -0.0346 -0.0136 91  PRO   C C   
1757 O  O   . PRO   B 85  ? 0.2739 0.2207 0.3432 0.0268  -0.0351 -0.0105 91  PRO   C O   
1758 C  CB  . PRO   B 85  ? 0.2981 0.2262 0.3700 0.0282  -0.0412 -0.0112 91  PRO   C CB  
1759 C  CG  . PRO   B 85  ? 0.3058 0.2362 0.3748 0.0238  -0.0436 -0.0066 91  PRO   C CG  
1760 C  CD  . PRO   B 85  ? 0.2850 0.2170 0.3472 0.0210  -0.0419 -0.0085 91  PRO   C CD  
1761 N  N   . ALA   B 86  ? 0.2824 0.2253 0.3598 0.0333  -0.0323 -0.0159 92  ALA   C N   
1762 C  CA  . ALA   B 86  ? 0.2874 0.2388 0.3709 0.0346  -0.0306 -0.0145 92  ALA   C CA  
1763 C  C   . ALA   B 86  ? 0.2813 0.2346 0.3689 0.0332  -0.0355 -0.0084 92  ALA   C C   
1764 O  O   . ALA   B 86  ? 0.2794 0.2267 0.3690 0.0335  -0.0394 -0.0064 92  ALA   C O   
1765 C  CB  . ALA   B 86  ? 0.2883 0.2407 0.3807 0.0395  -0.0277 -0.0182 92  ALA   C CB  
1766 N  N   . ARG   B 87  ? 0.2679 0.2281 0.3546 0.0309  -0.0356 -0.0055 93  ARG   C N   
1767 C  CA  . ARG   B 87  ? 0.2566 0.2175 0.3442 0.0285  -0.0401 0.0000  93  ARG   C CA  
1768 C  C   . ARG   B 87  ? 0.2525 0.2213 0.3401 0.0266  -0.0394 0.0022  93  ARG   C C   
1769 O  O   . ARG   B 87  ? 0.2560 0.2294 0.3422 0.0268  -0.0355 -0.0003 93  ARG   C O   
1770 C  CB  . ARG   B 87  ? 0.2639 0.2199 0.3433 0.0244  -0.0418 0.0015  93  ARG   C CB  
1771 C  CG  . ARG   B 87  ? 0.2192 0.1789 0.2914 0.0215  -0.0390 0.0003  93  ARG   C CG  
1772 C  CD  . ARG   B 87  ? 0.2364 0.1917 0.3025 0.0187  -0.0396 -0.0004 93  ARG   C CD  
1773 N  NE  . ARG   B 87  ? 0.2270 0.1858 0.2886 0.0152  -0.0391 0.0008  93  ARG   C NE  
1774 C  CZ  . ARG   B 87  ? 0.2530 0.2155 0.3117 0.0148  -0.0367 -0.0011 93  ARG   C CZ  
1775 N  NH1 . ARG   B 87  ? 0.2198 0.1848 0.2755 0.0119  -0.0365 -0.0001 93  ARG   C NH1 
1776 N  NH2 . ARG   B 87  ? 0.2476 0.2112 0.3065 0.0173  -0.0343 -0.0038 93  ARG   C NH2 
1777 N  N   . TYR   B 88  ? 0.2460 0.2159 0.3341 0.0243  -0.0434 0.0070  94  TYR   C N   
1778 C  CA  . TYR   B 88  ? 0.2498 0.2260 0.3362 0.0216  -0.0431 0.0090  94  TYR   C CA  
1779 C  C   . TYR   B 88  ? 0.2235 0.1982 0.3003 0.0173  -0.0425 0.0095  94  TYR   C C   
1780 O  O   . TYR   B 88  ? 0.2294 0.1995 0.3027 0.0151  -0.0448 0.0115  94  TYR   C O   
1781 C  CB  . TYR   B 88  ? 0.2735 0.2513 0.3644 0.0208  -0.0479 0.0138  94  TYR   C CB  
1782 C  CG  . TYR   B 88  ? 0.3117 0.2930 0.4143 0.0252  -0.0486 0.0134  94  TYR   C CG  
1783 C  CD1 . TYR   B 88  ? 0.3347 0.3239 0.4423 0.0258  -0.0468 0.0129  94  TYR   C CD1 
1784 C  CD2 . TYR   B 88  ? 0.3496 0.3262 0.4591 0.0289  -0.0507 0.0130  94  TYR   C CD2 
1785 C  CE1 . TYR   B 88  ? 0.3655 0.3591 0.4857 0.0299  -0.0469 0.0120  94  TYR   C CE1 
1786 C  CE2 . TYR   B 88  ? 0.3706 0.3508 0.4928 0.0335  -0.0509 0.0119  94  TYR   C CE2 
1787 C  CZ  . TYR   B 88  ? 0.3889 0.3782 0.5168 0.0340  -0.0488 0.0113  94  TYR   C CZ  
1788 O  OH  . TYR   B 88  ? 0.4386 0.4327 0.5806 0.0385  -0.0486 0.0099  94  TYR   C OH  
1789 N  N   . GLN   B 89  ? 0.1842 0.1629 0.2573 0.0162  -0.0394 0.0077  95  GLN   C N   
1790 C  CA  . GLN   B 89  ? 0.1746 0.1526 0.2404 0.0125  -0.0388 0.0079  95  GLN   C CA  
1791 C  C   . GLN   B 89  ? 0.1890 0.1708 0.2535 0.0096  -0.0401 0.0109  95  GLN   C C   
1792 O  O   . GLN   B 89  ? 0.2076 0.1941 0.2750 0.0103  -0.0396 0.0111  95  GLN   C O   
1793 C  CB  . GLN   B 89  ? 0.1786 0.1575 0.2410 0.0129  -0.0354 0.0043  95  GLN   C CB  
1794 C  CG  . GLN   B 89  ? 0.1748 0.1538 0.2316 0.0096  -0.0350 0.0043  95  GLN   C CG  
1795 C  CD  . GLN   B 89  ? 0.1928 0.1704 0.2464 0.0101  -0.0332 0.0012  95  GLN   C CD  
1796 O  OE1 . GLN   B 89  ? 0.2024 0.1768 0.2560 0.0119  -0.0328 -0.0009 95  GLN   C OE1 
1797 N  NE2 . GLN   B 89  ? 0.1734 0.1529 0.2241 0.0083  -0.0324 0.0008  95  GLN   C NE2 
1798 N  N   . SER   B 90  ? 0.1806 0.1603 0.2402 0.0059  -0.0415 0.0128  96  SER   C N   
1799 C  CA  . SER   B 90  ? 0.1717 0.1537 0.2284 0.0025  -0.0428 0.0155  96  SER   C CA  
1800 C  C   . SER   B 90  ? 0.1794 0.1636 0.2314 0.0003  -0.0398 0.0134  96  SER   C C   
1801 O  O   . SER   B 90  ? 0.1891 0.1725 0.2400 0.0012  -0.0374 0.0104  96  SER   C O   
1802 C  CB  . SER   B 90  ? 0.2103 0.1883 0.2633 -0.0009 -0.0456 0.0188  96  SER   C CB  
1803 O  OG  . SER   B 90  ? 0.2373 0.2123 0.2864 -0.0028 -0.0437 0.0172  96  SER   C OG  
1804 N  N   . HIS   B 91  ? 0.1788 0.1655 0.2282 -0.0023 -0.0405 0.0149  97  HIS   C N   
1805 C  CA  . HIS   B 91  ? 0.1768 0.1649 0.2218 -0.0046 -0.0381 0.0130  97  HIS   C CA  
1806 C  C   . HIS   B 91  ? 0.1880 0.1780 0.2351 -0.0019 -0.0357 0.0101  97  HIS   C C   
1807 O  O   . HIS   B 91  ? 0.1965 0.1859 0.2408 -0.0027 -0.0338 0.0079  97  HIS   C O   
1808 C  CB  . HIS   B 91  ? 0.1840 0.1693 0.2246 -0.0072 -0.0365 0.0118  97  HIS   C CB  
1809 C  CG  . HIS   B 91  ? 0.2075 0.1906 0.2440 -0.0110 -0.0384 0.0148  97  HIS   C CG  
1810 N  ND1 . HIS   B 91  ? 0.2527 0.2360 0.2833 -0.0151 -0.0382 0.0155  97  HIS   C ND1 
1811 C  CD2 . HIS   B 91  ? 0.2390 0.2188 0.2757 -0.0114 -0.0407 0.0173  97  HIS   C CD2 
