data_7I4V
# 
_entry.id   7I4V 
# 
_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   7I4V         pdb_00007i4v 10.2210/pdb7i4v/pdb 
WWPDB D_1001408318 ?            ?                   
# 
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                        7I4V 
_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 '1-[(3S)-3-(difluoromethyl)piperidin-1-yl]-2-[2-(methylsulfanyl)phenyl]ethan-1-one' 299.379   1   ?         ? ? 
? 
3 non-polymer syn 'ZINC ION'                                                                          65.409    2   ?         ? ? 
? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                78.133    3   ?         ? ? 
? 
5 water       nat water                                                                               18.015    357 ?         ? ? 
? 
# 
_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 '1-[(3S)-3-(difluoromethyl)piperidin-1-yl]-2-[2-(methylsulfanyl)phenyl]ethan-1-one' A1B3C 
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 
A1B3C non-polymer         . '1-[(3S)-3-(difluoromethyl)piperidin-1-yl]-2-[2-(methylsulfanyl)phenyl]ethan-1-one' ? 
'C15 H19 F2 N O S' 299.379 
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        A1B3C 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B3C 
_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 A1B3C 1   201 201 A1B3C LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 1   DMS   DMS A . 
F 3 ZN    1   201 1   ZN    ZN  C . 
G 4 DMS   1   202 1   DMS   DMS C . 
H 4 DMS   1   203 6   DMS   DMS C . 
I 5 HOH   1   301 357 HOH   HOH A . 
I 5 HOH   2   302 92  HOH   HOH A . 
I 5 HOH   3   303 41  HOH   HOH A . 
I 5 HOH   4   304 354 HOH   HOH A . 
I 5 HOH   5   305 166 HOH   HOH A . 
I 5 HOH   6   306 318 HOH   HOH A . 
I 5 HOH   7   307 226 HOH   HOH A . 
I 5 HOH   8   308 132 HOH   HOH A . 
I 5 HOH   9   309 232 HOH   HOH A . 
I 5 HOH   10  310 100 HOH   HOH A . 
I 5 HOH   11  311 320 HOH   HOH A . 
I 5 HOH   12  312 83  HOH   HOH A . 
I 5 HOH   13  313 293 HOH   HOH A . 
I 5 HOH   14  314 203 HOH   HOH A . 
I 5 HOH   15  315 124 HOH   HOH A . 
I 5 HOH   16  316 104 HOH   HOH A . 
I 5 HOH   17  317 176 HOH   HOH A . 
I 5 HOH   18  318 165 HOH   HOH A . 
I 5 HOH   19  319 75  HOH   HOH A . 
I 5 HOH   20  320 26  HOH   HOH A . 
I 5 HOH   21  321 168 HOH   HOH A . 
I 5 HOH   22  322 237 HOH   HOH A . 
I 5 HOH   23  323 235 HOH   HOH A . 
I 5 HOH   24  324 22  HOH   HOH A . 
I 5 HOH   25  325 98  HOH   HOH A . 
I 5 HOH   26  326 72  HOH   HOH A . 
I 5 HOH   27  327 317 HOH   HOH A . 
I 5 HOH   28  328 5   HOH   HOH A . 
I 5 HOH   29  329 139 HOH   HOH A . 
I 5 HOH   30  330 356 HOH   HOH A . 
I 5 HOH   31  331 239 HOH   HOH A . 
I 5 HOH   32  332 215 HOH   HOH A . 
I 5 HOH   33  333 164 HOH   HOH A . 
I 5 HOH   34  334 60  HOH   HOH A . 
I 5 HOH   35  335 53  HOH   HOH A . 
I 5 HOH   36  336 84  HOH   HOH A . 
I 5 HOH   37  337 111 HOH   HOH A . 
I 5 HOH   38  338 73  HOH   HOH A . 
I 5 HOH   39  339 218 HOH   HOH A . 
I 5 HOH   40  340 313 HOH   HOH A . 
I 5 HOH   41  341 251 HOH   HOH A . 
I 5 HOH   42  342 8   HOH   HOH A . 
I 5 HOH   43  343 348 HOH   HOH A . 
I 5 HOH   44  344 15  HOH   HOH A . 
I 5 HOH   45  345 16  HOH   HOH A . 
I 5 HOH   46  346 275 HOH   HOH A . 
I 5 HOH   47  347 154 HOH   HOH A . 
I 5 HOH   48  348 20  HOH   HOH A . 
I 5 HOH   49  349 307 HOH   HOH A . 
I 5 HOH   50  350 87  HOH   HOH A . 
I 5 HOH   51  351 3   HOH   HOH A . 
I 5 HOH   52  352 135 HOH   HOH A . 
I 5 HOH   53  353 90  HOH   HOH A . 
I 5 HOH   54  354 177 HOH   HOH A . 
I 5 HOH   55  355 28  HOH   HOH A . 
I 5 HOH   56  356 142 HOH   HOH A . 
I 5 HOH   57  357 210 HOH   HOH A . 
I 5 HOH   58  358 259 HOH   HOH A . 
I 5 HOH   59  359 267 HOH   HOH A . 
I 5 HOH   60  360 243 HOH   HOH A . 
I 5 HOH   61  361 238 HOH   HOH A . 
I 5 HOH   62  362 266 HOH   HOH A . 
I 5 HOH   63  363 82  HOH   HOH A . 
I 5 HOH   64  364 64  HOH   HOH A . 
I 5 HOH   65  365 155 HOH   HOH A . 
I 5 HOH   66  366 95  HOH   HOH A . 
