data_7I7U
# 
_entry.id   7I7U 
# 
_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   7I7U         pdb_00007i7u 10.2210/pdb7i7u/pdb 
WWPDB D_1001408425 ?            ?                   
# 
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                        7I7U 
_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-[(1S)-2-(methylamino)-1-(3-methylphenyl)-2-oxoethyl]-5-oxopyrrolidine-3-carboxamide' 289.330   1   ? ? ? 
? 
3 non-polymer syn 'ZINC ION'                                                                                   65.409    2   ? ? ? 
? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                         78.133    1   ? ? ? 
? 
5 water       nat water                                                                                        18.015    383 ? ? ? 
? 
# 
_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-[(1S)-2-(methylamino)-1-(3-methylphenyl)-2-oxoethyl]-5-oxopyrrolidine-3-carboxamide' A1B53 
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 
A1B53 non-polymer         . '(3S)-1-[(1S)-2-(methylamino)-1-(3-methylphenyl)-2-oxoethyl]-5-oxopyrrolidine-3-carboxamide' ? 
'C15 H19 N3 O3'  289.330 
ALA   'L-peptide linking' y ALANINE                                                                                      ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                     ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                   ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                              ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                     ? 
'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                         ? 
'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                                    ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                              ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                      ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                    ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                        ? 'H2 O' 
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                   ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                      ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                       ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                   ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                      ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                       ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                    ? 
'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                   ? 
'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                     ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                       ? 
'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                                                   ? 'Zn 2' 
65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 146 GLU GLU C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B53 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B53 
_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 A1B53 1   201 201 A1B53 LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 3 ZN    1   201 1   ZN    ZN  C . 
F 4 DMS   1   202 1   DMS   DMS C . 
G 5 HOH   1   301 304 HOH   HOH A . 
G 5 HOH   2   302 151 HOH   HOH A . 
G 5 HOH   3   303 287 HOH   HOH A . 
G 5 HOH   4   304 72  HOH   HOH A . 
G 5 HOH   5   305 228 HOH   HOH A . 
G 5 HOH   6   306 251 HOH   HOH A . 
G 5 HOH   7   307 233 HOH   HOH A . 
G 5 HOH   8   308 295 HOH   HOH A . 
G 5 HOH   9   309 184 HOH   HOH A . 
G 5 HOH   10  310 158 HOH   HOH A . 
G 5 HOH   11  311 102 HOH   HOH A . 
G 5 HOH   12  312 349 HOH   HOH A . 
G 5 HOH   13  313 74  HOH   HOH A . 
G 5 HOH   14  314 113 HOH   HOH A . 
G 5 HOH   15  315 146 HOH   HOH A . 
G 5 HOH   16  316 234 HOH   HOH A . 
G 5 HOH   17  317 313 HOH   HOH A . 
G 5 HOH   18  318 377 HOH   HOH A . 
G 5 HOH   19  319 96  HOH   HOH A . 
G 5 HOH   20  320 213 HOH   HOH A . 
G 5 HOH   21  321 132 HOH   HOH A . 
G 5 HOH   22  322 156 HOH   HOH A . 
G 5 HOH   23  323 76  HOH   HOH A . 
G 5 HOH   24  324 225 HOH   HOH A . 
G 5 HOH   25  325 135 HOH   HOH A . 
G 5 HOH   26  326 217 HOH   HOH A . 
G 5 HOH   27  327 223 HOH   HOH A . 
G 5 HOH   28  328 30  HOH   HOH A . 
G 5 HOH   29  329 299 HOH   HOH A . 
G 5 HOH   30  330 200 HOH   HOH A . 
G 5 HOH   31  331 174 HOH   HOH A . 
G 5 HOH   32  332 81  HOH   HOH A . 
G 5 HOH   33  333 143 HOH   HOH A . 
G 5 HOH   34  334 205 HOH   HOH A . 
G 5 HOH   35  335 254 HOH   HOH A . 
G 5 HOH   36  336 16  HOH   HOH A . 
G 5 HOH   37  337 9   HOH   HOH A . 
G 5 HOH   38  338 94  HOH   HOH A . 
G 5 HOH   39  339 321 HOH   HOH A . 
G 5 HOH   40  340 253 HOH   HOH A . 
G 5 HOH   41  341 297 HOH   HOH A . 
G 5 HOH   42  342 193 HOH   HOH A . 
G 5 HOH   43  343 303 HOH   HOH A . 
G 5 HOH   44  344 34  HOH   HOH A . 
G 5 HOH   45  345 131 HOH   HOH A . 
G 5 HOH   46  346 67  HOH   HOH A . 
G 5 HOH   47  347 289 HOH   HOH A . 
G 5 HOH   48  348 23  HOH   HOH A . 
G 5 HOH   49  349 238 HOH   HOH A . 
G 5 HOH   50  350 61  HOH   HOH A . 
G 5 HOH   51  351 3   HOH   HOH A . 
G 5 HOH   52  352 98  HOH   HOH A . 
G 5 HOH   53  353 56  HOH   HOH A . 
G 5 HOH   54  354 90  HOH   HOH A . 
G 5 HOH   55  355 216 HOH   HOH A . 
G 5 HOH   56  356 137 HOH   HOH A . 
G 5 HOH   57  357 372 HOH   HOH A . 
G 5 HOH   58  358 49  HOH   HOH A . 
G 5 HOH   59  359 350 HOH   HOH A . 
G 5 HOH   60  360 219 HOH   HOH A . 
G 5 HOH   61  361 86  HOH   HOH A . 
G 5 HOH   62  362 110 HOH   HOH A . 
G 5 HOH   63  363 248 HOH   HOH A . 
G 5 HOH   64  364 5   HOH   HOH A . 
G 5 HOH   65  365 319 HOH   HOH A . 
G 5 HOH   66  366 26  HOH   HOH A . 
G 5 HOH   67  367 371 HOH   HOH A . 
G 5 HOH   68  368 116 HOH   HOH A . 
G 5 HOH   69  369 52  HOH   HOH A . 
G 5 HOH   70  370 329 HOH   HOH A . 
G 5 HOH   71  371 302 HOH   HOH A . 
G 5 HOH   72  372 256 HOH   HOH A . 
G 5 HOH   73  373 11  HOH   HOH A . 
G 5 HOH   74  374 341 HOH   HOH A . 
G 5 HOH   75  375 160 HOH   HOH A . 
G 5 HOH   76  376 39  HOH   HOH A . 
G 5 HOH   77  377 123 HOH   HOH A . 
G 5 HOH   78  378 195 HOH   HOH A . 
G 5 HOH   79  379 27  HOH   HOH A . 
G 5 HOH   80  380 159 HOH   HOH A . 
G 5 HOH   81  381 44  HOH   HOH A . 
G 5 HOH   82  382 301 HOH   HOH A . 
G 5 HOH   83  383 328 HOH   HOH A . 
G 5 HOH   84  384 43  HOH   HOH A . 
G 5 HOH   85  385 250 HOH   HOH A . 
G 5 HOH   86  386 262 HOH   HOH A . 
G 5 HOH   87  387 104 HOH   HOH A . 
G 5 HOH   88  388 181 HOH   HOH A . 
G 5 HOH   89  389 70  HOH   HOH A . 
G 5 HOH   90  390 29  HOH   HOH A . 
G 5 HOH   91  391 323 HOH   HOH A . 
G 5 HOH   92  392 294 HOH   HOH A . 
G 5 HOH   93  393 249 HOH   HOH A . 
G 5 HOH   94  394 114 HOH   HOH A . 
G 5 HOH   95  395 208 HOH   HOH A . 
G 5 HOH   96  396 21  HOH   HOH A . 
G 5 HOH   97  397 150 HOH   HOH A . 
G 5 HOH   98  398 286 HOH   HOH A . 
G 5 HOH   99  399 41  HOH   HOH A . 
G 5 HOH   100 400 79  HOH   HOH A . 
G 5 HOH   101 401 224 HOH   HOH A . 
G 5 HOH   102 402 170 HOH   HOH A . 
G 5 HOH   103 403 296 HOH   HOH A . 
G 5 HOH   104 404 107 HOH   HOH A . 
G 5 HOH   105 405 373 HOH   HOH A . 
G 5 HOH   106 406 164 HOH   HOH A . 
G 5 HOH   107 407 148 HOH   HOH A . 
G 5 HOH   108 408 53  HOH   HOH A . 
G 5 HOH   109 409 18  HOH   HOH A . 
G 5 HOH   110 410 202 HOH   HOH A . 
G 5 HOH   111 411 45  HOH   HOH A . 
G 5 HOH   112 412 149 HOH   HOH A . 
G 5 HOH   113 413 199 HOH   HOH A . 
G 5 HOH   114 414 171 HOH   HOH A . 
G 5 HOH   115 415 48  HOH   HOH A . 
G 5 HOH   116 416 140 HOH   HOH A . 
G 5 HOH   117 417 291 HOH   HOH A . 
G 5 HOH   118 418 145 HOH   HOH A . 
G 5 HOH   119 419 326 HOH   HOH A . 
G 5 HOH   120 420 242 HOH   HOH A . 
G 5 HOH   121 421 362 HOH   HOH A . 
G 5 HOH   122 422 154 HOH   HOH A . 
G 5 HOH   123 423 278 HOH   HOH A . 
G 5 HOH   124 424 10  HOH   HOH A . 
G 5 HOH   125 425 78  HOH   HOH A . 
G 5 HOH   126 426 130 HOH   HOH A . 
G 5 HOH   127 427 51  HOH   HOH A . 
G 5 HOH   128 428 138 HOH   HOH A . 
G 5 HOH   129 429 57  HOH   HOH A . 
G 5 HOH   130 430 176 HOH   HOH A . 
G 5 HOH   131 431 259 HOH   HOH A . 
G 5 HOH   132 432 231 HOH   HOH A . 
G 5 HOH   133 433 269 HOH   HOH A . 
G 5 HOH   134 434 14  HOH   HOH A . 
G 5 HOH   135 435 147 HOH   HOH A . 
G 5 HOH   136 436 331 HOH   HOH A . 
G 5 HOH   137 437 13  HOH   HOH A . 
G 5 HOH   138 438 338 HOH   HOH A . 
G 5 HOH   139 439 305 HOH   HOH A . 
G 5 HOH   140 440 367 HOH   HOH A . 
G 5 HOH   141 441 64  HOH   HOH A . 
G 5 HOH   142 442 197 HOH   HOH A . 
G 5 HOH   143 443 93  HOH   HOH A . 
G 5 HOH   144 444 4   HOH   HOH A . 
G 5 HOH   145 445 378 HOH   HOH A . 
G 5 HOH   146 446 142 HOH   HOH A . 
G 5 HOH   147 447 327 HOH   HOH A . 
G 5 HOH   148 448 201 HOH   HOH A . 
G 5 HOH   149 449 207 HOH   HOH A . 
G 5 HOH   150 450 80  HOH   HOH A . 
G 5 HOH   151 451 337 HOH   HOH A . 
G 5 HOH   152 452 71  HOH   HOH A . 
G 5 HOH   153 453 288 HOH   HOH A . 
G 5 HOH   154 454 366 HOH   HOH A . 
G 5 HOH   155 455 281 HOH   HOH A . 
G 5 HOH   156 456 344 HOH   HOH A . 
G 5 HOH   157 457 388 HOH   HOH A . 
G 5 HOH   158 458 279 HOH   HOH A . 
G 5 HOH   159 459 311 HOH   HOH A . 
G 5 HOH   160 460 309 HOH   HOH A . 
G 5 HOH   161 461 271 HOH   HOH A . 
G 5 HOH   162 462 275 HOH   HOH A . 
G 5 HOH   163 463 353 HOH   HOH A . 
G 5 HOH   164 464 352 HOH   HOH A . 
G 5 HOH   165 465 270 HOH   HOH A . 
G 5 HOH   166 466 379 HOH   HOH A . 
G 5 HOH   167 467 360 HOH   HOH A . 
G 5 HOH   168 468 383 HOH   HOH A . 
G 5 HOH   169 469 307 HOH   HOH A . 
G 5 HOH   170 470 385 HOH   HOH A . 
G 5 HOH   171 471 236 HOH   HOH A . 
G 5 HOH   172 472 173 HOH   HOH A . 
G 5 HOH   173 473 189 HOH   HOH A . 
G 5 HOH   174 474 277 HOH   HOH A . 
G 5 HOH   175 475 240 HOH   HOH A . 
G 5 HOH   176 476 252 HOH   HOH A . 
G 5 HOH   177 477 356 HOH   HOH A . 
G 5 HOH   178 478 99  HOH   HOH A . 
G 5 HOH   179 479 380 HOH   HOH A . 
G 5 HOH   180 480 222 HOH   HOH A . 
G 5 HOH   181 481 167 HOH   HOH A . 
G 5 HOH   182 482 115 HOH   HOH A . 
G 5 HOH   183 483 324 HOH   HOH A . 
G 5 HOH   184 484 255 HOH   HOH A . 
G 5 HOH   185 485 376 HOH   HOH A . 
G 5 HOH   186 486 283 HOH   HOH A . 
G 5 HOH   187 487 347 HOH   HOH A . 
G 5 HOH   188 488 267 HOH   HOH A . 
H 5 HOH   1   301 276 HOH   HOH C . 
H 5 HOH   2   302 180 HOH   HOH C . 
H 5 HOH   3   303 194 HOH   HOH C . 
H 5 HOH   4   304 91  HOH   HOH C . 
H 5 HOH   5   305 364 HOH   HOH C . 
H 5 HOH   6   306 192 HOH   HOH C . 
H 5 HOH   7   307 77  HOH   HOH C . 
H 5 HOH   8   308 340 HOH   HOH C . 
H 5 HOH   9   309 105 HOH   HOH C . 
H 5 HOH   10  310 310 HOH   HOH C . 
H 5 HOH   11  311 268 HOH   HOH C . 
H 5 HOH   12  312 75  HOH   HOH C . 
H 5 HOH   13  313 183 HOH   HOH C . 
H 5 HOH   14  314 36  HOH   HOH C . 
H 5 HOH   15  315 6   HOH   HOH C . 
H 5 HOH   16  316 315 HOH   HOH C . 
H 5 HOH   17  317 133 HOH   HOH C . 
H 5 HOH   18  318 237 HOH   HOH C . 
H 5 HOH   19  319 59  HOH   HOH C . 
H 5 HOH   20  320 54  HOH   HOH C . 
H 5 HOH   21  321 241 HOH   HOH C . 
H 5 HOH   22  322 155 HOH   HOH C . 
H 5 HOH   23  323 152 HOH   HOH C . 
H 5 HOH   24  324 139 HOH   HOH C . 
H 5 HOH   25  325 136 HOH   HOH C . 
H 5 HOH   26  326 232 HOH   HOH C . 
H 5 HOH   27  327 121 HOH   HOH C . 
H 5 HOH   28  328 273 HOH   HOH C . 
H 5 HOH   29  329 334 HOH   HOH C . 
H 5 HOH   30  330 168 HOH   HOH C . 
H 5 HOH   31  331 165 HOH   HOH C . 
H 5 HOH   32  332 88  HOH   HOH C . 
H 5 HOH   33  333 119 HOH   HOH C . 
H 5 HOH   34  334 258 HOH   HOH C . 
H 5 HOH   35  335 17  HOH   HOH C . 
H 5 HOH   36  336 111 HOH   HOH C . 
H 5 HOH   37  337 126 HOH   HOH C . 
H 5 HOH   38  338 212 HOH   HOH C . 
H 5 HOH   39  339 66  HOH   HOH C . 
H 5 HOH   40  340 68  HOH   HOH C . 
H 5 HOH   41  341 1   HOH   HOH C . 
H 5 HOH   42  342 60  HOH   HOH C . 
H 5 HOH   43  343 211 HOH   HOH C . 
H 5 HOH   44  344 55  HOH   HOH C . 
H 5 HOH   45  345 109 HOH   HOH C . 
H 5 HOH   46  346 129 HOH   HOH C . 
H 5 HOH   47  347 191 HOH   HOH C . 
H 5 HOH   48  348 19  HOH   HOH C . 
H 5 HOH   49  349 92  HOH   HOH C . 
H 5 HOH   50  350 46  HOH   HOH C . 
H 5 HOH   51  351 368 HOH   HOH C . 
H 5 HOH   52  352 227 HOH   HOH C . 
H 5 HOH   53  353 100 HOH   HOH C . 
H 5 HOH   54  354 63  HOH   HOH C . 
H 5 HOH   55  355 87  HOH   HOH C . 
H 5 HOH   56  356 20  HOH   HOH C . 
H 5 HOH   57  357 359 HOH   HOH C . 
H 5 HOH   58  358 33  HOH   HOH C . 
H 5 HOH   59  359 22  HOH   HOH C . 
H 5 HOH   60  360 124 HOH   HOH C . 
H 5 HOH   61  361 335 HOH   HOH C . 
H 5 HOH   62  362 162 HOH   HOH C . 
H 5 HOH   63  363 188 HOH   HOH C . 
H 5 HOH   64  364 127 HOH   HOH C . 
H 5 HOH   65  365 351 HOH   HOH C . 
H 5 HOH   66  366 330 HOH   HOH C . 
H 5 HOH   67  367 31  HOH   HOH C . 
H 5 HOH   68  368 177 HOH   HOH C . 
H 5 HOH   69  369 112 HOH   HOH C . 
H 5 HOH   70  370 365 HOH   HOH C . 
H 5 HOH   71  371 118 HOH   HOH C . 
H 5 HOH   72  372 220 HOH   HOH C . 
H 5 HOH   73  373 69  HOH   HOH C . 
H 5 HOH   74  374 179 HOH   HOH C . 
H 5 HOH   75  375 370 HOH   HOH C . 
H 5 HOH   76  376 185 HOH   HOH C . 
H 5 HOH   77  377 12  HOH   HOH C . 
H 5 HOH   78  378 246 HOH   HOH C . 
H 5 HOH   79  379 58  HOH   HOH C . 
H 5 HOH   80  380 263 HOH   HOH C . 
H 5 HOH   81  381 369 HOH   HOH C . 
H 5 HOH   82  382 8   HOH   HOH C . 
H 5 HOH   83  383 308 HOH   HOH C . 
H 5 HOH   84  384 203 HOH   HOH C . 
H 5 HOH   85  385 274 HOH   HOH C . 
H 5 HOH   86  386 339 HOH   HOH C . 
H 5 HOH   87  387 172 HOH   HOH C . 
H 5 HOH   88  388 40  HOH   HOH C . 
H 5 HOH   89  389 38  HOH   HOH C . 
H 5 HOH   90  390 42  HOH   HOH C . 
H 5 HOH   91  391 37  HOH   HOH C . 
H 5 HOH   92  392 209 HOH   HOH C . 
H 5 HOH   93  393 106 HOH   HOH C . 
H 5 HOH   94  394 117 HOH   HOH C . 
H 5 HOH   95  395 82  HOH   HOH C . 
H 5 HOH   96  396 300 HOH   HOH C . 
H 5 HOH   97  397 186 HOH   HOH C . 
H 5 HOH   98  398 85  HOH   HOH C . 
H 5 HOH   99  399 15  HOH   HOH C . 
H 5 HOH   100 400 153 HOH   HOH C . 
H 5 HOH   101 401 293 HOH   HOH C . 
H 5 HOH   102 402 2   HOH   HOH C . 
H 5 HOH   103 403 178 HOH   HOH C . 
H 5 HOH   104 404 247 HOH   HOH C . 
H 5 HOH   105 405 312 HOH   HOH C . 
H 5 HOH   106 406 73  HOH   HOH C . 
H 5 HOH   107 407 244 HOH   HOH C . 
H 5 HOH   108 408 65  HOH   HOH C . 
H 5 HOH   109 409 245 HOH   HOH C . 
H 5 HOH   110 410 290 HOH   HOH C . 
H 5 HOH   111 411 101 HOH   HOH C . 
H 5 HOH   112 412 318 HOH   HOH C . 
H 5 HOH   113 413 314 HOH   HOH C . 
H 5 HOH   114 414 320 HOH   HOH C . 
H 5 HOH   115 415 206 HOH   HOH C . 
H 5 HOH   116 416 24  HOH   HOH C . 
H 5 HOH   117 417 120 HOH   HOH C . 
H 5 HOH   118 418 322 HOH   HOH C . 
H 5 HOH   119 419 190 HOH   HOH C . 
H 5 HOH   120 420 214 HOH   HOH C . 
H 5 HOH   121 421 108 HOH   HOH C . 
H 5 HOH   122 422 163 HOH   HOH C . 
H 5 HOH   123 423 361 HOH   HOH C . 
H 5 HOH   124 424 157 HOH   HOH C . 
H 5 HOH   125 425 47  HOH   HOH C . 
H 5 HOH   126 426 84  HOH   HOH C . 
H 5 HOH   127 427 230 HOH   HOH C . 
H 5 HOH   128 428 333 HOH   HOH C . 
H 5 HOH   129 429 128 HOH   HOH C . 
H 5 HOH   130 430 298 HOH   HOH C . 
H 5 HOH   131 431 196 HOH   HOH C . 
H 5 HOH   132 432 62  HOH   HOH C . 
H 5 HOH   133 433 50  HOH   HOH C . 
H 5 HOH   134 434 83  HOH   HOH C . 
H 5 HOH   135 435 210 HOH   HOH C . 
H 5 HOH   136 436 103 HOH   HOH C . 
H 5 HOH   137 437 332 HOH   HOH C . 
H 5 HOH   138 438 7   HOH   HOH C . 
H 5 HOH   139 439 28  HOH   HOH C . 
H 5 HOH   140 440 306 HOH   HOH C . 
H 5 HOH   141 441 125 HOH   HOH C . 
H 5 HOH   142 442 265 HOH   HOH C . 
H 5 HOH   143 443 95  HOH   HOH C . 
H 5 HOH   144 444 32  HOH   HOH C . 
H 5 HOH   145 445 35  HOH   HOH C . 
H 5 HOH   146 446 358 HOH   HOH C . 
H 5 HOH   147 447 325 HOH   HOH C . 
H 5 HOH   148 448 25  HOH   HOH C . 
H 5 HOH   149 449 122 HOH   HOH C . 
H 5 HOH   150 450 141 HOH   HOH C . 
H 5 HOH   151 451 144 HOH   HOH C . 
H 5 HOH   152 452 235 HOH   HOH C . 
H 5 HOH   153 453 161 HOH   HOH C . 
H 5 HOH   154 454 285 HOH   HOH C . 
H 5 HOH   155 455 134 HOH   HOH C . 
H 5 HOH   156 456 169 HOH   HOH C . 
H 5 HOH   157 457 198 HOH   HOH C . 
H 5 HOH   158 458 384 HOH   HOH C . 
H 5 HOH   159 459 357 HOH   HOH C . 
H 5 HOH   160 460 187 HOH   HOH C . 
H 5 HOH   161 461 336 HOH   HOH C . 
H 5 HOH   162 462 381 HOH   HOH C . 
H 5 HOH   163 463 97  HOH   HOH C . 
H 5 HOH   164 464 375 HOH   HOH C . 
H 5 HOH   165 465 292 HOH   HOH C . 
H 5 HOH   166 466 348 HOH   HOH C . 
H 5 HOH   167 467 89  HOH   HOH C . 
H 5 HOH   168 468 280 HOH   HOH C . 
H 5 HOH   169 469 260 HOH   HOH C . 
H 5 HOH   170 470 355 HOH   HOH C . 
H 5 HOH   171 471 284 HOH   HOH C . 
H 5 HOH   172 472 342 HOH   HOH C . 
H 5 HOH   173 473 257 HOH   HOH C . 
H 5 HOH   174 474 218 HOH   HOH C . 
H 5 HOH   175 475 229 HOH   HOH C . 
H 5 HOH   176 476 182 HOH   HOH C . 
H 5 HOH   177 477 243 HOH   HOH C . 
H 5 HOH   178 478 175 HOH   HOH C . 
H 5 HOH   179 479 387 HOH   HOH C . 
H 5 HOH   180 480 354 HOH   HOH C . 
H 5 HOH   181 481 389 HOH   HOH C . 
H 5 HOH   182 482 215 HOH   HOH C . 
H 5 HOH   183 483 239 HOH   HOH C . 
H 5 HOH   184 484 272 HOH   HOH C . 
H 5 HOH   185 485 343 HOH   HOH C . 
H 5 HOH   186 486 317 HOH   HOH C . 
H 5 HOH   187 487 226 HOH   HOH C . 
H 5 HOH   188 488 386 HOH   HOH C . 
H 5 HOH   189 489 221 HOH   HOH C . 
H 5 HOH   190 490 204 HOH   HOH C . 
H 5 HOH   191 491 264 HOH   HOH C . 
H 5 HOH   192 492 282 HOH   HOH C . 
H 5 HOH   193 493 345 HOH   HOH C . 
H 5 HOH   194 494 266 HOH   HOH C . 
H 5 HOH   195 495 382 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           7I7U 
_cell.length_a           86.886 
_cell.length_b           57.207 
_cell.length_c           64.801 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.60 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I7U 
_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          7I7U 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.53 
_exptl_crystal.density_percent_sol   51.29 
_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   2025-02-25 
_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   0.92204 
_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        0.92204 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I7U 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             64.62 
_reflns.d_resolution_high            1.31 
_reflns.number_obs                   73331 
_reflns.percent_possible_obs         96.2 
_reflns.pdbx_Rmerge_I_obs            0.061 
_reflns.pdbx_netI_over_sigmaI        18.7 
_reflns.pdbx_redundancy              5.8 
_reflns.pdbx_Rrim_I_all              0.066 
_reflns.pdbx_Rpim_I_all              0.026 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     425970 
_reflns.pdbx_chi_squared             0.66 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.31 
_reflns_shell.d_res_low                   1.33 
_reflns_shell.number_measured_all         6684 
_reflns_shell.number_unique_obs           2436 
_reflns_shell.Rmerge_I_obs                0.895 
_reflns_shell.pdbx_chi_squared            0.14 
_reflns_shell.pdbx_redundancy             2.7 
_reflns_shell.percent_possible_obs        64.3 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             1.139 
_reflns_shell.pdbx_Rpim_I_all             0.688 
_reflns_shell.pdbx_CC_half                0.283 
_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                                 7I7U 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     73218 
_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                             18.80 
_refine.ls_d_res_high                            1.310 
_refine.ls_percent_reflns_obs                    96.3 
_refine.ls_R_factor_obs                          0.1768 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1760 
_refine.ls_R_factor_R_free                       0.1929 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.970 
_refine.ls_number_reflns_R_free                  3639 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.963 
_refine.B_iso_mean                               20.68 
_refine.aniso_B[1][1]                            -0.91010 
_refine.aniso_B[2][2]                            -1.09190 
_refine.aniso_B[3][3]                            2.00200 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -2.31320 
_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             0.047 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.048 
_refine.pdbx_overall_SU_R_Blow_DPI               0.051 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.051 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I7U 
_refine_analyze.Luzzati_coordinate_error_obs    0.16 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2166 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         27 
_refine_hist.number_atoms_solvent             383 
_refine_hist.number_atoms_total               2576 
_refine_hist.d_res_high                       1.310 
_refine_hist.d_res_low                        18.80 
# 
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                  0.012 ? 2.00  2265 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.06  ? 2.00  3086 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  760  '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  405  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2243 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.72  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.52 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  280  '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  2046 '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                       1.31 
_refine_ls_shell.d_res_low                        1.32 
_refine_ls_shell.number_reflns_R_work             1388 
_refine_ls_shell.R_factor_R_work                  0.2996 
_refine_ls_shell.percent_reflns_obs               63.38 
_refine_ls_shell.R_factor_R_free                  0.3405 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.26 
_refine_ls_shell.number_reflns_R_free             77 
_refine_ls_shell.number_reflns_all                1465 
_refine_ls_shell.R_factor_all                     0.3018 
# 
_struct.entry_id                  7I7U 
_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-0038553-001 (A71EV2A-x5317)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I7U 
_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 3 ? 
F N N 4 ? 
G N N 5 ? 
H 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 7I7U A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I7U 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,G 
2 1 B,E,F,H 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.373 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.310 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.259 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.332 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.321 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.322 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 E ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 109.2 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 105.4 ? 
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_555 115.8 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 105.5 ? 
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_555 117.4 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.6 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.9 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 117.8 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 106.6 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.5 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 113.9 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7I7U 
_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 346 ? ? O A HOH 436 ? ? 1.59 
2 1 O A HOH 355 ? ? O C HOH 479 ? ? 1.93 
3 1 O C HOH 366 ? ? O C HOH 389 ? ? 2.00 
4 1 O C HOH 324 ? ? O C HOH 405 ? ? 2.00 
5 1 O A HOH 399 ? ? O A HOH 459 ? ? 2.02 
6 1 O A HOH 439 ? ? O A HOH 481 ? ? 2.09 
7 1 O C HOH 372 ? ? O C HOH 414 ? ? 2.10 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 14.9947 8.2069   14.4004 -0.0148 -0.0275 0.0006 0.0107 0.0098 0.0044 1.0592 0.7141 0.5482 0.5651  
-0.3758 -0.1765 -0.0183 0.0402 0.0842 0.0103 0.0448 -0.0056 -0.0066 -0.0634 -0.0266 
'X-RAY DIFFRACTION' 2 ? refined 25.9378 -20.3135 17.7929 -0.0177 -0.0265 0.0158 0.0057 0.0126 0.0134 0.5539 0.7840 0.2880 -0.1014 
-0.1003 -0.1138 0.0131  0.0010 0.1001 0.0169 0.0369 0.0333  0.0351  0.0028  -0.0500 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
5 1 Y 1 C ALA 147 ? B ALA 141 
6 1 Y 1 C MET 148 ? B MET 142 
7 1 Y 1 C GLU 149 ? B GLU 143 
8 1 Y 1 C GLN 150 ? B GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1B53 N1   N  N N 1   
A1B53 C4   C  Y N 2   
A1B53 C5   C  Y N 3   
A1B53 C6   C  Y N 4   
A1B53 C7   C  Y N 5   
A1B53 C8   C  N N 6   
A1B53 C10  C  N N 7   
A1B53 C13  C  N N 8   
A1B53 O2   O  N N 9   
A1B53 C14  C  N N 10  
A1B53 C11  C  N S 11  
A1B53 C12  C  N N 12  
A1B53 O1   O  N N 13  
A1B53 N2   N  N N 14  
A1B53 C2   C  N R 15  
A1B53 C1   C  N N 16  
A1B53 O    O  N N 17  
A1B53 N    N  N N 18  
A1B53 C    C  N N 19  
A1B53 C3   C  Y N 20  
A1B53 C9   C  Y N 21  
A1B53 H6   H  N N 22  
A1B53 H7   H  N N 23  
A1B53 H8   H  N N 24  
A1B53 H10  H  N N 25  
A1B53 H11  H  N N 26  
A1B53 H9   H  N N 27  
A1B53 H14  H  N N 28  
A1B53 H13  H  N N 29  
A1B53 H17  H  N N 30  
A1B53 H18  H  N N 31  
A1B53 H1   H  N N 32  
A1B53 H16  H  N N 33  
A1B53 H15  H  N N 34  
A1B53 H    H  N N 35  
A1B53 H5   H  N N 36  
A1B53 H2   H  N N 37  
A1B53 H3   H  N N 38  
A1B53 H4   H  N N 39  
A1B53 H12  H  N N 40  
ALA   N    N  N N 41  
ALA   CA   C  N S 42  
ALA   C    C  N N 43  
ALA   O    O  N N 44  
ALA   CB   C  N N 45  
ALA   OXT  O  N N 46  
ALA   H    H  N N 47  
ALA   H2   H  N N 48  
ALA   HA   H  N N 49  
ALA   HB1  H  N N 50  
ALA   HB2  H  N N 51  
ALA   HB3  H  N N 52  
ALA   HXT  H  N N 53  
ARG   N    N  N N 54  
ARG   CA   C  N S 55  
ARG   C    C  N N 56  
ARG   O    O  N N 57  
ARG   CB   C  N N 58  
ARG   CG   C  N N 59  
ARG   CD   C  N N 60  
ARG   NE   N  N N 61  
ARG   CZ   C  N N 62  
ARG   NH1  N  N N 63  
ARG   NH2  N  N N 64  
ARG   OXT  O  N N 65  
ARG   H    H  N N 66  
ARG   H2   H  N N 67  
ARG   HA   H  N N 68  
ARG   HB2  H  N N 69  
ARG   HB3  H  N N 70  
ARG   HG2  H  N N 71  
ARG   HG3  H  N N 72  
ARG   HD2  H  N N 73  
ARG   HD3  H  N N 74  
ARG   HE   H  N N 75  
ARG   HH11 H  N N 76  
ARG   HH12 H  N N 77  
ARG   HH21 H  N N 78  
ARG   HH22 H  N N 79  
ARG   HXT  H  N N 80  
ASN   N    N  N N 81  
ASN   CA   C  N S 82  
ASN   C    C  N N 83  
ASN   O    O  N N 84  
ASN   CB   C  N N 85  
ASN   CG   C  N N 86  
ASN   OD1  O  N N 87  
ASN   ND2  N  N N 88  
ASN   OXT  O  N N 89  
ASN   H    H  N N 90  
ASN   H2   H  N N 91  
ASN   HA   H  N N 92  
ASN   HB2  H  N N 93  
ASN   HB3  H  N N 94  
ASN   HD21 H  N N 95  
ASN   HD22 H  N N 96  
ASN   HXT  H  N N 97  
ASP   N    N  N N 98  
ASP   CA   C  N S 99  
ASP   C    C  N N 100 
ASP   O    O  N N 101 
ASP   CB   C  N N 102 
ASP   CG   C  N N 103 
ASP   OD1  O  N N 104 
ASP   OD2  O  N N 105 
ASP   OXT  O  N N 106 
ASP   H    H  N N 107 
ASP   H2   H  N N 108 
ASP   HA   H  N N 109 
ASP   HB2  H  N N 110 
ASP   HB3  H  N N 111 
ASP   HD2  H  N N 112 
ASP   HXT  H  N N 113 
CYS   N    N  N N 114 
CYS   CA   C  N R 115 
CYS   C    C  N N 116 
CYS   O    O  N N 117 
CYS   CB   C  N N 118 
CYS   SG   S  N N 119 
CYS   OXT  O  N N 120 
CYS   H    H  N N 121 
CYS   H2   H  N N 122 
CYS   HA   H  N N 123 
CYS   HB2  H  N N 124 
CYS   HB3  H  N N 125 
CYS   HG   H  N N 126 
CYS   HXT  H  N N 127 
DMS   S    S  N N 128 
DMS   O    O  N N 129 
DMS   C1   C  N N 130 
DMS   C2   C  N N 131 
DMS   H11  H  N N 132 
DMS   H12  H  N N 133 
DMS   H13  H  N N 134 
DMS   H21  H  N N 135 
DMS   H22  H  N N 136 
DMS   H23  H  N N 137 
GLN   N    N  N N 138 
GLN   CA   C  N S 139 
GLN   C    C  N N 140 
GLN   O    O  N N 141 
GLN   CB   C  N N 142 
GLN   CG   C  N N 143 
GLN   CD   C  N N 144 
GLN   OE1  O  N N 145 
GLN   NE2  N  N N 146 
GLN   OXT  O  N N 147 
GLN   H    H  N N 148 
GLN   H2   H  N N 149 
GLN   HA   H  N N 150 
GLN   HB2  H  N N 151 
GLN   HB3  H  N N 152 
GLN   HG2  H  N N 153 
GLN   HG3  H  N N 154 
GLN   HE21 H  N N 155 
GLN   HE22 H  N N 156 
GLN   HXT  H  N N 157 
GLU   N    N  N N 158 
GLU   CA   C  N S 159 
GLU   C    C  N N 160 
GLU   O    O  N N 161 
GLU   CB   C  N N 162 
GLU   CG   C  N N 163 
GLU   CD   C  N N 164 
GLU   OE1  O  N N 165 
GLU   OE2  O  N N 166 
GLU   OXT  O  N N 167 
GLU   H    H  N N 168 
GLU   H2   H  N N 169 
GLU   HA   H  N N 170 
GLU   HB2  H  N N 171 
GLU   HB3  H  N N 172 
GLU   HG2  H  N N 173 
GLU   HG3  H  N N 174 
GLU   HE2  H  N N 175 
GLU   HXT  H  N N 176 
GLY   N    N  N N 177 
GLY   CA   C  N N 178 
GLY   C    C  N N 179 
GLY   O    O  N N 180 
GLY   OXT  O  N N 181 
GLY   H    H  N N 182 
GLY   H2   H  N N 183 
GLY   HA2  H  N N 184 
GLY   HA3  H  N N 185 
GLY   HXT  H  N N 186 
HIS   N    N  N N 187 
HIS   CA   C  N S 188 
HIS   C    C  N N 189 
HIS   O    O  N N 190 
HIS   CB   C  N N 191 
HIS   CG   C  Y N 192 
HIS   ND1  N  Y N 193 
HIS   CD2  C  Y N 194 
HIS   CE1  C  Y N 195 
HIS   NE2  N  Y N 196 
HIS   OXT  O  N N 197 
HIS   H    H  N N 198 
HIS   H2   H  N N 199 
HIS   HA   H  N N 200 
HIS   HB2  H  N N 201 
HIS   HB3  H  N N 202 
HIS   HD1  H  N N 203 
HIS   HD2  H  N N 204 
HIS   HE1  H  N N 205 
HIS   HE2  H  N N 206 
HIS   HXT  H  N N 207 
HOH   O    O  N N 208 
HOH   H1   H  N N 209 
HOH   H2   H  N N 210 
ILE   N    N  N N 211 
ILE   CA   C  N S 212 
ILE   C    C  N N 213 
ILE   O    O  N N 214 
ILE   CB   C  N S 215 
ILE   CG1  C  N N 216 
ILE   CG2  C  N N 217 
ILE   CD1  C  N N 218 
ILE   OXT  O  N N 219 
ILE   H    H  N N 220 
ILE   H2   H  N N 221 
ILE   HA   H  N N 222 
ILE   HB   H  N N 223 
ILE   HG12 H  N N 224 
ILE   HG13 H  N N 225 
ILE   HG21 H  N N 226 
ILE   HG22 H  N N 227 
ILE   HG23 H  N N 228 
ILE   HD11 H  N N 229 
ILE   HD12 H  N N 230 
ILE   HD13 H  N N 231 
ILE   HXT  H  N N 232 
LEU   N    N  N N 233 
LEU   CA   C  N S 234 
LEU   C    C  N N 235 
LEU   O    O  N N 236 
LEU   CB   C  N N 237 
LEU   CG   C  N N 238 
LEU   CD1  C  N N 239 
LEU   CD2  C  N N 240 
LEU   OXT  O  N N 241 
LEU   H    H  N N 242 
LEU   H2   H  N N 243 
LEU   HA   H  N N 244 
LEU   HB2  H  N N 245 
LEU   HB3  H  N N 246 
LEU   HG   H  N N 247 
LEU   HD11 H  N N 248 
LEU   HD12 H  N N 249 
LEU   HD13 H  N N 250 
LEU   HD21 H  N N 251 
LEU   HD22 H  N N 252 
LEU   HD23 H  N N 253 
LEU   HXT  H  N N 254 
LYS   N    N  N N 255 
LYS   CA   C  N S 256 
LYS   C    C  N N 257 
LYS   O    O  N N 258 
LYS   CB   C  N N 259 
LYS   CG   C  N N 260 
LYS   CD   C  N N 261 
LYS   CE   C  N N 262 
LYS   NZ   N  N N 263 
LYS   OXT  O  N N 264 
LYS   H    H  N N 265 
LYS   H2   H  N N 266 
LYS   HA   H  N N 267 
LYS   HB2  H  N N 268 
LYS   HB3  H  N N 269 
LYS   HG2  H  N N 270 
LYS   HG3  H  N N 271 
LYS   HD2  H  N N 272 
LYS   HD3  H  N N 273 
LYS   HE2  H  N N 274 
LYS   HE3  H  N N 275 
LYS   HZ1  H  N N 276 
LYS   HZ2  H  N N 277 
LYS   HZ3  H  N N 278 
LYS   HXT  H  N N 279 
MET   N    N  N N 280 
MET   CA   C  N S 281 
MET   C    C  N N 282 
MET   O    O  N N 283 
MET   CB   C  N N 284 
MET   CG   C  N N 285 
MET   SD   S  N N 286 
MET   CE   C  N N 287 
MET   OXT  O  N N 288 
MET   H    H  N N 289 
MET   H2   H  N N 290 
MET   HA   H  N N 291 
MET   HB2  H  N N 292 
MET   HB3  H  N N 293 
MET   HG2  H  N N 294 
MET   HG3  H  N N 295 
MET   HE1  H  N N 296 
MET   HE2  H  N N 297 
MET   HE3  H  N N 298 
MET   HXT  H  N N 299 
PHE   N    N  N N 300 
PHE   CA   C  N S 301 
PHE   C    C  N N 302 
PHE   O    O  N N 303 
PHE   CB   C  N N 304 
PHE   CG   C  Y N 305 
PHE   CD1  C  Y N 306 
PHE   CD2  C  Y N 307 
PHE   CE1  C  Y N 308 
PHE   CE2  C  Y N 309 
PHE   CZ   C  Y N 310 
PHE   OXT  O  N N 311 
PHE   H    H  N N 312 
PHE   H2   H  N N 313 
PHE   HA   H  N N 314 
PHE   HB2  H  N N 315 
PHE   HB3  H  N N 316 
PHE   HD1  H  N N 317 
PHE   HD2  H  N N 318 
PHE   HE1  H  N N 319 
PHE   HE2  H  N N 320 
PHE   HZ   H  N N 321 
PHE   HXT  H  N N 322 
PRO   N    N  N N 323 
PRO   CA   C  N S 324 
PRO   C    C  N N 325 
PRO   O    O  N N 326 
PRO   CB   C  N N 327 
PRO   CG   C  N N 328 
PRO   CD   C  N N 329 
PRO   OXT  O  N N 330 
PRO   H    H  N N 331 
PRO   HA   H  N N 332 
PRO   HB2  H  N N 333 
PRO   HB3  H  N N 334 
PRO   HG2  H  N N 335 
PRO   HG3  H  N N 336 
PRO   HD2  H  N N 337 
PRO   HD3  H  N N 338 
PRO   HXT  H  N N 339 
SER   N    N  N N 340 
SER   CA   C  N S 341 
SER   C    C  N N 342 
SER   O    O  N N 343 
SER   CB   C  N N 344 
SER   OG   O  N N 345 
SER   OXT  O  N N 346 
SER   H    H  N N 347 
SER   H2   H  N N 348 
SER   HA   H  N N 349 
SER   HB2  H  N N 350 
SER   HB3  H  N N 351 
SER   HG   H  N N 352 
SER   HXT  H  N N 353 
THR   N    N  N N 354 
THR   CA   C  N S 355 
THR   C    C  N N 356 
THR   O    O  N N 357 
THR   CB   C  N R 358 
THR   OG1  O  N N 359 
THR   CG2  C  N N 360 
THR   OXT  O  N N 361 
THR   H    H  N N 362 
THR   H2   H  N N 363 
THR   HA   H  N N 364 
THR   HB   H  N N 365 
THR   HG1  H  N N 366 
THR   HG21 H  N N 367 
THR   HG22 H  N N 368 
THR   HG23 H  N N 369 
THR   HXT  H  N N 370 
TRP   N    N  N N 371 
TRP   CA   C  N S 372 
TRP   C    C  N N 373 
TRP   O    O  N N 374 
TRP   CB   C  N N 375 
TRP   CG   C  Y N 376 
TRP   CD1  C  Y N 377 
TRP   CD2  C  Y N 378 
TRP   NE1  N  Y N 379 
TRP   CE2  C  Y N 380 
TRP   CE3  C  Y N 381 
TRP   CZ2  C  Y N 382 
TRP   CZ3  C  Y N 383 
TRP   CH2  C  Y N 384 
TRP   OXT  O  N N 385 
TRP   H    H  N N 386 
TRP   H2   H  N N 387 
TRP   HA   H  N N 388 
TRP   HB2  H  N N 389 
TRP   HB3  H  N N 390 
TRP   HD1  H  N N 391 
TRP   HE1  H  N N 392 
TRP   HE3  H  N N 393 
TRP   HZ2  H  N N 394 
TRP   HZ3  H  N N 395 
TRP   HH2  H  N N 396 
TRP   HXT  H  N N 397 
TYR   N    N  N N 398 
TYR   CA   C  N S 399 
TYR   C    C  N N 400 
TYR   O    O  N N 401 
TYR   CB   C  N N 402 
TYR   CG   C  Y N 403 
TYR   CD1  C  Y N 404 
TYR   CD2  C  Y N 405 
TYR   CE1  C  Y N 406 
TYR   CE2  C  Y N 407 
TYR   CZ   C  Y N 408 
TYR   OH   O  N N 409 
TYR   OXT  O  N N 410 
TYR   H    H  N N 411 
TYR   H2   H  N N 412 
TYR   HA   H  N N 413 
TYR   HB2  H  N N 414 
TYR   HB3  H  N N 415 
TYR   HD1  H  N N 416 
TYR   HD2  H  N N 417 
TYR   HE1  H  N N 418 
TYR   HE2  H  N N 419 
TYR   HH   H  N N 420 
TYR   HXT  H  N N 421 
VAL   N    N  N N 422 
VAL   CA   C  N S 423 
VAL   C    C  N N 424 
VAL   O    O  N N 425 
VAL   CB   C  N N 426 
VAL   CG1  C  N N 427 
VAL   CG2  C  N N 428 
VAL   OXT  O  N N 429 
VAL   H    H  N N 430 
VAL   H2   H  N N 431 
VAL   HA   H  N N 432 
VAL   HB   H  N N 433 
VAL   HG11 H  N N 434 
VAL   HG12 H  N N 435 
VAL   HG13 H  N N 436 
VAL   HG21 H  N N 437 
VAL   HG22 H  N N 438 
VAL   HG23 H  N N 439 
VAL   HXT  H  N N 440 
ZN    ZN   ZN N N 441 
# 
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 
A1B53 C   N    sing N N 1   
A1B53 N   C1   sing N N 2   
A1B53 O   C1   doub N N 3   
A1B53 C1  C2   sing N N 4   
A1B53 C3  C2   sing N N 5   
A1B53 C3  C4   doub Y N 6   
A1B53 C4  C5   sing Y N 7   
A1B53 C5  C6   doub Y N 8   
A1B53 C6  C7   sing Y N 9   
A1B53 C8  C7   sing N N 10  
A1B53 C7  C9   doub Y N 11  
A1B53 C9  C3   sing Y N 12  
A1B53 C2  N1   sing N N 13  
A1B53 N1  C10  sing N N 14  
A1B53 C10 C11  sing N N 15  
A1B53 C12 C11  sing N N 16  
A1B53 N2  C12  sing N N 17  
A1B53 O1  C12  doub N N 18  
A1B53 C11 C13  sing N N 19  
A1B53 C13 C14  sing N N 20  
A1B53 N1  C14  sing N N 21  
A1B53 C14 O2   doub N N 22  
A1B53 C4  H6   sing N N 23  
A1B53 C5  H7   sing N N 24  
A1B53 C6  H8   sing N N 25  
A1B53 C8  H10  sing N N 26  
A1B53 C8  H11  sing N N 27  
A1B53 C8  H9   sing N N 28  
A1B53 C10 H14  sing N N 29  
A1B53 C10 H13  sing N N 30  
A1B53 C13 H17  sing N N 31  
A1B53 C13 H18  sing N N 32  
A1B53 C11 H1   sing N N 33  
A1B53 N2  H16  sing N N 34  
A1B53 N2  H15  sing N N 35  
A1B53 C2  H    sing N N 36  
A1B53 N   H5   sing N N 37  
A1B53 C   H2   sing N N 38  
A1B53 C   H3   sing N N 39  
A1B53 C   H4   sing N N 40  
A1B53 C9  H12  sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
DMS   S   O    doub N N 124 
DMS   S   C1   sing N N 125 
DMS   S   C2   sing N N 126 
DMS   C1  H11  sing N N 127 
DMS   C1  H12  sing N N 128 
DMS   C1  H13  sing N N 129 
DMS   C2  H21  sing N N 130 
DMS   C2  H22  sing N N 131 
DMS   C2  H23  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
PHE   N   CA   sing N N 287 
PHE   N   H    sing N N 288 
PHE   N   H2   sing N N 289 
PHE   CA  C    sing N N 290 
PHE   CA  CB   sing N N 291 
PHE   CA  HA   sing N N 292 
PHE   C   O    doub N N 293 
PHE   C   OXT  sing N N 294 
PHE   CB  CG   sing N N 295 
PHE   CB  HB2  sing N N 296 
PHE   CB  HB3  sing N N 297 
PHE   CG  CD1  doub Y N 298 
PHE   CG  CD2  sing Y N 299 
PHE   CD1 CE1  sing Y N 300 
PHE   CD1 HD1  sing N N 301 
PHE   CD2 CE2  doub Y N 302 
PHE   CD2 HD2  sing N N 303 
PHE   CE1 CZ   doub Y N 304 
PHE   CE1 HE1  sing N N 305 
PHE   CE2 CZ   sing Y N 306 
PHE   CE2 HE2  sing N N 307 
PHE   CZ  HZ   sing N N 308 
PHE   OXT HXT  sing N N 309 
PRO   N   CA   sing N N 310 
PRO   N   CD   sing N N 311 
PRO   N   H    sing N N 312 
PRO   CA  C    sing N N 313 
PRO   CA  CB   sing N N 314 
PRO   CA  HA   sing N N 315 
PRO   C   O    doub N N 316 
PRO   C   OXT  sing N N 317 
PRO   CB  CG   sing N N 318 
PRO   CB  HB2  sing N N 319 
PRO   CB  HB3  sing N N 320 
PRO   CG  CD   sing N N 321 
PRO   CG  HG2  sing N N 322 
PRO   CG  HG3  sing N N 323 
PRO   CD  HD2  sing N N 324 
PRO   CD  HD3  sing N N 325 
PRO   OXT HXT  sing N N 326 
SER   N   CA   sing N N 327 
SER   N   H    sing N N 328 
SER   N   H2   sing N N 329 
SER   CA  C    sing N N 330 
SER   CA  CB   sing N N 331 
SER   CA  HA   sing N N 332 
SER   C   O    doub N N 333 
SER   C   OXT  sing N N 334 
SER   CB  OG   sing N N 335 
SER   CB  HB2  sing N N 336 
SER   CB  HB3  sing N N 337 
SER   OG  HG   sing N N 338 
SER   OXT HXT  sing N N 339 
THR   N   CA   sing N N 340 
THR   N   H    sing N N 341 
THR   N   H2   sing N N 342 
THR   CA  C    sing N N 343 
THR   CA  CB   sing N N 344 
THR   CA  HA   sing N N 345 
THR   C   O    doub N N 346 
THR   C   OXT  sing N N 347 
THR   CB  OG1  sing N N 348 
THR   CB  CG2  sing N N 349 
THR   CB  HB   sing N N 350 
THR   OG1 HG1  sing N N 351 
THR   CG2 HG21 sing N N 352 
THR   CG2 HG22 sing N N 353 
THR   CG2 HG23 sing N N 354 
THR   OXT HXT  sing N N 355 
TRP   N   CA   sing N N 356 
TRP   N   H    sing N N 357 
TRP   N   H2   sing N N 358 
TRP   CA  C    sing N N 359 
TRP   CA  CB   sing N N 360 
TRP   CA  HA   sing N N 361 
TRP   C   O    doub N N 362 
TRP   C   OXT  sing N N 363 
TRP   CB  CG   sing N N 364 
TRP   CB  HB2  sing N N 365 
TRP   CB  HB3  sing N N 366 
TRP   CG  CD1  doub Y N 367 
TRP   CG  CD2  sing Y N 368 
TRP   CD1 NE1  sing Y N 369 
TRP   CD1 HD1  sing N N 370 
TRP   CD2 CE2  doub Y N 371 
TRP   CD2 CE3  sing Y N 372 
TRP   NE1 CE2  sing Y N 373 
TRP   NE1 HE1  sing N N 374 
TRP   CE2 CZ2  sing Y N 375 
TRP   CE3 CZ3  doub Y N 376 
TRP   CE3 HE3  sing N N 377 
TRP   CZ2 CH2  doub Y N 378 
TRP   CZ2 HZ2  sing N N 379 
TRP   CZ3 CH2  sing Y N 380 
TRP   CZ3 HZ3  sing N N 381 
TRP   CH2 HH2  sing N N 382 
TRP   OXT HXT  sing N N 383 
TYR   N   CA   sing N N 384 
TYR   N   H    sing N N 385 
TYR   N   H2   sing N N 386 
TYR   CA  C    sing N N 387 
TYR   CA  CB   sing N N 388 
TYR   CA  HA   sing N N 389 
TYR   C   O    doub N N 390 
TYR   C   OXT  sing N N 391 
TYR   CB  CG   sing N N 392 
TYR   CB  HB2  sing N N 393 
TYR   CB  HB3  sing N N 394 
TYR   CG  CD1  doub Y N 395 
TYR   CG  CD2  sing Y N 396 
TYR   CD1 CE1  sing Y N 397 
TYR   CD1 HD1  sing N N 398 
TYR   CD2 CE2  doub Y N 399 
TYR   CD2 HD2  sing N N 400 
TYR   CE1 CZ   doub Y N 401 
TYR   CE1 HE1  sing N N 402 
TYR   CE2 CZ   sing Y N 403 
TYR   CE2 HE2  sing N N 404 
TYR   CZ  OH   sing N N 405 
TYR   OH  HH   sing N N 406 
TYR   OXT HXT  sing N N 407 
VAL   N   CA   sing N N 408 
VAL   N   H    sing N N 409 
VAL   N   H2   sing N N 410 
VAL   CA  C    sing N N 411 
VAL   CA  CB   sing N N 412 
VAL   CA  HA   sing N N 413 
VAL   C   O    doub N N 414 
VAL   C   OXT  sing N N 415 
VAL   CB  CG1  sing N N 416 
VAL   CB  CG2  sing N N 417 
VAL   CB  HB   sing N N 418 
VAL   CG1 HG11 sing N N 419 
VAL   CG1 HG12 sing N N 420 
VAL   CG1 HG13 sing N N 421 
VAL   CG2 HG21 sing N N 422 
VAL   CG2 HG22 sing N N 423 
VAL   CG2 HG23 sing N N 424 
VAL   OXT HXT  sing N N 425 
# 
_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                    7I7U 
_atom_sites.fract_transf_matrix[1][1]   0.011509 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000926 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017480 
_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]   0.015482 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.684 8.116   24.784 1.00 16.67  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.939 8.215   24.019 1.00 17.11  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.082 7.015   23.102 1.00 16.80  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.367 6.014   23.261 1.00 17.13  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.136 8.286   24.971 1.00 20.48  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.241 7.061   25.670 1.00 23.06  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.020 7.095   22.148 1.00 15.21  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.269 5.976   21.235 1.00 14.73  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.678 6.431   19.846 1.00 14.20  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.399 7.562   19.452 1.00 16.06  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.392 5.568   19.146 1.00 13.12  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.852 5.911   17.807 1.00 13.14  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.819 4.698   16.901 1.00 12.52  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.750 3.550   17.365 1.00 13.60  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.301 6.414   17.928 1.00 14.08  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.922 4.935   15.588 1.00 12.68  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.151 3.880   14.584 1.00 12.57  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.631 3.966   14.206 1.00 13.37  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.112 5.081   13.904 1.00 13.46  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.293 4.079   13.310 1.00 12.58  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.801 4.247   13.635 1.00 14.36  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.508 2.875   12.363 1.00 13.94  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.997 4.778   12.378 1.00 15.41  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.346 2.822   14.183 1.00 12.85  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.759 2.803   13.781 1.00 13.75  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.866 1.962   12.501 1.00 13.83  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.858 0.726   12.562 1.00 13.98  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.625 2.208   14.914 1.00 15.24  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.667 3.111   16.130 1.00 14.98  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.531 4.201   16.186 1.00 15.79  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.846 2.879   17.226 1.00 16.16  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.529 5.072   17.272 1.00 16.65  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.868 3.727   18.340 1.00 16.54  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.687 4.841   18.337 1.00 17.35  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.721 5.713   19.430 1.00 19.37  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.926 2.626   11.348 1.00 14.49  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.995 1.992   10.025 1.00 14.91  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.237 2.504   9.317  1.00 16.02  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.465 3.718   9.276  1.00 15.54  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.690 2.250   9.193  1.00 16.01  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.356 3.746   9.101  1.00 16.59  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.828 1.636   7.798  1.00 17.60  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.105 1.599   8.845  1.00 17.32  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.346 2.030   8.195  1.00 16.99  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.182 2.904   9.108  1.00 16.49  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.273 2.609   10.310 1.00 16.49  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.627 4.062   8.603  1.00 15.84  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.323 5.031   9.457  1.00 15.65  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.429 6.217   9.794  1.00 14.88  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.922 7.360   9.919  1.00 15.65  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.675 5.483   8.884  1.00 16.69  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.759 4.427   8.985  1.00 21.41  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.515 4.340   9.970  1.00 23.68  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.803 3.562   8.003  1.00 20.47  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.136 5.936   10.011 1.00 14.28  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.152 6.969   10.360 1.00 13.99  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.462 6.658   11.693 1.00 13.68  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.216 5.474   12.015 1.00 14.11  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.063 7.053   9.278  1.00 14.77  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.570 7.440   7.906  1.00 16.13  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.199 8.661   7.693  1.00 17.14  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.402 6.597   6.822  1.00 17.94  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.649 9.033   6.430  1.00 17.83  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.806 6.979   5.545  1.00 18.92  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.437 8.194   5.359  1.00 19.52  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.879 8.602   4.114  1.00 23.08  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.137 7.712   12.440 1.00 13.57  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.354 7.634   13.677 1.00 13.56  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.120 8.508   13.448 1.00 12.63  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.261 9.724   13.162 1.00 13.40  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.176 8.177   14.875 1.00 14.20  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.372 8.513   16.135 1.00 14.39  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.297 8.878   17.312 1.00 15.88  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.752 9.956   18.154 1.00 16.20  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.077 9.752   19.287 1.00 18.06  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.795 8.514   19.688 1.00 19.02  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.636 10.782  19.998 1.00 17.42  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.914 7.911   13.477 1.00 12.38  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.635 8.621   13.237 1.00 12.89  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.943 8.824   14.568 1.00 13.30  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.638 7.840   15.264 1.00 13.36  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.702 7.821   12.297 1.00 13.49  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.484 8.674   11.912 1.00 13.69  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.421 7.331   11.041 1.00 14.73  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.699 10.097  14.928 1.00 11.93  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.086 10.424  16.226 1.00 13.30  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 19.948 11.419  16.033 1.00 12.75  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.803 12.051  14.947 1.00 14.19  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.126 11.033  17.228 1.00 15.06  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.113 9.965   17.681 1.00 17.68  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 22.823 12.300  16.678 1.00 14.89  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.129 11.610  17.096 1.00 12.99  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.114 12.689  17.027 1.00 12.73  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 18.904 14.012  17.045 1.00 13.54  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 19.836 14.171  17.858 1.00 14.30  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.243 12.679  18.286 1.00 12.71  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.397 11.431  18.376 1.00 13.44  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 16.812 10.411  18.975 1.00 14.68  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.193 11.462  17.779 1.00 14.36  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.554 14.953  16.148 1.00 12.71  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.303 16.242  16.119 1.00 13.16  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.267 16.930  17.489 1.00 14.84  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.276 17.479  17.929 1.00 15.67  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.697 17.136  15.034 1.00 14.24  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.495 18.446  14.782 1.00 15.52  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.747 19.328  13.795 1.00 15.95  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.491 20.537  13.361 1.00 16.77  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.458 21.700  13.998 1.00 20.15  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.877 21.797  15.189 1.00 19.22  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.056 22.772  13.472 1.00 21.09  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.110 16.835  18.182 1.00 14.21  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 17.979 17.527  19.467 1.00 15.32  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 18.836 16.921  20.598 1.00 16.01  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 18.957 17.549  21.662 1.00 17.47  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.491 17.684  19.876 1.00 15.88  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 15.829 16.434  20.373 1.00 15.15  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.179 15.571  19.505 1.00 15.77  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 15.622 16.002  21.644 1.00 15.94  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 14.679 14.593  20.264 1.00 15.55  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 14.887 14.825  21.556 1.00 16.22  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.377 15.700  20.396 1.00 15.16  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.245 15.021  21.356 1.00 14.74  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 21.720 14.968  20.911 1.00 16.21  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 22.542 14.355  21.580 1.00 17.35  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 19.722 13.628  21.677 1.00 14.55  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.323 13.624  22.271 1.00 15.46  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 17.895 12.198  22.526 1.00 16.12  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 18.249 14.426  23.602 1.00 17.05  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.051 15.612  19.765 1.00 15.25  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.436 15.582  19.284 1.00 16.12  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.418 16.222  20.269 1.00 17.84  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.118 17.240  20.912 1.00 18.11  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.524 16.255  17.910 1.00 15.68  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 25.604 15.599  20.405 1.00 16.90  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 26.664 16.096  21.303 1.00 17.57  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.587 17.107  20.585 1.00 17.82  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.528 17.247  19.341 1.00 16.54  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 27.518 14.913  21.797 1.00 19.59  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.237 14.385  20.658 1.00 19.11  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 26.676 13.799  22.458 1.00 19.82  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.522 17.765  21.338 1.00 17.95  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.502 18.623  20.714 1.00 18.07  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.366 17.821  19.749 1.00 17.66  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.635 18.308  18.648 1.00 18.31  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.419 19.321  21.769 1.00 19.72  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 31.667 19.955  21.164 1.00 27.38  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 31.612 21.148  20.462 1.00 32.11  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 32.935 19.466  21.078 1.00 31.10  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 32.850 21.416  20.079 1.00 32.72  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 33.683 20.411  20.384 1.00 33.73  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.718 16.562  20.103 1.00 16.51  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.536 15.763  19.201 1.00 16.84  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.779 15.472  17.907 1.00 15.99  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.381 15.483  16.838 1.00 16.52  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 31.998 14.447  19.831 1.00 18.08  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 32.985 13.727  18.944 1.00 26.88  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.143 14.181  18.764 1.00 29.44  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.532 12.634  18.305 1.00 28.99  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.438 15.256  17.989 1.00 15.50  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.659 15.066  16.772 1.00 14.67  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.737 16.317  15.860 1.00 13.94  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.947 16.207  14.641 1.00 14.88  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.175 14.795  17.078 1.00 15.26  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 26.914 13.431  17.681 1.00 16.81  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.584 12.445  17.256 1.00 15.82  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.052 13.346  18.592 1.00 15.64  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.529 17.508  16.433 1.00 13.98  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.566 18.748  15.645 1.00 14.20  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.972 19.024  15.084 1.00 15.03  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.081 19.581  13.979 1.00 15.95  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.098 19.947  16.525 1.00 15.28  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.597 20.020  16.640 1.00 15.03  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.837 19.698  17.732 1.00 16.42  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.673 20.462  15.627 1.00 16.07  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.501 19.954  17.479 1.00 16.16  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.370 20.388  16.172 1.00 16.38  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.827 20.908  14.302 1.00 17.65  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.237 20.784  15.442 1.00 17.46  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.713 21.244  13.574 1.00 18.00  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.443 21.213  14.136 1.00 18.04  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.032 18.600  15.801 1.00 14.66  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.399 18.817  15.351 1.00 15.90  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.845 17.810  14.272 1.00 17.17  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.913 17.968  13.675 1.00 17.94  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.350 18.771  16.546 1.00 17.58  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.049 16.735  14.058 1.00 15.87  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.323 15.680  13.048 1.00 15.48  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 31.056 15.506  12.182 1.00 15.36  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.674 14.389  11.839 1.00 15.38  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.698 14.356  13.763 1.00 16.82  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.054 14.531  14.417 1.00 19.08  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.097 14.495  13.741 1.00 22.13  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.076 14.835  15.745 1.00 20.23  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.422 16.602  11.818 1.00 14.83  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 29.121 16.580  11.164 1.00 14.07  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 29.168 16.131  9.723  1.00 15.68  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 30.031 16.590  8.949  1.00 17.76  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.517 18.000  11.238 1.00 14.42  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 27.118 18.155  10.640 1.00 15.43  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 26.074 17.385  11.452 1.00 15.52  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.686 19.619  10.585 1.00 18.69  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 28.248 15.238  9.347  1.00 15.00  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 28.082 14.836  7.943  1.00 15.12  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.829 15.547  7.360  1.00 15.60  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.892 16.097  6.249  1.00 17.37  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.958 13.300  7.832  1.00 14.96  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.615 12.894  6.387  1.00 16.50  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 29.257 12.625  8.302  1.00 16.47  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.683 15.494  8.064  1.00 15.18  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 24.434 16.048  7.561  1.00 15.97  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.460 16.251  8.706  1.00 16.11  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.509 15.486  9.687  1.00 15.41  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.827 15.045  6.526  1.00 16.45  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 22.409 15.298  6.077  1.00 17.45  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.999 16.150  5.086  1.00 19.79  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 21.216 14.674  6.589  1.00 16.65  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 20.624 16.075  4.939  1.00 20.53  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 20.124 15.165  5.843  1.00 18.45  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.970 13.742  7.598  1.00 16.87  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.802 14.726  6.064  1.00 19.21  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.668 