1812 C  CE1 . HIS   B 91  ? 0.2619 0.2422 0.2886 -0.0183 -0.0403 0.0185  97  HIS   C CE1 
1813 N  NE2 . HIS   B 91  ? 0.2541 0.2320 0.2844 -0.0163 -0.0420 0.0199  97  HIS   C NE2 
1814 N  N   . LEU   B 92  ? 0.1808 0.1729 0.2326 0.0010  -0.0359 0.0102  98  LEU   C N   
1815 C  CA  . LEU   B 92  ? 0.1715 0.1649 0.2240 0.0029  -0.0334 0.0077  98  LEU   C CA  
1816 C  C   . LEU   B 92  ? 0.1789 0.1763 0.2321 0.0018  -0.0331 0.0083  98  LEU   C C   
1817 O  O   . LEU   B 92  ? 0.1757 0.1761 0.2324 0.0013  -0.0349 0.0106  98  LEU   C O   
1818 C  CB  . LEU   B 92  ? 0.1753 0.1680 0.2320 0.0065  -0.0328 0.0065  98  LEU   C CB  
1819 C  CG  . LEU   B 92  ? 0.2123 0.2051 0.2681 0.0081  -0.0301 0.0038  98  LEU   C CG  
1820 C  CD1 . LEU   B 92  ? 0.2185 0.2074 0.2689 0.0073  -0.0296 0.0019  98  LEU   C CD1 
1821 C  CD2 . LEU   B 92  ? 0.2239 0.2156 0.2835 0.0113  -0.0292 0.0023  98  LEU   C CD2 
1822 N  N   . MET   B 93  ? 0.1653 0.1626 0.2154 0.0012  -0.0312 0.0066  99  MET   C N   
1823 C  CA  . MET   B 93  ? 0.1724 0.1729 0.2225 -0.0004 -0.0308 0.0072  99  MET   C CA  
1824 C  C   . MET   B 93  ? 0.1791 0.1803 0.2296 0.0011  -0.0284 0.0056  99  MET   C C   
1825 O  O   . MET   B 93  ? 0.1895 0.1870 0.2365 0.0019  -0.0274 0.0038  99  MET   C O   
1826 C  CB  . MET   B 93  ? 0.1743 0.1728 0.2192 -0.0031 -0.0309 0.0067  99  MET   C CB  
1827 C  CG  . MET   B 93  ? 0.2113 0.2088 0.2544 -0.0052 -0.0326 0.0078  99  MET   C CG  
1828 S  SD  . MET   B 93  ? 0.2428 0.2373 0.2802 -0.0079 -0.0317 0.0060  99  MET   C SD  
1829 C  CE  . MET   B 93  ? 0.2387 0.2299 0.2763 -0.0054 -0.0302 0.0031  99  MET   C CE  
1830 N  N   . LEU   B 94  ? 0.1636 0.1694 0.2181 0.0009  -0.0274 0.0062  100 LEU   C N   
1831 C  CA  . LEU   B 94  ? 0.1515 0.1581 0.2054 0.0016  -0.0243 0.0046  100 LEU   C CA  
1832 C  C   . LEU   B 94  ? 0.1532 0.1605 0.2037 -0.0015 -0.0236 0.0050  100 LEU   C C   
1833 O  O   . LEU   B 94  ? 0.1574 0.1673 0.2093 -0.0037 -0.0251 0.0068  100 LEU   C O   
1834 C  CB  . LEU   B 94  ? 0.1722 0.1838 0.2340 0.0037  -0.0225 0.0043  100 LEU   C CB  
1835 C  CG  . LEU   B 94  ? 0.2068 0.2172 0.2728 0.0070  -0.0232 0.0036  100 LEU   C CG  
1836 C  CD1 . LEU   B 94  ? 0.2165 0.2322 0.2918 0.0095  -0.0210 0.0027  100 LEU   C CD1 
1837 C  CD2 . LEU   B 94  ? 0.2260 0.2300 0.2856 0.0082  -0.0223 0.0013  100 LEU   C CD2 
1838 N  N   . ALA   B 95  ? 0.1500 0.1545 0.1955 -0.0019 -0.0214 0.0036  101 ALA   C N   
1839 C  CA  . ALA   B 95  ? 0.1678 0.1724 0.2097 -0.0050 -0.0206 0.0043  101 ALA   C CA  
1840 C  C   . ALA   B 95  ? 0.1788 0.1841 0.2190 -0.0052 -0.0168 0.0030  101 ALA   C C   
1841 O  O   . ALA   B 95  ? 0.1938 0.1973 0.2330 -0.0030 -0.0153 0.0011  101 ALA   C O   
1842 C  CB  . ALA   B 95  ? 0.1716 0.1696 0.2063 -0.0063 -0.0226 0.0042  101 ALA   C CB  
1843 N  N   . VAL   B 96  ? 0.1786 0.1861 0.2175 -0.0084 -0.0149 0.0037  102 VAL   C N   
1844 C  CA  . VAL   B 96  ? 0.1935 0.2008 0.2285 -0.0097 -0.0109 0.0025  102 VAL   C CA  
1845 C  C   . VAL   B 96  ? 0.2237 0.2222 0.2476 -0.0114 -0.0126 0.0026  102 VAL   C C   
1846 O  O   . VAL   B 96  ? 0.2411 0.2365 0.2615 -0.0137 -0.0152 0.0043  102 VAL   C O   
1847 C  CB  . VAL   B 96  ? 0.2196 0.2333 0.2584 -0.0131 -0.0083 0.0036  102 VAL   C CB  
1848 C  CG1 . VAL   B 96  ? 0.2363 0.2498 0.2700 -0.0153 -0.0033 0.0023  102 VAL   C CG1 
1849 C  CG2 . VAL   B 96  ? 0.2185 0.2412 0.2701 -0.0111 -0.0079 0.0038  102 VAL   C CG2 
1850 N  N   . GLY   B 97  ? 0.2224 0.2165 0.2413 -0.0100 -0.0118 0.0009  103 GLY   C N   
1851 C  CA  . GLY   B 97  ? 0.2482 0.2337 0.2570 -0.0114 -0.0144 0.0012  103 GLY   C CA  
1852 C  C   . GLY   B 97  ? 0.2593 0.2407 0.2635 -0.0097 -0.0138 -0.0010 103 GLY   C C   
1853 O  O   . GLY   B 97  ? 0.2595 0.2441 0.2687 -0.0069 -0.0116 -0.0030 103 GLY   C O   
1854 N  N   . HIS   B 98  ? 0.2550 0.2286 0.2493 -0.0117 -0.0161 -0.0005 104 HIS   C N   
1855 C  CA  . HIS   B 98  ? 0.2611 0.2296 0.2490 -0.0109 -0.0161 -0.0024 104 HIS   C CA  
1856 C  C   . HIS   B 98  ? 0.2574 0.2236 0.2488 -0.0075 -0.0201 -0.0032 104 HIS   C C   
1857 O  O   . HIS   B 98  ? 0.2532 0.2178 0.2471 -0.0069 -0.0242 -0.0018 104 HIS   C O   
1858 C  CB  . HIS   B 98  ? 0.2711 0.2313 0.2461 -0.0149 -0.0179 -0.0011 104 HIS   C CB  
1859 C  CG  . HIS   B 98  ? 0.2902 0.2444 0.2571 -0.0148 -0.0186 -0.0030 104 HIS   C CG  
1860 N  ND1 . HIS   B 98  ? 0.3278 0.2836 0.2920 -0.0150 -0.0131 -0.0060 104 HIS   C ND1 
1861 C  CD2 . HIS   B 98  ? 0.3049 0.2518 0.2671 -0.0144 -0.0243 -0.0026 104 HIS   C CD2 
1862 C  CE1 . HIS   B 98  ? 0.3485 0.2969 0.3045 -0.0152 -0.0157 -0.0072 104 HIS   C CE1 
1863 N  NE2 . HIS   B 98  ? 0.3396 0.2827 0.2945 -0.0148 -0.0227 -0.0050 104 HIS   C NE2 
1864 N  N   . SER   B 99  ? 0.2533 0.2187 0.2443 -0.0056 -0.0186 -0.0057 105 SER   C N   
1865 C  CA  . SER   B 99  ? 0.2693 0.2316 0.2620 -0.0031 -0.0222 -0.0066 105 SER   C CA  
1866 C  C   . SER   B 99  ? 0.3000 0.2586 0.2870 -0.0029 -0.0204 -0.0094 105 SER   C C   