I 5 HOH   67  367 62  HOH   HOH A . 
I 5 HOH   68  368 175 HOH   HOH A . 
I 5 HOH   69  369 48  HOH   HOH A . 
I 5 HOH   70  370 45  HOH   HOH A . 
I 5 HOH   71  371 153 HOH   HOH A . 
I 5 HOH   72  372 214 HOH   HOH A . 
I 5 HOH   73  373 12  HOH   HOH A . 
I 5 HOH   74  374 192 HOH   HOH A . 
I 5 HOH   75  375 260 HOH   HOH A . 
I 5 HOH   76  376 253 HOH   HOH A . 
I 5 HOH   77  377 40  HOH   HOH A . 
I 5 HOH   78  378 184 HOH   HOH A . 
I 5 HOH   79  379 183 HOH   HOH A . 
I 5 HOH   80  380 68  HOH   HOH A . 
I 5 HOH   81  381 236 HOH   HOH A . 
I 5 HOH   82  382 140 HOH   HOH A . 
I 5 HOH   83  383 197 HOH   HOH A . 
I 5 HOH   84  384 156 HOH   HOH A . 
I 5 HOH   85  385 148 HOH   HOH A . 
I 5 HOH   86  386 179 HOH   HOH A . 
I 5 HOH   87  387 305 HOH   HOH A . 
I 5 HOH   88  388 18  HOH   HOH A . 
I 5 HOH   89  389 52  HOH   HOH A . 
I 5 HOH   90  390 343 HOH   HOH A . 
I 5 HOH   91  391 24  HOH   HOH A . 
I 5 HOH   92  392 303 HOH   HOH A . 
I 5 HOH   93  393 50  HOH   HOH A . 
I 5 HOH   94  394 230 HOH   HOH A . 
I 5 HOH   95  395 43  HOH   HOH A . 
I 5 HOH   96  396 334 HOH   HOH A . 
I 5 HOH   97  397 314 HOH   HOH A . 
I 5 HOH   98  398 265 HOH   HOH A . 
I 5 HOH   99  399 196 HOH   HOH A . 
I 5 HOH   100 400 96  HOH   HOH A . 
I 5 HOH   101 401 66  HOH   HOH A . 
I 5 HOH   102 402 113 HOH   HOH A . 
I 5 HOH   103 403 149 HOH   HOH A . 
I 5 HOH   104 404 180 HOH   HOH A . 
I 5 HOH   105 405 270 HOH   HOH A . 
I 5 HOH   106 406 208 HOH   HOH A . 
I 5 HOH   107 407 258 HOH   HOH A . 
I 5 HOH   108 408 201 HOH   HOH A . 
I 5 HOH   109 409 47  HOH   HOH A . 
I 5 HOH   110 410 33  HOH   HOH A . 
I 5 HOH   111 411 347 HOH   HOH A . 
I 5 HOH   112 412 185 HOH   HOH A . 
I 5 HOH   113 413 342 HOH   HOH A . 
I 5 HOH   114 414 241 HOH   HOH A . 
I 5 HOH   115 415 246 HOH   HOH A . 
I 5 HOH   116 416 332 HOH   HOH A . 
I 5 HOH   117 417 190 HOH   HOH A . 
I 5 HOH   118 418 194 HOH   HOH A . 
I 5 HOH   119 419 316 HOH   HOH A . 
I 5 HOH   120 420 108 HOH   HOH A . 
I 5 HOH   121 421 324 HOH   HOH A . 
I 5 HOH   122 422 144 HOH   HOH A . 
I 5 HOH   123 423 217 HOH   HOH A . 
I 5 HOH   124 424 114 HOH   HOH A . 
I 5 HOH   125 425 2   HOH   HOH A . 
I 5 HOH   126 426 186 HOH   HOH A . 
I 5 HOH   127 427 138 HOH   HOH A . 
I 5 HOH   128 428 193 HOH   HOH A . 
I 5 HOH   129 429 294 HOH   HOH A . 
I 5 HOH   130 430 219 HOH   HOH A . 
I 5 HOH   131 431 340 HOH   HOH A . 
I 5 HOH   132 432 329 HOH   HOH A . 
I 5 HOH   133 433 309 HOH   HOH A . 
I 5 HOH   134 434 70  HOH   HOH A . 
I 5 HOH   135 435 29  HOH   HOH A . 
I 5 HOH   136 436 55  HOH   HOH A . 
I 5 HOH   137 437 76  HOH   HOH A . 
I 5 HOH   138 438 56  HOH   HOH A . 
I 5 HOH   139 439 67  HOH   HOH A . 
I 5 HOH   140 440 7   HOH   HOH A . 
I 5 HOH   141 441 311 HOH   HOH A . 
I 5 HOH   142 442 308 HOH   HOH A . 
I 5 HOH   143 443 350 HOH   HOH A . 
I 5 HOH   144 444 223 HOH   HOH A . 
I 5 HOH   145 445 242 HOH   HOH A . 
I 5 HOH   146 446 59  HOH   HOH A . 
I 5 HOH   147 447 326 HOH   HOH A . 
I 5 HOH   148 448 126 HOH   HOH A . 
I 5 HOH   149 449 325 HOH   HOH A . 
I 5 HOH   150 450 280 HOH   HOH A . 
I 5 HOH   151 451 121 HOH   HOH A . 
I 5 HOH   152 452 117 HOH   HOH A . 
I 5 HOH   153 453 181 HOH   HOH A . 
I 5 HOH   154 454 274 HOH   HOH A . 