13.284  7.783  1.00 17.23  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.602 13.809  7.063  1.00 18.59  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.650 17.310  8.649  1.00 16.77  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.622 17.505  9.654  1.00 16.72  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 20.380 18.129  9.032  1.00 17.58  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 20.479 18.916  8.074  1.00 17.53  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 22.126 18.329  10.837 1.00 17.94  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.718 19.686  10.452 1.00 17.91  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.769 20.866  10.270 1.00 20.07  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 22.099 21.822  9.519  1.00 21.10  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.667 20.844  10.857 1.00 18.48  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 19.214 17.822  9.594  1.00 16.32  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.967 18.379  9.094  1.00 15.96  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.998 18.562  10.256 1.00 16.02  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.472 17.587  10.792 1.00 15.71  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 17.366 17.477  7.985  1.00 17.96  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 16.108 17.988  7.323  1.00 22.04  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 15.283 18.598  8.012  1.00 25.02  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.929 17.737  6.114  1.00 24.09  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.779 19.822  10.668 1.00 16.46  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.886 20.139  11.779 0.50 16.73  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.895 20.083  11.804 0.50 17.71  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.441 19.685  11.514 1.00 17.94  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.765 19.182  12.426 1.00 17.91  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.923 21.649  12.031 0.50 16.96  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.989 21.549  12.221 0.50 21.10  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.973 22.041  13.003 0.50 17.22  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.646 22.359  11.115 0.50 26.40  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.966 19.837  10.264 1.00 17.64  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.586 19.430  9.945  1.00 17.71  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.346 17.940  10.135 1.00 17.22  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.205 17.555  10.357 1.00 18.17  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 12.193 19.859  8.531  1.00 20.12  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.725 19.007  7.533  1.00 26.01  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.401 17.120  10.103 1.00 15.56  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.308 15.661  10.305 1.00 15.54  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.758 15.202  11.706 1.00 14.72  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.681 13.996  12.009 1.00 14.13  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 14.177 14.926  9.273  1.00 15.96  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.663 15.102  7.851  1.00 17.08  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.527 14.431  6.805  1.00 16.20  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.433 12.967  6.927  1.00 15.08  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.583 12.115  5.917  1.00 16.11  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.838 12.565  4.687  1.00 17.81  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.460 10.798  6.121  1.00 15.12  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.341 16.122  12.525 1.00 14.43  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.947 15.785  13.812 1.00 13.74  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.102 14.776  13.657 1.00 13.36  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.312 13.932  14.542 1.00 14.11  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.931 15.276  14.859 1.00 14.67  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.514 15.075  16.247 1.00 14.99  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.352 15.917  16.683 1.00 16.18  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.142 14.058  16.920 1.00 15.56  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.902 14.902  12.575 1.00 13.02  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.013 13.968  12.373 1.00 12.39  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.352 14.673  12.247 1.00 13.05  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.426 15.798  11.672 1.00 13.95  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.807 13.143  11.090 1.00 13.03  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.696 12.032  11.131 1.00 14.05  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.635 11.314  9.785  1.00 14.92  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.930 11.019  12.241 1.00 14.57  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.400 13.998  12.691 1.00 12.65  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.788 14.466  12.518 1.00 12.75  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.637 13.240  12.385 1.00 13.10  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.418 12.209  13.059 1.00 13.31  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.230 15.314  13.728 1.00 13.66  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.681 15.885  13.664 1.00 13.64  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.757 17.273  14.329 1.00 15.06  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.703 14.936  14.277 1.00 14.52  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.620 13.312  11.454 1.00 13.25  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.542 12.217  11.188 1.00 12.46  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.955 12.727  11.342 1.00 13.28  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.302 13.777  10.771 1.00 13.58  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.337 11.624  9.776  1.00 12.63  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.368 10.521  9.496  1.00 14.62  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.894 11.091  9.622  1.00 14.54  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.762 12.031  12.135 1.00 12.95  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.176 12.372  12.335 1.00 12.44  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.058 11.213  11.868 1.00 13.81  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.595 10.070  11.651 1.00 14.12  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.448 12.746  13.793 1.00 14.77  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.143 11.671  14.667 1.00 15.00  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.360 11.484  11.675 1.00 14.58  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.301 10.441  11.259 1.00 16.26  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.929 9.719   12.467 1.00 17.92  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.099 10.318  13.551 1.00 19.88  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.397 11.045  10.386 1.00 18.88  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 33.104 12.021  11.137 1.00 21.17  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.285 8.414   12.277 1.00 18.40  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.864 7.605   13.346 1.00 19.69  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.199 7.028   12.896 1.00 21.34  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.425 6.813   11.690 1.00 20.46  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 31.926 6.414   13.708 1.00 19.95  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 31.805 5.510   12.602 1.00 20.95  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.514 6.882   14.098 1.00 19.96  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.049 6.707   13.868 1.00 22.69  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.333 6.094   13.561 1.00 24.42  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.141 4.584   13.333 1.00 24.90  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.705 4.031   12.384 1.00 26.70  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.345 6.420   14.672 1.00 28.63  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 36.832 5.933   15.900 1.00 32.82  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.598 7.902   14.796 1.00 29.02  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.319 3.942   14.163 1.00 24.67  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.064 2.501   14.010 1.00 25.22  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 33.823 2.223   13.143 1.00 23.79  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 32.883 3.022   13.161 1.00 22.90  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 34.862 1.869   15.377 1.00 27.44  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 33.791 1.072   12.451 1.00 22.32  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 32.664 0.682   11.605 1.00 22.49  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.566 0.081   12.466 1.00 21.45  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 31.850 -0.705  13.372 1.00 22.82  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.108 -0.339  10.545 1.00 24.71  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.971 0.267   9.433  1.00 29.85  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 34.351 -0.781  8.413  1.00 36.63  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 35.164 -1.675  8.675  1.00 38.00  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 33.750 -0.700  7.232  1.00 38.64  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.314 0.428   12.182 1.00 18.42  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.180 -0.108  12.932 1.00 18.06  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.587 -1.371  12.342 1.00 17.35  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 28.865 -1.724  11.189 1.00 18.73  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 27.615 -1.947  13.072 1.00 16.90  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.030 -3.234  12.674 1.00 16.82  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 25.586 -3.181  12.234 1.00 17.20  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.052 -4.215  11.829 1.00 17.75  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 27.198 -4.248  13.805 1.00 17.73  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 28.917 -4.679  14.144 1.00 22.50  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 24.930 -2.030  12.374 1.00 15.01  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.535 -1.920  11.953 1.00 14.44  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.461 -1.857  10.414 1.00 16.61  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.361 -1.304  9.771  1.00 18.33  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 22.911 -0.657  12.561 1.00 14.15  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 22.799 -0.725  14.080 1.00 15.79  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 22.460 -1.834  14.606 1.00 15.92  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 22.983 0.321   14.746 1.00 16.42  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.415 -2.423  9.847  1.00 17.56  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.146 -2.316  8.390  1.00 18.21  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.798 -1.603  8.228  1.00 17.22  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.887 -1.782  9.054  1.00 18.29  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 22.104 -3.660  7.735  1.00 22.74  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 21.068 -4.395  8.339  1.00 27.23  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 23.442 -4.390  7.915  1.00 23.73  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.679 -0.756  7.196  1.00 17.05  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.436 -0.019  6.982  1.00 16.15  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.484 -0.817  6.096  1.00 16.25  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.871 -1.331  5.024  1.00 16.92  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.753 1.375   6.345  1.00 15.58  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.846 2.146   7.109  1.00 16.71  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.487 2.237   6.199  1.00 15.76  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.513 2.444   8.613  1.00 16.74  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.207 -0.825  6.460  1.00 15.12  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 16.143 -1.448  5.676  1.00 15.20  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.894 -0.592  4.423  1.00 16.19  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.908 0.665   4.466  1.00 16.06  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.867 -1.476  6.489  1.00 15.23  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.685 -1.276  3.273  1.00 17.53  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 15.368 -0.597  2.013  1.00 18.50  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 14.076 -1.310  1.542  1.00 20.84  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 14.125 -2.263  0.740  1.00 21.92  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 16.554 -0.713  1.013  1.00 18.68  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.888 -0.126  1.528  1.00 18.15  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.868 1.394   1.794  1.00 17.64  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 19.183 1.873   2.281  1.00 16.86  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 19.370 3.018   2.936  1.00 18.09  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 18.367 3.871   3.098  1.00 17.37  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.577 3.347   3.381  1.00 20.11  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.935 -0.784  1.986  1.00 20.75  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.631 -1.444  1.867  1.00 21.38  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 10.474 -0.471  2.145  1.00 21.06  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.641 0.689   2.508  1.00 23.08  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.608 -2.590  2.872  1.00 20.50  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.526 -2.014  4.583  1.00 19.66  ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 9.207  -1.018  2.071  1.00 24.24  ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 8.029  -0.232  2.398  1.00 26.84  ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 7.236  -0.928  3.541  1.00 25.69  ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 6.001  -0.823  3.598  1.00 26.47  ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 7.112  -0.023  1.165  1.00 33.98  ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 6.567  -1.301  0.552  1.00 44.05  ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.577  -1.214  -0.225 1.00 47.64  ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 7.145  -2.391  0.821  1.00 46.80  ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.934  -1.621  4.457  1.00 23.09  ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.266  -2.257  5.619  1.00 21.03  ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.512  -1.218  6.429  1.00 21.10  ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.950  -0.072  6.572  1.00 20.77  ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.277  -2.987  6.507  1.00 19.68  ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.962  -4.544  5.846  1.00 21.23  ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.339  -1.617  6.932  1.00 19.03  ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.541  -0.823  7.876  1.00 18.82  ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.319  -1.585  9.187  1.00 17.10  ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.442  -1.209  9.967  1.00 17.67  ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.203  -0.373  7.295  1.00 21.98  ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.291  0.736   6.277  1.00 26.10  ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.895  1.254   5.931  1.00 31.66  ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.382  1.075   4.813  1.00 33.38  ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.223  1.951   6.855  1.00 27.29  ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.054  -2.709  9.396  1.00 15.00  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.077  -3.402  10.678 1.00 15.06  ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.539  -3.651  11.074 1.00 14.63  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.409  -3.831  10.212 1.00 15.96  ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.299  -4.711  10.672 1.00 18.96  ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 4.905  -5.641  9.802  1.00 24.37  ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 2.866  -4.536  10.256 1.00 18.67  ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 6.797  -3.589  12.362 1.00 13.69  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.165  -3.805  12.839 1.00 13.29  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.182  -3.860  14.354 1.00 12.79  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.141  -4.068  14.973 1.00 13.83  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 9.356  -3.648  14.957 1.00 12.21  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 9.526  -3.700  16.404 1.00 11.80  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 10.379 -2.531  16.825 1.00 12.34  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 11.369 -2.244  16.163 1.00 12.71  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 10.233 -5.044  16.756 1.00 13.47  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 10.588 -5.140  18.228 1.00 15.03  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 9.340  -6.247  16.364 1.00 14.70  ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.008 -1.860  17.935 1.00 12.06  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 10.858 -0.764  18.424 1.00 11.73  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 11.290 -0.985  19.872 1.00 12.72  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 10.588 -1.635  20.655 1.00 13.54  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 10.172 0.636   18.295 1.00 12.31  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 9.175  0.990   19.386 1.00 12.42  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 7.880  0.472   19.369 1.00 14.02  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 9.505  1.895   20.397 1.00 12.99  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 6.963  0.782   20.371 1.00 15.53  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 8.574  2.253   21.370 1.00 13.71  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 7.318  1.675   21.354 1.00 15.09  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 6.368  1.943   22.330 1.00 17.12  ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 12.436 -0.364  20.233 1.00 11.75  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 12.895 -0.409  21.623 1.00 11.29  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 12.420 0.799   22.413 1.00 11.87  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 12.661 1.956   22.033 1.00 12.23  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 14.458 -0.488  21.676 1.00 12.42  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 14.916 -0.615  23.106 1.00 13.25  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 14.614 -1.738  23.848 1.00 13.46  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 15.660 0.400   23.716 1.00 13.70  ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 14.957 -1.824  25.193 1.00 14.62  ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 16.036 0.311   25.051 1.00 14.01  ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 15.755 -0.843  25.757 1.00 15.35  ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 16.089 -0.943  27.104 1.00 18.16  ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 11.805 0.500   23.562 1.00 11.87  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 11.268 1.505   24.506 1.00 12.88  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 12.081 1.502   25.816 1.00 13.68  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 11.899 0.596   26.669 1.00 13.19  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 9.802  1.185   24.765 1.00 12.99  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 9.018  2.298   25.982 1.00 14.20  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 13.012 2.485   25.979 1.00 13.57  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 13.865 2.491   27.178 1.00 13.96  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 13.126 2.704   28.501 1.00 14.04  ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 13.518 2.133   29.514 1.00 15.54  ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 15.001 3.504   27.038 1.00 15.96  ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 14.568 4.846   27.130 1.00 17.45  ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 11.973 3.401   28.461 1.00 12.48  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 11.177 3.616   29.671 1.00 12.79  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 10.384 2.378   30.117 1.00 13.96  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 9.746  2.419   31.162 1.00 14.38  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 10.228 4.804   29.481 1.00 14.14  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 9.253  4.584   28.480 1.00 15.37  ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 10.450 1.284   29.337 1.00 14.06  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 9.884  -0.018  29.709 1.00 14.07  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 10.938 -1.146  29.671 1.00 14.92  ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 10.607 -2.315  29.953 1.00 15.86  ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 8.708  -0.370  28.783 1.00 14.44  ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 7.520  0.580   28.925 1.00 14.97  ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 6.761  0.289   30.203 1.00 14.30  ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 5.593  1.178   30.346 1.00 16.57  ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 5.617  2.346   30.981 1.00 16.11  ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 6.753  2.800   31.519 1.00 17.01  ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 4.500  3.071   31.105 1.00 17.05  ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 12.175 -0.854  29.217 1.00 15.30  ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 13.197 -1.905  28.966 1.00 16.82  ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 12.609 -3.041  28.097 1.00 18.54  ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 12.797 -4.243  28.391 1.00 20.98  ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 13.715 -2.505  30.275 1.00 20.63  ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 14.794 -1.692  30.781 1.00 21.44  ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 15.592 -2.511  31.773 1.00 22.18  ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 16.332 -1.540  32.545 1.00 23.16  ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 16.003 -1.147  33.774 1.00 20.00  ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 14.919 -1.645  34.374 1.00 21.50  ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 16.718 -0.221  34.388 1.00 21.02  ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 11.842 -2.686  27.065 1.00 16.48  ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 11.159 -3.692  26.270 1.00 16.85  ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 11.110 -3.320  24.811 1.00 15.77  ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 11.039 -2.127  24.472 1.00 15.56  ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 9.693  -3.818  26.761 1.00 20.81  ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 9.522  -4.771  27.954 1.00 30.27  ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 8.087  -5.243  28.103 1.00 38.88  ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 7.884  -5.927  29.438 1.00 44.99  ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 8.402  -5.080  30.549 1.00 48.91  ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 11.094 -4.333  23.951 1.00 14.93  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 10.862 -4.196  22.506 1.00 14.37  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 9.407  -4.541  22.227 1.00 15.67  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 8.907  -5.588  22.672 1.00 18.73  ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 11.786 -5.144  21.721 1.00 12.93  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 13.248 -4.817  21.859 1.00 15.07  ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 13.954 -4.131  20.873 1.00 18.37  ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 14.093 -5.125  22.869 1.00 15.60  ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 15.225 -4.084  21.297 1.00 16.98  ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 15.345 -4.647  22.499 1.00 18.28  ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 8.713  -3.671  21.478 1.00 13.36  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 7.281  -3.883  21.202 1.00 13.86  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 7.037  -3.981  19.711 1.00 13.39  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 7.508  -3.132  18.950 1.00 13.53  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 6.455  -2.651  21.706 1.00 14.40  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 6.399  -2.504  23.212 1.00 14.69  ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 5.579  -3.328  23.983 1.00 16.37  ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 7.095  -1.498  23.851 1.00 14.66  ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 5.480  -3.172  25.368 1.00 17.18  ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 6.999  -1.321  25.236 1.00 16.07  ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 6.165  -2.145  25.985 1.00 17.09  ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 6.106  -1.986  27.365 1.00 19.26  ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 6.197  -4.936  19.290 1.00 13.99  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 5.788  -4.963  17.877 1.00 14.06  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 4.753  -3.860  17.610 1.00 15.59  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 3.852  -3.609  18.451 1.00 18.38  ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 5.130  -6.342  17.692 1.00 15.85  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 4.764  -6.805  19.079 1.00 17.39  ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 5.627  -6.045  20.088 1.00 14.45  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 4.879  -3.216  16.477 1.00 14.14  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 3.975  -2.105  16.134 1.00 15.33  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 3.640  -2.104  14.664 1.00 14.80  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.447  -2.475  13.834 1.00 15.67  ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 4.551  -0.725  16.500 1.00 18.47  ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 4.474  -0.488  18.010 1.00 20.23  ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 5.964  -0.556  15.960 1.00 18.56  ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.444  -1.551  14.344 1.00 14.43  ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.046  -1.151  12.991 1.00 14.84  ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.255  0.377   12.923 1.00 14.86  ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 1.901  1.076   13.894 1.00 15.25  ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.562  -1.412  12.783 1.00 19.05  ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.335  -2.814  12.773 1.00 26.66  ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 2.846  0.897   11.837 1.00 14.90  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.164  2.318   11.761 1.00 14.78  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.779  2.894   10.422 1.00 15.37  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.714  2.174   9.411  1.00 16.03  ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.668  2.573   12.108 1.00 15.62  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.705  1.767   11.327 1.00 14.84  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.119  0.511   11.762 1.00 14.57  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.263  2.273   10.167 1.00 15.01  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.064  -0.217  11.049 1.00 15.28  ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.226  1.545   9.460  1.00 15.36  ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.586  0.285   9.892  1.00 14.87  ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.489  4.204   10.402 1.00 15.47  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.074  4.886   9.178  1.00 16.24  ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.229  5.119   8.210  1.00 16.13  ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.395  4.958   8.576  1.00 16.70  ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.353  6.196   9.521  1.00 18.42  ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.208  7.123   10.181 1.00 19.97  ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.932  5.487   6.965  1.00 16.20  ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.989  5.805   6.006  1.00 16.71  ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.625  7.157   6.349  1.00 17.50  ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.958  8.022   6.937  1.00 18.24  ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.406  5.807   4.580  1.00 18.78  ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.995  4.413   4.135  1.00 22.83  ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.568  4.422   2.668  1.00 30.34  ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.253  3.022   2.193  1.00 37.40  ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 2.391  2.920   0.713  1.00 41.57  ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.893  7.390   6.007  1.00 17.51  ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.535  8.685   6.347  1.00 17.51  ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.727  9.864   5.811  1.00 18.33  ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 5.383  9.892   4.627  1.00 20.63  ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.926  8.605   5.698  1.00 19.84  ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 8.104  7.156   5.262  1.00 22.37  ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.804  6.454   5.307  1.00 18.90  ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.440  10.822  6.687  1.00 17.60  ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.558  11.920  6.316  1.00 19.19  ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.930  13.203  7.065  1.00 18.18  ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.785  13.198  7.958  1.00 17.16  ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 3.085  11.553  6.600  1.00 24.10  ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.769  10.205  6.907  1.00 30.87  ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 4.246  14.309  6.701  1.00 19.42  ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.438  15.609  7.320  1.00 20.68  ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.345  15.722  8.393  1.00 21.92  ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 2.136  15.755  8.075  1.00 23.74  ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 4.252  16.688  6.228  1.00 21.43  ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.514  18.110  6.642  1.00 23.84  ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 5.975  18.335  6.986  1.00 24.39  ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 4.152  19.093  5.494  1.00 26.00  ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.749  15.710  9.679  1.00 20.33  ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.840  15.690  10.840 1.00 21.60  ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.090  16.843  11.793 1.00 21.92  ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.245  17.206  12.043 1.00 20.86  ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.066  14.366  11.579 1.00 22.72  ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.743  13.167  10.635 1.00 25.21  ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.337  14.310  12.963 1.00 25.09  ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.839  11.897  11.170 1.00 26.17  ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.011  17.444  12.319 1.00 22.90  ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.154  18.543  13.265 1.00 23.44  ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 2.517  17.956  14.630 1.00 24.64  ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 1.876  17.016  15.105 1.00 26.76  ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 0.833  19.339  13.385 1.00 24.43  ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.067  20.669  14.051 1.00 27.26  ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.768  21.672  13.404 1.00 29.09  ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.634  20.896  15.339 1.00 29.99  ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 2.004  22.893  14.023 1.00 31.37  ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 0.866  22.118  15.955 1.00 30.70  ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.534  23.114  15.290 1.00 31.40  ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 3.605  18.452  15.224 1.00 22.40  ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.070  17.979  16.517 1.00 21.35  ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 3.981  19.159  17.493 1.00 21.24  ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 4.474  20.240  17.173 1.00 22.51  ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 5.543  17.493  16.390 1.00 20.21  ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 6.073  17.040  17.756 1.00 20.54  ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 5.615  16.353  15.355 1.00 20.65  ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 3.454  18.924  18.691 1.00 21.34  ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 3.321  19.993  19.690 1.00 22.51  ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 4.670  20.469  20.221 1.00 22.47  ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 5.678  19.774  20.101 1.00 22.43  ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 2.433  19.530  20.855 1.00 25.37  ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 0.967  19.338  20.471 1.00 31.45  ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 0.309  20.551  19.850 1.00 41.61  ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 0.503  21.678  20.363 1.00 42.51  ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? -0.405 20.376  18.839 1.00 46.46  ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 4.657  21.655  20.862 1.00 23.17  ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 5.866  22.234  21.440 1.00 24.12  ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 6.460  21.344  22.499 1.00 24.08  ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 5.746  20.651  23.246 1.00 25.93  ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 5.547  23.600  22.058 1.00 24.94  ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 7.797  21.365  22.574 1.00 23.42  ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 8.535  20.631  23.605 1.00 23.52  ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 9.680  21.549  24.103 1.00 24.61  ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 9.781  22.674  23.626 1.00 25.73  ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 9.131  19.359  23.011 1.00 23.40  ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 10.141 19.680  22.064 1.00 22.70  ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 10.587 21.062  24.997 1.00 25.86  ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 11.728 21.926  25.364 1.00 25.83  ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 12.749 21.976  24.210 1.00 23.22  ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 13.603 22.847  24.234 1.00 23.28  ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 12.397 21.514  26.677 1.00 29.47  ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 13.078 20.178  26.571 1.00 31.59  ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 13.853 19.773  27.806 1.00 40.77  ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 14.961 20.317  28.019 1.00 43.93  ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 13.360 18.896  28.551 1.00 41.26  ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 12.618 21.120  23.164 1.00 21.17  ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 13.599 21.106  22.060 1.00 19.92  ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 13.171 21.820  20.800 1.00 19.43  ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.031 22.274  20.033 1.00 19.78  ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 13.927 19.662  21.713 1.00 19.60  ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 14.496 18.925  22.898 1.00 19.38  ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 15.795 19.164  23.329 1.00 21.77  ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 13.726 18.014  23.612 1.00 21.52  ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 16.341 18.465  24.399 1.00 23.64  ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 14.259 17.308  24.684 1.00 23.17  ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 15.558 17.559  25.093 1.00 24.41  ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.100 16.838  26.140 1.00 26.66  ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 11.846 21.913  20.547 1.00 19.80  ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 11.344 22.579  19.345 1.00 19.88  ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.013 23.269  19.662 1.00 21.08  ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 9.242  22.726  20.471 1.00 21.55  ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.018 21.534  18.261 1.00 19.18  ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.189 20.726  17.707 1.00 17.31  ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.104 21.297  16.834 1.00 17.70  ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 12.337 19.379  18.011 1.00 17.15  ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.147 20.543  16.289 1.00 16.65  ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 13.379 18.627  17.499 1.00 17.34  ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.292 19.219  16.658 1.00 16.45  ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.356 18.482  16.187 1.00 16.27  ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 9.694  24.369  18.964 1.00 22.49  ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 8.325  24.925  19.070 1.00 23.63  ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.340  23.968  18.371 1.00 24.34  ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 7.763  23.017  17.658 1.00 24.06  ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 8.437  26.261  18.315 1.00 25.52  ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 9.478  26.011  17.274 1.00 25.70  ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 10.489 25.045  17.912 1.00 22.88  ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.020  24.237  18.467 1.00 24.90  ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.025  23.418  17.750 1.00 24.48  ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.277  23.671  16.254 1.00 24.12  ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.512  24.816  15.847 1.00 25.32  ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 3.601  23.847  18.142 1.00 24.79  ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.377  22.596  15.470 1.00 23.35  ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.755  22.732  14.074 1.00 22.01  ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.400  21.449  13.318 1.00 21.82  ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.089  20.429  13.931 1.00 22.75  ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.285  22.966  13.999 1.00 23.23  ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.075  21.637  14.259 1.00 24.15  ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.500  21.806  14.580 1.00 24.17  ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.388 20.693  14.213 1.00 23.75  ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.503 19.496  14.761 1.00 26.54  ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 9.634  19.094  15.708 1.00 26.95  ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 11.445 18.652  14.327 1.00 20.52  ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.583  21.474  11.997 1.00 22.15  ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.436  20.294  11.185 1.00 23.11  ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.787  19.600  11.092 1.00 20.85  ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.805  20.243  10.812 1.00 22.26  ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.985  20.678  9.780  1.00 23.88  ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.510  21.003  9.735  1.00 24.59  ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.560  19.997  9.669  1.00 25.23  ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 3.059  22.307  9.856  1.00 25.64  ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 1.203  20.279  9.694  1.00 26.91  ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.700  22.602  9.869  1.00 27.46  ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.777  21.580  9.796  1.00 28.10  ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.569 21.821  9.835  1.00 30.80  ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.809  18.282  11.382 1.00 18.99  ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 8.022  17.461  11.254 1.00 17.97  ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.804  16.549  10.040 1.00 17.59  ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.713  15.969  9.869  1.00 17.80  ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.286  16.648  12.534 1.00 17.43  ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.535  15.776  12.428 1.00 16.68  ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.060 15.295  13.774 1.00 15.73  ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.090 16.008  14.770 1.00 18.03  ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.527 14.052  13.808 1.00 15.92  ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.803  16.462  9.154  1.00 16.28  ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.680  15.660  7.952  1.00 15.91  ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 9.299  14.267  8.141  1.00 15.90  ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 10.066 14.024  9.094  1.00 16.19  ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 9.336  16.393  6.780  1.00 18.12  ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.734 16.506  7.031  1.00 21.16  ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.904  13.344  7.224  1.00 16.14  ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.399  11.964  7.186  1.00 15.44  ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 9.151  11.261  8.543  1.00 14.77  ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.955  10.402  8.942  1.00 15.68  ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.932 11.950  6.813  1.00 16.72  ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 11.222 12.521  5.448  1.00 18.53  ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 11.346 11.702  4.342  1.00 21.17  ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 11.334 13.814  5.047  1.00 19.91  ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 11.564 12.512  3.301  1.00 21.12  ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 11.572 13.789  3.668  1.00 20.98  ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 8.011  11.538  9.158  1.00 14.53  ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.672  10.995  10.477 1.00 14.98  ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.592  9.902   10.295 1.00 15.13  ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.661  10.065  9.509  1.00 15.52  ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.111  12.134  11.365 1.00 16.32  ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.810  11.754  12.851 1.00 18.47  ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.049  11.404  13.565 1.00 19.12  ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.151  12.951  13.604 1.00 20.45  ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.707  8.815   11.072 1.00 14.97  ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.732  7.709   11.015 1.00 14.78  ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.158  7.537   12.420 1.00 15.06  ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 5.915  7.509   13.379 1.00 16.38  ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.495  6.435   10.620 1.00 16.54  ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.124  6.547   9.215  1.00 16.80  ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.251  5.165   8.760  1.00 18.92  ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.553  5.349   10.058 1.00 22.92  ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 3.829  7.396   12.548 1.00 14.51  ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.224  7.247   13.886 1.00 15.20  ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 2.714  5.837   14.137 1.00 14.88  ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.311  5.125   13.202 1.00 16.07  ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.007  8.186   14.062 1.00 17.78  ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.254  9.661   14.021 1.00 22.10  ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 0.952  10.430  14.392 1.00 23.85  ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.343  10.089  15.014 1.00 24.33  ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 2.735  5.435   15.403 1.00 14.58  ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.227  4.131   15.820 1.00 14.34  ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 1.624  4.293   17.231 1.00 13.38  ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 1.880  5.293   17.926 1.00 14.34  ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 3.397  3.097   15.925 1.00 15.16  ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 0.820  3.292   17.627 1.00 13.27  ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.324  3.241   18.973 1.00 13.82  ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 1.371  2.452   19.796 1.00 16.10  ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 1.682  1.307   19.504 1.00 18.01  ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -1.047 2.551   19.006 1.00 14.53  ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -1.510 2.358   20.456 1.00 15.50  ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -2.065 3.363   18.183 1.00 15.27  ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 1.865  3.112   20.826 1.00 16.72  ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 2.881  2.503   21.684 1.00 17.72  ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 3.324  3.473   22.751 1.00 17.38  ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.121  4.684   22.634 1.00 17.85  ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 3.855  2.938   23.868 1.00 18.13  ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 4.335  3.815   24.917 1.00 18.46  ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 5.619  4.565   24.539 1.00 17.50  ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 6.558  3.974   23.994 1.00 17.32  ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 4.561  3.027   26.226 1.00 17.90  ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 4.979  3.932   27.354 1.00 18.80  ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 4.086  4.817   27.920 1.00 19.90  ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 6.203  4.145   27.902 1.00 18.70  ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 4.788  5.528   28.808 1.00 19.80  ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 6.062  5.143   28.836 1.00 19.27  ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 5.693  5.826   24.863 1.00 17.78  ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 6.877  6.607   24.740 1.00 17.21  ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 6.858  7.775   25.727 1.00 18.79  ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 5.777  8.288   26.056 1.00 20.78  ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 7.165  7.013   23.293 1.00 18.93  ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 6.137  7.880   22.854 1.00 20.75  ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 8.078  8.163   26.180 1.00 16.82  ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 8.437  9.315   27.035 1.00 17.11  ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 9.616  10.036  26.363 1.00 17.99  ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 10.289 9.462   25.481 1.00 16.69  ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 8.835  8.857   28.442 1.00 19.30  ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 7.671  8.144   29.090 1.00 21.21  ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 7.920  7.565   30.468 1.00 24.23  ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 8.744  8.124   31.226 1.00 26.72  ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 7.283  6.548   30.797 1.00 21.89  ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 9.855  11.320  26.662 1.00 18.37  ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 10.885 12.068  25.892 1.00 18.34  ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 12.259 11.375  25.785 1.00 18.02  ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 12.830 11.307  24.679 1.00 17.39  ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 10.910 13.430  26.604 1.00 20.74  ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 9.479  13.584  27.121 1.00 21.16  ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 9.109  12.204  27.591 1.00 18.65  ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 12.771 10.783  26.865 1.00 16.77  ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 14.066 10.091  26.850 1.00 16.22  ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 14.082 8.775   26.078 1.00 14.86  ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 15.142 8.168   25.932 1.00 15.63  ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 12.929 8.335   25.576 1.00 13.92  ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 12.884 7.166   24.673 1.00 13.53  ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 13.405 7.516   23.269 1.00 13.80  ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 13.692 6.610   22.477 1.00 13.52  ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 11.447 6.596   24.548 1.00 13.36  ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 11.061 5.879   25.819 1.00 13.94  ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 11.926 5.210   26.389 1.00 14.74  ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 9.861  5.947   26.206 1.00 14.33  ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 13.593 8.825   22.960 1.00 13.55  ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 14.150 9.191   21.626 1.00 13.19  ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 15.492 8.476   21.411 1.00 13.52  ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 16.328 8.383   22.312 1.00 13.92  ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 14.331 10.705  21.549 1.00 13.97  ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 12.784 11.605  21.250 1.00 15.33  ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 15.678 7.961   20.197 1.00 12.47  ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 16.905 7.256   19.858 1.00 12.92  ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 16.726 5.754   19.772 1.00 13.10  ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 17.586 5.066   19.199 1.00 13.96  ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 15.652 5.220   20.377 1.00 13.03  ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 15.416 3.784   20.294 1.00 12.74  ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.191 3.353   18.845 1.00 12.12  ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 14.502 4.068   18.100 1.00 12.48  ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 15.706 2.175   18.451 1.00 11.97  ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 15.551 1.761   17.043 1.00 11.57  ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.192 1.120   16.761 1.00 11.43  ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 13.737 0.302   17.552 1.00 11.99  ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 16.698 0.787   16.711 1.00 12.00  ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 17.969 1.635   16.441 1.00 14.07  ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 16.408 -0.133  15.492 1.00 13.57  ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 19.246 0.785   16.322 1.00 16.89  ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 13.615 1.433   15.572 1.00 11.55  ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 12.506 0.702   14.980 1.00 11.49  ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.145 -0.139  13.853 1.00 12.17  ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 13.910 0.414   13.018 1.00 12.54  ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 11.516 1.710   14.333 1.00 12.37  ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.427 1.084   13.445 1.00 13.56  ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 9.421  0.270   14.313 1.00 13.86  ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.620  2.193   12.686 1.00 14.97  ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 12.835 -1.435  13.823 1.00 12.32  ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.391 -2.321  12.785 1.00 13.08  ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.332 -3.255  12.257 1.00 13.65  ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.298 -3.544  12.885 1.00 13.66  ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.569 -3.123  13.369 1.00 13.77  ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 14.117 -4.109  14.450 1.00 14.24  ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 15.352 -4.844  14.987 1.00 15.52  ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 16.127 -3.981  15.883 1.00 17.18  ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 17.436 -3.761  15.800 1.00 16.17  ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 18.126 -4.180  14.738 1.00 17.28  ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 18.042 -3.007  16.702 1.00 18.12  ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.584 -3.715  11.026 1.00 14.35  ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.710 -4.694  10.364 1.00 16.93  ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.573 -5.883  9.951  1.00 19.91  ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 13.753 -5.970  10.305 1.00 19.34  ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.013 -4.047  9.169  1.00 17.42  ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.173 -3.656  7.817  1.00 17.04  ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 11.973 -6.844  9.190  1.00 22.07  ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 12.744 -7.985  8.730  1.00 24.10  ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 13.964 -7.616  7.849  1.00 24.19  ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 14.921 -8.386  7.787  1.00 26.98  ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 11.851 -9.030  7.997  1.00 28.68  ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.367 -8.527  6.646  1.00 34.34  ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.395 -9.453  5.951  1.00 40.87  ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.170  -9.346  6.118  1.00 42.30  ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.914 -10.344 5.124  1.00 40.66  ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.961 -6.418  7.242  1.00 20.61  ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 15.048 -5.975  6.336  1.00 20.34  ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.177 -5.200  7.007  1.00 20.53  ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.218 -4.945  6.388  1.00 22.71  ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.441 -5.125  5.216  1.00 20.34  ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.334 -5.859  4.507  1.00 22.06  ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 12.005 -5.495  4.644  1.00 23.67  ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.408 -6.897  3.623  1.00 24.82  ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 11.309 -6.337  3.890  1.00 26.27  ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 12.115 -7.198  3.254  1.00 26.97  ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.951 -4.751  8.257  1.00 18.53  ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 16.979 -3.971  8.943  1.00 17.27  ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.378 -2.799  9.717  1.00 14.90  ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.181 -2.791  10.026 1.00 14.92  ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.214 -1.782  9.988  1.00 14.17  ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.776 -0.574  10.731 1.00 13.73  ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.938 0.364   9.865  1.00 12.68  ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.327 0.703   8.736  1.00 12.92  ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.007 0.179   11.328 1.00 13.87  ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.576 1.483   12.007 1.00 14.32  ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 18.759 -0.725  12.311 1.00 14.48  ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.758 0.733   10.359 1.00 12.75  ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.816 1.585   9.663  1.00 12.65  ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.962 3.047   10.081 1.00 12.91  ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.809 3.969   9.277  1.00 13.65  ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.362 1.086   9.940  1.00 13.43  ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.283 2.046   9.377  1.00 15.76  ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.162 -0.332  9.410  1.00 14.86  ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.163 3.282   11.374 1.00 12.50  ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.286 4.649   11.899 1.00 12.58  ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.456 4.660   13.396 1.00 12.31  ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 14.788 3.603   13.968 1.00 12.32  ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.349 5.851   14.011 1.00 12.01  ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.542 5.992   15.472 1.00 11.60  ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.362 6.726   16.083 1.00 12.06  ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 