1867 O  O   . SER   B 99  ? 0.3200 0.2806 0.3053 -0.0033 -0.0153 -0.0113 105 SER   C O   
1868 C  CB  . SER   B 99  ? 0.2809 0.2483 0.2845 -0.0001 -0.0228 -0.0064 105 SER   C CB  
1869 O  OG  . SER   B 99  ? 0.3232 0.2955 0.3324 0.0017  -0.0189 -0.0079 105 SER   C OG  
1870 N  N   . GLU   B 100 ? 0.3021 0.2551 0.2860 -0.0024 -0.0246 -0.0099 106 GLU   C N   
1871 C  CA  . GLU   B 100 ? 0.3283 0.2766 0.3062 -0.0023 -0.0240 -0.0126 106 GLU   C CA  
1872 C  C   . GLU   B 100 ? 0.3400 0.2869 0.3232 0.0001  -0.0278 -0.0132 106 GLU   C C   
1873 O  O   . GLU   B 100 ? 0.3395 0.2875 0.3281 0.0007  -0.0317 -0.0112 106 GLU   C O   
1874 C  CB  . GLU   B 100 ? 0.3699 0.3101 0.3346 -0.0060 -0.0269 -0.0120 106 GLU   C CB  
1875 C  CG  . GLU   B 100 ? 0.4507 0.3899 0.4060 -0.0093 -0.0220 -0.0126 106 GLU   C CG  
1876 C  CD  . GLU   B 100 ? 0.4689 0.3993 0.4108 -0.0134 -0.0264 -0.0108 106 GLU   C CD  
1877 O  OE1 . GLU   B 100 ? 0.5037 0.4276 0.4405 -0.0137 -0.0313 -0.0112 106 GLU   C OE1 
1878 O  OE2 . GLU   B 100 ? 0.4656 0.3954 0.4022 -0.0166 -0.0254 -0.0086 106 GLU   C OE2 
1879 N  N   . PRO   B 101 ? 0.3638 0.3076 0.3448 0.0010  -0.0270 -0.0161 107 PRO   C N   
1880 C  CA  . PRO   B 101 ? 0.3843 0.3253 0.3685 0.0023  -0.0315 -0.0164 107 PRO   C CA  
1881 C  C   . PRO   B 101 ? 0.3855 0.3216 0.3649 0.0001  -0.0377 -0.0145 107 PRO   C C   
1882 O  O   . PRO   B 101 ? 0.4221 0.3525 0.3905 -0.0027 -0.0392 -0.0143 107 PRO   C O   
1883 C  CB  . PRO   B 101 ? 0.4080 0.3443 0.3868 0.0025  -0.0295 -0.0200 107 PRO   C CB  
1884 C  CG  . PRO   B 101 ? 0.4134 0.3532 0.3920 0.0031  -0.0227 -0.0219 107 PRO   C CG  
1885 C  CD  . PRO   B 101 ? 0.3800 0.3218 0.3547 0.0005  -0.0220 -0.0194 107 PRO   C CD  
1886 N  N   . GLY   B 102 ? 0.3374 0.2760 0.3252 0.0013  -0.0413 -0.0129 108 GLY   C N   
1887 C  CA  . GLY   B 102 ? 0.3111 0.2470 0.2987 0.0002  -0.0471 -0.0111 108 GLY   C CA  
1888 C  C   . GLY   B 102 ? 0.2909 0.2317 0.2857 0.0009  -0.0471 -0.0090 108 GLY   C C   
1889 O  O   . GLY   B 102 ? 0.2853 0.2259 0.2850 0.0011  -0.0514 -0.0079 108 GLY   C O   
1890 N  N   . ASP   B 103 ? 0.2598 0.2053 0.2561 0.0013  -0.0422 -0.0086 109 ASP   C N   
1891 C  CA  . ASP   B 103 ? 0.2517 0.2013 0.2536 0.0015  -0.0418 -0.0069 109 ASP   C CA  
1892 C  C   . ASP   B 103 ? 0.2356 0.1907 0.2479 0.0034  -0.0411 -0.0070 109 ASP   C C   
1893 O  O   . ASP   B 103 ? 0.2296 0.1873 0.2463 0.0034  -0.0415 -0.0060 109 ASP   C O   
1894 C  CB  . ASP   B 103 ? 0.2446 0.1968 0.2433 0.0003  -0.0375 -0.0061 109 ASP   C CB  
1895 C  CG  . ASP   B 103 ? 0.2743 0.2208 0.2625 -0.0026 -0.0387 -0.0051 109 ASP   C CG  
1896 O  OD1 . ASP   B 103 ? 0.2821 0.2236 0.2677 -0.0034 -0.0439 -0.0039 109 ASP   C OD1 
1897 O  OD2 . ASP   B 103 ? 0.2805 0.2278 0.2635 -0.0041 -0.0347 -0.0053 109 ASP   C OD2 
1898 N  N   . CYS   B 104 ? 0.2219 0.1780 0.2376 0.0047  -0.0403 -0.0083 110 CYS   C N   
1899 C  CA  . CYS   B 104 ? 0.2195 0.1803 0.2439 0.0057  -0.0396 -0.0081 110 CYS   C CA  
1900 C  C   . CYS   B 104 ? 0.2214 0.1825 0.2507 0.0055  -0.0426 -0.0080 110 CYS   C C   
1901 O  O   . CYS   B 104 ? 0.2270 0.1845 0.2552 0.0052  -0.0464 -0.0084 110 CYS   C O   
1902 C  CB  . CYS   B 104 ? 0.2222 0.1828 0.2488 0.0066  -0.0389 -0.0092 110 CYS   C CB  
1903 S  SG  . CYS   B 104 ? 0.2827 0.2444 0.3075 0.0078  -0.0347 -0.0098 110 CYS   C SG  
1904 N  N   . GLY   B 105 ? 0.2000 0.1654 0.2347 0.0055  -0.0410 -0.0075 111 GLY   C N   
1905 C  CA  . GLY   B 105 ? 0.2122 0.1786 0.2527 0.0055  -0.0429 -0.0081 111 GLY   C CA  
1906 C  C   . GLY   B 105 ? 0.2157 0.1815 0.2556 0.0053  -0.0436 -0.0075 111 GLY   C C   
1907 O  O   . GLY   B 105 ? 0.2266 0.1939 0.2724 0.0055  -0.0440 -0.0084 111 GLY   C O   
1908 N  N   . GLY   B 106 ? 0.1940 0.1576 0.2271 0.0046  -0.0432 -0.0063 112 GLY   C N   
1909 C  CA  . GLY   B 106 ? 0.1826 0.1448 0.2144 0.0039  -0.0440 -0.0056 112 GLY   C CA  
1910 C  C   . GLY   B 106 ? 0.1841 0.1507 0.2198 0.0036  -0.0409 -0.0058 112 GLY   C C   
1911 O  O   . GLY   B 106 ? 0.1852 0.1552 0.2209 0.0033  -0.0380 -0.0055 112 GLY   C O   
1912 N  N   . ILE   B 107 ? 0.1722 0.1382 0.2114 0.0037  -0.0419 -0.0065 113 ILE   C N   
1913 C  CA  . ILE   B 107 ? 0.1775 0.1469 0.2195 0.0030  -0.0390 -0.0073 113 ILE   C CA  
1914 C  C   . ILE   B 107 ? 0.1761 0.1453 0.2132 0.0014  -0.0377 -0.0058 113 ILE   C C   
1915 O  O   . ILE   B 107 ? 0.1919 0.1573 0.2252 0.0009  -0.0396 -0.0048 113 ILE   C O   
1916 C  CB  . ILE   B 107 ? 0.2193 0.1885 0.2682 0.0039  -0.0398 -0.0096 113 ILE   C CB  
1917 C  CG1 . ILE   B 107 ? 0.2477 0.2196 0.3031 0.0048  -0.0396 -0.0112 113 ILE   C CG1 
1918 C  CG2 . ILE   B 107 ? 0.2338 0.2046 0.2835 0.0028  -0.0370 -0.0108 113 ILE   C CG2 
1919 C  CD1 . ILE   B 107 ? 0.2887 0.2613 0.3532 0.0060  -0.0401 -0.0141 113 ILE   C CD1 
1920 N  N   . LEU   B 108 ? 0.1662 0.1393 0.2035 0.0003  -0.0349 -0.0056 114 LEU   C N   
1921 C  CA  . LEU   B 108 ? 0.1752 0.1490 0.2093 -0.0016 -0.0338 -0.0044 114 LEU   C CA  
1922 C  C   . LEU   B 108 ? 0.1827 0.1565 0.2190 -0.0025 -0.0329 -0.0063 114 LEU   C C   