I 5 HOH   155 455 297 HOH   HOH A . 
I 5 HOH   156 456 353 HOH   HOH A . 
I 5 HOH   157 457 146 HOH   HOH A . 
I 5 HOH   158 458 187 HOH   HOH A . 
I 5 HOH   159 459 189 HOH   HOH A . 
I 5 HOH   160 460 202 HOH   HOH A . 
I 5 HOH   161 461 116 HOH   HOH A . 
I 5 HOH   162 462 231 HOH   HOH A . 
I 5 HOH   163 463 157 HOH   HOH A . 
I 5 HOH   164 464 212 HOH   HOH A . 
I 5 HOH   165 465 103 HOH   HOH A . 
I 5 HOH   166 466 284 HOH   HOH A . 
I 5 HOH   167 467 355 HOH   HOH A . 
I 5 HOH   168 468 249 HOH   HOH A . 
J 5 HOH   1   301 335 HOH   HOH C . 
J 5 HOH   2   302 292 HOH   HOH C . 
J 5 HOH   3   303 120 HOH   HOH C . 
J 5 HOH   4   304 344 HOH   HOH C . 
J 5 HOH   5   305 141 HOH   HOH C . 
J 5 HOH   6   306 328 HOH   HOH C . 
J 5 HOH   7   307 341 HOH   HOH C . 
J 5 HOH   8   308 339 HOH   HOH C . 
J 5 HOH   9   309 256 HOH   HOH C . 
J 5 HOH   10  310 173 HOH   HOH C . 
J 5 HOH   11  311 271 HOH   HOH C . 
J 5 HOH   12  312 109 HOH   HOH C . 
J 5 HOH   13  313 51  HOH   HOH C . 
J 5 HOH   14  314 61  HOH   HOH C . 
J 5 HOH   15  315 6   HOH   HOH C . 
J 5 HOH   16  316 182 HOH   HOH C . 
J 5 HOH   17  317 171 HOH   HOH C . 
J 5 HOH   18  318 273 HOH   HOH C . 
J 5 HOH   19  319 136 HOH   HOH C . 
J 5 HOH   20  320 49  HOH   HOH C . 
J 5 HOH   21  321 220 HOH   HOH C . 
J 5 HOH   22  322 323 HOH   HOH C . 
J 5 HOH   23  323 128 HOH   HOH C . 
J 5 HOH   24  324 130 HOH   HOH C . 
J 5 HOH   25  325 122 HOH   HOH C . 
J 5 HOH   26  326 327 HOH   HOH C . 
J 5 HOH   27  327 170 HOH   HOH C . 
J 5 HOH   28  328 36  HOH   HOH C . 
J 5 HOH   29  329 1   HOH   HOH C . 
J 5 HOH   30  330 46  HOH   HOH C . 
J 5 HOH   31  331 209 HOH   HOH C . 
J 5 HOH   32  332 276 HOH   HOH C . 
J 5 HOH   33  333 268 HOH   HOH C . 
J 5 HOH   34  334 277 HOH   HOH C . 
J 5 HOH   35  335 91  HOH   HOH C . 
J 5 HOH   36  336 88  HOH   HOH C . 
J 5 HOH   37  337 85  HOH   HOH C . 
J 5 HOH   38  338 27  HOH   HOH C . 
J 5 HOH   39  339 229 HOH   HOH C . 
J 5 HOH   40  340 9   HOH   HOH C . 
J 5 HOH   41  341 106 HOH   HOH C . 
J 5 HOH   42  342 105 HOH   HOH C . 
J 5 HOH   43  343 13  HOH   HOH C . 
J 5 HOH   44  344 252 HOH   HOH C . 
J 5 HOH   45  345 287 HOH   HOH C . 
J 5 HOH   46  346 80  HOH   HOH C . 
J 5 HOH   47  347 336 HOH   HOH C . 
J 5 HOH   48  348 205 HOH   HOH C . 
J 5 HOH   49  349 25  HOH   HOH C . 
J 5 HOH   50  350 93  HOH   HOH C . 
J 5 HOH   51  351 145 HOH   HOH C . 
J 5 HOH   52  352 304 HOH   HOH C . 
J 5 HOH   53  353 79  HOH   HOH C . 
J 5 HOH   54  354 178 HOH   HOH C . 
J 5 HOH   55  355 319 HOH   HOH C . 
J 5 HOH   56  356 289 HOH   HOH C . 
J 5 HOH   57  357 97  HOH   HOH C . 
J 5 HOH   58  358 78  HOH   HOH C . 
J 5 HOH   59  359 188 HOH   HOH C . 
J 5 HOH   60  360 39  HOH   HOH C . 
J 5 HOH   61  361 161 HOH   HOH C . 
J 5 HOH   62  362 198 HOH   HOH C . 
J 5 HOH   63  363 211 HOH   HOH C . 
J 5 HOH   64  364 110 HOH   HOH C . 
J 5 HOH   65  365 169 HOH   HOH C . 
J 5 HOH   66  366 38  HOH   HOH C . 
J 5 HOH   67  367 54  HOH   HOH C . 
J 5 HOH   68  368 290 HOH   HOH C . 
J 5 HOH   69  369 279 HOH   HOH C . 
J 5 HOH   70  370 330 HOH   HOH C . 
J 5 HOH   71  371 125 HOH   HOH C . 
J 5 HOH   72  372 158 HOH   HOH C . 
J 5 HOH   73  373 191 HOH   HOH C . 
J 5 HOH   74  374 227 HOH   HOH C . 
J 5 HOH   75  375 30  HOH   HOH C . 