12.760 7.591   15.442 1.00 12.87  ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 15.877 6.688   15.849 1.00 12.29  ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.014 8.033   15.119 1.00 14.10  ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.042 5.735   15.609 1.00 14.08  ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.283 8.859   15.596 1.00 14.91  ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.085 6.451   17.362 1.00 11.73  ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.029 7.180   18.088 1.00 11.70  ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.370 8.685   18.085 1.00 12.44  ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 13.531 9.043   18.356 1.00 12.01  ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 11.930 6.689   19.540 1.00 12.17  ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 10.924 7.530   20.347 1.00 13.11  ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 11.491 5.224   19.571 1.00 13.00  ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.389 9.544   17.771 1.00 12.79  ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 11.564 10.996  17.722 1.00 13.27  ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 10.441 11.753  18.421 1.00 15.07  ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 10.715 12.838  18.921 1.00 16.88  ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 11.714 11.435  16.270 1.00 14.62  ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 11.797 12.847  16.089 1.00 15.44  ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.202  11.215  18.490 1.00 14.77  ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.087  11.978  19.122 1.00 16.06  ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 7.212  11.002  19.974 1.00 17.67  ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 7.385  9.778   19.865 1.00 16.33  ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.189  12.684  18.039 1.00 16.45  ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 6.373  11.724  17.365 1.00 17.08  ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 7.970  13.563  17.048 1.00 16.71  ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 6.189  11.497  20.691 1.00 18.40  ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 5.256  10.587  21.366 1.00 19.53  ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 4.338  11.289  22.349 1.00 20.70  ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 4.292  12.510  22.366 1.00 21.78  ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 3.767  10.498  23.255 1.00 21.00  ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 2.827  10.961  24.273 1.00 21.49  ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 1.454  10.375  24.018 1.00 22.41  ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.111  10.029  22.869 1.00 22.11  ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 0.661  10.273  25.081 1.00 22.17  ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? -0.725 9.809   25.027 1.00 23.44  ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.915 8.517   24.288 1.00 21.83  ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.969 8.305   23.681 1.00 22.19  ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -1.606 10.904  24.457 1.00 26.50  ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -1.688 12.089  25.376 1.00 30.21  ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -2.057 11.962  26.550 1.00 33.35  ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -1.320 13.243  24.847 1.00 30.92  ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.010  7.593   24.499 1.00 18.58  ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? -0.100 6.285   23.900 1.00 17.81  ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 0.249  6.269   22.432 1.00 15.94  ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.076  5.211   21.839 1.00 17.80  ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 0.942  7.306   21.925 1.00 15.86  ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 1.482  7.285   20.544 1.00 15.44  ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.022  7.340   20.596 1.00 16.29  ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 3.601  7.849   21.579 1.00 17.70  ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.000  8.515   19.770 1.00 15.67  ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? -0.510 8.510   19.527 1.00 17.43  ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.969 9.909   19.126 1.00 19.80  ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.904 7.425   18.472 1.00 17.98  ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 3.653  6.830   19.553 1.00 13.66  ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.113  6.974   19.428 1.00 14.35  ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.341  7.339   17.926 1.00 14.56  ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 4.740  6.721   17.049 1.00 15.04  ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 5.840  5.680   19.857 1.00 14.32  ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 5.312  4.451   19.121 1.00 14.68  ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 7.361  5.821   19.695 1.00 14.75  ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.240  8.289   17.664 1.00 13.91  ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 6.566  8.675   16.286 1.00 13.57  ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.026  8.357   16.003 1.00 13.67  ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 8.891  8.515   16.874 1.00 14.87  ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.293  7.900   14.787 1.00 12.03  ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 9.669  7.511   14.394 1.00 12.49  ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.130 8.329   13.199 1.00 13.70  ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.387  8.494   12.226 1.00 14.55  ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 9.657  6.024   13.949 1.00 13.29  ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.040  5.077   14.972 1.00 13.35  ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 9.787  4.605   16.052 1.00 13.12  ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 7.717  4.680   14.855 1.00 14.32  ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.228  3.729   16.978 1.00 12.90  ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.165  3.799   15.770 1.00 14.16  ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 7.922  3.344   16.844 1.00 12.88  ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.390 8.802   13.279 1.00 12.63  ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.018 9.491   12.141 1.00 13.31  ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.510 8.404   11.175 1.00 13.22  ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.387 7.614   11.532 1.00 13.57  ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.164 10.359  12.639 1.00 13.15  ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.981 8.383   9.933  1.00 13.14  ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.400 7.380   8.955  1.00 14.26  ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.813 7.681   8.454  1.00 14.10  ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.171 8.855   8.273  1.00 14.87  ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.451 7.443   7.736  1.00 16.51  ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.703 6.416   6.672  1.00 21.98  ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.835 5.235   7.015  1.00 18.83  ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.861 6.816   5.482  1.00 27.90  ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.575 6.627   8.143  1.00 13.06  ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.905 6.764   7.516  1.00 13.32  ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 16.024 5.949   6.207  1.00 14.43  ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 17.096 5.963   5.596  1.00 13.57  ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.082 6.431   8.465  1.00 13.54  ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.094 7.338   9.709  1.00 14.50  ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.103 4.957   8.850  1.00 14.18  ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.954 5.248   5.786  1.00 14.30  ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 15.021 4.334   4.637  1.00 14.14  ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 15.281 5.031   3.322  1.00 15.26  ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.763 4.392   2.365  1.00 16.31  ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.758 3.458   4.563  1.00 14.62  ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.663 2.467   5.730  1.00 14.66  ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.336 1.717   5.588  1.00 15.70  ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 11.195 2.605   5.849  1.00 15.79  ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.925  2.216   5.931  1.00 18.07  ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.592  0.954   5.658  1.00 18.12  ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.975  3.101   6.225  1.00 17.93  ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.991 6.351   3.226  1.00 14.86  ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 15.243 7.071   1.971  1.00 15.97  ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 16.692 7.596   1.875  1.00 15.81  ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 17.080 8.097   0.811  1.00 17.05  ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 14.260 8.243   1.848  1.00 16.79  ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 14.470 9.300   2.924  1.00 20.01  ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.575 8.926   4.128  1.00 19.23  ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 14.496 10.508  2.582  1.00 22.96  ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.485 7.536   2.967  1.00 14.70  ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.860 8.083   3.013  1.00 14.70  ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.823 7.041   2.461  1.00 15.02  ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 20.501 6.332   3.201  1.00 15.55  ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 19.219 8.473   4.465  1.00 14.88  ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 18.236 9.485   5.103  1.00 16.35  ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.619 9.754   6.576  1.00 16.11  ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 18.232 10.814  4.343  1.00 18.42  ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 19.814 6.911   1.127  1.00 14.83  ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 20.571 5.823   0.493  1.00 15.78  ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 22.074 5.958   0.688  1.00 15.85  ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 22.779 4.933   0.727  1.00 17.38  ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 20.230 5.703   -1.023 1.00 16.44  ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 18.714 5.656   -1.343 1.00 19.19  ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 18.512 5.405   -2.835 1.00 20.66  ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.953 4.600   -0.544 1.00 20.25  ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 22.567 7.195   0.869  1.00 15.29  ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.992 7.432   1.036  1.00 15.37  ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 24.549 6.825   2.344  1.00 16.34  ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.777 6.701   2.482  1.00 17.88  ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 24.296 8.944   0.918  1.00 15.97  ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 23.483 9.788   1.861  1.00 15.76  ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 22.315 10.439  1.579  1.00 16.63  ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 23.790 10.077  3.245  1.00 16.08  ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 21.860 11.096  2.708  1.00 17.70  ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 22.776 10.927  3.722  1.00 16.63  ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.872 9.770   4.090  1.00 16.96  ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.789 11.425  5.033  1.00 17.77  ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.891 10.286  5.375  1.00 18.27  ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.869 11.108  5.822  1.00 17.63  ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.671 6.477   3.323  1.00 15.27  ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 24.160 5.823   4.545  1.00 17.19  ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.852 4.485   4.238  1.00 19.39  ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.706 4.048   5.032  1.00 20.13  ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.995 5.545   5.499  1.00 16.25  ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.422 6.772   6.188  1.00 16.56  ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 21.155 6.402   6.979  1.00 17.64  ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.492 7.416   7.131  1.00 17.26  ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.548 3.861   3.042  1.00 21.04  ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 25.111 2.549   2.650  1.00 23.56  ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 26.460 2.619   1.937  1.00 27.72  ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 27.021 1.568   1.604  1.00 28.69  ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 24.134 1.774   1.725  1.00 23.47  ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.789 1.442   2.304  1.00 27.47  ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 22.637 1.543   3.535  1.00 27.98  ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.864 1.094   1.521  1.00 33.49  ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.988 3.823   1.687  1.00 29.24  ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 28.264 3.952   0.965  1.00 32.83  ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 29.236 4.959   1.628  1.00 35.19  ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.840 5.661   2.547  1.00 34.76  ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 27.947 4.379   -0.478 1.00 37.12  ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 27.263 5.734   -0.535 1.00 43.82  ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 26.424 6.017   -1.767 1.00 50.31  ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 26.115 7.208   -2.012 1.00 49.51  ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 26.076 5.050   -2.485 1.00 53.35  ? 145 GLU   A OE2 1 
ATOM   1078 N  N   . GLU   A 1 140 ? 30.459 5.099   1.072  1.00 38.19  ? 146 GLU   A N   1 
ATOM   1079 C  CA  . GLU   A 1 140 ? 31.548 6.042   1.404  1.00 41.56  ? 146 GLU   A CA  1 
ATOM   1080 C  C   . GLU   A 1 140 ? 32.688 5.374   2.140  1.00 43.66  ? 146 GLU   A C   1 
ATOM   1081 O  O   . GLU   A 1 140 ? 33.593 4.874   1.479  1.00 44.67  ? 146 GLU   A O   1 
ATOM   1082 C  CB  . GLU   A 1 140 ? 31.083 7.306   2.130  1.00 45.23  ? 146 GLU   A CB  1 
ATOM   1083 C  CG  . GLU   A 1 140 ? 32.167 8.338   2.377  1.00 51.24  ? 146 GLU   A CG  1 
ATOM   1084 C  CD  . GLU   A 1 140 ? 32.278 9.415   1.315  1.00 59.01  ? 146 GLU   A CD  1 
ATOM   1085 O  OE1 . GLU   A 1 140 ? 31.235 10.012  0.960  1.00 61.42  ? 146 GLU   A OE1 1 
ATOM   1086 O  OE2 . GLU   A 1 140 ? 33.409 9.665   0.838  1.00 59.98  ? 146 GLU   A OE2 1 
ATOM   1087 N  N   . SER   B 1 1   ? 21.964 -21.345 7.648  1.00 19.79  ? 7   SER   C N   1 
ATOM   1088 C  CA  . SER   B 1 1   ? 20.827 -21.140 8.568  1.00 19.52  ? 7   SER   C CA  1 
ATOM   1089 C  C   . SER   B 1 1   ? 20.818 -22.221 9.657  1.00 18.81  ? 7   SER   C C   1 
ATOM   1090 O  O   . SER   B 1 1   ? 21.493 -23.255 9.522  1.00 19.55  ? 7   SER   C O   1 
ATOM   1091 C  CB  . SER   B 1 1   ? 19.507 -21.205 7.792  1.00 22.88  ? 7   SER   C CB  1 
ATOM   1092 O  OG  . SER   B 1 1   ? 19.326 -22.517 7.279  1.00 27.41  ? 7   SER   C OG  1 
ATOM   1093 N  N   . GLY   B 1 2   ? 20.044 -21.994 10.728 1.00 18.10  ? 8   GLY   C N   1 
ATOM   1094 C  CA  . GLY   B 1 2   ? 19.916 -22.990 11.788 1.00 17.66  ? 8   GLY   C CA  1 
ATOM   1095 C  C   . GLY   B 1 2   ? 19.655 -22.385 13.147 1.00 16.73  ? 8   GLY   C C   1 
ATOM   1096 O  O   . GLY   B 1 2   ? 20.022 -21.243 13.392 1.00 17.20  ? 8   GLY   C O   1 
ATOM   1097 N  N   . ALA   B 1 3   ? 18.983 -23.121 14.029 1.00 15.49  ? 9   ALA   C N   1 
ATOM   1098 C  CA  . ALA   B 1 3   ? 18.677 -22.628 15.373 1.00 14.91  ? 9   ALA   C CA  1 
ATOM   1099 C  C   . ALA   B 1 3   ? 18.799 -23.744 16.403 1.00 14.13  ? 9   ALA   C C   1 
ATOM   1100 O  O   . ALA   B 1 3   ? 18.817 -24.939 16.040 1.00 15.68  ? 9   ALA   C O   1 
ATOM   1101 C  CB  . ALA   B 1 3   ? 17.234 -22.097 15.396 1.00 16.99  ? 9   ALA   C CB  1 
ATOM   1102 N  N   . ILE   B 1 4   ? 18.833 -23.358 17.695 1.00 13.72  ? 10  ILE   C N   1 
ATOM   1103 C  CA  . ILE   B 1 4   ? 18.749 -24.293 18.821 1.00 14.25  ? 10  ILE   C CA  1 
ATOM   1104 C  C   . ILE   B 1 4   ? 17.343 -24.115 19.425 1.00 14.22  ? 10  ILE   C C   1 
ATOM   1105 O  O   . ILE   B 1 4   ? 16.919 -22.961 19.635 1.00 15.14  ? 10  ILE   C O   1 
ATOM   1106 C  CB  . ILE   B 1 4   ? 19.800 -23.982 19.900 1.00 14.72  ? 10  ILE   C CB  1 
ATOM   1107 C  CG1 . ILE   B 1 4   ? 21.233 -23.837 19.323 1.00 15.64  ? 10  ILE   C CG1 1 
ATOM   1108 C  CG2 . ILE   B 1 4   ? 19.730 -25.068 21.008 1.00 16.21  ? 10  ILE   C CG2 1 
ATOM   1109 C  CD1 . ILE   B 1 4   ? 22.251 -23.234 20.360 1.00 17.00  ? 10  ILE   C CD1 1 
ATOM   1110 N  N   . TYR   B 1 5   ? 16.641 -25.224 19.714 1.00 13.90  ? 11  TYR   C N   1 
ATOM   1111 C  CA  . TYR   B 1 5   ? 15.313 -25.162 20.311 1.00 14.96  ? 11  TYR   C CA  1 
ATOM   1112 C  C   . TYR   B 1 5   ? 15.400 -25.848 21.690 1.00 15.13  ? 11  TYR   C C   1 
ATOM   1113 O  O   . TYR   B 1 5   ? 15.487 -27.066 21.759 1.00 16.45  ? 11  TYR   C O   1 
ATOM   1114 C  CB  . TYR   B 1 5   ? 14.253 -25.863 19.402 1.00 15.77  ? 11  TYR   C CB  1 
ATOM   1115 C  CG  . TYR   B 1 5   ? 14.048 -25.110 18.105 1.00 17.03  ? 11  TYR   C CG  1 
ATOM   1116 C  CD1 . TYR   B 1 5   ? 13.209 -23.997 18.045 1.00 16.91  ? 11  TYR   C CD1 1 
ATOM   1117 C  CD2 . TYR   B 1 5   ? 14.736 -25.470 16.952 1.00 18.26  ? 11  TYR   C CD2 1 
ATOM   1118 C  CE1 . TYR   B 1 5   ? 13.078 -23.262 16.876 1.00 18.11  ? 11  TYR   C CE1 1 
ATOM   1119 C  CE2 . TYR   B 1 5   ? 14.592 -24.757 15.771 1.00 19.31  ? 11  TYR   C CE2 1 
ATOM   1120 C  CZ  . TYR   B 1 5   ? 13.774 -23.647 15.742 1.00 19.49  ? 11  TYR   C CZ  1 
ATOM   1121 O  OH  . TYR   B 1 5   ? 13.671 -22.910 14.579 1.00 21.56  ? 11  TYR   C OH  1 
ATOM   1122 N  N   . VAL   B 1 6   ? 15.411 -25.103 22.772 1.00 15.71  ? 12  VAL   C N   1 
ATOM   1123 C  CA  . VAL   B 1 6   ? 15.498 -25.646 24.139 1.00 16.89  ? 12  VAL   C CA  1 
ATOM   1124 C  C   . VAL   B 1 6   ? 14.351 -25.034 24.968 1.00 17.58  ? 12  VAL   C C   1 
ATOM   1125 O  O   . VAL   B 1 6   ? 14.173 -23.818 24.967 1.00 16.62  ? 12  VAL   C O   1 
ATOM   1126 C  CB  . VAL   B 1 6   ? 16.908 -25.374 24.746 1.00 17.92  ? 12  VAL   C CB  1 
ATOM   1127 C  CG1 . VAL   B 1 6   ? 17.268 -23.873 24.675 1.00 17.82  ? 12  VAL   C CG1 1 
ATOM   1128 C  CG2 . VAL   B 1 6   ? 16.975 -25.906 26.184 1.00 19.25  ? 12  VAL   C CG2 1 
ATOM   1129 N  N   . GLY   B 1 7   ? 13.529 -25.863 25.642 1.00 18.50  ? 13  GLY   C N   1 
ATOM   1130 C  CA  . GLY   B 1 7   ? 12.411 -25.327 26.412 1.00 18.67  ? 13  GLY   C CA  1 
ATOM   1131 C  C   . GLY   B 1 7   ? 11.483 -24.483 25.553 1.00 18.72  ? 13  GLY   C C   1 
ATOM   1132 O  O   . GLY   B 1 7   ? 11.217 -24.857 24.407 1.00 19.74  ? 13  GLY   C O   1 
ATOM   1133 N  N   . ASN   B 1 8   ? 11.162 -23.265 26.000 1.00 17.75  ? 14  ASN   C N   1 
ATOM   1134 C  CA  . ASN   B 1 8   ? 10.374 -22.357 25.167 1.00 18.32  ? 14  ASN   C CA  1 
ATOM   1135 C  C   . ASN   B 1 8   ? 11.241 -21.260 24.581 1.00 17.60  ? 14  ASN   C C   1 
ATOM   1136 O  O   . ASN   B 1 8   ? 10.790 -20.132 24.420 1.00 17.69  ? 14  ASN   C O   1 
ATOM   1137 C  CB  . ASN   B 1 8   ? 9.129  -21.793 25.900 1.00 20.78  ? 14  ASN   C CB  1 
ATOM   1138 C  CG  . ASN   B 1 8   ? 8.027  -22.840 26.072 1.00 27.49  ? 14  ASN   C CG  1 
ATOM   1139 O  OD1 . ASN   B 1 8   ? 7.135  -22.991 25.227 1.00 29.99  ? 14  ASN   C OD1 1 
ATOM   1140 N  ND2 . ASN   B 1 8   ? 8.122  -23.620 27.131 1.00 29.28  ? 14  ASN   C ND2 1 
ATOM   1141 N  N   . TYR   B 1 9   ? 12.467 -21.619 24.206 1.00 15.76  ? 15  TYR   C N   1 
ATOM   1142 C  CA  . TYR   B 1 9   ? 13.437 -20.657 23.617 1.00 15.90  ? 15  TYR   C CA  1 
ATOM   1143 C  C   . TYR   B 1 9   ? 13.911 -21.129 22.234 1.00 14.82  ? 15  TYR   C C   1 
ATOM   1144 O  O   . TYR   B 1 9   ? 14.094 -22.347 22.021 1.00 16.18  ? 15  TYR   C O   1 
ATOM   1145 C  CB  . TYR   B 1 9   ? 14.675 -20.505 24.519 1.00 16.69  ? 15  TYR   C CB  1 
ATOM   1146 C  CG  . TYR   B 1 9   ? 14.371 -19.993 25.915 1.00 17.10  ? 15  TYR   C CG  1 
ATOM   1147 C  CD1 . TYR   B 1 9   ? 13.821 -18.730 26.110 1.00 19.21  ? 15  TYR   C CD1 1 
ATOM   1148 C  CD2 . TYR   B 1 9   ? 14.674 -20.755 27.037 1.00 18.85  ? 15  TYR   C CD2 1 
ATOM   1149 C  CE1 . TYR   B 1 9   ? 13.563 -18.249 27.395 1.00 21.30  ? 15  TYR   C CE1 1 
ATOM   1150 C  CE2 . TYR   B 1 9   ? 14.454 -20.265 28.323 1.00 21.55  ? 15  TYR   C CE2 1 
ATOM   1151 C  CZ  . TYR   B 1 9   ? 13.908 -19.012 28.491 1.00 23.88  ? 15  TYR   C CZ  1 
ATOM   1152 O  OH  . TYR   B 1 9   ? 13.665 -18.537 29.767 1.00 28.50  ? 15  TYR   C OH  1 
ATOM   1153 N  N   . ARG   B 1 10  ? 14.140 -20.188 21.342 1.00 14.10  ? 16  ARG   C N   1 
ATOM   1154 C  CA  . ARG   B 1 10  ? 14.744 -20.412 20.019 1.00 14.39  ? 16  ARG   C CA  1 
ATOM   1155 C  C   . ARG   B 1 10  ? 16.008 -19.536 20.000 1.00 13.90  ? 16  ARG   C C   1 
ATOM   1156 O  O   . ARG   B 1 10  ? 15.911 -18.317 20.205 1.00 14.63  ? 16  ARG   C O   1 
ATOM   1157 C  CB  . ARG   B 1 10  ? 13.764 -19.983 18.892 1.00 16.05  ? 16  ARG   C CB  1 
ATOM   1158 C  CG  . ARG   B 1 10  ? 14.395 -19.792 17.501 1.00 17.35  ? 16  ARG   C CG  1 
ATOM   1159 C  CD  . ARG   B 1 10  ? 13.333 -19.526 16.442 1.00 17.31  ? 16  ARG   C CD  1 
ATOM   1160 N  NE  . ARG   B 1 10  ? 13.770 -18.562 15.408 1.00 18.73  ? 16  ARG   C NE  1 
ATOM   1161 C  CZ  . ARG   B 1 10  ? 14.258 -18.885 14.206 1.00 19.21  ? 16  ARG   C CZ  1 
ATOM   1162 N  NH1 . ARG   B 1 10  ? 14.518 -20.162 13.900 1.00 19.02  ? 16  ARG   C NH1 1 
ATOM   1163 N  NH2 . ARG   B 1 10  ? 14.571 -17.931 13.332 1.00 19.55  ? 16  ARG   C NH2 1 
ATOM   1164 N  N   . VAL   B 1 11  ? 17.195 -20.129 19.769 1.00 14.02  ? 17  VAL   C N   1 
ATOM   1165 C  CA  . VAL   B 1 11  ? 18.491 -19.425 19.732 1.00 13.71  ? 17  VAL   C CA  1 
ATOM   1166 C  C   . VAL   B 1 11  ? 18.952 -19.372 18.296 1.00 13.79  ? 17  VAL   C C   1 
ATOM   1167 O  O   . VAL   B 1 11  ? 19.104 -20.436 17.654 1.00 14.17  ? 17  VAL   C O   1 
ATOM   1168 C  CB  . VAL   B 1 11  ? 19.562 -20.143 20.593 1.00 14.30  ? 17  VAL   C CB  1 
ATOM   1169 C  CG1 . VAL   B 1 11  ? 20.819 -19.282 20.690 1.00 16.52  ? 17  VAL   C CG1 1 
ATOM   1170 C  CG2 . VAL   B 1 11  ? 19.017 -20.519 21.984 1.00 15.29  ? 17  VAL   C CG2 1 
ATOM   1171 N  N   . VAL   B 1 12  ? 19.189 -18.154 17.769 1.00 13.12  ? 18  VAL   C N   1 
ATOM   1172 C  CA  A VAL   B 1 12  ? 19.634 -17.982 16.378 0.50 12.78  ? 18  VAL   C CA  1 
ATOM   1173 C  CA  B VAL   B 1 12  ? 19.589 -17.994 16.371 0.50 14.53  ? 18  VAL   C CA  1 
ATOM   1174 C  C   . VAL   B 1 12  ? 20.775 -16.992 16.289 1.00 13.97  ? 18  VAL   C C   1 
ATOM   1175 O  O   . VAL   B 1 12  ? 21.044 -16.230 17.252 1.00 14.71  ? 18  VAL   C O   1 
ATOM   1176 C  CB  A VAL   B 1 12  ? 18.486 -17.466 15.453 0.50 12.68  ? 18  VAL   C CB  1 
ATOM   1177 C  CB  B VAL   B 1 12  ? 18.316 -17.464 15.599 0.50 17.83  ? 18  VAL   C CB  1 
ATOM   1178 C  CG1 A VAL   B 1 12  ? 17.505 -18.573 15.125 0.50 13.86  ? 18  VAL   C CG1 1 
ATOM   1179 C  CG1 B VAL   B 1 12  ? 18.556 -17.261 14.116 0.50 18.05  ? 18  VAL   C CG1 1 
ATOM   1180 C  CG2 A VAL   B 1 12  ? 17.837 -16.175 15.996 0.50 10.12  ? 18  VAL   C CG2 1 
ATOM   1181 C  CG2 B VAL   B 1 12  ? 17.132 -18.392 15.783 0.50 20.46  ? 18  VAL   C CG2 1 
ATOM   1182 N  N   . ASN   B 1 13  ? 21.459 -16.936 15.125 1.00 12.82  ? 19  ASN   C N   1 
ATOM   1183 C  CA  . ASN   B 1 13  ? 22.470 -15.887 14.931 1.00 13.44  ? 19  ASN   C CA  1 
ATOM   1184 C  C   . ASN   B 1 13  ? 21.660 -14.544 14.868 1.00 13.91  ? 19  ASN   C C   1 
ATOM   1185 O  O   . ASN   B 1 13  ? 20.639 -14.463 14.180 1.00 13.64  ? 19  ASN   C O   1 
ATOM   1186 C  CB  . ASN   B 1 13  ? 23.163 -16.044 13.554 1.00 13.90  ? 19  ASN   C CB  1 
ATOM   1187 C  CG  . ASN   B 1 13  ? 24.000 -17.309 13.481 1.00 13.55  ? 19  ASN   C CG  1 
ATOM   1188 O  OD1 . ASN   B 1 13  ? 23.534 -18.376 13.065 1.00 15.36  ? 19  ASN   C OD1 1 
ATOM   1189 N  ND2 . ASN   B 1 13  ? 25.257 -17.207 13.912 1.00 13.94  ? 19  ASN   C ND2 1 
ATOM   1190 N  N   . ARG   B 1 14  ? 22.146 -13.508 15.583 1.00 13.33  ? 20  ARG   C N   1 
ATOM   1191 C  CA  . ARG   B 1 14  ? 21.408 -12.221 15.605 1.00 13.10  ? 20  ARG   C CA  1 
ATOM   1192 C  C   . ARG   B 1 14  ? 21.253 -11.680 14.169 1.00 14.79  ? 20  ARG   C C   1 
ATOM   1193 O  O   . ARG   B 1 14  ? 20.185 -11.137 13.820 1.00 15.02  ? 20  ARG   C O   1 
ATOM   1194 C  CB  . ARG   B 1 14  ? 22.170 -11.210 16.468 1.00 13.05  ? 20  ARG   C CB  1 
ATOM   1195 C  CG  . ARG   B 1 14  ? 21.381 -9.894  16.718 1.00 14.72  ? 20  ARG   C CG  1 
ATOM   1196 C  CD  . ARG   B 1 14  ? 22.244 -8.918  17.473 1.00 15.72  ? 20  ARG   C CD  1 
ATOM   1197 N  NE  . ARG   B 1 14  ? 21.577 -7.660  17.913 1.00 15.76  ? 20  ARG   C NE  1 
ATOM   1198 C  CZ  . ARG   B 1 14  ? 21.494 -6.560  17.176 1.00 16.40  ? 20  ARG   C CZ  1 
ATOM   1199 N  NH1 . ARG   B 1 14  ? 21.838 -6.586  15.891 1.00 17.42  ? 20  ARG   C NH1 1 
ATOM   1200 N  NH2 . ARG   B 1 14  ? 20.989 -5.439  17.696 1.00 15.87  ? 20  ARG   C NH2 1 
ATOM   1201 N  N   . HIS   B 1 15  ? 22.274 -11.882 13.318 1.00 13.78  ? 21  HIS   C N   1 
ATOM   1202 C  CA  . HIS   B 1 15  ? 22.186 -11.341 11.934 1.00 15.00  ? 21  HIS   C CA  1 
ATOM   1203 C  C   . HIS   B 1 15  ? 21.173 -12.070 11.045 1.00 15.97  ? 21  HIS   C C   1 
ATOM   1204 O  O   . HIS   B 1 15  ? 20.854 -11.554 9.975  1.00 17.80  ? 21  HIS   C O   1 
ATOM   1205 C  CB  . HIS   B 1 15  ? 23.586 -11.254 11.267 1.00 15.24  ? 21  HIS   C CB  1 
ATOM   1206 C  CG  . HIS   B 1 15  ? 24.168 -12.571 10.828 1.00 14.61  ? 21  HIS   C CG  1 
ATOM   1207 N  ND1 . HIS   B 1 15  ? 24.907 -13.380 11.698 1.00 16.06  ? 21  HIS   C ND1 1 
ATOM   1208 C  CD2 . HIS   B 1 15  ? 24.160 -13.139 9.597  1.00 15.85  ? 21  HIS   C CD2 1 
ATOM   1209 C  CE1 . HIS   B 1 15  ? 25.284 -14.437 10.972 1.00 16.92  ? 21  HIS   C CE1 1 
ATOM   1210 N  NE2 . HIS   B 1 15  ? 24.868 -14.329 9.704  1.00 16.12  ? 21  HIS   C NE2 1 
ATOM   1211 N  N   . LEU   B 1 16  ? 20.656 -13.236 11.484 1.00 14.92  ? 22  LEU   C N   1 
ATOM   1212 C  CA  . LEU   B 1 16  ? 19.628 -13.985 10.750 1.00 16.23  ? 22  LEU   C CA  1 
ATOM   1213 C  C   . LEU   B 1 16  ? 18.244 -13.922 11.418 1.00 16.91  ? 22  LEU   C C   1 
ATOM   1214 O  O   . LEU   B 1 16  ? 17.317 -14.642 10.994 1.00 17.94  ? 22  LEU   C O   1 
ATOM   1215 C  CB  . LEU   B 1 16  ? 20.075 -15.439 10.535 1.00 16.19  ? 22  LEU   C CB  1 
ATOM   1216 C  CG  . LEU   B 1 16  ? 21.371 -15.563 9.725  1.00 16.94  ? 22  LEU   C CG  1 
ATOM   1217 C  CD1 . LEU   B 1 16  ? 21.803 -17.030 9.627  1.00 17.92  ? 22  LEU   C CD1 1 
ATOM   1218 C  CD2 . LEU   B 1 16  ? 21.254 -14.941 8.332  1.00 17.31  ? 22  LEU   C CD2 1 
ATOM   1219 N  N   . ALA   B 1 17  ? 18.108 -13.148 12.538 1.00 16.92  ? 23  ALA   C N   1 
ATOM   1220 C  CA  . ALA   B 1 17  ? 16.823 -13.087 13.244 1.00 16.90  ? 23  ALA   C CA  1 
ATOM   1221 C  C   . ALA   B 1 17  ? 15.703 -12.552 12.371 1.00 18.16  ? 23  ALA   C C   1 
ATOM   1222 O  O   . ALA   B 1 17  ? 15.914 -11.616 11.557 1.00 18.19  ? 23  ALA   C O   1 
ATOM   1223 C  CB  . ALA   B 1 17  ? 16.968 -12.240 14.516 1.00 17.80  ? 23  ALA   C CB  1 
ATOM   1224 N  N   . THR   B 1 18  ? 14.518 -13.147 12.528 1.00 17.35  ? 24  THR   C N   1 
ATOM   1225 C  CA  . THR   B 1 18  ? 13.344 -12.736 11.741 1.00 17.87  ? 24  THR   C CA  1 
ATOM   1226 C  C   . THR   B 1 18  ? 12.529 -11.645 12.500 1.00 18.21  ? 24  THR   C C   1 
ATOM   1227 O  O   . THR   B 1 18  ? 12.768 -11.362 13.684 1.00 18.72  ? 24  THR   C O   1 
ATOM   1228 C  CB  . THR   B 1 18  ? 12.415 -13.970 11.505 1.00 19.53  ? 24  THR   C CB  1 
ATOM   1229 O  OG1 . THR   B 1 18  ? 11.894 -14.364 12.767 1.00 19.90  ? 24  THR   C OG1 1 
ATOM   1230 C  CG2 . THR   B 1 18  ? 13.134 -15.150 10.809 1.00 20.81  ? 24  THR   C CG2 1 
ATOM   1231 N  N   . HIS   B 1 19  ? 11.469 -11.077 11.823 1.00 18.85  ? 25  HIS   C N   1 
ATOM   1232 C  CA  . HIS   B 1 19  ? 10.569 -10.143 12.501 1.00 20.26  ? 25  HIS   C CA  1 
ATOM   1233 C  C   . HIS   B 1 19  ? 9.876  -10.875 13.650 1.00 18.91  ? 25  HIS   C C   1 
ATOM   1234 O  O   . HIS   B 1 19  ? 9.781  -10.292 14.726 1.00 19.66  ? 25  HIS   C O   1 
ATOM   1235 C  CB  . HIS   B 1 19  ? 9.464  -9.634  11.534 1.00 22.16  ? 25  HIS   C CB  1 
ATOM   1236 C  CG  . HIS   B 1 19  ? 8.316  -8.935  12.236 1.00 24.47  ? 25  HIS   C CG  1 
ATOM   1237 N  ND1 . HIS   B 1 19  ? 8.461  -7.668  12.788 1.00 27.10  ? 25  HIS   C ND1 1 
ATOM   1238 C  CD2 . HIS   B 1 19  ? 7.088  -9.409  12.559 1.00 26.92  ? 25  HIS   C CD2 1 
ATOM   1239 C  CE1 . HIS   B 1 19  ? 7.274  -7.356  13.299 1.00 27.23  ? 25  HIS   C CE1 1 
ATOM   1240 N  NE2 . HIS   B 1 19  ? 6.426  -8.389  13.228 1.00 27.62  ? 25  HIS   C NE2 1 
ATOM   1241 N  N   . ASN   B 1 20  ? 9.468  -12.153 13.461 1.00 18.66  ? 26  ASN   C N   1 
ATOM   1242 C  CA  . ASN   B 1 20  ? 8.827  -12.878 14.555 1.00 19.66  ? 26  ASN   C CA  1 
ATOM   1243 C  C   . ASN   B 1 20  ? 9.770  -13.036 15.741 1.00 18.34  ? 26  ASN   C C   1 
ATOM   1244 O  O   . ASN   B 1 20  ? 9.339  -12.934 16.884 1.00 18.04  ? 26  ASN   C O   1 
ATOM   1245 C  CB  . ASN   B 1 20  ? 8.294  -14.252 14.122 1.00 21.69  ? 26  ASN   C CB  1 
ATOM   1246 C  CG  . ASN   B 1 20  ? 7.494  -14.927 15.230 1.00 28.21  ? 26  ASN   C CG  1 
ATOM   1247 O  OD1 . ASN   B 1 20  ? 6.373  -14.511 15.553 1.00 30.49  ? 26  ASN   C OD1 1 
ATOM   1248 N  ND2 . ASN   B 1 20  ? 8.063  -15.944 15.875 1.00 30.29  ? 26  ASN   C ND2 1 
ATOM   1249 N  N   . ASP   B 1 21  ? 11.091 -13.240 15.476 1.00 17.69  ? 27  ASP   C N   1 
ATOM   1250 C  CA  . ASP   B 1 21  ? 12.039 -13.323 16.578 1.00 17.72  ? 27  ASP   C CA  1 
ATOM   1251 C  C   . ASP   B 1 21  ? 12.087 -12.007 17.378 1.00 17.17  ? 27  ASP   C C   1 
ATOM   1252 O  O   . ASP   B 1 21  ? 12.045 -12.022 18.619 1.00 17.73  ? 27  ASP   C O   1 
ATOM   1253 C  CB  . ASP   B 1 21  ? 13.465 -13.646 16.074 1.00 16.82  ? 27  ASP   C CB  1 
ATOM   1254 C  CG  . ASP   B 1 21  ? 13.655 -15.062 15.571 1.00 17.88  ? 27  ASP   C CG  1 
ATOM   1255 O  OD1 . ASP   B 1 21  ? 13.074 -15.990 16.173 1.00 18.23  ? 27  ASP   C OD1 1 
ATOM   1256 O  OD2 . ASP   B 1 21  ? 14.373 -15.241 14.558 1.00 17.48  ? 27  ASP   C OD2 1 
ATOM   1257 N  N   . TRP   B 1 22  ? 12.184 -10.861 16.673 1.00 17.11  ? 28  TRP   C N   1 
ATOM   1258 C  CA  . TRP   B 1 22  ? 12.241 -9.568  17.351 1.00 17.21  ? 28  TRP   C CA  1 
ATOM   1259 C  C   . TRP   B 1 22  ? 10.902 -9.220  18.062 1.00 17.27  ? 28  TRP   C C   1 
ATOM   1260 O  O   . TRP   B 1 22  ? 10.922 -8.588  19.125 1.00 17.79  ? 28  TRP   C O   1 
ATOM   1261 C  CB  . TRP   B 1 22  ? 12.602 -8.468  16.360 1.00 16.95  ? 28  TRP   C CB  1 
ATOM   1262 C  CG  . TRP   B 1 22  ? 14.086 -8.421  16.090 1.00 16.58  ? 28  TRP   C CG  1 
ATOM   1263 C  CD1 . TRP   B 1 22  ? 14.731 -8.904  14.983 1.00 17.14  ? 28  TRP   C CD1 1 
ATOM   1264 C  CD2 . TRP   B 1 22  ? 15.106 -7.830  16.921 1.00 15.99  ? 28  TRP   C CD2 1 
ATOM   1265 N  NE1 . TRP   B 1 22  ? 16.084 -8.617  15.056 1.00 17.90  ? 28  TRP   C NE1 1 
ATOM   1266 C  CE2 . TRP   B 1 22  ? 16.340 -7.986  16.251 1.00 17.06  ? 28  TRP   C CE2 1 
ATOM   1267 C  CE3 . TRP   B 1 22  ? 15.091 -7.141  18.143 1.00 18.08  ? 28  TRP   C CE3 1 
ATOM   1268 C  CZ2 . TRP   B 1 22  ? 17.523 -7.447  16.728 1.00 17.41  ? 28  TRP   C CZ2 1 
ATOM   1269 C  CZ3 . TRP   B 1 22  ? 16.297 -6.670  18.652 1.00 19.34  ? 28  TRP   C CZ3 1 
ATOM   1270 C  CH2 . TRP   B 1 22  ? 17.492 -6.823  17.936 1.00 18.50  ? 28  TRP   C CH2 1 
ATOM   1271 N  N   . ALA   B 1 23  ? 9.771  -9.704  17.525 1.00 17.29  ? 29  ALA   C N   1 
ATOM   1272 C  CA  . ALA   B 1 23  ? 8.441  -9.476  18.133 1.00 18.99  ? 29  ALA   C CA  1 
ATOM   1273 C  C   . ALA   B 1 23  ? 8.204  -10.359 19.378 1.00 20.36  ? 29  ALA   C C   1 
ATOM   1274 O  O   . ALA   B 1 23  ? 7.230  -10.145 20.112 1.00 21.73  ? 29  ALA   C O   1 
ATOM   1275 C  CB  . ALA   B 1 23  ? 7.338  -9.735  17.114 1.00 19.82  ? 29  ALA   C CB  1 
ATOM   1276 N  N   . ASN   B 1 24  ? 9.062  -11.391 19.587 1.00 19.61  ? 30  ASN   C N   1 
ATOM   1277 C  CA  . ASN   B 1 24  ? 8.965  -12.295 20.736 1.00 18.36  ? 30  ASN   C CA  1 
ATOM   1278 C  C   . ASN   B 1 24  ? 10.356 -12.357 21.428 1.00 18.22  ? 30  ASN   C C   1 
ATOM   1279 O  O   . ASN   B 1 24  ? 10.789 -13.414 21.863 1.00 18.23  ? 30  ASN   C O   1 
ATOM   1280 C  CB  . ASN   B 1 24  ? 8.509  -13.673 20.233 1.00 19.55  ? 30  ASN   C CB  1 
ATOM   1281 C  CG  . ASN   B 1 24  ? 7.072  -13.629 19.766 1.00 21.18  ? 30  ASN   C CG  1 
ATOM   1282 O  OD1 . ASN   B 1 24  ? 6.116  -13.618 20.597 1.00 23.29  ? 30  ASN   C OD1 1 
ATOM   1283 N  ND2 . ASN   B 1 24  ? 6.886  -13.531 18.448 1.00 22.60  ? 30  ASN   C ND2 1 
ATOM   1284 N  N   . LEU   B 1 25  ? 11.049 -11.235 21.523 1.00 18.83  ? 31  LEU   C N   1 
ATOM   1285 C  CA  . LEU   B 1 25  ? 12.430 -11.190 21.998 1.00 18.10  ? 31  LEU   C CA  1 
ATOM   1286 C  C   . LEU   B 1 25  ? 12.583 -11.504 23.477 1.00 19.06  ? 31  LEU   C C   1 
ATOM   1287 O  O   . LEU   B 1 25  ? 11.808 -11.009 24.309 1.00 20.51  ? 31  LEU   C O   1 
ATOM   1288 C  CB  . LEU   B 1 25  ? 12.989 -9.787  21.705 1.00 18.84  ? 31  LEU   C CB  1 
ATOM   1289 C  CG  . LEU   B 1 25  ? 14.467 -9.623  22.072 1.00 19.28  ? 31  LEU   C CG  1 
ATOM   1290 C  CD1 . LEU   B 1 25  ? 15.375 -10.494 21.189 1.00 19.46  ? 31  LEU   C CD1 1 
ATOM   1291 C  CD2 . LEU   B 1 25  ? 14.884 -8.182  21.954 1.00 20.69  ? 31  LEU   C CD2 1 
ATOM   1292 N  N   . VAL   B 1 26  ? 13.566 -12.349 23.803 1.00 18.12  ? 32  VAL   C N   1 
ATOM   1293 C  CA  . VAL   B 1 26  ? 13.926 -12.620 25.194 1.00 18.49  ? 32  VAL   C CA  1 
ATOM   1294 C  C   . VAL   B 1 26  ? 15.266 -11.902 25.515 1.00 19.07  ? 32  VAL   C C   1 
ATOM   1295 O  O   . VAL   B 1 26  ? 15.378 -11.212 26.542 1.00 20.35  ? 32  VAL   C O   1 
ATOM   1296 C  CB  . VAL   B 1 26  ? 14.076 -14.144 25.436 1.00 19.20  ? 32  VAL   C CB  1 
ATOM   1297 C  CG1 . VAL   B 1 26  ? 14.613 -14.424 26.842 1.00 21.14  ? 32  VAL   C CG1 1 
ATOM   1298 C  CG2 . VAL   B 1 26  ? 12.738 -14.855 25.238 1.00 18.98  ? 32  VAL   C CG2 1 
ATOM   1299 N  N   . TRP   B 1 27  ? 16.278 -12.043 24.637 1.00 17.61  ? 33  TRP   C N   1 
ATOM   1300 C  CA  . TRP   B 1 27  ? 17.594 -11.470 24.907 1.00 17.22  ? 33  TRP   C CA  1 
ATOM   1301 C  C   . TRP   B 1 27  ? 18.381 -11.414 23.591 1.00 16.97  ? 33  TRP   C C   1 
ATOM   1302 O  O   . TRP   B 1 27  ? 18.182 -12.285 22.732 1.00 17.23  ? 33  TRP   C O   1 
ATOM   1303 C  CB  . TRP   B 1 27  ? 18.338 -12.363 25.953 1.00 18.18  ? 33  TRP   C CB  1 
ATOM   1304 C  CG  . TRP   B 1 27  ? 19.813 -12.108 26.137 1.00 18.62  ? 33  TRP   C CG  1 
ATOM   1305 C  CD1 . TRP   B 1 27  ? 20.394 -11.151 26.926 1.00 20.40  ? 33  TRP   C CD1 1 
ATOM   1306 C  CD2 . TRP   B 1 27  ? 20.898 -12.811 25.500 1.00 17.45  ? 33  TRP   C CD2 1 
ATOM   1307 N  NE1 . TRP   B 1 27  ? 21.780 -11.251 26.859 1.00 20.77  ? 33  TRP   C NE1 1 
ATOM   1308 C  CE2 . TRP   B 1 27  ? 22.106 -12.273 26.003 1.00 18.64  ? 33  TRP   C CE2 1 
ATOM   1309 C  CE3 . TRP   B 1 27  ? 20.967 -13.845 24.548 1.00 17.64  ? 33  TRP   C CE3 1 
ATOM   1310 C  CZ2 . TRP   B 1 27  ? 23.363 -12.748 25.606 1.00 18.90  ? 33  TRP   C CZ2 1 
ATOM   1311 C  CZ3 . TRP   B 1 27  ? 22.220 -14.349 24.210 1.00 18.47  ? 33  TRP   C CZ3 1 
ATOM   1312 C  CH2 . TRP   B 1 27  ? 23.387 -13.750 24.677 1.00 18.79  ? 33  TRP   C CH2 1 
ATOM   1313 N  N   . GLU   B 1 28  ? 19.217 -10.400 23.418 1.00 16.75  ? 34  GLU   C N   1 
ATOM   1314 C  CA  . GLU   B 1 28  ? 20.077 -10.326 22.244 1.00 17.25  ? 34  GLU   C CA  1 
ATOM   1315 C  C   . GLU   B 1 28  ? 21.388 -9.656  22.591 1.00 17.16  ? 34  GLU   C C   1 
ATOM   1316 O  O   . GLU   B 1 28  ? 21.434 -8.779  23.489 1.00 16.94  ? 34  GLU   C O   1 
ATOM   1317 C  CB  . GLU   B 1 28  ? 19.392 -9.637  21.065 1.00 17.49  ? 34  GLU   C CB  1 
ATOM   1318 C  CG  . GLU   B 1 28  ? 18.856 -8.261  21.376 1.00 18.67  ? 34  GLU   C CG  1 
ATOM   1319 C  CD  . GLU   B 1 28  ? 19.819 -7.092  21.301 1.00 20.77  ? 34  GLU   C CD  1 
ATOM   1320 O  OE1 . GLU   B 1 28  ? 19.585 -6.065  21.982 1.00 24.23  ? 34  GLU   C OE1 1 
ATOM   1321 O  OE2 . GLU   B 1 28  ? 20.816 -7.193  20.550 1.00 19.18  ? 34  GLU   C OE2 1 
ATOM   1322 N  N   . ASP   B 1 29  ? 22.466 -10.025 21.878 1.00 15.93  ? 35  ASP   C N   1 
ATOM   1323 C  CA  . ASP   B 1 29  ? 23.756 -9.400  22.113 1.00 15.99  ? 35  ASP   C CA  1 
ATOM   1324 C  C   . ASP   B 1 29  ? 24.517 -9.350  20.785 1.00 15.99  ? 35  ASP   C C   1 
ATOM   1325 O  O   . ASP   B 1 29  ? 24.943 -10.387 20.284 1.00 16.04  ? 35  ASP   C O   1 
ATOM   1326 C  CB  . ASP   B 1 29  ? 24.517 -10.191 23.202 1.00 16.71  ? 35  ASP   C CB  1 
ATOM   1327 C  CG  . ASP   B 1 29  ? 25.857 -9.612  23.594 1.00 23.32  ? 35  ASP   C CG  1 
ATOM   1328 O  OD1 . ASP   B 1 29  ? 26.573 -9.122  22.709 1.00 23.81  ? 35  ASP   C OD1 1 
ATOM   1329 O  OD2 . ASP   B 1 29  ? 26.225 -9.728  24.774 1.00 24.67  ? 35  ASP   C OD2 1 
ATOM   1330 N  N   . SER   B 1 30  ? 24.681 -8.148  20.204 1.00 15.81  ? 36  SER   C N   1 
ATOM   1331 C  CA  A SER   B 1 30  ? 25.381 -7.976  18.931 0.50 15.95  ? 36  SER   C CA  1 
ATOM   1332 C  CA  B SER   B 1 30  ? 25.366 -8.034  18.917 0.50 16.31  ? 36  SER   C CA  1 
ATOM   1333 C  C   . SER   B 1 30  ? 26.847 -8.435  19.008 1.00 16.44  ? 36  SER   C C   1 
ATOM   1334 O  O   . SER   B 1 30  ? 27.357 -9.045  18.046 1.00 16.00  ? 36  SER   C O   1 
ATOM   1335 C  CB  A SER   B 1 30  ? 25.320 -6.515  18.488 0.50 17.38  ? 36  SER   C CB  1 
ATOM   1336 C  CB  B SER   B 1 30  ? 25.217 -6.634  18.345 0.50 18.71  ? 36  SER   C CB  1 
ATOM   1337 O  OG  A SER   B 1 30  ? 26.181 -6.249  17.389 0.50 17.07  ? 36  SER   C OG  1 
ATOM   1338 O  OG  B SER   B 1 30  ? 25.722 -5.711  19.292 0.50 20.26  ? 36  SER   C OG  1 
ATOM   1339 N  N   . SER   B 1 31  ? 27.514 -8.157  20.143 1.00 16.49  ? 37  SER   C N   1 
ATOM   1340 C  CA  . SER   B 1 31  ? 28.936 -8.551  20.275 1.00 16.26  ? 37  SER   C CA  1 
ATOM   1341 C  C   . SER   B 1 31  ? 29.113 -10.068 20.217 1.00 15.61  ? 37  SER   C C   1 
ATOM   1342 O  O   . SER   B 1 31  ? 30.195 -10.518 19.841 1.00 16.25  ? 37  SER   C O   1 
ATOM   1343 C  CB  . SER   B 1 31  ? 29.546 -7.986  21.545 1.00 20.28  ? 37  SER   C CB  1 
ATOM   1344 O  OG  . SER   B 1 31  ? 29.168 -8.707  22.698 1.00 26.18  ? 37  SER   C OG  1 
ATOM   1345 N  N   . ARG   B 1 32  ? 28.059 -10.854 20.542 1.00 15.46  ? 38  ARG   C N   1 
ATOM   1346 C  CA  . ARG   B 1 32  ? 28.147 -12.321 20.479 1.00 14.85  ? 38  ARG   C CA  1 
ATOM   1347 C  C   . ARG   B 1 32  ? 27.515 -12.903 19.195 1.00 14.70  ? 38  ARG   C C   1 
ATOM   1348 O  O   . ARG   B 1 32  ? 27.524 -14.124 18.988 1.00 14.17  ? 38  ARG   C O   1 
ATOM   1349 C  CB  . ARG   B 1 32  ? 27.414 -12.936 21.695 1.00 16.44  ? 38  ARG   C CB  1 
ATOM   1350 C  CG  . ARG   B 1 32  ? 28.085 -12.587 23.001 1.00 17.35  ? 38  ARG   C CG  1 
ATOM   1351 C  CD  . ARG   B 1 32  ? 27.357 -13.146 24.232 1.00 15.21  ? 38  ARG   C CD  1 
ATOM   1352 N  NE  . ARG   B 1 32  ? 27.413 -14.624 24.283 1.00 14.63  ? 38  ARG   C NE  1 
ATOM   1353 C  CZ  . ARG   B 1 32  ? 27.412 -15.356 25.397 1.00 14.64  ? 38  ARG   C CZ  1 
ATOM   1354 N  NH1 . ARG   B 1 32  ? 27.313 -14.776 26.585 1.00 15.76  ? 38  ARG   C NH1 1 
ATOM   1355 N  NH2 . ARG   B 1 32  ? 27.540 -16.679 25.328 1.00 14.79  ? 38  ARG   C NH2 1 
ATOM   1356 N  N   . ASP   B 1 33  ? 26.817 -12.060 18.397 1.00 13.48  ? 39  ASP   C N   1 
ATOM   1357 C  CA  . ASP   B 1 33  ? 26.031 -12.508 17.253 1.00 13.64  ? 39  ASP   C CA  1 
ATOM   1358 C  C   . ASP   B 1 33  ? 24.918 -13.478 17.694 1.00 13.23  ? 39  ASP   C C   1 
ATOM   1359 O  O   . ASP   B 1 33  ? 24.627 -14.419 16.963 1.00 13.50  ? 39  ASP   C O   1 
ATOM   1360 C  CB  . ASP   B 1 33  ? 26.874 -13.125 16.133 1.00 14.10  ? 39  ASP   C CB  1 
ATOM   1361 C  CG  . ASP   B 1 33  ? 26.101 -13.446 14.862 1.00 15.52  ? 39  ASP   C CG  1 
ATOM   1362 O  OD1 . ASP   B 1 33  ? 25.197 -12.654 14.491 1.00 15.98  ? 39  ASP   C OD1 1 
ATOM   1363 O  OD2 . ASP   B 1 33  ? 26.402 -14.479 14.220 1.00 14.30  ? 39  ASP   C OD2 1 
ATOM   1364 N  N   . LEU   B 1 34  ? 24.282 -13.241 18.875 1.00 13.37  ? 40  LEU   C N   1 
ATOM   1365 C  CA  . LEU   B 1 34  ? 23.189 -14.133 19.319 1.00 13.39  ? 40  LEU   C CA  1 
ATOM   1366 C  C   . LEU   B 1 34  ? 21.901 -13.389 19.572 1.00 13.44  ? 40  LEU   C C   1 
ATOM   1367 O  O   . LEU   B 1 34  ? 21.928 -12.237 20.043 1.00 14.26  ? 40  LEU   C O   1 
ATOM   1368 C  CB  . LEU   B 1 34  ? 23.559 -14.851 20.634 1.00 13.72  ? 40  LEU   C CB  1 
ATOM   1369 C  CG  . LEU   B 1 34  ? 24.660 -15.945 20.545 1.00 14.19  ? 40  LEU   C CG  1 
ATOM   1370 C  CD1 . LEU   B 1 34  ? 24.898 -16.556 21.953 1.00 15.69  ? 40  LEU   C CD1 1 
ATOM   1371 C  CD2 . LEU   B 1 34  ? 24.268 -17.065 19.569 1.00 15.40  ? 40  LEU   C CD2 1 
ATOM   1372 N  N   . LEU   B 1 35  ? 20.796 -14.086 19.371 1.00 13.16  ? 41  LEU   C N   1 
ATOM   1373 C  CA  . LEU   B 1 35  ? 19.459 -13.561 19.719 1.00 13.78  ? 41  LEU   C CA  1 
ATOM   1374 C  C   . LEU   B 1 35  ? 18.623 -14.776 20.134 1.00 14.49  ? 41  LEU   C C   1 
ATOM   1375 O  O   . LEU   B 1 35  ? 18.723 -15.848 19.531 1.00 15.69  ? 41  LEU   C O   1 
ATOM   1376 C  CB  . LEU   B 1 35  ? 18.824 -12.828 18.510 1.00 13.94  ? 41  LEU   C CB  1 
ATOM   1377 C  CG  . LEU   B 1 35  ? 17.416 -12.250 18.766 1.00 14.45  ? 41  LEU   C CG  1 
ATOM   1378 C  CD1 . LEU   B 1 35  ? 17.235 -10.931 18.026 1.00 16.57  ? 41  LEU   C CD1 1 
ATOM   1379 C  CD2 . LEU   B 1 35  ? 16.300 -13.261 18.435 1.00 14.98  ? 41  LEU   C CD2 1 
ATOM   1380 N  N   . VAL   B 1 36  ? 17.842 -14.606 21.204 1.00 14.58  ? 42  VAL   C N   1 
ATOM   1381 C  CA  . VAL   B 1 36  ? 16.951 -15.634 21.721 1.00 14.56  ? 42  VAL   C CA  1 
ATOM   1382 C  C   . VAL   B 1 36  ? 15.526 -15.094 21.727 1.00 14.83  ? 42  VAL   C C   1 
ATOM   1383 O  O   . VAL   B 1 36  ? 15.289 -13.979 22.238 1.00 15.71  ? 42  VAL   C O   1 
ATOM   1384 C  CB  . VAL   B 1 36  ? 17.364 -16.086 23.144 1.00 14.91  ? 42  VAL   C CB  1 
ATOM   1385 C  CG1 . VAL   B 1 36  ? 16.392 -17.137 23.694 1.00 16.46  ? 42  VAL   C CG1 1 
ATOM   1386 C  CG2 . VAL   B 1 36  ? 18.813 -16.630 23.137 1.00 15.72  ? 42  VAL   C CG2 1 
ATOM   1387 N  N   . SER   B 1 37  ? 14.598 -15.865 21.163 1.00 14.27  ? 43  SER   C N   1 
ATOM   1388 C  CA  . SER   B 1 37  ? 13.181 -15.509 21.146 1.00 14.91  ? 43  SER   C CA  1 
ATOM   1389 C  C   . SER   B 1 37  ? 12.379 -16.593 21.856 1.00 16.22  ? 43  SER   C C   1 
ATOM   1390 O  O   . SER   B 1 37  ? 12.870 -17.709 22.095 1.00 15.87  ? 43  SER   C O   1 
ATOM   1391 C  CB  . SER   B 1 37  ? 12.703 -15.301 19.711 1.00 17.12  ? 43  SER   C CB  1 
ATOM   1392 O  OG  . SER   B 1 37  ? 12.843 -16.464 18.907 1.00 17.84  ? 43  SER   C OG  1 
ATOM   1393 N  N   . SER   B 1 38  ? 11.131 -16.270 22.219 1.00 16.98  ? 44  SER   C N   1 
ATOM   1394 C  CA  . SER   B 1 38  ? 10.250 -17.241 22.874 1.00 18.31  ? 44  SER   C CA  1 
ATOM   1395 C  C   . SER   B 1 38  ? 9.418  -18.033 21.850 1.00 20.04  ? 44  SER   C C   1 
ATOM   1396 O  O   . SER   B 1 38  ? 9.097  -17.534 20.772 1.00 21.21  ? 44  SER   C O   1 
ATOM   1397 C  CB  . SER   B 1 38  ? 9.339  -16.540 23.884 1.00 20.81  ? 44  SER   C CB  1 
ATOM   1398 O  OG  . SER   B 1 38  ? 8.520  -15.616 23.192 1.00 25.92  ? 44  SER   C OG  1 
ATOM   1399 N  N   . THR   B 1 39  ? 9.061  -19.273 22.190 1.00 20.49  ? 45  THR   C N   1 
ATOM   1400 C  CA  . THR   B 1 39  ? 8.301  -20.160 21.309 1.00 20.88  ? 45  THR   C CA  1 
ATOM   1401 C  C   . THR   B 1 39  ? 7.017  -20.623 22.025 1.00 23.10  ? 45  THR   C C   1 
ATOM   1402 O  O   . THR   B 1 39  ? 6.974  -20.689 23.244 1.00 22.70  ? 45  THR   C O   1 
ATOM   1403 C  CB  . THR   B 1 39  ? 9.148  -21.420 20.942 1.00 21.11  ? 45  THR   C CB  1 
ATOM   1404 O  OG1 . THR   B 1 39  ? 9.407  -22.171 22.124 1.00 21.28  ? 45  THR   C OG1 1 
ATOM   1405 C  CG2 . THR   B 1 39  ? 10.510 -21.067 20.299 1.00 20.89  ? 45  THR   C CG2 1 
ATOM   1406 N  N   . THR   B 1 40  ? 6.022  -21.011 21.243 1.00 25.41  ? 46  THR   C N   1 
ATOM   1407 C  CA  . THR   B 1 40  ? 4.776  -21.537 21.801 1.00 27.77  ? 46  THR   C CA  1 
ATOM   1408 C  C   . THR   B 1 40  ? 4.964  -23.013 22.152 1.00 27.82  ? 46  THR   C C   1 
ATOM   1409 O  O   . THR   B 1 40  ? 4.553  -23.457 23.231 1.00 29.29  ? 46  THR   C O   1 
ATOM   1410 C  CB  . THR   B 1 40  ? 3.625  -21.276 20.832 1.00 31.97  ? 46  THR   C CB  1 
ATOM   1411 O  OG1 . THR   B 1 40  ? 3.939  -21.896 19.589 1.00 35.62  ? 46  THR   C OG1 1 
ATOM   1412 C  CG2 . THR   B 1 40  ? 3.426  -19.791 20.564 1.00 31.83  ? 46  THR   C CG2 1 
ATOM   1413 N  N   . ALA   B 1 41  ? 5.634  -23.775 21.259 1.00 26.00  ? 47  ALA   C N   1 
ATOM   1414 C  CA  . ALA   B 1 41  ? 5.880  -25.186 21.524 1.00 26.14  ? 47  ALA   C CA  1 
ATOM   1415 C  C   . ALA   B 1 41  ? 7.232  -25.424 22.199 1.00 24.45  ? 47  ALA   C C   1 
ATOM   1416 O  O   . ALA   B 1 41  ? 8.156  -24.649 22.003 1.00 23.79  ? 47  ALA   C O   1 
ATOM   1417 C  CB  . ALA   B 1 41  ? 5.810  -25.973 20.222 1.00 27.13  ? 47  ALA   C CB  1 
ATOM   1418 N  N   . GLN   B 1 42  ? 7.359  -26.490 22.978 1.00 23.29  ? 48  GLN   C N   1 
ATOM   1419 C  CA  . GLN   B 1 42  ? 8.608  -26.837 23.657 1.00 23.60  ? 48  GLN   C CA  1 
ATOM   1420 C  C   . GLN   B 1 42  ? 9.568  -27.498 22.682 1.00 22.87  ? 48  GLN   C C   1 
ATOM   1421 O  O   . GLN   B 1 42  ? 9.153  -28.285 21.821 1.00 24.57  ? 48  GLN   C O   1 
ATOM   1422 C  CB  . GLN   B 1 42  ? 8.345  -27.781 24.848 1.00 27.80  ? 48  GLN   C CB  1 
ATOM   1423 C  CG  . GLN   B 1 42  ? 7.696  -27.059 26.033 1.00 35.92  ? 48  GLN   C CG  1 
ATOM   1424 C  CD  . GLN   B 1 42  ? 7.500  -28.019 27.177 1.00 45.63  ? 48  GLN   C CD  1 
ATOM   1425 O  OE1 . GLN   B 1 42  ? 6.630  -28.896 27.144 1.00 50.06  ? 48  GLN   C OE1 1 
ATOM   1426 N  NE2 . GLN   B 1 42  ? 8.303  -27.879 28.221 1.00 47.88  ? 48  GLN   C NE2 1 
ATOM   1427 N  N   . GLY   B 1 43  ? 10.833 -27.137 22.815 1.00 20.74  ? 49  GLY   C N   1 
ATOM   1428 C  CA  . GLY   B 1 43  ? 11.950 -27.678 22.033 1.00 20.58  ? 49  GLY   C CA  1 
ATOM   1429 C  C   . GLY   B 1 43  ? 12.602 -28.827 22.766 1.00 20.16  ? 49  GLY   C C   1 
ATOM   1430 O  O   . GLY   B 1 43  ? 12.352 -29.028 23.967 1.00 22.56  ? 49  GLY   C O   1 
ATOM   1431 N  N   . CYS   B 1 44  ? 13.443 -29.578 22.052 1.00 18.81  ? 50  CYS   C N   1 
ATOM   1432 C  CA  . CYS   B 1 44  ? 14.007 -30.800 22.595 1.00 19.16  ? 50  CYS   C CA  1 
ATOM   1433 C  C   . CYS   B 1 44  ? 15.522 -30.858 22.652 1.00 19.26  ? 50  CYS   C C   1 
ATOM   1434 O  O   . CYS   B 1 44  ? 16.068 -31.906 23.031 1.00 21.82  ? 50  CYS   C O   1 
ATOM   1435 C  CB  . CYS   B 1 44  ? 13.456 -31.983 21.805 1.00 19.65  ? 50  CYS   C CB  1 
ATOM   1436 S  SG  . CYS   B 1 44  ? 11.644 -32.058 21.825 1.00 25.08  ? 50  CYS   C SG  1 
ATOM   1437 N  N   . ASP   B 1 45  ? 16.214 -29.803 22.242 1.00 16.41  ? 51  ASP   C N   1 
ATOM   1438 C  CA  . ASP   B 1 45  ? 17.667 -29.784 22.289 1.00 16.52  ? 51  ASP   C CA  1 
ATOM   1439 C  C   . ASP   B 1 45  ? 18.077 -29.594 23.768 1.00 17.72  ? 51  ASP   C C   1 
ATOM   1440 O  O   . ASP   B 1 45  ? 17.367 -28.937 24.566 1.00 19.70  ? 51  ASP   C O   1 
ATOM   1441 C  CB  . ASP   B 1 45  ? 18.219 -28.616 21.449 1.00 17.11  ? 51  ASP   C CB  1 
ATOM   1442 C  CG  . ASP   B 1 45  ? 18.044 -28.800 19.958 1.00 20.22  ? 51  ASP   C CG  1 
ATOM   1443 O  OD1 . ASP   B 1 45  ? 18.045 -29.955 19.493 1.00 21.23  ? 51  ASP   C OD1 1 
ATOM   1444 O  OD2 . ASP   B 1 45  ? 17.898 -27.780 19.242 1.00 18.30  ? 51  ASP   C OD2 1 
ATOM   1445 N  N   . THR   B 1 46  ? 19.219 -30.188 24.134 1.00 16.08  ? 52  THR   C N   1 
ATOM   1446 C  CA  . THR   B 1 46  ? 19.800 -30.017 25.467 1.00 15.82  ? 52  THR   C CA  1 
ATOM   1447 C  C   . THR   B 1 46  ? 21.091 -29.193 25.288 1.00 15.69  ? 52  THR   C C   1 
ATOM   1448 O  O   . THR   B 1 46  ? 21.894 -29.495 24.387 1.00 16.18  ? 52  THR   C O   1 
ATOM   1449 C  CB  . THR   B 1 46  ? 20.215 -31.391 26.018 1.00 18.43  ? 52  THR   C CB  1 
ATOM   1450 O  OG1 . THR   B 1 46  ? 19.030 -32.193 26.235 1.00 20.34  ? 52  THR   C OG1 1 
ATOM   1451 C  CG2 . THR   B 1 46  ? 21.011 -31.293 27.340 1.00 20.73  ? 52  THR   C CG2 1 
ATOM   1452 N  N   . ILE   B 1 47  ? 21.268 -28.149 26.108 1.00 15.04  ? 53  ILE   C N   1 
ATOM   1453 C  CA  . ILE   B 1 47  ? 22.495 -27.352 26.053 1.00 15.12  ? 53  ILE   C CA  1 
ATOM   1454 C  C   . ILE   B 1 47  ? 23.589 -28.051 26.876 1.00 14.72  ? 53  ILE   C C   1 
ATOM   1455 O  O   . ILE   B 1 47  ? 23.359 -28.480 28.019 1.00 15.04  ? 53  ILE   C O   1 
ATOM   1456 C  CB  . ILE   B 1 47  ? 22.256 -25.949 26.654 1.00 15.98  ? 53  ILE   C CB  1 
ATOM   1457 C  CG1 . ILE   B 1 47  ? 21.053 -25.257 26.031 1.00 16.90  ? 53  ILE   C CG1 1 
ATOM   1458 C  CG2 . ILE   B 1 47  ? 23.510 -25.089 26.555 1.00 16.44  ? 53  ILE   C CG2 1 
ATOM   1459 C  CD1 . ILE   B 1 47  ? 21.193 -25.127 24.452 1.00 18.93  ? 53  ILE   C CD1 1 
ATOM   1460 N  N   . ALA   B 1 48  ? 24.809 -28.107 26.338 1.00 13.99  ? 54  ALA   C N   1 
ATOM   1461 C  CA  . ALA   B 1 48  ? 25.944 -28.673 27.066 1.00 13.54  ? 54  ALA   C CA  1 
ATOM   1462 C  C   . ALA   B 1 48  ? 26.319 -27.749 28.223 1.00 13.28  ? 54  ALA   C C   1 
ATOM   1463 O  O   . ALA   B 1 48  ? 26.287 -26.506 28.084 1.00 14.04  ? 54  ALA   C O   1 
ATOM   1464 C  CB  . ALA   B 1 48  ? 27.144 -28.769 26.130 1.00 14.19  ? 54  ALA   C CB  1 
ATOM   1465 N  N   . ARG   B 1 49  ? 26.661 -28.344 29.380 1.00 13.20  ? 55  ARG   C N   1 
ATOM   1466 C  CA  . ARG   B 1 49  ? 27.125 -27.581 30.548 1.00 13.75  ? 55  ARG   C CA  1 
ATOM   1467 C  C   . ARG   B 1 49  ? 28.458 -28.259 30.909 1.00 14.20  ? 55  ARG   C C   1 
ATOM   1468 O  O   . ARG   B 1 49  ? 28.505 -29.296 31.610 1.00 15.99  ? 55  ARG   C O   1 
ATOM   1469 C  CB  . ARG   B 1 49  ? 26.103 -27.627 31.693 1.00 14.46  ? 55  ARG   C CB  1 
ATOM   1470 C  CG  . ARG   B 1 49  ? 24.734 -27.074 31.278 1.00 13.80  ? 55  ARG   C CG  1 
ATOM   1471 C  CD  . ARG   B 1 49  ? 24.738 -25.581 30.933 1.00 15.34  ? 55  ARG   C CD  1 
ATOM   1472 N  NE  . ARG   B 1 49  ? 23.376 -25.135 30.566 1.00 15.45  ? 55  ARG   C NE  1 
ATOM   1473 C  CZ  . ARG   B 1 49  ? 23.120 -24.034 29.850 1.00 16.09  ? 55  ARG   C CZ  1 
ATOM   1474 N  NH1 . ARG   B 1 49  ? 24.103 -23.213 29.507 1.00 15.62  ? 55  ARG   C NH1 1 
ATOM   1475 N  NH2 . ARG   B 1 49  ? 21.857 -23.718 29.521 1.00 17.23  ? 55  ARG   C NH2 1 
ATOM   1476 N  N   . CYS   B 1 50  ? 29.550 -27.677 30.405 1.00 13.39  ? 56  CYS   C N   1 
ATOM   1477 C  CA  . CYS   B 1 50  ? 30.873 -28.297 30.418 1.00 13.15  ? 56  CYS   C CA  1 
ATOM   1478 C  C   . CYS   B 1 50  ? 31.939 -27.337 29.884 1.00 13.48  ? 56  CYS   C C   1 
ATOM   1479 O  O   . CYS   B 1 50  ? 31.631 -26.230 29.435 1.00 14.27  ? 56  CYS   C O   1 
ATOM   1480 C  CB  . CYS   B 1 50  ? 30.792 -29.517 29.486 1.00 13.42  ? 56  CYS   C CB  1 
ATOM   1481 S  SG  . CYS   B 1 50  ? 30.676 -29.088 27.713 1.00 13.80  ? 56  CYS   C SG  1 
ATOM   1482 N  N   . ASP   B 1 51  ? 33.217 -27.799 29.908 1.00 14.85  ? 57  ASP   C N   1 
ATOM   1483 C  CA  . ASP   B 1 51  ? 34.341 -27.069 29.317 1.00 15.47  ? 57  ASP   C CA  1 
ATOM   1484 C  C   . ASP   B 1 51  ? 35.008 -27.924 28.193 1.00 16.36  ? 57  ASP   C C   1 
ATOM   1485 O  O   . ASP   B 1 51  ? 36.227 -27.834 27.983 1.00 16.97  ? 57  ASP   C O   1 
ATOM   1486 C  CB  . ASP   B 1 51  ? 35.369 -26.660 30.393 1.00 17.61  ? 57  ASP   C CB  1 
ATOM   1487 C  CG  . ASP   B 1 51  ? 36.050 -27.788 31.111 1.00 21.93  ? 57  ASP   C CG  1 
ATOM   1488 O  OD1 . ASP   B 1 51  ? 35.729 -28.956 30.824 1.00 21.52  ? 57  ASP   C OD1 1 
ATOM   1489 O  OD2 . ASP   B 1 51  ? 36.969 -27.497 31.936 1.00 28.89  ? 57  ASP   C OD2 1 
ATOM   1490 N  N   . CYS   B 1 52  ? 34.219 -28.769 27.497 1.00 15.78  ? 58  CYS   C N   1 
ATOM   1491 C  CA  . CYS   B 1 52  ? 34.766 -29.559 26.360 1.00 14.72  ? 58  CYS   C CA  1 
ATOM   1492 C  C   . CYS   B 1 52  ? 35.427 -28.681 25.333 1.00 13.81  ? 58  CYS   C C   1 
ATOM   1493 O  O   . CYS   B 1 52  ? 34.988 -27.536 25.105 1.00 14.14  ? 58  CYS   C O   1 
ATOM   1494 C  CB  . CYS   B 1 52  ? 33.679 -30.374 25.660 1.00 14.08  ? 58  CYS   C CB  1 
ATOM   1495 S  SG  . CYS   B 1 52  ? 33.081 -31.808 26.584 1.00 15.08  ? 58  CYS   C SG  1 
ATOM   1496 N  N   . GLN   B 1 53  ? 36.504 -29.199 24.743 1.00 13.48  ? 59  GLN   C N   1 
ATOM   1497 C  CA  . GLN   B 1 53  ? 37.162 -28.582 23.605 1.00 14.76  ? 59  GLN   C CA  1 
ATOM   1498 C  C   . GLN   B 1 53  ? 37.201 -29.524 22.395 1.00 14.19  ? 59  GLN   C C   1 
ATOM   1499 O  O   . GLN   B 1 53  ? 37.972 -29.292 21.448 1.00 14.12  ? 59  GLN   C O   1 
ATOM   1500 C  CB  . GLN   B 1 53  ? 38.584 -28.128 23.957 1.00 14.56  ? 59  GLN   C CB  1 
ATOM   1501 C  CG  . GLN   B 1 53  ? 38.623 -26.880 24.874 1.00 17.66  ? 59  GLN   C CG  1 
ATOM   1502 C  CD  . GLN   B 1 53  ? 40.000 -26.309 25.041 1.00 22.21  ? 59  GLN   C CD  1 
ATOM   1503 O  OE1 . GLN   B 1 53  ? 40.543 -26.334 26.165 1.00 22.84  ? 59  GLN   C OE1 1 
ATOM   1504 N  NE2 . GLN   B 1 53  ? 40.561 -25.782 23.945 1.00 19.29  ? 59  GLN   C NE2 1 
ATOM   1505 N  N   . THR   B 1 54  ? 36.422 -30.623 22.410 1.00 14.20  ? 60  THR   C N   1 
ATOM   1506 C  CA  . THR   B 1 54  ? 36.291 -31.476 21.226 1.00 14.39  ? 60  THR   C CA  1 
ATOM   1507 C  C   . THR   B 1 54  ? 34.802 -31.743 21.015 1.00 14.00  ? 60  THR   C C   1 
ATOM   1508 O  O   . THR   B 1 54  ? 34.028 -31.832 21.973 1.00 14.64  ? 60  THR   C O   1 
ATOM   1509 C  CB  . THR   B 1 54  ? 37.045 -32.789 21.316 1.00 17.87  ? 60  THR   C CB  1 
ATOM   1510 O  OG1 . THR   B 1 54  ? 36.542 -33.552 22.367 1.00 20.99  ? 60  THR   C OG1 1 
ATOM   1511 C  CG2 . THR   B 1 54  ? 38.536 -32.600 21.548 1.00 18.39  ? 60  THR   C CG2 1 
ATOM   1512 N  N   . GLY   B 1 55  ? 34.405 -31.823 19.741 1.00 12.61  ? 61  GLY   C N   1 
ATOM   1513 C  CA  . GLY   B 1 55  ? 32.997 -32.046 19.419 1.00 12.87  ? 61  GLY   C CA  1 
ATOM   1514 C  C   . GLY   B 1 55  ? 32.854 -32.257 17.919 1.00 12.43  ? 61  GLY   C C   1 
ATOM   1515 O  O   . GLY   B 1 55  ? 33.839 -32.570 17.236 1.00 13.81  ? 61  GLY   C O   1 
ATOM   1516 N  N   . VAL   B 1 56  ? 31.619 -32.133 17.449 1.00 11.74  ? 62  VAL   C N   1 
ATOM   1517 C  CA  . VAL   B 1 56  ? 31.306 -32.330 16.015 1.00 11.67  ? 62  VAL   C CA  1 
ATOM   1518 C  C   . VAL   B 1 56  ? 30.409 -31.186 15.597 1.00 11.69  ? 62  VAL   C C   1 
ATOM   1519 O  O   . VAL   B 1 56  ? 29.445 -30.886 16.300 1.00 13.00  ? 62  VAL   C O   1 
ATOM   1520 C  CB  . VAL   B 1 56  ? 30.551 -33.688 15.854 1.00 12.75  ? 62  VAL   C CB  1 
ATOM   1521 C  CG1 . VAL   B 1 56  ? 30.072 -33.877 14.415 1.00 14.03  ? 62  VAL   C CG1 1 
ATOM   1522 C  CG2 . VAL   B 1 56  ? 31.466 -34.871 16.251 1.00 13.33  ? 62  VAL   C CG2 1 
ATOM   1523 N  N   . TYR   B 1 57  ? 30.662 -30.608 14.399 1.00 11.71  ? 63  TYR   C N   1 
ATOM   1524 C  CA  . TYR   B 1 57  ? 29.774 -29.536 13.912 1.00 11.00  ? 63  TYR   C CA  1 
ATOM   1525 C  C   . TYR   B 1 57  ? 29.200 -29.875 12.527 1.00 12.03  ? 63  TYR   C C   1 
ATOM   1526 O  O   . TYR   B 1 57  ? 29.854 -30.582 11.748 1.00 13.25  ? 63  TYR   C O   1 
ATOM   1527 C  CB  . TYR   B 1 57  ? 30.447 -28.114 13.862 1.00 12.16  ? 63  TYR   C CB  1 
ATOM   1528 C  CG  . TYR   B 1 57  ? 31.308 -27.817 12.643 1.00 12.24  ? 63  TYR   C CG  1 
ATOM   1529 C  CD1 . TYR   B 1 57  ? 32.605 -28.301 12.552 1.00 13.02  ? 63  TYR   C CD1 1 
ATOM   1530 C  CD2 . TYR   B 1 57  ? 30.854 -26.969 11.633 1.00 12.75  ? 63  TYR   C CD2 1 
ATOM   1531 C  CE1 . TYR   B 1 57  ? 33.414 -28.013 11.443 1.00 14.01  ? 63  TYR   C CE1 1 
ATOM   1532 C  CE2 . TYR   B 1 57  ? 31.660 -26.655 10.532 1.00 13.39  ? 63  TYR   C CE2 1 
ATOM   1533 C  CZ  . TYR   B 1 57  ? 32.934 -27.186 10.441 1.00 13.95  ? 63  TYR   C CZ  1 
ATOM   1534 O  OH  . TYR   B 1 57  ? 33.769 -26.888 9.371  1.00 15.95  ? 63  TYR   C OH  1 
ATOM   1535 N  N   . TYR   B 1 58  ? 28.016 -29.304 12.249 1.00 11.84  ? 64  TYR   C N   1 
ATOM   1536 C  CA  . TYR   B 1 58  ? 27.410 -29.476 10.928 1.00 12.36  ? 64  TYR   C CA  1 
ATOM   1537 C  C   . TYR   B 1 58  ? 27.800 -28.336 9.998  1.00 12.65  ? 64  TYR   C C   1 
ATOM   1538 O  O   . TYR   B 1 58  ? 27.560 -27.146 10.308 1.00 12.69  ? 64  TYR   C O   1 
ATOM   1539 C  CB  . TYR   B 1 58  ? 25.878 -29.587 11.014 1.00 12.99  ? 64  TYR   C CB  1 
ATOM   1540 C  CG  . TYR   B 1 58  ? 25.284 -29.851 9.639  1.00 14.09  ? 64  TYR   C CG  1 
ATOM   1541 C  CD1 . TYR   B 1 58  ? 25.586 -31.016 8.943  1.00 14.49  ? 64  TYR   C CD1 1 
ATOM   1542 C  CD2 . TYR   B 1 58  ? 24.410 -28.954 9.057  1.00 14.55  ? 64  TYR   C CD2 1 
ATOM   1543 C  CE1 . TYR   B 1 58  ? 25.095 -31.245 7.660  1.00 15.32  ? 64  TYR   C CE1 1 
ATOM   1544 C  CE2 . TYR   B 1 58  ? 23.884 -29.189 7.783  1.00 15.55  ? 64  TYR   C CE2 1 
ATOM   1545 C  CZ  . TYR   B 1 58  ? 24.205 -30.355 7.112  1.00 16.12  ? 64  TYR   C CZ  1 
ATOM   1546 O  OH  . TYR   B 1 58  ? 23.740 -30.608 5.826  1.00 19.14  ? 64  TYR   C OH  1 
ATOM   1547 N  N   . CYS   B 1 59  ? 28.303 -28.707 8.805  1.00 12.31  ? 65  CYS   C N   1 
ATOM   1548 C  CA  . CYS   B 1 59  ? 28.701 -27.765 7.747  1.00 12.90  ? 65  CYS   C CA  1 
ATOM   1549 C  C   . CYS   B 1 59  ? 27.757 -27.937 6.529  1.00 14.07  ? 65  CYS   C C   1 
ATOM   1550 O  O   . CYS   B 1 59  ? 27.910 -28.890 5.748  1.00 14.37  ? 65  CYS   C O   1 
ATOM   1551 C  CB  . CYS   B 1 59  ? 30.153 -28.014 7.375  1.00 12.93  ? 65  CYS   C CB  1 
ATOM   1552 S  SG  . CYS   B 1 59  ? 30.735 -26.966 6.006  1.00 15.44  ? 65  CYS   C SG  1 
ATOM   1553 N  N   . SER   B 1 60  ? 26.748 -27.065 6.418  1.00 15.11  ? 66  SER   C N   1 
ATOM   1554 C  CA  . SER   B 1 60  ? 25.760 -27.217 5.358  1.00 15.59  ? 66  SER   C CA  1 
ATOM   1555 C  C   . SER   B 1 60  ? 26.365 -27.140 3.961  1.00 15.55  ? 66  SER   C C   1 
ATOM   1556 O  O   . SER   B 1 60  ? 25.941 -27.898 3.090  1.00 16.95  ? 66  SER   C O   1 
ATOM   1557 C  CB  . SER   B 1 60  ? 24.669 -26.159 5.487  1.00 19.02  ? 66  SER   C CB  1 
ATOM   1558 O  OG  . SER   B 1 60  ? 23.706 -26.407 4.476  1.00 23.64  ? 66  SER   C OG  1 
ATOM   1559 N  N   . SER   B 1 61  ? 27.392 -26.285 3.772  1.00 14.68  ? 67  SER   C N   1 
ATOM   1560 C  CA  . SER   B 1 61  ? 28.022 -26.137 2.435  1.00 15.22  ? 67  SER   C CA  1 
ATOM   1561 C  C   . SER   B 1 61  ? 28.849 -27.346 2.011  1.00 16.35  ? 67  SER   C C   1 
ATOM   1562 O  O   . SER   B 1 61  ? 29.307 -27.400 0.865  1.00 17.94  ? 67  SER   C O   1 
ATOM   1563 C  CB  . SER   B 1 61  ? 28.873 -24.882 2.396  1.00 16.51  ? 67  SER   C CB  1 
ATOM   1564 O  OG  . SER   B 1 61  ? 29.997 -24.958 3.248  1.00 17.36  ? 67  SER   C OG  1 
ATOM   1565 N  N   . ARG   B 1 62  ? 29.009 -28.348 2.882  1.00 15.11  ? 68  ARG   C N   1 
ATOM   1566 C  CA  . ARG   B 1 62  ? 29.649 -29.618 2.534  1.00 15.64  ? 68  ARG   C CA  1 
ATOM   1567 C  C   . ARG   B 1 62  ? 28.717 -30.815 2.782  1.00 16.35  ? 68  ARG   C C   1 