1923 O  O   . LEU   B 108 ? 0.1784 0.1546 0.2175 -0.0025 -0.0313 -0.0077 114 LEU   C O   
1924 C  CB  . LEU   B 108 ? 0.1714 0.1496 0.2048 -0.0023 -0.0319 -0.0029 114 LEU   C CB  
1925 C  CG  . LEU   B 108 ? 0.1900 0.1700 0.2215 -0.0046 -0.0310 -0.0017 114 LEU   C CG  
1926 C  CD1 . LEU   B 108 ? 0.1982 0.1763 0.2263 -0.0057 -0.0317 -0.0005 114 LEU   C CD1 
1927 C  CD2 . LEU   B 108 ? 0.1943 0.1790 0.2271 -0.0048 -0.0300 -0.0001 114 LEU   C CD2 
1928 N  N   . ARG   B 109 ? 0.1712 0.1419 0.2057 -0.0034 -0.0337 -0.0065 115 ARG   C N   
1929 C  CA  . ARG   B 109 ? 0.1816 0.1514 0.2176 -0.0043 -0.0327 -0.0089 115 ARG   C CA  
1930 C  C   . ARG   B 109 ? 0.1983 0.1675 0.2299 -0.0070 -0.0324 -0.0078 115 ARG   C C   
1931 O  O   . ARG   B 109 ? 0.2026 0.1702 0.2310 -0.0079 -0.0338 -0.0056 115 ARG   C O   
1932 C  CB  . ARG   B 109 ? 0.2194 0.1844 0.2588 -0.0026 -0.0348 -0.0108 115 ARG   C CB  
1933 C  CG  . ARG   B 109 ? 0.2929 0.2581 0.3381 0.0001  -0.0361 -0.0120 115 ARG   C CG  
1934 C  CD  . ARG   B 109 ? 0.3690 0.3291 0.4183 0.0019  -0.0392 -0.0136 115 ARG   C CD  
1935 N  NE  . ARG   B 109 ? 0.4557 0.4161 0.5093 0.0019  -0.0367 -0.0173 115 ARG   C NE  
1936 C  CZ  . ARG   B 109 ? 0.5095 0.4730 0.5707 0.0033  -0.0346 -0.0206 115 ARG   C CZ  
1937 N  NH1 . ARG   B 109 ? 0.5342 0.5001 0.6003 0.0049  -0.0358 -0.0204 115 ARG   C NH1 
1938 N  NH2 . ARG   B 109 ? 0.5212 0.4852 0.5851 0.0028  -0.0312 -0.0244 115 ARG   C NH2 
1939 N  N   . CYS   B 110 ? 0.1900 0.1600 0.2208 -0.0088 -0.0305 -0.0094 116 CYS   C N   
1940 C  CA  . CYS   B 110 ? 0.2032 0.1717 0.2298 -0.0118 -0.0307 -0.0089 116 CYS   C CA  
1941 C  C   . CYS   B 110 ? 0.2220 0.1858 0.2496 -0.0117 -0.0303 -0.0126 116 CYS   C C   
1942 O  O   . CYS   B 110 ? 0.2115 0.1739 0.2440 -0.0092 -0.0300 -0.0153 116 CYS   C O   
1943 C  CB  . CYS   B 110 ? 0.1987 0.1713 0.2227 -0.0144 -0.0294 -0.0079 116 CYS   C CB  
1944 S  SG  . CYS   B 110 ? 0.1883 0.1619 0.2124 -0.0151 -0.0265 -0.0111 116 CYS   C SG  
1945 N  N   . GLN   B 111 ? 0.2458 0.2072 0.2692 -0.0147 -0.0302 -0.0132 117 GLN   C N   
1946 C  CA  . GLN   B 111 ? 0.2523 0.2087 0.2764 -0.0147 -0.0295 -0.0172 117 GLN   C CA  
1947 C  C   . GLN   B 111 ? 0.2575 0.2157 0.2843 -0.0141 -0.0258 -0.0214 117 GLN   C C   
1948 O  O   . GLN   B 111 ? 0.2808 0.2354 0.3107 -0.0130 -0.0244 -0.0257 117 GLN   C O   
1949 C  CB  . GLN   B 111 ? 0.2826 0.2360 0.3008 -0.0186 -0.0300 -0.0171 117 GLN   C CB  
1950 C  CG  . GLN   B 111 ? 0.3210 0.2782 0.3343 -0.0222 -0.0284 -0.0166 117 GLN   C CG  
1951 C  CD  . GLN   B 111 ? 0.4381 0.3921 0.4457 -0.0263 -0.0296 -0.0164 117 GLN   C CD  
1952 O  OE1 . GLN   B 111 ? 0.4576 0.4146 0.4628 -0.0288 -0.0315 -0.0127 117 GLN   C OE1 
1953 N  NE2 . GLN   B 111 ? 0.4674 0.4154 0.4732 -0.0271 -0.0287 -0.0206 117 GLN   C NE2 
1954 N  N   . HIS   B 112 ? 0.2271 0.1905 0.2530 -0.0150 -0.0240 -0.0203 118 HIS   C N   
1955 C  CA  . HIS   B 112 ? 0.2314 0.1966 0.2585 -0.0155 -0.0201 -0.0239 118 HIS   C CA  
1956 C  C   . HIS   B 112 ? 0.2396 0.2076 0.2743 -0.0122 -0.0192 -0.0250 118 HIS   C C   
1957 O  O   . HIS   B 112 ? 0.2618 0.2314 0.2990 -0.0125 -0.0155 -0.0284 118 HIS   C O   
1958 C  CB  . HIS   B 112 ? 0.2262 0.1944 0.2465 -0.0194 -0.0188 -0.0222 118 HIS   C CB  
1959 C  CG  . HIS   B 112 ? 0.2294 0.1954 0.2424 -0.0231 -0.0202 -0.0210 118 HIS   C CG  
1960 N  ND1 . HIS   B 112 ? 0.2306 0.1988 0.2412 -0.0244 -0.0234 -0.0162 118 HIS   C ND1 
1961 C  CD2 . HIS   B 112 ? 0.2507 0.2125 0.2588 -0.0259 -0.0188 -0.0242 118 HIS   C CD2 
1962 C  CE1 . HIS   B 112 ? 0.2537 0.2194 0.2585 -0.0280 -0.0243 -0.0162 118 HIS   C CE1 
1963 N  NE2 . HIS   B 112 ? 0.2671 0.2284 0.2693 -0.0292 -0.0218 -0.0210 118 HIS   C NE2 
1964 N  N   . GLY   B 113 ? 0.2249 0.1934 0.2630 -0.0094 -0.0223 -0.0221 119 GLY   C N   
1965 C  CA  . GLY   B 113 ? 0.2127 0.1838 0.2578 -0.0067 -0.0221 -0.0228 119 GLY   C CA  
1966 C  C   . GLY   B 113 ? 0.1883 0.1619 0.2325 -0.0059 -0.0243 -0.0187 119 GLY   C C   
1967 O  O   . GLY   B 113 ? 0.1868 0.1597 0.2264 -0.0066 -0.0264 -0.0154 119 GLY   C O   
1968 N  N   . VAL   B 114 ? 0.1723 0.1488 0.2209 -0.0047 -0.0235 -0.0191 120 VAL   C N   
1969 C  CA  . VAL   B 114 ? 0.1766 0.1547 0.2246 -0.0038 -0.0254 -0.0159 120 VAL   C CA  
1970 C  C   . VAL   B 114 ? 0.1799 0.1604 0.2224 -0.0063 -0.0244 -0.0133 120 VAL   C C   
1971 O  O   . VAL   B 114 ? 0.1852 0.1674 0.2263 -0.0085 -0.0218 -0.0142 120 VAL   C O   
1972 C  CB  . VAL   B 114 ? 0.1937 0.1738 0.2485 -0.0021 -0.0252 -0.0173 120 VAL   C CB  
1973 C  CG1 . VAL   B 114 ? 0.1993 0.1804 0.2525 -0.0015 -0.0269 -0.0143 120 VAL   C CG1 
1974 C  CG2 . VAL   B 114 ? 0.2025 0.1802 0.2638 0.0007  -0.0276 -0.0193 120 VAL   C CG2 
1975 N  N   . VAL   B 115 ? 0.1689 0.1495 0.2086 -0.0059 -0.0264 -0.0101 121 VAL   C N   
1976 C  CA  . VAL   B 115 ? 0.1615 0.1444 0.1977 -0.0076 -0.0263 -0.0074 121 VAL   C CA  
1977 C  C   . VAL   B 115 ? 0.1744 0.1588 0.2127 -0.0061 -0.0268 -0.0059 121 VAL   C C   