J 5 HOH   76  376 338 HOH   HOH C . 
J 5 HOH   77  377 123 HOH   HOH C . 
J 5 HOH   78  378 312 HOH   HOH C . 
J 5 HOH   79  379 321 HOH   HOH C . 
J 5 HOH   80  380 143 HOH   HOH C . 
J 5 HOH   81  381 150 HOH   HOH C . 
J 5 HOH   82  382 310 HOH   HOH C . 
J 5 HOH   83  383 58  HOH   HOH C . 
J 5 HOH   84  384 10  HOH   HOH C . 
J 5 HOH   85  385 254 HOH   HOH C . 
J 5 HOH   86  386 244 HOH   HOH C . 
J 5 HOH   87  387 134 HOH   HOH C . 
J 5 HOH   88  388 69  HOH   HOH C . 
J 5 HOH   89  389 322 HOH   HOH C . 
J 5 HOH   90  390 74  HOH   HOH C . 
J 5 HOH   91  391 233 HOH   HOH C . 
J 5 HOH   92  392 37  HOH   HOH C . 
J 5 HOH   93  393 102 HOH   HOH C . 
J 5 HOH   94  394 224 HOH   HOH C . 
J 5 HOH   95  395 333 HOH   HOH C . 
J 5 HOH   96  396 42  HOH   HOH C . 
J 5 HOH   97  397 160 HOH   HOH C . 
J 5 HOH   98  398 14  HOH   HOH C . 
J 5 HOH   99  399 21  HOH   HOH C . 
J 5 HOH   100 400 89  HOH   HOH C . 
J 5 HOH   101 401 23  HOH   HOH C . 
J 5 HOH   102 402 228 HOH   HOH C . 
J 5 HOH   103 403 94  HOH   HOH C . 
J 5 HOH   104 404 35  HOH   HOH C . 
J 5 HOH   105 405 118 HOH   HOH C . 
J 5 HOH   106 406 107 HOH   HOH C . 
J 5 HOH   107 407 204 HOH   HOH C . 
J 5 HOH   108 408 71  HOH   HOH C . 
J 5 HOH   109 409 147 HOH   HOH C . 
J 5 HOH   110 410 216 HOH   HOH C . 
J 5 HOH   111 411 133 HOH   HOH C . 
J 5 HOH   112 412 81  HOH   HOH C . 
J 5 HOH   113 413 77  HOH   HOH C . 
J 5 HOH   114 414 34  HOH   HOH C . 
J 5 HOH   115 415 286 HOH   HOH C . 
J 5 HOH   116 416 152 HOH   HOH C . 
J 5 HOH   117 417 32  HOH   HOH C . 
J 5 HOH   118 418 44  HOH   HOH C . 
J 5 HOH   119 419 315 HOH   HOH C . 
J 5 HOH   120 420 221 HOH   HOH C . 
J 5 HOH   121 421 174 HOH   HOH C . 
J 5 HOH   122 422 247 HOH   HOH C . 
J 5 HOH   123 423 101 HOH   HOH C . 
J 5 HOH   124 424 234 HOH   HOH C . 
J 5 HOH   125 425 131 HOH   HOH C . 
J 5 HOH   126 426 337 HOH   HOH C . 
J 5 HOH   127 427 151 HOH   HOH C . 
J 5 HOH   128 428 291 HOH   HOH C . 
J 5 HOH   129 429 306 HOH   HOH C . 
J 5 HOH   130 430 206 HOH   HOH C . 
J 5 HOH   131 431 240 HOH   HOH C . 
J 5 HOH   132 432 4   HOH   HOH C . 
J 5 HOH   133 433 99  HOH   HOH C . 
J 5 HOH   134 434 19  HOH   HOH C . 
J 5 HOH   135 435 127 HOH   HOH C . 
J 5 HOH   136 436 200 HOH   HOH C . 
J 5 HOH   137 437 63  HOH   HOH C . 
J 5 HOH   138 438 31  HOH   HOH C . 
J 5 HOH   139 439 65  HOH   HOH C . 
J 5 HOH   140 440 57  HOH   HOH C . 
J 5 HOH   141 441 245 HOH   HOH C . 
J 5 HOH   142 442 11  HOH   HOH C . 
J 5 HOH   143 443 207 HOH   HOH C . 
J 5 HOH   144 444 167 HOH   HOH C . 
J 5 HOH   145 445 278 HOH   HOH C . 
J 5 HOH   146 446 264 HOH   HOH C . 
J 5 HOH   147 447 172 HOH   HOH C . 
J 5 HOH   148 448 199 HOH   HOH C . 
J 5 HOH   149 449 281 HOH   HOH C . 
J 5 HOH   150 450 137 HOH   HOH C . 
J 5 HOH   151 451 17  HOH   HOH C . 
J 5 HOH   152 452 262 HOH   HOH C . 
J 5 HOH   153 453 300 HOH   HOH C . 
J 5 HOH   154 454 299 HOH   HOH C . 
J 5 HOH   155 455 129 HOH   HOH C . 
J 5 HOH   156 456 261 HOH   HOH C . 
J 5 HOH   157 457 119 HOH   HOH C . 
J 5 HOH   158 458 345 HOH   HOH C . 
J 5 HOH   159 459 301 HOH   HOH C . 
J 5 HOH   160 460 346 HOH   HOH C . 
J 5 HOH   161 461 115 HOH   HOH C . 
J 5 HOH   162 462 272 HOH   HOH C . 
J 5 HOH   163 463 86  HOH   HOH C . 