ATOM   1568 O  O   . ARG   B 1 62  ? 29.116 -31.966 2.582  1.00 17.26  ? 68  ARG   C O   1 
ATOM   1569 C  CB  . ARG   B 1 62  ? 30.948 -29.823 3.337  1.00 16.14  ? 68  ARG   C CB  1 
ATOM   1570 C  CG  . ARG   B 1 62  ? 32.009 -28.746 3.080  1.00 20.06  ? 68  ARG   C CG  1 
ATOM   1571 C  CD  . ARG   B 1 62  ? 32.669 -28.992 1.756  1.00 20.41  ? 68  ARG   C CD  1 
ATOM   1572 N  NE  . ARG   B 1 62  ? 33.706 -27.979 1.471  1.00 23.48  ? 68  ARG   C NE  1 
ATOM   1573 C  CZ  . ARG   B 1 62  ? 33.508 -26.841 0.815  1.00 27.04  ? 68  ARG   C CZ  1 
ATOM   1574 N  NH1 . ARG   B 1 62  ? 32.294 -26.521 0.369  1.00 27.88  ? 68  ARG   C NH1 1 
ATOM   1575 N  NH2 . ARG   B 1 62  ? 34.534 -26.031 0.548  1.00 26.79  ? 68  ARG   C NH2 1 
ATOM   1576 N  N   . ARG   B 1 63  ? 27.495 -30.563 3.313  1.00 16.82  ? 69  ARG   C N   1 
ATOM   1577 C  CA  . ARG   B 1 63  ? 26.534 -31.604 3.740  1.00 17.68  ? 69  ARG   C CA  1 
ATOM   1578 C  C   . ARG   B 1 63  ? 27.245 -32.638 4.622  1.00 18.75  ? 69  ARG   C C   1 
ATOM   1579 O  O   . ARG   B 1 63  ? 27.096 -33.860 4.417  1.00 20.55  ? 69  ARG   C O   1 
ATOM   1580 C  CB  . ARG   B 1 63  ? 25.899 -32.291 2.521  1.00 19.66  ? 69  ARG   C CB  1 
ATOM   1581 C  CG  . ARG   B 1 63  ? 25.009 -31.402 1.707  1.00 22.60  ? 69  ARG   C CG  1 
ATOM   1582 C  CD  . ARG   B 1 63  ? 23.776 -30.985 2.418  1.00 29.10  ? 69  ARG   C CD  1 
ATOM   1583 N  NE  . ARG   B 1 63  ? 22.777 -30.546 1.457  1.00 33.08  ? 69  ARG   C NE  1 
ATOM   1584 C  CZ  . ARG   B 1 63  ? 22.585 -29.288 1.090  1.00 33.72  ? 69  ARG   C CZ  1 
ATOM   1585 N  NH1 . ARG   B 1 63  ? 23.337 -28.315 1.599  1.00 31.65  ? 69  ARG   C NH1 1 
ATOM   1586 N  NH2 . ARG   B 1 63  ? 21.632 -28.986 0.223  1.00 33.51  ? 69  ARG   C NH2 1 
ATOM   1587 N  N   . LYS   B 1 64  ? 28.088 -32.150 5.564  1.00 16.71  ? 70  LYS   C N   1 
ATOM   1588 C  CA  . LYS   B 1 64  ? 28.890 -33.066 6.359  1.00 17.17  ? 70  LYS   C CA  1 
ATOM   1589 C  C   . LYS   B 1 64  ? 29.004 -32.603 7.789  1.00 15.40  ? 70  LYS   C C   1 
ATOM   1590 O  O   . LYS   B 1 64  ? 29.027 -31.393 8.051  1.00 15.07  ? 70  LYS   C O   1 
ATOM   1591 C  CB  . LYS   B 1 64  ? 30.316 -33.125 5.774  1.00 22.53  ? 70  LYS   C CB  1 
ATOM   1592 C  CG  . LYS   B 1 64  ? 30.475 -34.150 4.656  1.00 33.06  ? 70  LYS   C CG  1 
ATOM   1593 C  CD  . LYS   B 1 64  ? 31.940 -34.535 4.440  1.00 41.34  ? 70  LYS   C CD  1 
ATOM   1594 C  CE  . LYS   B 1 64  ? 32.090 -35.345 3.176  1.00 48.17  ? 70  LYS   C CE  1 
ATOM   1595 N  NZ  . LYS   B 1 64  ? 33.519 -35.643 2.864  1.00 53.33  ? 70  LYS   C NZ  1 
ATOM   1596 N  N   . HIS   B 1 65  ? 29.118 -33.563 8.702  1.00 14.58  ? 71  HIS   C N   1 
ATOM   1597 C  CA  . HIS   B 1 65  ? 29.430 -33.291 10.109 1.00 14.73  ? 71  HIS   C CA  1 
ATOM   1598 C  C   . HIS   B 1 65  ? 30.910 -33.563 10.276 1.00 15.95  ? 71  HIS   C C   1 
ATOM   1599 O  O   . HIS   B 1 65  ? 31.393 -34.657 9.918  1.00 18.63  ? 71  HIS   C O   1 
ATOM   1600 C  CB  . HIS   B 1 65  ? 28.600 -34.193 11.044 1.00 14.81  ? 71  HIS   C CB  1 
ATOM   1601 C  CG  . HIS   B 1 65  ? 27.133 -33.906 10.998 1.00 13.32  ? 71  HIS   C CG  1 
ATOM   1602 N  ND1 . HIS   B 1 65  ? 26.492 -33.142 11.963 1.00 16.69  ? 71  HIS   C ND1 1 
ATOM   1603 C  CD2 . HIS   B 1 65  ? 26.226 -34.324 10.091 1.00 13.80  ? 71  HIS   C CD2 1 
ATOM   1604 C  CE1 . HIS   B 1 65  ? 25.194 -33.159 11.636 1.00 14.80  ? 71  HIS   C CE1 1 
ATOM   1605 N  NE2 . HIS   B 1 65  ? 24.979 -33.866 10.524 1.00 17.01  ? 71  HIS   C NE2 1 
ATOM   1606 N  N   . TYR   B 1 66  ? 31.661 -32.608 10.860 1.00 13.80  ? 72  TYR   C N   1 
ATOM   1607 C  CA  . TYR   B 1 66  ? 33.106 -32.794 11.000 1.00 13.51  ? 72  TYR   C CA  1 
ATOM   1608 C  C   . TYR   B 1 66  ? 33.470 -32.848 12.484 1.00 13.08  ? 72  TYR   C C   1 
ATOM   1609 O  O   . TYR   B 1 66  ? 33.077 -31.957 13.238 1.00 13.66  ? 72  TYR   C O   1 
ATOM   1610 C  CB  . TYR   B 1 66  ? 33.832 -31.561 10.409 1.00 14.40  ? 72  TYR   C CB  1 
ATOM   1611 C  CG  . TYR   B 1 66  ? 33.792 -31.470 8.892  1.00 15.13  ? 72  TYR   C CG  1 
ATOM   1612 C  CD1 . TYR   B 1 66  ? 34.648 -32.225 8.112  1.00 16.99  ? 72  TYR   C CD1 1 
ATOM   1613 C  CD2 . TYR   B 1 66  ? 33.008 -30.521 8.252  1.00 15.94  ? 72  TYR   C CD2 1 
ATOM   1614 C  CE1 . TYR   B 1 66  ? 34.644 -32.115 6.719  1.00 18.53  ? 72  TYR   C CE1 1 
ATOM   1615 C  CE2 . TYR   B 1 66  ? 33.000 -30.394 6.864  1.00 17.48  ? 72  TYR   C CE2 1 
ATOM   1616 C  CZ  . TYR   B 1 66  ? 33.843 -31.177 6.108  1.00 18.40  ? 72  TYR   C CZ  1 
ATOM   1617 O  OH  . TYR   B 1 66  ? 33.809 -31.021 4.727  1.00 20.34  ? 72  TYR   C OH  1 
ATOM   1618 N  N   . PRO   B 1 67  ? 34.309 -33.818 12.887 1.00 13.34  ? 73  PRO   C N   1 
ATOM   1619 C  CA  . PRO   B 1 67  ? 34.847 -33.791 14.266 1.00 13.40  ? 73  PRO   C CA  1 
ATOM   1620 C  C   . PRO   B 1 67  ? 35.953 -32.729 14.351 1.00 14.61  ? 73  PRO   C C   1 
ATOM   1621 O  O   . PRO   B 1 67  ? 36.790 -32.620 13.433 1.00 16.82  ? 73  PRO   C O   1 
ATOM   1622 C  CB  . PRO   B 1 67  ? 35.448 -35.195 14.463 1.00 15.59  ? 73  PRO   C CB  1 
ATOM   1623 C  CG  . PRO   B 1 67  ? 35.608 -35.763 13.092 1.00 17.77  ? 73  PRO   C CG  1 
ATOM   1624 C  CD  . PRO   B 1 67  ? 34.806 -34.979 12.095 1.00 14.50  ? 73  PRO   C CD  1 
ATOM   1625 N  N   . VAL   B 1 68  ? 35.929 -31.927 15.416 1.00 13.44  ? 74  VAL   C N   1 
ATOM   1626 C  CA  . VAL   B 1 68  ? 36.885 -30.822 15.521 1.00 13.50  ? 74  VAL   C CA  1 
ATOM   1627 C  C   . VAL   B 1 68  ? 37.298 -30.632 16.962 1.00 12.83  ? 74  VAL   C C   1 
ATOM   1628 O  O   . VAL   B 1 68  ? 36.551 -30.918 17.888 1.00 13.67  ? 74  VAL   C O   1 
ATOM   1629 C  CB  . VAL   B 1 68  ? 36.261 -29.449 15.048 1.00 15.10  ? 74  VAL   C CB  1 
ATOM   1630 C  CG1 . VAL   B 1 68  ? 36.179 -29.330 13.509 1.00 17.40  ? 74  VAL   C CG1 1 
ATOM   1631 C  CG2 . VAL   B 1 68  ? 34.908 -29.173 15.727 1.00 15.86  ? 74  VAL   C CG2 1 
ATOM   1632 N  N   . SER   B 1 69  ? 38.518 -30.080 17.129 1.00 12.78  ? 75  SER   C N   1 
ATOM   1633 C  CA  . SER   B 1 69  ? 39.003 -29.462 18.376 1.00 13.43  ? 75  SER   C CA  1 
ATOM   1634 C  C   . SER   B 1 69  ? 38.706 -27.956 18.275 1.00 13.09  ? 75  SER   C C   1 
ATOM   1635 O  O   . SER   B 1 69  ? 38.828 -27.362 17.190 1.00 13.57  ? 75  SER   C O   1 
ATOM   1636 C  CB  . SER   B 1 69  ? 40.510 -29.641 18.499 1.00 15.88  ? 75  SER   C CB  1 
ATOM   1637 O  OG  . SER   B 1 69  ? 40.812 -31.016 18.672 1.00 19.92  ? 75  SER   C OG  1 
ATOM   1638 N  N   . PHE   B 1 70  ? 38.249 -27.344 19.368 1.00 12.13  ? 76  PHE   C N   1 
ATOM   1639 C  CA  . PHE   B 1 70  ? 37.897 -25.921 19.325 1.00 12.24  ? 76  PHE   C CA  1 
ATOM   1640 C  C   . PHE   B 1 70  ? 38.385 -25.191 20.573 1.00 12.73  ? 76  PHE   C C   1 
ATOM   1641 O  O   . PHE   B 1 70  ? 38.569 -25.804 21.642 1.00 13.61  ? 76  PHE   C O   1 
ATOM   1642 C  CB  . PHE   B 1 70  ? 36.364 -25.688 19.103 1.00 12.73  ? 76  PHE   C CB  1 
ATOM   1643 C  CG  . PHE   B 1 70  ? 35.470 -26.400 20.101 1.00 11.97  ? 76  PHE   C CG  1 
ATOM   1644 C  CD1 . PHE   B 1 70  ? 35.040 -27.710 19.870 1.00 13.10  ? 76  PHE   C CD1 1 
ATOM   1645 C  CD2 . PHE   B 1 70  ? 35.048 -25.753 21.249 1.00 13.07  ? 76  PHE   C CD2 1 
ATOM   1646 C  CE1 . PHE   B 1 70  ? 34.219 -28.350 20.789 1.00 13.14  ? 76  PHE   C CE1 1 
ATOM   1647 C  CE2 . PHE   B 1 70  ? 34.190 -26.392 22.151 1.00 13.47  ? 76  PHE   C CE2 1 
ATOM   1648 C  CZ  . PHE   B 1 70  ? 33.813 -27.689 21.933 1.00 13.57  ? 76  PHE   C CZ  1 
ATOM   1649 N  N   . SER   B 1 71  ? 38.637 -23.901 20.440 1.00 12.72  ? 77  SER   C N   1 
ATOM   1650 C  CA  . SER   B 1 71  ? 39.267 -23.115 21.509 1.00 13.93  ? 77  SER   C CA  1 
ATOM   1651 C  C   . SER   B 1 71  ? 38.295 -22.730 22.616 1.00 14.67  ? 77  SER   C C   1 
ATOM   1652 O  O   . SER   B 1 71  ? 37.088 -23.019 22.543 1.00 15.21  ? 77  SER   C O   1 
ATOM   1653 C  CB  . SER   B 1 71  ? 39.997 -21.909 20.920 1.00 14.43  ? 77  SER   C CB  1 
ATOM   1654 O  OG  . SER   B 1 71  ? 39.080 -21.004 20.316 1.00 16.47  ? 77  SER   C OG  1 
ATOM   1655 N  N   . LYS   B 1 72  ? 38.804 -22.089 23.665 1.00 15.17  ? 78  LYS   C N   1 
ATOM   1656 C  CA  . LYS   B 1 72  ? 37.939 -21.667 24.785 1.00 15.15  ? 78  LYS   C CA  1 
ATOM   1657 C  C   . LYS   B 1 72  ? 37.242 -20.348 24.397 1.00 15.83  ? 78  LYS   C C   1 
ATOM   1658 O  O   . LYS   B 1 72  ? 37.812 -19.534 23.653 1.00 16.91  ? 78  LYS   C O   1 
ATOM   1659 C  CB  . LYS   B 1 72  ? 38.812 -21.446 26.047 1.00 18.49  ? 78  LYS   C CB  1 
ATOM   1660 C  CG  . LYS   B 1 72  ? 39.503 -22.725 26.519 1.00 22.02  ? 78  LYS   C CG  1 
ATOM   1661 C  CD  . LYS   B 1 72  ? 40.396 -22.449 27.713 1.00 31.33  ? 78  LYS   C CD  1 
ATOM   1662 C  CE  . LYS   B 1 72  ? 41.352 -23.579 28.027 1.00 38.68  ? 78  LYS   C CE  1 
ATOM   1663 N  NZ  . LYS   B 1 72  ? 42.561 -23.080 28.749 1.00 43.55  ? 78  LYS   C NZ  1 
ATOM   1664 N  N   . PRO   B 1 73  ? 35.999 -20.099 24.865 1.00 15.18  ? 79  PRO   C N   1 
ATOM   1665 C  CA  . PRO   B 1 73  ? 35.277 -18.857 24.458 1.00 15.76  ? 79  PRO   C CA  1 
ATOM   1666 C  C   . PRO   B 1 73  ? 36.068 -17.612 24.802 1.00 17.01  ? 79  PRO   C C   1 
ATOM   1667 O  O   . PRO   B 1 73  ? 36.501 -17.457 25.964 1.00 18.29  ? 79  PRO   C O   1 
ATOM   1668 C  CB  . PRO   B 1 73  ? 33.978 -18.876 25.258 1.00 17.30  ? 79  PRO   C CB  1 
ATOM   1669 C  CG  . PRO   B 1 73  ? 33.878 -20.267 25.816 1.00 18.75  ? 79  PRO   C CG  1 
ATOM   1670 C  CD  . PRO   B 1 73  ? 35.225 -20.966 25.787 1.00 16.50  ? 79  PRO   C CD  1 
ATOM   1671 N  N   . SER   B 1 74  ? 36.271 -16.722 23.816 1.00 14.91  ? 80  SER   C N   1 
ATOM   1672 C  CA  . SER   B 1 74  ? 37.122 -15.559 24.056 1.00 15.90  ? 80  SER   C CA  1 
ATOM   1673 C  C   . SER   B 1 74  ? 36.741 -14.390 23.152 1.00 16.49  ? 80  SER   C C   1 
ATOM   1674 O  O   . SER   B 1 74  ? 35.854 -14.535 22.310 1.00 15.61  ? 80  SER   C O   1 
ATOM   1675 C  CB  . SER   B 1 74  ? 38.591 -15.926 23.853 1.00 20.57  ? 80  SER   C CB  1 
ATOM   1676 O  OG  . SER   B 1 74  ? 38.928 -16.197 22.509 1.00 26.83  ? 80  SER   C OG  1 
ATOM   1677 N  N   . LEU   B 1 75  ? 37.408 -13.235 23.339 1.00 16.66  ? 81  LEU   C N   1 
ATOM   1678 C  CA  . LEU   B 1 75  ? 37.180 -12.024 22.536 1.00 17.17  ? 81  LEU   C CA  1 
ATOM   1679 C  C   . LEU   B 1 75  ? 38.194 -12.072 21.382 1.00 17.32  ? 81  LEU   C C   1 
ATOM   1680 O  O   . LEU   B 1 75  ? 39.420 -12.012 21.623 1.00 19.28  ? 81  LEU   C O   1 
ATOM   1681 C  CB  . LEU   B 1 75  ? 37.424 -10.768 23.414 1.00 18.58  ? 81  LEU   C CB  1 
ATOM   1682 C  CG  . LEU   B 1 75  ? 37.189 -9.408  22.745 1.00 20.65  ? 81  LEU   C CG  1 
ATOM   1683 C  CD1 . LEU   B 1 75  ? 35.703 -9.198  22.452 1.00 20.58  ? 81  LEU   C CD1 1 
ATOM   1684 C  CD2 . LEU   B 1 75  ? 37.709 -8.267  23.673 1.00 22.95  ? 81  LEU   C CD2 1 
ATOM   1685 N  N   . ILE   B 1 76  ? 37.712 -12.274 20.138 1.00 17.84  ? 82  ILE   C N   1 
ATOM   1686 C  CA  . ILE   B 1 76  ? 38.559 -12.493 18.957 1.00 18.90  ? 82  ILE   C CA  1 
ATOM   1687 C  C   . ILE   B 1 76  ? 38.273 -11.462 17.882 1.00 18.46  ? 82  ILE   C C   1 
ATOM   1688 O  O   . ILE   B 1 76  ? 37.097 -11.136 17.653 1.00 17.67  ? 82  ILE   C O   1 
ATOM   1689 C  CB  . ILE   B 1 76  ? 38.242 -13.915 18.427 1.00 21.60  ? 82  ILE   C CB  1 
ATOM   1690 C  CG1 . ILE   B 1 76  ? 38.618 -14.972 19.481 1.00 24.73  ? 82  ILE   C CG1 1 
ATOM   1691 C  CG2 . ILE   B 1 76  ? 38.897 -14.192 17.050 1.00 23.22  ? 82  ILE   C CG2 1 
ATOM   1692 C  CD1 . ILE   B 1 76  ? 38.439 -16.316 19.121 1.00 26.02  ? 82  ILE   C CD1 1 
ATOM   1693 N  N   . PHE   B 1 77  ? 39.333 -10.954 17.220 1.00 19.08  ? 83  PHE   C N   1 
ATOM   1694 C  CA  . PHE   B 1 77  ? 39.137 -10.027 16.110 1.00 19.37  ? 83  PHE   C CA  1 
ATOM   1695 C  C   . PHE   B 1 77  ? 38.757 -10.886 14.884 1.00 20.58  ? 83  PHE   C C   1 
ATOM   1696 O  O   . PHE   B 1 77  ? 39.473 -11.851 14.542 1.00 22.60  ? 83  PHE   C O   1 
ATOM   1697 C  CB  . PHE   B 1 77  ? 40.435 -9.245  15.786 1.00 19.95  ? 83  PHE   C CB  1 
ATOM   1698 C  CG  . PHE   B 1 77  ? 40.137 -8.081  14.862 1.00 20.94  ? 83  PHE   C CG  1 
ATOM   1699 C  CD1 . PHE   B 1 77  ? 39.415 -6.983  15.310 1.00 22.23  ? 83  PHE   C CD1 1 
ATOM   1700 C  CD2 . PHE   B 1 77  ? 40.509 -8.121  13.517 1.00 22.72  ? 83  PHE   C CD2 1 
ATOM   1701 C  CE1 . PHE   B 1 77  ? 39.102 -5.933  14.444 1.00 23.72  ? 83  PHE   C CE1 1 
ATOM   1702 C  CE2 . PHE   B 1 77  ? 40.193 -7.064  12.658 1.00 23.44  ? 83  PHE   C CE2 1 
ATOM   1703 C  CZ  . PHE   B 1 77  ? 39.506 -5.978  13.128 1.00 23.25  ? 83  PHE   C CZ  1 
ATOM   1704 N  N   . VAL   B 1 78  ? 37.619 -10.548 14.248 1.00 17.71  ? 84  VAL   C N   1 
ATOM   1705 C  CA  . VAL   B 1 78  ? 37.128 -11.298 13.102 1.00 17.60  ? 84  VAL   C CA  1 
ATOM   1706 C  C   . VAL   B 1 78  ? 37.204 -10.367 11.898 1.00 17.51  ? 84  VAL   C C   1 
ATOM   1707 O  O   . VAL   B 1 78  ? 36.731 -9.226  11.986 1.00 17.53  ? 84  VAL   C O   1 
ATOM   1708 C  CB  . VAL   B 1 78  ? 35.648 -11.701 13.368 1.00 17.70  ? 84  VAL   C CB  1 
ATOM   1709 C  CG1 . VAL   B 1 78  ? 35.106 -12.503 12.195 1.00 18.90  ? 84  VAL   C CG1 1 
ATOM   1710 C  CG2 . VAL   B 1 78  ? 35.511 -12.498 14.660 1.00 18.77  ? 84  VAL   C CG2 1 
ATOM   1711 N  N   . GLU   B 1 79  ? 37.702 -10.845 10.755 1.00 16.49  ? 85  GLU   C N   1 
ATOM   1712 C  CA  . GLU   B 1 79  ? 37.726 -10.023 9.536  1.00 16.71  ? 85  GLU   C CA  1 
ATOM   1713 C  C   . GLU   B 1 79  ? 36.319 -9.777  8.988  1.00 16.78  ? 85  GLU   C C   1 
ATOM   1714 O  O   . GLU   B 1 79  ? 35.355 -10.454 9.369  1.00 16.41  ? 85  GLU   C O   1 
ATOM   1715 C  CB  . GLU   B 1 79  ? 38.603 -10.676 8.447  1.00 18.66  ? 85  GLU   C CB  1 
ATOM   1716 C  CG  . GLU   B 1 79  ? 40.089 -10.699 8.815  1.00 22.60  ? 85  GLU   C CG  1 
ATOM   1717 C  CD  . GLU   B 1 79  ? 40.691 -9.328  9.097  1.00 31.20  ? 85  GLU   C CD  1 
ATOM   1718 O  OE1 . GLU   B 1 79  ? 40.356 -8.355  8.377  1.00 33.18  ? 85  GLU   C OE1 1 
ATOM   1719 O  OE2 . GLU   B 1 79  ? 41.503 -9.222  10.047 1.00 34.00  ? 85  GLU   C OE2 1 
ATOM   1720 N  N   . ALA   B 1 80  ? 36.189 -8.793  8.088  1.00 17.82  ? 86  ALA   C N   1 
ATOM   1721 C  CA  . ALA   B 1 80  ? 34.894 -8.475  7.503  1.00 18.62  ? 86  ALA   C CA  1 
ATOM   1722 C  C   . ALA   B 1 80  ? 34.272 -9.670  6.797  1.00 19.25  ? 86  ALA   C C   1 
ATOM   1723 O  O   . ALA   B 1 80  ? 34.980 -10.476 6.176  1.00 20.94  ? 86  ALA   C O   1 
ATOM   1724 C  CB  . ALA   B 1 80  ? 35.071 -7.328  6.505  1.00 19.79  ? 86  ALA   C CB  1 
ATOM   1725 N  N   . SER   B 1 81  ? 32.949 -9.808  6.954  1.00 18.06  ? 87  SER   C N   1 
ATOM   1726 C  CA  . SER   B 1 81  ? 32.213 -10.853 6.276  1.00 18.95  ? 87  SER   C CA  1 
ATOM   1727 C  C   . SER   B 1 81  ? 31.071 -10.183 5.486  1.00 20.05  ? 87  SER   C C   1 
ATOM   1728 O  O   . SER   B 1 81  ? 30.924 -8.939  5.516  1.00 20.63  ? 87  SER   C O   1 
ATOM   1729 C  CB  . SER   B 1 81  ? 31.642 -11.830 7.301  1.00 18.36  ? 87  SER   C CB  1 
ATOM   1730 O  OG  . SER   B 1 81  ? 30.629 -11.157 8.052  1.00 18.57  ? 87  SER   C OG  1 
ATOM   1731 N  N   . GLU   B 1 82  ? 30.240 -10.992 4.820  1.00 21.81  ? 88  GLU   C N   1 
ATOM   1732 C  CA  . GLU   B 1 82  ? 29.128 -10.382 4.092  1.00 23.13  ? 88  GLU   C CA  1 
ATOM   1733 C  C   . GLU   B 1 82  ? 28.086 -9.736  5.032  1.00 22.65  ? 88  GLU   C C   1 
ATOM   1734 O  O   . GLU   B 1 82  ? 27.328 -8.871  4.596  1.00 23.94  ? 88  GLU   C O   1 
ATOM   1735 C  CB  . GLU   B 1 82  ? 28.507 -11.368 3.107  1.00 27.72  ? 88  GLU   C CB  1 
ATOM   1736 C  CG  . GLU   B 1 82  ? 27.704 -12.496 3.705  1.00 35.79  ? 88  GLU   C CG  1 
ATOM   1737 C  CD  . GLU   B 1 82  ? 26.948 -13.243 2.623  1.00 43.18  ? 88  GLU   C CD  1 
ATOM   1738 O  OE1 . GLU   B 1 82  ? 27.548 -13.476 1.547  1.00 43.73  ? 88  GLU   C OE1 1 
ATOM   1739 O  OE2 . GLU   B 1 82  ? 25.758 -13.575 2.840  1.00 44.75  ? 88  GLU   C OE2 1 
ATOM   1740 N  N   . TYR   B 1 83  ? 28.098 -10.078 6.339  1.00 19.67  ? 89  TYR   C N   1 
ATOM   1741 C  CA  . TYR   B 1 83  ? 27.077 -9.592  7.260  1.00 19.33  ? 89  TYR   C CA  1 
ATOM   1742 C  C   . TYR   B 1 83  ? 27.585 -8.712  8.436  1.00 19.63  ? 89  TYR   C C   1 
ATOM   1743 O  O   . TYR   B 1 83  ? 26.746 -8.117  9.113  1.00 21.35  ? 89  TYR   C O   1 
ATOM   1744 C  CB  . TYR   B 1 83  ? 26.233 -10.778 7.781  1.00 18.80  ? 89  TYR   C CB  1 
ATOM   1745 C  CG  . TYR   B 1 83  ? 27.065 -11.968 8.239  1.00 18.08  ? 89  TYR   C CG  1 
ATOM   1746 C  CD1 . TYR   B 1 83  ? 27.458 -12.964 7.341  1.00 18.47  ? 89  TYR   C CD1 1 
ATOM   1747 C  CD2 . TYR   B 1 83  ? 27.500 -12.076 9.557  1.00 17.39  ? 89  TYR   C CD2 1 
ATOM   1748 C  CE1 . TYR   B 1 83  ? 28.245 -14.046 7.754  1.00 17.42  ? 89  TYR   C CE1 1 
ATOM   1749 C  CE2 . TYR   B 1 83  ? 28.278 -13.154 9.981  1.00 17.89  ? 89  TYR   C CE2 1 
ATOM   1750 C  CZ  . TYR   B 1 83  ? 28.654 -14.138 9.074  1.00 17.56  ? 89  TYR   C CZ  1 
ATOM   1751 O  OH  . TYR   B 1 83  ? 29.465 -15.189 9.461  1.00 18.89  ? 89  TYR   C OH  1 
ATOM   1752 N  N   . TYR   B 1 84  ? 28.911 -8.592  8.687  1.00 17.62  ? 90  TYR   C N   1 
ATOM   1753 C  CA  . TYR   B 1 84  ? 29.465 -7.677  9.696  1.00 17.58  ? 90  TYR   C CA  1 
ATOM   1754 C  C   . TYR   B 1 84  ? 30.786 -7.080  9.173  1.00 18.06  ? 90  TYR   C C   1 
ATOM   1755 O  O   . TYR   B 1 84  ? 31.517 -7.748  8.429  1.00 17.32  ? 90  TYR   C O   1 
ATOM   1756 C  CB  . TYR   B 1 84  ? 29.825 -8.409  11.031 1.00 16.83  ? 90  TYR   C CB  1 
ATOM   1757 C  CG  . TYR   B 1 84  ? 28.647 -8.832  11.882 1.00 15.94  ? 90  TYR   C CG  1 
ATOM   1758 C  CD1 . TYR   B 1 84  ? 27.766 -7.890  12.424 1.00 17.05  ? 90  TYR   C CD1 1 
ATOM   1759 C  CD2 . TYR   B 1 84  ? 28.466 -10.145 12.219 1.00 15.14  ? 90  TYR   C CD2 1 
ATOM   1760 C  CE1 . TYR   B 1 84  ? 26.702 -8.277  13.250 1.00 17.02  ? 90  TYR   C CE1 1 
ATOM   1761 C  CE2 . TYR   B 1 84  ? 27.399 -10.547 13.034 1.00 14.98  ? 90  TYR   C CE2 1 
ATOM   1762 C  CZ  . TYR   B 1 84  ? 26.527 -9.611  13.576 1.00 16.42  ? 90  TYR   C CZ  1 
ATOM   1763 O  OH  . TYR   B 1 84  ? 25.455 -10.019 14.387 1.00 16.17  ? 90  TYR   C OH  1 
ATOM   1764 N  N   . PRO   B 1 85  ? 31.143 -5.865  9.607  1.00 18.77  ? 91  PRO   C N   1 
ATOM   1765 C  CA  . PRO   B 1 85  ? 32.494 -5.362  9.319  1.00 18.51  ? 91  PRO   C CA  1 
ATOM   1766 C  C   . PRO   B 1 85  ? 33.534 -6.130  10.157 1.00 18.37  ? 91  PRO   C C   1 
ATOM   1767 O  O   . PRO   B 1 85  ? 33.185 -6.930  11.066 1.00 18.29  ? 91  PRO   C O   1 
ATOM   1768 C  CB  . PRO   B 1 85  ? 32.392 -3.887  9.766  1.00 18.90  ? 91  PRO   C CB  1 
ATOM   1769 C  CG  . PRO   B 1 85  ? 31.444 -3.933  10.920 1.00 19.62  ? 91  PRO   C CG  1 
ATOM   1770 C  CD  . PRO   B 1 85  ? 30.399 -4.977  10.539 1.00 19.25  ? 91  PRO   C CD  1 
ATOM   1771 N  N   . ALA   B 1 86  ? 34.839 -5.833  9.933  1.00 18.21  ? 92  ALA   C N   1 
ATOM   1772 C  CA  . ALA   B 1 86  ? 35.902 -6.383  10.777 1.00 19.46  ? 92  ALA   C CA  1 
ATOM   1773 C  C   . ALA   B 1 86  ? 35.695 -5.809  12.194 1.00 20.20  ? 92  ALA   C C   1 
ATOM   1774 O  O   . ALA   B 1 86  ? 35.446 -4.591  12.333 1.00 22.03  ? 92  ALA   C O   1 
ATOM   1775 C  CB  . ALA   B 1 86  ? 37.274 -5.973  10.228 1.00 19.71  ? 92  ALA   C CB  1 
ATOM   1776 N  N   . ARG   B 1 87  ? 35.694 -6.667  13.207 1.00 19.09  ? 93  ARG   C N   1 
ATOM   1777 C  CA  . ARG   B 1 87  ? 35.385 -6.224  14.561 1.00 18.69  ? 93  ARG   C CA  1 
ATOM   1778 C  C   . ARG   B 1 87  ? 35.798 -7.294  15.569 1.00 18.03  ? 93  ARG   C C   1 
ATOM   1779 O  O   . ARG   B 1 87  ? 36.061 -8.449  15.198 1.00 18.01  ? 93  ARG   C O   1 
ATOM   1780 C  CB  . ARG   B 1 87  ? 33.843 -6.001  14.674 1.00 20.08  ? 93  ARG   C CB  1 
ATOM   1781 C  CG  . ARG   B 1 87  ? 33.051 -7.320  14.693 1.00 18.62  ? 93  ARG   C CG  1 
ATOM   1782 C  CD  . ARG   B 1 87  ? 31.553 -7.057  14.634 1.00 18.65  ? 93  ARG   C CD  1 
ATOM   1783 N  NE  . ARG   B 1 87  ? 30.887 -8.317  14.933 1.00 19.75  ? 93  ARG   C NE  1 
ATOM   1784 C  CZ  . ARG   B 1 87  ? 29.822 -8.484  15.695 1.00 20.30  ? 93  ARG   C CZ  1 
ATOM   1785 N  NH1 . ARG   B 1 87  ? 29.255 -7.441  16.300 1.00 20.60  ? 93  ARG   C NH1 1 
ATOM   1786 N  NH2 . ARG   B 1 87  ? 29.367 -9.703  15.934 1.00 19.28  ? 93  ARG   C NH2 1 
ATOM   1787 N  N   . TYR   B 1 88  ? 35.713 -6.967  16.868 1.00 18.78  ? 94  TYR   C N   1 
ATOM   1788 C  CA  . TYR   B 1 88  ? 35.895 -7.974  17.911 1.00 19.88  ? 94  TYR   C CA  1 
ATOM   1789 C  C   . TYR   B 1 88  ? 34.544 -8.620  18.204 1.00 17.70  ? 94  TYR   C C   1 
ATOM   1790 O  O   . TYR   B 1 88  ? 33.525 -7.925  18.356 1.00 19.68  ? 94  TYR   C O   1 
ATOM   1791 C  CB  . TYR   B 1 88  ? 36.378 -7.318  19.228 1.00 22.24  ? 94  TYR   C CB  1 
ATOM   1792 C  CG  . TYR   B 1 88  ? 37.833 -6.954  19.127 1.00 24.59  ? 94  TYR   C CG  1 
ATOM   1793 C  CD1 . TYR   B 1 88  ? 38.816 -7.899  19.348 1.00 25.98  ? 94  TYR   C CD1 1 
ATOM   1794 C  CD2 . TYR   B 1 88  ? 38.220 -5.672  18.737 1.00 26.29  ? 94  TYR   C CD2 1 
ATOM   1795 C  CE1 . TYR   B 1 88  ? 40.162 -7.580  19.204 1.00 27.86  ? 94  TYR   C CE1 1 
ATOM   1796 C  CE2 . TYR   B 1 88  ? 39.554 -5.341  18.580 1.00 27.46  ? 94  TYR   C CE2 1 
ATOM   1797 C  CZ  . TYR   B 1 88  ? 40.524 -6.286  18.844 1.00 28.69  ? 94  TYR   C CZ  1 
ATOM   1798 O  OH  . TYR   B 1 88  ? 41.837 -5.911  18.667 1.00 31.06  ? 94  TYR   C OH  1 
ATOM   1799 N  N   . GLN   B 1 89  ? 34.536 -9.953  18.275 1.00 16.73  ? 95  GLN   C N   1 
ATOM   1800 C  CA  . GLN   B 1 89  ? 33.315 -10.698 18.641 1.00 15.99  ? 95  GLN   C CA  1 
ATOM   1801 C  C   . GLN   B 1 89  ? 33.639 -11.430 19.949 1.00 15.71  ? 95  GLN   C C   1 
ATOM   1802 O  O   . GLN   B 1 89  ? 34.738 -12.008 20.087 1.00 16.65  ? 95  GLN   C O   1 
ATOM   1803 C  CB  . GLN   B 1 89  ? 32.942 -11.680 17.521 1.00 16.87  ? 95  GLN   C CB  1 
ATOM   1804 C  CG  . GLN   B 1 89  ? 31.653 -12.433 17.841 1.00 17.09  ? 95  GLN   C CG  1 
ATOM   1805 C  CD  . GLN   B 1 89  ? 30.978 -13.034 16.623 1.00 16.10  ? 95  GLN   C CD  1 
ATOM   1806 O  OE1 . GLN   B 1 89  ? 30.905 -12.417 15.534 1.00 17.47  ? 95  GLN   C OE1 1 
ATOM   1807 N  NE2 . GLN   B 1 89  ? 30.438 -14.224 16.811 1.00 16.51  ? 95  GLN   C NE2 1 
ATOM   1808 N  N   . SER   B 1 90  ? 32.744 -11.391 20.920 1.00 14.55  ? 96  SER   C N   1 
ATOM   1809 C  CA  . SER   B 1 90  ? 32.974 -12.029 22.211 1.00 15.52  ? 96  SER   C CA  1 
ATOM   1810 C  C   . SER   B 1 90  ? 32.350 -13.444 22.279 1.00 14.99  ? 96  SER   C C   1 
ATOM   1811 O  O   . SER   B 1 90  ? 31.489 -13.800 21.459 1.00 14.82  ? 96  SER   C O   1 
ATOM   1812 C  CB  . SER   B 1 90  ? 32.461 -11.154 23.368 1.00 17.21  ? 96  SER   C CB  1 
ATOM   1813 O  OG  . SER   B 1 90  ? 31.054 -11.094 23.283 1.00 17.68  ? 96  SER   C OG  1 
ATOM   1814 N  N   . HIS   B 1 91  ? 32.818 -14.235 23.280 1.00 14.45  ? 97  HIS   C N   1 
ATOM   1815 C  CA  . HIS   B 1 91  ? 32.341 -15.600 23.554 1.00 13.73  ? 97  HIS   C CA  1 
ATOM   1816 C  C   . HIS   B 1 91  ? 32.430 -16.471 22.268 1.00 14.12  ? 97  HIS   C C   1 
ATOM   1817 O  O   . HIS   B 1 91  ? 31.547 -17.301 22.027 1.00 15.01  ? 97  HIS   C O   1 
ATOM   1818 C  CB  . HIS   B 1 91  ? 30.888 -15.565 24.113 1.00 14.10  ? 97  HIS   C CB  1 
ATOM   1819 C  CG  . HIS   B 1 91  ? 30.759 -14.812 25.420 1.00 16.34  ? 97  HIS   C CG  1 
ATOM   1820 N  ND1 . HIS   B 1 91  ? 30.772 -15.474 26.636 1.00 18.93  ? 97  HIS   C ND1 1 
ATOM   1821 C  CD2 . HIS   B 1 91  ? 30.685 -13.466 25.657 1.00 16.93  ? 97  HIS   C CD2 1 
ATOM   1822 C  CE1 . HIS   B 1 91  ? 30.665 -14.532 27.578 1.00 18.37  ? 97  HIS   C CE1 1 
ATOM   1823 N  NE2 . HIS   B 1 91  ? 30.583 -13.305 27.044 1.00 18.17  ? 97  HIS   C NE2 1 
ATOM   1824 N  N   . LEU   B 1 92  ? 33.510 -16.306 21.517 1.00 13.43  ? 98  LEU   C N   1 
ATOM   1825 C  CA  . LEU   B 1 92  ? 33.697 -17.001 20.258 1.00 13.06  ? 98  LEU   C CA  1 
ATOM   1826 C  C   . LEU   B 1 92  ? 34.782 -18.074 20.437 1.00 13.29  ? 98  LEU   C C   1 
ATOM   1827 O  O   . LEU   B 1 92  ? 35.774 -17.866 21.143 1.00 14.31  ? 98  LEU   C O   1 
ATOM   1828 C  CB  . LEU   B 1 92  ? 34.172 -15.981 19.167 1.00 14.40  ? 98  LEU   C CB  1 
ATOM   1829 C  CG  . LEU   B 1 92  ? 34.278 -16.534 17.732 1.00 15.31  ? 98  LEU   C CG  1 
ATOM   1830 C  CD1 . LEU   B 1 92  ? 32.910 -16.886 17.184 1.00 16.23  ? 98  LEU   C CD1 1 
ATOM   1831 C  CD2 . LEU   B 1 92  ? 34.916 -15.488 16.779 1.00 17.18  ? 98  LEU   C CD2 1 
ATOM   1832 N  N   . MET   B 1 93  ? 34.585 -19.236 19.779 1.00 12.36  ? 99  MET   C N   1 
ATOM   1833 C  CA  . MET   B 1 93  ? 35.538 -20.346 19.849 1.00 11.59  ? 99  MET   C CA  1 
ATOM   1834 C  C   . MET   B 1 93  ? 35.930 -20.669 18.399 1.00 12.36  ? 99  MET   C C   1 
ATOM   1835 O  O   . MET   B 1 93  ? 35.048 -20.730 17.547 1.00 14.04  ? 99  MET   C O   1 
ATOM   1836 C  CB  . MET   B 1 93  ? 34.831 -21.580 20.463 1.00 14.07  ? 99  MET   C CB  1 
ATOM   1837 C  CG  . MET   B 1 93  ? 34.382 -21.294 21.891 1.00 14.64  ? 99  MET   C CG  1 
ATOM   1838 S  SD  . MET   B 1 93  ? 33.322 -22.616 22.517 1.00 15.95  ? 99  MET   C SD  1 
ATOM   1839 C  CE  . MET   B 1 93  ? 31.869 -22.504 21.413 1.00 16.49  ? 99  MET   C CE  1 
ATOM   1840 N  N   . LEU   B 1 94  ? 37.211 -20.920 18.116 1.00 12.31  ? 100 LEU   C N   1 
ATOM   1841 C  CA  . LEU   B 1 94  ? 37.638 -21.210 16.747 1.00 12.81  ? 100 LEU   C CA  1 
ATOM   1842 C  C   . LEU   B 1 94  ? 38.084 -22.682 16.613 1.00 13.23  ? 100 LEU   C C   1 
ATOM   1843 O  O   . LEU   B 1 94  ? 38.567 -23.301 17.555 1.00 14.55  ? 100 LEU   C O   1 
ATOM   1844 C  CB  . LEU   B 1 94  ? 38.887 -20.367 16.380 1.00 14.13  ? 100 LEU   C CB  1 
ATOM   1845 C  CG  . LEU   B 1 94  ? 38.738 -18.870 16.350 1.00 15.41  ? 100 LEU   C CG  1 
ATOM   1846 C  CD1 . LEU   B 1 94  ? 40.056 -18.230 15.904 1.00 17.37  ? 100 LEU   C CD1 1 
ATOM   1847 C  CD2 . LEU   B 1 94  ? 37.540 -18.428 15.460 1.00 17.17  ? 100 LEU   C CD2 1 
ATOM   1848 N  N   . ALA   B 1 95  ? 37.933 -23.202 15.408 1.00 13.13  ? 101 ALA   C N   1 
ATOM   1849 C  CA  . ALA   B 1 95  ? 38.453 -24.519 15.022 1.00 13.29  ? 101 ALA   C CA  1 
ATOM   1850 C  C   . ALA   B 1 95  ? 38.981 -24.415 13.570 1.00 13.15  ? 101 ALA   C C   1 
ATOM   1851 O  O   . ALA   B 1 95  ? 38.631 -23.479 12.853 1.00 13.37  ? 101 ALA   C O   1 
ATOM   1852 C  CB  . ALA   B 1 95  ? 37.337 -25.582 15.054 1.00 14.22  ? 101 ALA   C CB  1 
ATOM   1853 N  N   . VAL   B 1 96  ? 39.836 -25.360 13.165 1.00 13.28  ? 102 VAL   C N   1 
ATOM   1854 C  CA  . VAL   B 1 96  ? 40.282 -25.427 11.776 1.00 14.12  ? 102 VAL   C CA  1 
ATOM   1855 C  C   . VAL   B 1 96  ? 39.213 -26.164 10.985 1.00 15.14  ? 102 VAL   C C   1 
ATOM   1856 O  O   . VAL   B 1 96  ? 38.903 -27.347 11.265 1.00 16.52  ? 102 VAL   C O   1 
ATOM   1857 C  CB  . VAL   B 1 96  ? 41.653 -26.139 11.711 1.00 15.56  ? 102 VAL   C CB  1 
ATOM   1858 C  CG1 . VAL   B 1 96  ? 42.095 -26.287 10.252 1.00 17.23  ? 102 VAL   C CG1 1 
ATOM   1859 C  CG2 . VAL   B 1 96  ? 42.688 -25.364 12.526 1.00 16.81  ? 102 VAL   C CG2 1 
ATOM   1860 N  N   . GLY   B 1 97  ? 38.631 -25.461 10.016 1.00 15.83  ? 103 GLY   C N   1 
ATOM   1861 C  CA  . GLY   B 1 97  ? 37.551 -26.074 9.253  1.00 16.88  ? 103 GLY   C CA  1 
ATOM   1862 C  C   . GLY   B 1 97  ? 36.885 -25.109 8.327  1.00 17.10  ? 103 GLY   C C   1 
ATOM   1863 O  O   . GLY   B 1 97  ? 37.155 -23.890 8.359  1.00 18.64  ? 103 GLY   C O   1 
ATOM   1864 N  N   . HIS   B 1 98  ? 35.995 -25.656 7.490  1.00 17.45  ? 104 HIS   C N   1 
ATOM   1865 C  CA  . HIS   B 1 98  ? 35.308 -24.863 6.497  1.00 16.64  ? 104 HIS   C CA  1 
ATOM   1866 C  C   . HIS   B 1 98  ? 34.036 -24.184 7.028  1.00 15.94  ? 104 HIS   C C   1 
ATOM   1867 O  O   . HIS   B 1 98  ? 33.237 -24.823 7.731  1.00 15.60  ? 104 HIS   C O   1 
ATOM   1868 C  CB  . HIS   B 1 98  ? 34.946 -25.763 5.317  1.00 19.38  ? 104 HIS   C CB  1 
ATOM   1869 C  CG  . HIS   B 1 98  ? 34.386 -24.990 4.192  1.00 22.12  ? 104 HIS   C CG  1 
ATOM   1870 N  ND1 . HIS   B 1 98  ? 35.152 -24.052 3.504  1.00 24.87  ? 104 HIS   C ND1 1 
ATOM   1871 C  CD2 . HIS   B 1 98  ? 33.115 -24.956 3.738  1.00 24.86  ? 104 HIS   C CD2 1 
ATOM   1872 C  CE1 . HIS   B 1 98  ? 34.330 -23.502 2.624  1.00 27.14  ? 104 HIS   C CE1 1 
ATOM   1873 N  NE2 . HIS   B 1 98  ? 33.091 -24.028 2.714  1.00 27.34  ? 104 HIS   C NE2 1 
ATOM   1874 N  N   . SER   B 1 99  ? 33.804 -22.902 6.655  1.00 16.21  ? 105 SER   C N   1 
ATOM   1875 C  CA  . SER   B 1 99  ? 32.593 -22.145 7.056  1.00 16.45  ? 105 SER   C CA  1 
ATOM   1876 C  C   . SER   B 1 99  ? 32.323 -20.995 6.049  1.00 17.91  ? 105 SER   C C   1 
ATOM   1877 O  O   . SER   B 1 99  ? 33.169 -20.105 5.938  1.00 20.12  ? 105 SER   C O   1 
ATOM   1878 C  CB  . SER   B 1 99  ? 32.824 -21.546 8.445  1.00 17.60  ? 105 SER   C CB  1 
ATOM   1879 O  OG  . SER   B 1 99  ? 31.735 -20.716 8.832  1.00 19.40  ? 105 SER   C OG  1 
ATOM   1880 N  N   . GLU   B 1 100 ? 31.207 -21.070 5.296  1.00 18.12  ? 106 GLU   C N   1 
ATOM   1881 C  CA  . GLU   B 1 100 ? 30.738 -20.024 4.344  1.00 18.16  ? 106 GLU   C CA  1 
ATOM   1882 C  C   . GLU   B 1 100 ? 29.623 -19.279 5.102  1.00 17.33  ? 106 GLU   C C   1 
ATOM   1883 O  O   . GLU   B 1 100 ? 29.080 -19.788 6.099  1.00 16.67  ? 106 GLU   C O   1 
ATOM   1884 C  CB  . GLU   B 1 100 ? 30.043 -20.653 3.071  1.00 21.25  ? 106 GLU   C CB  1 
ATOM   1885 C  CG  . GLU   B 1 100 ? 30.720 -21.793 2.373  1.00 31.50  ? 106 GLU   C CG  1 
ATOM   1886 C  CD  . GLU   B 1 100 ? 31.468 -21.506 1.099  1.00 40.85  ? 106 GLU   C CD  1 
ATOM   1887 O  OE1 . GLU   B 1 100 ? 31.539 -20.329 0.675  1.00 44.42  ? 106 GLU   C OE1 1 
ATOM   1888 O  OE2 . GLU   B 1 100 ? 32.064 -22.471 0.578  1.00 42.47  ? 106 GLU   C OE2 1 
ATOM   1889 N  N   . PRO   B 1 101 ? 29.224 -18.079 4.640  1.00 17.67  ? 107 PRO   C N   1 
ATOM   1890 C  CA  . PRO   B 1 101 ? 28.121 -17.379 5.322  1.00 17.34  ? 107 PRO   C CA  1 
ATOM   1891 C  C   . PRO   B 1 101 ? 26.841 -18.225 5.506  1.00 17.61  ? 107 PRO   C C   1 
ATOM   1892 O  O   . PRO   B 1 101 ? 26.241 -18.184 6.587  1.00 17.64  ? 107 PRO   C O   1 
ATOM   1893 C  CB  . PRO   B 1 101 ? 27.864 -16.128 4.433  1.00 19.44  ? 107 PRO   C CB  1 
ATOM   1894 C  CG  . PRO   B 1 101 ? 29.044 -16.008 3.561  1.00 21.94  ? 107 PRO   C CG  1 
ATOM   1895 C  CD  . PRO   B 1 101 ? 29.778 -17.303 3.495  1.00 19.38  ? 107 PRO   C CD  1 
ATOM   1896 N  N   . GLY   B 1 102 ? 26.502 -19.073 4.531  1.00 15.95  ? 108 GLY   C N   1 
ATOM   1897 C  CA  . GLY   B 1 102 ? 25.292 -19.902 4.641  1.00 16.01  ? 108 GLY   C CA  1 
ATOM   1898 C  C   . GLY   B 1 102 ? 25.384 -21.003 5.692  1.00 15.06  ? 108 GLY   C C   1 
ATOM   1899 O  O   . GLY   B 1 102 ? 24.395 -21.671 6.012  1.00 17.13  ? 108 GLY   C O   1 
ATOM   1900 N  N   . ASP   B 1 103 ? 26.603 -21.259 6.205  1.00 13.97  ? 109 ASP   C N   1 
ATOM   1901 C  CA  . ASP   B 1 103 ? 26.785 -22.273 7.240  1.00 13.27  ? 109 ASP   C CA  1 
ATOM   1902 C  C   . ASP   B 1 103 ? 26.418 -21.784 8.640  1.00 13.72  ? 109 ASP   C C   1 
ATOM   1903 O  O   . ASP   B 1 103 ? 26.325 -22.573 9.583  1.00 13.79  ? 109 ASP   C O   1 
ATOM   1904 C  CB  . ASP   B 1 103 ? 28.251 -22.757 7.260  1.00 14.16  ? 109 ASP   C CB  1 
ATOM   1905 C  CG  . ASP   B 1 103 ? 28.549 -23.561 6.029  1.00 16.14  ? 109 ASP   C CG  1 
ATOM   1906 O  OD1 . ASP   B 1 103 ? 27.703 -24.336 5.622  1.00 16.68  ? 109 ASP   C OD1 1 
ATOM   1907 O  OD2 . ASP   B 1 103 ? 29.684 -23.440 5.489  1.00 16.96  ? 109 ASP   C OD2 1 
ATOM   1908 N  N   . CYS   B 1 104 ? 26.234 -20.446 8.831  1.00 12.99  ? 110 CYS   C N   1 
ATOM   1909 C  CA  . CYS   B 1 104 ? 25.842 -19.904 10.153 1.00 13.12  ? 110 CYS   C CA  1 
ATOM   1910 C  C   . CYS   B 1 104 ? 24.579 -20.612 10.641 1.00 13.81  ? 110 CYS   C C   1 
ATOM   1911 O  O   . CYS   B 1 104 ? 23.638 -20.831 9.873  1.00 15.33  ? 110 CYS   C O   1 
ATOM   1912 C  CB  . CYS   B 1 104 ? 25.614 -18.392 10.070 1.00 13.79  ? 110 CYS   C CB  1 
ATOM   1913 S  SG  . CYS   B 1 104 ? 27.143 -17.436 9.955  1.00 15.90  ? 110 CYS   C SG  1 
ATOM   1914 N  N   . GLY   B 1 105 ? 24.578 -20.965 11.914 1.00 11.82  ? 111 GLY   C N   1 
ATOM   1915 C  CA  . GLY   B 1 105 ? 23.417 -21.641 12.502 1.00 13.50  ? 111 GLY   C CA  1 
ATOM   1916 C  C   . GLY   B 1 105 ? 23.640 -23.139 12.701 1.00 13.45  ? 111 GLY   C C   1 
ATOM   1917 O  O   . GLY   B 1 105 ? 22.878 -23.783 13.426 1.00 14.35  ? 111 GLY   C O   1 
ATOM   1918 N  N   . GLY   B 1 106 ? 24.667 -23.712 12.028 1.00 13.39  ? 112 GLY   C N   1 
ATOM   1919 C  CA  . GLY   B 1 106 ? 24.972 -25.144 12.192 1.00 13.77  ? 112 GLY   C CA  1 
ATOM   1920 C  C   . GLY   B 1 106 ? 25.355 -25.438 13.631 1.00 13.03  ? 112 GLY   C C   1 
ATOM   1921 O  O   . GLY   B 1 106 ? 26.088 -24.637 14.236 1.00 12.81  ? 112 GLY   C O   1 
ATOM   1922 N  N   . ILE   B 1 107 ? 24.921 -26.569 14.161 1.00 12.88  ? 113 ILE   C N   1 
ATOM   1923 C  CA  . ILE   B 1 107 ? 25.214 -26.872 15.555 1.00 11.87  ? 113 ILE   C CA  1 
ATOM   1924 C  C   . ILE   B 1 107 ? 26.588 -27.495 15.751 1.00 12.23  ? 113 ILE   C C   1 
ATOM   1925 O  O   . ILE   B 1 107 ? 26.983 -28.379 14.974 1.00 12.92  ? 113 ILE   C O   1 
ATOM   1926 C  CB  . ILE   B 1 107 ? 24.073 -27.809 16.102 1.00 15.07  ? 113 ILE   C CB  1 
ATOM   1927 C  CG1 . ILE   B 1 107 ? 22.854 -26.871 16.521 1.00 18.40  ? 113 ILE   C CG1 1 
ATOM   1928 C  CG2 . ILE   B 1 107 ? 24.529 -28.675 17.319 1.00 15.37  ? 113 ILE   C CG2 1 
ATOM   1929 C  CD1 . ILE   B 1 107 ? 21.513 -27.607 16.886 1.00 22.51  ? 113 ILE   C CD1 1 
ATOM   1930 N  N   . LEU   B 1 108 ? 27.275 -27.075 16.853 1.00 11.98  ? 114 LEU   C N   1 
ATOM   1931 C  CA  . LEU   B 1 108 ? 28.460 -27.761 17.360 1.00 11.51  ? 114 LEU   C CA  1 
ATOM   1932 C  C   . LEU   B 1 108 ? 27.953 -28.508 18.631 1.00 12.02  ? 114 LEU   C C   1 
ATOM   1933 O  O   . LEU   B 1 108 ? 27.324 -27.903 19.505 1.00 11.94  ? 114 LEU   C O   1 
ATOM   1934 C  CB  . LEU   B 1 108 ? 29.516 -26.703 17.765 1.00 11.91  ? 114 LEU   C CB  1 
ATOM   1935 C  CG  . LEU   B 1 108 ? 30.706 -27.228 18.559 1.00 12.70  ? 114 LEU   C CG  1 
ATOM   1936 C  CD1 . LEU   B 1 108 ? 31.598 -28.162 17.684 1.00 13.72  ? 114 LEU   C CD1 1 
ATOM   1937 C  CD2 . LEU   B 1 108 ? 31.560 -26.053 19.079 1.00 13.49  ? 114 LEU   C CD2 1 
ATOM   1938 N  N   . ARG   B 1 109 ? 28.237 -29.817 18.700 1.00 11.79  ? 115 ARG   C N   1 
ATOM   1939 C  CA  A ARG   B 1 109 ? 27.787 -30.647 19.843 0.50 12.38  ? 115 ARG   C CA  1 
ATOM   1940 C  CA  B ARG   B 1 109 ? 27.768 -30.683 19.797 0.50 13.14  ? 115 ARG   C CA  1 
ATOM   1941 C  C   . ARG   B 1 109 ? 28.910 -31.474 20.396 1.00 13.06  ? 115 ARG   C C   1 
ATOM   1942 O  O   . ARG   B 1 109 ? 29.835 -31.893 19.670 1.00 13.79  ? 115 ARG   C O   1 
ATOM   1943 C  CB  A ARG   B 1 109 ? 26.631 -31.584 19.414 0.50 13.73  ? 115 ARG   C CB  1 
ATOM   1944 C  CB  B ARG   B 1 109 ? 26.711 -31.642 19.189 0.50 16.28  ? 115 ARG   C CB  1 
ATOM   1945 C  CG  A ARG   B 1 109 ? 27.043 -32.540 18.288 0.50 13.94  ? 115 ARG   C CG  1 
ATOM   1946 C  CG  B ARG   B 1 109 ? 26.157 -32.714 20.097 0.50 20.04  ? 115 ARG   C CG  1 
ATOM   1947 C  CD  A ARG   B 1 109 ? 25.956 -33.515 17.805 0.50 19.32  ? 115 ARG   C CD  1 
ATOM   1948 C  CD  B ARG   B 1 109 ? 25.267 -33.702 19.322 0.50 21.40  ? 115 ARG   C CD  1 
ATOM   1949 N  NE  A ARG   B 1 109 ? 24.662 -32.873 17.578 0.50 26.68  ? 115 ARG   C NE  1 
ATOM   1950 N  NE  B ARG   B 1 109 ? 24.121 -33.037 18.690 0.50 23.50  ? 115 ARG   C NE  1 
ATOM   1951 C  CZ  A ARG   B 1 109 ? 24.063 -32.765 16.402 0.50 31.28  ? 115 ARG   C CZ  1 
ATOM   1952 C  CZ  B ARG   B 1 109 ? 23.055 -32.591 19.344 0.50 24.92  ? 115 ARG   C CZ  1 
ATOM   1953 N  NH1 A ARG   B 1 109 ? 24.642 -33.242 15.309 0.50 32.75  ? 115 ARG   C NH1 1 
ATOM   1954 N  NH1 B ARG   B 1 109 ? 22.969 -32.734 20.661 0.50 24.32  ? 115 ARG   C NH1 1 
ATOM   1955 N  NH2 A ARG   B 1 109 ? 22.884 -32.171 16.304 0.50 31.30  ? 115 ARG   C NH2 1 
ATOM   1956 N  NH2 B ARG   B 1 109 ? 22.078 -31.980 18.691 0.50 24.49  ? 115 ARG   C NH2 1 
ATOM   1957 N  N   . CYS   B 1 110 ? 28.833 -31.699 21.718 1.00 12.69  ? 116 CYS   C N   1 
ATOM   1958 C  CA  . CYS   B 1 110 ? 29.798 -32.581 22.394 1.00 13.36  ? 116 CYS   C CA  1 
ATOM   1959 C  C   . CYS   B 1 110 ? 28.967 -33.698 23.086 1.00 14.76  ? 116 CYS   C C   1 
ATOM   1960 O  O   . CYS   B 1 110 ? 27.739 -33.789 22.901 1.00 14.64  ? 116 CYS   C O   1 
ATOM   1961 C  CB  . CYS   B 1 110 ? 30.633 -31.804 23.413 1.00 13.24  ? 116 CYS   C CB  1 
ATOM   1962 S  SG  . CYS   B 1 110 ? 29.606 -31.137 24.775 1.00 13.62  ? 116 CYS   C SG  1 
ATOM   1963 N  N   . GLN   B 1 111 ? 29.619 -34.540 23.940 1.00 15.56  ? 117 GLN   C N   1 
ATOM   1964 C  CA  . GLN   B 1 111 ? 28.867 -35.592 24.635 1.00 17.63  ? 117 GLN   C CA  1 
ATOM   1965 C  C   . GLN   B 1 111 ? 27.784 -35.047 25.585 1.00 17.75  ? 117 GLN   C C   1 
ATOM   1966 O  O   . GLN   B 1 111 ? 26.815 -35.762 25.923 1.00 19.46  ? 117 GLN   C O   1 
ATOM   1967 C  CB  . GLN   B 1 111 ? 29.810 -36.549 25.407 1.00 19.54  ? 117 GLN   C CB  1 
ATOM   1968 C  CG  . GLN   B 1 111 ? 30.438 -35.881 26.625 1.00 22.51  ? 117 GLN   C CG  1 
ATOM   1969 C  CD  . GLN   B 1 111 ? 31.407 -36.781 27.382 1.00 32.32  ? 117 GLN   C CD  1 
ATOM   1970 O  OE1 . GLN   B 1 111 ? 32.611 -36.800 27.095 1.00 36.39  ? 117 GLN   C OE1 1 
ATOM   1971 N  NE2 . GLN   B 1 111 ? 30.910 -37.480 28.390 1.00 32.18  ? 117 GLN   C NE2 1 
ATOM   1972 N  N   . HIS   B 1 112 ? 27.883 -33.756 25.969 1.00 15.80  ? 118 HIS   C N   1 
ATOM   1973 C  CA  . HIS   B 1 112 ? 26.919 -33.167 26.906 1.00 15.38  ? 118 HIS   C CA  1 
ATOM   1974 C  C   . HIS   B 1 112 ? 25.744 -32.474 26.266 1.00 16.10  ? 118 HIS   C C   1 
ATOM   1975 O  O   . HIS   B 1 112 ? 24.785 -32.103 26.964 1.00 17.45  ? 118 HIS   C O   1 
ATOM   1976 C  CB  . HIS   B 1 112 ? 27.636 -32.203 27.854 1.00 15.86  ? 118 HIS   C CB  1 
ATOM   1977 C  CG  . HIS   B 1 112 ? 28.821 -32.834 28.528 1.00 16.12  ? 118 HIS   C CG  1 
ATOM   1978 N  ND1 . HIS   B 1 112 ? 30.136 -32.574 28.149 1.00 15.22  ? 118 HIS   C ND1 1 
ATOM   1979 C  CD2 . HIS   B 1 112 ? 28.843 -33.673 29.590 1.00 17.88  ? 118 HIS   C CD2 1 
ATOM   1980 C  CE1 . HIS   B 1 112 ? 30.903 -33.275 28.958 1.00 17.23  ? 118 HIS   C CE1 1 
ATOM   1981 N  NE2 . HIS   B 1 112 ? 30.170 -33.963 29.840 1.00 18.45  ? 118 HIS   C NE2 1 
ATOM   1982 N  N   . GLY   B 1 113 ? 25.814 -32.236 24.957 1.00 14.81  ? 119 GLY   C N   1 
ATOM   1983 C  CA  . GLY   B 1 113 ? 24.736 -31.535 24.267 1.00 14.40  ? 119 GLY   C CA  1 
ATOM   1984 C  C   . GLY   B 1 113 ? 25.241 -30.474 23.303 1.00 13.56  ? 119 GLY   C C   1 
ATOM   1985 O  O   . GLY   B 1 113 ? 26.371 -30.561 22.809 1.00 13.35  ? 119 GLY   C O   1 
ATOM   1986 N  N   . VAL   B 1 114 ? 24.388 -29.470 23.034 1.00 13.35  ? 120 VAL   C N   1 
ATOM   1987 C  CA  . VAL   B 1 114 ? 24.713 -28.383 22.100 1.00 13.32  ? 120 VAL   C CA  1 
ATOM   1988 C  C   . VAL   B 1 114 ? 25.644 -27.357 22.754 1.00 12.86  ? 120 VAL   C C   1 
ATOM   1989 O  O   . VAL   B 1 114 ? 25.371 -26.830 23.853 1.00 13.74  ? 120 VAL   C O   1 
ATOM   1990 C  CB  . VAL   B 1 114 ? 23.407 -27.693 21.615 1.00 14.54  ? 120 VAL   C CB  1 
ATOM   1991 C  CG1 . VAL   B 1 114 ? 23.761 -26.485 20.732 1.00 15.43  ? 120 VAL   C CG1 1 
ATOM   1992 C  CG2 . VAL   B 1 114 ? 22.483 -28.674 20.874 1.00 16.17  ? 120 VAL   C CG2 1 
ATOM   1993 N  N   . VAL   B 1 115 ? 26.821 -27.130 22.139 1.00 12.06  ? 121 VAL   C N   1 
ATOM   1994 C  CA  . VAL   B 1 115 ? 27.843 -26.197 22.642 1.00 12.13  ? 121 VAL   C CA  1 
ATOM   1995 C  C   . VAL   B 1 115 ? 27.606 -24.782 22.129 1.00 13.06  ? 121 VAL   C C   1 
ATOM   1996 O  O   . VAL   B 1 115 ? 27.849 -23.790 22.832 1.00 13.63  ? 121 VAL   C O   1 
ATOM   1997 C  CB  . VAL   B 1 115 ? 29.242 -26.733 22.227 1.00 11.95  ? 121 VAL   C CB  1 
ATOM   1998 C  CG1 . VAL   B 1 115 ? 30.319 -25.731 22.595 1.00 13.10  ? 121 VAL   C CG1 1 
ATOM   1999 C  CG2 . VAL   B 1 115 ? 29.501 -28.106 22.858 1.00 13.73  ? 121 VAL   C CG2 1 
ATOM   2000 N  N   . GLY   B 1 116 ? 27.258 -24.693 20.853 1.00 12.40  ? 122 GLY   C N   1 
ATOM   2001 C  CA  . GLY   B 1 116 ? 27.014 -23.400 20.232 1.00 13.48  ? 122 GLY   C CA  1 
ATOM   2002 C  C   . GLY   B 1 116 ? 26.695 -23.572 18.763 1.00 12.15  ? 122 GLY   C C   1 
ATOM   2003 O  O   . GLY   B 1 116 ? 26.365 -24.690 18.334 1.00 12.67  ? 122 GLY   C O   1 
ATOM   2004 N  N   . ILE   B 1 117 ? 26.654 -22.411 18.036 1.00 11.48  ? 123 ILE   C N   1 
ATOM   2005 C  CA  . ILE   B 1 117 ? 26.317 -22.432 16.616 1.00 11.66  ? 123 ILE   C CA  1 
ATOM   2006 C  C   . ILE   B 1 117 ? 27.364 -21.715 15.798 1.00 11.68  ? 123 ILE   C C   1 
ATOM   2007 O  O   . ILE   B 1 117 ? 28.006 -20.751 16.266 1.00 12.76  ? 123 ILE   C O   1 
ATOM   2008 C  CB  . ILE   B 1 117 ? 24.907 -21.801 16.339 1.00 13.32  ? 123 ILE   C CB  1 
ATOM   2009 C  CG1 . ILE   B 1 117 ? 24.813 -20.399 16.969 1.00 15.03  ? 123 ILE   C CG1 1 
ATOM   2010 C  CG2 . ILE   B 1 117 ? 23.783 -22.738 16.811 1.00 14.95  ? 123 ILE   C CG2 1 
ATOM   2011 C  CD1 . ILE   B 1 117 ? 23.445 -19.612 16.559 1.00 15.44  ? 123 ILE   C CD1 1 
ATOM   2012 N  N   . VAL   B 1 118 ? 27.523 -22.139 14.531 1.00 11.60  ? 124 VAL   C N   1 
ATOM   2013 C  CA  . VAL   B 1 118 ? 28.458 -21.458 13.614 1.00 11.87  ? 124 VAL   C CA  1 
ATOM   2014 C  C   . VAL   B 1 118 ? 28.089 -19.975 13.488 1.00 11.74  ? 124 VAL   C C   1 
ATOM   2015 O  O   . VAL   B 1 118 ? 26.889 -19.654 13.311 1.00 12.45  ? 124 VAL   C O   1 
ATOM   2016 C  CB  . VAL   B 1 118 ? 28.415 -22.121 12.218 1.00 12.04  ? 124 VAL   C CB  1 
ATOM   2017 C  CG1 . VAL   B 1 118 ? 29.279 -21.361 11.213 1.00 12.98  ? 124 VAL   C CG1 1 
ATOM   2018 C  CG2 . VAL   B 1 118 ? 28.888 -23.566 12.303 1.00 13.26  ? 124 VAL   C CG2 1 
ATOM   2019 N  N   . SER   B 1 119 ? 29.107 -19.083 13.586 1.00 11.82  ? 125 SER   C N   1 
ATOM   2020 C  CA  . SER   B 1 119 ? 28.899 -17.639 13.467 1.00 12.49  ? 125 SER   C CA  1 
ATOM   2021 C  C   . SER   B 1 119 ? 29.910 -16.950 12.544 1.00 13.91  ? 125 SER   C C   1 
ATOM   2022 O  O   . SER   B 1 119 ? 29.571 -15.880 11.991 1.00 13.72  ? 125 SER   C O   1 
ATOM   2023 C  CB  . SER   B 1 119 ? 28.951 -17.037 14.872 1.00 13.30  ? 125 SER   C CB  1 
ATOM   2024 O  OG  . SER   B 1 119 ? 28.836 -15.608 14.841 1.00 14.12  ? 125 SER   C OG  1 
ATOM   2025 N  N   . THR   B 1 120 ? 31.156 -17.494 12.425 1.00 13.66  ? 126 THR   C N   1 
ATOM   2026 C  CA  . THR   B 1 120 ? 32.181 -16.816 11.601 1.00 13.57  ? 126 THR   C CA  1 
ATOM   2027 C  C   . THR   B 1 120 ? 32.875 -17.845 10.705 1.00 13.25  ? 126 THR   C C   1 
ATOM   2028 O  O   . THR   B 1 120 ? 32.804 -19.073 10.938 1.00 13.06  ? 126 THR   C O   1 
ATOM   2029 C  CB  . THR   B 1 120 ? 33.259 -16.076 12.485 1.00 13.81  ? 126 THR   C CB  1 
ATOM   2030 O  OG1 . THR   B 1 120 ? 34.120 -17.037 13.128 1.00 15.21  ? 126 THR   C OG1 1 
ATOM   2031 C  CG2 . THR   B 1 120 ? 32.652 -15.134 13.504 1.00 14.67  ? 126 THR   C CG2 1 
ATOM   2032 N  N   . GLY   B 1 121 ? 33.583 -17.334 9.703  1.00 14.73  ? 127 GLY   C N   1 
ATOM   2033 C  CA  . GLY   B 1 121 ? 34.342 -18.190 8.795  1.00 15.82  ? 127 GLY   C CA  1 
ATOM   2034 C  C   . GLY   B 1 121 ? 35.368 -17.352 8.062  1.00 19.44  ? 127 GLY   C C   1 
ATOM   2035 O  O   . GLY   B 1 121 ? 35.109 -16.210 7.698  1.00 21.66  ? 127 GLY   C O   1 
ATOM   2036 N  N   . GLY   B 1 122 ? 36.505 -17.938 7.781  1.00 23.15  ? 128 GLY   C N   1 
ATOM   2037 C  CA  . GLY   B 1 122 ? 37.547 -17.221 7.041  1.00 25.49  ? 128 GLY   C CA  1 
ATOM   2038 C  C   . GLY   B 1 122 ? 38.908 -17.772 7.327  1.00 25.05  ? 128 GLY   C C   1 
ATOM   2039 O  O   . GLY   B 1 122 ? 39.138 -18.282 8.407  1.00 25.12  ? 128 GLY   C O   1 
ATOM   2040 N  N   . ASN   B 1 123 ? 39.835 -17.635 6.371  1.00 23.91  ? 129 ASN   C N   1 
ATOM   2041 C  CA  . ASN   B 1 123 ? 41.224 -18.062 6.552  1.00 23.95  ? 129 ASN   C CA  1 
ATOM   2042 C  C   . ASN   B 1 123 ? 41.331 -19.543 6.964  1.00 22.34  ? 129 ASN   C C   1 
ATOM   2043 O  O   . ASN   B 1 123 ? 42.287 -19.886 7.669  1.00 24.82  ? 129 ASN   C O   1 
ATOM   2044 C  CB  . ASN   B 1 123 ? 41.948 -17.157 7.599  1.00 27.29  ? 129 ASN   C CB  1 
ATOM   2045 C  CG  . ASN   B 1 123 ? 42.778 -16.025 7.032  1.00 34.06  ? 129 ASN   C CG  1 
ATOM   2046 O  OD1 . ASN   B 1 123 ? 43.121 -15.990 5.846  1.00 35.05  ? 129 ASN   C OD1 1 
ATOM   2047 N  ND2 . ASN   B 1 123 ? 43.134 -15.056 7.875  1.00 36.63  ? 129 ASN   C ND2 1 
ATOM   2048 N  N   . GLY   B 1 124 ? 40.384 -20.405 6.539  1.00 19.74  ? 130 GLY   C N   1 
ATOM   2049 C  CA  . GLY   B 1 124 ? 40.403 -21.835 6.905  1.00 18.83  ? 130 GLY   C CA  1 
ATOM   2050 C  C   . GLY   B 1 124 ? 40.016 -22.132 8.346  1.00 17.44  ? 130 GLY   C C   1 
ATOM   2051 O  O   . GLY   B 1 124 ? 40.250 -23.236 8.852  1.00 17.34  ? 130 GLY   C O   1 
ATOM   2052 N  N   . LEU   B 1 125 ? 39.368 -21.151 8.994  1.00 16.41  ? 131 LEU   C N   1 
ATOM   2053 C  CA  . LEU   B 1 125 ? 38.909 -21.298 10.374 1.00 15.28  ? 131 LEU   C CA  1 
ATOM   2054 C  C   . LEU   B 1 125 ? 37.375 -21.194 10.409 1.00 15.82  ? 131 LEU   C C   1 
ATOM   2055 O  O   . LEU   B 1 125 ? 36.757 -20.537 9.538  1.00 17.81  ? 131 LEU   C O   1 
ATOM   2056 C  CB  . LEU   B 1 125 ? 39.507 -20.193 11.281 1.00 16.67  ? 131 LEU   C CB  1 
ATOM   2057 C  CG  . LEU   B 1 125 ? 41.055 -20.214 11.391 1.00 19.71  ? 131 LEU   C CG  1 
ATOM   2058 C  CD1 . LEU   B 1 125 ? 41.631 -18.897 11.889 1.00 23.25  ? 131 LEU   C CD1 1 
ATOM   2059 C  CD2 . LEU   B 1 125 ? 41.548 -21.367 12.175 1.00 22.10  ? 131 LEU   C CD2 1 
ATOM   2060 N  N   . VAL   B 1 126 ? 36.774 -21.835 11.372 1.00 13.06  ? 132 VAL   C N   1 
ATOM   2061 C  CA  . VAL   B 1 126 ? 35.327 -21.706 11.605 1.00 12.24  ? 132 VAL   C CA  1 
ATOM   2062 C  C   . VAL   B 1 126 ? 35.172 -21.259 13.068 1.00 12.18  ? 132 VAL   C C   1 
ATOM   2063 O  O   . VAL   B 1 126 ? 35.850 -21.777 13.967 1.00 13.13  ? 132 VAL   C O   1 
ATOM   2064 C  CB  . VAL   B 1 126 ? 34.566 -23.043 11.362 1.00 13.09  ? 132 VAL   C CB  1 
ATOM   2065 C  CG1 . VAL   B 1 126 ? 35.188 -24.218 12.081 1.00 14.80  ? 132 VAL   C CG1 1 
ATOM   2066 C  CG2 . VAL   B 1 126 ? 33.058 -22.933 11.692 1.00 14.12  ? 132 VAL   C CG2 1 
ATOM   2067 N  N   . GLY   B 1 127 ? 34.295 -20.282 13.280 1.00 12.02  ? 133 GLY   C N   1 
ATOM   2068 C  CA  . GLY   B 1 127 ? 34.077 -19.786 14.632 1.00 12.22  ? 133 GLY   C CA  1 
ATOM   2069 C  C   . GLY   B 1 127 ? 32.649 -20.093 15.076 1.00 12.85  ? 133 GLY   C C   1 
ATOM   2070 O  O   . GLY   B 1 127 ? 31.697 -19.961 14.301 1.00 13.24  ? 133 GLY   C O   1 
ATOM   2071 N  N   . PHE   B 1 128 ? 32.517 -20.461 16.345 1.00 11.14  ? 134 PHE   C N   1 
ATOM   2072 C  CA  . PHE   B 1 128 ? 31.219 -20.816 16.960 1.00 11.71  ? 134 PHE   C CA  1 
ATOM   2073 C  C   . PHE   B 1 128 ? 30.900 -19.877 18.115 1.00 12.15  ? 134 PHE   C C   1 
ATOM   2074 O  O   . PHE   B 1 128 ? 31.747 -19.608 18.961 1.00 13.10  ? 134 PHE   C O   1 
ATOM   2075 C  CB  . PHE   B 1 128 ? 31.295 -22.256 17.541 1.00 12.34  ? 134 PHE   C CB  1 
ATOM   2076 C  CG  . PHE   B 1 128 ? 31.808 -23.291 16.558 1.00 12.13  ? 134 PHE   C CG  1 
ATOM   2077 C  CD1 . PHE   B 1 128 ? 30.963 -23.864 15.627 1.00 12.63  ? 134 PHE   C CD1 1 
ATOM   2078 C  CD2 . PHE   B 1 128 ? 33.152 -23.661 16.555 1.00 13.27  ? 134 PHE   C CD2 1 
ATOM   2079 C  CE1 . PHE   B 1 128 ? 31.433 -24.828 14.744 1.00 13.46  ? 134 PHE   C CE1 1 
ATOM   2080 C  CE2 . PHE   B 1 128 ? 33.628 -24.622 15.656 1.00 14.27  ? 134 PHE   C CE2 1 
ATOM   2081 C  CZ  . PHE   B 1 128 ? 32.773 -25.189 14.751 1.00 13.42  ? 134 PHE   C CZ  1 
ATOM   2082 N  N   . ALA   B 1 129 ? 29.649 -19.378 18.129 1.00 11.54  ? 135 ALA   C N   1 
ATOM   2083 C  CA  . ALA   B 1 129 ? 29.172 -18.581 19.253 1.00 11.87  ? 135 ALA   C CA  1 
ATOM   2084 C  C   . ALA   B 1 129 ? 28.793 -19.571 20.391 1.00 13.44  ? 135 ALA   C C   1 
ATOM   2085 O  O   . ALA   B 1 129 ? 27.882 -20.398 20.224 1.00 12.97  ? 135 ALA   C O   1 
ATOM   2086 C  CB  . ALA   B 1 129 ? 27.931 -17.781 18.813 1.00 12.99  ? 135 ALA   C CB  1 
ATOM   2087 N  N   . ASP   B 1 130 ? 29.451 -19.468 21.535 1.00 12.93  ? 136 ASP   C N   1 
ATOM   2088 C  CA  . ASP   B 1 130 ? 29.182 -20.363 22.677 1.00 13.02  ? 136 ASP   C CA  1 
ATOM   2089 C  C   . ASP   B 1 130 ? 27.855 -20.012 23.302 1.00 13.05  ? 136 ASP   C C   1 
ATOM   2090 O  O   . ASP   B 1 130 ? 27.502 -18.836 23.404 1.00 13.37  ? 136 ASP   C O   1 
ATOM   2091 C  CB  . ASP   B 1 130 ? 30.287 -20.145 23.737 1.00 14.43  ? 136 ASP   C CB  1 
ATOM   2092 C  CG  . ASP   B 1 130 ? 30.194 -21.076 24.930 1.00 16.50  ? 136 ASP   C CG  1 
ATOM   2093 O  OD1 . ASP   B 1 130 ? 30.027 -22.286 24.724 1.00 16.14  ? 136 ASP   C OD1 1 
ATOM   2094 O  OD2 . ASP   B 1 130 ? 30.183 -20.564 26.082 1.00 19.38  ? 136 ASP   C OD2 1 
ATOM   2095 N  N   . VAL   B 1 131 ? 27.152 -21.019 23.810 1.00 12.74  ? 137 VAL   C N   1 
ATOM   2096 C  CA  . VAL   B 1 131 ? 25.904 -20.818 24.580 1.00 13.22  ? 137 VAL   C CA  1 
ATOM   2097 C  C   . VAL   B 1 131 ? 25.968 -21.496 25.968 1.00 13.98  ? 137 VAL   C C   1 
ATOM   2098 O  O   . VAL   B 1 131 ? 24.994 -21.435 26.730 1.00 14.26  ? 137 VAL   C O   1 
ATOM   2099 C  CB  . VAL   B 1 131 ? 24.608 -21.253 23.845 1.00 13.96  ? 137 VAL   C CB  1 
ATOM   2100 C  CG1 . VAL   B 1 131 ? 24.452 -20.455 22.522 1.00 13.58  ? 137 VAL   C CG1 1 
ATOM   2101 C  CG2 . VAL   B 1 131 ? 24.628 -22.758 23.553 1.00 14.34  ? 137 VAL   C CG2 1 
ATOM   2102 N  N   . ARG   B 1 132 ? 27.083 -22.169 26.289 1.00 13.09  ? 138 ARG   C N   1 
ATOM   2103 C  CA  . ARG   B 1 132 ? 27.189 -22.953 27.543 1.00 12.73  ? 138 ARG   C CA  1 
ATOM   2104 C  C   . ARG   B 1 132 ? 27.140 -22.133 28.813 1.00 14.07  ? 138 ARG   C C   1 
ATOM   2105 O  O   . ARG   B 1 132 ? 26.829 -22.678 29.890 1.00 15.43  ? 138 ARG   C O   1 
ATOM   2106 C  CB  . ARG   B 1 132 ? 28.447 -23.811 27.524 1.00 12.32  ? 138 ARG   C CB  1 
ATOM   2107 C  CG  . ARG   B 1 132 ? 28.421 -24.890 26.418 1.00 12.78  ? 138 ARG   C CG  1 
ATOM   2108 C  CD  . ARG   B 1 132 ? 29.742 -25.637 26.439 1.00 13.30  ? 138 ARG   C CD  1 
ATOM   2109 N  NE  . ARG   B 1 132 ? 30.829 -24.747 25.991 1.00 13.11  ? 138 ARG   C NE  1 
ATOM   2110 C  CZ  . ARG   B 1 132 ? 32.093 -25.137 25.831 1.00 14.09  ? 138 ARG   C CZ  1 
ATOM   2111 N  NH1 . ARG   B 1 132 ? 32.468 -26.370 26.166 1.00 13.53  ? 138 ARG   C NH1 1 
ATOM   2112 N  NH2 . ARG   B 1 132 ? 33.001 -24.285 25.376 1.00 14.18  ? 138 ARG   C NH2 1 
ATOM   2113 N  N   . ASP   B 1 133 ? 27.417 -20.826 28.724 1.00 14.08  ? 139 ASP   C N   1 
ATOM   2114 C  CA  . ASP   B 1 133 ? 27.375 -19.966 29.916 1.00 14.36  ? 139 ASP   C CA  1 
ATOM   2115 C  C   . ASP   B 1 133 ? 25.956 -19.407 30.154 1.00 15.64  ? 139 ASP   C C   1 
ATOM   2116 O  O   . ASP   B 1 133 ? 25.746 -18.815 31.218 1.00 16.64  ? 139 ASP   C O   1 
ATOM   2117 C  CB  . ASP   B 1 133 ? 28.346 -18.780 29.763 1.00 16.26  ? 139 ASP   C CB  1 
ATOM   2118 C  CG  . ASP   B 1 133 ? 27.990 -17.851 28.629 1.00 17.09  ? 139 ASP   C CG  1 
ATOM   2119 O  OD1 . ASP   B 1 133 ? 27.647 -18.353 27.547 1.00 16.98  ? 139 ASP   C OD1 1 
ATOM   2120 O  OD2 . ASP   B 1 133 ? 28.011 -16.595 28.840 1.00 19.85  ? 139 ASP   C OD2 1 
ATOM   2121 N  N   . LEU   B 1 134 ? 24.998 -19.614 29.221 1.00 15.02  ? 140 LEU   C N   1 
ATOM   2122 C  CA  . LEU   B 1 134 ? 23.633 -19.040 29.318 1.00 15.01  ? 140 LEU   C CA  1 
ATOM   2123 C  C   . LEU   B 1 134 ? 22.778 -20.008 30.107 1.00 15.49  ? 140 LEU   C C   1 
ATOM   2124 O  O   . LEU   B 1 134 ? 21.966 -20.750 29.550 1.00 15.67  ? 140 LEU   C O   1 
ATOM   2125 C  CB  . LEU   B 1 134 ? 23.067 -18.790 27.907 1.00 14.79  ? 140 LEU   C CB  1 
ATOM   2126 C  CG  . LEU   B 1 134 ? 23.939 -17.846 27.036 1.00 15.85  ? 140 LEU   C CG  1 
ATOM   2127 C  CD1 . LEU   B 1 134 ? 23.365 -17.726 25.594 1.00 17.31  ? 140 LEU   C CD1 1 
ATOM   2128 C  CD2 . LEU   B 1 134 ? 24.051 -16.438 27.665 1.00 17.19  ? 140 LEU   C CD2 1 
ATOM   2129 N  N   . LEU   B 1 135 ? 23.000 -20.037 31.455 1.00 15.44  ? 141 LEU   C N   1 
ATOM   2130 C  CA  . LEU   B 1 135 ? 22.352 -21.073 32.278 1.00 16.59  ? 141 LEU   C CA  1 
ATOM   2131 C  C   . LEU   B 1 135 ? 20.833 -20.955 32.320 1.00 16.40  ? 141 LEU   C C   1 
ATOM   2132 O  O   . LEU   B 1 135 ? 20.149 -21.977 32.506 1.00 17.56  ? 141 LEU   C O   1 
ATOM   2133 C  CB  . LEU   B 1 135 ? 22.940 -21.109 33.713 1.00 16.09  ? 141 LEU   C CB  1 
ATOM   2134 C  CG  . LEU   B 1 135 ? 24.498 -21.108 33.783 1.00 17.08  ? 141 LEU   C CG  1 
ATOM   2135 C  CD1 . LEU   B 1 135 ? 24.984 -21.094 35.265 1.00 17.84  ? 141 LEU   C CD1 1 
ATOM   2136 C  CD2 . LEU   B 1 135 ? 25.107 -22.280 32.998 1.00 18.03  ? 141 LEU   C CD2 1 
ATOM   2137 N  N   . TRP   B 1 136 ? 20.313 -19.737 32.101 1.00 16.67  ? 142 TRP   C N   1 
ATOM   2138 C  CA  . TRP   B 1 136 ? 18.869 -19.496 32.134 1.00 17.24  ? 142 TRP   C CA  1 
ATOM   2139 C  C   . TRP   B 1 136 ? 18.125 -20.209 31.002 1.00 17.73  ? 142 TRP   C C   1 
ATOM   2140 O  O   . TRP   B 1 136 ? 16.899 -20.337 31.071 1.00 19.16  ? 142 TRP   C O   1 
ATOM   2141 C  CB  . TRP   B 1 136 ? 18.593 -17.981 32.130 1.00 17.68  ? 142 TRP   C CB  1 
ATOM   2142 C  CG  . TRP   B 1 136 ? 19.279 -17.238 31.020 1.00 17.19  ? 142 TRP   C CG  1 
ATOM   2143 C  CD1 . TRP   B 1 136 ? 20.465 -16.564 31.090 1.00 18.41  ? 142 TRP   C CD1 1 
ATOM   2144 C  CD2 . TRP   B 1 136 ? 18.775 -17.024 29.682 1.00 17.88  ? 142 TRP   C CD2 1 
ATOM   2145 N  NE1 . TRP   B 1 136 ? 20.755 -15.986 29.857 1.00 19.07  ? 142 TRP   C NE1 1 
ATOM   2146 C  CE2 . TRP   B 1 136 ? 19.711 -16.221 28.997 1.00 18.83  ? 142 TRP   C CE2 1 
ATOM   2147 C  CE3 . TRP   B 1 136 ? 17.613 -17.417 29.023 1.00 17.77  ? 142 TRP   C CE3 1 
ATOM   2148 C  CZ2 . TRP   B 1 136 ? 19.530 -15.834 27.662 1.00 18.64  ? 142 TRP   C CZ2 1 
ATOM   2149 C  CZ3 . TRP   B 1 136 ? 17.411 -16.996 27.718 1.00 18.18  ? 142 TRP   C CZ3 1 
ATOM   2150 C  CH2 . TRP   B 1 136 ? 18.363 -16.227 27.053 1.00 18.17  ? 142 TRP   C CH2 1 
ATOM   2151 N  N   . LEU   B 1 137 ? 18.830 -20.685 29.953 1.00 16.79  ? 143 LEU   C N   1 
ATOM   2152 C  CA  . LEU   B 1 137 ? 18.150 -21.452 28.903 1.00 17.42  ? 143 LEU   C CA  1 
ATOM   2153 C  C   . LEU   B 1 137 ? 17.558 -22.754 29.470 1.00 20.02  ? 143 LEU   C C   1 
ATOM   2154 O  O   . LEU   B 1 137 ? 16.653 -23.321 28.855 1.00 21.17  ? 143 LEU   C O   1 
ATOM   2155 C  CB  . LEU   B 1 137 ? 19.098 -21.794 27.755 1.00 17.44  ? 143 LEU   C CB  1 
ATOM   2156 C  CG  . LEU   B 1 137 ? 19.529 -20.608 26.885 1.00 17.08  ? 143 LEU   C CG  1 
ATOM   2157 C  CD1 . LEU   B 1 137 ? 20.716 -21.019 25.956 1.00 16.75  ? 143 LEU   C CD1 1 
ATOM   2158 C  CD2 . LEU   B 1 137 ? 18.365 -20.068 26.029 1.00 17.91  ? 143 LEU   C CD2 1 
ATOM   2159 N  N   . ASP   B 1 138 ? 18.080 -23.252 30.612 1.00 18.54  ? 144 ASP   C N   1 
ATOM   2160 C  CA  . ASP   B 1 138 ? 17.615 -24.523 31.189 1.00 20.27  ? 144 ASP   C CA  1 
ATOM   2161 C  C   . ASP   B 1 138 ? 16.364 -24.380 32.059 1.00 23.39  ? 144 ASP   C C   1 
ATOM   2162 O  O   . ASP   B 1 138 ? 15.888 -25.401 32.588 1.00 24.14  ? 144 ASP   C O   1 
ATOM   2163 C  CB  . ASP   B 1 138 ? 18.716 -25.202 32.034 1.00 20.45  ? 144 ASP   C CB  1 
ATOM   2164 C  CG  . ASP   B 1 138 ? 19.953 -25.621 31.246 1.00 21.84  ? 144 ASP   C CG  1 
ATOM   2165 O  OD1 . ASP   B 1 138 ? 19.890 -25.641 30.002 1.00 21.15  ? 144 ASP   C OD1 1 
ATOM   2166 O  OD2 . ASP   B 1 138 ? 20.992 -25.923 31.888 1.00 24.22  ? 144 ASP   C OD2 1 
ATOM   2167 N  N   . GLU   B 1 139 ? 15.859 -23.163 32.243 1.00 24.80  ? 145 GLU   C N   1 
ATOM   2168 C  CA  . GLU   B 1 139 ? 14.701 -22.963 33.119 1.00 29.44  ? 145 GLU   C CA  1 
ATOM   2169 C  C   . GLU   B 1 139 ? 13.612 -22.113 32.461 1.00 33.48  ? 145 GLU   C C   1 
ATOM   2170 O  O   . GLU   B 1 139 ? 13.875 -21.373 31.521 1.00 34.54  ? 145 GLU   C O   1 
ATOM   2171 C  CB  . GLU   B 1 139 ? 15.179 -22.378 34.459 1.00 33.78  ? 145 GLU   C CB  1 
ATOM   2172 C  CG  . GLU   B 1 139 ? 15.851 -21.030 34.293 1.00 40.96  ? 145 GLU   C CG  1 
ATOM   2173 C  CD  . GLU   B 1 139 ? 16.845 -20.624 35.366 1.00 50.00  ? 145 GLU   C CD  1 
ATOM   2174 O  OE1 . GLU   B 1 139 ? 17.183 -19.418 35.437 1.00 50.87  ? 145 GLU   C OE1 1 
ATOM   2175 O  OE2 . GLU   B 1 139 ? 17.282 -21.509 36.135 1.00 52.50  ? 145 GLU   C OE2 1 
ATOM   2176 N  N   . GLU   B 1 140 ? 12.371 -22.259 32.930 1.00 36.14  ? 146 GLU   C N   1 
ATOM   2177 C  CA  . GLU   B 1 140 ? 11.228 -21.541 32.367 1.00 38.69  ? 146 GLU   C CA  1 
ATOM   2178 C  C   . GLU   B 1 140 ? 11.364 -20.020 32.460 1.00 39.89  ? 146 GLU   C C   1 
ATOM   2179 O  O   . GLU   B 1 140 ? 11.989 -19.504 33.389 1.00 40.78  ? 146 GLU   C O   1 
ATOM   2180 C  CB  . GLU   B 1 140 ? 9.923  -22.032 33.032 1.00 42.99  ? 146 GLU   C CB  1 
ATOM   2181 C  CG  . GLU   B 1 140 ? 8.675  -21.290 32.574 1.00 51.21  ? 146 GLU   C CG  1 
ATOM   2182 C  CD  . GLU   B 1 140 ? 7.957  -20.559 33.692 1.00 60.15  ? 146 GLU   C CD  1 
ATOM   2183 O  OE1 . GLU   B 1 140 ? 7.637  -21.204 34.717 1.00 60.71  ? 146 GLU   C OE1 1 
ATOM   2184 O  OE2 . GLU   B 1 140 ? 7.723  -19.337 33.546 1.00 64.20  ? 146 GLU   C OE2 1 
HETATM 2185 N  N1  . A1B53 C 2 .   ? 9.285  15.471  21.761 0.66 18.14  ? 201 A1B53 A N1  1 
HETATM 2186 C  C4  . A1B53 C 2 .   ? 7.193  13.353  24.102 0.66 18.61  ? 201 A1B53 A C4  1 
HETATM 2187 C  C5  . A1B53 C 2 .   ? 6.999  12.027  24.439 0.66 18.11  ? 201 A1B53 A C5  1 
HETATM 2188 C  C6  . A1B53 C 2 .   ? 7.756  11.043  23.831 0.66 17.27  ? 201 A1B53 A C6  1 
HETATM 2189 C  C7  . A1B53 C 2 .   ? 8.748  11.370  22.915 0.66 17.18  ? 201 A1B53 A C7  1 
HETATM 2190 C  C8  . A1B53 C 2 .   ? 9.623  10.300  22.316 0.66 17.24  ? 201 A1B53 A C8  1 
HETATM 2191 C  C10 . A1B53 C 2 .   ? 9.220  15.303  20.303 0.66 17.53  ? 201 A1B53 A C10 1 
HETATM 2192 C  C13 . A1B53 C 2 .   ? 11.163 16.573  20.952 0.66 17.42  ? 201 A1B53 A C13 1 
HETATM 2193 O  O2  . A1B53 C 2 .   ? 10.644 16.396  23.339 0.66 20.75  ? 201 A1B53 A O2  1 
HETATM 2194 C  C14 . A1B53 C 2 .   ? 10.391 16.130  22.175 0.66 18.94  ? 201 A1B53 A C14 1 
HETATM 2195 C  C11 . A1B53 C 2 .   ? 10.628 15.642  19.849 0.66 16.84  ? 201 A1B53 A C11 1 
HETATM 2196 C  C12 . A1B53 C 2 .   ? 10.604 16.259  18.460 0.66 16.76  ? 201 A1B53 A C12 1 
HETATM 2197 O  O1  . A1B53 C 2 .   ? 10.072 17.355  18.254 0.66 17.70  ? 201 A1B53 A O1  1 
HETATM 2198 N  N2  . A1B53 C 2 .   ? 11.048 15.489  17.474 0.66 15.59  ? 201 A1B53 A N2  1 
HETATM 2199 C  C2  . A1B53 C 2 .   ? 8.154  15.146  22.646 0.66 19.19  ? 201 A1B53 A C2  1 
HETATM 2200 C  C1  . A1B53 C 2 .   ? 6.823  15.483  21.947 0.66 20.26  ? 201 A1B53 A C1  1 
HETATM 2201 O  O   . A1B53 C 2 .   ? 6.379  14.764  21.050 0.66 19.95  ? 201 A1B53 A O   1 
HETATM 2202 N  N   . A1B53 C 2 .   ? 6.250  16.609  22.337 0.66 20.26  ? 201 A1B53 A N   1 
HETATM 2203 C  C   . A1B53 C 2 .   ? 4.978  17.045  21.792 0.66 21.06  ? 201 A1B53 A C   1 
HETATM 2204 C  C3  . A1B53 C 2 .   ? 8.154  13.712  23.164 0.66 18.34  ? 201 A1B53 A C3  1 
HETATM 2205 C  C9  . A1B53 C 2 .   ? 8.940  12.713  22.599 0.66 17.95  ? 201 A1B53 A C9  1 
HETATM 2206 ZN ZN  . ZN    D 3 .   ? 11.212 -4.023  5.806  1.00 20.12  2 202 ZN    A ZN  1 
HETATM 2207 ZN ZN  . ZN    E 3 .   ? 30.847 -31.199 26.736 1.00 14.28  2 201 ZN    C ZN  1 
HETATM 2208 S  S   . DMS   F 4 .   ? 20.715 -31.429 9.814  1.00 100.62 ? 202 DMS   C S   1 
HETATM 2209 O  O   . DMS   F 4 .   ? 20.815 -30.485 8.654  1.00 100.61 ? 202 DMS   C O   1 
HETATM 2210 C  C1  . DMS   F 4 .   ? 22.362 -32.065 10.176 1.00 100.62 ? 202 DMS   C C1  1 
HETATM 2211 C  C2  . DMS   F 4 .   ? 20.580 -30.440 11.326 1.00 100.64 ? 202 DMS   C C2  1 
HETATM 2212 O  O   . HOH   G 5 .   ? 3.099  9.361   9.119  1.00 36.27  ? 301 HOH   A O   1 
HETATM 2213 O  O   . HOH   G 5 .   ? 2.110  23.153  21.369 1.00 29.75  ? 302 HOH   A O   1 
HETATM 2214 O  O   . HOH   G 5 .   ? 11.303 8.884   4.299  1.00 23.35  ? 303 HOH   A O   1 
HETATM 2215 O  O   . HOH   G 5 .   ? 35.433 -3.930  7.729  1.00 23.37  ? 304 HOH   A O   1 
HETATM 2216 O  O   . HOH   G 5 .   ? 37.601 14.904  14.087 1.00 48.85  ? 305 HOH   A O   1 