1978 O  O   . VAL   B 115 ? 0.1710 0.1569 0.2080 -0.0075 -0.0263 -0.0045 121 VAL   C O   
1979 C  CB  . VAL   B 115 ? 0.1709 0.1536 0.2042 -0.0080 -0.0279 -0.0051 121 VAL   C CB  
1980 C  CG1 . VAL   B 115 ? 0.1832 0.1690 0.2154 -0.0089 -0.0284 -0.0021 121 VAL   C CG1 
1981 C  CG2 . VAL   B 115 ? 0.1765 0.1573 0.2073 -0.0100 -0.0276 -0.0062 121 VAL   C CG2 
1982 N  N   . GLY   B 116 ? 0.1708 0.1540 0.2114 -0.0037 -0.0282 -0.0061 122 GLY   C N   
1983 C  CA  . GLY   B 116 ? 0.1828 0.1665 0.2247 -0.0023 -0.0288 -0.0051 122 GLY   C CA  
1984 C  C   . GLY   B 116 ? 0.1755 0.1570 0.2182 -0.0001 -0.0306 -0.0056 122 GLY   C C   
1985 O  O   . GLY   B 116 ? 0.1794 0.1588 0.2224 0.0004  -0.0316 -0.0066 122 GLY   C O   
1986 N  N   . ILE   B 117 ? 0.1683 0.1496 0.2112 0.0010  -0.0312 -0.0048 123 ILE   C N   
1987 C  CA  . ILE   B 117 ? 0.1717 0.1501 0.2139 0.0026  -0.0330 -0.0054 123 ILE   C CA  
1988 C  C   . ILE   B 117 ? 0.1691 0.1471 0.2083 0.0034  -0.0328 -0.0043 123 ILE   C C   
1989 O  O   . ILE   B 117 ? 0.1748 0.1546 0.2149 0.0035  -0.0317 -0.0035 123 ILE   C O   
1990 C  CB  . ILE   B 117 ? 0.1964 0.1741 0.2425 0.0032  -0.0341 -0.0068 123 ILE   C CB  
1991 C  CG1 . ILE   B 117 ? 0.2015 0.1808 0.2491 0.0026  -0.0329 -0.0062 123 ILE   C CG1 
1992 C  CG2 . ILE   B 117 ? 0.2170 0.1950 0.2676 0.0031  -0.0346 -0.0086 123 ILE   C CG2 
1993 C  CD1 . ILE   B 117 ? 0.2371 0.2154 0.2886 0.0029  -0.0343 -0.0075 123 ILE   C CD1 
1994 N  N   . VAL   B 118 ? 0.1633 0.1383 0.1988 0.0039  -0.0338 -0.0045 124 VAL   C N   
1995 C  CA  . VAL   B 118 ? 0.1643 0.1388 0.1967 0.0045  -0.0327 -0.0043 124 VAL   C CA  
1996 C  C   . VAL   B 118 ? 0.1625 0.1365 0.1970 0.0057  -0.0327 -0.0051 124 VAL   C C   
1997 O  O   . VAL   B 118 ? 0.1759 0.1478 0.2117 0.0059  -0.0346 -0.0060 124 VAL   C O   
1998 C  CB  . VAL   B 118 ? 0.1765 0.1468 0.2030 0.0041  -0.0338 -0.0047 124 VAL   C CB  
1999 C  CG1 . VAL   B 118 ? 0.1923 0.1621 0.2154 0.0045  -0.0317 -0.0053 124 VAL   C CG1 
2000 C  CG2 . VAL   B 118 ? 0.1827 0.1525 0.2066 0.0025  -0.0341 -0.0036 124 VAL   C CG2 
2001 N  N   . SER   B 119 ? 0.1682 0.1441 0.2039 0.0066  -0.0309 -0.0047 125 SER   C N   
2002 C  CA  . SER   B 119 ? 0.1711 0.1458 0.2089 0.0078  -0.0311 -0.0052 125 SER   C CA  
2003 C  C   . SER   B 119 ? 0.1898 0.1637 0.2264 0.0093  -0.0293 -0.0063 125 SER   C C   
2004 O  O   . SER   B 119 ? 0.2061 0.1768 0.2426 0.0104  -0.0297 -0.0077 125 SER   C O   
2005 C  CB  . SER   B 119 ? 0.1891 0.1665 0.2313 0.0073  -0.0311 -0.0036 125 SER   C CB  
2006 O  OG  . SER   B 119 ? 0.1961 0.1715 0.2403 0.0084  -0.0317 -0.0037 125 SER   C OG  
2007 N  N   . THR   B 120 ? 0.1923 0.1689 0.2283 0.0093  -0.0271 -0.0060 126 THR   C N   
2008 C  CA  . THR   B 120 ? 0.2113 0.1882 0.2475 0.0108  -0.0244 -0.0076 126 THR   C CA  
2009 C  C   . THR   B 120 ? 0.2165 0.1949 0.2487 0.0095  -0.0220 -0.0079 126 THR   C C   
2010 O  O   . THR   B 120 ? 0.1982 0.1776 0.2285 0.0075  -0.0228 -0.0063 126 THR   C O   
2011 C  CB  . THR   B 120 ? 0.2417 0.2228 0.2857 0.0125  -0.0237 -0.0065 126 THR   C CB  
2012 O  OG1 . THR   B 120 ? 0.2641 0.2505 0.3107 0.0114  -0.0231 -0.0045 126 THR   C OG1 
2013 C  CG2 . THR   B 120 ? 0.2488 0.2286 0.2964 0.0131  -0.0262 -0.0053 126 THR   C CG2 
2014 N  N   . GLY   B 121 ? 0.2275 0.2057 0.2584 0.0103  -0.0188 -0.0101 127 GLY   C N   
2015 C  CA  . GLY   B 121 ? 0.2506 0.2309 0.2780 0.0085  -0.0156 -0.0104 127 GLY   C CA  
2016 C  C   . GLY   B 121 ? 0.2653 0.2467 0.2937 0.0098  -0.0110 -0.0133 127 GLY   C C   
2017 O  O   . GLY   B 121 ? 0.2559 0.2351 0.2864 0.0122  -0.0106 -0.0155 127 GLY   C O   
2018 N  N   . GLY   B 122 ? 0.2820 0.2669 0.3090 0.0080  -0.0072 -0.0137 128 GLY   C N   
2019 C  CA  . GLY   B 122 ? 0.2974 0.2840 0.3253 0.0088  -0.0016 -0.0171 128 GLY   C CA  
2020 C  C   . GLY   B 122 ? 0.3027 0.2973 0.3363 0.0075  0.0022  -0.0165 128 GLY   C C   
2021 O  O   . GLY   B 122 ? 0.2862 0.2856 0.3262 0.0073  -0.0001 -0.0134 128 GLY   C O   
2022 N  N   . ASN   B 123 ? 0.3140 0.3101 0.3450 0.0064  0.0083  -0.0195 129 ASN   C N   
2023 C  CA  . ASN   B 123 ? 0.3168 0.3213 0.3539 0.0047  0.0128  -0.0194 129 ASN   C CA  
2024 C  C   . ASN   B 123 ? 0.3158 0.3221 0.3505 0.0009  0.0104  -0.0152 129 ASN   C C   
2025 O  O   . ASN   B 123 ? 0.3211 0.3353 0.3653 0.0006  0.0111  -0.0137 129 ASN   C O   
2026 C  CB  . ASN   B 123 ? 0.3462 0.3587 0.3997 0.0088  0.0140  -0.0202 129 ASN   C CB  
2027 C  CG  . ASN   B 123 ? 0.4212 0.4320 0.4781 0.0126  0.0172  -0.0248 129 ASN   C CG  
2028 O  OD1 . ASN   B 123 ? 0.4548 0.4637 0.5057 0.0116  0.0228  -0.0288 129 ASN   C OD1 
2029 N  ND2 . ASN   B 123 ? 0.4613 0.4720 0.5271 0.0169  0.0135  -0.0243 129 ASN   C ND2 
2030 N  N   . GLY   B 124 ? 0.3015 0.3004 0.3242 -0.0019 0.0070  -0.0134 130 GLY   C N   
2031 C  CA  . GLY   B 124 ? 0.2822 0.2814 0.3023 -0.0053 0.0043  -0.0097 130 GLY   C CA  
2032 C  C   . GLY   B 124 ? 0.2457 0.2474 0.2736 -0.0037 -0.0007 -0.0069 130 GLY   C C   
2033 O  O   . GLY   B 124 ? 0.2567 0.2601 0.2847 -0.0063 -0.0023 -0.0043 130 GLY   C O   