J 5 HOH   164 464 349 HOH   HOH C . 
J 5 HOH   165 465 263 HOH   HOH C . 
J 5 HOH   166 466 255 HOH   HOH C . 
J 5 HOH   167 467 222 HOH   HOH C . 
J 5 HOH   168 468 283 HOH   HOH C . 
J 5 HOH   169 469 250 HOH   HOH C . 
J 5 HOH   170 470 225 HOH   HOH C . 
J 5 HOH   171 471 285 HOH   HOH C . 
J 5 HOH   172 472 195 HOH   HOH C . 
J 5 HOH   173 473 296 HOH   HOH C . 
J 5 HOH   174 474 163 HOH   HOH C . 
J 5 HOH   175 475 162 HOH   HOH C . 
J 5 HOH   176 476 331 HOH   HOH C . 
J 5 HOH   177 477 351 HOH   HOH C . 
J 5 HOH   178 478 295 HOH   HOH C . 
J 5 HOH   179 479 302 HOH   HOH C . 
J 5 HOH   180 480 112 HOH   HOH C . 
J 5 HOH   181 481 159 HOH   HOH C . 
J 5 HOH   182 482 282 HOH   HOH C . 
J 5 HOH   183 483 288 HOH   HOH C . 
J 5 HOH   184 484 213 HOH   HOH C . 
J 5 HOH   185 485 248 HOH   HOH C . 
J 5 HOH   186 486 298 HOH   HOH C . 
J 5 HOH   187 487 269 HOH   HOH C . 
J 5 HOH   188 488 352 HOH   HOH C . 
J 5 HOH   189 489 257 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           7I4V 
_cell.length_a           86.749 
_cell.length_b           57.036 
_cell.length_c           64.923 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.72 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I4V 
_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          7I4V 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.52 
_exptl_crystal.density_percent_sol   51.15 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-01-16 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92201 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I4V 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             39.21 
_reflns.d_resolution_high            1.15 
_reflns.number_obs                   74807 
_reflns.percent_possible_obs         66.9 
_reflns.pdbx_Rmerge_I_obs            0.055 
_reflns.pdbx_netI_over_sigmaI        19.8 
_reflns.pdbx_redundancy              6.0 
_reflns.pdbx_Rrim_I_all              0.060 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     452251 
_reflns.pdbx_chi_squared             1.17 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.15 
_reflns_shell.d_res_low                   1.17 
_reflns_shell.number_measured_all         324 
_reflns_shell.number_unique_obs           203 
_reflns_shell.Rmerge_I_obs                0.771 
_reflns_shell.pdbx_chi_squared            0.42 
_reflns_shell.pdbx_redundancy             1.6 
_reflns_shell.percent_possible_obs        3.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.6 
_reflns_shell.pdbx_Rrim_I_all             1.090 
_reflns_shell.pdbx_Rpim_I_all             0.771 
_reflns_shell.pdbx_CC_half                0.299 
_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                                 7I4V 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     74799 
_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                             39.20 
_refine.ls_d_res_high                            1.150 
_refine.ls_percent_reflns_obs                    66.8 
_refine.ls_R_factor_obs                          0.1826 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1821 
_refine.ls_R_factor_R_free                       0.1920 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.030 
_refine.ls_number_reflns_R_free                  3766 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.946 
_refine.correlation_coeff_Fo_to_Fc_free          0.963 
_refine.B_iso_mean                               19.54 
_refine.aniso_B[1][1]                            -0.21290 
_refine.aniso_B[2][2]                            -0.27070 
_refine.aniso_B[3][3]                            0.48360 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.25550 
_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             0.048 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.047 
_refine.pdbx_overall_SU_R_Blow_DPI               0.051 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.049 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I4V 
_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         34 
_refine_hist.number_atoms_solvent             356 
_refine_hist.number_atoms_total               2556 
_refine_hist.d_res_high                       1.150 
_refine_hist.d_res_low                        39.20 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.014 ? 2.00  2266 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.13  ? 2.00  3085 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  757  '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  402  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2266 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           5.02  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.13 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  279  '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  2117 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.15 
_refine_ls_shell.d_res_low                        1.22 
_refine_ls_shell.number_reflns_R_work             1420 
_refine_ls_shell.R_factor_R_work                  0.3165 
_refine_ls_shell.percent_reflns_obs               8.63 
_refine_ls_shell.R_factor_R_free                  0.3063 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.08 
_refine_ls_shell.number_reflns_R_free             76 
_refine_ls_shell.number_reflns_all                1496 
_refine_ls_shell.R_factor_all                     0.3159 
# 
_struct.entry_id                  7I4V 
_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-0036758-001 (A71EV2A-x4746)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I4V 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I4V A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I4V C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,I 
2 1 B,F,G,H,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.297 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.256 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.317 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.323 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.277 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
# 
_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_555 111.1 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.4 ? 
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_555 117.9 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 105.7 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 100.7 ? 
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_555 114.4 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.4 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F 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 ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 118.2 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 106.1 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.0 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.6 ? 