HETATM 2217 O  O   . HOH   G 5 .   ? 14.198 17.376  4.253  1.00 39.09  ? 306 HOH   A O   1 
HETATM 2218 O  O   . HOH   G 5 .   ? -3.219 9.998   27.788 1.00 43.26  ? 307 HOH   A O   1 
HETATM 2219 O  O   . HOH   G 5 .   ? 2.755  -3.050  20.741 1.00 30.88  ? 308 HOH   A O   1 
HETATM 2220 O  O   . HOH   G 5 .   ? 27.900 8.035   1.717  1.00 36.71  ? 309 HOH   A O   1 
HETATM 2221 O  O   . HOH   G 5 .   ? 8.391  -2.807  31.858 1.00 27.73  ? 310 HOH   A O   1 
HETATM 2222 O  O   . HOH   G 5 .   ? 4.022  14.208  20.026 1.00 29.26  ? 311 HOH   A O   1 
HETATM 2223 O  O   . HOH   G 5 .   ? 0.497  -1.034  19.333 1.00 27.63  ? 312 HOH   A O   1 
HETATM 2224 O  O   . HOH   G 5 .   ? 8.771  19.033  19.829 1.00 19.94  ? 313 HOH   A O   1 
HETATM 2225 O  O   . HOH   G 5 .   ? 17.498 0.996   28.229 1.00 26.10  ? 314 HOH   A O   1 
HETATM 2226 O  O   . HOH   G 5 .   ? 28.182 3.112   4.962  1.00 34.01  ? 315 HOH   A O   1 
HETATM 2227 O  O   . HOH   G 5 .   ? 12.339 22.174  12.759 1.00 36.56  ? 316 HOH   A O   1 
HETATM 2228 O  O   . HOH   G 5 .   ? 35.100 16.439  19.772 1.00 48.88  ? 317 HOH   A O   1 
HETATM 2229 O  O   . HOH   G 5 .   ? 9.636  22.093  10.287 1.00 48.84  ? 318 HOH   A O   1 
HETATM 2230 O  O   . HOH   G 5 .   ? 4.702  -3.647  28.894 1.00 29.31  ? 319 HOH   A O   1 
HETATM 2231 O  O   . HOH   G 5 .   ? 4.183  9.461   27.832 1.00 34.82  ? 320 HOH   A O   1 
HETATM 2232 O  O   . HOH   G 5 .   ? 23.516 21.745  7.270  1.00 26.68  ? 321 HOH   A O   1 
HETATM 2233 O  O   . HOH   G 5 .   ? 20.167 19.957  5.644  1.00 43.13  ? 322 HOH   A O   1 
HETATM 2234 O  O   . HOH   G 5 .   ? 7.489  20.369  17.605 1.00 22.50  ? 323 HOH   A O   1 
HETATM 2235 O  O   . HOH   G 5 .   ? 29.515 22.337  19.328 1.00 33.05  ? 324 HOH   A O   1 
HETATM 2236 O  O   . HOH   G 5 .   ? 30.568 10.572  15.721 1.00 30.59  ? 325 HOH   A O   1 
HETATM 2237 O  O   . HOH   G 5 .   ? 33.868 14.173  9.730  1.00 32.73  ? 326 HOH   A O   1 
HETATM 2238 O  O   . HOH   G 5 .   ? 10.392 17.156  25.908 1.00 33.41  ? 327 HOH   A O   1 
HETATM 2239 O  O   . HOH   G 5 .   ? 19.406 10.078  19.648 1.00 14.28  ? 328 HOH   A O   1 
HETATM 2240 O  O   . HOH   G 5 .   ? 33.751 11.154  15.519 1.00 42.18  ? 329 HOH   A O   1 
HETATM 2241 O  O   . HOH   G 5 .   ? 21.958 2.385   -0.858 1.00 34.52  ? 330 HOH   A O   1 
HETATM 2242 O  O   . HOH   G 5 .   ? 3.260  20.819  24.323 1.00 32.25  ? 331 HOH   A O   1 
HETATM 2243 O  O   . HOH   G 5 .   ? 15.381 14.225  26.313 1.00 38.54  ? 332 HOH   A O   1 
HETATM 2244 O  O   . HOH   G 5 .   ? 24.973 5.174   21.440 1.00 31.48  ? 333 HOH   A O   1 
HETATM 2245 O  O   . HOH   G 5 .   ? 12.125 16.572  27.870 1.00 33.12  ? 334 HOH   A O   1 
HETATM 2246 O  O   . HOH   G 5 .   ? 4.000  -8.203  9.716  1.00 51.43  ? 335 HOH   A O   1 
HETATM 2247 O  O   . HOH   G 5 .   ? -0.076 1.262   15.754 1.00 14.13  ? 336 HOH   A O   1 
HETATM 2248 O  O   . HOH   G 5 .   ? 22.691 0.890   17.393 1.00 17.66  ? 337 HOH   A O   1 
HETATM 2249 O  O   . HOH   G 5 .   ? 10.550 10.166  31.350 1.00 23.34  ? 338 HOH   A O   1 
HETATM 2250 O  O   . HOH   G 5 .   ? 1.184  12.150  21.153 1.00 38.86  ? 339 HOH   A O   1 
HETATM 2251 O  O   . HOH   G 5 .   ? 14.928 11.382  0.029  1.00 33.79  ? 340 HOH   A O   1 
HETATM 2252 O  O   . HOH   G 5 .   ? -1.507 13.901  22.199 1.00 55.72  ? 341 HOH   A O   1 
HETATM 2253 O  O   . HOH   G 5 .   ? 11.663 17.983  4.924  1.00 37.53  ? 342 HOH   A O   1 
HETATM 2254 O  O   . HOH   G 5 .   ? 23.326 11.752  21.933 1.00 34.39  ? 343 HOH   A O   1 
HETATM 2255 O  O   . HOH   G 5 .   ? 14.188 13.687  23.952 1.00 20.25  ? 344 HOH   A O   1 
HETATM 2256 O  O   . HOH   G 5 .   ? 8.465  25.081  23.699 1.00 26.18  ? 345 HOH   A O   1 
HETATM 2257 O  O   . HOH   G 5 .   ? 6.170  2.290   5.400  1.00 28.10  ? 346 HOH   A O   1 
HETATM 2258 O  O   . HOH   G 5 .   ? 29.983 11.611  18.459 1.00 29.79  ? 347 HOH   A O   1 
HETATM 2259 O  O   . HOH   G 5 .   ? 11.381 12.683  11.107 1.00 16.67  ? 348 HOH   A O   1 
HETATM 2260 O  O   . HOH   G 5 .   ? 31.132 -2.061  15.664 1.00 45.54  ? 349 HOH   A O   1 
HETATM 2261 O  O   . HOH   G 5 .   ? 21.037 -4.159  14.177 1.00 18.10  ? 350 HOH   A O   1 
HETATM 2262 O  O   . HOH   G 5 .   ? 13.837 3.988   23.487 1.00 13.75  ? 351 HOH   A O   1 
HETATM 2263 O  O   . HOH   G 5 .   ? 31.686 19.961  11.760 1.00 22.56  ? 352 HOH   A O   1 
HETATM 2264 O  O   . HOH   G 5 .   ? 16.671 3.863   23.647 1.00 18.42  ? 353 HOH   A O   1 
HETATM 2265 O  O   . HOH   G 5 .   ? 10.797 5.468   3.312  1.00 26.16  ? 354 HOH   A O   1 
HETATM 2266 O  O   . HOH   G 5 .   ? 23.476 -6.487  12.033 1.00 31.78  ? 355 HOH   A O   1 
HETATM 2267 O  O   . HOH   G 5 .   ? 5.577  5.373   32.644 1.00 23.41  ? 356 HOH   A O   1 
HETATM 2268 O  O   . HOH   G 5 .   ? 23.628 3.739   -2.352 1.00 48.99  ? 357 HOH   A O   1 
HETATM 2269 O  O   . HOH   G 5 .   ? 1.463  5.286   27.112 1.00 29.02  ? 358 HOH   A O   1 
HETATM 2270 O  O   . HOH   G 5 .   ? 20.775 -1.119  3.002  1.00 32.89  ? 359 HOH   A O   1 
HETATM 2271 O  O   . HOH   G 5 .   ? 34.093 -2.349  13.532 1.00 33.83  ? 360 HOH   A O   1 
HETATM 2272 O  O   . HOH   G 5 .   ? 18.461 21.933  9.550  1.00 20.45  ? 361 HOH   A O   1 
HETATM 2273 O  O   . HOH   G 5 .   ? 3.886  12.954  17.616 1.00 27.42  ? 362 HOH   A O   1 
HETATM 2274 O  O   . HOH   G 5 .   ? 36.559 18.134  14.542 1.00 32.68  ? 363 HOH   A O   1 
HETATM 2275 O  O   . HOH   G 5 .   ? 29.002 3.367   12.675 1.00 16.51  ? 364 HOH   A O   1 
HETATM 2276 O  O   . HOH   G 5 .   ? 20.256 17.886  24.111 1.00 35.52  ? 365 HOH   A O   1 
HETATM 2277 O  O   . HOH   G 5 .   ? 9.620  4.024   33.460 1.00 14.78  ? 366 HOH   A O   1 
HETATM 2278 O  O   . HOH   G 5 .   ? 3.300  -0.499  2.910  1.00 45.76  ? 367 HOH   A O   1 
HETATM 2279 O  O   . HOH   G 5 .   ? 27.013 -1.286  8.854  1.00 26.87  ? 368 HOH   A O   1 
HETATM 2280 O  O   . HOH   G 5 .   ? 12.154 11.160  29.580 1.00 20.55  ? 369 HOH   A O   1 
HETATM 2281 O  O   . HOH   G 5 .   ? 21.662 4.824   24.717 1.00 41.53  ? 370 HOH   A O   1 
HETATM 2282 O  O   . HOH   G 5 .   ? 36.829 2.475   10.037 1.00 38.59  ? 371 HOH   A O   1 
HETATM 2283 O  O   . HOH   G 5 .   ? 17.174 -3.455  27.799 1.00 35.58  ? 372 HOH   A O   1 
HETATM 2284 O  O   . HOH   G 5 .   ? 29.457 11.928  21.332 1.00 34.14  ? 373 HOH   A O   1 
HETATM 2285 O  O   . HOH   G 5 .   ? 9.325  19.282  26.793 1.00 40.66  ? 374 HOH   A O   1 
HETATM 2286 O  O   . HOH   G 5 .   ? 35.334 10.777  12.348 1.00 49.24  ? 375 HOH   A O   1 
HETATM 2287 O  O   . HOH   G 5 .   ? 13.306 11.392  9.169  1.00 14.49  ? 376 HOH   A O   1 
HETATM 2288 O  O   . HOH   G 5 .   ? 6.726  -6.966  23.830 1.00 26.79  ? 377 HOH   A O   1 
HETATM 2289 O  O   . HOH   G 5 .   ? 7.212  26.481  14.317 1.00 37.05  ? 378 HOH   A O   1 
HETATM 2290 O  O   . HOH   G 5 .   ? 17.641 20.031  17.024 1.00 17.91  ? 379 HOH   A O   1 
HETATM 2291 O  O   . HOH   G 5 .   ? 28.942 15.815  4.315  1.00 34.24  ? 380 HOH   A O   1 
HETATM 2292 O  O   . HOH   G 5 .   ? 30.634 2.968   14.886 1.00 23.82  ? 381 HOH   A O   1 
HETATM 2293 O  O   . HOH   G 5 .   ? 5.085  8.377   2.249  1.00 34.44  ? 382 HOH   A O   1 
HETATM 2294 O  O   . HOH   G 5 .   ? 15.949 23.926  14.888 1.00 41.94  ? 383 HOH   A O   1 
HETATM 2295 O  O   . HOH   G 5 .   ? 20.896 -2.550  16.865 1.00 16.74  ? 384 HOH   A O   1 
HETATM 2296 O  O   . HOH   G 5 .   ? 9.268  3.157   2.844  1.00 33.82  ? 385 HOH   A O   1 
HETATM 2297 O  O   . HOH   G 5 .   ? 32.863 16.557  9.251  1.00 36.22  ? 386 HOH   A O   1 
HETATM 2298 O  O   . HOH   G 5 .   ? 16.379 9.374   -1.648 1.00 23.60  ? 387 HOH   A O   1 
HETATM 2299 O  O   . HOH   G 5 .   ? 16.576 21.249  19.218 1.00 25.27  ? 388 HOH   A O   1 
HETATM 2300 O  O   . HOH   G 5 .   ? 30.467 4.579   5.789  1.00 24.51  ? 389 HOH   A O   1 
HETATM 2301 O  O   . HOH   G 5 .   ? 22.982 -0.657  5.340  1.00 22.19  ? 390 HOH   A O   1 
HETATM 2302 O  O   . HOH   G 5 .   ? 14.029 25.025  26.050 1.00 36.33  ? 391 HOH   A O   1 
HETATM 2303 O  O   . HOH   G 5 .   ? 3.182  0.388   29.009 1.00 37.84  ? 392 HOH   A O   1 
HETATM 2304 O  O   . HOH   G 5 .   ? 30.241 -1.424  8.690  1.00 31.90  ? 393 HOH   A O   1 
HETATM 2305 O  O   . HOH   G 5 .   ? 2.403  16.327  19.322 1.00 26.36  ? 394 HOH   A O   1 
HETATM 2306 O  O   . HOH   G 5 .   ? 32.337 2.061   6.031  1.00 36.89  ? 395 HOH   A O   1 
HETATM 2307 O  O   . HOH   G 5 .   ? 4.149  0.075   24.033 1.00 21.20  ? 396 HOH   A O   1 
HETATM 2308 O  O   . HOH   G 5 .   ? 1.709  11.230  27.593 1.00 41.60  ? 397 HOH   A O   1 
HETATM 2309 O  O   . HOH   G 5 .   ? 11.764 -7.018  24.769 1.00 31.44  ? 398 HOH   A O   1 
HETATM 2310 O  O   . HOH   G 5 .   ? 27.385 -1.315  15.880 1.00 27.01  ? 399 HOH   A O   1 
HETATM 2311 O  O   . HOH   G 5 .   ? 17.819 10.676  26.113 1.00 22.87  ? 400 HOH   A O   1 
HETATM 2312 O  O   . HOH   G 5 .   ? 30.936 15.632  22.833 1.00 28.99  ? 401 HOH   A O   1 
HETATM 2313 O  O   . HOH   G 5 .   ? 25.306 17.857  4.574  1.00 35.01  ? 402 HOH   A O   1 
HETATM 2314 O  O   . HOH   G 5 .   ? 24.316 -3.456  16.139 1.00 35.48  ? 403 HOH   A O   1 
HETATM 2315 O  O   . HOH   G 5 .   ? 17.086 6.293   27.014 1.00 26.66  ? 404 HOH   A O   1 
HETATM 2316 O  O   . HOH   G 5 .   ? 6.056  -3.641  31.483 1.00 31.33  ? 405 HOH   A O   1 
HETATM 2317 O  O   . HOH   G 5 .   ? 2.077  14.688  16.834 1.00 35.78  ? 406 HOH   A O   1 
HETATM 2318 O  O   . HOH   G 5 .   ? 0.227  5.920   5.990  1.00 28.56  ? 407 HOH   A O   1 
HETATM 2319 O  O   . HOH   G 5 .   ? 19.537 2.914   19.364 1.00 20.70  ? 408 HOH   A O   1 
HETATM 2320 O  O   . HOH   G 5 .   ? 14.512 -2.477  17.947 1.00 20.31  ? 409 HOH   A O   1 
HETATM 2321 O  O   . HOH   G 5 .   ? 36.353 -0.328  12.498 1.00 34.73  ? 410 HOH   A O   1 
HETATM 2322 O  O   . HOH   G 5 .   ? 3.878  -3.963  5.972  1.00 30.58  ? 411 HOH   A O   1 
HETATM 2323 O  O   . HOH   G 5 .   ? 18.121 17.779  4.164  1.00 37.51  ? 412 HOH   A O   1 
HETATM 2324 O  O   . HOH   G 5 .   ? 25.453 19.736  21.690 1.00 28.36  ? 413 HOH   A O   1 
HETATM 2325 O  O   . HOH   G 5 .   ? 28.000 17.572  24.228 1.00 25.57  ? 414 HOH   A O   1 
HETATM 2326 O  O   . HOH   G 5 .   ? 3.143  7.593   24.477 1.00 22.15  ? 415 HOH   A O   1 
HETATM 2327 O  O   . HOH   G 5 .   ? 0.615  -1.291  9.145  1.00 43.53  ? 416 HOH   A O   1 
HETATM 2328 O  O   . HOH   G 5 .   ? 15.156 21.788  8.266  1.00 32.56  ? 417 HOH   A O   1 
HETATM 2329 O  O   . HOH   G 5 .   ? 32.095 8.787   7.620  1.00 24.55  ? 418 HOH   A O   1 
HETATM 2330 O  O   . HOH   G 5 .   ? 6.199  18.140  24.858 1.00 60.51  ? 419 HOH   A O   1 
HETATM 2331 O  O   . HOH   G 5 .   ? 35.999 15.200  11.020 1.00 42.87  ? 420 HOH   A O   1 
HETATM 2332 O  O   . HOH   G 5 .   ? 15.272 -4.970  0.430  1.00 42.50  ? 421 HOH   A O   1 
HETATM 2333 O  O   . HOH   G 5 .   ? 22.512 19.472  19.616 1.00 37.61  ? 422 HOH   A O   1 
HETATM 2334 O  O   . HOH   G 5 .   ? 34.134 18.663  10.807 1.00 29.04  ? 423 HOH   A O   1 
HETATM 2335 O  O   . HOH   G 5 .   ? 17.615 0.762   20.222 1.00 19.60  ? 424 HOH   A O   1 
HETATM 2336 O  O   . HOH   G 5 .   ? 15.413 15.207  3.473  1.00 31.64  ? 425 HOH   A O   1 
HETATM 2337 O  O   . HOH   G 5 .   ? 5.278  26.665  20.005 1.00 26.24  ? 426 HOH   A O   1 
HETATM 2338 O  O   . HOH   G 5 .   ? 7.365  13.824  4.714  1.00 23.98  ? 427 HOH   A O   1 
HETATM 2339 O  O   . HOH   G 5 .   ? 14.549 24.344  17.947 1.00 33.95  ? 428 HOH   A O   1 
HETATM 2340 O  O   . HOH   G 5 .   ? 8.344  6.611   33.772 1.00 21.21  ? 429 HOH   A O   1 
HETATM 2341 O  O   . HOH   G 5 .   ? 34.069 5.080   16.662 1.00 34.75  ? 430 HOH   A O   1 
HETATM 2342 O  O   . HOH   G 5 .   ? 19.101 16.873  26.352 1.00 46.23  ? 431 HOH   A O   1 
HETATM 2343 O  O   . HOH   G 5 .   ? 19.519 -0.406  33.296 1.00 36.79  ? 432 HOH   A O   1 
HETATM 2344 O  O   . HOH   G 5 .   ? 8.645  -6.531  9.680  1.00 31.82  ? 433 HOH   A O   1 
HETATM 2345 O  O   . HOH   G 5 .   ? 0.596  -1.212  16.709 1.00 22.29  ? 434 HOH   A O   1 
HETATM 2346 O  O   . HOH   G 5 .   ? 19.823 13.269  2.181  1.00 33.04  ? 435 HOH   A O   1 
HETATM 2347 O  O   . HOH   G 5 .   ? 6.002  2.997   6.812  1.00 34.72  ? 436 HOH   A O   1 
HETATM 2348 O  O   . HOH   G 5 .   ? 23.346 19.150  6.338  1.00 21.34  ? 437 HOH   A O   1 
HETATM 2349 O  O   . HOH   G 5 .   ? 36.661 16.143  16.690 1.00 41.02  ? 438 HOH   A O   1 
HETATM 2350 O  O   . HOH   G 5 .   ? 3.425  -0.450  21.286 1.00 31.79  ? 439 HOH   A O   1 
HETATM 2351 O  O   . HOH   G 5 .   ? 25.062 10.662  23.000 1.00 39.33  ? 440 HOH   A O   1 
HETATM 2352 O  O   . HOH   G 5 .   ? 17.261 -2.374  19.608 1.00 21.57  ? 441 HOH   A O   1 
HETATM 2353 O  O   . HOH   G 5 .   ? 6.384  24.086  10.584 1.00 38.68  ? 442 HOH   A O   1 
HETATM 2354 O  O   . HOH   G 5 .   ? 22.797 3.390   20.816 1.00 22.49  ? 443 HOH   A O   1 
HETATM 2355 O  O   . HOH   G 5 .   ? 21.081 9.986   21.935 1.00 17.52  ? 444 HOH   A O   1 
HETATM 2356 O  O   . HOH   G 5 .   ? 17.879 24.425  10.578 1.00 37.38  ? 445 HOH   A O   1 
HETATM 2357 O  O   . HOH   G 5 .   ? 16.912 -4.073  2.810  1.00 28.17  ? 446 HOH   A O   1 
HETATM 2358 O  O   . HOH   G 5 .   ? 19.409 21.580  6.916  1.00 44.35  ? 447 HOH   A O   1 
HETATM 2359 O  O   . HOH   G 5 .   ? 17.113 -5.726  12.218 1.00 38.41  ? 448 HOH   A O   1 
HETATM 2360 O  O   . HOH   G 5 .   ? 31.155 19.513  8.967  1.00 42.19  ? 449 HOH   A O   1 
HETATM 2361 O  O   . HOH   G 5 .   ? 21.042 -4.781  11.454 1.00 33.27  ? 450 HOH   A O   1 
HETATM 2362 O  O   . HOH   G 5 .   ? 35.567 11.788  17.305 1.00 46.99  ? 451 HOH   A O   1 
HETATM 2363 O  O   . HOH   G 5 .   ? 23.436 8.219   21.748 1.00 26.72  ? 452 HOH   A O   1 
HETATM 2364 O  O   . HOH   G 5 .   ? 19.707 9.308   -0.908 1.00 30.39  ? 453 HOH   A O   1 
HETATM 2365 O  O   . HOH   G 5 .   ? 7.593  -4.750  2.859  1.00 40.84  ? 454 HOH   A O   1 
HETATM 2366 O  O   . HOH   G 5 .   ? 34.228 7.758   16.725 1.00 32.94  ? 455 HOH   A O   1 
HETATM 2367 O  O   . HOH   G 5 .   ? 22.983 16.784  23.914 1.00 50.41  ? 456 HOH   A O   1 
HETATM 2368 O  O   . HOH   G 5 .   ? 7.915  11.687  3.602  1.00 38.16  ? 457 HOH   A O   1 
HETATM 2369 O  O   . HOH   G 5 .   ? 8.153  11.368  31.529 1.00 36.97  ? 458 HOH   A O   1 
HETATM 2370 O  O   . HOH   G 5 .   ? 25.526 -1.072  16.637 1.00 37.41  ? 459 HOH   A O   1 
HETATM 2371 O  O   . HOH   G 5 .   ? 9.844  -4.153  -0.526 1.00 51.49  ? 460 HOH   A O   1 
HETATM 2372 O  O   . HOH   G 5 .   ? 19.144 -3.436  33.702 1.00 48.24  ? 461 HOH   A O   1 
HETATM 2373 O  O   . HOH   G 5 .   ? 28.239 0.346   4.878  1.00 53.01  ? 462 HOH   A O   1 
HETATM 2374 O  O   . HOH   G 5 .   ? 31.976 7.023   5.433  1.00 32.42  ? 463 HOH   A O   1 
HETATM 2375 O  O   . HOH   G 5 .   ? 33.383 -4.212  5.705  1.00 43.68  ? 464 HOH   A O   1 
HETATM 2376 O  O   . HOH   G 5 .   ? 2.749  -0.338  26.455 1.00 34.97  ? 465 HOH   A O   1 
HETATM 2377 O  O   . HOH   G 5 .   ? 6.560  3.244   3.202  1.00 41.39  ? 466 HOH   A O   1 
HETATM 2378 O  O   . HOH   G 5 .   ? 16.854 -5.073  34.248 1.00 33.09  ? 467 HOH   A O   1 
HETATM 2379 O  O   . HOH   G 5 .   ? 18.658 3.243   26.066 1.00 41.88  ? 468 HOH   A O   1 
HETATM 2380 O  O   . HOH   G 5 .   ? 8.781  11.121  1.358  1.00 50.40  ? 469 HOH   A O   1 
HETATM 2381 O  O   . HOH   G 5 .   ? 11.796 24.406  14.460 1.00 40.60  ? 470 HOH   A O   1 
HETATM 2382 O  O   . HOH   G 5 .   ? 29.880 0.670   16.564 1.00 36.06  ? 471 HOH   A O   1 
HETATM 2383 O  O   . HOH   G 5 .   ? 18.623 2.065   22.656 1.00 34.57  ? 472 HOH   A O   1 
HETATM 2384 O  O   . HOH   G 5 .   ? 23.862 1.016   19.814 1.00 35.94  ? 473 HOH   A O   1 
HETATM 2385 O  O   . HOH   G 5 .   ? 0.190  0.029   23.113 1.00 29.84  ? 474 HOH   A O   1 
HETATM 2386 O  O   . HOH   G 5 .   ? 30.364 7.055   17.799 1.00 34.75  ? 475 HOH   A O   1 
HETATM 2387 O  O   . HOH   G 5 .   ? 21.387 2.916   23.127 1.00 36.36  ? 476 HOH   A O   1 
HETATM 2388 O  O   . HOH   G 5 .   ? 12.400 -5.022  33.104 1.00 32.02  ? 477 HOH   A O   1 
HETATM 2389 O  O   . HOH   G 5 .   ? 31.379 4.548   17.010 1.00 26.75  ? 478 HOH   A O   1 
HETATM 2390 O  O   . HOH   G 5 .   ? 4.913  28.560  18.119 1.00 36.09  ? 479 HOH   A O   1 
HETATM 2391 O  O   . HOH   G 5 .   ? 37.850 -4.610  6.653  1.00 28.82  ? 480 HOH   A O   1 
HETATM 2392 O  O   . HOH   G 5 .   ? 2.570  -1.655  22.769 1.00 33.95  ? 481 HOH   A O   1 
HETATM 2393 O  O   . HOH   G 5 .   ? 21.533 -1.039  18.938 1.00 33.47  ? 482 HOH   A O   1 
HETATM 2394 O  O   . HOH   G 5 .   ? 2.477  -5.206  22.487 1.00 43.27  ? 483 HOH   A O   1 
HETATM 2395 O  O   . HOH   G 5 .   ? 0.945  16.085  21.968 1.00 40.58  ? 484 HOH   A O   1 
HETATM 2396 O  O   . HOH   G 5 .   ? 9.796  25.925  13.633 1.00 45.92  ? 485 HOH   A O   1 
HETATM 2397 O  O   . HOH   G 5 .   ? 28.999 1.263   19.070 1.00 50.58  ? 486 HOH   A O   1 
HETATM 2398 O  O   . HOH   G 5 .   ? 4.142  -6.962  23.423 1.00 48.55  ? 487 HOH   A O   1 
HETATM 2399 O  O   . HOH   G 5 .   ? 26.580 0.468   20.079 1.00 51.98  ? 488 HOH   A O   1 
HETATM 2400 O  O   . HOH   H 5 .   ? 17.815 -33.330 24.137 1.00 47.10  ? 301 HOH   C O   1 
HETATM 2401 O  O   . HOH   H 5 .   ? 31.180 -23.921 -1.272 1.00 25.61  ? 302 HOH   C O   1 
HETATM 2402 O  O   . HOH   H 5 .   ? 29.453 -25.817 -1.160 1.00 26.59  ? 303 HOH   C O   1 
HETATM 2403 O  O   . HOH   H 5 .   ? 39.059 -18.693 21.559 1.00 28.66  ? 304 HOH   C O   1 
HETATM 2404 O  O   . HOH   H 5 .   ? 16.481 -17.083 11.052 1.00 41.37  ? 305 HOH   C O   1 
HETATM 2405 O  O   . HOH   H 5 .   ? 14.857 -18.665 32.067 1.00 38.00  ? 306 HOH   C O   1 
HETATM 2406 O  O   . HOH   H 5 .   ? 38.436 -7.397  6.913  1.00 21.98  ? 307 HOH   C O   1 
HETATM 2407 O  O   . HOH   H 5 .   ? 18.035 -5.977  24.086 1.00 26.98  ? 308 HOH   C O   1 
HETATM 2408 O  O   . HOH   H 5 .   ? 19.897 -4.123  20.248 1.00 23.60  ? 309 HOH   C O   1 
HETATM 2409 O  O   . HOH   H 5 .   ? 24.760 -5.933  15.188 1.00 31.61  ? 310 HOH   C O   1 
HETATM 2410 O  O   . HOH   H 5 .   ? 36.384 -2.558  10.931 1.00 30.25  ? 311 HOH   C O   1 
HETATM 2411 O  O   . HOH   H 5 .   ? 30.983 -18.179 26.892 1.00 19.10  ? 312 HOH   C O   1 
HETATM 2412 O  O   . HOH   H 5 .   ? 24.774 -9.694  26.993 1.00 43.18  ? 313 HOH   C O   1 
HETATM 2413 O  O   . HOH   H 5 .   ? 23.072 -5.938  21.166 1.00 21.06  ? 314 HOH   C O   1 
HETATM 2414 O  O   . HOH   H 5 .   ? 20.859 -18.770 12.862 1.00 15.68  ? 315 HOH   C O   1 
HETATM 2415 O  O   . HOH   H 5 .   ? 16.497 -15.826 8.750  1.00 48.77  ? 316 HOH   C O   1 
HETATM 2416 O  O   . HOH   H 5 .   ? 21.963 -26.232 34.352 1.00 27.66  ? 317 HOH   C O   1 
HETATM 2417 O  O   . HOH   H 5 .   ? 19.382 -32.239 19.826 1.00 41.51  ? 318 HOH   C O   1 
HETATM 2418 O  O   . HOH   H 5 .   ? 37.430 -31.974 10.919 1.00 25.06  ? 319 HOH   C O   1 
HETATM 2419 O  O   . HOH   H 5 .   ? 18.042 -27.554 16.576 1.00 20.03  ? 320 HOH   C O   1 
HETATM 2420 O  O   . HOH   H 5 .   ? 35.222 -32.815 3.299  1.00 35.10  ? 321 HOH   C O   1 
HETATM 2421 O  O   . HOH   H 5 .   ? 14.856 -23.946 12.389 1.00 33.78  ? 322 HOH   C O   1 
HETATM 2422 O  O   . HOH   H 5 .   ? 10.354 -17.551 18.384 1.00 29.98  ? 323 HOH   C O   1 
HETATM 2423 O  O   . HOH   H 5 .   ? 36.257 -17.711 11.617 1.00 28.77  ? 324 HOH   C O   1 
HETATM 2424 O  O   . HOH   H 5 .   ? 36.417 -26.272 34.281 1.00 32.80  ? 325 HOH   C O   1 
HETATM 2425 O  O   . HOH   H 5 .   ? 37.342 -10.530 4.842  1.00 37.72  ? 326 HOH   C O   1 
HETATM 2426 O  O   . HOH   H 5 .   ? 42.771 -11.346 11.166 1.00 27.21  ? 327 HOH   C O   1 
HETATM 2427 O  O   . HOH   H 5 .   ? 17.638 -24.144 8.651  1.00 39.61  ? 328 HOH   C O   1 
HETATM 2428 O  O   . HOH   H 5 .   ? 25.702 -35.704 2.978  1.00 45.12  ? 329 HOH   C O   1 
HETATM 2429 O  O   . HOH   H 5 .   ? 26.693 -5.523  9.943  1.00 23.79  ? 330 HOH   C O   1 
HETATM 2430 O  O   . HOH   H 5 .   ? 7.275  -30.252 22.008 1.00 28.62  ? 331 HOH   C O   1 
HETATM 2431 O  O   . HOH   H 5 .   ? 18.750 -8.816  13.784 1.00 27.11  ? 332 HOH   C O   1 
HETATM 2432 O  O   . HOH   H 5 .   ? 22.002 -28.747 4.840  1.00 27.33  ? 333 HOH   C O   1 
HETATM 2433 O  O   . HOH   H 5 .   ? 28.422 -5.229  18.596 1.00 42.15  ? 334 HOH   C O   1 
HETATM 2434 O  O   . HOH   H 5 .   ? 31.220 -21.516 28.436 1.00 18.75  ? 335 HOH   C O   1 
HETATM 2435 O  O   . HOH   H 5 .   ? 25.918 -37.825 24.350 1.00 33.00  ? 336 HOH   C O   1 
HETATM 2436 O  O   . HOH   H 5 .   ? 26.751 -15.223 30.858 1.00 29.98  ? 337 HOH   C O   1 
HETATM 2437 O  O   . HOH   H 5 .   ? 14.852 -28.892 25.671 1.00 41.66  ? 338 HOH   C O   1 
HETATM 2438 O  O   . HOH   H 5 .   ? 24.020 -8.140  9.475  1.00 25.10  ? 339 HOH   C O   1 
HETATM 2439 O  O   . HOH   H 5 .   ? 26.521 -31.278 14.882 1.00 22.11  ? 340 HOH   C O   1 
HETATM 2440 O  O   . HOH   H 5 .   ? 40.681 -27.321 15.154 1.00 14.04  ? 341 HOH   C O   1 
HETATM 2441 O  O   . HOH   H 5 .   ? 24.864 -15.756 7.344  1.00 19.99  ? 342 HOH   C O   1 
HETATM 2442 O  O   . HOH   H 5 .   ? 14.106 -24.262 29.353 1.00 34.74  ? 343 HOH   C O   1 
HETATM 2443 O  O   . HOH   H 5 .   ? 32.758 -23.721 29.182 1.00 18.78  ? 344 HOH   C O   1 
HETATM 2444 O  O   . HOH   H 5 .   ? 40.755 -25.309 7.095  1.00 39.03  ? 345 HOH   C O   1 
HETATM 2445 O  O   . HOH   H 5 .   ? 37.499 -18.801 28.168 1.00 25.50  ? 346 HOH   C O   1 
HETATM 2446 O  O   . HOH   H 5 .   ? 6.926  -9.258  22.719 1.00 41.33  ? 347 HOH   C O   1 
HETATM 2447 O  O   . HOH   H 5 .   ? 30.043 -15.305 19.635 1.00 16.61  ? 348 HOH   C O   1 
HETATM 2448 O  O   . HOH   H 5 .   ? 20.937 -25.703 13.907 1.00 21.95  ? 349 HOH   C O   1 
HETATM 2449 O  O   . HOH   H 5 .   ? 19.383 -27.750 28.275 1.00 20.09  ? 350 HOH   C O   1 
HETATM 2450 O  O   . HOH   H 5 .   ? 32.680 -5.282  18.319 1.00 47.33  ? 351 HOH   C O   1 
HETATM 2451 O  O   . HOH   H 5 .   ? 35.986 -28.531 2.975  1.00 40.09  ? 352 HOH   C O   1 
HETATM 2452 O  O   . HOH   H 5 .   ? 10.037 -8.875  24.034 1.00 31.19  ? 353 HOH   C O   1 
HETATM 2453 O  O   . HOH   H 5 .   ? 40.300 -29.680 11.878 1.00 25.77  ? 354 HOH   C O   1 
HETATM 2454 O  O   . HOH   H 5 .   ? 32.161 -10.499 13.750 1.00 20.02  ? 355 HOH   C O   1 
HETATM 2455 O  O   . HOH   H 5 .   ? 26.091 -25.304 8.798  1.00 14.76  ? 356 HOH   C O   1 
HETATM 2456 O  O   . HOH   H 5 .   ? 31.081 -33.000 0.864  1.00 40.21  ? 357 HOH   C O   1 
HETATM 2457 O  O   . HOH   H 5 .   ? 12.083 -24.292 21.780 1.00 18.75  ? 358 HOH   C O   1 
HETATM 2458 O  O   . HOH   H 5 .   ? 35.326 -13.177 8.668  1.00 19.53  ? 359 HOH   C O   1 
HETATM 2459 O  O   . HOH   H 5 .   ? 9.356  -8.097  21.409 1.00 28.43  ? 360 HOH   C O   1 
HETATM 2460 O  O   . HOH   H 5 .   ? 41.771 -13.733 9.952  1.00 37.31  ? 361 HOH   C O   1 
HETATM 2461 O  O   . HOH   H 5 .   ? 13.474 -11.232 28.619 1.00 38.26  ? 362 HOH   C O   1 
HETATM 2462 O  O   . HOH   H 5 .   ? 31.628 -35.371 31.798 1.00 40.95  ? 363 HOH   C O   1 
HETATM 2463 O  O   . HOH   H 5 .   ? 36.411 -21.294 6.836  1.00 26.53  ? 364 HOH   C O   1 
HETATM 2464 O  O   . HOH   H 5 .   ? 31.352 -6.139  5.654  1.00 38.81  ? 365 HOH   C O   1 
HETATM 2465 O  O   . HOH   H 5 .   ? 36.493 -32.626 25.047 1.00 42.79  ? 366 HOH   C O   1 
HETATM 2466 O  O   . HOH   H 5 .   ? 23.064 -8.525  14.065 1.00 16.85  ? 367 HOH   C O   1 
HETATM 2467 O  O   . HOH   H 5 .   ? 10.730 -16.942 12.526 1.00 34.61  ? 368 HOH   C O   1 
HETATM 2468 O  O   . HOH   H 5 .   ? 10.599 -16.963 15.093 1.00 33.22  ? 369 HOH   C O   1 
HETATM 2469 O  O   . HOH   H 5 .   ? 20.209 -32.042 15.350 1.00 44.08  ? 370 HOH   C O   1 
HETATM 2470 O  O   . HOH   H 5 .   ? 13.316 -29.491 19.213 1.00 31.31  ? 371 HOH   C O   1 
HETATM 2471 O  O   . HOH   H 5 .   ? 34.207 -33.755 24.067 1.00 39.65  ? 372 HOH   C O   1 
HETATM 2472 O  O   . HOH   H 5 .   ? 23.266 -25.422 8.975  1.00 21.19  ? 373 HOH   C O   1 
HETATM 2473 O  O   . HOH   H 5 .   ? 23.790 -33.633 29.160 1.00 29.88  ? 374 HOH   C O   1 
HETATM 2474 O  O   . HOH   H 5 .   ? 3.384  -12.823 20.347 1.00 43.75  ? 375 HOH   C O   1 
HETATM 2475 O  O   . HOH   H 5 .   ? 27.261 -35.752 20.873 1.00 26.57  ? 376 HOH   C O   1 
HETATM 2476 O  O   . HOH   H 5 .   ? 33.138 -9.848  11.078 1.00 16.17  ? 377 HOH   C O   1 
HETATM 2477 O  O   . HOH   H 5 .   ? 35.059 -35.005 18.126 1.00 34.53  ? 378 HOH   C O   1 
HETATM 2478 O  O   . HOH   H 5 .   ? 29.876 -13.131 12.956 1.00 16.40  ? 379 HOH   C O   1 
HETATM 2479 O  O   . HOH   H 5 .   ? 30.221 -15.899 30.528 1.00 30.39  ? 380 HOH   C O   1 
HETATM 2480 O  O   . HOH   H 5 .   ? 5.826  -12.555 23.250 1.00 51.43  ? 381 HOH   C O   1 
HETATM 2481 O  O   . HOH   H 5 .   ? 23.060 -28.206 12.696 1.00 22.72  ? 382 HOH   C O   1 
HETATM 2482 O  O   . HOH   H 5 .   ? 24.530 -13.861 5.429  1.00 41.41  ? 383 HOH   C O   1 
HETATM 2483 O  O   . HOH   H 5 .   ? 11.064 -6.523  13.251 1.00 26.75  ? 384 HOH   C O   1 
HETATM 2484 O  O   . HOH   H 5 .   ? 42.044 -12.634 20.603 1.00 40.57  ? 385 HOH   C O   1 
HETATM 2485 O  O   . HOH   H 5 .   ? 4.806  -25.156 25.554 1.00 45.40  ? 386 HOH   C O   1 
HETATM 2486 O  O   . HOH   H 5 .   ? 3.945  -8.384  14.714 1.00 30.25  ? 387 HOH   C O   1 
HETATM 2487 O  O   . HOH   H 5 .   ? 31.401 -12.199 10.638 1.00 16.72  ? 388 HOH   C O   1 
HETATM 2488 O  O   . HOH   H 5 .   ? 37.967 -31.478 25.767 1.00 28.02  ? 389 HOH   C O   1 
HETATM 2489 O  O   . HOH   H 5 .   ? 10.162 -24.841 19.918 1.00 22.36  ? 390 HOH   C O   1 
HETATM 2490 O  O   . HOH   H 5 .   ? 35.778 -24.701 24.651 1.00 18.18  ? 391 HOH   C O   1 
HETATM 2491 O  O   . HOH   H 5 .   ? 22.329 -23.789 6.127  1.00 34.64  ? 392 HOH   C O   1 
HETATM 2492 O  O   . HOH   H 5 .   ? 22.992 -33.400 5.465  1.00 38.27  ? 393 HOH   C O   1 
HETATM 2493 O  O   . HOH   H 5 .   ? 11.724 -22.625 28.786 1.00 27.74  ? 394 HOH   C O   1 
HETATM 2494 O  O   . HOH   H 5 .   ? 26.948 -12.085 27.652 1.00 26.21  ? 395 HOH   C O   1 
HETATM 2495 O  O   . HOH   H 5 .   ? 39.073 -14.560 13.527 1.00 41.33  ? 396 HOH   C O   1 
HETATM 2496 O  O   . HOH   H 5 .   ? 22.660 -13.771 29.827 1.00 36.15  ? 397 HOH   C O   1 
HETATM 2497 O  O   . HOH   H 5 .   ? 37.098 -29.325 10.087 1.00 22.42  ? 398 HOH   C O   1 
HETATM 2498 O  O   . HOH   H 5 .   ? 28.320 -16.357 22.082 1.00 14.52  ? 399 HOH   C O   1 
HETATM 2499 O  O   . HOH   H 5 .   ? 14.741 -18.534 10.472 1.00 34.85  ? 400 HOH   C O   1 
HETATM 2500 O  O   . HOH   H 5 .   ? 37.958 -20.319 4.896  1.00 38.65  ? 401 HOH   C O   1 
HETATM 2501 O  O   . HOH   H 5 .   ? 28.992 -36.366 7.844  1.00 21.37  ? 402 HOH   C O   1 
HETATM 2502 O  O   . HOH   H 5 .   ? 6.036  -16.891 22.287 1.00 49.94  ? 403 HOH   C O   1 
HETATM 2503 O  O   . HOH   H 5 .   ? 45.503 -14.756 4.654  1.00 35.03  ? 404 HOH   C O   1 
HETATM 2504 O  O   . HOH   H 5 .   ? 36.821 -16.033 12.556 1.00 35.47  ? 405 HOH   C O   1 
HETATM 2505 O  O   . HOH   H 5 .   ? 30.456 -18.107 8.391  1.00 26.80  ? 406 HOH   C O   1 
HETATM 2506 O  O   . HOH   H 5 .   ? 11.003 -12.012 9.075  1.00 34.15  ? 407 HOH   C O   1 
HETATM 2507 O  O   . HOH   H 5 .   ? 43.489 -25.756 23.679 1.00 22.91  ? 408 HOH   C O   1 
HETATM 2508 O  O   . HOH   H 5 .   ? 30.340 -10.450 27.711 1.00 43.82  ? 409 HOH   C O   1 
HETATM 2509 O  O   . HOH   H 5 .   ? 9.441  -27.353 19.044 1.00 36.34  ? 410 HOH   C O   1 
HETATM 2510 O  O   . HOH   H 5 .   ? 31.635 -13.540 4.337  1.00 33.76  ? 411 HOH   C O   1 
HETATM 2511 O  O   . HOH   H 5 .   ? 38.504 -25.999 28.333 1.00 32.71  ? 412 HOH   C O   1 
HETATM 2512 O  O   . HOH   H 5 .   ? 39.070 -16.592 3.722  1.00 48.45  ? 413 HOH   C O   1 
HETATM 2513 O  O   . HOH   H 5 .   ? 32.425 -34.553 24.844 1.00 33.57  ? 414 HOH   C O   1 
HETATM 2514 O  O   . HOH   H 5 .   ? 11.123 -21.732 13.669 1.00 42.89  ? 415 HOH   C O   1 
HETATM 2515 O  O   . HOH   H 5 .   ? 34.579 -13.433 25.508 1.00 20.51  ? 416 HOH   C O   1 
HETATM 2516 O  O   . HOH   H 5 .   ? 8.877  -13.401 10.853 1.00 24.36  ? 417 HOH   C O   1 
HETATM 2517 O  O   . HOH   H 5 .   ? 42.361 -12.125 13.987 1.00 37.73  ? 418 HOH   C O   1 
HETATM 2518 O  O   . HOH   H 5 .   ? 20.580 -23.704 34.865 1.00 29.31  ? 419 HOH   C O   1 
HETATM 2519 O  O   . HOH   H 5 .   ? 10.469 -30.899 25.272 1.00 32.17  ? 420 HOH   C O   1 
HETATM 2520 O  O   . HOH   H 5 .   ? 26.786 -6.031  22.070 1.00 29.77  ? 421 HOH   C O   1 
HETATM 2521 O  O   . HOH   H 5 .   ? 39.060 -13.025 25.787 1.00 27.45  ? 422 HOH   C O   1 
HETATM 2522 O  O   . HOH   H 5 .   ? 10.356 -17.032 33.448 1.00 49.15  ? 423 HOH   C O   1 
HETATM 2523 O  O   . HOH   H 5 .   ? 21.809 -18.913 5.957  1.00 28.81  ? 424 HOH   C O   1 
HETATM 2524 O  O   . HOH   H 5 .   ? 26.253 -31.076 30.842 1.00 19.64  ? 425 HOH   C O   1 
HETATM 2525 O  O   . HOH   H 5 .   ? 4.322  -10.493 19.586 1.00 37.16  ? 426 HOH   C O   1 
HETATM 2526 O  O   . HOH   H 5 .   ? 4.859  -28.062 23.349 1.00 36.83  ? 427 HOH   C O   1 
HETATM 2527 O  O   . HOH   H 5 .   ? 37.968 -23.603 4.386  1.00 47.00  ? 428 HOH   C O   1 
HETATM 2528 O  O   . HOH   H 5 .   ? 35.298 -13.784 5.963  1.00 36.67  ? 429 HOH   C O   1 
HETATM 2529 O  O   . HOH   H 5 .   ? 9.910  -18.488 26.759 1.00 31.29  ? 430 HOH   C O   1 
HETATM 2530 O  O   . HOH   H 5 .   ? 35.106 -4.136  17.629 1.00 29.44  ? 431 HOH   C O   1 
HETATM 2531 O  O   . HOH   H 5 .   ? 35.855 -28.647 7.777  1.00 20.79  ? 432 HOH   C O   1 
HETATM 2532 O  O   . HOH   H 5 .   ? 33.226 -30.395 31.706 1.00 21.00  ? 433 HOH   C O   1 
HETATM 2533 O  O   . HOH   H 5 .   ? 20.489 -32.323 22.334 1.00 29.54  ? 434 HOH   C O   1 
HETATM 2534 O  O   . HOH   H 5 .   ? 34.626 -23.242 -0.841 1.00 42.40  ? 435 HOH   C O   1 
HETATM 2535 O  O   . HOH   H 5 .   ? 37.843 -13.807 10.130 1.00 32.50  ? 436 HOH   C O   1 
HETATM 2536 O  O   . HOH   H 5 .   ? 4.161  -12.852 17.297 1.00 46.45  ? 437 HOH   C O   1 
HETATM 2537 O  O   . HOH   H 5 .   ? 40.156 -29.996 14.573 1.00 19.14  ? 438 HOH   C O   1 
HETATM 2538 O  O   . HOH   H 5 .   ? 32.918 -14.380 9.374  1.00 16.31  ? 439 HOH   C O   1 
HETATM 2539 O  O   . HOH   H 5 .   ? 23.885 -3.325  18.829 1.00 45.02  ? 440 HOH   C O   1 
HETATM 2540 O  O   . HOH   H 5 .   ? 6.657  -22.982 18.501 1.00 33.23  ? 441 HOH   C O   1 
HETATM 2541 O  O   . HOH   H 5 .   ? 6.617  -17.036 19.073 1.00 54.32  ? 442 HOH   C O   1 
HETATM 2542 O  O   . HOH   H 5 .   ? 41.901 -12.380 18.056 1.00 26.20  ? 443 HOH   C O   1 
HETATM 2543 O  O   . HOH   H 5 .   ? 17.296 -25.333 12.762 1.00 26.87  ? 444 HOH   C O   1 
HETATM 2544 O  O   . HOH   H 5 .   ? 18.775 -8.283  25.580 1.00 21.78  ? 445 HOH   C O   1 
HETATM 2545 O  O   . HOH   H 5 .   ? 23.525 -31.146 13.368 1.00 34.98  ? 446 HOH   C O   1 
HETATM 2546 O  O   . HOH   H 5 .   ? 23.125 -7.664  25.795 1.00 47.59  ? 447 HOH   C O   1 
HETATM 2547 O  O   . HOH   H 5 .   ? 18.924 -19.137 10.872 1.00 20.92  ? 448 HOH   C O   1 
HETATM 2548 O  O   . HOH   H 5 .   ? 16.509 -20.606 11.590 1.00 28.47  ? 449 HOH   C O   1 
HETATM 2549 O  O   . HOH   H 5 .   ? 15.350 -29.860 17.904 1.00 47.54  ? 450 HOH   C O   1 
HETATM 2550 O  O   . HOH   H 5 .   ? 34.274 -15.627 27.254 1.00 35.29  ? 451 HOH   C O   1 
HETATM 2551 O  O   . HOH   H 5 .   ? 33.993 -36.130 8.807  1.00 45.23  ? 452 HOH   C O   1 
HETATM 2552 O  O   . HOH   H 5 .   ? 44.454 -20.804 27.544 1.00 39.46  ? 453 HOH   C O   1 
HETATM 2553 O  O   . HOH   H 5 .   ? 23.683 -17.572 33.378 1.00 22.92  ? 454 HOH   C O   1 
HETATM 2554 O  O   . HOH   H 5 .   ? 6.695  -20.122 18.228 1.00 34.93  ? 455 HOH   C O   1 
HETATM 2555 O  O   . HOH   H 5 .   ? 42.082 -31.563 15.685 1.00 33.59  ? 456 HOH   C O   1 
HETATM 2556 O  O   . HOH   H 5 .   ? 36.735 -24.641 27.281 1.00 33.27  ? 457 HOH   C O   1 
HETATM 2557 O  O   . HOH   H 5 .   ? 42.484 -19.814 29.325 1.00 48.11  ? 458 HOH   C O   1 
HETATM 2558 O  O   . HOH   H 5 .   ? 43.778 -25.520 26.127 1.00 37.42  ? 459 HOH   C O   1 
HETATM 2559 O  O   . HOH   H 5 .   ? 31.733 -15.775 7.073  1.00 31.89  ? 460 HOH   C O   1 
HETATM 2560 O  O   . HOH   H 5 .   ? 24.337 -16.612 3.284  1.00 43.59  ? 461 HOH   C O   1 
HETATM 2561 O  O   . HOH   H 5 .   ? 34.968 -30.268 33.850 1.00 45.55  ? 462 HOH   C O   1 
HETATM 2562 O  O   . HOH   H 5 .   ? 34.470 -31.921 29.550 1.00 25.32  ? 463 HOH   C O   1 
HETATM 2563 O  O   . HOH   H 5 .   ? 20.605 -19.796 36.154 1.00 36.02  ? 464 HOH   C O   1 
HETATM 2564 O  O   . HOH   H 5 .   ? 33.741 -20.516 -2.093 1.00 41.30  ? 465 HOH   C O   1 
HETATM 2565 O  O   . HOH   H 5 .   ? 21.343 -17.548 34.690 1.00 27.38  ? 466 HOH   C O   1 
HETATM 2566 O  O   . HOH   H 5 .   ? 26.222 -35.540 7.459  1.00 26.08  ? 467 HOH   C O   1 
HETATM 2567 O  O   . HOH   H 5 .   ? 24.115 -15.641 31.581 1.00 33.25  ? 468 HOH   C O   1 
HETATM 2568 O  O   . HOH   H 5 .   ? 8.946  -19.227 17.037 1.00 36.69  ? 469 HOH   C O   1 
HETATM 2569 O  O   . HOH   H 5 .   ? 10.399 -20.035 29.101 1.00 35.86  ? 470 HOH   C O   1 
HETATM 2570 O  O   . HOH   H 5 .   ? 41.465 -29.907 22.358 1.00 46.79  ? 471 HOH   C O   1 
HETATM 2571 O  O   . HOH   H 5 .   ? 26.346 -15.884 -0.947 1.00 70.04  ? 472 HOH   C O   1 
HETATM 2572 O  O   . HOH   H 5 .   ? 21.555 -26.944 10.276 1.00 34.50  ? 473 HOH   C O   1 
HETATM 2573 O  O   . HOH   H 5 .   ? 22.849 -16.721 5.422  1.00 40.25  ? 474 HOH   C O   1 
HETATM 2574 O  O   . HOH   H 5 .   ? 16.538 -27.597 14.243 1.00 35.17  ? 475 HOH   C O   1 
HETATM 2575 O  O   . HOH   H 5 .   ? 28.624 -12.610 30.388 1.00 55.11  ? 476 HOH   C O   1 
HETATM 2576 O  O   . HOH   H 5 .   ? 18.631 -26.148 10.314 1.00 47.50  ? 477 HOH   C O   1 
HETATM 2577 O  O   . HOH   H 5 .   ? 32.784 -19.392 29.091 1.00 34.20  ? 478 HOH   C O   1 
HETATM 2578 O  O   . HOH   H 5 .   ? 22.408 -7.951  11.370 1.00 32.21  ? 479 HOH   C O   1 
HETATM 2579 O  O   . HOH   H 5 .   ? 10.179 -21.409 16.335 1.00 34.76  ? 480 HOH   C O   1 
HETATM 2580 O  O   . HOH   H 5 .   ? 41.522 -15.359 13.461 1.00 36.38  ? 481 HOH   C O   1 
HETATM 2581 O  O   . HOH   H 5 .   ? 18.110 -17.963 8.498  1.00 40.33  ? 482 HOH   C O   1 
HETATM 2582 O  O   . HOH   H 5 .   ? 18.273 -16.495 38.418 1.00 36.37  ? 483 HOH   C O   1 
HETATM 2583 O  O   . HOH   H 5 .   ? 17.203 -28.991 28.934 1.00 43.36  ? 484 HOH   C O   1 
HETATM 2584 O  O   . HOH   H 5 .   ? 22.791 -12.008 6.023  1.00 38.58  ? 485 HOH   C O   1 
HETATM 2585 O  O   . HOH   H 5 .   ? 37.251 -23.133 -1.603 1.00 34.30  ? 486 HOH   C O   1 
HETATM 2586 O  O   . HOH   H 5 .   ? 9.186  -23.499 17.750 1.00 33.77  ? 487 HOH   C O   1 
HETATM 2587 O  O   . HOH   H 5 .   ? 42.630 -21.189 32.884 1.00 39.67  ? 488 HOH   C O   1 
HETATM 2588 O  O   . HOH   H 5 .   ? 35.570 -20.332 29.413 1.00 37.73  ? 489 HOH   C O   1 
HETATM 2589 O  O   . HOH   H 5 .   ? 35.412 -23.072 29.107 1.00 28.48  ? 490 HOH   C O   1 
HETATM 2590 O  O   . HOH   H 5 .   ? 3.187  -8.862  21.944 1.00 55.47  ? 491 HOH   C O   1 
HETATM 2591 O  O   . HOH   H 5 .   ? 39.376 -2.628  10.729 1.00 36.37  ? 492 HOH   C O   1 
HETATM 2592 O  O   . HOH   H 5 .   ? 25.289 -35.533 0.339  1.00 52.97  ? 493 HOH   C O   1 
HETATM 2593 O  O   . HOH   H 5 .   ? 34.658 -10.769 26.537 1.00 41.76  ? 494 HOH   C O   1 
HETATM 2594 O  O   . HOH   H 5 .   ? 19.867 -15.225 34.672 1.00 38.35  ? 495 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   ? 0.2204 0.2024 0.2106 0.0018  0.0020  -0.0087 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2239 0.2064 0.2198 0.0029  -0.0001 -0.0073 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2185 0.2014 0.2185 0.0055  -0.0011 -0.0034 7   SER   A C   
4    O O   . SER   A 1   ? 0.2234 0.2064 0.2211 0.0060  -0.0009 -0.0015 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2661 0.2519 0.2601 -0.0005 -0.0039 -0.0070 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2987 0.2874 0.2900 -0.0013 -0.0070 -0.0030 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1963 0.1792 0.2024 0.0069  -0.0015 -0.0025 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1889 0.1716 0.1992 0.0089  -0.0014 0.0002  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1809 0.1625 0.1962 0.0101  0.0005  -0.0005 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2048 0.1854 0.2200 0.0100  0.0020  -0.0024 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1656 0.1473 0.1856 0.0110  0.0007  0.0010  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1647 0.1457 0.1888 0.0114  0.0029  0.0002  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1566 0.1364 0.1828 0.0118  0.0053  0.0008  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1703 0.1494 0.1970 0.0123  0.0050  0.0024  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1743 0.1570 0.2037 0.0111  0.0014  0.0001  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1584 0.1376 0.1858 0.0111  0.0079  -0.0004 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1566 0.1345 0.1864 0.0105  0.0112  -0.0010 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1641 0.1426 0.2013 0.0109  0.0122  -0.0014 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1645 0.1443 0.2026 0.0104  0.0116  -0.0019 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1582 0.1362 0.1835 0.0082  0.0138  -0.0022 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1824 0.1614 0.2018 0.0078  0.0126  -0.0014 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1757 0.1519 0.2021 0.0064  0.0179  -0.0039 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1961 0.1774 0.2121 0.0054  0.0138  -0.0012 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1558 0.1332 0.1992 0.0118  0.0140  -0.0009 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1639 0.1423 0.2163 0.0124  0.0156  -0.0012 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1652 0.1408 0.2195 0.0109  0.0218  -0.0039 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1668 0.1396 0.2248 0.0116  0.0244  -0.0039 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1794 0.1597 0.2399 0.0149  0.0128  0.0023  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1759 0.1597 0.2335 0.0150  0.0070  0.0042  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1842 0.1712 0.2445 0.0142  0.0052  0.0037  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1928 0.1766 0.2446 0.0150  0.0039  0.0061  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1954 0.1852 0.2520 0.0132  0.0007  0.0044  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1978 0.1848 0.2459 0.0140  -0.0006 0.0070  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2064 0.1962 0.2566 0.0129  -0.0021 0.0058  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2325 0.2250 0.2784 0.0109  -0.0059 0.0056  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1744 0.1504 0.2258 0.0083  0.0243  -0.0064 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1805 0.1544 0.2316 0.0053  0.0306  -0.0099 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1921 0.1674 0.2492 0.0046  0.0333  -0.0114 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1857 0.1636 0.2412 0.0043  0.0306  -0.0104 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1982 0.1723 0.2378 0.0014  0.0312  -0.0112 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2061 0.1833 0.2410 0.0009  0.0273  -0.0092 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2195 0.1921 0.2572 -0.0032 0.0377  -0.0153 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2064 0.1800 0.2717 0.0046  0.0388  -0.0136 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1992 0.1746 0.2716 0.0039  0.0420  -0.0151 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1893 0.1689 0.2683 0.0070  0.0367  -0.0117 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1874 0.1681 0.2710 0.0104  0.0323  -0.0083 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1808 0.1628 0.2583 0.0051  0.0362  -0.0122 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1756 0.1614 0.2577 0.0069  0.0311  -0.0096 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1692 0.1549 0.2412 0.0059  0.0263  -0.0083 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1780 0.1657 0.2509 0.0052  0.0242  -0.0077 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1849 0.1735 0.2758 0.0059  0.0340  -0.0107 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2393 0.2295 0.3447 0.0083  0.0375  -0.0107 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2634 0.2577 0.3787 0.0112  0.0337  -0.0074 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.2279 0.2149 0.3349 0.0070  0.0448  -0.0141 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1652 0.1486 0.2288 0.0060  0.0249  -0.0078 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1643 0.1475 0.2197 0.0056  0.0211  -0.0065 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1612 0.1441 0.2145 0.0079  0.0170  -0.0048 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1666 0.1485 0.2210 0.0091  0.0175  -0.0045 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1775 0.1594 0.2243 0.0028  0.0233  -0.0070 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1947 0.1773 0.2409 -0.0006 0.0272  -0.0083 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2065 0.1901 0.2546 -0.0013 0.0266  -0.0074 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2189 0.2008 0.2620 -0.0038 0.0320  -0.0106 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2154 0.1998 0.2622 -0.0050 0.0302  -0.0082 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2317 0.2147 0.2725 -0.0079 0.0357  -0.0118 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2382 0.2225 0.2809 -0.0083 0.0347  -0.0102 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2837 0.2693 0.3240 -0.0128 0.0384  -0.0110 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1606 0.1440 0.2110 0.0081  0.0134  -0.0039 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1619 0.1450 0.2084 0.0093  0.0100  -0.0029 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1529 0.1344 0.1925 0.0087  0.0100  -0.0030 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1628 0.1438 0.2025 0.0079  0.0101  -0.0032 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1680 0.1536 0.2179 0.0095  0.0063  -0.0024 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1725 0.1578 0.2165 0.0094  0.0032  -0.0023 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1893 0.1781 0.2359 0.0082  -0.0005 -0.0020 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1957 0.1834 0.2364 0.0064  -0.0017 -0.0039 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2210 0.2090 0.2562 0.0058  -0.0036 -0.0039 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2330 0.2223 0.2674 0.0070  -0.0049 -0.0014 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2151 0.2015 0.2453 0.0037  -0.0035 -0.0067 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1517 0.1323 0.1863 0.0090  0.0102  -0.0024 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1599 0.1401 0.1897 0.0088  0.0103  -0.0017 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1661 0.1458 0.1935 0.0100  0.0082  -0.0018 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1673 0.1472 0.1930 0.0105  0.0073  -0.0016 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1686 0.1494 0.1946 0.0075  0.0121  -0.0011 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1717 0.1537 0.1948 0.0072  0.0118  0.0009  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1838 0.1649 0.2110 0.0053  0.0150  -0.0020 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1491 0.1278 0.1765 0.0101  0.0079  -0.0021 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1675 0.1454 0.1924 0.0106  0.0069  -0.0032 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1610 0.1376 0.1858 0.0113  0.0087  -0.0027 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1785 0.1550 0.2057 0.0115  0.0099  -0.0008 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1895 0.1671 0.2157 0.0094  0.0055  -0.0053 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2214 0.2016 0.2488 0.0090  0.0030  -0.0046 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1866 0.1626 0.2165 0.0086  0.0067  -0.0061 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1651 0.1409 0.1876 0.0117  0.0090  -0.0040 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1615 0.1358 0.1864 0.0129  0.0114  -0.0036 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1717 0.1426 0.2002 0.0123  0.0127  -0.0052 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1821 0.1520 0.2092 0.0104  0.0119  -0.0083 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1624 0.1360 0.1845 0.0129  0.0125  -0.0059 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1718 0.1484 0.1905 0.0132  0.0115  -0.0045 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1886 0.1660 0.2031 0.0121  0.0096  -0.0051 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1821 0.1606 0.2029 0.0146  0.0128  -0.0020 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1599 0.1297 0.1933 0.0135  0.0145  -0.0026 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1656 0.1313 0.2031 0.0127  0.0163  -0.0040 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1884 0.1502 0.2252 0.0116  0.0184  -0.0090 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1997 0.1593 0.2364 0.0092  0.0186  -0.0123 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1776 0.1424 0.2210 0.0145  0.0182  0.0007  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1938 0.1539 0.2420 0.0137  0.0202  0.0003  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1972 0.1566 0.2522 0.0158  0.0220  0.0062  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2074 0.1621 0.2676 0.0149  0.0241  0.0071  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2507 0.1988 0.3161 0.0153  0.0280  0.0046  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2399 0.1853 0.3051 0.0158  0.0305  -0.0002 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2623 0.2060 0.3330 0.0145  0.0301  0.0062  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1808 0.1424 0.2167 0.0127  0.0202  -0.0100 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1966 0.1543 0.2312 0.0110  0.0234  -0.0155 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.2074 0.1667 0.2342 0.0071  0.0208  -0.0197 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2277 0.1841 0.2520 0.0040  0.0231  -0.0249 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.2032 0.1601 0.2401 0.0131  0.0270  -0.0157 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.1944 0.1558 0.2254 0.0131  0.0250  -0.0154 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2005 0.1665 0.2323 0.0154  0.0227  -0.0102 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2065 0.1682 0.2309 0.0107  0.0255  -0.0195 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.1987 0.1673 0.2248 0.0145  0.0218  -0.0115 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2095 0.1757 0.2311 0.0118  0.0234  -0.0166 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1962 0.1603 0.2195 0.0069  0.0162  -0.0173 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.1918 0.1588 0.2094 0.0036  0.0128  -0.0192 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.2090 0.1780 0.2290 0.0023  0.0098  -0.0182 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2231 0.1958 0.2403 -0.0001 0.0063  -0.0184 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.1896 0.1604 0.2028 0.0044  0.0103  -0.0169 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2024 0.1720 0.2130 0.0050  0.0132  -0.0182 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2110 0.1842 0.2173 0.0054  0.0107  -0.0156 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2247 0.1920 0.2311 0.0012  0.0159  -0.0238 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1955 0.1626 0.2213 0.0037  0.0111  -0.0166 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.2049 0.1740 0.2336 0.0024  0.0090  -0.0159 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.2269 0.1964 0.2545 -0.0020 0.0080  -0.0198 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2321 0.1977 0.2583 -0.0042 0.0109  -0.0239 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1983 0.1651 0.2324 0.0041  0.0111  -0.0136 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.2129 0.1877 0.2416 -0.0035 0.0042  -0.0187 24  THR   A N   
135  C CA  . THR   A 18  ? 0.2207 0.1981 0.2487 -0.0085 0.0022  -0.0216 24  THR   A CA  
136  C C   . THR   A 18  ? 0.2226 0.1982 0.2563 -0.0099 0.0038  -0.0228 24  THR   A C   
137  O O   . THR   A 18  ? 0.2056 0.1789 0.2439 -0.0069 0.0058  -0.0204 24  THR   A O   
138  C CB  . THR   A 18  ? 0.2436 0.2289 0.2719 -0.0093 -0.0032 -0.0186 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2343 0.2217 0.2700 -0.0064 -0.0037 -0.0151 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2477 0.2347 0.2707 -0.0079 -0.0049 -0.0165 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2237 0.2013 0.2570 -0.0152 0.0026  -0.0261 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2236 0.2003 0.2626 -0.0170 0.0038  -0.0271 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2145 0.1964 0.2601 -0.0145 0.0015  -0.0225 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2220 0.2012 0.2725 -0.0132 0.0041  -0.0216 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.2442 0.2238 0.2813 -0.0241 0.0022  -0.0315 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.3384 0.3196 0.3824 -0.0265 0.0023  -0.0317 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.3998 0.3733 0.4470 -0.0269 0.0073  -0.0339 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.3808 0.3706 0.4302 -0.0280 -0.0019 -0.0293 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4043 0.3817 0.4572 -0.0295 0.0061  -0.0335 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4130 0.4006 0.4680 -0.0300 0.0006  -0.0307 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.1974 0.1863 0.2436 -0.0134 -0.0028 -0.0194 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.1976 0.1909 0.2514 -0.0108 -0.0038 -0.0156 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1882 0.1767 0.2426 -0.0064 -0.0001 -0.0137 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1930 0.1819 0.2528 -0.0056 0.0017  -0.0125 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2100 0.2110 0.2660 -0.0100 -0.0084 -0.0120 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3167 0.3220 0.3826 -0.0077 -0.0084 -0.0088 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3455 0.3549 0.4182 -0.0100 -0.0090 -0.0091 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3433 0.3474 0.4108 -0.0034 -0.0070 -0.0062 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1853 0.1697 0.2339 -0.0041 0.0012  -0.0136 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1760 0.1569 0.2245 -0.0009 0.0042  -0.0116 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1675 0.1440 0.2182 -0.0017 0.0076  -0.0121 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1785 0.1550 0.2318 -0.0008 0.0093  -0.0100 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1864 0.1644 0.2290 0.0011  0.0049  -0.0113 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2057 0.1870 0.2459 0.0024  0.0023  -0.0099 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.1908 0.1754 0.2349 0.0034  0.0013  -0.0078 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.1930 0.1733 0.2279 0.0023  0.0017  -0.0108 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1697 0.1422 0.2193 -0.0037 0.0089  -0.0148 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1732 0.1406 0.2257 -0.0044 0.0124  -0.0147 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1812 0.1511 0.2388 -0.0068 0.0123  -0.0148 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.1927 0.1602 0.2531 -0.0067 0.0149  -0.0127 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1893 0.1509 0.2404 -0.0063 0.0147  -0.0184 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1882 0.1459 0.2369 -0.0033 0.0167  -0.0175 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2074 0.1650 0.2515 -0.0032 0.0163  -0.0200 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.2017 0.1558 0.2531 -0.0002 0.0194  -0.0135 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2051 0.1591 0.2498 0.0000  0.0191  -0.0182 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2069 0.1592 0.2563 0.0021  0.0206  -0.0138 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2207 0.1738 0.2761 0.0006  0.0208  -0.0092 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2203 0.1701 0.2730 0.0053  0.0229  -0.0095 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2252 0.1762 0.2825 0.0035  0.0225  -0.0046 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2264 0.1759 0.2831 0.0060  0.0235  -0.0046 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1740 0.1496 0.2335 -0.0092 0.0093  -0.0164 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.1864 0.1656 0.2521 -0.0116 0.0092  -0.0165 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.1998 0.1830 0.2695 -0.0092 0.0096  -0.0134 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2067 0.1927 0.2822 -0.0109 0.0106  -0.0132 29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2052 0.1903 0.2725 -0.0153 0.0055  -0.0188 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1842 0.1678 0.2510 -0.0059 0.0093  -0.0114 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1774 0.1637 0.2470 -0.0040 0.0107  -0.0094 30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1792 0.1614 0.2430 -0.0022 0.0129  -0.0077 30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1795 0.1630 0.2419 -0.0004 0.0133  -0.0067 30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1916 0.1833 0.2642 -0.0024 0.0078  -0.0087 30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2158 0.2134 0.2957 -0.0046 0.0053  -0.0091 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2509 0.2517 0.3383 -0.0054 0.0070  -0.0089 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2304 0.2301 0.3081 -0.0065 0.0014  -0.0100 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1749 0.1525 0.2360 -0.0028 0.0145  -0.0070 31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1678 0.1427 0.2240 -0.0012 0.0157  -0.0045 31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1880 0.1645 0.2433 -0.0020 0.0180  -0.0023 31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2132 0.1902 0.2714 -0.0043 0.0201  -0.0020 31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1741 0.1438 0.2300 -0.0015 0.0169  -0.0036 31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.1885 0.1564 0.2414 0.0003  0.0177  0.0002  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.1906 0.1592 0.2399 0.0027  0.0160  -0.0005 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2307 0.1932 0.2862 0.0004  0.0196  0.0019  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1805 0.1580 0.2314 -0.0009 0.0180  -0.0010 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.1825 0.1615 0.2305 -0.0028 0.0204  0.0008  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.1904 0.1682 0.2342 -0.0029 0.0201  0.0051  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2130 0.1914 0.2556 -0.0055 0.0217  0.0081  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.1803 0.1616 0.2264 -0.0024 0.0210  -0.0009 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2009 0.1839 0.2421 -0.0056 0.0238  0.0003  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.1967 0.1797 0.2494 -0.0019 0.0216  -0.0038 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.1859 0.1629 0.2279 -0.0004 0.0182  0.0060  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1966 0.1737 0.2365 -0.0001 0.0178  0.0107  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1987 0.1738 0.2396 0.0032  0.0163  0.0104  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1901 0.1653 0.2301 0.0045  0.0153  0.0068  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2031 0.1847 0.2373 -0.0023 0.0179  0.0125  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2156 0.1998 0.2476 -0.0021 0.0165  0.0178  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2446 0.2307 0.2766 -0.0038 0.0163  0.0239  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2055 0.1915 0.2357 -0.0003 0.0149  0.0181  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2531 0.2429 0.2841 -0.0031 0.0143  0.0283  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2272 0.2169 0.2569 -0.0010 0.0136  0.0245  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2089 0.1941 0.2380 0.0016  0.0143  0.0142  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2360 0.2292 0.2647 0.0001  0.0119  0.0265  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2132 0.2011 0.2403 0.0025  0.0129  0.0159  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2290 0.2209 0.2564 0.0019  0.0118  0.0218  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2067 0.1800 0.2504 0.0046  0.0166  0.0142  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2062 0.1778 0.2514 0.0076  0.0162  0.0138  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2157 0.1887 0.2636 0.0089  0.0163  0.0202  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2141 0.1873 0.2646 0.0079  0.0168  0.0252  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2222 0.1884 0.2710 0.0084  0.0175  0.0096  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2216 0.1835 0.2754 0.0075  0.0196  0.0111  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2481 0.2066 0.3079 0.0096  0.0216  0.0157  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2605 0.2167 0.3244 0.0088  0.0231  0.0194  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2275 0.1858 0.2888 0.0122  0.0220  0.0160  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1991 0.1736 0.2474 0.0112  0.0157  0.0207  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1922 0.1692 0.2449 0.0129  0.0156  0.0274  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1924 0.1674 0.2490 0.0163  0.0169  0.0256  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1889 0.1665 0.2415 0.0165  0.0159  0.0230  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2166 0.2015 0.2643 0.0105  0.0130  0.0318  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2649 0.2550 0.3175 0.0115  0.0118  0.0401  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3008 0.2892 0.3607 0.0153  0.0130  0.0415  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2899 0.2864 0.3391 0.0082  0.0098  0.0453  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1970 0.1668 0.2617 0.0187  0.0198  0.0265  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1997 0.1668 0.2691 0.0217  0.0225  0.0241  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2123 0.1794 0.2812 0.0216  0.0224  0.0238  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2120 0.1858 0.2839 0.0236  0.0212  0.0291  36  SER   A C   
244  O O   . SER   A 30  ? 0.2118 0.1861 0.2826 0.0247  0.0220  0.0256  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2019 0.1616 0.2809 0.0236  0.0268  0.0247  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2548 0.2142 0.3327 0.0234  0.0269  0.0233  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2042 0.1611 0.2891 0.0264  0.0305  0.0225  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.3189 0.2795 0.4047 0.0247  0.0269  0.0320  36  SER   A OG  
249  N N   . SER   A 31  ? 0.2052 0.1848 0.2802 0.0235  0.0190  0.0376  37  SER   A N   
250  C CA  . SER   A 31  ? 0.2023 0.1900 0.2805 0.0247  0.0172  0.0433  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1977 0.1904 0.2661 0.0224  0.0147  0.0395  37  SER   A C   