2034 N  N   . LEU   B 125 ? 0.2149 0.2160 0.2481 0.0001  -0.0034 -0.0073 131 LEU   C N   
2035 C  CA  . LEU   B 125 ? 0.2219 0.2243 0.2604 0.0012  -0.0080 -0.0048 131 LEU   C CA  
2036 C  C   . LEU   B 125 ? 0.2280 0.2231 0.2609 0.0022  -0.0118 -0.0049 131 LEU   C C   
2037 O  O   . LEU   B 125 ? 0.2596 0.2503 0.2885 0.0035  -0.0112 -0.0070 131 LEU   C O   
2038 C  CB  . LEU   B 125 ? 0.2336 0.2419 0.2839 0.0045  -0.0079 -0.0049 131 LEU   C CB  
2039 C  CG  . LEU   B 125 ? 0.2619 0.2786 0.3206 0.0040  -0.0042 -0.0051 131 LEU   C CG  
2040 C  CD1 . LEU   B 125 ? 0.2753 0.2965 0.3457 0.0080  -0.0036 -0.0063 131 LEU   C CD1 
2041 C  CD2 . LEU   B 125 ? 0.2588 0.2796 0.3202 0.0012  -0.0067 -0.0019 131 LEU   C CD2 
2042 N  N   . VAL   B 126 ? 0.1783 0.1722 0.2110 0.0014  -0.0156 -0.0028 132 VAL   C N   
2043 C  CA  . VAL   B 126 ? 0.1906 0.1792 0.2205 0.0023  -0.0191 -0.0028 132 VAL   C CA  
2044 C  C   . VAL   B 126 ? 0.1852 0.1766 0.2217 0.0035  -0.0211 -0.0016 132 VAL   C C   
2045 O  O   . VAL   B 126 ? 0.1915 0.1868 0.2313 0.0022  -0.0216 0.0002  132 VAL   C O   
2046 C  CB  . VAL   B 126 ? 0.2188 0.2025 0.2418 0.0001  -0.0214 -0.0021 132 VAL   C CB  
2047 C  CG1 . VAL   B 126 ? 0.2442 0.2301 0.2678 -0.0023 -0.0218 -0.0001 132 VAL   C CG1 
2048 C  CG2 . VAL   B 126 ? 0.2173 0.1967 0.2399 0.0013  -0.0249 -0.0024 132 VAL   C CG2 
2049 N  N   . GLY   B 127 ? 0.1750 0.1639 0.2127 0.0054  -0.0227 -0.0023 133 GLY   C N   
2050 C  CA  . GLY   B 127 ? 0.1752 0.1658 0.2176 0.0058  -0.0246 -0.0009 133 GLY   C CA  
2051 C  C   . GLY   B 127 ? 0.1782 0.1654 0.2182 0.0050  -0.0269 -0.0009 133 GLY   C C   
2052 O  O   . GLY   B 127 ? 0.1799 0.1631 0.2168 0.0055  -0.0275 -0.0023 133 GLY   C O   
2053 N  N   . PHE   B 128 ? 0.1658 0.1546 0.2071 0.0036  -0.0279 0.0005  134 PHE   C N   
2054 C  CA  . PHE   B 128 ? 0.1692 0.1557 0.2092 0.0026  -0.0292 -0.0001 134 PHE   C CA  
2055 C  C   . PHE   B 128 ? 0.1666 0.1539 0.2090 0.0022  -0.0298 0.0009  134 PHE   C C   
2056 O  O   . PHE   B 128 ? 0.1692 0.1591 0.2130 0.0013  -0.0301 0.0027  134 PHE   C O   
2057 C  CB  . PHE   B 128 ? 0.1713 0.1581 0.2094 0.0006  -0.0293 0.0002  134 PHE   C CB  
2058 C  CG  . PHE   B 128 ? 0.1724 0.1580 0.2075 0.0002  -0.0290 0.0001  134 PHE   C CG  
2059 C  CD1 . PHE   B 128 ? 0.1701 0.1515 0.2024 0.0005  -0.0300 -0.0011 134 PHE   C CD1 
2060 C  CD2 . PHE   B 128 ? 0.1872 0.1758 0.2223 -0.0010 -0.0279 0.0013  134 PHE   C CD2 
2061 C  CE1 . PHE   B 128 ? 0.1806 0.1600 0.2088 -0.0005 -0.0301 -0.0007 134 PHE   C CE1 
2062 C  CE2 . PHE   B 128 ? 0.1896 0.1768 0.2212 -0.0021 -0.0274 0.0014  134 PHE   C CE2 
2063 C  CZ  . PHE   B 128 ? 0.1929 0.1751 0.2204 -0.0020 -0.0285 0.0005  134 PHE   C CZ  
2064 N  N   . ALA   B 129 ? 0.1539 0.1390 0.1967 0.0024  -0.0303 -0.0002 135 ALA   C N   
2065 C  CA  . ALA   B 129 ? 0.1524 0.1377 0.1963 0.0011  -0.0307 0.0008  135 ALA   C CA  
2066 C  C   . ALA   B 129 ? 0.1550 0.1412 0.1973 -0.0015 -0.0300 0.0005  135 ALA   C C   
2067 O  O   . ALA   B 129 ? 0.1508 0.1362 0.1933 -0.0016 -0.0294 -0.0015 135 ALA   C O   
2068 C  CB  . ALA   B 129 ? 0.1640 0.1467 0.2091 0.0017  -0.0311 -0.0005 135 ALA   C CB  
2069 N  N   . ASP   B 130 ? 0.1589 0.1466 0.1999 -0.0035 -0.0302 0.0024  136 ASP   C N   
2070 C  CA  . ASP   B 130 ? 0.1726 0.1606 0.2108 -0.0064 -0.0292 0.0018  136 ASP   C CA  
2071 C  C   . ASP   B 130 ? 0.1783 0.1653 0.2164 -0.0080 -0.0278 0.0003  136 ASP   C C   
2072 O  O   . ASP   B 130 ? 0.1826 0.1689 0.2214 -0.0083 -0.0282 0.0014  136 ASP   C O   
2073 C  CB  . ASP   B 130 ? 0.1799 0.1691 0.2156 -0.0088 -0.0305 0.0046  136 ASP   C CB  
2074 C  CG  . ASP   B 130 ? 0.2709 0.2598 0.3022 -0.0122 -0.0296 0.0038  136 ASP   C CG  
2075 O  OD1 . ASP   B 130 ? 0.2638 0.2525 0.2948 -0.0120 -0.0286 0.0017  136 ASP   C OD1 
2076 O  OD2 . ASP   B 130 ? 0.3086 0.2969 0.3362 -0.0154 -0.0300 0.0052  136 ASP   C OD2 
2077 N  N   . VAL   B 131 ? 0.1700 0.1570 0.2074 -0.0094 -0.0258 -0.0022 137 VAL   C N   
2078 C  CA  . VAL   B 131 ? 0.1671 0.1542 0.2051 -0.0114 -0.0235 -0.0041 137 VAL   C CA  
2079 C  C   . VAL   B 131 ? 0.1814 0.1685 0.2146 -0.0152 -0.0213 -0.0051 137 VAL   C C   
2080 O  O   . VAL   B 131 ? 0.1934 0.1809 0.2264 -0.0174 -0.0183 -0.0072 137 VAL   C O   
2081 C  CB  . VAL   B 131 ? 0.1852 0.1726 0.2289 -0.0094 -0.0225 -0.0073 137 VAL   C CB  
2082 C  CG1 . VAL   B 131 ? 0.1845 0.1712 0.2315 -0.0066 -0.0248 -0.0065 137 VAL   C CG1 
2083 C  CG2 . VAL   B 131 ? 0.1810 0.1679 0.2257 -0.0081 -0.0224 -0.0095 137 VAL   C CG2 
2084 N  N   . ARG   B 132 ? 0.1744 0.1611 0.2036 -0.0161 -0.0225 -0.0039 138 ARG   C N   
2085 C  CA  . ARG   B 132 ? 0.1630 0.1489 0.1869 -0.0197 -0.0207 -0.0053 138 ARG   C CA  
2086 C  C   . ARG   B 132 ? 0.1872 0.1723 0.2050 -0.0242 -0.0197 -0.0039 138 ARG   C C   
2087 O  O   . ARG   B 132 ? 0.2121 0.1962 0.2250 -0.0277 -0.0169 -0.0062 138 ARG   C O   
2088 C  CB  . ARG   B 132 ? 0.1610 0.1465 0.1821 -0.0200 -0.0228 -0.0040 138 ARG   C CB  