# 
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                   7I4V 
_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 312 ? ? O A HOH 390 ? ? 1.37 
2  1 O   A HOH 388 ? ? O A HOH 449 ? ? 1.85 
3  1 O   C HOH 301 ? ? O C HOH 405 ? ? 1.86 
4  1 O   A HOH 431 ? ? O A HOH 446 ? ? 1.87 
5  1 O   C HOH 322 ? ? O C HOH 406 ? ? 1.87 
6  1 O   C HOH 395 ? ? O C HOH 455 ? ? 1.94 
7  1 O   C HOH 388 ? ? O C HOH 426 ? ? 1.99 
8  1 OE2 A GLU 88  ? ? O A HOH 301 ? ? 2.10 
9  1 O   A HOH 421 ? ? O A HOH 451 ? ? 2.13 
10 1 O   C HOH 344 ? ? O C HOH 471 ? ? 2.18 
# 
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 14.9714 8.2299   14.4500 -0.0186 -0.0187 0.0029 0.0132 -0.0026 0.0043 1.4169 0.8463 0.7270 0.9264  
-0.5862 -0.4144 -0.0010 0.0543  0.1266 0.0374 0.0528 0.0303 -0.0335 -0.0802 -0.0519 
'X-RAY DIFFRACTION' 2 ? refined 25.8304 -20.1814 17.8254 -0.0216 -0.0122 0.0134 0.0077 -0.0035 0.0153 0.5838 0.9052 0.2609 -0.3008 
-0.1429 -0.1117 0.0017  -0.0031 0.1042 0.0264 0.0433 0.0143 0.0354  -0.0013 -0.0451 
# 
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 
A1B3C C4   C  Y N 1   
A1B3C C5   C  Y N 2   
A1B3C C6   C  Y N 3   
A1B3C C7   C  N N 4   
A1B3C C8   C  N N 5   
A1B3C C10  C  N N 6   
A1B3C C13  C  N N 7   
A1B3C F1   F  N N 8   
A1B3C F    F  N N 9   
A1B3C C12  C  N S 10  
A1B3C C11  C  N N 11  
A1B3C C9   C  N N 12  
A1B3C C14  C  N N 13  
A1B3C N    N  N N 14  
A1B3C O    O  N N 15  
A1B3C C1   C  Y N 16  
A1B3C S    S  N N 17  
A1B3C C    C  N N 18  
A1B3C C3   C  Y N 19  
A1B3C C2   C  Y N 20  
A1B3C H6   H  N N 21  
A1B3C H7   H  N N 22  
A1B3C H8   H  N N 23  
A1B3C H9   H  N N 24  
A1B3C H12  H  N N 25  
A1B3C H13  H  N N 26  
A1B3C H16  H  N N 27  
A1B3C H    H  N N 28  
A1B3C H14  H  N N 29  
A1B3C H15  H  N N 30  
A1B3C H11  H  N N 31  
A1B3C H10  H  N N 32  
A1B3C H17  H  N N 33  
A1B3C H18  H  N N 34  
A1B3C H1   H  N N 35  
A1B3C H2   H  N N 36  
A1B3C H3   H  N N 37  
A1B3C H5   H  N N 38  
A1B3C H4   H  N N 39  
ALA   N    N  N N 40  
ALA   CA   C  N S 41  
ALA   C    C  N N 42  
ALA   O    O  N N 43  
ALA   CB   C  N N 44  
ALA   OXT  O  N N 45  
ALA   H    H  N N 46  
ALA   H2   H  N N 47  
ALA   HA   H  N N 48  
ALA   HB1  H  N N 49  
ALA   HB2  H  N N 50  
ALA   HB3  H  N N 51  
ALA   HXT  H  N N 52  
ARG   N    N  N N 53  
ARG   CA   C  N S 54  
ARG   C    C  N N 55  
ARG   O    O  N N 56  
ARG   CB   C  N N 57  
ARG   CG   C  N N 58  
ARG   CD   C  N N 59  
ARG   NE   N  N N 60  
ARG   CZ   C  N N 61  
ARG   NH1  N  N N 62  
ARG   NH2  N  N N 63  
ARG   OXT  O  N N 64  
ARG   H    H  N N 65  
ARG   H2   H  N N 66  
ARG   HA   H  N N 67  
ARG   HB2  H  N N 68  
ARG   HB3  H  N N 69  
ARG   HG2  H  N N 70  
ARG   HG3  H  N N 71  
ARG   HD2  H  N N 72  
ARG   HD3  H  N N 73  
ARG   HE   H  N N 74  
ARG   HH11 H  N N 75  
ARG   HH12 H  N N 76  
ARG   HH21 H  N N 77  
ARG   HH22 H  N N 78  
ARG   HXT  H  N N 79  
ASN   N    N  N N 80  
ASN   CA   C  N S 81  
ASN   C    C  N N 82  
ASN   O    O  N N 83  
ASN   CB   C  N N 84  
ASN   CG   C  N N 85  
ASN   OD1  O  N N 86  
ASN   ND2  N  N N 87  
ASN   OXT  O  N N 88  
ASN   H    H  N N 89  
ASN   H2   H  N N 90  
ASN   HA   H  N N 91  
ASN   HB2  H  N N 92  
ASN   HB3  H  N N 93  
ASN   HD21 H  N N 94  
ASN   HD22 H  N N 95  
ASN   HXT  H  N N 96  
ASP   N    N  N N 97  
ASP   CA   C  N S 98  
ASP   C    C  N N 99  
ASP   O    O  N N 100 
ASP   CB   C  N N 101 
ASP   CG   C  N N 102 
ASP   OD1  O  N N 103 
ASP   OD2  O  N N 104 