252  O O   . SER   A 31  ? 0.2073 0.2050 0.2781 0.0236  0.0143  0.0413  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2292 0.2237 0.3116 0.0239  0.0145  0.0538  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3055 0.3052 0.3776 0.0190  0.0109  0.0546  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1805 0.1716 0.2392 0.0192  0.0135  0.0343  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1821 0.1764 0.2320 0.0170  0.0118  0.0304  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1747 0.1635 0.2211 0.0178  0.0134  0.0226  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1687 0.1593 0.2089 0.0163  0.0123  0.0196  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1892 0.1857 0.2315 0.0127  0.0100  0.0302  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2008 0.2047 0.2435 0.0101  0.0079  0.0378  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1918 0.1975 0.2263 0.0050  0.0072  0.0368  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1795 0.1870 0.2065 0.0025  0.0070  0.0320  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.1936 0.2052 0.2134 -0.0028 0.0066  0.0317  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2145 0.2298 0.2324 -0.0065 0.0060  0.0360  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1828 0.1947 0.1970 -0.0048 0.0072  0.0270  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1721 0.1542 0.2220 0.0194  0.0158  0.0192  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1663 0.1439 0.2119 0.0189  0.0168  0.0122  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1637 0.1417 0.2022 0.0163  0.0145  0.0094  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1749 0.1524 0.2088 0.0157  0.0138  0.0056  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1781 0.1567 0.2225 0.0200  0.0177  0.0098  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1852 0.1596 0.2248 0.0189  0.0186  0.0033  39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.2014 0.1710 0.2423 0.0183  0.0201  0.0002  39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1935 0.1698 0.2279 0.0182  0.0177  0.0014  39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1592 0.1379 0.1977 0.0148  0.0137  0.0115  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1526 0.1317 0.1864 0.0125  0.0125  0.0089  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1613 0.1373 0.1973 0.0116  0.0131  0.0074  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1719 0.1463 0.2119 0.0117  0.0142  0.0101  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1602 0.1440 0.1908 0.0104  0.0116  0.0118  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1731 0.1607 0.2000 0.0099  0.0107  0.0123  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1840 0.1759 0.2070 0.0064  0.0104  0.0142  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1813 0.1670 0.2053 0.0104  0.0105  0.0080  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1571 0.1326 0.1910 0.0105  0.0123  0.0039  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1580 0.1320 0.1944 0.0091  0.0126  0.0023  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1622 0.1385 0.1971 0.0080  0.0118  0.0008  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1653 0.1426 0.1979 0.0087  0.0106  -0.0004 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1701 0.1406 0.2083 0.0091  0.0128  -0.0010 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1692 0.1387 0.2104 0.0071  0.0130  -0.0028 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1878 0.1527 0.2317 0.0065  0.0147  -0.0049 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1795 0.1520 0.2202 0.0061  0.0108  -0.0051 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1632 0.1402 0.2000 0.0063  0.0128  0.0010  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1523 0.1312 0.1899 0.0054  0.0132  -0.0005 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1611 0.1399 0.2036 0.0046  0.0133  -0.0021 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1647 0.1424 0.2089 0.0033  0.0145  -0.0013 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1548 0.1354 0.1897 0.0034  0.0153  0.0007  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1788 0.1604 0.2162 0.0025  0.0172  -0.0017 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1802 0.1620 0.2102 0.0036  0.0148  0.0023  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1554 0.1357 0.2009 0.0051  0.0120  -0.0037 43  SER   A N   
298  C CA  . SER   A 37  ? 0.1464 0.1284 0.1979 0.0041  0.0117  -0.0049 43  SER   A CA  
299  C C   . SER   A 37  ? 0.1612 0.1459 0.2176 0.0042  0.0131  -0.0051 43  SER   A C   
300  O O   . SER   A 37  ? 0.1656 0.1503 0.2206 0.0052  0.0142  -0.0049 43  SER   A O   
301  C CB  . SER   A 37  ? 0.1754 0.1581 0.2277 0.0040  0.0085  -0.0060 43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1782 0.1627 0.2291 0.0054  0.0062  -0.0055 43  SER   A OG  
303  N N   . SER   A 38  ? 0.1679 0.1550 0.2311 0.0031  0.0139  -0.0058 44  SER   A N   
304  C CA  . SER   A 38  ? 0.1859 0.1757 0.2563 0.0036  0.0160  -0.0061 44  SER   A CA  
305  C C   . SER   A 38  ? 0.2035 0.1970 0.2804 0.0055  0.0126  -0.0050 44  SER   A C   
306  O O   . SER   A 38  ? 0.2277 0.2232 0.3044 0.0050  0.0085  -0.0045 44  SER   A O   
307  C CB  . SER   A 38  ? 0.2168 0.2081 0.2925 0.0014  0.0190  -0.0071 44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2439 0.2372 0.3232 0.0005  0.0161  -0.0071 44  SER   A OG  
309  N N   . THR   A 39  ? 0.2072 0.2019 0.2901 0.0072  0.0146  -0.0044 45  THR   A N   
310  C CA  . THR   A 39  ? 0.2196 0.2183 0.3101 0.0094  0.0114  -0.0017 45  THR   A CA  
311  C C   . THR   A 39  ? 0.2348 0.2373 0.3388 0.0103  0.0143  -0.0012 45  THR   A C   
312  O O   . THR   A 39  ? 0.2236 0.2240 0.3297 0.0096  0.0201  -0.0036 45  THR   A O   
313  C CB  . THR   A 39  ? 0.2250 0.2210 0.3121 0.0115  0.0113  -0.0004 45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2381 0.2308 0.3271 0.0119  0.0172  -0.0021 45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2304 0.2230 0.3050 0.0107  0.0092  -0.0010 45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2467 0.2552 0.3602 0.0116  0.0103  0.0022  46  THR   A N   
317  C CA  . THR   A 40  ? 0.2619 0.2750 0.3909 0.0131  0.0129  0.0036  46  THR   A CA  
318  C C   . THR   A 40  ? 0.2669 0.2771 0.4020 0.0164  0.0168  0.0048  46  THR   A C   
319  O O   . THR   A 40  ? 0.2873 0.2963 0.4309 0.0172  0.0233  0.0029  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3093 0.3314 0.4471 0.0128  0.0066  0.0076  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3630 0.3867 0.4974 0.0139  0.0009  0.0115  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3154 0.3394 0.4477 0.0089  0.0041  0.0053  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.2662 0.2746 0.3965 0.0180  0.0135  0.0074  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.2726 0.2773 0.4084 0.0209  0.0174  0.0087  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.2613 0.2577 0.3849 0.0195  0.0223  0.0041  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.2553 0.2496 0.3652 0.0172  0.0199  0.0023  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.2992 0.3066 0.4368 0.0230  0.0113  0.0148  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.2424 0.2342 0.3714 0.0206  0.0290  0.0024  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.2506 0.2353 0.3686 0.0184  0.0338  -0.0020 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.2406 0.2227 0.3517 0.0194  0.0303  0.0005  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.2548 0.2379 0.3743 0.0225  0.0281  0.0052  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.2773 0.2579 0.4037 0.0182  0.0432  -0.0057 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.3407 0.3230 0.4705 0.0157  0.0483  -0.0098 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.4256 0.4032 0.5629 0.0149  0.0587  -0.0144 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.4376 0.4151 0.5912 0.0185  0.0620  -0.0126 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.4562 0.4299 0.5820 0.0098  0.0641  -0.0203 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.2081 0.1871 0.3047 0.0168  0.0298  -0.0020 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.2067 0.1833 0.2962 0.0173  0.0271  -0.0001 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.1999 0.1704 0.2889 0.0165  0.0331  -0.0025 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.2176 0.1852 0.3088 0.0145  0.0400  -0.0069 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.1967 0.1650 0.2805 0.0170  0.0308  -0.0005 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.1977 0.1598 0.2816 0.0161  0.0364  -0.0024 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.2079 0.1679 0.2777 0.0122  0.0370  -0.0056 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.2169 0.1718 0.2857 0.0104  0.0419  -0.0080 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.2069 0.1676 0.2991 0.0197  0.0346  0.0031  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.2596 0.2230 0.3723 0.0243  0.0354  0.0077  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.1822 0.1460 0.2422 0.0110  0.0321  -0.0053 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.1791 0.1423 0.2272 0.0075  0.0322  -0.0075 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.2082 0.1707 0.2522 0.0029  0.0376  -0.0124 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.2283 0.1923 0.2758 0.0025  0.0393  -0.0138 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.1763 0.1439 0.2174 0.0080  0.0260  -0.0053 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.1964 0.1650 0.2385 0.0110  0.0210  -0.0012 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.1986 0.1643 0.2420 0.0116  0.0218  0.0003  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.2037 0.1756 0.2446 0.0121  0.0166  0.0005  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.2232 0.1841 0.2599 -0.0011 0.0402  -0.0150 52  THR   A N   
356  C CA  . THR   A 46  ? 0.2334 0.1951 0.2634 -0.0070 0.0445  -0.0194 52  THR   A CA  
357  C C   . THR   A 46  ? 0.2229 0.1893 0.2421 -0.0097 0.0402  -0.0180 52  THR   A C   
358  O O   . THR   A 46  ? 0.2371 0.2039 0.2539 -0.0083 0.0369  -0.0156 52  THR   A O   
359  C CB  . THR   A 46  ? 0.2923 0.2486 0.3231 -0.0107 0.0520  -0.0242 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3510 0.3052 0.3784 -0.0109 0.0509  -0.0233 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3020 0.2534 0.3462 -0.0072 0.0569  -0.0251 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2212 0.1918 0.2348 -0.0134 0.0401  -0.0186 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2107 0.1868 0.2162 -0.0157 0.0359  -0.0161 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2142 0.1914 0.2119 -0.0225 0.0389  -0.0189 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.2239 0.1999 0.2190 -0.0279 0.0443  -0.0234 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2025 0.1830 0.2065 -0.0163 0.0336  -0.0138 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2147 0.1938 0.2264 -0.0107 0.0316  -0.0121 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2046 0.1913 0.2029 -0.0175 0.0289  -0.0097 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2142 0.1929 0.2290 -0.0052 0.0267  -0.0089 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2002 0.1807 0.1936 -0.0231 0.0354  -0.0166 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2028 0.1864 0.1884 -0.0301 0.0370  -0.0185 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2150 0.2060 0.1941 -0.0355 0.0357  -0.0171 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2114 0.2068 0.1920 -0.0326 0.0312  -0.0123 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2026 0.1892 0.1869 -0.0285 0.0328  -0.0152 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.2339 0.2264 0.2058 -0.0440 0.0398  -0.0213 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.2460 0.2467 0.2102 -0.0508 0.0385  -0.0196 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.2765 0.2826 0.2327 -0.0585 0.0382  -0.0206 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.2929 0.2973 0.2427 -0.0665 0.0438  -0.0268 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.2499 0.2477 0.2121 -0.0552 0.0445  -0.0245 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.2419 0.2345 0.2132 -0.0478 0.0451  -0.0239 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.2329 0.2304 0.2069 -0.0430 0.0385  -0.0166 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.2219 0.2145 0.2042 -0.0371 0.0396  -0.0169 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.2354 0.2290 0.2229 -0.0311 0.0348  -0.0120 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.2251 0.2240 0.2108 -0.0300 0.0293  -0.0063 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.2599 0.2495 0.2547 -0.0267 0.0359  -0.0128 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.2729 0.2859 0.2296 -0.0565 0.0320  -0.0145 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.2807 0.2992 0.2324 -0.0620 0.0308  -0.0146 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.2725 0.3012 0.2264 -0.0594 0.0233  -0.0062 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.2956 0.3260 0.2553 -0.0531 0.0195  -0.0006 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.2714 0.2809 0.2267 -0.0589 0.0342  -0.0190 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2584 0.2647 0.2239 -0.0469 0.0298  -0.0139 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.3117 0.3471 0.2622 -0.0644 0.0216  -0.0054 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.3399 0.3853 0.2946 -0.0618 0.0152  0.0024  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.3250 0.3678 0.2834 -0.0585 0.0154  0.0013  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.3314 0.3835 0.2908 -0.0602 0.0118  0.0055  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.4278 0.4873 0.3760 -0.0711 0.0116  0.0067  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.5576 0.6195 0.4966 -0.0819 0.0146  0.0009  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.6001 0.6753 0.5346 -0.0896 0.0107  0.0049  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5969 0.6477 0.5336 -0.0829 0.0209  -0.0075 57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.2952 0.3260 0.2561 -0.0539 0.0195  -0.0037 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2691 0.2967 0.2333 -0.0506 0.0197  -0.0044 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2657 0.2992 0.2368 -0.0441 0.0148  0.0022  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2598 0.2938 0.2355 -0.0386 0.0125  0.0060  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2555 0.2699 0.2224 -0.0459 0.0241  -0.0090 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.2798 0.2851 0.2417 -0.0528 0.0319  -0.0176 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2376 0.2756 0.2098 -0.0450 0.0137  0.0035  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2311 0.2734 0.2106 -0.0388 0.0105  0.0085  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2111 0.2465 0.1921 -0.0356 0.0128  0.0058  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2153 0.2549 0.2012 -0.0324 0.0113  0.0088  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2656 0.3223 0.2473 -0.0423 0.0066  0.0142  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3145 0.3794 0.2978 -0.0432 0.0030  0.0199  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3781 0.4581 0.3667 -0.0451 -0.0014 0.0272  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.3978 0.4884 0.3821 -0.0531 -0.0039 0.0298  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3186 0.4009 0.3173 -0.0381 -0.0026 0.0313  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.1892 0.2145 0.1662 -0.0371 0.0169  0.0004  60  THR   A N   
416  C CA  . THR   A 54  ? 0.1921 0.2097 0.1705 -0.0337 0.0189  -0.0013 60  THR   A CA  
417  C C   . THR   A 54  ? 0.1902 0.1965 0.1692 -0.0298 0.0213  -0.0040 60  THR   A C   
418  O O   . THR   A 54  ? 0.2086 0.2119 0.1858 -0.0321 0.0232  -0.0065 60  THR   A O   
419  C CB  . THR   A 54  ? 0.2429 0.2600 0.2176 -0.0396 0.0215  -0.0041 60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3147 0.3265 0.2847 -0.0453 0.0253  -0.0090 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2351 0.2645 0.2097 -0.0441 0.0189  -0.0015 60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1789 0.1803 0.1610 -0.0242 0.0210  -0.0030 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1763 0.1685 0.1601 -0.0204 0.0224  -0.0043 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1705 0.1592 0.1563 -0.0157 0.0215  -0.0025 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1831 0.1745 0.1679 -0.0165 0.0212  -0.0014 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1641 0.1474 0.1524 -0.0115 0.0211  -0.0020 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1596 0.1400 0.1488 -0.0079 0.0198  -0.0001 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1655 0.1463 0.1570 -0.0037 0.0173  0.0010  62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1699 0.1493 0.1637 -0.0029 0.0174  0.0003  62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.1830 0.1555 0.1733 -0.0081 0.0223  -0.0002 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2034 0.1734 0.1943 -0.0049 0.0204  0.0028  62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.1999 0.1709 0.1878 -0.0130 0.0256  -0.0019 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1616 0.1443 0.1524 -0.0015 0.0155  0.0024  63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1568 0.1394 0.1495 0.0017  0.0135  0.0028  63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1707 0.1508 0.1618 0.0030  0.0122  0.0041  63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1822 0.1619 0.1703 0.0018  0.0127  0.0050  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1621 0.1497 0.1559 0.0028  0.0128  0.0028  63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1632 0.1530 0.1556 0.0033  0.0131  0.0029  63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1827 0.1758 0.1741 0.0013  0.0144  0.0033  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1708 0.1598 0.1629 0.0051  0.0126  0.0022  63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.2014 0.1967 0.1920 0.0015  0.0155  0.0032  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1798 0.1706 0.1705 0.0049  0.0140  0.0016  63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1964 0.1903 0.1866 0.0034  0.0155  0.0021  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.2218 0.2177 0.2110 0.0030  0.0176  0.0012  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1582 0.1372 0.1511 0.0049  0.0103  0.0045  64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1534 0.1316 0.1440 0.0053  0.0083  0.0060  64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1608 0.1417 0.1485 0.0053  0.0079  0.0045  64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1643 0.1462 0.1542 0.0064  0.0079  0.0027  64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.1669 0.1434 0.1615 0.0067  0.0063  0.0075  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.1781 0.1553 0.1701 0.0062  0.0035  0.0101  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.1819 0.1578 0.1717 0.0051  0.0032  0.0133  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.1833 0.1627 0.1746 0.0062  0.0010  0.0096  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.1972 0.1749 0.1834 0.0038  0.0002  0.0164  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.1878 0.1691 0.1753 0.0044  -0.0019 0.0120  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2058 0.1865 0.1910 0.0034  -0.0026 0.0159  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.2421 0.2255 0.2224 0.0009  -0.0059 0.0191  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1622 0.1437 0.1451 0.0037  0.0080  0.0050  65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.1755 0.1590 0.1549 0.0029  0.0088  0.0028  65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.1873 0.1706 0.1618 0.0010  0.0064  0.0038  65  CYS   A C   
460  O O   . CYS   A 59  ? 0.1826 0.1659 0.1526 -0.0010 0.0056  0.0063  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.1771 0.1623 0.1542 0.0016  0.0115  0.0022  65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.1930 0.1802 0.1663 0.0002  0.0142  -0.0012 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.1855 0.1692 0.1609 0.0012  0.0049  0.0022  66  SER   A N   
464  C CA  . SER   A 60  ? 0.1916 0.1766 0.1622 -0.0015 0.0019  0.0035  66  SER   A CA  
465  C C   . SER   A 60  ? 0.1949 0.1815 0.1570 -0.0053 0.0032  0.0017  66  SER   A C   
466  O O   . SER   A 60  ? 0.2152 0.2035 0.1717 -0.0083 0.0005  0.0047  66  SER   A O   
467  C CB  . SER   A 60  ? 0.2159 0.2014 0.1891 -0.0013 0.0002  0.0018  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.2352 0.2203 0.2075 -0.0019 0.0032  -0.0034 66  SER   A OG  
469  N N   . SER   A 61  ? 0.1755 0.1617 0.1370 -0.0052 0.0077  -0.0025 67  SER   A N   
470  C CA  . SER   A 61  ? 0.1815 0.1690 0.1355 -0.0090 0.0104  -0.0051 67  SER   A CA  
471  C C   . SER   A 61  ? 0.1975 0.1857 0.1473 -0.0105 0.0107  -0.0019 67  SER   A C   
472  O O   . SER   A 61  ? 0.2047 0.1942 0.1474 -0.0142 0.0129  -0.0036 67  SER   A O   
473  C CB  . SER   A 61  ? 0.1978 0.1846 0.1548 -0.0080 0.0159  -0.0106 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.2110 0.1981 0.1748 -0.0046 0.0181  -0.0097 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.1977 0.1848 0.1518 -0.0082 0.0089  0.0025  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.1990 0.1858 0.1499 -0.0097 0.0088  0.0063  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.2097 0.1950 0.1622 -0.0092 0.0045  0.0125  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.2225 0.2066 0.1735 -0.0103 0.0044  0.0165  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.2022 0.1887 0.1577 -0.0079 0.0122  0.0053  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.2081 0.1969 0.1638 -0.0082 0.0167  0.0006  68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.2018 0.1920 0.1496 -0.0123 0.0190  0.0001  68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.2291 0.2217 0.1788 -0.0124 0.0243  -0.0047 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.2238 0.2166 0.1717 -0.0135 0.0271  -0.0093 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.2372 0.2287 0.1804 -0.0152 0.0245  -0.0101 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.2339 0.2285 0.1854 -0.0132 0.0328  -0.0134 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2130 0.1980 0.1703 -0.0071 0.0015  0.0134  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.2310 0.2146 0.1935 -0.0055 -0.0017 0.0193  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.2526 0.2322 0.2196 -0.0038 0.0009  0.0207  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.2838 0.2614 0.2519 -0.0041 0.0000  0.0259  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.2802 0.2660 0.2376 -0.0086 -0.0055 0.0251  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.2896 0.2792 0.2458 -0.0100 -0.0093 0.0252  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.2984 0.2912 0.2531 -0.0122 -0.0144 0.0333  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.3107 0.3089 0.2604 -0.0158 -0.0178 0.0321  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.2732 0.2753 0.2114 -0.0218 -0.0186 0.0311  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.2950 0.2961 0.2258 -0.0244 -0.0160 0.0314  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.2861 0.2929 0.2197 -0.0257 -0.0213 0.0291  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2260 0.2048 0.1954 -0.0025 0.0042  0.0164  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2307 0.2066 0.2029 -0.0022 0.0069  0.0167  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.2154 0.1909 0.1929 -0.0004 0.0087  0.0133  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.2117 0.1898 0.1897 0.0006  0.0088  0.0102  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.2821 0.2597 0.2489 -0.0048 0.0096  0.0153  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.4040 0.3806 0.3655 -0.0075 0.0089  0.0197  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.5140 0.4911 0.4722 -0.0100 0.0123  0.0186  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.5937 0.5706 0.5451 -0.0132 0.0117  0.0227  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.6442 0.6245 0.5896 -0.0147 0.0092  0.0228  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.2046 0.1768 0.1858 -0.0004 0.0106  0.0139  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.1964 0.1686 0.1810 -0.0002 0.0128  0.0107  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2132 0.1872 0.1951 -0.0028 0.0153  0.0092  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2533 0.2250 0.2333 -0.0048 0.0166  0.0107  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.1780 0.1452 0.1680 0.0004  0.0141  0.0115  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2038 0.1703 0.1985 0.0031  0.0118  0.0132  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2441 0.2113 0.2425 0.0044  0.0120  0.0108  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2102 0.1760 0.2065 0.0044  0.0091  0.0176  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2252 0.1919 0.2281 0.0066  0.0098  0.0134  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2421 0.2084 0.2440 0.0066  0.0077  0.0177  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.1822 0.1608 0.1646 -0.0030 0.0158  0.0066  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.1877 0.1701 0.1688 -0.0056 0.0177  0.0056  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.1804 0.1647 0.1636 -0.0074 0.0188  0.0039  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.1808 0.1670 0.1663 -0.0060 0.0177  0.0032  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.1927 0.1808 0.1736 -0.0045 0.0175  0.0049  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.1979 0.1853 0.1749 -0.0043 0.0173  0.0055  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2204 0.2078 0.1938 -0.0069 0.0189  0.0065  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.1978 0.1850 0.1742 -0.0024 0.0160  0.0049  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.2323 0.2196 0.2009 -0.0076 0.0190  0.0070  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2173 0.2045 0.1888 -0.0035 0.0161  0.0049  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.2315 0.2190 0.1988 -0.0061 0.0177  0.0060  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.2609 0.2487 0.2221 -0.0080 0.0180  0.0060  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.1883 0.1731 0.1702 -0.0112 0.0208  0.0033  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.1877 0.1762 0.1703 -0.0144 0.0216  0.0015  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2033 0.2013 0.1877 -0.0142 0.0201  0.0024  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2374 0.2388 0.2221 -0.0135 0.0202  0.0034  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2118 0.1982 0.1922 -0.0193 0.0245  0.0004  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2327 0.2165 0.2115 -0.0184 0.0248  0.0023  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.1959 0.1778 0.1753 -0.0135 0.0226  0.0042  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.1830 0.1851 0.1691 -0.0147 0.0189  0.0023  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.1938 0.2051 0.1836 -0.0140 0.0172  0.0044  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1850 0.2027 0.1747 -0.0182 0.0164  0.0049  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1980 0.2123 0.1850 -0.0204 0.0169  0.0031  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2324 0.2435 0.2259 -0.0087 0.0158  0.0056  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2557 0.2638 0.2491 -0.0056 0.0166  0.0052  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2356 0.2414 0.2283 -0.0076 0.0152  0.0046  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1757 0.2035 0.1691 -0.0193 0.0149  0.0077  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1775 0.2144 0.1720 -0.0228 0.0127  0.0101  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1745 0.2145 0.1755 -0.0175 0.0106  0.0138  75  SER   A C   
545  O O   . SER   A 69  ? 0.1777 0.2177 0.1840 -0.0127 0.0111  0.0150  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2265 0.2740 0.2233 -0.0267 0.0119  0.0124  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3259 0.3704 0.3167 -0.0324 0.0141  0.0088  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1746 0.2164 0.1751 -0.0186 0.0089  0.0153  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1705 0.2138 0.1773 -0.0137 0.0074  0.0188  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1740 0.2272 0.1828 -0.0168 0.0044  0.0239  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1831 0.2402 0.1858 -0.0235 0.0036  0.0233  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1855 0.2180 0.1900 -0.0103 0.0086  0.0157  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1795 0.2071 0.1772 -0.0142 0.0095  0.0123  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1801 0.2006 0.1730 -0.0159 0.0120  0.0079  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1812 0.2111 0.1780 -0.0161 0.0084  0.0138  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1922 0.2077 0.1807 -0.0192 0.0139  0.0045  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1892 0.2143 0.1801 -0.0199 0.0103  0.0100  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1865 0.2046 0.1739 -0.0214 0.0133  0.0052  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1708 0.2285 0.1884 -0.0123 0.0028  0.0292  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1759 0.2441 0.1971 -0.0147 -0.0006 0.0360  77  SER   A CA  
561  C C   . SER   A 71  ? 0.1774 0.2425 0.1930 -0.0170 -0.0014 0.0357  77  SER   A C   
562  O O   . SER   A 71  ? 0.1896 0.2440 0.2010 -0.0152 0.0010  0.0306  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1973 0.2709 0.2317 -0.0087 -0.0014 0.0424  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2189 0.2829 0.2570 -0.0025 0.0008  0.0408  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1750 0.2499 0.1906 -0.0213 -0.0047 0.0415  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.1840 0.2566 0.1944 -0.0238 -0.0052 0.0417  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.1931 0.2605 0.2113 -0.0166 -0.0049 0.0446  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.1981 0.2679 0.2271 -0.0110 -0.0053 0.0491  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2068 0.2927 0.2140 -0.0315 -0.0091 0.0477  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.2602 0.3497 0.2575 -0.0403 -0.0085 0.0430  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.3527 0.4555 0.3446 -0.0495 -0.0124 0.0482  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.4450 0.5502 0.4258 -0.0593 -0.0109 0.0422  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.4983 0.6120 0.4692 -0.0697 -0.0129 0.0438  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.1971 0.2573 0.2110 -0.0167 -0.0037 0.0421  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.1964 0.2512 0.2177 -0.0104 -0.0031 0.0444  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2005 0.2644 0.2315 -0.0087 -0.0061 0.0545  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2272 0.3008 0.2559 -0.0140 -0.0094 0.0603  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2303 0.2792 0.2443 -0.0131 -0.0019 0.0410  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2660 0.3147 0.2693 -0.0198 -0.0006 0.0352  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2196 0.2761 0.2224 -0.0228 -0.0020 0.0364  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.1886 0.2494 0.2307 -0.0015 -0.0048 0.0565  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2019 0.2709 0.2564 0.0012  -0.0069 0.0664  80  SER   A CA  
583  C C   . SER   A 74  ? 0.1884 0.2489 0.2534 0.0087  -0.0038 0.0670  80  SER   A C   
584  O O   . SER   A 74  ? 0.1803 0.2295 0.2423 0.0112  -0.0003 0.0593  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2587 0.3375 0.3195 0.0013  -0.0081 0.0697  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3470 0.4268 0.3991 -0.0027 -0.0078 0.0635  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.1977 0.2642 0.2760 0.0119  -0.0050 0.0766  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2122 0.2710 0.3025 0.0187  -0.0014 0.0779  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2240 0.2838 0.3251 0.0235  0.0017  0.0770  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2402 0.3114 0.3505 0.0240  -0.0004 0.0845  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2164 0.2817 0.3162 0.0192  -0.0042 0.0899  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2453 0.3023 0.3583 0.0257  -0.0003 0.0924  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2594 0.3030 0.3644 0.0256  0.0028  0.0843  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2663 0.3315 0.3901 0.0261  -0.0036 0.1064  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2081 0.2568 0.3076 0.0265  0.0067  0.0677  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2219 0.2700 0.3288 0.0302  0.0107  0.0645  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2263 0.2640 0.3425 0.0357  0.0169  0.0612  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2181 0.2457 0.3288 0.0356  0.0185  0.0561  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2417 0.2868 0.3348 0.0269  0.0111  0.0552  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2730 0.3278 0.3571 0.0208  0.0059  0.0577  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2711 0.3134 0.3688 0.0299  0.0160  0.0500  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.2896 0.3423 0.3625 0.0176  0.0062  0.0506  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2330 0.2731 0.3640 0.0401  0.0207  0.0638  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.2401 0.2699 0.3806 0.0449  0.0279  0.0597  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.2617 0.2832 0.3913 0.0434  0.0318  0.0476  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.2886 0.3146 0.4135 0.0417  0.0315  0.0448  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2439 0.2791 0.4052 0.0502  0.0316  0.0663  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.2796 0.3035 0.4527 0.0549  0.0394  0.0636  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.3027 0.3214 0.4812 0.0564  0.0393  0.0682  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.3146 0.3324 0.4925 0.0571  0.0473  0.0556  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.3318 0.3390 0.5211 0.0602  0.0472  0.0650  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.3239 0.3304 0.5121 0.0605  0.0554  0.0520  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.3325 0.3336 0.5269 0.0622  0.0554  0.0567  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.2390 0.2488 0.3633 0.0432  0.0350  0.0406  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.2318 0.2342 0.3452 0.0410  0.0382  0.0298  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.2303 0.2237 0.3530 0.0439  0.0465  0.0248  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.2459 0.2336 0.3758 0.0458  0.0486  0.0266  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.2242 0.2213 0.3224 0.0371  0.0345  0.0255  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.2342 0.2247 0.3215 0.0346  0.0371  0.0154  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.2298 0.2350 0.3198 0.0340  0.0275  0.0299  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.2327 0.2242 0.3539 0.0435  0.0515  0.0180  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.2479 0.2306 0.3769 0.0452  0.0605  0.0118  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.2541 0.2259 0.3737 0.0422  0.0622  0.0042  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.2584 0.2299 0.3639 0.0385  0.0566  0.0024  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.2841 0.2681 0.4117 0.0443  0.0656  0.0058  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.3531 0.3475 0.4943 0.0479  0.0660  0.0128  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.4741 0.4695 0.6374 0.0538  0.0698  0.0203  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.4859 0.4717 0.6576 0.0558  0.0776  0.0160  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.5287 0.5349 0.7016 0.0562  0.0651  0.0306  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.2630 0.2260 0.3913 0.0435  0.0706  -0.0006 86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.2811 0.2338 0.4016 0.0400  0.0731  -0.0085 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.2870 0.2389 0.3890 0.0341  0.0716  -0.0171 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.3108 0.2661 0.4084 0.0328  0.0730  -0.0201 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.2903 0.2336 0.4237 0.0418  0.0839  -0.0133 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.2836 0.2311 0.3751 0.0302  0.0684  -0.0206 87  SER   A N   
636  C CA  . SER   A 81  ? 0.2908 0.2375 0.3653 0.0242  0.0664  -0.0280 87  SER   A CA  
637  C C   . SER   A 81  ? 0.3087 0.2467 0.3796 0.0203  0.0694  -0.0348 87  SER   A C   
638  O O   . SER   A 81  ? 0.3211 0.2535 0.4030 0.0227  0.0734  -0.0337 87  SER   A O   
639  C CB  . SER   A 81  ? 0.2905 0.2439 0.3548 0.0231  0.0569  -0.0234 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.2817 0.2337 0.3471 0.0235  0.0529  -0.0199 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.3297 0.2672 0.3857 0.0141  0.0670  -0.0411 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.3327 0.2633 0.3854 0.0098  0.0689  -0.0470 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.2987 0.2302 0.3533 0.0113  0.0626  -0.0411 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.3011 0.2268 0.3566 0.0089  0.0646  -0.0444 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.3839 0.3148 0.4210 0.0021  0.0682  -0.0549 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.4118 0.3504 0.4380 0.0005  0.0585  -0.0509 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.5325 0.4726 0.5440 -0.0073 0.0564  -0.0568 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.5744 0.5121 0.5826 -0.0116 0.0555  -0.0603 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.5399 0.4843 0.5435 -0.0093 0.0553  -0.0575 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.2701 0.2085 0.3258 0.0150  0.0560  -0.0327 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.2536 0.1932 0.3101 0.0157  0.0505  -0.0276 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.2433 0.1821 0.3128 0.0208  0.0515  -0.0202 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.2477 0.1846 0.3192 0.0206  0.0496  -0.0177 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.2499 0.1971 0.2977 0.0152  0.0427  -0.0239 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.2507 0.1993 0.2863 0.0102  0.0406  -0.0294 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.2835 0.2303 0.3134 0.0058  0.0389  -0.0333 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.2785 0.2308 0.3083 0.0096  0.0403  -0.0303 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.3098 0.2594 0.3289 0.0009  0.0361  -0.0370 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.3025 0.2568 0.3210 0.0048  0.0378  -0.0341 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.3204 0.2735 0.3336 0.0004  0.0356  -0.0372 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.3513 0.3078 0.3538 -0.0046 0.0323  -0.0396 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.2442 0.1852 0.3229 0.0251  0.0543  -0.0161 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.2405 0.1823 0.3325 0.0298  0.0547  -0.0075 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.2518 0.1920 0.3571 0.0338  0.0617  -0.0067 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.2578 0.2005 0.3605 0.0335  0.0637  -0.0102 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.2291 0.1807 0.3190 0.0314  0.0474  0.0007  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.2081 0.1626 0.2870 0.0283  0.0407  0.0013  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.2131 0.1654 0.2940 0.0278  0.0392  0.0044  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.2081 0.1675 0.2760 0.0259  0.0364  -0.0006 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.2018 0.1569 0.2739 0.0251  0.0339  0.0048  90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.2124 0.1741 0.2723 0.0236  0.0313  0.0000  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.2011 0.1607 0.2632 0.0231  0.0302  0.0023  90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.2004 0.1622 0.2556 0.0207  0.0259  0.0023  90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.2657 0.2027 0.3860 0.0378  0.0651  -0.0010 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.2747 0.2122 0.4109 0.0427  0.0711  0.0022  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.2790 0.2288 0.4170 0.0453  0.0654  0.0107  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.2765 0.2333 0.4044 0.0433  0.0572  0.0145  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.2955 0.2271 0.4470 0.0462  0.0746  0.0082  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.2994 0.2336 0.4434 0.0442  0.0669  0.0132  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.2701 0.2046 0.3946 0.0383  0.0628  0.0047  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.2803 0.2335 0.4323 0.0496  0.0696  0.0144  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.2696 0.2355 0.4250 0.0517  0.0641  0.0231  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.2617 0.2326 0.4221 0.0532  0.0579  0.0346  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.2750 0.2403 0.4467 0.0557  0.0609  0.0385  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.2670 0.2355 0.4395 0.0564  0.0707  0.0253  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.2522 0.2325 0.4024 0.0506  0.0495  0.0390  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.2333 0.2185 0.3845 0.0502  0.0435  0.0486  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2298 0.2273 0.3720 0.0474  0.0357  0.0532  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2435 0.2438 0.3771 0.0454  0.0350  0.0478  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.2552 0.2317 0.3958 0.0470  0.0427  0.0437  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.2728 0.2508 0.3940 0.0419  0.0381  0.0367  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.2789 0.2486 0.3908 0.0388  0.0385  0.0298  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.2774 0.2503 0.3747 0.0347  0.0328  0.0278  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.3157 0.2909 0.4018 0.0322  0.0306  0.0227  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.3205 0.2968 0.4067 0.0330  0.0329  0.0193  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.2424 0.2193 0.3180 0.0288  0.0262  0.0215  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2318 0.2357 0.3740 0.0461  0.0301  0.0622  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2440 0.2584 0.3757 0.0419  0.0231  0.0655  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2227 0.2323 0.3372 0.0372  0.0207  0.0587  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2431 0.2462 0.3565 0.0367  0.0213  0.0582  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2478 0.2723 0.3872 0.0418  0.0184  0.0787  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2483 0.2818 0.4042 0.0458  0.0189  0.0870  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2534 0.2983 0.4069 0.0438  0.0156  0.0884  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2562 0.2867 0.4314 0.0516  0.0234  0.0928  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2662 0.3202 0.4360 0.0475  0.0162  0.0958  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2705 0.3097 0.4631 0.0558  0.0244  0.1006  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2755 0.3269 0.4653 0.0537  0.0206  0.1021  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3005 0.3617 0.5080 0.0576  0.0214  0.1097  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.2023 0.2148 0.3045 0.0338  0.0184  0.0533  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1954 0.2046 0.2828 0.0295  0.0162  0.0474  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1896 0.2086 0.2702 0.0252  0.0108  0.0524  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1888 0.2165 0.2710 0.0245  0.0090  0.0557  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1931 0.1971 0.2720 0.0287  0.0181  0.0376  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1890 0.1899 0.2549 0.0249  0.0159  0.0325  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.1812 0.1758 0.2406 0.0245  0.0179  0.0238  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2111 0.1999 0.2741 0.0264  0.0217  0.0199  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1866 0.1821 0.2361 0.0216  0.0156  0.0206  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1755 0.1938 0.2492 0.0218  0.0086  0.0531  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1704 0.1975 0.2367 0.0166  0.0044  0.0571  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1753 0.2004 0.2284 0.0126  0.0041  0.0491  96  SER   A C   
721  O O   . SER   A 90  ? 0.1829 0.1997 0.2326 0.0139  0.0064  0.0415  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1979 0.2261 0.2645 0.0146  0.0028  0.0630  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2413 0.2601 0.3026 0.0141  0.0049  0.0566  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1778 0.2112 0.2242 0.0074  0.0012  0.0512  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1733 0.2052 0.2082 0.0030  0.0013  0.0444  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1666 0.1939 0.2007 0.0056  0.0033  0.0380  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1823 0.2040 0.2095 0.0043  0.0046  0.0315  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1937 0.2190 0.2226 0.0012  0.0026  0.0404  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2154 0.2454 0.2433 -0.0024 0.0010  0.0462  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2501 0.2854 0.2688 -0.0093 0.0000  0.0461  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2305 0.2607 0.2652 -0.0005 0.0004  0.0526  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2481 0.2871 0.2673 -0.0117 -0.0015 0.0524  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2440 0.2801 0.2730 -0.0063 -0.0015 0.0569  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1601 0.1907 0.2013 0.0086  0.0036  0.0404  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1673 0.1940 0.2079 0.0108  0.0057  0.0350  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1676 0.2020 0.2052 0.0074  0.0043  0.0357  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1680 0.2120 0.2096 0.0058  0.0020  0.0420  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1813 0.2060 0.2328 0.0163  0.0082  0.0363  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.2104 0.2305 0.2609 0.0182  0.0112  0.0303  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2241 0.2355 0.2669 0.0177  0.0122  0.0236  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2322 0.2507 0.2942 0.0230  0.0148  0.0314  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1691 0.1995 0.2002 0.0063  0.0056  0.0298  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1658 0.2021 0.1937 0.0029  0.0049  0.0296  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1695 0.2030 0.1997 0.0059  0.0073  0.0265  99  MET   A C   
745  O O   . MET   A 93  ? 0.1899 0.2150 0.2175 0.0080  0.0092  0.0218  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1927 0.2255 0.2102 -0.0019 0.0051  0.0249  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.1964 0.2317 0.2102 -0.0059 0.0037  0.0268  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2288 0.2579 0.2322 -0.0110 0.0057  0.0201  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2829 0.3001 0.2879 -0.0052 0.0079  0.0155  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1585 0.1995 0.1933 0.0057  0.0072  0.0293  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1673 0.2060 0.2042 0.0081  0.0101  0.0262  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1649 0.2053 0.1952 0.0041  0.0101  0.0236  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1789 0.2255 0.2062 -0.0006 0.0080  0.0254  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1934 0.2392 0.2429 0.0115  0.0112  0.0309  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2457 0.2894 0.3047 0.0162  0.0124  0.0338  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2610 0.3110 0.3341 0.0200  0.0148  0.0377  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2790 0.3109 0.3345 0.0186  0.0154  0.0276  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1640 0.1986 0.1914 0.0053  0.0127  0.0193  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1627 0.1978 0.1844 0.0018  0.0134  0.0170  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1504 0.1838 0.1742 0.0042  0.0166  0.0149  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1625 0.1923 0.1901 0.0080  0.0186  0.0138  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1792 0.2057 0.1911 -0.0004 0.0133  0.0130  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1491 0.1850 0.1701 0.0013  0.0175  0.0140  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1568 0.1907 0.1777 0.0024  0.0208  0.0115  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.1922 0.2165 0.2030 0.0012  0.0211  0.0078  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.2192 0.2411 0.2239 -0.0019 0.0199  0.0074  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1624 0.2041 0.1856 -0.0005 0.0218  0.0128  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1762 0.2152 0.1975 -0.0002 0.0257  0.0098  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1641 0.2170 0.1991 0.0008  0.0209  0.0177  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.2021 0.2213 0.2119 0.0036  0.0229  0.0054  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.2203 0.2317 0.2213 0.0026  0.0225  0.0030  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.2174 0.2251 0.2179 0.0045  0.0244  0.0004  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.2206 0.2298 0.2278 0.0071  0.0260  0.0000  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.2311 0.2342 0.2236 0.0027  0.0245  -0.0014 104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.2371 0.2371 0.2272 0.0031  0.0262  -0.0045 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.2258 0.2222 0.2169 0.0048  0.0239  -0.0050 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.2248 0.2192 0.2140 0.0047  0.0205  -0.0032 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.2341 0.2315 0.2146 -0.0003 0.0262  -0.0054 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.2475 0.2427 0.2241 -0.0013 0.0282  -0.0091 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.2600 0.2567 0.2394 -0.0014 0.0334  -0.0127 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.2492 0.2411 0.2203 -0.0026 0.0258  -0.0100 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.2615 0.2550 0.2358 -0.0032 0.0345  -0.0163 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.2573 0.2485 0.2263 -0.0042 0.0296  -0.0146 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.2286 0.2240 0.2229 0.0062  0.0264  -0.0076 105 SER   A N   
785  C CA  . SER   A 99  ? 0.2225 0.2143 0.2171 0.0071  0.0250  -0.0088 105 SER   A CA  
786  C C   . SER   A 99  ? 0.2434 0.2327 0.2378 0.0065  0.0291  -0.0135 105 SER   A C   
787  O O   . SER   A 99  ? 0.2667 0.2575 0.2654 0.0071  0.0339  -0.0153 105 SER   A O   
788  C CB  . SER   A 99  ? 0.2416 0.2343 0.2433 0.0098  0.0231  -0.0060 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.2607 0.2565 0.2713 0.0122  0.0262  -0.0053 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.2211 0.2069 0.2110 0.0049  0.0275  -0.0156 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.2264 0.2089 0.2148 0.0032  0.0308  -0.0208 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.2373 0.2172 0.2290 0.0045  0.0285  -0.0206 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.2202 0.2010 0.2130 0.0059  0.0240  -0.0167 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.2581 0.2403 0.2349 -0.0021 0.0303  -0.0234 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.2827 0.2674 0.2559 -0.0037 0.0329  -0.0235 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.3248 0.3101 0.2857 -0.0094 0.0321  -0.0249 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.3589 0.3427 0.3137 -0.0132 0.0319  -0.0282 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.2958 0.2833 0.2527 -0.0107 0.0318  -0.0225 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.2424 0.2188 0.2368 0.0040  0.0322  -0.0249 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.2414 0.2152 0.2403 0.0055  0.0304  -0.0243 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.2388 0.2136 0.2323 0.0037  0.0242  -0.0223 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.2292 0.2042 0.2273 0.0062  0.0214  -0.0189 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.2728 0.2420 0.2732 0.0037  0.0362  -0.0305 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.2771 0.2467 0.2802 0.0043  0.0422  -0.0327 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.2465 0.2206 0.2415 0.0024  0.0392  -0.0306 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.2257 0.2016 0.2100 -0.0004 0.0220  -0.0235 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.2192 0.1969 0.2002 -0.0019 0.0161  -0.0207 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.2007 0.1806 0.1833 0.0007  0.0124  -0.0151 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.2102 0.1912 0.1925 0.0004  0.0082  -0.0123 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.1878 0.1683 0.1728 0.0030  0.0144  -0.0135 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.1817 0.1636 0.1687 0.0050  0.0119  -0.0091 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.1831 0.1644 0.1769 0.0076  0.0111  -0.0075 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.1789 0.1608 0.1740 0.0084  0.0092  -0.0047 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.1789 0.1625 0.1661 0.0056  0.0142  -0.0081 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.1885 0.1729 0.1683 0.0026  0.0144  -0.0084 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.2002 0.1844 0.1754 0.0007  0.0111  -0.0067 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.1933 0.1788 0.1724 0.0022  0.0178  -0.0098 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.1790 0.1588 0.1770 0.0085  0.0129  -0.0095 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.1727 0.1521 0.1764 0.0105  0.0121  -0.0076 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.1771 0.1566 0.1799 0.0098  0.0086  -0.0063 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.1832 0.1627 0.1830 0.0079  0.0067  -0.0073 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.1819 0.1589 0.1900 0.0111  0.0145  -0.0099 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.1970 0.1741 0.2114 0.0136  0.0190  -0.0095 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.1626 0.1428 0.1684 0.0109  0.0080  -0.0039 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1680 0.1481 0.1748 0.0106  0.0058  -0.0028 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.1706 0.1512 0.1759 0.0104  0.0052  -0.0008 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.1807 0.1609 0.1888 0.0107  0.0047  0.0003  111 GLY   A O   
828  N N   . GLY   A 106 ? 0.1708 0.1519 0.1724 0.0099  0.0058  -0.0006 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.1677 0.1484 0.1680 0.0094  0.0058  0.0012  112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.1590 0.1398 0.1617 0.0094  0.0075  0.0015  112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1627 0.1453 0.1661 0.0094  0.0085  0.0011  112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1573 0.1362 0.1613 0.0089  0.0079  0.0023  113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1519 0.1307 0.1570 0.0077  0.0102  0.0015  113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1508 0.1310 0.1525 0.0057  0.0116  0.0015  113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1590 0.1379 0.1587 0.0053  0.0117  0.0021  113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1571 0.1328 0.1661 0.0078  0.0113  0.0015  113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.1817 0.1578 0.1950 0.0091  0.0105  0.0012  113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.1775 0.1518 0.1862 0.0052  0.0149  -0.0001 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2162 0.1899 0.2357 0.0099  0.0115  0.0017  113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1515 0.1346 0.1527 0.0038  0.0127  0.0010  114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1510 0.1362 0.1494 0.0007  0.0141  0.0008  114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1604 0.1433 0.1587 -0.0021 0.0167  -0.0012 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1645 0.1478 0.1642 -0.0024 0.0170  -0.0018 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1600 0.1515 0.1585 0.0000  0.0131  0.0023  114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1744 0.1705 0.1703 -0.0043 0.0139  0.0025  114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1788 0.1750 0.1728 -0.0050 0.0145  0.0024  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1892 0.1928 0.1868 -0.0048 0.0122  0.0056  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1637 0.1440 0.1604 -0.0046 0.0190  -0.0025 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.1744 0.1514 0.1711 -0.0079 0.0228  -0.0054 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.1828 0.1607 0.1752 -0.0131 0.0252  -0.0072 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.1830 0.1626 0.1734 -0.0135 0.0242  -0.0060 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.1837 0.1539 0.1856 -0.0053 0.0247  -0.0057 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.1908 0.1576 0.1927 -0.0045 0.0248  -0.0042 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.2067 0.1676 0.2154 -0.0016 0.0262  -0.0030 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.2261 0.1890 0.2377 0.0026  0.0219  0.0001  115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.2115 0.1735 0.2294 0.0050  0.0218  0.0006  115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.2251 0.1844 0.2471 0.0039  0.0261  -0.0021 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.2347 0.1993 0.2545 0.0078  0.0176  0.0033  115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.1925 0.1697 0.1830 -0.0177 0.0287  -0.0105 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2266 0.2043 0.2123 -0.0242 0.0317  -0.0134 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.2665 0.2358 0.2542 -0.0264 0.0379  -0.0178 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.2590 0.2229 0.2529 -0.0221 0.0393  -0.0177 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.2317 0.2181 0.2121 -0.0295 0.0303  -0.0133 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.2274 0.2134 0.2067 -0.0323 0.0329  -0.0161 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.2957 0.2640 0.2788 -0.0334 0.0422  -0.0220 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.3236 0.2830 0.3091 -0.0360 0.0495  -0.0271 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.3245 0.2824 0.3122 -0.0363 0.0525  -0.0298 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.3605 0.3103 0.3544 -0.0353 0.0583  -0.0328 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.3840 0.3425 0.3633 -0.0449 0.0542  -0.0321 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.4557 0.4227 0.4263 -0.0528 0.0538  -0.0346 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.5405 0.5087 0.5037 -0.0627 0.0574  -0.0394 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.5575 0.5331 0.5167 -0.0653 0.0534  -0.0369 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.5407 0.5021 0.5022 -0.0688 0.0654  -0.0466 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.2778 0.2435 0.2618 -0.0370 0.0486  -0.0282 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.2741 0.2396 0.2591 -0.0380 0.0513  -0.0306 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.2743 0.2383 0.2674 -0.0301 0.0487  -0.0272 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.3014 0.2642 0.2972 -0.0302 0.0516  -0.0292 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.2739 0.2489 0.2500 -0.0442 0.0488  -0.0302 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.2975 0.2756 0.2651 -0.0531 0.0508  -0.0334 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.3165 0.3032 0.2797 -0.0550 0.0452  -0.0294 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.3353 0.3094 0.2983 -0.0613 0.0580  -0.0405 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.3513 0.3396 0.3073 -0.0641 0.0486  -0.0338 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.3631 0.3436 0.3181 -0.0685 0.0565  -0.0409 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.2475 0.2126 0.2440 -0.0237 0.0432  -0.0220 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.2294 0.1941 0.2327 -0.0171 0.0403  -0.0189 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.1980 0.1684 0.1997 -0.0136 0.0334  -0.0140 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.1987 0.1722 0.1960 -0.0147 0.0310  -0.0125 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.1871 0.1587 0.1926 -0.0096 0.0307  -0.0119 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.1803 0.1562 0.1852 -0.0063 0.0252  -0.0081 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.1666 0.1487 0.1665 -0.0092 0.0234  -0.0069 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.1695 0.1535 0.1679 -0.0123 0.0249  -0.0079 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.1804 0.1552 0.1913 -0.0018 0.0233  -0.0067 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.1853 0.1636 0.1953 0.0007  0.0188  -0.0039 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.1877 0.1580 0.2045 0.0012  0.0239  -0.0062 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1669 0.1529 0.1647 -0.0086 0.0204  -0.0043 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1642 0.1571 0.1593 -0.0108 0.0183  -0.0017 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1657 0.1603 0.1645 -0.0065 0.0153  0.0015  121 VAL   A C   