2089 C  CG  . ARG   B 132 ? 0.1645 0.1497 0.1898 -0.0166 -0.0233 -0.0055 138 ARG   C CG  
2090 C  CD  . ARG   B 132 ? 0.1636 0.1488 0.1863 -0.0176 -0.0254 -0.0038 138 ARG   C CD  
2091 N  NE  . ARG   B 132 ? 0.1623 0.1498 0.1864 -0.0166 -0.0280 0.0000  138 ARG   C NE  
2092 C  CZ  . ARG   B 132 ? 0.1893 0.1781 0.2133 -0.0170 -0.0299 0.0020  138 ARG   C CZ  
2093 N  NH1 . ARG   B 132 ? 0.1950 0.1826 0.2164 -0.0189 -0.0300 0.0011  138 ARG   C NH1 
2094 N  NH2 . ARG   B 132 ? 0.1751 0.1666 0.2024 -0.0155 -0.0318 0.0048  138 ARG   C NH2 
2095 N  N   . ASP   B 133 ? 0.1877 0.1726 0.2052 -0.0243 -0.0221 -0.0003 139 ASP   C N   
2096 C  CA  . ASP   B 133 ? 0.2020 0.1852 0.2130 -0.0290 -0.0220 0.0018  139 ASP   C CA  
2097 C  C   . ASP   B 133 ? 0.2093 0.1926 0.2214 -0.0306 -0.0183 -0.0002 139 ASP   C C   
2098 O  O   . ASP   B 133 ? 0.2331 0.2145 0.2385 -0.0354 -0.0173 0.0011  139 ASP   C O   
2099 C  CB  . ASP   B 133 ? 0.2336 0.2158 0.2442 -0.0286 -0.0268 0.0069  139 ASP   C CB  
2100 C  CG  . ASP   B 133 ? 0.2828 0.2656 0.3005 -0.0245 -0.0279 0.0077  139 ASP   C CG  
2101 O  OD1 . ASP   B 133 ? 0.2782 0.2626 0.3018 -0.0205 -0.0271 0.0053  139 ASP   C OD1 
2102 O  OD2 . ASP   B 133 ? 0.2929 0.2735 0.3095 -0.0257 -0.0299 0.0107  139 ASP   C OD2 
2103 N  N   . LEU   B 134 ? 0.1948 0.1801 0.2149 -0.0271 -0.0165 -0.0032 140 LEU   C N   
2104 C  CA  . LEU   B 134 ? 0.1970 0.1832 0.2199 -0.0287 -0.0132 -0.0052 140 LEU   C CA  
2105 C  C   . LEU   B 134 ? 0.2103 0.1979 0.2322 -0.0313 -0.0078 -0.0099 140 LEU   C C   
2106 O  O   . LEU   B 134 ? 0.2187 0.2086 0.2483 -0.0286 -0.0056 -0.0140 140 LEU   C O   
2107 C  CB  . LEU   B 134 ? 0.1946 0.1824 0.2270 -0.0239 -0.0143 -0.0062 140 LEU   C CB  
2108 C  CG  . LEU   B 134 ? 0.2189 0.2052 0.2523 -0.0210 -0.0190 -0.0024 140 LEU   C CG  
2109 C  CD1 . LEU   B 134 ? 0.2236 0.2107 0.2647 -0.0168 -0.0200 -0.0040 140 LEU   C CD1 
2110 C  CD2 . LEU   B 134 ? 0.2218 0.2056 0.2509 -0.0240 -0.0204 0.0013  140 LEU   C CD2 
2111 N  N   . LEU   B 135 ? 0.2087 0.1944 0.2211 -0.0367 -0.0059 -0.0094 141 LEU   C N   
2112 C  CA  . LEU   B 135 ? 0.2217 0.2081 0.2318 -0.0394 -0.0003 -0.0145 141 LEU   C CA  
2113 C  C   . LEU   B 135 ? 0.2342 0.2239 0.2510 -0.0402 0.0051  -0.0186 141 LEU   C C   
2114 O  O   . LEU   B 135 ? 0.2569 0.2485 0.2779 -0.0396 0.0096  -0.0240 141 LEU   C O   
2115 C  CB  . LEU   B 135 ? 0.2337 0.2166 0.2303 -0.0458 0.0006  -0.0133 141 LEU   C CB  
2116 C  CG  . LEU   B 135 ? 0.2502 0.2302 0.2405 -0.0459 -0.0056 -0.0084 141 LEU   C CG  
2117 C  CD1 . LEU   B 135 ? 0.2663 0.2426 0.2430 -0.0525 -0.0049 -0.0078 141 LEU   C CD1 
2118 C  CD2 . LEU   B 135 ? 0.2433 0.2242 0.2390 -0.0409 -0.0079 -0.0096 141 LEU   C CD2 
2119 N  N   . TRP   B 136 ? 0.2343 0.2247 0.2531 -0.0413 0.0047  -0.0162 142 TRP   C N   
2120 C  CA  . TRP   B 136 ? 0.2436 0.2378 0.2694 -0.0427 0.0097  -0.0196 142 TRP   C CA  
2121 C  C   . TRP   B 136 ? 0.2654 0.2638 0.3058 -0.0368 0.0098  -0.0234 142 TRP   C C   
2122 O  O   . TRP   B 136 ? 0.2728 0.2754 0.3212 -0.0376 0.0144  -0.0274 142 TRP   C O   
2123 C  CB  . TRP   B 136 ? 0.2485 0.2415 0.2724 -0.0456 0.0082  -0.0154 142 TRP   C CB  
2124 C  CG  . TRP   B 136 ? 0.2527 0.2439 0.2796 -0.0412 0.0014  -0.0109 142 TRP   C CG  
2125 C  CD1 . TRP   B 136 ? 0.2668 0.2537 0.2868 -0.0411 -0.0039 -0.0058 142 TRP   C CD1 
2126 C  CD2 . TRP   B 136 ? 0.2421 0.2355 0.2801 -0.0365 -0.0008 -0.0116 142 TRP   C CD2 
2127 N  NE1 . TRP   B 136 ? 0.2664 0.2528 0.2926 -0.0365 -0.0084 -0.0037 142 TRP   C NE1 
2128 C  CE2 . TRP   B 136 ? 0.2521 0.2420 0.2884 -0.0338 -0.0066 -0.0072 142 TRP   C CE2 
2129 C  CE3 . TRP   B 136 ? 0.2463 0.2442 0.2958 -0.0344 0.0016  -0.0157 142 TRP   C CE3 
2130 C  CZ2 . TRP   B 136 ? 0.2589 0.2492 0.3029 -0.0294 -0.0098 -0.0069 142 TRP   C CZ2 
2131 C  CZ3 . TRP   B 136 ? 0.2562 0.2544 0.3134 -0.0304 -0.0024 -0.0148 142 TRP   C CZ3 
2132 C  CH2 . TRP   B 136 ? 0.2568 0.2509 0.3104 -0.0282 -0.0078 -0.0105 142 TRP   C CH2 
2133 N  N   . LEU   B 137 ? 0.2612 0.2584 0.3050 -0.0314 0.0049  -0.0223 143 LEU   C N   
2134 C  CA  . LEU   B 137 ? 0.2698 0.2699 0.3262 -0.0262 0.0040  -0.0254 143 LEU   C CA  
2135 C  C   . LEU   B 137 ? 0.3291 0.3315 0.3907 -0.0259 0.0090  -0.0315 143 LEU   C C   
2136 O  O   . LEU   B 137 ? 0.3366 0.3424 0.4104 -0.0229 0.0096  -0.0348 143 LEU   C O   
2137 C  CB  . LEU   B 137 ? 0.2467 0.2441 0.3032 -0.0213 -0.0019 -0.0230 143 LEU   C CB  
2138 C  CG  . LEU   B 137 ? 0.2407 0.2364 0.2960 -0.0197 -0.0069 -0.0183 143 LEU   C CG  
2139 C  CD1 . LEU   B 137 ? 0.2374 0.2307 0.2917 -0.0157 -0.0114 -0.0166 143 LEU   C CD1 
2140 C  CD2 . LEU   B 137 ? 0.2361 0.2341 0.3006 -0.0183 -0.0076 -0.0191 143 LEU   C CD2 
2141 N  N   . ASP   B 138 ? 0.3679 0.3681 0.4205 -0.0290 0.0119  -0.0329 144 ASP   C N   
2142 C  CA  . ASP   B 138 ? 0.4257 0.4265 0.4804 -0.0293 0.0169  -0.0388 144 ASP   C CA  
2143 C  C   . ASP   B 138 ? 0.4653 0.4698 0.5222 -0.0334 0.0247  -0.0435 144 ASP   C C   
2144 O  O   . ASP   B 138 ? 0.4785 0.4838 0.5383 -0.0334 0.0296  -0.0493 144 ASP   C O   