ASP   OXT  O  N N 105 
ASP   H    H  N N 106 
ASP   H2   H  N N 107 
ASP   HA   H  N N 108 
ASP   HB2  H  N N 109 
ASP   HB3  H  N N 110 
ASP   HD2  H  N N 111 
ASP   HXT  H  N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  H  N N 126 
DMS   S    S  N N 127 
DMS   O    O  N N 128 
DMS   C1   C  N N 129 
DMS   C2   C  N N 130 
DMS   H11  H  N N 131 
DMS   H12  H  N N 132 
DMS   H13  H  N N 133 
DMS   H21  H  N N 134 
DMS   H22  H  N N 135 
DMS   H23  H  N N 136 
GLN   N    N  N N 137 
GLN   CA   C  N S 138 
GLN   C    C  N N 139 
GLN   O    O  N N 140 
GLN   CB   C  N N 141 
GLN   CG   C  N N 142 
GLN   CD   C  N N 143 
GLN   OE1  O  N N 144 
GLN   NE2  N  N N 145 
GLN   OXT  O  N N 146 
GLN   H    H  N N 147 
GLN   H2   H  N N 148 
GLN   HA   H  N N 149 
GLN   HB2  H  N N 150 
GLN   HB3  H  N N 151 
GLN   HG2  H  N N 152 
GLN   HG3  H  N N 153 
GLN   HE21 H  N N 154 
GLN   HE22 H  N N 155 
GLN   HXT  H  N N 156 
GLU   N    N  N N 157 
GLU   CA   C  N S 158 
GLU   C    C  N N 159 
GLU   O    O  N N 160 
GLU   CB   C  N N 161 
GLU   CG   C  N N 162 
GLU   CD   C  N N 163 
GLU   OE1  O  N N 164 
GLU   OE2  O  N N 165 
GLU   OXT  O  N N 166 
GLU   H    H  N N 167 
GLU   H2   H  N N 168 
GLU   HA   H  N N 169 
GLU   HB2  H  N N 170 
GLU   HB3  H  N N 171 
GLU   HG2  H  N N 172 
GLU   HG3  H  N N 173 
GLU   HE2  H  N N 174 
GLU   HXT  H  N N 175 
GLY   N    N  N N 176 
GLY   CA   C  N N 177 
GLY   C    C  N N 178 
GLY   O    O  N N 179 
GLY   OXT  O  N N 180 
GLY   H    H  N N 181 
GLY   H2   H  N N 182 
GLY   HA2  H  N N 183 
GLY   HA3  H  N N 184 
GLY   HXT  H  N N 185 
HIS   N    N  N N 186 
HIS   CA   C  N S 187 
HIS   C    C  N N 188 
HIS   O    O  N N 189 
HIS   CB   C  N N 190 
HIS   CG   C  Y N 191 
HIS   ND1  N  Y N 192 
HIS   CD2  C  Y N 193 
HIS   CE1  C  Y N 194 
HIS   NE2  N  Y N 195 
HIS   OXT  O  N N 196 
HIS   H    H  N N 197 
HIS   H2   H  N N 198 
HIS   HA   H  N N 199 
HIS   HB2  H  N N 200 
HIS   HB3  H  N N 201 
HIS   HD1  H  N N 202 
HIS   HD2  H  N N 203 
HIS   HE1  H  N N 204 
HIS   HE2  H  N N 205 
HIS   HXT  H  N N 206 
HOH   O    O  N N 207 
HOH   H1   H  N N 208 
HOH   H2   H  N N 209 
ILE   N    N  N N 210 
ILE   CA   C  N S 211 
ILE   C    C  N N 212 
ILE   O    O  N N 213 
ILE   CB   C  N S 214 
ILE   CG1  C  N N 215 
ILE   CG2  C  N N 216 
ILE   CD1  C  N N 217 
ILE   OXT  O  N N 218 
ILE   H    H  N N 219 
ILE   H2   H  N N 220 
ILE   HA   H  N N 221 
ILE   HB   H  N N 222 
ILE   HG12 H  N N 223 
ILE   HG13 H  N N 224 
ILE   HG21 H  N N 225 
ILE   HG22 H  N N 226 
ILE   HG23 H  N N 227 
ILE   HD11 H  N N 228 
ILE   HD12 H  N N 229 
ILE   HD13 H  N N 230 
ILE   HXT  H  N N 231 
LEU   N    N  N N 232 
LEU   CA   C  N S 233 
LEU   C    C  N N 234 
LEU   O    O  N N 235 
LEU   CB   C  N N 236 
LEU   CG   C  N N 237 
LEU   CD1  C  N N 238 
LEU   CD2  C  N N 239 
LEU   OXT  O  N N 240 
LEU   H    H  N N 241 
LEU   H2   H  N N 242 
LEU   HA   H  N N 243 
LEU   HB2  H  N N 244 
LEU   HB3  H  N N 245 
LEU   HG   H  N N 246 
LEU   HD11 H  N N 247 
LEU   HD12 H  N N 248 
LEU   HD13 H  N N 249 
LEU   HD21 H  N N 250 
LEU   HD22 H  N N 251 
LEU   HD23 H  N N 252 
LEU   HXT  H  N N 253 
LYS   N    N  N N 254 
LYS   CA   C  N S 255 
LYS   C    C  N N 256 
LYS   O    O  N N 257 
LYS   CB   C  N N 258 
LYS   CG   C  N N 259 
LYS   CD   C  N N 260 
LYS   CE   C  N N 261 
LYS   NZ   N  N N 262 
LYS   OXT  O  N N 263 
LYS   H    H  N N 264 
LYS   H2   H  N N 265 
LYS   HA   H  N N 266 
LYS   HB2  H  N N 267 