898  O O   . VAL   A 115 ? 0.1736 0.1726 0.1725 -0.0077 0.0141  0.0040  121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.1738 0.1704 0.1661 -0.0126 0.0174  -0.0007 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2005 0.2058 0.1925 -0.0139 0.0144  0.0035  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.1939 0.1886 0.1821 -0.0179 0.0208  -0.0043 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1605 0.1521 0.1624 -0.0021 0.0141  0.0017  122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1602 0.1523 0.1655 0.0015  0.0121  0.0037  122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1574 0.1462 0.1642 0.0048  0.0113  0.0028  122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1588 0.1447 0.1646 0.0047  0.0119  0.0014  122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1527 0.1417 0.1620 0.0073  0.0102  0.0038  123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1483 0.1347 0.1577 0.0094  0.0096  0.0025  123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1533 0.1415 0.1634 0.0106  0.0100  0.0032  123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1616 0.1525 0.1750 0.0112  0.0104  0.0052  123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1572 0.1408 0.1689 0.0106  0.0089  0.0013  123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1788 0.1630 0.1939 0.0111  0.0093  0.0022  123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.1803 0.1622 0.1925 0.0099  0.0089  0.0006  123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.1892 0.1706 0.2067 0.0117  0.0089  0.0006  123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1503 0.1372 0.1582 0.0111  0.0101  0.0018  124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1491 0.1372 0.1582 0.0121  0.0115  0.0015  124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.1575 0.1441 0.1711 0.0138  0.0125  0.0009  124 VAL   A C   
917  O O   . VAL   A 118 ? 0.1532 0.1367 0.1664 0.0136  0.0117  -0.0008 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.1571 0.1436 0.1618 0.0114  0.0117  -0.0006 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.1683 0.1555 0.1744 0.0122  0.0143  -0.0020 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1685 0.1559 0.1695 0.0099  0.0112  0.0004  124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.1594 0.1482 0.1783 0.0153  0.0142  0.0026  125 SER   A N   
922  C CA  . SER   A 119 ? 0.1643 0.1509 0.1890 0.0171  0.0159  0.0026  125 SER   A CA  
923  C C   . SER   A 119 ? 0.1854 0.1722 0.2150 0.0188  0.0195  0.0019  125 SER   A C   
924  O O   . SER   A 119 ? 0.2086 0.1912 0.2415 0.0197  0.0221  -0.0005 125 SER   A O   
925  C CB  . SER   A 119 ? 0.1792 0.1681 0.2082 0.0175  0.0148  0.0068  125 SER   A CB  
926  O OG  . SER   A 119 ? 0.1880 0.1746 0.2240 0.0194  0.0166  0.0080  125 SER   A OG  
927  N N   . THR   A 120 ? 0.1797 0.1710 0.2104 0.0191  0.0201  0.0035  126 THR   A N   
928  C CA  . THR   A 120 ? 0.1936 0.1856 0.2310 0.0211  0.0243  0.0029  126 THR   A CA  
929  C C   . THR   A 120 ? 0.2147 0.2092 0.2476 0.0197  0.0252  0.0012  126 THR   A C   
930  O O   . THR   A 120 ? 0.1995 0.1956 0.2254 0.0174  0.0223  0.0015  126 THR   A O   
931  C CB  . THR   A 120 ? 0.1932 0.1902 0.2416 0.0238  0.0246  0.0091  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.1989 0.2035 0.2466 0.0226  0.0219  0.0130  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.1956 0.1909 0.2483 0.0248  0.0233  0.0122  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.2219 0.2172 0.2600 0.0209  0.0296  -0.0003 127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.2363 0.2349 0.2709 0.0194  0.0307  -0.0013 127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.2495 0.2476 0.2894 0.0204  0.0369  -0.0044 127 GLY   A C   
937  O O   . GLY   A 121 ? 0.2613 0.2567 0.3096 0.0229  0.0406  -0.0052 127 GLY   A O   
938  N N   . GLY   A 122 ? 0.2548 0.2542 0.2889 0.0181  0.0384  -0.0069 128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.2598 0.2592 0.2975 0.0182  0.0449  -0.0106 128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.2669 0.2742 0.3104 0.0188  0.0456  -0.0072 128 GLY   A C   
941  O O   . GLY   A 122 ? 0.2595 0.2727 0.3079 0.0201  0.0417  -0.0014 128 GLY   A O   
942  N N   . ASN   A 123 ? 0.2639 0.2718 0.3067 0.0174  0.0508  -0.0110 129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.2753 0.2908 0.3245 0.0178  0.0527  -0.0085 129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.2545 0.2757 0.2993 0.0159  0.0467  -0.0039 129 ASN   A C   
945  O O   . ASN   A 123 ? 0.2535 0.2828 0.3068 0.0168  0.0464  0.0003  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.3065 0.3264 0.3739 0.0226  0.0564  -0.0053 129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.3536 0.3676 0.4267 0.0240  0.0646  -0.0111 129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.3956 0.4077 0.4639 0.0214  0.0702  -0.0170 129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.3604 0.3712 0.4432 0.0277  0.0659  -0.0097 129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.2192 0.2361 0.2506 0.0126  0.0428  -0.0052 130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.2100 0.2304 0.2363 0.0102  0.0382  -0.0019 130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.1841 0.2073 0.2142 0.0114  0.0333  0.0027  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.2078 0.2342 0.2343 0.0088  0.0302  0.0049  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.1825 0.2031 0.2171 0.0142  0.0327  0.0034  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.1761 0.1985 0.2121 0.0145  0.0280  0.0075  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.1920 0.2065 0.2204 0.0142  0.0259  0.0051  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.2128 0.2213 0.2384 0.0147  0.0282  0.0011  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.1730 0.2001 0.2223 0.0182  0.0287  0.0118  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.1886 0.2256 0.2480 0.0188  0.0299  0.0157  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2125 0.2526 0.2872 0.0234  0.0320  0.0198  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.1940 0.2388 0.2503 0.0151  0.0251  0.0198  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.1595 0.1745 0.1850 0.0129  0.0220  0.0074  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.1720 0.1805 0.1927 0.0130  0.0201  0.0058  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1721 0.1840 0.1971 0.0134  0.0176  0.0099  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1761 0.1939 0.2014 0.0113  0.0158  0.0128  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1762 0.1807 0.1872 0.0102  0.0185  0.0038  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.1802 0.1885 0.1890 0.0074  0.0171  0.0057  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.1844 0.1836 0.1925 0.0105  0.0166  0.0027  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.1643 0.1725 0.1916 0.0152  0.0173  0.0098  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1581 0.1691 0.1884 0.0151  0.0150  0.0138  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1632 0.1688 0.1874 0.0137  0.0134  0.0116  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1813 0.1809 0.2028 0.0144  0.0142  0.0080  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1422 0.1506 0.1643 0.0113  0.0113  0.0138  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1511 0.1550 0.1685 0.0099  0.0105  0.0117  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1649 0.1705 0.1852 0.0096  0.0095  0.0148  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1728 0.1849 0.1951 0.0081  0.0084  0.0190  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1629 0.1677 0.1743 0.0062  0.0100  0.0105  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1650 0.1688 0.1734 0.0058  0.0109  0.0086  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1650 0.1630 0.1705 0.0067  0.0114  0.0057  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1752 0.1847 0.1842 0.0042  0.0110  0.0102  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1635 0.1607 0.1659 0.0059  0.0121  0.0047  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1744 0.1830 0.1806 0.0034  0.0121  0.0085  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1616 0.1636 0.1642 0.0043  0.0127  0.0059  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1532 0.1535 0.1733 0.0105  0.0098  0.0129  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1609 0.1621 0.1827 0.0097  0.0091  0.0154  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1613 0.1637 0.1772 0.0056  0.0087  0.0144  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1682 0.1663 0.1810 0.0050  0.0095  0.0105  135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1602 0.1553 0.1842 0.0117  0.0100  0.0132  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1587 0.1672 0.1734 0.0023  0.0077  0.0180  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1746 0.1842 0.1830 -0.0027 0.0083  0.0162  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1740 0.1797 0.1820 -0.0032 0.0095  0.0145  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1826 0.1879 0.1945 -0.0014 0.0089  0.0172  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2007 0.2192 0.2074 -0.0070 0.0066  0.0209  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.2719 0.2923 0.2709 -0.0136 0.0078  0.0185  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2344 0.2512 0.2298 -0.0151 0.0098  0.0136  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3462 0.3712 0.3427 -0.0176 0.0070  0.0213  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1632 0.1660 0.1670 -0.0060 0.0116  0.0103  137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1675 0.1674 0.1712 -0.0073 0.0135  0.0083  137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.1828 0.1851 0.1804 -0.0138 0.0158  0.0065  137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.1727 0.1730 0.1699 -0.0156 0.0182  0.0044  137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.1713 0.1648 0.1784 -0.0040 0.0148  0.0044  137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1827 0.1740 0.1943 0.0009  0.0128  0.0056  137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.1809 0.1716 0.1862 -0.0049 0.0167  0.0009  137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.1812 0.1881 0.1741 -0.0178 0.0155  0.0069  138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.1809 0.1895 0.1668 -0.0251 0.0184  0.0038  138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.1947 0.2082 0.1769 -0.0299 0.0183  0.0064  138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.2099 0.2234 0.1864 -0.0361 0.0220  0.0025  138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.1870 0.1999 0.1686 -0.0289 0.0179  0.0036  138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.1888 0.1956 0.1726 -0.0256 0.0194  0.0000  138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.2018 0.2134 0.1813 -0.0299 0.0188  0.0001  138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.1995 0.2187 0.1817 -0.0279 0.0141  0.0063  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2269 0.2519 0.2078 -0.0302 0.0125  0.0079  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.2296 0.2539 0.2050 -0.0358 0.0151  0.0037  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2213 0.2530 0.2070 -0.0273 0.0087  0.0138  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.1871 0.2048 0.1726 -0.0275 0.0145  0.0129  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.2007 0.2234 0.1827 -0.0323 0.0140  0.0166  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.1997 0.2166 0.1844 -0.0305 0.0166  0.0145  139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.2156 0.2356 0.1966 -0.0350 0.0171  0.0166  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.2075 0.2373 0.1932 -0.0306 0.0090  0.0256  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.2467 0.2715 0.2422 -0.0221 0.0078  0.0279  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.2376 0.2565 0.2366 -0.0173 0.0088  0.0237  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.2820 0.3088 0.2816 -0.0208 0.0060  0.0340  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.1861 0.1955 0.1770 -0.0245 0.0180  0.0108  140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.1863 0.1910 0.1812 -0.0225 0.0200  0.0091  140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.1922 0.1941 0.1844 -0.0264 0.0253  0.0026  140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.1993 0.1958 0.1958 -0.0233 0.0276  -0.0018 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.1877 0.1871 0.1905 -0.0151 0.0186  0.0084  140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2046 0.2057 0.2110 -0.0111 0.0148  0.0137  140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2014 0.1970 0.2137 -0.0052 0.0142  0.0116  140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2294 0.2332 0.2373 -0.0119 0.0134  0.0195  140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.1909 0.1968 0.1758 -0.0337 0.0274  0.0024  141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.2049 0.2081 0.1865 -0.0386 0.0337  -0.0046 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.2052 0.2032 0.1938 -0.0357 0.0374  -0.0079 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.2252 0.2189 0.2163 -0.0362 0.0427  -0.0140 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.2149 0.2242 0.1856 -0.0485 0.0356  -0.0045 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.2495 0.2663 0.2133 -0.0524 0.0312  0.0000  141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.2698 0.2932 0.2220 -0.0636 0.0333  -0.0008 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.2633 0.2780 0.2281 -0.0506 0.0311  -0.0031 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.1966 0.1949 0.1895 -0.0325 0.0348  -0.0039 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.1965 0.1911 0.1964 -0.0302 0.0377  -0.0066 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.2074 0.1970 0.2164 -0.0237 0.0379  -0.0095 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.2253 0.2127 0.2414 -0.0222 0.0410  -0.0123 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.2029 0.1989 0.2050 -0.0290 0.0348  -0.0013 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.1992 0.1953 0.2044 -0.0237 0.0290  0.0038  142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.2101 0.2102 0.2116 -0.0245 0.0252  0.0098  142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.2019 0.1941 0.2149 -0.0170 0.0268  0.0033  142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.2224 0.2204 0.2297 -0.0184 0.0216  0.0124  142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.2084 0.2016 0.2219 -0.0143 0.0226  0.0083  142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.2119 0.2005 0.2320 -0.0136 0.0281  -0.0005 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.2220 0.2119 0.2413 -0.0089 0.0203  0.0083  142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.2274 0.2140 0.2528 -0.0086 0.0248  0.0004  142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.2196 0.2064 0.2439 -0.0066 0.0213  0.0042  142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.1939 0.1828 0.2035 -0.0201 0.0344  -0.0083 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.2170 0.2019 0.2342 -0.0148 0.0343  -0.0103 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.2448 0.2268 0.2651 -0.0163 0.0403  -0.0155 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.2521 0.2314 0.2813 -0.0122 0.0411  -0.0166 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.2057 0.1905 0.2212 -0.0119 0.0303  -0.0083 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.2090 0.1953 0.2249 -0.0087 0.0251  -0.0039 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.2233 0.2101 0.2368 -0.0069 0.0223  -0.0025 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.2160 0.2002 0.2395 -0.0045 0.0237  -0.0038 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.2679 0.2505 0.2811 -0.0228 0.0450  -0.0188 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.3001 0.2789 0.3161 -0.0251 0.0523  -0.0247 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.3514 0.3293 0.3725 -0.0269 0.0582  -0.0281 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.3635 0.3378 0.3888 -0.0284 0.0653  -0.0334 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.3023 0.2818 0.3077 -0.0324 0.0556  -0.0278 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.3542 0.3346 0.3550 -0.0317 0.0512  -0.0256 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.3593 0.3382 0.3656 -0.0252 0.0468  -0.0225 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.4328 0.4159 0.4238 -0.0383 0.0522  -0.0268 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.3695 0.3505 0.3911 -0.0268 0.0560  -0.0254 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.4134 0.3943 0.4397 -0.0289 0.0618  -0.0285 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.4398 0.4219 0.4754 -0.0239 0.0584  -0.0253 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.4338 0.4167 0.4702 -0.0197 0.0516  -0.0208 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.4706 0.4548 0.4850 -0.0374 0.0644  -0.0294 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.5561 0.5447 0.5642 -0.0376 0.0572  -0.0225 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.6412 0.6345 0.6358 -0.0458 0.0572  -0.0209 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.6310 0.6280 0.6222 -0.0463 0.0525  -0.0148 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.6820 0.6754 0.6696 -0.0520 0.0619  -0.0256 145 GLU   A OE2 
1078 N N   . GLU   A 140 ? 0.4756 0.4582 0.5173 -0.0254 0.0635  -0.0279 146 GLU   A N   
1079 C CA  . GLU   A 140 ? 0.5148 0.4992 0.5651 -0.0227 0.0619  -0.0259 146 GLU   A CA  
1080 C C   . GLU   A 140 ? 0.5365 0.5202 0.6022 -0.0178 0.0642  -0.0275 146 GLU   A C   
1081 O O   . GLU   A 140 ? 0.5473 0.5307 0.6192 -0.0198 0.0715  -0.0316 146 GLU   A O   
1082 C CB  . GLU   A 140 ? 0.5615 0.5475 0.6095 -0.0198 0.0537  -0.0202 146 GLU   A CB  
1083 C CG  . GLU   A 140 ? 0.6346 0.6223 0.6900 -0.0184 0.0524  -0.0186 146 GLU   A CG  
1084 C CD  . GLU   A 140 ? 0.7345 0.7239 0.7837 -0.0234 0.0536  -0.0172 146 GLU   A CD  
1085 O OE1 . GLU   A 140 ? 0.7682 0.7579 0.8076 -0.0255 0.0505  -0.0137 146 GLU   A OE1 
1086 O OE2 . GLU   A 140 ? 0.7445 0.7351 0.7993 -0.0252 0.0577  -0.0190 146 GLU   A OE2 
1087 N N   . SER   B 1   ? 0.2474 0.2391 0.2654 0.0002  -0.0033 0.0346  7   SER   C N   
1088 C CA  . SER   B 1   ? 0.2403 0.2344 0.2669 -0.0008 -0.0038 0.0353  7   SER   C CA  
1089 C C   . SER   B 1   ? 0.2323 0.2246 0.2578 -0.0014 -0.0034 0.0321  7   SER   C C   
1090 O O   . SER   B 1   ? 0.2453 0.2344 0.2631 -0.0014 -0.0039 0.0296  7   SER   C O   
1091 C CB  . SER   B 1   ? 0.2818 0.2774 0.3102 -0.0023 -0.0081 0.0384  7   SER   C CB  
1092 O OG  . SER   B 1   ? 0.3427 0.3354 0.3633 -0.0036 -0.0117 0.0368  7   SER   C OG  
1093 N N   . GLY   B 2   ? 0.2203 0.2143 0.2532 -0.0019 -0.0022 0.0323  8   GLY   C N   
1094 C CA  . GLY   B 2   ? 0.2157 0.2079 0.2475 -0.0024 -0.0016 0.0299  8   GLY   C CA  
1095 C C   . GLY   B 2   ? 0.2012 0.1948 0.2396 -0.0017 0.0019  0.0295  8   GLY   C C   
1096 O O   . GLY   B 2   ? 0.2053 0.2005 0.2477 -0.0006 0.0042  0.0296  8   GLY   C O   
1097 N N   . ALA   B 3   ? 0.1853 0.1782 0.2251 -0.0025 0.0023  0.0290  9   ALA   C N   
1098 C CA  . ALA   B 3   ? 0.1761 0.1697 0.2207 -0.0017 0.0060  0.0285  9   ALA   C CA  
1099 C C   . ALA   B 3   ? 0.1686 0.1594 0.2088 -0.0016 0.0071  0.0265  9   ALA   C C   
1100 O O   . ALA   B 3   ? 0.1906 0.1791 0.2261 -0.0026 0.0048  0.0262  9   ALA   C O   
1101 C CB  . ALA   B 3   ? 0.1983 0.1949 0.2524 -0.0026 0.0062  0.0316  9   ALA   C CB  
1102 N N   . ILE   B 4   ? 0.1631 0.1536 0.2046 -0.0005 0.0106  0.0253  10  ILE   C N   
1103 C CA  . ILE   B 4   ? 0.1719 0.1598 0.2097 -0.0002 0.0123  0.0243  10  ILE   C CA  
1104 C C   . ILE   B 4   ? 0.1686 0.1579 0.2138 -0.0008 0.0147  0.0266  10  ILE   C C   
1105 O O   . ILE   B 4   ? 0.1775 0.1690 0.2288 -0.0002 0.0169  0.0273  10  ILE   C O   
1106 C CB  . ILE   B 4   ? 0.1800 0.1663 0.2129 0.0019  0.0145  0.0213  10  ILE   C CB  
1107 C CG1 . ILE   B 4   ? 0.1932 0.1793 0.2217 0.0027  0.0127  0.0192  10  ILE   C CG1 
1108 C CG2 . ILE   B 4   ? 0.2016 0.1849 0.2294 0.0024  0.0159  0.0208  10  ILE   C CG2 
1109 C CD1 . ILE   B 4   ? 0.2115 0.1970 0.2374 0.0045  0.0143  0.0162  10  ILE   C CD1 
1110 N N   . TYR   B 5   ? 0.1651 0.1529 0.2102 -0.0019 0.0147  0.0278  11  TYR   C N   
1111 C CA  . TYR   B 5   ? 0.1755 0.1647 0.2282 -0.0025 0.0175  0.0303  11  TYR   C CA  
1112 C C   . TYR   B 5   ? 0.1804 0.1663 0.2281 -0.0014 0.0212  0.0295  11  TYR   C C   
1113 O O   . TYR   B 5   ? 0.1994 0.1826 0.2430 -0.0022 0.0202  0.0297  11  TYR   C O   
1114 C CB  . TYR   B 5   ? 0.1831 0.1740 0.2421 -0.0052 0.0143  0.0331  11  TYR   C CB  
1115 C CG  . TYR   B 5   ? 0.1964 0.1906 0.2600 -0.0060 0.0106  0.0344  11  TYR   C CG  
1116 C CD1 . TYR   B 5   ? 0.1903 0.1885 0.2637 -0.0058 0.0120  0.0367  11  TYR   C CD1 
1117 C CD2 . TYR   B 5   ? 0.2143 0.2075 0.2721 -0.0068 0.0061  0.0334  11  TYR   C CD2 
1118 C CE1 . TYR   B 5   ? 0.2033 0.2044 0.2804 -0.0062 0.0086  0.0382  11  TYR   C CE1 
1119 C CE2 . TYR   B 5   ? 0.2257 0.2216 0.2864 -0.0072 0.0030  0.0348  11  TYR   C CE2 
1120 C CZ  . TYR   B 5   ? 0.2234 0.2234 0.2937 -0.0069 0.0041  0.0374  11  TYR   C CZ  
1121 O OH  . TYR   B 5   ? 0.2480 0.2505 0.3207 -0.0071 0.0009  0.0392  11  TYR   C OH  
1122 N N   . VAL   B 6   ? 0.1880 0.1736 0.2353 0.0005  0.0255  0.0286  12  VAL   C N   
1123 C CA  . VAL   B 6   ? 0.2061 0.1884 0.2473 0.0019  0.0293  0.0279  12  VAL   C CA  
1124 C C   . VAL   B 6   ? 0.2123 0.1956 0.2600 0.0025  0.0346  0.0296  12  VAL   C C   
1125 O O   . VAL   B 6   ? 0.1979 0.1833 0.2503 0.0033  0.0362  0.0291  12  VAL   C O   
1126 C CB  . VAL   B 6   ? 0.2233 0.2032 0.2545 0.0041  0.0290  0.0242  12  VAL   C CB  
1127 C CG1 . VAL   B 6   ? 0.2204 0.2023 0.2543 0.0050  0.0295  0.0221  12  VAL   C CG1 
1128 C CG2 . VAL   B 6   ? 0.2438 0.2201 0.2675 0.0058  0.0326  0.0238  12  VAL   C CG2 
1129 N N   . GLY   B 7   ? 0.2241 0.2059 0.2729 0.0022  0.0378  0.0320  13  GLY   C N   
1130 C CA  . GLY   B 7   ? 0.2237 0.2065 0.2792 0.0030  0.0436  0.0340  13  GLY   C CA  
1131 C C   . GLY   B 7   ? 0.2182 0.2060 0.2871 0.0017  0.0430  0.0360  13  GLY   C C   
1132 O O   . GLY   B 7   ? 0.2284 0.2188 0.3028 -0.0006 0.0382  0.0377  13  GLY   C O   
1133 N N   . ASN   B 8   ? 0.2042 0.1931 0.2771 0.0034  0.0469  0.0355  14  ASN   C N   
1134 C CA  . ASN   B 8   ? 0.2056 0.1992 0.2913 0.0027  0.0461  0.0376  14  ASN   C CA  
1135 C C   . ASN   B 8   ? 0.1968 0.1912 0.2808 0.0034  0.0434  0.0351  14  ASN   C C   
1136 O O   . ASN   B 8   ? 0.1945 0.1911 0.2865 0.0042  0.0451  0.0358  14  ASN   C O   
1137 C CB  . ASN   B 8   ? 0.2330 0.2281 0.3285 0.0038  0.0527  0.0400  14  ASN   C CB  
1138 C CG  . ASN   B 8   ? 0.3152 0.3116 0.4177 0.0022  0.0546  0.0439  14  ASN   C CG  
1139 O OD1 . ASN   B 8   ? 0.3414 0.3422 0.4559 0.0002  0.0520  0.0473  14  ASN   C OD1 
1140 N ND2 . ASN   B 8   ? 0.3418 0.3342 0.4365 0.0031  0.0586  0.0436  14  ASN   C ND2 
1141 N N   . TYR   B 9   ? 0.1773 0.1698 0.2517 0.0032  0.0392  0.0325  15  TYR   C N   
1142 C CA  . TYR   B 9   ? 0.1796 0.1725 0.2521 0.0037  0.0366  0.0301  15  TYR   C CA  
1143 C C   . TYR   B 9   ? 0.1656 0.1601 0.2373 0.0019  0.0304  0.0309  15  TYR   C C   
1144 O O   . TYR   B 9   ? 0.1850 0.1781 0.2517 0.0008  0.0278  0.0311  15  TYR   C O   
1145 C CB  . TYR   B 9   ? 0.1946 0.1837 0.2559 0.0055  0.0376  0.0256  15  TYR   C CB  
1146 C CG  . TYR   B 9   ? 0.2013 0.1878 0.2606 0.0075  0.0435  0.0240  15  TYR   C CG  
1147 C CD1 . TYR   B 9   ? 0.2252 0.2127 0.2919 0.0086  0.0471  0.0239  15  TYR   C CD1 
1148 C CD2 . TYR   B 9   ? 0.2280 0.2108 0.2774 0.0086  0.0456  0.0225  15  TYR   C CD2 
1149 C CE1 . TYR   B 9   ? 0.2537 0.2381 0.3175 0.0106  0.0529  0.0219  15  TYR   C CE1 
1150 C CE2 . TYR   B 9   ? 0.2644 0.2443 0.3101 0.0107  0.0510  0.0207  15  TYR   C CE2 
1151 C CZ  . TYR   B 9   ? 0.2913 0.2720 0.3440 0.0117  0.0547  0.0201  15  TYR   C CZ  
1152 O OH  . TYR   B 9   ? 0.3525 0.3297 0.4007 0.0139  0.0604  0.0180  15  TYR   C OH  
1153 N N   . ARG   B 10  ? 0.1544 0.1511 0.2302 0.0019  0.0283  0.0312  16  ARG   C N   
1154 C CA  . ARG   B 10  ? 0.1585 0.1562 0.2320 0.0007  0.0230  0.0316  16  ARG   C CA  
1155 C C   . ARG   B 10  ? 0.1541 0.1507 0.2233 0.0020  0.0231  0.0287  16  ARG   C C   
1156 O O   . ARG   B 10  ? 0.1613 0.1588 0.2358 0.0031  0.0256  0.0285  16  ARG   C O   
1157 C CB  . ARG   B 10  ? 0.1749 0.1767 0.2582 -0.0005 0.0205  0.0356  16  ARG   C CB  
1158 C CG  . ARG   B 10  ? 0.1918 0.1946 0.2728 -0.0011 0.0158  0.0362  16  ARG   C CG  
1159 C CD  . ARG   B 10  ? 0.1871 0.1938 0.2768 -0.0022 0.0127  0.0404  16  ARG   C CD  
1160 N NE  . ARG   B 10  ? 0.2044 0.2124 0.2948 -0.0017 0.0107  0.0417  16  ARG   C NE  
1161 C CZ  . ARG   B 10  ? 0.2124 0.2203 0.2972 -0.0024 0.0063  0.0422  16  ARG   C CZ  
1162 N NH1 . ARG   B 10  ? 0.2132 0.2191 0.2904 -0.0038 0.0033  0.0409  16  ARG   C NH1 
1163 N NH2 . ARG   B 10  ? 0.2159 0.2249 0.3020 -0.0017 0.0053  0.0440  16  ARG   C NH2 
1164 N N   . VAL   B 11  ? 0.1592 0.1539 0.2197 0.0020  0.0207  0.0264  17  VAL   C N   
1165 C CA  . VAL   B 11  ? 0.1567 0.1506 0.2137 0.0031  0.0205  0.0236  17  VAL   C CA  
1166 C C   . VAL   B 11  ? 0.1572 0.1525 0.2142 0.0023  0.0170  0.0251  17  VAL   C C   
1167 O O   . VAL   B 11  ? 0.1639 0.1585 0.2160 0.0014  0.0141  0.0256  17  VAL   C O   
1168 C CB  . VAL   B 11  ? 0.1682 0.1592 0.2160 0.0039  0.0206  0.0201  17  VAL   C CB  
1169 C CG1 . VAL   B 11  ? 0.1969 0.1876 0.2432 0.0049  0.0206  0.0172  17  VAL   C CG1 
1170 C CG2 . VAL   B 11  ? 0.1822 0.1711 0.2276 0.0047  0.0237  0.0193  17  VAL   C CG2 
1171 N N   . VAL   B 12  ? 0.1466 0.1434 0.2085 0.0027  0.0175  0.0258  18  VAL   C N   
1172 C CA  A VAL   B 12  ? 0.1421 0.1401 0.2034 0.0023  0.0148  0.0276  18  VAL   C CA  
1173 C CA  B VAL   B 12  ? 0.1642 0.1622 0.2257 0.0023  0.0148  0.0277  18  VAL   C CA  
1174 C C   . VAL   B 12  ? 0.1570 0.1548 0.2190 0.0032  0.0161  0.0260  18  VAL   C C   
1175 O O   . VAL   B 12  ? 0.1658 0.1628 0.2304 0.0040  0.0188  0.0236  18  VAL   C O   
1176 C CB  A VAL   B 12  ? 0.1375 0.1382 0.2061 0.0017  0.0136  0.0320  18  VAL   C CB  
1177 C CB  B VAL   B 12  ? 0.2024 0.2032 0.2719 0.0017  0.0139  0.0321  18  VAL   C CB  
1178 C CG1 A VAL   B 12  ? 0.1524 0.1538 0.2204 0.0002  0.0108  0.0339  18  VAL   C CG1 
1179 C CG1 B VAL   B 12  ? 0.2051 0.2071 0.2736 0.0013  0.0109  0.0347  18  VAL   C CG1 
1180 C CG2 A VAL   B 12  ? 0.1014 0.1035 0.1796 0.0026  0.0169  0.0330  18  VAL   C CG2 
1181 C CG2 B VAL   B 12  ? 0.2350 0.2365 0.3060 0.0005  0.0127  0.0336  18  VAL   C CG2 
1182 N N   . ASN   B 13  ? 0.1430 0.1412 0.2029 0.0031  0.0144  0.0273  19  ASN   C N   
1183 C CA  . ASN   B 13  ? 0.1500 0.1483 0.2124 0.0038  0.0160  0.0265  19  ASN   C CA  
1184 C C   . ASN   B 13  ? 0.1523 0.1520 0.2243 0.0041  0.0179  0.0290  19  ASN   C C   
1185 O O   . ASN   B 13  ? 0.1472 0.1485 0.2225 0.0038  0.0167  0.0328  19  ASN   C O   
1186 C CB  . ASN   B 13  ? 0.1569 0.1555 0.2158 0.0038  0.0144  0.0284  19  ASN   C CB  
1187 C CG  . ASN   B 13  ? 0.1559 0.1529 0.2060 0.0038  0.0128  0.0262  19  ASN   C CG  
1188 O OD1 . ASN   B 13  ? 0.1808 0.1771 0.2257 0.0032  0.0105  0.0269  19  ASN   C OD1 
1189 N ND2 . ASN   B 13  ? 0.1613 0.1578 0.2105 0.0045  0.0141  0.0233  19  ASN   C ND2 
1190 N N   . ARG   B 14  ? 0.1436 0.1426 0.2203 0.0047  0.0207  0.0267  20  ARG   C N   
1191 C CA  . ARG   B 14  ? 0.1373 0.1369 0.2235 0.0052  0.0230  0.0288  20  ARG   C CA  
1192 C C   . ARG   B 14  ? 0.1570 0.1583 0.2466 0.0052  0.0219  0.0338  20  ARG   C C   
1193 O O   . ARG   B 14  ? 0.1573 0.1600 0.2533 0.0055  0.0221  0.0375  20  ARG   C O   
1194 C CB  . ARG   B 14  ? 0.1360 0.1338 0.2260 0.0057  0.0258  0.0250  20  ARG   C CB  
1195 C CG  . ARG   B 14  ? 0.1540 0.1515 0.2538 0.0063  0.0289  0.0263  20  ARG   C CG  
1196 C CD  . ARG   B 14  ? 0.1663 0.1615 0.2695 0.0065  0.0313  0.0221  20  ARG   C CD  
1197 N NE  . ARG   B 14  ? 0.1643 0.1580 0.2765 0.0073  0.0347  0.0222  20  ARG   C NE  
1198 C CZ  . ARG   B 14  ? 0.1695 0.1634 0.2902 0.0076  0.0362  0.0254  20  ARG   C CZ  
1199 N NH1 . ARG   B 14  ? 0.1817 0.1775 0.3026 0.0073  0.0344  0.0297  20  ARG   C NH1 
1200 N NH2 . ARG   B 14  ? 0.1608 0.1527 0.2896 0.0084  0.0396  0.0247  20  ARG   C NH2 
1201 N N   . HIS   B 15  ? 0.1458 0.1469 0.2308 0.0051  0.0208  0.0342  21  HIS   C N   
1202 C CA  . HIS   B 15  ? 0.1603 0.1625 0.2471 0.0054  0.0202  0.0392  21  HIS   C CA  
1203 C C   . HIS   B 15  ? 0.1732 0.1770 0.2566 0.0050  0.0166  0.0430  21  HIS   C C   
1204 O O   . HIS   B 15  ? 0.1955 0.2002 0.2806 0.0054  0.0157  0.0475  21  HIS   C O   
1205 C CB  . HIS   B 15  ? 0.1647 0.1662 0.2481 0.0056  0.0209  0.0389  21  HIS   C CB  
1206 C CG  . HIS   B 15  ? 0.1604 0.1613 0.2334 0.0053  0.0186  0.0377  21  HIS   C CG  
1207 N ND1 . HIS   B 15  ? 0.1805 0.1805 0.2492 0.0051  0.0185  0.0330  21  HIS   C ND1 
1208 C CD2 . HIS   B 15  ? 0.1783 0.1793 0.2447 0.0054  0.0166  0.0405  21  HIS   C CD2 
1209 C CE1 . HIS   B 15  ? 0.1944 0.1938 0.2547 0.0050  0.0166  0.0332  21  HIS   C CE1 
1210 N NE2 . HIS   B 15  ? 0.1848 0.1846 0.2431 0.0052  0.0155  0.0374  21  HIS   C NE2 
1211 N N   . LEU   B 16  ? 0.1615 0.1652 0.2402 0.0042  0.0145  0.0412  22  LEU   C N   
1212 C CA  . LEU   B 16  ? 0.1784 0.1835 0.2548 0.0035  0.0107  0.0442  22  LEU   C CA  
1213 C C   . LEU   B 16  ? 0.1839 0.1908 0.2678 0.0032  0.0107  0.0453  22  LEU   C C   
1214 O O   . LEU   B 16  ? 0.1967 0.2050 0.2799 0.0022  0.0073  0.0472  22  LEU   C O   
1215 C CB  . LEU   B 16  ? 0.1820 0.1854 0.2478 0.0026  0.0081  0.0418  22  LEU   C CB  
1216 C CG  . LEU   B 16  ? 0.1944 0.1963 0.2529 0.0031  0.0083  0.0413  22  LEU   C CG  
1217 C CD1 . LEU   B 16  ? 0.2108 0.2106 0.2595 0.0025  0.0062  0.0385  22  LEU   C CD1 
1218 C CD2 . LEU   B 16  ? 0.1990 0.2016 0.2570 0.0036  0.0071  0.0459  22  LEU   C CD2 
1219 N N   . ALA   B 17  ? 0.1818 0.1884 0.2726 0.0039  0.0146  0.0435  23  ALA   C N   
1220 C CA  . ALA   B 17  ? 0.1786 0.1867 0.2768 0.0039  0.0156  0.0445  23  ALA   C CA  
1221 C C   . ALA   B 17  ? 0.1909 0.2022 0.2969 0.0040  0.0136  0.0500  23  ALA   C C   
1222 O O   . ALA   B 17  ? 0.1901 0.2019 0.2991 0.0049  0.0136  0.0530  23  ALA   C O   
1223 C CB  . ALA   B 17  ? 0.1889 0.1954 0.2921 0.0049  0.0205  0.0415  23  ALA   C CB  
1224 N N   . THR   B 18  ? 0.1786 0.1921 0.2885 0.0033  0.0120  0.0516  24  THR   C N   
1225 C CA  . THR   B 18  ? 0.1811 0.1983 0.2996 0.0034  0.0094  0.0570  24  THR   C CA  
1226 C C   . THR   B 18  ? 0.1806 0.1992 0.3120 0.0049  0.0138  0.0585  24  THR   C C   
1227 O O   . THR   B 18  ? 0.1875 0.2038 0.3200 0.0056  0.0187  0.0549  24  THR   C O   
1228 C CB  . THR   B 18  ? 0.2017 0.2210 0.3194 0.0015  0.0050  0.0581  24  THR   C CB  
1229 O OG1 . THR   B 18  ? 0.2051 0.2242 0.3268 0.0013  0.0084  0.0559  24  THR   C OG1 
1230 C CG2 . THR   B 18  ? 0.2229 0.2401 0.3277 0.0000  0.0008  0.0562  24  THR   C CG2 
1231 N N   . HIS   B 19  ? 0.1842 0.2065 0.3255 0.0054  0.0119  0.0639  25  HIS   C N   
1232 C CA  . HIS   B 19  ? 0.1971 0.2210 0.3517 0.0070  0.0161  0.0657  25  HIS   C CA  
1233 C C   . HIS   B 19  ? 0.1790 0.2032 0.3362 0.0064  0.0186  0.0633  25  HIS   C C   
1234 O O   . HIS   B 19  ? 0.1876 0.2100 0.3493 0.0078  0.0244  0.0611  25  HIS   C O   
1235 C CB  . HIS   B 19  ? 0.2161 0.2447 0.3812 0.0076  0.0126  0.0724  25  HIS   C CB  
1236 C CG  . HIS   B 19  ? 0.2395 0.2705 0.4197 0.0091  0.0165  0.0746  25  HIS   C CG  
1237 N ND1 . HIS   B 19  ? 0.2713 0.3001 0.4583 0.0114  0.0224  0.0742  25  HIS   C ND1 
1238 C CD2 . HIS   B 19  ? 0.2663 0.3011 0.4554 0.0087  0.0161  0.0765  25  HIS   C CD2 
1239 C CE1 . HIS   B 19  ? 0.2677 0.2993 0.4677 0.0125  0.0250  0.0765  25  HIS   C CE1 
1240 N NE2 . HIS   B 19  ? 0.2707 0.3061 0.4726 0.0109  0.0216  0.0779  25  HIS   C NE2 
1241 N N   . ASN   B 20  ? 0.1766 0.2023 0.3301 0.0044  0.0147  0.0634  26  ASN   C N   
1242 C CA  . ASN   B 20  ? 0.1884 0.2142 0.3444 0.0038  0.0175  0.0616  26  ASN   C CA  
1243 C C   . ASN   B 20  ? 0.1762 0.1971 0.3235 0.0044  0.0224  0.0558  26  ASN   C C   
1244 O O   . ASN   B 20  ? 0.1715 0.1914 0.3225 0.0053  0.0276  0.0543  26  ASN   C O   
1245 C CB  . ASN   B 20  ? 0.2142 0.2420 0.3679 0.0013  0.0124  0.0625  26  ASN   C CB  
1246 C CG  . ASN   B 20  ? 0.2950 0.3233 0.4536 0.0008  0.0159  0.0617  26  ASN   C CG  
1247 O OD1 . ASN   B 20  ? 0.3184 0.3500 0.4901 0.0015  0.0183  0.0647  26  ASN   C OD1 
1248 N ND2 . ASN   B 20  ? 0.3258 0.3506 0.4745 -0.0002 0.0169  0.0578  26  ASN   C ND2 
1249 N N   . ASP   B 21  ? 0.1730 0.1907 0.3085 0.0040  0.0209  0.0527  27  ASP   C N   
1250 C CA  . ASP   B 21  ? 0.1774 0.1908 0.3051 0.0046  0.0248  0.0473  27  ASP   C CA  
1251 C C   . ASP   B 21  ? 0.1691 0.1807 0.3026 0.0067  0.0304  0.0459  27  ASP   C C   
1252 O O   . ASP   B 21  ? 0.1775 0.1866 0.3096 0.0075  0.0349  0.0426  27  ASP   C O   
1253 C CB  . ASP   B 21  ? 0.1707 0.1816 0.2868 0.0040  0.0221  0.0447  27  ASP   C CB  
1254 C CG  . ASP   B 21  ? 0.1870 0.1977 0.2947 0.0022  0.0176  0.0444  27  ASP   C CG  
1255 O OD1 . ASP   B 21  ? 0.1916 0.2023 0.2988 0.0014  0.0179  0.0438  27  ASP   C OD1 
1256 O OD2 . ASP   B 21  ? 0.1840 0.1945 0.2857 0.0017  0.0141  0.0448  27  ASP   C OD2 
1257 N N   . TRP   B 22  ? 0.1660 0.1785 0.3055 0.0076  0.0303  0.0482  28  TRP   C N   
1258 C CA  . TRP   B 22  ? 0.1660 0.1763 0.3116 0.0095  0.0355  0.0468  28  TRP   C CA  
1259 C C   . TRP   B 22  ? 0.1626 0.1744 0.3192 0.0108  0.0398  0.0485  28  TRP   C C   
1260 O O   . TRP   B 22  ? 0.1698 0.1783 0.3278 0.0122  0.0453  0.0453  28  TRP   C O   
1261 C CB  . TRP   B 22  ? 0.1609 0.1717 0.3114 0.0101  0.0344  0.0496  28  TRP   C CB  
1262 C CG  . TRP   B 22  ? 0.1602 0.1682 0.3015 0.0095  0.0332  0.0466  28  TRP   C CG  
1263 C CD1 . TRP   B 22  ? 0.1691 0.1781 0.3040 0.0085  0.0287  0.0482  28  TRP   C CD1 
1264 C CD2 . TRP   B 22  ? 0.1551 0.1590 0.2934 0.0100  0.0365  0.0413  28  TRP   C CD2 
1265 N NE1 . TRP   B 22  ? 0.1816 0.1877 0.3109 0.0084  0.0295  0.0448  28  TRP   C NE1 
1266 C CE2 . TRP   B 22  ? 0.1712 0.1744 0.3026 0.0091  0.0339  0.0405  28  TRP   C CE2 
1267 C CE3 . TRP   B 22  ? 0.1818 0.1824 0.3228 0.0111  0.0415  0.0373  28  TRP   C CE3 
1268 C CZ2 . TRP   B 22  ? 0.1776 0.1775 0.3065 0.0091  0.0357  0.0361  28  TRP   C CZ2 
1269 C CZ3 . TRP   B 22  ? 0.2004 0.1973 0.3371 0.0110  0.0428  0.0323  28  TRP   C CZ3 
1270 C CH2 . TRP   B 22  ? 0.1915 0.1884 0.3230 0.0099  0.0397  0.0319  28  TRP   C CH2 
1271 N N   . ALA   B 23  ? 0.1590 0.1753 0.3226 0.0102  0.0373  0.0532  29  ALA   C N   
1272 C CA  . ALA   B 23  ? 0.1759 0.1944 0.3512 0.0113  0.0413  0.0555  29  ALA   C CA  
1273 C C   . ALA   B 23  ? 0.1955 0.2121 0.3661 0.0111  0.0451  0.0522  29  ALA   C C   
1274 O O   . ALA   B 23  ? 0.2097 0.2271 0.3888 0.0124  0.0500  0.0532  29  ALA   C O   
1275 C CB  . ALA   B 23  ? 0.1811 0.2056 0.3664 0.0106  0.0368  0.0618  29  ALA   C CB  
1276 N N   . ASN   B 24  ? 0.1912 0.2054 0.3486 0.0096  0.0428  0.0487  30  ASN   C N   
1277 C CA  . ASN   B 24  ? 0.1782 0.1901 0.3293 0.0094  0.0460  0.0459  30  ASN   C CA  
1278 C C   . ASN   B 24  ? 0.1828 0.1894 0.3201 0.0097  0.0469  0.0399  30  ASN   C C   
1279 O O   . ASN   B 24  ? 0.1868 0.1915 0.3143 0.0087  0.0459  0.0377  30  ASN   C O   
1280 C CB  . ASN   B 24  ? 0.1927 0.2074 0.3427 0.0070  0.0415  0.0484  30  ASN   C CB  
1281 C CG  . ASN   B 24  ? 0.2066 0.2268 0.3713 0.0067  0.0409  0.0538  30  ASN   C CG  
1282 O OD1 . ASN   B 24  ? 0.2305 0.2515 0.4030 0.0076  0.0461  0.0549  30  ASN   C OD1 
1283 N ND2 . ASN   B 24  ? 0.2218 0.2458 0.3911 0.0056  0.0348  0.0575  30  ASN   C ND2 
1284 N N   . LEU   B 25  ? 0.1915 0.1955 0.3285 0.0109  0.0485  0.0375  31  LEU   C N   
1285 C CA  . LEU   B 25  ? 0.1875 0.1872 0.3130 0.0109  0.0482  0.0321  31  LEU   C CA  
1286 C C   . LEU   B 25  ? 0.2037 0.1993 0.3213 0.0119  0.0525  0.0276  31  LEU   C C   
1287 O O   . LEU   B 25  ? 0.2210 0.2152 0.3431 0.0135  0.0581  0.0272  31  LEU   C O   
1288 C CB  . LEU   B 25  ? 0.1958 0.1942 0.3258 0.0118  0.0492  0.0310  31  LEU   C CB  
1289 C CG  . LEU   B 25  ? 0.2059 0.2005 0.3262 0.0116  0.0483  0.0256  31  LEU   C CG  
1290 C CD1 . LEU   B 25  ? 0.2101 0.2062 0.3231 0.0099  0.0426  0.0262  31  LEU   C CD1 
1291 C CD2 . LEU   B 25  ? 0.2224 0.2151 0.3487 0.0124  0.0502  0.0244  31  LEU   C CD2 
1292 N N   . VAL   B 26  ? 0.1965 0.1900 0.3020 0.0111  0.0501  0.0244  32  VAL   C N   
1293 C CA  . VAL   B 26  ? 0.2059 0.1950 0.3017 0.0122  0.0534  0.0198  32  VAL   C CA  
1294 C C   . VAL   B 26  ? 0.2164 0.2021 0.3060 0.0126  0.0524  0.0145  32  VAL   C C   
1295 O O   . VAL   B 26  ? 0.2348 0.2166 0.3219 0.0140  0.0563  0.0105  32  VAL   C O   
1296 C CB  . VAL   B 26  ? 0.2179 0.2069 0.3047 0.0112  0.0512  0.0201  32  VAL   C CB  
1297 C CG1 . VAL   B 26  ? 0.2480 0.2322 0.3231 0.0126  0.0539  0.0155  32  VAL   C CG1 
1298 C CG2 . VAL   B 26  ? 0.2119 0.2038 0.3055 0.0107  0.0524  0.0250  32  VAL   C CG2 
1299 N N   . TRP   B 27  ? 0.1982 0.1853 0.2856 0.0113  0.0474  0.0144  33  TRP   C N   
1300 C CA  . TRP   B 27  ? 0.1957 0.1802 0.2783 0.0113  0.0461  0.0097  33  TRP   C CA  
1301 C C   . TRP   B 27  ? 0.1908 0.1780 0.2759 0.0099  0.0416  0.0116  33  TRP   C C   
1302 O O   . TRP   B 27  ? 0.1933 0.1834 0.2779 0.0090  0.0386  0.0152  33  TRP   C O   
1303 C CB  . TRP   B 27  ? 0.2131 0.1948 0.2829 0.0116  0.0451  0.0056  33  TRP   C CB  
1304 C CG  . TRP   B 27  ? 0.2210 0.2011 0.2853 0.0113  0.0421  0.0011  33  TRP   C CG  
1305 C CD1 . TRP   B 27  ? 0.2451 0.2219 0.3081 0.0119  0.0434  -0.0039 33  TRP   C CD1 
1306 C CD2 . TRP   B 27  ? 0.2070 0.1888 0.2672 0.0102  0.0373  0.0012  33  TRP   C CD2 
1307 N NE1 . TRP   B 27  ? 0.2512 0.2280 0.3100 0.0111  0.0393  -0.0069 33  TRP   C NE1 
1308 C CE2 . TRP   B 27  ? 0.2237 0.2037 0.2809 0.0102  0.0358  -0.0037 33  TRP   C CE2 
1309 C CE3 . TRP   B 27  ? 0.2088 0.1935 0.2680 0.0092  0.0341  0.0048  33  TRP   C CE3 
1310 C CZ2 . TRP   B 27  ? 0.2276 0.2089 0.2815 0.0095  0.0316  -0.0047 33  TRP   C CZ2 
1311 C CZ3 . TRP   B 27  ? 0.2207 0.2059 0.2751 0.0087  0.0303  0.0034  33  TRP   C CZ3 
1312 C CH2 . TRP   B 27  ? 0.2257 0.2097 0.2786 0.0089  0.0292  -0.0010 33  TRP   C CH2 
1313 N N   . GLU   B 28  ? 0.1875 0.1736 0.2754 0.0099  0.0414  0.0093  34  GLU   C N   
1314 C CA  . GLU   B 28  ? 0.1925 0.1808 0.2821 0.0088  0.0378  0.0110  34  GLU   C CA  
1315 C C   . GLU   B 28  ? 0.1925 0.1787 0.2808 0.0086  0.0372  0.0064  34  GLU   C C   
1316 O O   . GLU   B 28  ? 0.1902 0.1733 0.2801 0.0092  0.0399  0.0025  34  GLU   C O   
1317 C CB  . GLU   B 28  ? 0.1913 0.1822 0.2910 0.0087  0.0381  0.0162  34  GLU   C CB  
1318 C CG  . GLU   B 28  ? 0.2038 0.1930 0.3126 0.0097  0.0421  0.0160  34  GLU   C CG  
1319 C CD  . GLU   B 28  ? 0.2297 0.2169 0.3426 0.0096  0.0428  0.0134  34  GLU   C CD  
1320 O OE1 . GLU   B 28  ? 0.2729 0.2571 0.3907 0.0105  0.0464  0.0109  34  GLU   C OE1 
1321 O OE2 . GLU   B 28  ? 0.2097 0.1980 0.3211 0.0086  0.0400  0.0139  34  GLU   C OE2 
1322 N N   . ASP   B 29  ? 0.1772 0.1649 0.2632 0.0076  0.0339  0.0066  35  ASP   C N   
1323 C CA  . ASP   B 29  ? 0.1782 0.1647 0.2647 0.0072  0.0330  0.0026  35  ASP   C CA  
1324 C C   . ASP   B 29  ? 0.1762 0.1653 0.2661 0.0063  0.0310  0.0057  35  ASP   C C   
1325 O O   . ASP   B 29  ? 0.1781 0.1689 0.2625 0.0060  0.0284  0.0070  35  ASP   C O   
1326 C CB  . ASP   B 29  ? 0.1910 0.1760 0.2678 0.0074  0.0310  -0.0022 35  ASP   C CB  
1327 C CG  . ASP   B 29  ? 0.2749 0.2588 0.3524 0.0068  0.0295  -0.0068 35  ASP   C CG  
1328 O OD1 . ASP   B 29  ? 0.2784 0.2641 0.3622 0.0059  0.0287  -0.0055 35  ASP   C OD1 
1329 O OD2 . ASP   B 29  ? 0.2948 0.2764 0.3662 0.0072  0.0288  -0.0116 35  ASP   C OD2 
1330 N N   . SER   B 30  ? 0.1709 0.1599 0.2698 0.0061  0.0326  0.0070  36  SER   C N   
1331 C CA  A SER   B 30  ? 0.1708 0.1620 0.2732 0.0055  0.0316  0.0104  36  SER   C CA  
1332 C CA  B SER   B 30  ? 0.1755 0.1667 0.2775 0.0055  0.0315  0.0105  36  SER   C CA  
1333 C C   . SER   B 30  ? 0.1781 0.1698 0.2768 0.0048  0.0293  0.0074  36  SER   C C   
1334 O O   . SER   B 30  ? 0.1726 0.1664 0.2689 0.0046  0.0279  0.0101  36  SER   C O   
1335 C CB  A SER   B 30  ? 0.1857 0.1759 0.2988 0.0054  0.0343  0.0121  36  SER   C CB  
1336 C CB  B SER   B 30  ? 0.2026 0.1932 0.3152 0.0055  0.0341  0.0129  36  SER   C CB  
1337 O OG  A SER   B 30  ? 0.1801 0.1719 0.2965 0.0049  0.0339  0.0149  36  SER   C OG  
1338 O OG  B SER   B 30  ? 0.2218 0.2095 0.3385 0.0052  0.0356  0.0078  36  SER   C OG  
1339 N N   . SER   B 31  ? 0.1795 0.1694 0.2776 0.0046  0.0289  0.0017  37  SER   C N   
1340 C CA  . SER   B 31  ? 0.1769 0.1679 0.2730 0.0040  0.0264  -0.0012 37  SER   C CA  
1341 C C   . SER   B 31  ? 0.1714 0.1639 0.2578 0.0045  0.0238  -0.0005 37  SER   C C   
1342 O O   . SER   B 31  ? 0.1791 0.1734 0.2649 0.0043  0.0221  -0.0007 37  SER   C O   
1343 C CB  . SER   B 31  ? 0.2283 0.2171 0.3251 0.0035  0.0257  -0.0075 37  SER   C CB  
1344 O OG  . SER   B 31  ? 0.3067 0.2938 0.3943 0.0043  0.0245  -0.0107 37  SER   C OG  
1345 N N   . ARG   B 32  ? 0.1719 0.1637 0.2518 0.0052  0.0238  0.0005  38  ARG   C N   
1346 C CA  . ARG   B 32  ? 0.1668 0.1595 0.2380 0.0056  0.0215  0.0013  38  ARG   C CA  
1347 C C   . ARG   B 32  ? 0.1647 0.1589 0.2350 0.0055  0.0215  0.0066  38  ARG   C C   
1348 O O   . ARG   B 32  ? 0.1601 0.1547 0.2237 0.0058  0.0198  0.0075  38  ARG   C O   
1349 C CB  . ARG   B 32  ? 0.1899 0.1806 0.2541 0.0063  0.0215  -0.0008 38  ARG   C CB  
1350 C CG  . ARG   B 32  ? 0.2028 0.1916 0.2648 0.0066  0.0208  -0.0063 38  ARG   C CG  
1351 C CD  . ARG   B 32  ? 0.1792 0.1655 0.2332 0.0076  0.0214  -0.0082 38  ARG   C CD  
1352 N NE  . ARG   B 32  ? 0.1745 0.1612 0.2203 0.0081  0.0194  -0.0068 38  ARG   C NE  
1353 C CZ  . ARG   B 32  ? 0.1781 0.1628 0.2153 0.0091  0.0187  -0.0089 38  ARG   C CZ  
1354 N NH1 . ARG   B 32  ? 0.1941 0.1762 0.2285 0.0098  0.0197  -0.0127 38  ARG   C NH1 
1355 N NH2 . ARG   B 32  ? 0.1820 0.1670 0.2129 0.0096  0.0170  -0.0072 38  ARG   C NH2 
1356 N N   . ASP   B 33  ? 0.1469 0.1417 0.2236 0.0053  0.0233  0.0101  39  ASP   C N   
1357 C CA  . ASP   B 33  ? 0.1488 0.1449 0.2245 0.0052  0.0228  0.0151  39  ASP   C CA  
1358 C C   . ASP   B 33  ? 0.1455 0.1411 0.2161 0.0053  0.0220  0.0156  39  ASP   C C   
1359 O O   . ASP   B 33  ? 0.1502 0.1464 0.2164 0.0051  0.0202  0.0181  39  ASP   C O   
1360 C CB  . ASP   B 33  ? 0.1554 0.1526 0.2277 0.0052  0.0213  0.0169  39  ASP   C CB  
1361 C CG  . ASP   B 33  ? 0.1737 0.1717 0.2443 0.0051  0.0205  0.0218  39  ASP   C CG  
1362 O OD1 . ASP   B 33  ? 0.1775 0.1761 0.2536 0.0050  0.0215  0.0248  39  ASP   C OD1 
1363 O OD2 . ASP   B 33  ? 0.1604 0.1585 0.2244 0.0051  0.0188  0.0226  39  ASP   C OD2 
1364 N N   . LEU   B 34  ? 0.1475 0.1417 0.2188 0.0057  0.0236  0.0134  40  LEU   C N   
1365 C CA  . LEU   B 34  ? 0.1491 0.1429 0.2167 0.0058  0.0235  0.0144  40  LEU   C CA  
1366 C C   . LEU   B 34  ? 0.1475 0.1414 0.2217 0.0061  0.0262  0.0161  40  LEU   C C   
1367 O O   . LEU   B 34  ? 0.1565 0.1493 0.2360 0.0066  0.0287  0.0145  40  LEU   C O   
1368 C CB  . LEU   B 34  ? 0.1564 0.1482 0.2167 0.0063  0.0234  0.0104  40  LEU   C CB  
1369 C CG  . LEU   B 34  ? 0.1649 0.1565 0.2178 0.0063  0.0206  0.0089  40  LEU   C CG  
1370 C CD1 . LEU   B 34  ? 0.1870 0.1764 0.2328 0.0072  0.0206  0.0055  40  LEU   C CD1 
1371 C CD2 . LEU   B 34  ? 0.1810 0.1734 0.2307 0.0058  0.0187  0.0123  40  LEU   C CD2 
1372 N N   . LEU   B 35  ? 0.1437 0.1386 0.2178 0.0058  0.0258  0.0191  41  LEU   C N   
1373 C CA  . LEU   B 35  ? 0.1491 0.1445 0.2300 0.0062  0.0285  0.0210  41  LEU   C CA  
1374 C C   . LEU   B 35  ? 0.1593 0.1548 0.2365 0.0059  0.0282  0.0220  41  LEU   C C   
1375 O O   . LEU   B 35  ? 0.1758 0.1720 0.2484 0.0049  0.0251  0.0233  41  LEU   C O   
1376 C CB  . LEU   B 35  ? 0.1474 0.1454 0.2368 0.0060  0.0279  0.0257  41  LEU   C CB  
1377 C CG  . LEU   B 35  ? 0.1505 0.1497 0.2489 0.0066  0.0306  0.0283  41  LEU   C CG  
1378 C CD1 . LEU   B 35  ? 0.1738 0.1742 0.2816 0.0072  0.0315  0.0312  41  LEU   C CD1 
1379 C CD2 . LEU   B 35  ? 0.1562 0.1577 0.2553 0.0058  0.0288  0.0318  41  LEU   C CD2 
1380 N N   . VAL   B 36  ? 0.1602 0.1545 0.2393 0.0067  0.0318  0.0211  42  VAL   C N   
1381 C CA  . VAL   B 36  ? 0.1606 0.1549 0.2378 0.0064  0.0326  0.0223  42  VAL   C CA  
1382 C C   . VAL   B 36  ? 0.1599 0.1562 0.2474 0.0068  0.0355  0.0257  42  VAL   C C   
1383 O O   . VAL   B 36  ? 0.1697 0.1650 0.2622 0.0080  0.0393  0.0246  42  VAL   C O   
1384 C CB  . VAL   B 36  ? 0.1691 0.1598 0.2376 0.0074  0.0349  0.0184  42  VAL   C CB  
1385 C CG1 . VAL   B 36  ? 0.1893 0.1797 0.2564 0.0073  0.0365  0.0203  42  VAL   C CG1 
1386 C CG2 . VAL   B 36  ? 0.1829 0.1721 0.2423 0.0073  0.0316  0.0154  42  VAL   C CG2 
1387 N N   . SER   B 37  ? 0.1508 0.1496 0.2418 0.0056  0.0338  0.0295  43  SER   C N   
1388 C CA  . SER   B 37  ? 0.1543 0.1558 0.2564 0.0058  0.0361  0.0331  43  SER   C CA  
1389 C C   . SER   B 37  ? 0.1713 0.1725 0.2725 0.0053  0.0379  0.0340  43  SER   C C   
1390 O O   . SER   B 37  ? 0.1704 0.1697 0.2628 0.0045  0.0363  0.0326  43  SER   C O   
1391 C CB  . SER   B 37  ? 0.1785 0.1840 0.2880 0.0047  0.0319  0.0375  43  SER   C CB  
1392 O OG  . SER   B 37  ? 0.1889 0.1954 0.2935 0.0028  0.0269  0.0386  43  SER   C OG  
1393 N N   . SER   B 38  ? 0.1770 0.1801 0.2881 0.0059  0.0416  0.0367  44  SER   C N   
1394 C CA  . SER   B 38  ? 0.1933 0.1966 0.3058 0.0054  0.0440  0.0382  44  SER   C CA  
1395 C C   . SER   B 38  ? 0.2114 0.2189 0.3311 0.0030  0.0395  0.0426  44  SER   C C   
1396 O O   . SER   B 38  ? 0.2226 0.2336 0.3497 0.0024  0.0359  0.0452  44  SER   C O   
1397 C CB  . SER   B 38  ? 0.2227 0.2257 0.3423 0.0073  0.0512  0.0387  44  SER   C CB  
1398 O OG  . SER   B 38  ? 0.2816 0.2886 0.4147 0.0076  0.0512  0.0421  44  SER   C OG  
1399 N N   . THR   B 39  ? 0.2181 0.2249 0.3355 0.0017  0.0395  0.0433  45  THR   C N   
1400 C CA  . THR   B 39  ? 0.2199 0.2299 0.3436 -0.0009 0.0349  0.0467  45  THR   C CA  
1401 C C   . THR   B 39  ? 0.2443 0.2560 0.3774 -0.0013 0.0392  0.0496  45  THR   C C   
1402 O O   . THR   B 39  ? 0.2413 0.2501 0.3711 0.0003  0.0454  0.0484  45  THR   C O   
1403 C CB  . THR   B 39  ? 0.2275 0.2347 0.3398 -0.0026 0.0303  0.0448  45  THR   C CB  
1404 O OG1 . THR   B 39  ? 0.2335 0.2367 0.3383 -0.0019 0.0343  0.0430  45  THR   C OG1 
1405 C CG2 . THR   B 39  ? 0.2286 0.2340 0.3312 -0.0021 0.0267  0.0418  45  THR   C CG2 
1406 N N   . THR   B 40  ? 0.2684 0.2845 0.4126 -0.0034 0.0357  0.0534  46  THR   C N   
1407 C CA  . THR   B 40  ? 0.2939 0.3122 0.4490 -0.0042 0.0394  0.0567  46  THR   C CA  
1408 C C   . THR   B 40  ? 0.2981 0.3130 0.4459 -0.0060 0.0388  0.0559  46  THR   C C   
1409 O O   . THR   B 40  ? 0.3171 0.3302 0.4656 -0.0054 0.0449  0.0566  46  THR   C O   
1410 C CB  . THR   B 40  ? 0.3395 0.3644 0.5108 -0.0058 0.0354  0.0611  46  THR   C CB  
1411 O OG1 . THR   B 40  ? 0.3866 0.4124 0.5544 -0.0084 0.0268  0.0610  46  THR   C OG1 
1412 C CG2 . THR   B 40  ? 0.3342 0.3621 0.5130 -0.0036 0.0367  0.0623  46  THR   C CG2 
1413 N N   . ALA   B 41  ? 0.2780 0.2916 0.4183 -0.0081 0.0319  0.0544  47  ALA   C N   
1414 C CA  . ALA   B 41  ? 0.2833 0.2931 0.4168 -0.0098 0.0311  0.0536  47  ALA   C CA  
1415 C C   . ALA   B 41  ? 0.2694 0.2733 0.3863 -0.0079 0.0329  0.0496  47  ALA   C C   
1416 O O   . ALA   B 41  ? 0.2636 0.2667 0.3736 -0.0063 0.0318  0.0470  47  ALA   C O   
1417 C CB  . ALA   B 41  ? 0.2951 0.3061 0.4296 -0.0130 0.0228  0.0540  47  ALA   C CB  
1418 N N   . GLN   B 42  ? 0.2579 0.2579 0.3691 -0.0081 0.0354  0.0493  48  GLN   C N   
1419 C CA  . GLN   B 42  ? 0.2688 0.2633 0.3647 -0.0063 0.0367  0.0459  48  GLN   C CA  
1420 C C   . GLN   B 42  ? 0.2629 0.2554 0.3507 -0.0077 0.0300  0.0437  48  GLN   C C   
1421 O O   . GLN   B 42  ? 0.2827 0.2761 0.3747 -0.0104 0.0255  0.0449  48  GLN   C O   
1422 C CB  . GLN   B 42  ? 0.3243 0.3150 0.4170 -0.0058 0.0421  0.0471  48  GLN   C CB  
1423 C CG  . GLN   B 42  ? 0.4258 0.4169 0.5221 -0.0035 0.0501  0.0484  48  GLN   C CG  
1424 C CD  . GLN   B 42  ? 0.5517 0.5387 0.6434 -0.0028 0.0554  0.0498  48  GLN   C CD  
1425 O OE1 . GLN   B 42  ? 0.6049 0.5925 0.7046 -0.0049 0.0564  0.0532  48  GLN   C OE1 
1426 N NE2 . GLN   B 42  ? 0.5860 0.5686 0.6647 0.0001  0.0590  0.0475  48  GLN   C NE2 
1427 N N   . GLY   B 43  ? 0.2404 0.2305 0.3171 -0.0057 0.0295  0.0403  49  GLY   C N   
1428 C CA  . GLY   B 43  ? 0.2421 0.2300 0.3099 -0.0062 0.0243  0.0378  49  GLY   C CA  
1429 C C   . GLY   B 43  ? 0.2417 0.2244 0.2999 -0.0056 0.0254  0.0367  49  GLY   C C   
1430 O O   . GLY   B 43  ? 0.2733 0.2541 0.3299 -0.0043 0.0305  0.0375  49  GLY   C O   
1431 N N   . CYS   B 44  ? 0.2276 0.2080 0.2791 -0.0063 0.0211  0.0350  50  CYS   C N   
1432 C CA  . CYS   B 44  ? 0.2363 0.2117 0.2799 -0.0058 0.0216  0.0343  50  CYS   C CA  
1433 C C   . CYS   B 44  ? 0.2422 0.2150 0.2747 -0.0037 0.0201  0.0312  50  CYS   C C   
1434 O O   . CYS   B 44  ? 0.2782 0.2468 0.3041 -0.0031 0.0201  0.0308  50  CYS   C O   
1435 C CB  . CYS   B 44  ? 0.2419 0.2158 0.2890 -0.0088 0.0183  0.0355  50  CYS   C CB  
1436 S SG  . CYS   B 44  ? 0.3046 0.2819 0.3665 -0.0116 0.0198  0.0396  50  CYS   C SG  
1437 N N   . ASP   B 45  ? 0.2058 0.1809 0.2368 -0.0026 0.0188  0.0292  51  ASP   C N   
1438 C CA  . ASP   B 45  ? 0.2107 0.1841 0.2329 -0.0007 0.0174  0.0263  51  ASP   C CA  
1439 C C   . ASP   B 45  ? 0.2283 0.1999 0.2451 0.0019  0.0212  0.0255  51  ASP   C C   
1440 O O   . ASP   B 45  ? 0.2519 0.2247 0.2718 0.0024  0.0249  0.0264  51  ASP   C O   
1441 C CB  . ASP   B 45  ? 0.2166 0.1932 0.2403 -0.0004 0.0154  0.0247  51  ASP   C CB  
1442 C CG  . ASP   B 45  ? 0.2548 0.2325 0.2810 -0.0024 0.0113  0.0252  51  ASP   C CG  
1443 O OD1 . ASP   B 45  ? 0.2693 0.2443 0.2930 -0.0036 0.0092  0.0253  51  ASP   C OD1 
1444 O OD2 . ASP   B 45  ? 0.2279 0.2089 0.2585 -0.0027 0.0103  0.0256  51  ASP   C OD2 
1445 N N   . THR   B 46  ? 0.2113 0.1801 0.2196 0.0035  0.0202  0.0238  52  THR   C N   
1446 C CA  . THR   B 46  ? 0.2108 0.1779 0.2124 0.0061  0.0225  0.0227  52  THR   C CA  
1447 C C   . THR   B 46  ? 0.2096 0.1784 0.2082 0.0075  0.0202  0.0194  52  THR   C C   
1448 O O   . THR   B 46  ? 0.2160 0.1850 0.2137 0.0073  0.0170  0.0183  52  THR   C O   
1449 C CB  . THR   B 46  ? 0.2476 0.2103 0.2423 0.0071  0.0224  0.0236  52  THR   C CB  
1450 O OG1 . THR   B 46  ? 0.2712 0.2321 0.2695 0.0057  0.0249  0.0268  52  THR   C OG1 
1451 C CG2 . THR   B 46  ? 0.2802 0.2411 0.2663 0.0101  0.0238  0.0224  52  THR   C CG2 
1452 N N   . ILE   B 47  ? 0.2014 0.1712 0.1988 0.0090  0.0220  0.0177  53  ILE   C N   
1453 C CA  . ILE   B 47  ? 0.2026 0.1739 0.1980 0.0101  0.0199  0.0144  53  ILE   C CA  
1454 C C   . ILE   B 47  ? 0.2012 0.1701 0.1880 0.0123  0.0185  0.0131  53  ILE   C C   
1455 O O   . ILE   B 47  ? 0.2081 0.1743 0.1891 0.0136  0.0205  0.0138  53  ILE   C O   
1456 C CB  . ILE   B 47  ? 0.2122 0.1850 0.2099 0.0107  0.0222  0.0127  53  ILE   C CB  
1457 C CG1 . ILE   B 47  ? 0.2201 0.1952 0.2268 0.0090  0.0241  0.0146  53  ILE   C CG1 
1458 C CG2 . ILE   B 47  ? 0.2177 0.1921 0.2148 0.0115  0.0198  0.0093  53  ILE   C CG2 
1459 C CD1 . ILE   B 47  ? 0.2430 0.2208 0.2555 0.0073  0.0210  0.0154  53  ILE   C CD1 
1460 N N   . ALA   B 48  ? 0.1919 0.1618 0.1778 0.0128  0.0152  0.0114  54  ALA   C N   
1461 C CA  . ALA   B 48  ? 0.1890 0.1574 0.1680 0.0150  0.0133  0.0101  54  ALA   C CA  
1462 C C   . ALA   B 48  ? 0.1868 0.1555 0.1623 0.0165  0.0136  0.0075  54  ALA   C C   
1463 O O   . ALA   B 48  ? 0.1942 0.1653 0.1740 0.0158  0.0140  0.0055  54  ALA   C O   
1464 C CB  . ALA   B 48  ? 0.1960 0.1662 0.1770 0.0152  0.0101  0.0088  54  ALA   C CB  
1465 N N   . ARG   B 49  ? 0.1894 0.1555 0.1566 0.0186  0.0133  0.0076  55  ARG   C N   
1466 C CA  . ARG   B 49  ? 0.1982 0.1641 0.1601 0.0202  0.0128  0.0047  55  ARG   C CA  
1467 C C   . ARG   B 49  ? 0.2057 0.1714 0.1625 0.0222  0.0087  0.0039  55  ARG   C C   
1468 O O   . ARG   B 49  ? 0.2318 0.1945 0.1813 0.0240  0.0086  0.0060  55  ARG   C O   
1469 C CB  . ARG   B 49  ? 0.2104 0.1729 0.1661 0.0211  0.0168  0.0059  55  ARG   C CB  
1470 C CG  . ARG   B 49  ? 0.1996 0.1627 0.1620 0.0192  0.0211  0.0073  55  ARG   C CG  
1471 C CD  . ARG   B 49  ? 0.2161 0.1819 0.1848 0.0181  0.0213  0.0042  55  ARG   C CD  
1472 N NE  . ARG   B 49  ? 0.2150 0.1814 0.1906 0.0167  0.0254  0.0062  55  ARG   C NE  
1473 C CZ  . ARG   B 49  ? 0.2194 0.1885 0.2035 0.0153  0.0259  0.0051  55  ARG   C CZ  
1474 N NH1 . ARG   B 49  ? 0.2120 0.1831 0.1984 0.0152  0.0230  0.0020  55  ARG   C NH1 
1475 N NH2 . ARG   B 49  ? 0.2313 0.2012 0.2222 0.0142  0.0294  0.0074  55  ARG   C NH2 
1476 N N   . CYS   B 50  ? 0.1928 0.1619 0.1541 0.0220  0.0053  0.0013  56  CYS   C N   
1477 C CA  . CYS   B 50  ? 0.1898 0.1600 0.1498 0.0237  0.0012  0.0009  56  CYS   C CA  
1478 C C   . CYS   B 50  ? 0.1902 0.1647 0.1573 0.0231  -0.0016 -0.0023 56  CYS   C C   
1479 O O   . CYS   B 50  ? 0.1976 0.1740 0.1706 0.0213  -0.0003 -0.0039 56  CYS   C O   
1480 C CB  . CYS   B 50  ? 0.1930 0.1620 0.1549 0.0235  0.0017  0.0041  56  CYS   C CB  
1481 S SG  . CYS   B 50  ? 0.1934 0.1653 0.1656 0.0209  0.0025  0.0040  56  CYS   C SG  
1482 N N   . ASP   B 51  ? 0.2068 0.1831 0.1743 0.0246  -0.0054 -0.0028 57  ASP   C N   
1483 C CA  . ASP   B 51  ? 0.2104 0.1912 0.1862 0.0241  -0.0080 -0.0052 57  ASP   C CA  
1484 C C   . ASP   B 51  ? 0.2197 0.2017 0.2002 0.0245  -0.0084 -0.0032 57  ASP   C C   
1485 O O   . ASP   B 51  ? 0.2246 0.2100 0.2102 0.0253  -0.0111 -0.0044 57  ASP   C O   
1486 C CB  . ASP   B 51  ? 0.2377 0.2201 0.2112 0.0255  -0.0125 -0.0083 57  ASP   C CB  
1487 C CG  . ASP   B 51  ? 0.2948 0.2763 0.2622 0.0283  -0.0157 -0.0068 57  ASP   C CG  
1488 O OD1 . ASP   B 51  ? 0.2914 0.2704 0.2559 0.0292  -0.0140 -0.0034 57  ASP   C OD1 
1489 O OD2 . ASP   B 51  ? 0.3828 0.3661 0.3488 0.0295  -0.0202 -0.0092 57  ASP   C OD2 
1490 N N   . CYS   B 52  ? 0.2137 0.1930 0.1929 0.0240  -0.0056 -0.0004 58  CYS   C N   
1491 C CA  . CYS   B 52  ? 0.1989 0.1786 0.1818 0.0244  -0.0054 0.0011  58  CYS   C CA  
1492 C C   . CYS   B 52  ? 0.1832 0.1668 0.1747 0.0232  -0.0053 -0.0003 58  CYS   C C   
1493 O O   . CYS   B 52  ? 0.1856 0.1709 0.1808 0.0214  -0.0041 -0.0015 58  CYS   C O   
1494 C CB  . CYS   B 52  ? 0.1928 0.1687 0.1735 0.0233  -0.0025 0.0037  58  CYS   C CB  
1495 S SG  . CYS   B 52  ? 0.2101 0.1807 0.1821 0.0248  -0.0021 0.0064  58  CYS   C SG  
1496 N N   . GLN   B 53  ? 0.1773 0.1625 0.1724 0.0246  -0.0063 0.0000  59  GLN   C N   
1497 C CA  . GLN   B 53  ? 0.1897 0.1783 0.1928 0.0238  -0.0053 -0.0006 59  GLN   C CA  
1498 C C   . GLN   B 53  ? 0.1833 0.1697 0.1861 0.0242  -0.0031 0.0013  59  GLN   C C   
1499 O O   . GLN   B 53  ? 0.1798 0.1685 0.1882 0.0244  -0.0020 0.0011  59  GLN   C O   
1500 C CB  . GLN   B 53  ? 0.1835 0.1766 0.1930 0.0250  -0.0080 -0.0024 59  GLN   C CB  
1501 C CG  . GLN   B 53  ? 0.2213 0.2168 0.2329 0.0239  -0.0101 -0.0051 59  GLN   C CG  
1502 C CD  . GLN   B 53  ? 0.2745 0.2750 0.2944 0.0245  -0.0129 -0.0071 59  GLN   C CD  
1503 O OE1 . GLN   B 53  ? 0.2826 0.2842 0.3009 0.0256  -0.0170 -0.0086 59  GLN   C OE1 
1504 N NE2 . GLN   B 53  ? 0.2336 0.2370 0.2624 0.0236  -0.0109 -0.0068 59  GLN   C NE2 
1505 N N   . THR   B 54  ? 0.1872 0.1690 0.1834 0.0245  -0.0023 0.0029  60  THR   C N   
1506 C CA  . THR   B 54  ? 0.1909 0.1698 0.1860 0.0245  -0.0003 0.0042  60  THR   C CA  
1507 C C   . THR   B 54  ? 0.1888 0.1639 0.1793 0.0224  0.0011  0.0053  60  THR   C C   
1508 O O   . THR   B 54  ? 0.1986 0.1721 0.1856 0.0220  0.0006  0.0059  60  THR   C O   
1509 C CB  . THR   B 54  ? 0.2364 0.2130 0.2296 0.0271  -0.0008 0.0049  60  THR   C CB  
1510 O OG1 . THR   B 54  ? 0.2789 0.2522 0.2664 0.0279  -0.0020 0.0060  60  THR   C OG1 
1511 C CG2 . THR   B 54  ? 0.2397 0.2205 0.2386 0.0294  -0.0024 0.0041  60  THR   C CG2 
1512 N N   . GLY   B 55  ? 0.1716 0.1453 0.1622 0.0211  0.0027  0.0057  61  GLY   C N   
1513 C CA  . GLY   B 55  ? 0.1770 0.1476 0.1645 0.0188  0.0034  0.0068  61  GLY   C CA  
1514 C C   . GLY   B 55  ? 0.1721 0.1411 0.1590 0.0179  0.0045  0.0069  61  GLY   C C   
1515 O O   . GLY   B 55  ? 0.1895 0.1584 0.1768 0.0194  0.0052  0.0063  61  GLY   C O   
1516 N N   . VAL   B 56  ? 0.1642 0.1319 0.1500 0.0155  0.0046  0.0078  62  VAL   C N   
1517 C CA  . VAL   B 56  ? 0.1646 0.1303 0.1485 0.0143  0.0050  0.0078  62  VAL   C CA  
1518 C C   . VAL   B 56  ? 0.1630 0.1315 0.1497 0.0121  0.0049  0.0088  62  VAL   C C   
1519 O O   . VAL   B 56  ? 0.1788 0.1480 0.1672 0.0108  0.0045  0.0096  62  VAL   C O   
1520 C CB  . VAL   B 56  ? 0.1818 0.1418 0.1609 0.0134  0.0043  0.0081  62  VAL   C CB  
1521 C CG1 . VAL   B 56  ? 0.1998 0.1574 0.1760 0.0119  0.0039  0.0078  62  VAL   C CG1 
1522 C CG2 . VAL   B 56  ? 0.1911 0.1478 0.1676 0.0159  0.0046  0.0075  62  VAL   C CG2 
1523 N N   . TYR   B 57  ? 0.1627 0.1324 0.1498 0.0118  0.0056  0.0089  63  TYR   C N   
1524 C CA  . TYR   B 57  ? 0.1520 0.1241 0.1419 0.0099  0.0053  0.0102  63  TYR   C CA  
1525 C C   . TYR   B 57  ? 0.1674 0.1369 0.1529 0.0086  0.0045  0.0109  63  TYR   C C   
1526 O O   . TYR   B 57  ? 0.1854 0.1520 0.1661 0.0097  0.0050  0.0099  63  TYR   C O   
1527 C CB  . TYR   B 57  ? 0.1633 0.1400 0.1588 0.0105  0.0067  0.0105  63  TYR   C CB  
1528 C CG  . TYR   B 57  ? 0.1644 0.1415 0.1592 0.0114  0.0083  0.0107  63  TYR   C CG  
1529 C CD1 . TYR   B 57  ? 0.1746 0.1513 0.1687 0.0135  0.0096  0.0095  63  TYR   C CD1 
1530 C CD2 . TYR   B 57  ? 0.1703 0.1485 0.1656 0.0103  0.0087  0.0125  63  TYR   C CD2 
1531 C CE1 . TYR   B 57  ? 0.1872 0.1642 0.1809 0.0145  0.0118  0.0100  63  TYR   C CE1 
1532 C CE2 . TYR   B 57  ? 0.1787 0.1572 0.1729 0.0114  0.0107  0.0131  63  TYR   C CE2 
1533 C CZ  . TYR   B 57  ? 0.1863 0.1641 0.1796 0.0134  0.0125  0.0118  63  TYR   C CZ  
1534 O OH  . TYR   B 57  ? 0.2119 0.1898 0.2043 0.0146  0.0153  0.0126  63  TYR   C OH  