2145 C  CB  . ASP   B 138 ? 0.4688 0.4647 0.5102 -0.0320 0.0167  -0.0381 144 ASP   C CB  
2146 C  CG  . ASP   B 138 ? 0.5292 0.5218 0.5694 -0.0282 0.0108  -0.0355 144 ASP   C CG  
2147 O  OD1 . ASP   B 138 ? 0.5338 0.5273 0.5836 -0.0230 0.0077  -0.0359 144 ASP   C OD1 
2148 O  OD2 . ASP   B 138 ? 0.5906 0.5796 0.6198 -0.0308 0.0090  -0.0331 144 ASP   C OD2 
2149 N  N   . GLU   B 139 ? 0.4854 0.4916 0.5397 -0.0375 0.0264  -0.0412 145 GLU   C N   
2150 C  CA  . GLU   B 139 ? 0.5116 0.5218 0.5674 -0.0424 0.0346  -0.0456 145 GLU   C CA  
2151 C  C   . GLU   B 139 ? 0.5158 0.5315 0.5839 -0.0419 0.0353  -0.0456 145 GLU   C C   
2152 O  O   . GLU   B 139 ? 0.5237 0.5384 0.5928 -0.0402 0.0294  -0.0406 145 GLU   C O   
2153 C  CB  . GLU   B 139 ? 0.5669 0.5733 0.6054 -0.0502 0.0374  -0.0433 145 GLU   C CB  
2154 C  CG  . GLU   B 139 ? 0.6570 0.6596 0.6870 -0.0519 0.0312  -0.0355 145 GLU   C CG  
2155 C  CD  . GLU   B 139 ? 0.7797 0.7761 0.7921 -0.0567 0.0295  -0.0319 145 GLU   C CD  
2156 O  OE1 . GLU   B 139 ? 0.7982 0.7920 0.8007 -0.0625 0.0295  -0.0279 145 GLU   C OE1 
2157 O  OE2 . GLU   B 139 ? 0.8181 0.8118 0.8266 -0.0549 0.0276  -0.0327 145 GLU   C OE2 
2158 N  N1  . A1B4B C .   ? 0.2233 0.2010 0.2956 -0.0083 -0.0083 0.0185  201 A1B4B A N1  
2159 C  C4  . A1B4B C .   ? 0.2206 0.1932 0.2895 -0.0071 -0.0083 0.0223  201 A1B4B A C4  
2160 C  C5  . A1B4B C .   ? 0.2383 0.2181 0.3056 -0.0069 -0.0076 0.0185  201 A1B4B A C5  
2161 C  C6  . A1B4B C .   ? 0.2791 0.2551 0.3353 -0.0039 -0.0071 0.0222  201 A1B4B A C6  
2162 C  C7  . A1B4B C .   ? 0.3195 0.2974 0.3705 -0.0021 -0.0056 0.0218  201 A1B4B A C7  
2163 C  C8  . A1B4B C .   ? 0.3301 0.3084 0.3825 -0.0015 0.0000  0.0248  201 A1B4B A C8  
2164 C  C10 . A1B4B C .   ? 0.3489 0.3295 0.3904 0.0022  -0.0019 0.0214  201 A1B4B A C10 
2165 C  C13 . A1B4B C .   ? 0.2103 0.1907 0.2913 -0.0107 -0.0096 0.0141  201 A1B4B A C13 
2166 BR BR  . A1B4B C .   ? 0.4302 0.4080 0.4740 -0.0016 -0.0154 0.0157  201 A1B4B A BR  
2167 C  C12 . A1B4B C .   ? 0.3574 0.3361 0.4023 -0.0007 -0.0091 0.0190  201 A1B4B A C12 
2168 C  C11 . A1B4B C .   ? 0.3511 0.3308 0.3911 0.0013  -0.0074 0.0187  201 A1B4B A C11 
2169 F  F1  . A1B4B C .   ? 0.3675 0.3494 0.4049 0.0045  0.0004  0.0211  201 A1B4B A F1  
2170 C  C9  . A1B4B C .   ? 0.3444 0.3244 0.3921 0.0007  0.0019  0.0245  201 A1B4B A C9  
2171 F  F   . A1B4B C .   ? 0.3572 0.3380 0.4072 0.0013  0.0082  0.0275  201 A1B4B A F   
2172 O  O1  . A1B4B C .   ? 0.2198 0.2041 0.2908 -0.0075 -0.0077 0.0154  201 A1B4B A O1  
2173 C  C3  . A1B4B C .   ? 0.2195 0.1914 0.2882 -0.0071 -0.0126 0.0204  201 A1B4B A C3  
2174 C  C2  . A1B4B C .   ? 0.2208 0.1949 0.2982 -0.0095 -0.0129 0.0162  201 A1B4B A C2  
2175 C  C1  . A1B4B C .   ? 0.2106 0.1895 0.2893 -0.0103 -0.0133 0.0123  201 A1B4B A C1  
2176 C  C   . A1B4B C .   ? 0.2099 0.1907 0.2954 -0.0121 -0.0144 0.0077  201 A1B4B A C   
2177 O  O   . A1B4B C .   ? 0.2114 0.1918 0.3050 -0.0140 -0.0125 0.0068  201 A1B4B A O   
2178 N  N   . A1B4B C .   ? 0.2030 0.1857 0.2851 -0.0113 -0.0172 0.0046  201 A1B4B A N   
2184 N  N1  . A1B4B F .   ? 0.2293 0.1889 0.2578 0.0144  -0.0251 -0.0159 201 A1B4B C N1  
2185 C  C4  . A1B4B F .   ? 0.2334 0.1865 0.2574 0.0138  -0.0275 -0.0177 201 A1B4B C C4  
2186 C  C5  . A1B4B F .   ? 0.2592 0.2214 0.2845 0.0135  -0.0226 -0.0160 201 A1B4B C C5  
2187 C  C6  . A1B4B F .   ? 0.3061 0.2635 0.3211 0.0113  -0.0226 -0.0176 201 A1B4B C C6  
2188 C  C7  . A1B4B F .   ? 0.3582 0.3184 0.3694 0.0098  -0.0193 -0.0174 201 A1B4B C C7  
2189 C  C8  . A1B4B F .   ? 0.3704 0.3304 0.3786 0.0100  -0.0145 -0.0203 201 A1B4B C C8  
2190 C  C10 . A1B4B F .   ? 0.3959 0.3604 0.3992 0.0058  -0.0130 -0.0169 201 A1B4B C C10 
2191 C  C13 . A1B4B F .   ? 0.1982 0.1612 0.2349 0.0156  -0.0260 -0.0136 201 A1B4B C C13 
2192 BR BR  . A1B4B F .   ? 0.4664 0.4291 0.4807 0.0075  -0.0262 -0.0117 201 A1B4B C BR  
2193 C  C12 . A1B4B F .   ? 0.3984 0.3607 0.4084 0.0078  -0.0207 -0.0146 201 A1B4B C C12 
2194 C  C11 . A1B4B F .   ? 0.3946 0.3587 0.4005 0.0058  -0.0179 -0.0143 201 A1B4B C C11 
2195 F  F1  . A1B4B F .   ? 0.4004 0.3680 0.4012 0.0036  -0.0094 -0.0166 201 A1B4B C F1  
2196 C  C9  . A1B4B F .   ? 0.3933 0.3559 0.3978 0.0079  -0.0111 -0.0201 201 A1B4B C C9  
2197 F  F   . A1B4B F .   ? 0.4171 0.3807 0.4200 0.0080  -0.0054 -0.0233 201 A1B4B C F   
2198 O  O1  . A1B4B F .   ? 0.2376 0.2054 0.2675 0.0139  -0.0207 -0.0145 201 A1B4B C O1  
2199 C  C3  . A1B4B F .   ? 0.2185 0.1714 0.2451 0.0126  -0.0316 -0.0156 201 A1B4B C C3  
2200 C  C2  . A1B4B F .   ? 0.2032 0.1597 0.2377 0.0134  -0.0318 -0.0133 201 A1B4B C C2  
2201 C  C1  . A1B4B F .   ? 0.1983 0.1608 0.2359 0.0139  -0.0295 -0.0115 201 A1B4B C C1  
2202 C  C   . A1B4B F .   ? 0.2035 0.1688 0.2476 0.0143  -0.0304 -0.0090 201 A1B4B C C   
2203 O  O   . A1B4B F .   ? 0.1918 0.1554 0.2395 0.0161  -0.0305 -0.0092 201 A1B4B C O   
2204 N  N   . A1B4B F .   ? 0.2064 0.1754 0.2516 0.0127  -0.0310 -0.0066 201 A1B4B C N   
# 