1535 N N   . TYR   B 58  ? 0.1639 0.1347 0.1513 0.0066  0.0032  0.0125  64  TYR   C N   
1536 C CA  . TYR   B 58  ? 0.1724 0.1414 0.1558 0.0053  0.0016  0.0132  64  TYR   C CA  
1537 C C   . TYR   B 58  ? 0.1749 0.1465 0.1592 0.0058  0.0027  0.0146  64  TYR   C C   
1538 O O   . TYR   B 58  ? 0.1720 0.1476 0.1625 0.0055  0.0034  0.0161  64  TYR   C O   
1539 C CB  . TYR   B 58  ? 0.1797 0.1487 0.1651 0.0028  -0.0010 0.0146  64  TYR   C CB  
1540 C CG  . TYR   B 58  ? 0.1960 0.1628 0.1765 0.0013  -0.0036 0.0150  64  TYR   C CG  
1541 C CD1 . TYR   B 58  ? 0.2054 0.1670 0.1782 0.0014  -0.0045 0.0131  64  TYR   C CD1 
1542 C CD2 . TYR   B 58  ? 0.1998 0.1696 0.1834 0.0000  -0.0053 0.0174  64  TYR   C CD2 
1543 C CE1 . TYR   B 58  ? 0.2186 0.1779 0.1856 0.0002  -0.0072 0.0130  64  TYR   C CE1 
1544 C CE2 . TYR   B 58  ? 0.2149 0.1828 0.1931 -0.0012 -0.0083 0.0179  64  TYR   C CE2 
1545 C CZ  . TYR   B 58  ? 0.2268 0.1893 0.1964 -0.0012 -0.0094 0.0155  64  TYR   C CZ  
1546 O OH  . TYR   B 58  ? 0.2681 0.2281 0.2310 -0.0023 -0.0127 0.0154  64  TYR   C OH  
1547 N N   . CYS   B 59  ? 0.1737 0.1426 0.1514 0.0065  0.0030  0.0141  65  CYS   C N   
1548 C CA  . CYS   B 59  ? 0.1810 0.1514 0.1577 0.0072  0.0045  0.0158  65  CYS   C CA  
1549 C C   . CYS   B 59  ? 0.1987 0.1669 0.1691 0.0057  0.0016  0.0169  65  CYS   C C   
1550 O O   . CYS   B 59  ? 0.2069 0.1704 0.1687 0.0060  0.0009  0.0153  65  CYS   C O   
1551 C CB  . CYS   B 59  ? 0.1827 0.1519 0.1566 0.0096  0.0078  0.0145  65  CYS   C CB  
1552 S SG  . CYS   B 59  ? 0.2148 0.1852 0.1867 0.0107  0.0105  0.0169  65  CYS   C SG  
1553 N N   . SER   B 60  ? 0.2094 0.1806 0.1840 0.0043  -0.0003 0.0195  66  SER   C N   
1554 C CA  . SER   B 60  ? 0.2177 0.1874 0.1872 0.0027  -0.0040 0.0207  66  SER   C CA  
1555 C C   . SER   B 60  ? 0.2211 0.1883 0.1814 0.0040  -0.0031 0.0212  66  SER   C C   
1556 O O   . SER   B 60  ? 0.2431 0.2062 0.1947 0.0033  -0.0060 0.0202  66  SER   C O   
1557 C CB  . SER   B 60  ? 0.2572 0.2313 0.2342 0.0014  -0.0058 0.0240  66  SER   C CB  
1558 O OG  . SER   B 60  ? 0.3178 0.2905 0.2899 -0.0001 -0.0101 0.0251  66  SER   C OG  
1559 N N   . SER   B 61  ? 0.2089 0.1780 0.1709 0.0061  0.0011  0.0225  67  SER   C N   
1560 C CA  . SER   B 61  ? 0.2195 0.1861 0.1726 0.0076  0.0030  0.0234  67  SER   C CA  
1561 C C   . SER   B 61  ? 0.2388 0.1999 0.1825 0.0090  0.0046  0.0201  67  SER   C C   
1562 O O   . SER   B 61  ? 0.2630 0.2211 0.1976 0.0104  0.0062  0.0204  67  SER   C O   
1563 C CB  . SER   B 61  ? 0.2327 0.2029 0.1917 0.0093  0.0075  0.0260  67  SER   C CB  
1564 O OG  . SER   B 61  ? 0.2412 0.2126 0.2059 0.0106  0.0111  0.0242  67  SER   C OG  
1565 N N   . ARG   B 62  ? 0.2231 0.1826 0.1684 0.0088  0.0042  0.0170  68  ARG   C N   
1566 C CA  . ARG   B 62  ? 0.2345 0.1882 0.1715 0.0100  0.0054  0.0136  68  ARG   C CA  
1567 C C   . ARG   B 62  ? 0.2459 0.1956 0.1796 0.0078  0.0010  0.0111  68  ARG   C C   
1568 O O   . ARG   B 62  ? 0.2614 0.2057 0.1887 0.0086  0.0015  0.0081  68  ARG   C O   
1569 C CB  . ARG   B 62  ? 0.2388 0.1935 0.1810 0.0122  0.0097  0.0123  68  ARG   C CB  
1570 C CG  . ARG   B 62  ? 0.2858 0.2442 0.2322 0.0142  0.0144  0.0145  68  ARG   C CG  
1571 C CD  . ARG   B 62  ? 0.2949 0.2493 0.2313 0.0162  0.0175  0.0143  68  ARG   C CD  
1572 N NE  . ARG   B 62  ? 0.3311 0.2889 0.2721 0.0181  0.0226  0.0168  68  ARG   C NE  
1573 C CZ  . ARG   B 62  ? 0.3753 0.3354 0.3167 0.0179  0.0236  0.0203  68  ARG   C CZ  
1574 N NH1 . ARG   B 62  ? 0.3874 0.3471 0.3248 0.0160  0.0194  0.0219  68  ARG   C NH1 
1575 N NH2 . ARG   B 62  ? 0.3697 0.3324 0.3158 0.0197  0.0288  0.0224  68  ARG   C NH2 
1576 N N   . ARG   B 63  ? 0.2490 0.2015 0.1885 0.0053  -0.0030 0.0124  69  ARG   C N   
1577 C CA  . ARG   B 63  ? 0.2608 0.2105 0.2004 0.0029  -0.0070 0.0106  69  ARG   C CA  
1578 C C   . ARG   B 63  ? 0.2750 0.2218 0.2156 0.0041  -0.0047 0.0079  69  ARG   C C   
1579 O O   . ARG   B 63  ? 0.3016 0.2426 0.2366 0.0034  -0.0062 0.0052  69  ARG   C O   
1580 C CB  . ARG   B 63  ? 0.2911 0.2356 0.2203 0.0015  -0.0109 0.0091  69  ARG   C CB  
1581 C CG  . ARG   B 63  ? 0.3277 0.2750 0.2560 0.0001  -0.0144 0.0119  69  ARG   C CG  
1582 C CD  . ARG   B 63  ? 0.4050 0.3570 0.3436 -0.0024 -0.0178 0.0141  69  ARG   C CD  
1583 N NE  . ARG   B 63  ? 0.4559 0.4090 0.3919 -0.0040 -0.0227 0.0162  69  ARG   C NE  
1584 C CZ  . ARG   B 63  ? 0.4615 0.4192 0.4004 -0.0034 -0.0226 0.0200  69  ARG   C CZ  
1585 N NH1 . ARG   B 63  ? 0.4321 0.3936 0.3768 -0.0014 -0.0177 0.0220  69  ARG   C NH1 
1586 N NH2 . ARG   B 63  ? 0.4594 0.4180 0.3958 -0.0048 -0.0277 0.0220  69  ARG   C NH2 
1587 N N   . LYS   B 64  ? 0.2457 0.1962 0.1931 0.0059  -0.0012 0.0087  70  LYS   C N   
1588 C CA  . LYS   B 64  ? 0.2520 0.2002 0.2002 0.0075  0.0009  0.0066  70  LYS   C CA  
1589 C C   . LYS   B 64  ? 0.2249 0.1778 0.1824 0.0077  0.0018  0.0077  70  LYS   C C   
1590 O O   . LYS   B 64  ? 0.2171 0.1752 0.1803 0.0078  0.0026  0.0097  70  LYS   C O   
1591 C CB  . LYS   B 64  ? 0.3217 0.2684 0.2659 0.0105  0.0050  0.0056  70  LYS   C CB  
1592 C CG  . LYS   B 64  ? 0.4611 0.4006 0.3944 0.0111  0.0050  0.0031  70  LYS   C CG  
1593 C CD  . LYS   B 64  ? 0.5673 0.5049 0.4985 0.0145  0.0098  0.0017  70  LYS   C CD  
1594 C CE  . LYS   B 64  ? 0.6602 0.5905 0.5795 0.0153  0.0105  -0.0008 70  LYS   C CE  
1595 N NZ  . LYS   B 64  ? 0.7267 0.6552 0.6443 0.0189  0.0160  -0.0018 70  LYS   C NZ  
1596 N N   . HIS   B 65  ? 0.2150 0.1655 0.1735 0.0081  0.0018  0.0065  71  HIS   C N   
1597 C CA  . HIS   B 65  ? 0.2134 0.1675 0.1788 0.0090  0.0028  0.0072  71  HIS   C CA  
1598 C C   . HIS   B 65  ? 0.2290 0.1828 0.1942 0.0121  0.0057  0.0060  71  HIS   C C   
1599 O O   . HIS   B 65  ? 0.2662 0.2151 0.2266 0.0133  0.0064  0.0044  71  HIS   C O   
1600 C CB  . HIS   B 65  ? 0.2149 0.1665 0.1813 0.0076  0.0012  0.0071  71  HIS   C CB  
1601 C CG  . HIS   B 65  ? 0.1949 0.1476 0.1636 0.0046  -0.0014 0.0085  71  HIS   C CG  
1602 N ND1 . HIS   B 65  ? 0.2339 0.1909 0.2093 0.0038  -0.0014 0.0103  71  HIS   C ND1 
1603 C CD2 . HIS   B 65  ? 0.2030 0.1529 0.1685 0.0023  -0.0041 0.0082  71  HIS   C CD2 
1604 C CE1 . HIS   B 65  ? 0.2095 0.1665 0.1864 0.0011  -0.0037 0.0113  71  HIS   C CE1 
1605 N NE2 . HIS   B 65  ? 0.2407 0.1936 0.2120 0.0000  -0.0058 0.0102  71  HIS   C NE2 
1606 N N   . TYR   B 66  ? 0.1981 0.1570 0.1692 0.0134  0.0072  0.0068  72  TYR   C N   
1607 C CA  . TYR   B 66  ? 0.1937 0.1533 0.1663 0.0163  0.0096  0.0059  72  TYR   C CA  
1608 C C   . TYR   B 66  ? 0.1857 0.1478 0.1635 0.0172  0.0090  0.0059  72  TYR   C C   
1609 O O   . TYR   B 66  ? 0.1903 0.1562 0.1725 0.0162  0.0082  0.0067  72  TYR   C O   
1610 C CB  . TYR   B 66  ? 0.2022 0.1663 0.1786 0.0170  0.0119  0.0068  72  TYR   C CB  
1611 C CG  . TYR   B 66  ? 0.2142 0.1759 0.1847 0.0169  0.0133  0.0071  72  TYR   C CG  
1612 C CD1 . TYR   B 66  ? 0.2406 0.1986 0.2063 0.0190  0.0158  0.0059  72  TYR   C CD1 
1613 C CD2 . TYR   B 66  ? 0.2241 0.1874 0.1942 0.0151  0.0125  0.0088  72  TYR   C CD2 
1614 C CE1 . TYR   B 66  ? 0.2633 0.2187 0.2221 0.0192  0.0174  0.0061  72  TYR   C CE1 
1615 C CE2 . TYR   B 66  ? 0.2465 0.2076 0.2101 0.0152  0.0137  0.0093  72  TYR   C CE2 
1616 C CZ  . TYR   B 66  ? 0.2615 0.2185 0.2191 0.0173  0.0162  0.0079  72  TYR   C CZ  
1617 O OH  . TYR   B 66  ? 0.2895 0.2439 0.2394 0.0176  0.0175  0.0084  72  TYR   C OH  
1618 N N   . PRO   B 67  ? 0.1900 0.1499 0.1670 0.0195  0.0096  0.0050  73  PRO   C N   
1619 C CA  . PRO   B 67  ? 0.1883 0.1510 0.1698 0.0209  0.0088  0.0052  73  PRO   C CA  
1620 C C   . PRO   B 67  ? 0.1995 0.1680 0.1877 0.0222  0.0099  0.0052  73  PRO   C C   
1621 O O   . PRO   B 67  ? 0.2270 0.1960 0.2161 0.0235  0.0122  0.0050  73  PRO   C O   
1622 C CB  . PRO   B 67  ? 0.2184 0.1767 0.1972 0.0232  0.0092  0.0046  73  PRO   C CB  
1623 C CG  . PRO   B 67  ? 0.2490 0.2030 0.2231 0.0236  0.0111  0.0037  73  PRO   C CG  
1624 C CD  . PRO   B 67  ? 0.2082 0.1627 0.1801 0.0211  0.0111  0.0038  73  PRO   C CD  
1625 N N   . VAL   B 68  ? 0.1818 0.1544 0.1745 0.0218  0.0084  0.0053  74  VAL   C N   
1626 C CA  . VAL   B 68  ? 0.1783 0.1564 0.1783 0.0224  0.0090  0.0050  74  VAL   C CA  
1627 C C   . VAL   B 68  ? 0.1677 0.1486 0.1712 0.0232  0.0067  0.0044  74  VAL   C C   
1628 O O   . VAL   B 68  ? 0.1800 0.1593 0.1801 0.0227  0.0050  0.0045  74  VAL   C O   
1629 C CB  . VAL   B 68  ? 0.1967 0.1775 0.1995 0.0201  0.0097  0.0056  74  VAL   C CB  
1630 C CG1 . VAL   B 68  ? 0.2272 0.2064 0.2275 0.0197  0.0121  0.0065  74  VAL   C CG1 
1631 C CG2 . VAL   B 68  ? 0.2073 0.1873 0.2081 0.0180  0.0080  0.0060  74  VAL   C CG2 
1632 N N   . SER   B 69  ? 0.1632 0.1486 0.1737 0.0245  0.0067  0.0037  75  SER   C N   
1633 C CA  . SER   B 69  ? 0.1686 0.1579 0.1838 0.0248  0.0040  0.0027  75  SER   C CA  
1634 C C   . SER   B 69  ? 0.1616 0.1541 0.1816 0.0226  0.0045  0.0022  75  SER   C C   
1635 O O   . SER   B 69  ? 0.1662 0.1599 0.1895 0.0218  0.0071  0.0029  75  SER   C O   
1636 C CB  . SER   B 69  ? 0.1963 0.1891 0.2180 0.0272  0.0035  0.0022  75  SER   C CB  
1637 O OG  . SER   B 69  ? 0.2498 0.2395 0.2676 0.0295  0.0031  0.0029  75  SER   C OG  
1638 N N   . PHE   B 70  ? 0.1491 0.1426 0.1691 0.0216  0.0023  0.0011  76  PHE   C N   
1639 C CA  . PHE   B 70  ? 0.1481 0.1440 0.1729 0.0195  0.0029  0.0004  76  PHE   C CA  
1640 C C   . PHE   B 70  ? 0.1521 0.1508 0.1807 0.0195  0.0001  -0.0019 76  PHE   C C   
1641 O O   . PHE   B 70  ? 0.1648 0.1628 0.1895 0.0208  -0.0026 -0.0028 76  PHE   C O   
1642 C CB  . PHE   B 70  ? 0.1569 0.1499 0.1770 0.0176  0.0041  0.0015  76  PHE   C CB  
1643 C CG  . PHE   B 70  ? 0.1506 0.1405 0.1637 0.0177  0.0027  0.0014  76  PHE   C CG  
1644 C CD1 . PHE   B 70  ? 0.1683 0.1544 0.1751 0.0184  0.0029  0.0028  76  PHE   C CD1 
1645 C CD2 . PHE   B 70  ? 0.1645 0.1548 0.1772 0.0172  0.0016  0.0001  76  PHE   C CD2 
1646 C CE1 . PHE   B 70  ? 0.1716 0.1548 0.1728 0.0184  0.0021  0.0032  76  PHE   C CE1 
1647 C CE2 . PHE   B 70  ? 0.1728 0.1601 0.1789 0.0174  0.0011  0.0004  76  PHE   C CE2 
1648 C CZ  . PHE   B 70  ? 0.1770 0.1609 0.1777 0.0181  0.0014  0.0022  76  PHE   C CZ  
1649 N N   . SER   B 71  ? 0.1486 0.1502 0.1845 0.0181  0.0007  -0.0030 77  SER   C N   
1650 C CA  . SER   B 71  ? 0.1614 0.1658 0.2021 0.0179  -0.0023 -0.0058 77  SER   C CA  
1651 C C   . SER   B 71  ? 0.1734 0.1755 0.2085 0.0170  -0.0036 -0.0074 77  SER   C C   
1652 O O   . SER   B 71  ? 0.1834 0.1822 0.2123 0.0166  -0.0019 -0.0061 77  SER   C O   
1653 C CB  . SER   B 71  ? 0.1628 0.1709 0.2146 0.0166  -0.0010 -0.0064 77  SER   C CB  
1654 O OG  . SER   B 71  ? 0.1887 0.1956 0.2415 0.0148  0.0019  -0.0054 77  SER   C OG  
1655 N N   . LYS   B 72  ? 0.1784 0.1821 0.2159 0.0169  -0.0066 -0.0105 78  LYS   C N   
1656 C CA  . LYS   B 72  ? 0.1810 0.1822 0.2125 0.0164  -0.0075 -0.0125 78  LYS   C CA  
1657 C C   . LYS   B 72  ? 0.1881 0.1890 0.2244 0.0142  -0.0048 -0.0131 78  LYS   C C   
1658 O O   . LYS   B 72  ? 0.1978 0.2013 0.2434 0.0131  -0.0037 -0.0131 78  LYS   C O   
1659 C CB  . LYS   B 72  ? 0.2228 0.2255 0.2542 0.0171  -0.0122 -0.0161 78  LYS   C CB  
1660 C CG  . LYS   B 72  ? 0.2689 0.2720 0.2957 0.0195  -0.0153 -0.0152 78  LYS   C CG  
1661 C CD  . LYS   B 72  ? 0.3861 0.3912 0.4131 0.0202  -0.0207 -0.0185 78  LYS   C CD  
1662 C CE  . LYS   B 72  ? 0.4790 0.4858 0.5049 0.0228  -0.0242 -0.0173 78  LYS   C CE  
1663 N NZ  . LYS   B 72  ? 0.5373 0.5483 0.5691 0.0230  -0.0297 -0.0205 78  LYS   C NZ  
1664 N N   . PRO   B 73  ? 0.1828 0.1804 0.2136 0.0137  -0.0032 -0.0132 79  PRO   C N   
1665 C CA  . PRO   B 73  ? 0.1885 0.1857 0.2246 0.0119  -0.0003 -0.0133 79  PRO   C CA  
1666 C C   . PRO   B 73  ? 0.2011 0.2001 0.2451 0.0108  -0.0016 -0.0168 79  PRO   C C   
1667 O O   . PRO   B 73  ? 0.2183 0.2169 0.2597 0.0112  -0.0048 -0.0205 79  PRO   C O   
1668 C CB  . PRO   B 73  ? 0.2117 0.2053 0.2404 0.0120  0.0011  -0.0136 79  PRO   C CB  
1669 C CG  . PRO   B 73  ? 0.2337 0.2256 0.2531 0.0137  -0.0003 -0.0125 79  PRO   C CG  
1670 C CD  . PRO   B 73  ? 0.2042 0.1984 0.2244 0.0149  -0.0036 -0.0129 79  PRO   C CD  
1671 N N   . SER   B 74  ? 0.1707 0.1716 0.2242 0.0094  0.0006  -0.0157 80  SER   C N   
1672 C CA  . SER   B 74  ? 0.1796 0.1822 0.2423 0.0082  -0.0007 -0.0189 80  SER   C CA  
1673 C C   . SER   B 74  ? 0.1842 0.1869 0.2555 0.0066  0.0031  -0.0173 80  SER   C C   
1674 O O   . SER   B 74  ? 0.1740 0.1756 0.2435 0.0066  0.0062  -0.0135 80  SER   C O   
1675 C CB  . SER   B 74  ? 0.2355 0.2421 0.3040 0.0086  -0.0033 -0.0193 80  SER   C CB  
1676 O OG  . SER   B 74  ? 0.3125 0.3212 0.3858 0.0087  -0.0006 -0.0154 80  SER   C OG  
1677 N N   . LEU   B 75  ? 0.1829 0.1866 0.2636 0.0051  0.0025  -0.0200 81  LEU   C N   
1678 C CA  . LEU   B 75  ? 0.1862 0.1898 0.2764 0.0036  0.0061  -0.0185 81  LEU   C CA  
1679 C C   . LEU   B 75  ? 0.1841 0.1913 0.2826 0.0034  0.0073  -0.0155 81  LEU   C C   
1680 O O   . LEU   B 75  ? 0.2058 0.2160 0.3107 0.0030  0.0049  -0.0176 81  LEU   C O   
1681 C CB  . LEU   B 75  ? 0.2025 0.2046 0.2988 0.0021  0.0049  -0.0235 81  LEU   C CB  
1682 C CG  . LEU   B 75  ? 0.2255 0.2267 0.3323 0.0006  0.0085  -0.0223 81  LEU   C CG  
1683 C CD1 . LEU   B 75  ? 0.2271 0.2252 0.3297 0.0011  0.0122  -0.0195 81  LEU   C CD1 
1684 C CD2 . LEU   B 75  ? 0.2529 0.2526 0.3665 -0.0011 0.0066  -0.0281 81  LEU   C CD2 
1685 N N   . ILE   B 76  ? 0.1909 0.1981 0.2888 0.0039  0.0108  -0.0105 82  ILE   C N   
1686 C CA  . ILE   B 76  ? 0.2016 0.2117 0.3048 0.0042  0.0128  -0.0071 82  ILE   C CA  
1687 C C   . ILE   B 76  ? 0.1938 0.2035 0.3040 0.0032  0.0170  -0.0035 82  ILE   C C   
1688 O O   . ILE   B 76  ? 0.1858 0.1929 0.2926 0.0032  0.0187  -0.0016 82  ILE   C O   
1689 C CB  . ILE   B 76  ? 0.2394 0.2491 0.3323 0.0059  0.0129  -0.0043 82  ILE   C CB  
1690 C CG1 . ILE   B 76  ? 0.2810 0.2910 0.3675 0.0071  0.0088  -0.0073 82  ILE   C CG1 
1691 C CG2 . ILE   B 76  ? 0.2582 0.2698 0.3542 0.0066  0.0159  -0.0004 82  ILE   C CG2 
1692 C CD1 . ILE   B 76  ? 0.3005 0.3098 0.3784 0.0087  0.0087  -0.0053 82  ILE   C CD1 
1693 N N   . PHE   B 77  ? 0.1974 0.2097 0.3178 0.0027  0.0189  -0.0022 83  PHE   C N   
1694 C CA  . PHE   B 77  ? 0.1991 0.2109 0.3259 0.0021  0.0234  0.0020  83  PHE   C CA  
1695 C C   . PHE   B 77  ? 0.2173 0.2288 0.3359 0.0037  0.0258  0.0070  83  PHE   C C   
1696 O O   . PHE   B 77  ? 0.2433 0.2565 0.3589 0.0049  0.0256  0.0076  83  PHE   C O   
1697 C CB  . PHE   B 77  ? 0.2009 0.2155 0.3416 0.0010  0.0251  0.0022  83  PHE   C CB  
1698 C CG  . PHE   B 77  ? 0.2115 0.2248 0.3593 0.0002  0.0297  0.0063  83  PHE   C CG  
1699 C CD1 . PHE   B 77  ? 0.2274 0.2380 0.3793 -0.0011 0.0300  0.0050  83  PHE   C CD1 
1700 C CD2 . PHE   B 77  ? 0.2331 0.2475 0.3827 0.0010  0.0341  0.0117  83  PHE   C CD2 
1701 C CE1 . PHE   B 77  ? 0.2445 0.2537 0.4030 -0.0016 0.0343  0.0093  83  PHE   C CE1 
1702 C CE2 . PHE   B 77  ? 0.2408 0.2537 0.3961 0.0005  0.0384  0.0160  83  PHE   C CE2 
1703 C CZ  . PHE   B 77  ? 0.2376 0.2480 0.3978 -0.0008 0.0384  0.0149  83  PHE   C CZ  
1704 N N   . VAL   B 78  ? 0.1830 0.1921 0.2978 0.0038  0.0277  0.0104  84  VAL   C N   
1705 C CA  . VAL   B 78  ? 0.1847 0.1931 0.2909 0.0051  0.0293  0.0148  84  VAL   C CA  
1706 C C   . VAL   B 78  ? 0.1818 0.1900 0.2936 0.0050  0.0336  0.0197  84  VAL   C C   
1707 O O   . VAL   B 78  ? 0.1802 0.1874 0.2985 0.0041  0.0348  0.0206  84  VAL   C O   
1708 C CB  . VAL   B 78  ? 0.1898 0.1957 0.2869 0.0053  0.0274  0.0151  84  VAL   C CB  
1709 C CG1 . VAL   B 78  ? 0.2084 0.2133 0.2964 0.0064  0.0282  0.0191  84  VAL   C CG1 
1710 C CG2 . VAL   B 78  ? 0.2053 0.2108 0.2971 0.0054  0.0237  0.0105  84  VAL   C CG2 
1711 N N   . GLU   B 79  ? 0.1697 0.1785 0.2784 0.0062  0.0361  0.0232  85  GLU   C N   
1712 C CA  . GLU   B 79  ? 0.1715 0.1797 0.2836 0.0064  0.0405  0.0286  85  GLU   C CA  
1713 C C   . GLU   B 79  ? 0.1754 0.1811 0.2811 0.0067  0.0403  0.0321  85  GLU   C C   
1714 O O   . GLU   B 79  ? 0.1737 0.1784 0.2714 0.0068  0.0370  0.0307  85  GLU   C O   
1715 C CB  . GLU   B 79  ? 0.1972 0.2061 0.3057 0.0080  0.0437  0.0314  85  GLU   C CB  
1716 C CG  . GLU   B 79  ? 0.2428 0.2549 0.3610 0.0078  0.0449  0.0291  85  GLU   C CG  
1717 C CD  . GLU   B 79  ? 0.3461 0.3596 0.4797 0.0061  0.0469  0.0291  85  GLU   C CD  
1718 O OE1 . GLU   B 79  ? 0.3704 0.3826 0.5077 0.0058  0.0503  0.0334  85  GLU   C OE1 
1719 O OE2 . GLU   B 79  ? 0.3778 0.3938 0.5202 0.0050  0.0449  0.0249  85  GLU   C OE2 
1720 N N   . ALA   B 80  ? 0.1873 0.1924 0.2974 0.0068  0.0438  0.0370  86  ALA   C N   
1721 C CA  . ALA   B 80  ? 0.1997 0.2029 0.3049 0.0072  0.0434  0.0410  86  ALA   C CA  
1722 C C   . ALA   B 80  ? 0.2128 0.2149 0.3037 0.0084  0.0413  0.0425  86  ALA   C C   
1723 O O   . ALA   B 80  ? 0.2362 0.2384 0.3210 0.0094  0.0425  0.0428  86  ALA   C O   
1724 C CB  . ALA   B 80  ? 0.2127 0.2152 0.3241 0.0076  0.0478  0.0467  86  ALA   C CB  
1725 N N   . SER   B 81  ? 0.1995 0.2007 0.2859 0.0083  0.0383  0.0429  87  SER   C N   
1726 C CA  . SER   B 81  ? 0.2154 0.2154 0.2892 0.0090  0.0357  0.0444  87  SER   C CA  
1727 C C   . SER   B 81  ? 0.2299 0.2292 0.3027 0.0094  0.0353  0.0496  87  SER   C C   
1728 O O   . SER   B 81  ? 0.2340 0.2336 0.3162 0.0092  0.0374  0.0521  87  SER   C O   
1729 C CB  . SER   B 81  ? 0.2093 0.2094 0.2789 0.0084  0.0317  0.0398  87  SER   C CB  
1730 O OG  . SER   B 81  ? 0.2100 0.2103 0.2852 0.0076  0.0304  0.0394  87  SER   C OG  
1731 N N   . GLU   B 82  ? 0.2560 0.2544 0.3183 0.0098  0.0324  0.0513  88  GLU   C N   
1732 C CA  . GLU   B 82  ? 0.2730 0.2711 0.3347 0.0102  0.0312  0.0564  88  GLU   C CA  
1733 C C   . GLU   B 82  ? 0.2636 0.2629 0.3341 0.0093  0.0295  0.0557  88  GLU   C C   
1734 O O   . GLU   B 82  ? 0.2785 0.2780 0.3531 0.0098  0.0296  0.0602  88  GLU   C O   
1735 C CB  . GLU   B 82  ? 0.3360 0.3328 0.3844 0.0107  0.0279  0.0582  88  GLU   C CB  
1736 C CG  . GLU   B 82  ? 0.4399 0.4367 0.4833 0.0097  0.0232  0.0545  88  GLU   C CG  
1737 C CD  . GLU   B 82  ? 0.5378 0.5333 0.5696 0.0100  0.0195  0.0569  88  GLU   C CD  
1738 O OE1 . GLU   B 82  ? 0.5482 0.5419 0.5714 0.0111  0.0209  0.0588  88  GLU   C OE1 
1739 O OE2 . GLU   B 82  ? 0.5575 0.5538 0.5890 0.0091  0.0153  0.0569  88  GLU   C OE2 
1740 N N   . TYR   B 83  ? 0.2246 0.2244 0.2984 0.0083  0.0285  0.0504  89  TYR   C N   
1741 C CA  . TYR   B 83  ? 0.2178 0.2182 0.2985 0.0077  0.0274  0.0494  89  TYR   C CA  
1742 C C   . TYR   B 83  ? 0.2181 0.2184 0.3093 0.0071  0.0299  0.0458  89  TYR   C C   
1743 O O   . TYR   B 83  ? 0.2378 0.2381 0.3352 0.0069  0.0299  0.0454  89  TYR   C O   
1744 C CB  . TYR   B 83  ? 0.2131 0.2138 0.2874 0.0071  0.0235  0.0468  89  TYR   C CB  
1745 C CG  . TYR   B 83  ? 0.2065 0.2065 0.2739 0.0068  0.0227  0.0421  89  TYR   C CG  
1746 C CD1 . TYR   B 83  ? 0.2151 0.2142 0.2725 0.0072  0.0216  0.0427  89  TYR   C CD1 
1747 C CD2 . TYR   B 83  ? 0.1967 0.1967 0.2674 0.0063  0.0232  0.0371  89  TYR   C CD2 
1748 C CE1 . TYR   B 83  ? 0.2039 0.2022 0.2558 0.0072  0.0211  0.0387  89  TYR   C CE1 
1749 C CE2 . TYR   B 83  ? 0.2051 0.2046 0.2700 0.0063  0.0223  0.0333  89  TYR   C CE2 
1750 C CZ  . TYR   B 83  ? 0.2041 0.2029 0.2602 0.0068  0.0214  0.0342  89  TYR   C CZ  
1751 O OH  . TYR   B 83  ? 0.2229 0.2210 0.2739 0.0070  0.0209  0.0307  89  TYR   C OH  
1752 N N   . TYR   B 84  ? 0.1919 0.1921 0.2855 0.0069  0.0321  0.0431  90  TYR   C N   
1753 C CA  . TYR   B 84  ? 0.1880 0.1880 0.2919 0.0061  0.0341  0.0397  90  TYR   C CA  
1754 C C   . TYR   B 84  ? 0.1923 0.1924 0.3016 0.0061  0.0373  0.0408  90  TYR   C C   
1755 O O   . TYR   B 84  ? 0.1846 0.1853 0.2882 0.0066  0.0378  0.0420  90  TYR   C O   
1756 C CB  . TYR   B 84  ? 0.1792 0.1793 0.2810 0.0054  0.0321  0.0331  90  TYR   C CB  
1757 C CG  . TYR   B 84  ? 0.1691 0.1687 0.2678 0.0053  0.0299  0.0311  90  TYR   C CG  
1758 C CD1 . TYR   B 84  ? 0.1812 0.1799 0.2868 0.0053  0.0309  0.0312  90  TYR   C CD1 
1759 C CD2 . TYR   B 84  ? 0.1619 0.1617 0.2517 0.0054  0.0272  0.0289  90  TYR   C CD2 
1760 C CE1 . TYR   B 84  ? 0.1817 0.1800 0.2850 0.0053  0.0296  0.0295  90  TYR   C CE1 
1761 C CE2 . TYR   B 84  ? 0.1608 0.1601 0.2483 0.0053  0.0256  0.0274  90  TYR   C CE2 
1762 C CZ  . TYR   B 84  ? 0.1769 0.1756 0.2713 0.0053  0.0270  0.0276  90  TYR   C CZ  
1763 O OH  . TYR   B 84  ? 0.1745 0.1728 0.2671 0.0053  0.0262  0.0263  90  TYR   C OH  
1764 N N   . PRO   B 85  ? 0.1977 0.1972 0.3183 0.0054  0.0398  0.0400  91  PRO   C N   
1765 C CA  . PRO   B 85  ? 0.1919 0.1919 0.3194 0.0049  0.0428  0.0401  91  PRO   C CA  
1766 C C   . PRO   B 85  ? 0.1901 0.1915 0.3165 0.0042  0.0411  0.0343  91  PRO   C C   
1767 O O   . PRO   B 85  ? 0.1909 0.1924 0.3116 0.0040  0.0378  0.0300  91  PRO   C O   
1768 C CB  . PRO   B 85  ? 0.1931 0.1915 0.3335 0.0040  0.0451  0.0400  91  PRO   C CB  
1769 C CG  . PRO   B 85  ? 0.2028 0.2003 0.3424 0.0037  0.0426  0.0358  91  PRO   C CG  
1770 C CD  . PRO   B 85  ? 0.2017 0.1999 0.3298 0.0048  0.0399  0.0380  91  PRO   C CD  
1771 N N   . ALA   B 86  ? 0.1854 0.1880 0.3185 0.0037  0.0435  0.0341  92  ALA   C N   
1772 C CA  . ALA   B 86  ? 0.2001 0.2045 0.3349 0.0030  0.0417  0.0287  92  ALA   C CA  
1773 C C   . ALA   B 86  ? 0.2078 0.2113 0.3484 0.0016  0.0395  0.0230  92  ALA   C C   
1774 O O   . ALA   B 86  ? 0.2286 0.2303 0.3781 0.0007  0.0413  0.0235  92  ALA   C O   
1775 C CB  . ALA   B 86  ? 0.1997 0.2058 0.3434 0.0026  0.0451  0.0301  92  ALA   C CB  
1776 N N   . ARG   B 87  ? 0.1956 0.1995 0.3302 0.0016  0.0357  0.0181  93  ARG   C N   
1777 C CA  . ARG   B 87  ? 0.1902 0.1926 0.3274 0.0006  0.0336  0.0126  93  ARG   C CA  
1778 C C   . ARG   B 87  ? 0.1837 0.1872 0.3142 0.0007  0.0296  0.0076  93  ARG   C C   
1779 O O   . ARG   B 87  ? 0.1854 0.1905 0.3084 0.0018  0.0285  0.0087  93  ARG   C O   
1780 C CB  . ARG   B 87  ? 0.2100 0.2099 0.3430 0.0012  0.0338  0.0141  93  ARG   C CB  
1781 C CG  . ARG   B 87  ? 0.1957 0.1958 0.3160 0.0023  0.0314  0.0147  93  ARG   C CG  
1782 C CD  . ARG   B 87  ? 0.1973 0.1958 0.3156 0.0029  0.0320  0.0171  93  ARG   C CD  
1783 N NE  . ARG   B 87  ? 0.2147 0.2134 0.3223 0.0036  0.0294  0.0164  93  ARG   C NE  
1784 C CZ  . ARG   B 87  ? 0.2232 0.2205 0.3276 0.0038  0.0286  0.0150  93  ARG   C CZ  
1785 N NH1 . ARG   B 87  ? 0.2255 0.2210 0.3362 0.0036  0.0303  0.0137  93  ARG   C NH1 
1786 N NH2 . ARG   B 87  ? 0.2132 0.2108 0.3086 0.0043  0.0265  0.0145  93  ARG   C NH2 
1787 N N   . TYR   B 88  ? 0.1933 0.1954 0.3249 -0.0001 0.0273  0.0021  94  TYR   C N   
1788 C CA  . TYR   B 88  ? 0.2098 0.2123 0.3333 0.0004  0.0234  -0.0023 94  TYR   C CA  
1789 C C   . TYR   B 88  ? 0.1863 0.1868 0.2994 0.0015  0.0228  -0.0016 94  TYR   C C   
1790 O O   . TYR   B 88  ? 0.2118 0.2099 0.3260 0.0014  0.0245  -0.0010 94  TYR   C O   
1791 C CB  . TYR   B 88  ? 0.2385 0.2400 0.3666 -0.0008 0.0209  -0.0087 94  TYR   C CB  
1792 C CG  . TYR   B 88  ? 0.2639 0.2682 0.4022 -0.0021 0.0201  -0.0102 94  TYR   C CG  
1793 C CD1 . TYR   B 88  ? 0.2811 0.2886 0.4174 -0.0016 0.0171  -0.0116 94  TYR   C CD1 
1794 C CD2 . TYR   B 88  ? 0.2813 0.2852 0.4324 -0.0036 0.0227  -0.0095 94  TYR   C CD2 
1795 C CE1 . TYR   B 88  ? 0.3002 0.3109 0.4474 -0.0027 0.0165  -0.0126 94  TYR   C CE1 
1796 C CE2 . TYR   B 88  ? 0.2916 0.2983 0.4535 -0.0049 0.0223  -0.0105 94  TYR   C CE2 
1797 C CZ  . TYR   B 88  ? 0.3065 0.3169 0.4667 -0.0045 0.0191  -0.0121 94  TYR   C CZ  
1798 O OH  . TYR   B 88  ? 0.3312 0.3450 0.5039 -0.0058 0.0189  -0.0127 94  TYR   C OH  
1799 N N   . GLN   B 89  ? 0.1769 0.1783 0.2804 0.0026  0.0208  -0.0014 95  GLN   C N   
1800 C CA  . GLN   B 89  ? 0.1713 0.1710 0.2652 0.0035  0.0201  -0.0009 95  GLN   C CA  
1801 C C   . GLN   B 89  ? 0.1701 0.1692 0.2576 0.0039  0.0168  -0.0056 95  GLN   C C   
1802 O O   . GLN   B 89  ? 0.1815 0.1826 0.2686 0.0041  0.0146  -0.0072 95  GLN   C O   
1803 C CB  . GLN   B 89  ? 0.1842 0.1847 0.2721 0.0043  0.0206  0.0037  95  GLN   C CB  
1804 C CG  . GLN   B 89  ? 0.1903 0.1891 0.2699 0.0049  0.0198  0.0045  95  GLN   C CG  
1805 C CD  . GLN   B 89  ? 0.1790 0.1781 0.2546 0.0053  0.0204  0.0093  95  GLN   C CD  
1806 O OE1 . GLN   B 89  ? 0.1948 0.1945 0.2745 0.0051  0.0223  0.0130  95  GLN   C OE1 
1807 N NE2 . GLN   B 89  ? 0.1872 0.1856 0.2545 0.0057  0.0188  0.0094  95  GLN   C NE2 
1808 N N   . SER   B 90  ? 0.1578 0.1544 0.2406 0.0041  0.0166  -0.0078 96  SER   C N   
1809 C CA  . SER   B 90  ? 0.1728 0.1684 0.2484 0.0048  0.0137  -0.0120 96  SER   C CA  
1810 C C   . SER   B 90  ? 0.1697 0.1649 0.2349 0.0060  0.0129  -0.0100 96  SER   C C   
1811 O O   . SER   B 90  ? 0.1681 0.1632 0.2318 0.0061  0.0147  -0.0060 96  SER   C O   
1812 C CB  . SER   B 90  ? 0.1953 0.1878 0.2708 0.0045  0.0142  -0.0161 96  SER   C CB  
1813 O OG  . SER   B 90  ? 0.2027 0.1932 0.2758 0.0050  0.0171  -0.0137 96  SER   C OG  
1814 N N   . HIS   B 91  ? 0.1654 0.1600 0.2236 0.0069  0.0101  -0.0129 97  HIS   C N   
1815 C CA  . HIS   B 91  ? 0.1598 0.1535 0.2083 0.0081  0.0092  -0.0115 97  HIS   C CA  
1816 C C   . HIS   B 91  ? 0.1643 0.1596 0.2125 0.0083  0.0096  -0.0073 97  HIS   C C   
1817 O O   . HIS   B 91  ? 0.1778 0.1719 0.2206 0.0086  0.0103  -0.0047 97  HIS   C O   
1818 C CB  . HIS   B 91  ? 0.1670 0.1578 0.2109 0.0083  0.0115  -0.0109 97  HIS   C CB  
1819 C CG  . HIS   B 91  ? 0.1968 0.1851 0.2389 0.0085  0.0116  -0.0153 97  HIS   C CG  
1820 N ND1 . HIS   B 91  ? 0.2334 0.2197 0.2662 0.0097  0.0100  -0.0177 97  HIS   C ND1 
1821 C CD2 . HIS   B 91  ? 0.2026 0.1898 0.2509 0.0077  0.0130  -0.0178 97  HIS   C CD2 
1822 C CE1 . HIS   B 91  ? 0.2272 0.2111 0.2596 0.0096  0.0105  -0.0218 97  HIS   C CE1 
1823 N NE2 . HIS   B 91  ? 0.2214 0.2056 0.2633 0.0084  0.0124  -0.0222 97  HIS   C NE2 
1824 N N   . LEU   B 92  ? 0.1528 0.1507 0.2067 0.0080  0.0092  -0.0068 98  LEU   C N   
1825 C CA  . LEU   B 92  ? 0.1479 0.1469 0.2014 0.0084  0.0100  -0.0033 98  LEU   C CA  
1826 C C   . LEU   B 92  ? 0.1515 0.1516 0.2019 0.0096  0.0077  -0.0042 98  LEU   C C   
1827 O O   . LEU   B 92  ? 0.1629 0.1646 0.2163 0.0099  0.0055  -0.0071 98  LEU   C O   
1828 C CB  . LEU   B 92  ? 0.1612 0.1621 0.2238 0.0075  0.0122  -0.0015 98  LEU   C CB  
1829 C CG  . LEU   B 92  ? 0.1729 0.1745 0.2343 0.0079  0.0137  0.0025  98  LEU   C CG  
1830 C CD1 . LEU   B 92  ? 0.1870 0.1866 0.2430 0.0077  0.0145  0.0054  98  LEU   C CD1 
1831 C CD2 . LEU   B 92  ? 0.1930 0.1964 0.2633 0.0073  0.0162  0.0042  98  LEU   C CD2 
1832 N N   . MET   B 93  ? 0.1419 0.1411 0.1866 0.0104  0.0079  -0.0017 99  MET   C N   
1833 C CA  . MET   B 93  ? 0.1329 0.1327 0.1748 0.0119  0.0062  -0.0021 99  MET   C CA  
1834 C C   . MET   B 93  ? 0.1419 0.1424 0.1853 0.0122  0.0083  0.0006  99  MET   C C   
1835 O O   . MET   B 93  ? 0.1647 0.1635 0.2053 0.0116  0.0100  0.0031  99  MET   C O   
1836 C CB  . MET   B 93  ? 0.1685 0.1653 0.2009 0.0128  0.0050  -0.0018 99  MET   C CB  
1837 C CG  . MET   B 93  ? 0.1771 0.1727 0.2065 0.0128  0.0036  -0.0042 99  MET   C CG  
1838 S SD  . MET   B 93  ? 0.1984 0.1902 0.2174 0.0136  0.0034  -0.0029 99  MET   C SD  
1839 C CE  . MET   B 93  ? 0.2055 0.1960 0.2250 0.0120  0.0062  0.0004  99  MET   C CE  
1840 N N   . LEU   B 94  ? 0.1393 0.1420 0.1865 0.0133  0.0082  0.0003  100 LEU   C N   
1841 C CA  . LEU   B 94  ? 0.1453 0.1482 0.1933 0.0138  0.0108  0.0028  100 LEU   C CA  
1842 C C   . LEU   B 94  ? 0.1530 0.1545 0.1952 0.0158  0.0102  0.0030  100 LEU   C C   
1843 O O   . LEU   B 94  ? 0.1699 0.1718 0.2111 0.0169  0.0077  0.0013  100 LEU   C O   
1844 C CB  . LEU   B 94  ? 0.1572 0.1639 0.2157 0.0138  0.0123  0.0026  100 LEU   C CB  
1845 C CG  . LEU   B 94  ? 0.1703 0.1785 0.2367 0.0120  0.0134  0.0026  100 LEU   C CG  
1846 C CD1 . LEU   B 94  ? 0.1903 0.2021 0.2675 0.0121  0.0152  0.0029  100 LEU   C CD1 
1847 C CD2 . LEU   B 94  ? 0.1945 0.2004 0.2575 0.0111  0.0158  0.0055  100 LEU   C CD2 
1848 N N   . ALA   B 95  ? 0.1537 0.1532 0.1920 0.0162  0.0125  0.0051  101 ALA   C N   
1849 C CA  . ALA   B 95  ? 0.1579 0.1556 0.1915 0.0181  0.0129  0.0054  101 ALA   C CA  
1850 C C   . ALA   B 95  ? 0.1558 0.1535 0.1904 0.0188  0.0167  0.0073  101 ALA   C C   
1851 O O   . ALA   B 95  ? 0.1577 0.1560 0.1943 0.0176  0.0187  0.0089  101 ALA   C O   
1852 C CB  . ALA   B 95  ? 0.1745 0.1676 0.1982 0.0180  0.0118  0.0057  101 ALA   C CB  
1853 N N   . VAL   B 96  ? 0.1581 0.1550 0.1914 0.0209  0.0181  0.0072  102 VAL   C N   
1854 C CA  . VAL   B 96  ? 0.1695 0.1654 0.2016 0.0219  0.0222  0.0090  102 VAL   C CA  
1855 C C   . VAL   B 96  ? 0.1880 0.1785 0.2087 0.0215  0.0224  0.0097  102 VAL   C C   
1856 O O   . VAL   B 96  ? 0.2088 0.1958 0.2230 0.0221  0.0207  0.0085  102 VAL   C O   
1857 C CB  . VAL   B 96  ? 0.1860 0.1832 0.2220 0.0245  0.0239  0.0085  102 VAL   C CB  
1858 C CG1 . VAL   B 96  ? 0.2086 0.2040 0.2421 0.0259  0.0290  0.0102  102 VAL   C CG1 
1859 C CG2 . VAL   B 96  ? 0.1957 0.1988 0.2443 0.0246  0.0230  0.0077  102 VAL   C CG2 
1860 N N   . GLY   B 97  ? 0.1978 0.1875 0.2161 0.0203  0.0241  0.0116  103 GLY   C N   
1861 C CA  . GLY   B 97  ? 0.2162 0.2012 0.2240 0.0196  0.0233  0.0121  103 GLY   C CA  
1862 C C   . GLY   B 97  ? 0.2194 0.2045 0.2258 0.0183  0.0244  0.0146  103 GLY   C C   
1863 O O   . GLY   B 97  ? 0.2351 0.2238 0.2493 0.0178  0.0259  0.0160  103 GLY   C O   
1864 N N   . HIS   B 98  ? 0.2285 0.2094 0.2251 0.0178  0.0235  0.0152  104 HIS   C N   
1865 C CA  . HIS   B 98  ? 0.2193 0.1998 0.2131 0.0168  0.0240  0.0178  104 HIS   C CA  
1866 C C   . HIS   B 98  ? 0.2090 0.1911 0.2055 0.0145  0.0208  0.0188  104 HIS   C C   
1867 O O   . HIS   B 98  ? 0.2058 0.1866 0.2004 0.0134  0.0175  0.0173  104 HIS   C O   
1868 C CB  . HIS   B 98  ? 0.2599 0.2351 0.2414 0.0173  0.0240  0.0178  104 HIS   C CB  
1869 C CG  . HIS   B 98  ? 0.2961 0.2709 0.2735 0.0167  0.0246  0.0208  104 HIS   C CG  
1870 N ND1 . HIS   B 98  ? 0.3293 0.3059 0.3097 0.0179  0.0289  0.0234  104 HIS   C ND1 
1871 C CD2 . HIS   B 98  ? 0.3332 0.3063 0.3050 0.0150  0.0211  0.0219  104 HIS   C CD2 
1872 C CE1 . HIS   B 98  ? 0.3601 0.3357 0.3354 0.0171  0.0279  0.0262  104 HIS   C CE1 
1873 N NE2 . HIS   B 98  ? 0.3651 0.3387 0.3351 0.0154  0.0230  0.0253  104 HIS   C NE2 
1874 N N   . SER   B 99  ? 0.2101 0.1946 0.2112 0.0138  0.0219  0.0215  105 SER   C N   
1875 C CA  . SER   B 99  ? 0.2114 0.1975 0.2160 0.0119  0.0193  0.0229  105 SER   C CA  
1876 C C   . SER   B 99  ? 0.2292 0.2163 0.2350 0.0118  0.0209  0.0268  105 SER   C C   
1877 O O   . SER   B 99  ? 0.2543 0.2436 0.2666 0.0125  0.0243  0.0280  105 SER   C O   
1878 C CB  . SER   B 99  ? 0.2217 0.2110 0.2360 0.0114  0.0191  0.0213  105 SER   C CB  
1879 O OG  . SER   B 99  ? 0.2426 0.2334 0.2612 0.0099  0.0176  0.0225  105 SER   C OG  
1880 N N   . GLU   B 100 ? 0.2345 0.2199 0.2341 0.0110  0.0185  0.0288  106 GLU   C N   
1881 C CA  . GLU   B 100 ? 0.2347 0.2208 0.2345 0.0109  0.0192  0.0331  106 GLU   C CA  
1882 C C   . GLU   B 100 ? 0.2208 0.2094 0.2283 0.0093  0.0167  0.0341  106 GLU   C C   
1883 O O   . GLU   B 100 ? 0.2117 0.2006 0.2211 0.0083  0.0144  0.0316  106 GLU   C O   
1884 C CB  . GLU   B 100 ? 0.2791 0.2617 0.2667 0.0109  0.0168  0.0346  106 GLU   C CB  
1885 C CG  . GLU   B 100 ? 0.4138 0.3924 0.3907 0.0121  0.0178  0.0325  106 GLU   C CG  
1886 C CD  . GLU   B 100 ? 0.5350 0.5117 0.5053 0.0140  0.0216  0.0350  106 GLU   C CD  
1887 O OE1 . GLU   B 100 ? 0.5782 0.5569 0.5526 0.0144  0.0239  0.0389  106 GLU   C OE1 
1888 O OE2 . GLU   B 100 ? 0.5597 0.5327 0.5212 0.0153  0.0230  0.0329  106 GLU   C OE2 
1889 N N   . PRO   B 101 ? 0.2230 0.2133 0.2351 0.0093  0.0176  0.0379  107 PRO   C N   
1890 C CA  . PRO   B 101 ? 0.2156 0.2080 0.2353 0.0080  0.0156  0.0390  107 PRO   C CA  
1891 C C   . PRO   B 101 ? 0.2205 0.2122 0.2364 0.0067  0.0110  0.0382  107 PRO   C C   
1892 O O   . PRO   B 101 ? 0.2184 0.2115 0.2403 0.0058  0.0100  0.0367  107 PRO   C O   
1893 C CB  . PRO   B 101 ? 0.2408 0.2342 0.2637 0.0085  0.0170  0.0440  107 PRO   C CB  
1894 C CG  . PRO   B 101 ? 0.2741 0.2663 0.2932 0.0100  0.0207  0.0453  107 PRO   C CG  
1895 C CD  . PRO   B 101 ? 0.2452 0.2352 0.2560 0.0105  0.0208  0.0418  107 PRO   C CD  
1896 N N   . GLY   B 102 ? 0.2036 0.1929 0.2095 0.0066  0.0084  0.0388  108 GLY   C N   
1897 C CA  . GLY   B 102 ? 0.2055 0.1942 0.2086 0.0051  0.0037  0.0381  108 GLY   C CA  
1898 C C   . GLY   B 102 ? 0.1941 0.1815 0.1966 0.0044  0.0031  0.0338  108 GLY   C C   
1899 O O   . GLY   B 102 ? 0.2205 0.2075 0.2228 0.0029  -0.0002 0.0331  108 GLY   C O   
1900 N N   . ASP   B 103 ? 0.1806 0.1673 0.1829 0.0055  0.0062  0.0311  109 ASP   C N   
1901 C CA  . ASP   B 103 ? 0.1723 0.1578 0.1741 0.0052  0.0057  0.0274  109 ASP   C CA  
1902 C C   . ASP   B 103 ? 0.1743 0.1622 0.1848 0.0047  0.0062  0.0266  109 ASP   C C   
1903 O O   . ASP   B 103 ? 0.1756 0.1626 0.1858 0.0044  0.0056  0.0242  109 ASP   C O   
1904 C CB  . ASP   B 103 ? 0.1852 0.1691 0.1837 0.0069  0.0085  0.0251  109 ASP   C CB  
1905 C CG  . ASP   B 103 ? 0.2149 0.1952 0.2032 0.0075  0.0082  0.0250  109 ASP   C CG  
1906 O OD1 . ASP   B 103 ? 0.2245 0.2023 0.2069 0.0064  0.0049  0.0247  109 ASP   C OD1 
1907 O OD2 . ASP   B 103 ? 0.2262 0.2059 0.2124 0.0092  0.0114  0.0250  109 ASP   C OD2 
1908 N N   . CYS   B 104 ? 0.1614 0.1522 0.1799 0.0047  0.0077  0.0285  110 CYS   C N   
1909 C CA  . CYS   B 104 ? 0.1599 0.1525 0.1861 0.0043  0.0085  0.0274  110 CYS   C CA  
1910 C C   . CYS   B 104 ? 0.1689 0.1611 0.1948 0.0031  0.0061  0.0274  110 CYS   C C   
1911 O O   . CYS   B 104 ? 0.1886 0.1808 0.2131 0.0021  0.0036  0.0296  110 CYS   C O   
1912 C CB  . CYS   B 104 ? 0.1648 0.1598 0.1993 0.0045  0.0103  0.0299  110 CYS   C CB  
1913 S SG  . CYS   B 104 ? 0.1900 0.1858 0.2283 0.0057  0.0139  0.0294  110 CYS   C SG  
1914 N N   . GLY   B 105 ? 0.1433 0.1351 0.1707 0.0031  0.0068  0.0249  111 GLY   C N   
1915 C CA  . GLY   B 105 ? 0.1645 0.1559 0.1925 0.0019  0.0053  0.0250  111 GLY   C CA  
1916 C C   . GLY   B 105 ? 0.1673 0.1556 0.1882 0.0017  0.0040  0.0230  111 GLY   C C   
1917 O O   . GLY   B 105 ? 0.1787 0.1663 0.2002 0.0009  0.0035  0.0227  111 GLY   C O   
1918 N N   . GLY   B 106 ? 0.1693 0.1557 0.1838 0.0025  0.0037  0.0218  112 GLY   C N   
1919 C CA  . GLY   B 106 ? 0.1774 0.1604 0.1855 0.0026  0.0027  0.0198  112 GLY   C CA  
1920 C C   . GLY   B 106 ? 0.1678 0.1504 0.1769 0.0034  0.0042  0.0177  112 GLY   C C   
1921 O O   . GLY   B 106 ? 0.1633 0.1478 0.1756 0.0045  0.0060  0.0168  112 GLY   C O   
1922 N N   . ILE   B 107 ? 0.1677 0.1477 0.1740 0.0029  0.0033  0.0171  113 ILE   C N   
1923 C CA  . ILE   B 107 ? 0.1551 0.1346 0.1614 0.0039  0.0046  0.0157  113 ILE   C CA  
1924 C C   . ILE   B 107 ? 0.1616 0.1395 0.1636 0.0058  0.0049  0.0136  113 ILE   C C   
1925 O O   . ILE   B 107 ? 0.1728 0.1480 0.1701 0.0060  0.0040  0.0132  113 ILE   C O   
1926 C CB  . ILE   B 107 ? 0.1964 0.1738 0.2023 0.0026  0.0040  0.0165  113 ILE   C CB  
1927 C CG1 . ILE   B 107 ? 0.2353 0.2156 0.2482 0.0015  0.0049  0.0184  113 ILE   C CG1 
1928 C CG2 . ILE   B 107 ? 0.2022 0.1771 0.2046 0.0039  0.0050  0.0153  113 ILE   C CG2 
1929 C CD1 . ILE   B 107 ? 0.2870 0.2662 0.3020 -0.0002 0.0047  0.0201  113 ILE   C CD1 
1930 N N   . LEU   B 108 ? 0.1575 0.1367 0.1610 0.0071  0.0060  0.0122  114 LEU   C N   
1931 C CA  . LEU   B 108 ? 0.1531 0.1310 0.1532 0.0090  0.0059  0.0105  114 LEU   C CA  
1932 C C   . LEU   B 108 ? 0.1611 0.1369 0.1587 0.0093  0.0059  0.0105  114 LEU   C C   
1933 O O   . LEU   B 108 ? 0.1590 0.1359 0.1587 0.0090  0.0068  0.0107  114 LEU   C O   
1934 C CB  . LEU   B 108 ? 0.1557 0.1370 0.1598 0.0102  0.0065  0.0091  114 LEU   C CB  
1935 C CG  . LEU   B 108 ? 0.1664 0.1475 0.1687 0.0122  0.0059  0.0073  114 LEU   C CG  
1936 C CD1 . LEU   B 108 ? 0.1807 0.1602 0.1804 0.0134  0.0057  0.0072  114 LEU   C CD1 
1937 C CD2 . LEU   B 108 ? 0.1735 0.1581 0.1809 0.0128  0.0060  0.0057  114 LEU   C CD2 
1938 N N   . ARG   B 109 ? 0.1609 0.1333 0.1538 0.0101  0.0052  0.0104  115 ARG   C N   
1939 C CA  A ARG   B 109 ? 0.1702 0.1400 0.1602 0.0105  0.0055  0.0110  115 ARG   C CA  
1940 C CA  B ARG   B 109 ? 0.1799 0.1495 0.1699 0.0105  0.0055  0.0111  115 ARG   C CA  
1941 C C   . ARG   B 109 ? 0.1806 0.1487 0.1669 0.0129  0.0049  0.0102  115 ARG   C C   
1942 O O   . ARG   B 109 ? 0.1903 0.1578 0.1758 0.0139  0.0044  0.0094  115 ARG   C O   
1943 C CB  A ARG   B 109 ? 0.1887 0.1552 0.1777 0.0087  0.0054  0.0127  115 ARG   C CB  
1944 C CB  B ARG   B 109 ? 0.2211 0.1875 0.2100 0.0086  0.0051  0.0125  115 ARG   C CB  
1945 C CG  A ARG   B 109 ? 0.1934 0.1568 0.1794 0.0086  0.0042  0.0121  115 ARG   C CG  
1946 C CG  B ARG   B 109 ? 0.2708 0.2335 0.2571 0.0087  0.0058  0.0137  115 ARG   C CG  
1947 C CD  A ARG   B 109 ? 0.2631 0.2228 0.2482 0.0064  0.0034  0.0132  115 ARG   C CD  
1948 C CD  B ARG   B 109 ? 0.2892 0.2485 0.2754 0.0065  0.0050  0.0148  115 ARG   C CD  
1949 N NE  A ARG   B 109 ? 0.3540 0.3160 0.3437 0.0040  0.0031  0.0146  115 ARG   C NE  
1950 N NE  B ARG   B 109 ? 0.3135 0.2751 0.3043 0.0040  0.0045  0.0158  115 ARG   C NE  
1951 C CZ  A ARG   B 109 ? 0.4118 0.3740 0.4027 0.0020  0.0014  0.0149  115 ARG   C CZ  
1952 C CZ  B ARG   B 109 ? 0.3295 0.2928 0.3245 0.0029  0.0058  0.0174  115 ARG   C CZ  
1953 N NH1 A ARG   B 109 ? 0.4326 0.3924 0.4193 0.0022  0.0000  0.0135  115 ARG   C NH1 
1954 N NH1 B ARG   B 109 ? 0.3225 0.2850 0.3165 0.0041  0.0080  0.0182  115 ARG   C NH1 
1955 N NH2 A ARG   B 109 ? 0.4095 0.3742 0.4055 0.0000  0.0010  0.0166  115 ARG   C NH2 
1956 N NH2 B ARG   B 109 ? 0.3215 0.2873 0.3217 0.0008  0.0051  0.0185  115 ARG   C NH2 
1957 N N   . CYS   B 110 ? 0.1770 0.1442 0.1609 0.0140  0.0052  0.0105  116 CYS   C N   
1958 C CA  . CYS   B 110 ? 0.1874 0.1527 0.1674 0.0165  0.0043  0.0103  116 CYS   C CA  
1959 C C   . CYS   B 110 ? 0.2080 0.1688 0.1840 0.0165  0.0053  0.0124  116 CYS   C C   
1960 O O   . CYS   B 110 ? 0.2065 0.1660 0.1837 0.0143  0.0065  0.0137  116 CYS   C O   
1961 C CB  . CYS   B 110 ? 0.1849 0.1532 0.1649 0.0183  0.0034  0.0088  116 CYS   C CB  
1962 S SG  . CYS   B 110 ? 0.1905 0.1587 0.1683 0.0178  0.0048  0.0091  116 CYS   C SG  
1963 N N   . GLN   B 111 ? 0.2203 0.1788 0.1921 0.0189  0.0047  0.0130  117 GLN   C N   
1964 C CA  . GLN   B 111 ? 0.2493 0.2032 0.2174 0.0190  0.0060  0.0154  117 GLN   C CA  
1965 C C   . GLN   B 111 ? 0.2509 0.2052 0.2182 0.0181  0.0080  0.0166  117 GLN   C C   
1966 O O   . GLN   B 111 ? 0.2741 0.2250 0.2403 0.0172  0.0100  0.0190  117 GLN   C O   
1967 C CB  . GLN   B 111 ? 0.2758 0.2272 0.2394 0.0221  0.0050  0.0164  117 GLN   C CB  
1968 C CG  . GLN   B 111 ? 0.3136 0.2676 0.2741 0.0243  0.0038  0.0157  117 GLN   C CG  
1969 C CD  . GLN   B 111 ? 0.4399 0.3920 0.3961 0.0276  0.0022  0.0169  117 GLN   C CD  
1970 O OE1 . GLN   B 111 ? 0.4901 0.4443 0.4483 0.0293  -0.0001 0.0156  117 GLN   C OE1 
1971 N NE2 . GLN   B 111 ? 0.4412 0.3895 0.3919 0.0287  0.0034  0.0196  117 GLN   C NE2 
1972 N N   . HIS   B 112 ? 0.2246 0.1827 0.1930 0.0181  0.0080  0.0149  118 HIS   C N   
1973 C CA  . HIS   B 112 ? 0.2196 0.1779 0.1869 0.0177  0.0104  0.0157  118 HIS   C CA  
1974 C C   . HIS   B 112 ? 0.2261 0.1861 0.1995 0.0149  0.0122  0.0161  118 HIS   C C   
1975 O O   . HIS   B 112 ? 0.2432 0.2030 0.2168 0.0145  0.0149  0.0171  118 HIS   C O   
1976 C CB  . HIS   B 112 ? 0.2259 0.1865 0.1903 0.0195  0.0095  0.0134  118 HIS   C CB  
1977 C CG  . HIS   B 112 ? 0.2314 0.1909 0.1902 0.0223  0.0070  0.0132  118 HIS   C CG  
1978 N ND1 . HIS   B 112 ? 0.2183 0.1807 0.1793 0.0234  0.0038  0.0110  118 HIS   C ND1 
1979 C CD2 . HIS   B 112 ? 0.2572 0.2132 0.2090 0.0244  0.0073  0.0152  118 HIS   C CD2 
1980 C CE1 . HIS   B 112 ? 0.2460 0.2070 0.2017 0.0260  0.0019  0.0117  118 HIS   C CE1 
1981 N NE2 . HIS   B 112 ? 0.2649 0.2218 0.2144 0.0268  0.0039  0.0143  118 HIS   C NE2 
1982 N N   . GLY   B 113 ? 0.2075 0.1694 0.1858 0.0133  0.0108  0.0153  119 GLY   C N   
1983 C CA  . GLY   B 113 ? 0.1996 0.1636 0.1840 0.0108  0.0118  0.0159  119 GLY   C CA  
1984 C C   . GLY   B 113 ? 0.1863 0.1540 0.1749 0.0102  0.0103  0.0140  119 GLY   C C   
1985 O O   . GLY   B 113 ? 0.1838 0.1521 0.1713 0.0112  0.0085  0.0126  119 GLY   C O   
1986 N N   . VAL   B 114 ? 0.1810 0.1513 0.1749 0.0087  0.0115  0.0145  120 VAL   C N   
1987 C CA  . VAL   B 114 ? 0.1780 0.1517 0.1764 0.0081  0.0105  0.0134  120 VAL   C CA  
1988 C C   . VAL   B 114 ? 0.1715 0.1472 0.1698 0.0096  0.0107  0.0110  120 VAL   C C   
1989 O O   . VAL   B 114 ? 0.1830 0.1586 0.1805 0.0103  0.0123  0.0103  120 VAL   C O   
1990 C CB  . VAL   B 114 ? 0.1907 0.1663 0.1955 0.0061  0.0116  0.0152  120 VAL   C CB  
1991 C CG1 . VAL   B 114 ? 0.1993 0.1783 0.2087 0.0058  0.0109  0.0145  120 VAL   C CG1 
1992 C CG2 . VAL   B 114 ? 0.2114 0.1855 0.2174 0.0042  0.0107  0.0173  120 VAL   C CG2 
1993 N N   . VAL   B 115 ? 0.1608 0.1379 0.1595 0.0103  0.0090  0.0095  121 VAL   C N   
1994 C CA  . VAL   B 115 ? 0.1605 0.1399 0.1605 0.0114  0.0085  0.0070  121 VAL   C CA  
1995 C C   . VAL   B 115 ? 0.1692 0.1513 0.1757 0.0103  0.0094  0.0066  121 VAL   C C   
1996 O O   . VAL   B 115 ? 0.1754 0.1587 0.1838 0.0107  0.0100  0.0047  121 VAL   C O   
1997 C CB  . VAL   B 115 ? 0.1586 0.1383 0.1572 0.0127  0.0065  0.0059  121 VAL   C CB  
1998 C CG1 . VAL   B 115 ? 0.1711 0.1537 0.1729 0.0135  0.0056  0.0034  121 VAL   C CG1 
1999 C CG2 . VAL   B 115 ? 0.1842 0.1609 0.1766 0.0142  0.0056  0.0064  121 VAL   C CG2 
2000 N N   . GLY   B 116 ? 0.1595 0.1425 0.1692 0.0091  0.0094  0.0084  122 GLY   C N   
2001 C CA  . GLY   B 116 ? 0.1702 0.1557 0.1863 0.0082  0.0103  0.0088  122 GLY   C CA  
2002 C C   . GLY   B 116 ? 0.1527 0.1387 0.1702 0.0071  0.0097  0.0111  122 GLY   C C   
2003 O O   . GLY   B 116 ? 0.1613 0.1453 0.1748 0.0067  0.0086  0.0122  122 GLY   C O   
2004 N N   . ILE   B 117 ? 0.1417 0.1299 0.1646 0.0065  0.0104  0.0120  123 ILE   C N   
2005 C CA  . ILE   B 117 ? 0.1436 0.1323 0.1671 0.0056  0.0096  0.0145  123 ILE   C CA  
2006 C C   . ILE   B 117 ? 0.1426 0.1328 0.1683 0.0061  0.0102  0.0145  123 ILE   C C   
2007 O O   . ILE   B 117 ? 0.1543 0.1460 0.1845 0.0066  0.0114  0.0131  123 ILE   C O   
2008 C CB  . ILE   B 117 ? 0.1626 0.1525 0.1910 0.0044  0.0100  0.0171  123 ILE   C CB  
2009 C CG1 . ILE   B 117 ? 0.1815 0.1731 0.2165 0.0047  0.0121  0.0166  123 ILE   C CG1 
2010 C CG2 . ILE   B 117 ? 0.1843 0.1728 0.2109 0.0035  0.0094  0.0179  123 ILE   C CG2 
2011 C CD1 . ILE   B 117 ? 0.1840 0.1772 0.2255 0.0038  0.0127  0.0197  123 ILE   C CD1 
2012 N N   . VAL   B 118 ? 0.1428 0.1324 0.1655 0.0060  0.0095  0.0160  124 VAL   C N   
2013 C CA  . VAL   B 118 ? 0.1452 0.1361 0.1697 0.0066  0.0107  0.0167  124 VAL   C CA  
2014 C C   . VAL   B 118 ? 0.1403 0.1335 0.1722 0.0061  0.0120  0.0184  124 VAL   C C   
2015 O O   . VAL   B 118 ? 0.1486 0.1421 0.1824 0.0052  0.0115  0.0205  124 VAL   C O   
2016 C CB  . VAL   B 118 ? 0.1499 0.1391 0.1685 0.0065  0.0099  0.0185  124 VAL   C CB  
2017 C CG1 . VAL   B 118 ? 0.1609 0.1512 0.1811 0.0073  0.0118  0.0199  124 VAL   C CG1 
2018 C CG2 . VAL   B 118 ? 0.1685 0.1550 0.1803 0.0072  0.0089  0.0166  124 VAL   C CG2 
2019 N N   . SER   B 119 ? 0.1392 0.1339 0.1761 0.0067  0.0138  0.0175  125 SER   C N   
2020 C CA  . SER   B 119 ? 0.1445 0.1408 0.1892 0.0063  0.0155  0.0190  125 SER   C CA  
2021 C C   . SER   B 119 ? 0.1611 0.1585 0.2090 0.0067  0.0175  0.0204  125 SER   C C   
2022 O O   . SER   B 119 ? 0.1567 0.1549 0.2097 0.0065  0.0189  0.0231  125 SER   C O   
2023 C CB  . SER   B 119 ? 0.1531 0.1498 0.2025 0.0062  0.0160  0.0159  125 SER   C CB  
2024 O OG  . SER   B 119 ? 0.1604 0.1581 0.2180 0.0058  0.0179  0.0168  125 SER   C OG  
2025 N N   . THR   B 120 ? 0.1585 0.1560 0.2045 0.0076  0.0179  0.0189  126 THR   C N   
2026 C CA  . THR   B 120 ? 0.1555 0.1543 0.2058 0.0081  0.0205  0.0204  126 THR   C CA  
2027 C C   . THR   B 120 ? 0.1541 0.1518 0.1976 0.0092  0.0210  0.0210  126 THR   C C   
2028 O O   . THR   B 120 ? 0.1545 0.1506 0.1911 0.0096  0.0192  0.0193  126 THR   C O   
2029 C CB  . THR   B 120 ? 0.1550 0.1557 0.2140 0.0080  0.0214  0.0176  126 THR   C CB  
2030 O OG1 . THR   B 120 ? 0.1734 0.1745 0.2300 0.0087  0.0200  0.0145  126 THR   C OG1 
2031 C CG2 . THR   B 120 ? 0.1639 0.1648 0.2287 0.0070  0.0210  0.0160  126 THR   C CG2 
2032 N N   . GLY   B 121 ? 0.1719 0.1703 0.2175 0.0098  0.0239  0.0233  127 GLY   C N   
2033 C CA  . GLY   B 121 ? 0.1882 0.1853 0.2276 0.0112  0.0254  0.0239  127 GLY   C CA  
2034 C C   . GLY   B 121 ? 0.2316 0.2302 0.2768 0.0118  0.0295  0.0261  127 GLY   C C   
2035 O O   . GLY   B 121 ? 0.2577 0.2571 0.3081 0.0113  0.0311  0.0289  127 GLY   C O   
2036 N N   . GLY   B 122 ? 0.2787 0.2775 0.3234 0.0132  0.0316  0.0253  128 GLY   C N   
2037 C CA  . GLY   B 122 ? 0.3058 0.3062 0.3566 0.0140  0.0362  0.0277  128 GLY   C CA  
2038 C C   . GLY   B 122 ? 0.2982 0.3004 0.3532 0.0152  0.0378  0.0256  128 GLY   C C   
2039 O O   . GLY   B 122 ? 0.2980 0.3013 0.3551 0.0151  0.0348  0.0221  128 GLY   C O   
2040 N N   . ASN   B 123 ? 0.2831 0.2857 0.3397 0.0166  0.0426  0.0280  129 ASN   C N   
2041 C CA  . ASN   B 123 ? 0.2807 0.2857 0.3436 0.0179  0.0448  0.0266  129 ASN   C CA  
2042 C C   . ASN   B 123 ? 0.2633 0.2666 0.3189 0.0192  0.0423  0.0234  129 ASN   C C   
2043 O O   . ASN   B 123 ? 0.2915 0.2976 0.3540 0.0199  0.0418  0.0212  129 ASN   C O   
2044 C CB  . ASN   B 123 ? 0.3163 0.3259 0.3946 0.0166  0.0439  0.0248  129 ASN   C CB  
2045 C CG  . ASN   B 123 ? 0.3974 0.4095 0.4871 0.0163  0.0488  0.0278  129 ASN   C CG  
2046 O OD1 . ASN   B 123 ? 0.4112 0.4222 0.4983 0.0177  0.0539  0.0314  129 ASN   C OD1 
2047 N ND2 . ASN   B 123 ? 0.4246 0.4399 0.5273 0.0145  0.0476  0.0263  129 ASN   C ND2 
2048 N N   . GLY   B 124 ? 0.2363 0.2352 0.2786 0.0195  0.0405  0.0233  130 GLY   C N   
2049 C CA  . GLY   B 124 ? 0.2279 0.2245 0.2631 0.0207  0.0382  0.0205  130 GLY   C CA  
2050 C C   . GLY   B 124 ? 0.2091 0.2069 0.2467 0.0196  0.0332  0.0174  130 GLY   C C   
2051 O O   . GLY   B 124 ? 0.2093 0.2059 0.2437 0.0207  0.0314  0.0152  130 GLY   C O   
2052 N N   . LEU   B 125 ? 0.1938 0.1934 0.2363 0.0176  0.0310  0.0174  131 LEU   C N   
2053 C CA  . LEU   B 125 ? 0.1788 0.1791 0.2227 0.0166  0.0266  0.0147  131 LEU   C CA  
2054 C C   . LEU   B 125 ? 0.1886 0.1864 0.2261 0.0150  0.0243  0.0153  131 LEU   C C   
2055 O O   . LEU   B 125 ? 0.2145 0.2116 0.2506 0.0143  0.0257  0.0180  131 LEU   C O   
2056 C CB  . LEU   B 125 ? 0.1909 0.1955 0.2470 0.0156  0.0260  0.0134  131 LEU   C CB  
2057 C CG  . LEU   B 125 ? 0.2252 0.2333 0.2903 0.0168  0.0276  0.0127  131 LEU   C CG  
2058 C CD1 . LEU   B 125 ? 0.2644 0.2765 0.3424 0.0154  0.0277  0.0121  131 LEU   C CD1 
2059 C CD2 . LEU   B 125 ? 0.2562 0.2644 0.3191 0.0183  0.0249  0.0102  131 LEU   C CD2 
2060 N N   . VAL   B 126 ? 0.1551 0.1518 0.1893 0.0146  0.0209  0.0133  132 VAL   C N   
2061 C CA  . VAL   B 126 ? 0.1466 0.1416 0.1769 0.0131  0.0188  0.0138  132 VAL   C CA  
2062 C C   . VAL   B 126 ? 0.1436 0.1403 0.1789 0.0123  0.0167  0.0115  132 VAL   C C   
2063 O O   . VAL   B 126 ? 0.1551 0.1526 0.1912 0.0131  0.0153  0.0091  132 VAL   C O   
2064 C CB  . VAL   B 126 ? 0.1620 0.1531 0.1822 0.0132  0.0170  0.0136  132 VAL   C CB  
2065 C CG1 . VAL   B 126 ? 0.1849 0.1749 0.2026 0.0145  0.0159  0.0113  132 VAL   C CG1 
2066 C CG2 . VAL   B 126 ? 0.1762 0.1662 0.1941 0.0115  0.0148  0.0142  132 VAL   C CG2 
2067 N N   . GLY   B 127 ? 0.1403 0.1376 0.1787 0.0109  0.0165  0.0122  133 GLY   C N   
2068 C CA  . GLY   B 127 ? 0.1413 0.1395 0.1835 0.0102  0.0150  0.0099  133 GLY   C CA  
2069 C C   . GLY   B 127 ? 0.1515 0.1477 0.1890 0.0094  0.0136  0.0102  133 GLY   C C   
2070 O O   . GLY   B 127 ? 0.1574 0.1526 0.1931 0.0087  0.0140  0.0127  133 GLY   C O   
2071 N N   . PHE   B 128 ? 0.1306 0.1263 0.1664 0.0096  0.0119  0.0078  134 PHE   C N   
2072 C CA  . PHE   B 128 ? 0.1398 0.1335 0.1716 0.0090  0.0111  0.0080  134 PHE   C CA  
2073 C C   . PHE   B 128 ? 0.1440 0.1382 0.1795 0.0086  0.0113  0.0061  134 PHE   C C   
2074 O O   . PHE   B 128 ? 0.1551 0.1502 0.1924 0.0092  0.0105  0.0033  134 PHE   C O   
2075 C CB  . PHE   B 128 ? 0.1509 0.1424 0.1755 0.0099  0.0095  0.0070  134 PHE   C CB  
2076 C CG  . PHE   B 128 ? 0.1500 0.1403 0.1705 0.0107  0.0093  0.0080  134 PHE   C CG  
2077 C CD1 . PHE   B 128 ? 0.1584 0.1467 0.1748 0.0099  0.0093  0.0100  134 PHE   C CD1 
2078 C CD2 . PHE   B 128 ? 0.1639 0.1552 0.1851 0.0121  0.0092  0.0067  134 PHE   C CD2 
2079 C CE1 . PHE   B 128 ? 0.1711 0.1575 0.1828 0.0107  0.0093  0.0103  134 PHE   C CE1 
2080 C CE2 . PHE   B 128 ? 0.1784 0.1680 0.1957 0.0131  0.0097  0.0074  134 PHE   C CE2 
2081 C CZ  . PHE   B 128 ? 0.1703 0.1572 0.1824 0.0124  0.0098  0.0091  134 PHE   C CZ  
2082 N N   . ALA   B 129 ? 0.1360 0.1297 0.1728 0.0077  0.0123  0.0075  135 ALA   C N   
2083 C CA  . ALA   B 129 ? 0.1394 0.1328 0.1788 0.0076  0.0131  0.0056  135 ALA   C CA  
2084 C C   . ALA   B 129 ? 0.1623 0.1536 0.1948 0.0082  0.0122  0.0042  135 ALA   C C   
2085 O O   . ALA   B 129 ? 0.1580 0.1480 0.1868 0.0080  0.0122  0.0063  135 ALA   C O   
2086 C CB  . ALA   B 129 ? 0.1521 0.1456 0.1959 0.0067  0.0148  0.0082  135 ALA   C CB  
2087 N N   . ASP   B 130 ? 0.1566 0.1474 0.1873 0.0090  0.0113  0.0010  136 ASP   C N   
2088 C CA  . ASP   B 130 ? 0.1609 0.1495 0.1843 0.0099  0.0106  -0.0001 136 ASP   C CA  
2089 C C   . ASP   B 130 ? 0.1620 0.1490 0.1849 0.0096  0.0129  0.0004  136 ASP   C C   
2090 O O   . ASP   B 130 ? 0.1642 0.1516 0.1922 0.0091  0.0146  -0.0004 136 ASP   C O   
2091 C CB  . ASP   B 130 ? 0.1792 0.1681 0.2010 0.0109  0.0087  -0.0039 136 ASP   C CB  
2092 C CG  . ASP   B 130 ? 0.2091 0.1956 0.2222 0.0123  0.0077  -0.0048 136 ASP   C CG  
2093 O OD1 . ASP   B 130 ? 0.2065 0.1918 0.2150 0.0128  0.0073  -0.0027 136 ASP   C OD1 
2094 O OD2 . ASP   B 130 ? 0.2469 0.2321 0.2573 0.0128  0.0076  -0.0076 136 ASP   C OD2 
2095 N N   . VAL   B 131 ? 0.1607 0.1456 0.1778 0.0101  0.0134  0.0016  137 VAL   C N   
2096 C CA  . VAL   B 131 ? 0.1675 0.1509 0.1839 0.0101  0.0161  0.0022  137 VAL   C CA  
2097 C C   . VAL   B 131 ? 0.1809 0.1615 0.1888 0.0115  0.0163  0.0007  137 VAL   C C   
2098 O O   . VAL   B 131 ? 0.1857 0.1644 0.1917 0.0119  0.0191  0.0012  137 VAL   C O   
2099 C CB  . VAL   B 131 ? 0.1759 0.1594 0.1951 0.0089  0.0175  0.0061  137 VAL   C CB  
2100 C CG1 . VAL   B 131 ? 0.1676 0.1538 0.1946 0.0077  0.0173  0.0078  137 VAL   C CG1 
2101 C CG2 . VAL   B 131 ? 0.1828 0.1651 0.1970 0.0089  0.0159  0.0079  137 VAL   C CG2 
2102 N N   . ARG   B 132 ? 0.1715 0.1517 0.1742 0.0126  0.0135  -0.0007 138 ARG   C N   
2103 C CA  . ARG   B 132 ? 0.1709 0.1483 0.1645 0.0143  0.0132  -0.0014 138 ARG   C CA  
2104 C C   . ARG   B 132 ? 0.1897 0.1654 0.1795 0.0152  0.0143  -0.0046 138 ARG   C C   
2105 O O   . ARG   B 132 ? 0.2106 0.1834 0.1923 0.0166  0.0153  -0.0045 138 ARG   C O   
2106 C CB  . ARG   B 132 ? 0.1668 0.1446 0.1568 0.0154  0.0095  -0.0020 138 ARG   C CB  
2107 C CG  . ARG   B 132 ? 0.1721 0.1501 0.1634 0.0148  0.0090  0.0011  138 ARG   C CG  
2108 C CD  . ARG   B 132 ? 0.1794 0.1578 0.1681 0.0163  0.0057  0.0003  138 ARG   C CD  
2109 N NE  . ARG   B 132 ? 0.1740 0.1557 0.1684 0.0160  0.0039  -0.0020 138 ARG   C NE  
2110 C CZ  . ARG   B 132 ? 0.1856 0.1690 0.1808 0.0171  0.0012  -0.0028 138 ARG   C CZ  
2111 N NH1 . ARG   B 132 ? 0.1809 0.1625 0.1707 0.0188  -0.0002 -0.0017 138 ARG   C NH1 
2112 N NH2 . ARG   B 132 ? 0.1834 0.1701 0.1853 0.0167  0.0001  -0.0046 138 ARG   C NH2 
2113 N N   . ASP   B 133 ? 0.1876 0.1646 0.1828 0.0146  0.0143  -0.0074 139 ASP   C N   
2114 C CA  . ASP   B 133 ? 0.1931 0.1680 0.1845 0.0154  0.0153  -0.0111 139 ASP   C CA  
2115 C C   . ASP   B 133 ? 0.2093 0.1824 0.2025 0.0152  0.0204  -0.0101 139 ASP   C C   
2116 O O   . ASP   B 133 ? 0.2245 0.1947 0.2130 0.0162  0.0222  -0.0130 139 ASP   C O   
2117 C CB  . ASP   B 133 ? 0.2147 0.1913 0.2118 0.0146  0.0130  -0.0150 139 ASP   C CB  
2118 C CG  . ASP   B 133 ? 0.2208 0.1996 0.2290 0.0130  0.0148  -0.0138 139 ASP   C CG  
2119 O OD1 . ASP   B 133 ? 0.2175 0.1981 0.2296 0.0122  0.0153  -0.0099 139 ASP   C OD1 
2120 O OD2 . ASP   B 133 ? 0.2544 0.2327 0.2671 0.0124  0.0159  -0.0167 139 ASP   C OD2 
2121 N N   . LEU   B 134 ? 0.1989 0.1734 0.1984 0.0141  0.0226  -0.0061 140 LEU   C N   
2122 C CA  . LEU   B 134 ? 0.1976 0.1713 0.2014 0.0139  0.0274  -0.0046 140 LEU   C CA  
2123 C C   . LEU   B 134 ? 0.2067 0.1779 0.2039 0.0149  0.0302  -0.0024 140 LEU   C C   
2124 O O   . LEU   B 134 ? 0.2077 0.1798 0.2079 0.0141  0.0313  0.0017  140 LEU   C O   
2125 C CB  . LEU   B 134 ? 0.1902 0.1672 0.2046 0.0122  0.0277  -0.0012 140 LEU   C CB  
2126 C CG  . LEU   B 134 ? 0.2006 0.1800 0.2217 0.0112  0.0253  -0.0026 140 LEU   C CG  
2127 C CD1 . LEU   B 134 ? 0.2152 0.1975 0.2450 0.0098  0.0253  0.0014  140 LEU   C CD1 
2128 C CD2 . LEU   B 134 ? 0.2171 0.1951 0.2409 0.0116  0.0271  -0.0064 140 LEU   C CD2 
2129 N N   . LEU   B 135 ? 0.2106 0.1782 0.1978 0.0167  0.0312  -0.0051 141 LEU   C N   
2130 C CA  . LEU   B 135 ? 0.2287 0.1935 0.2081 0.0180  0.0339  -0.0026 141 LEU   C CA  
2131 C C   . LEU   B 135 ? 0.2247 0.1892 0.2092 0.0177  0.0397  0.0004  141 LEU   C C   
2132 O O   . LEU   B 135 ? 0.2404 0.2039 0.2229 0.0179  0.0418  0.0041  141 LEU   C O   
2133 C CB  . LEU   B 135 ? 0.2280 0.1889 0.1945 0.0202  0.0336  -0.0060 141 LEU   C CB  
2134 C CG  . LEU   B 135 ? 0.2416 0.2034 0.2040 0.0205  0.0273  -0.0095 141 LEU   C CG  
2135 C CD1 . LEU   B 135 ? 0.2570 0.2148 0.2060 0.0228  0.0265  -0.0128 141 LEU   C CD1 
2136 C CD2 . LEU   B 135 ? 0.2525 0.2165 0.2161 0.0200  0.0235  -0.0065 141 LEU   C CD2 
2137 N N   . TRP   B 136 ? 0.2253 0.1906 0.2175 0.0173  0.0423  -0.0007 142 TRP   C N   
2138 C CA  . TRP   B 136 ? 0.2303 0.1957 0.2290 0.0173  0.0480  0.0022  142 TRP   C CA  
2139 C C   . TRP   B 136 ? 0.2322 0.2013 0.2402 0.0154  0.0473  0.0073  142 TRP   C C   
2140 O O   . TRP   B 136 ? 0.2484 0.2178 0.2618 0.0153  0.0516  0.0105  142 TRP   C O   
2141 C CB  . TRP   B 136 ? 0.2336 0.1991 0.2390 0.0175  0.0505  -0.0004 142 TRP   C CB  
2142 C CG  . TRP   B 136 ? 0.2237 0.1924 0.2371 0.0160  0.0464  -0.0015 142 TRP   C CG  
2143 C CD1 . TRP   B 136 ? 0.2402 0.2082 0.2511 0.0160  0.0430  -0.0059 142 TRP   C CD1 
2144 C CD2 . TRP   B 136 ? 0.2270 0.1999 0.2525 0.0143  0.0455  0.0021  142 TRP   C CD2 
2145 N NE1 . TRP   B 136 ? 0.2440 0.2156 0.2650 0.0144  0.0405  -0.0050 142 TRP   C NE1 
2146 C CE2 . TRP   B 136 ? 0.2373 0.2116 0.2666 0.0135  0.0421  -0.0001 142 TRP   C CE2 
2147 C CE3 . TRP   B 136 ? 0.2221 0.1975 0.2556 0.0134  0.0472  0.0070  142 TRP   C CE3 
2148 C CZ2 . TRP   B 136 ? 0.2302 0.2082 0.2698 0.0120  0.0405  0.0028  142 TRP   C CZ2 
2149 C CZ3 . TRP   B 136 ? 0.2225 0.2018 0.2664 0.0119  0.0450  0.0095  142 TRP   C CZ3 
2150 C CH2 . TRP   B 136 ? 0.2213 0.2016 0.2674 0.0114  0.0418  0.0075  142 TRP   C CH2 
2151 N N   . LEU   B 137 ? 0.2188 0.1903 0.2288 0.0139  0.0420  0.0081  143 LEU   C N   
2152 C CA  . LEU   B 137 ? 0.2235 0.1978 0.2406 0.0120  0.0409  0.0124  143 LEU   C CA  
2153 C C   . LEU   B 137 ? 0.2586 0.2308 0.2713 0.0122  0.0429  0.0153  143 LEU   C C   
2154 O O   . LEU   B 137 ? 0.2703 0.2442 0.2899 0.0107  0.0433  0.0190  143 LEU   C O   
2155 C CB  . LEU   B 137 ? 0.2228 0.1992 0.2406 0.0107  0.0352  0.0123  143 LEU   C CB  
2156 C CG  . LEU   B 137 ? 0.2152 0.1941 0.2397 0.0101  0.0334  0.0109  143 LEU   C CG  
2157 C CD1 . LEU   B 137 ? 0.2112 0.1914 0.2338 0.0093  0.0283  0.0102  143 LEU   C CD1 
2158 C CD2 . LEU   B 137 ? 0.2209 0.2029 0.2567 0.0088  0.0348  0.0142  143 LEU   C CD2 
2159 N N   . ASP   B 138 ? 0.2449 0.2133 0.2462 0.0141  0.0438  0.0138  144 ASP   C N   
2160 C CA  . ASP   B 138 ? 0.2692 0.2352 0.2658 0.0144  0.0459  0.0169  144 ASP   C CA  
2161 C C   . ASP   B 138 ? 0.3088 0.2732 0.3068 0.0154  0.0528  0.0189  144 ASP   C C   
2162 O O   . ASP   B 138 ? 0.3201 0.2823 0.3148 0.0157  0.0554  0.0220  144 ASP   C O   
2163 C CB  . ASP   B 138 ? 0.2771 0.2395 0.2604 0.0163  0.0438  0.0151  144 ASP   C CB  
2164 C CG  . ASP   B 138 ? 0.2947 0.2584 0.2766 0.0157  0.0375  0.0137  144 ASP   C CG  
2165 O OD1 . ASP   B 138 ? 0.2823 0.2490 0.2723 0.0137  0.0350  0.0147  144 ASP   C OD1 
2166 O OD2 . ASP   B 138 ? 0.3287 0.2904 0.3012 0.0174  0.0351  0.0117  144 ASP   C OD2 
2167 N N   . GLU   B 139 ? 0.3247 0.2900 0.3276 0.0159  0.0561  0.0175  145 GLU   C N   
2168 C CA  . GLU   B 139 ? 0.3836 0.3472 0.3878 0.0172  0.0634  0.0193  145 GLU   C CA  
2169 C C   . GLU   B 139 ? 0.4286 0.3960 0.4475 0.0161  0.0661  0.0211  145 GLU   C C   
2170 O O   . GLU   B 139 ? 0.4386 0.4091 0.4646 0.0150  0.0625  0.0199  145 GLU   C O   
2171 C CB  . GLU   B 139 ? 0.4443 0.4032 0.4360 0.0200  0.0664  0.0153  145 GLU   C CB  
2172 C CG  . GLU   B 139 ? 0.5347 0.4942 0.5274 0.0203  0.0642  0.0103  145 GLU   C CG  
2173 C CD  . GLU   B 139 ? 0.6553 0.6105 0.6340 0.0225  0.0634  0.0051  145 GLU   C CD  
2174 O OE1 . GLU   B 139 ? 0.6661 0.6208 0.6459 0.0228  0.0631  0.0009  145 GLU   C OE1 
2175 O OE2 . GLU   B 139 ? 0.6919 0.6440 0.6588 0.0238  0.0627  0.0054  145 GLU   C OE2 
2176 N N   . GLU   B 140 ? 0.4605 0.4278 0.4848 0.0166  0.0724  0.0244  146 GLU   C N   
2177 C CA  . GLU   B 140 ? 0.4864 0.4577 0.5260 0.0158  0.0752  0.0268  146 GLU   C CA  
2178 C C   . GLU   B 140 ? 0.5009 0.4720 0.5427 0.0172  0.0768  0.0233  146 GLU   C C   
2179 O O   . GLU   B 140 ? 0.5172 0.4840 0.5483 0.0193  0.0786  0.0190  146 GLU   C O   
2180 C CB  . GLU   B 140 ? 0.5394 0.5102 0.5838 0.0163  0.0825  0.0311  146 GLU   C CB  
2181 C CG  . GLU   B 140 ? 0.6364 0.6117 0.6977 0.0159  0.0860  0.0339  146 GLU   C CG  
2182 C CD  . GLU   B 140 ? 0.7505 0.7232 0.8117 0.0188  0.0951  0.0335  146 GLU   C CD  
2183 O OE1 . GLU   B 140 ? 0.7611 0.7302 0.8153 0.0202  0.1007  0.0348  146 GLU   C OE1 
2184 O OE2 . GLU   B 140 ? 0.7992 0.7730 0.8670 0.0198  0.0969  0.0319  146 GLU   C OE2 
2185 N N1  . A1B53 C .   ? 0.2246 0.1968 0.2679 0.0212  0.0378  -0.0122 201 A1B53 A N1  
2186 C C4  . A1B53 C .   ? 0.2327 0.2119 0.2624 0.0168  0.0412  -0.0178 201 A1B53 A C4  
2187 C C5  . A1B53 C .   ? 0.2281 0.2108 0.2493 0.0146  0.0382  -0.0169 201 A1B53 A C5  
2188 C C6  . A1B53 C .   ? 0.2187 0.2030 0.2345 0.0138  0.0320  -0.0136 201 A1B53 A C6  
2189 C C7  . A1B53 C .   ? 0.2174 0.2001 0.2352 0.0149  0.0289  -0.0116 201 A1B53 A C7  
2190 C C8  . A1B53 C .   ? 0.2195 0.2034 0.2321 0.0138  0.0235  -0.0089 201 A1B53 A C8  
2191 C C10 . A1B53 C .   ? 0.2139 0.1918 0.2602 0.0204  0.0327  -0.0036 201 A1B53 A C10 
2192 C C13 . A1B53 C .   ? 0.2162 0.1872 0.2585 0.0149  0.0336  -0.0089 201 A1B53 A C13 
2193 O O2  . A1B53 C .   ? 0.2635 0.2263 0.2986 0.0160  0.0415  -0.0227 201 A1B53 A O2  
2194 C C14 . A1B53 C .   ? 0.2376 0.2041 0.2779 0.0191  0.0385  -0.0164 201 A1B53 A C14 
2195 C C11 . A1B53 C .   ? 0.2068 0.1851 0.2480 0.0144  0.0289  -0.0019 201 A1B53 A C11 
2196 C C12 . A1B53 C .   ? 0.2027 0.1839 0.2501 0.0146  0.0280  0.0041  201 A1B53 A C12 
2197 O O1  . A1B53 C .   ? 0.2118 0.1887 0.2720 0.0211  0.0325  0.0049  201 A1B53 A O1  
2198 N N2  . A1B53 C .   ? 0.1881 0.1778 0.2265 0.0066  0.0227  0.0084  201 A1B53 A N2  
2199 C C2  . A1B53 C .   ? 0.2373 0.2115 0.2803 0.0209  0.0414  -0.0145 201 A1B53 A C2  
2200 C C1  . A1B53 C .   ? 0.2451 0.2238 0.3009 0.0251  0.0437  -0.0093 201 A1B53 A C1  
2201 O O   . A1B53 C .   ? 0.2386 0.2237 0.2957 0.0262  0.0396  -0.0035 201 A1B53 A O   
2202 N N   . A1B53 C .   ? 0.2430 0.2182 0.3086 0.0273  0.0504  -0.0114 201 A1B53 A N   
2203 C C   . A1B53 C .   ? 0.2467 0.2265 0.3270 0.0316  0.0532  -0.0060 201 A1B53 A C   
2204 C C3  . A1B53 C .   ? 0.2291 0.2067 0.2609 0.0180  0.0378  -0.0151 201 A1B53 A C3  
2205 C C9  . A1B53 C .   ? 0.2257 0.2053 0.2511 0.0168  0.0317  -0.0123 201 A1B53 A C9  
# 