LYS   HB3  H  N N 268 
LYS   HG2  H  N N 269 
LYS   HG3  H  N N 270 
LYS   HD2  H  N N 271 
LYS   HD3  H  N N 272 
LYS   HE2  H  N N 273 
LYS   HE3  H  N N 274 
LYS   HZ1  H  N N 275 
LYS   HZ2  H  N N 276 
LYS   HZ3  H  N N 277 
LYS   HXT  H  N N 278 
MET   N    N  N N 279 
MET   CA   C  N S 280 
MET   C    C  N N 281 
MET   O    O  N N 282 
MET   CB   C  N N 283 
MET   CG   C  N N 284 
MET   SD   S  N N 285 
MET   CE   C  N N 286 
MET   OXT  O  N N 287 
MET   H    H  N N 288 
MET   H2   H  N N 289 
MET   HA   H  N N 290 
MET   HB2  H  N N 291 
MET   HB3  H  N N 292 
MET   HG2  H  N N 293 
MET   HG3  H  N N 294 
MET   HE1  H  N N 295 
MET   HE2  H  N N 296 
MET   HE3  H  N N 297 
MET   HXT  H  N N 298 
PHE   N    N  N N 299 
PHE   CA   C  N S 300 
PHE   C    C  N N 301 
PHE   O    O  N N 302 
PHE   CB   C  N N 303 
PHE   CG   C  Y N 304 
PHE   CD1  C  Y N 305 
PHE   CD2  C  Y N 306 
PHE   CE1  C  Y N 307 
PHE   CE2  C  Y N 308 
PHE   CZ   C  Y N 309 
PHE   OXT  O  N N 310 
PHE   H    H  N N 311 
PHE   H2   H  N N 312 
PHE   HA   H  N N 313 
PHE   HB2  H  N N 314 
PHE   HB3  H  N N 315 
PHE   HD1  H  N N 316 
PHE   HD2  H  N N 317 
PHE   HE1  H  N N 318 
PHE   HE2  H  N N 319 
PHE   HZ   H  N N 320 
PHE   HXT  H  N N 321 
PRO   N    N  N N 322 
PRO   CA   C  N S 323 
PRO   C    C  N N 324 
PRO   O    O  N N 325 
PRO   CB   C  N N 326 
PRO   CG   C  N N 327 
PRO   CD   C  N N 328 
PRO   OXT  O  N N 329 
PRO   H    H  N N 330 
PRO   HA   H  N N 331 
PRO   HB2  H  N N 332 
PRO   HB3  H  N N 333 
PRO   HG2  H  N N 334 
PRO   HG3  H  N N 335 
PRO   HD2  H  N N 336 
PRO   HD3  H  N N 337 
PRO   HXT  H  N N 338 
SER   N    N  N N 339 
SER   CA   C  N S 340 
SER   C    C  N N 341 
SER   O    O  N N 342 
SER   CB   C  N N 343 
SER   OG   O  N N 344 
SER   OXT  O  N N 345 
SER   H    H  N N 346 
SER   H2   H  N N 347 
SER   HA   H  N N 348 
SER   HB2  H  N N 349 
SER   HB3  H  N N 350 
SER   HG   H  N N 351 
SER   HXT  H  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TRP   N    N  N N 370 
TRP   CA   C  N S 371 
TRP   C    C  N N 372 
TRP   O    O  N N 373 
TRP   CB   C  N N 374 
TRP   CG   C  Y N 375 
TRP   CD1  C  Y N 376 
TRP   CD2  C  Y N 377 
TRP   NE1  N  Y N 378 
TRP   CE2  C  Y N 379 
TRP   CE3  C  Y N 380 
TRP   CZ2  C  Y N 381 
TRP   CZ3  C  Y N 382 
TRP   CH2  C  Y N 383 
TRP   OXT  O  N N 384 
TRP   H    H  N N 385 
TRP   H2   H  N N 386 
TRP   HA   H  N N 387 
TRP   HB2  H  N N 388 
TRP   HB3  H  N N 389 
TRP   HD1  H  N N 390 
TRP   HE1  H  N N 391 
TRP   HE3  H  N N 392 
TRP   HZ2  H  N N 393 
TRP   HZ3  H  N N 394 
TRP   HH2  H  N N 395 
TRP   HXT  H  N N 396 
TYR   N    N  N N 397 
TYR   CA   C  N S 398 
TYR   C    C  N N 399 
TYR   O    O  N N 400 
TYR   CB   C  N N 401 
TYR   CG   C  Y N 402 
TYR   CD1  C  Y N 403 
TYR   CD2  C  Y N 404 
TYR   CE1  C  Y N 405 
TYR   CE2  C  Y N 406 
TYR   CZ   C  Y N 407 
TYR   OH   O  N N 408 
TYR   OXT  O  N N 409 
TYR   H    H  N N 410 
TYR   H2   H  N N 411 
TYR   HA   H  N N 412 
TYR   HB2  H  N N 413 
TYR   HB3  H  N N 414 
TYR   HD1  H  N N 415 
TYR   HD2  H  N N 416 
TYR   HE1  H  N N 417 
TYR   HE2  H  N N 418 
TYR   HH   H  N N 419 
TYR   HXT  H  N N 420 
VAL   N    N  N N 421 
VAL   CA   C  N S 422 
VAL   C    C  N N 423 
VAL   O    O  N N 424 
VAL   CB   C  N N 425 
VAL   CG1  C  N N 426 
VAL   CG2  C  N N 427 
VAL   OXT  O  N N 428 
VAL   H    H  N N 429 
VAL   H2   H  N N 430 
VAL   HA   H  N N 431 
VAL   HB   H  N N 432 
VAL   HG11 H  N N 433 
VAL   HG12 H  N N 434 
VAL   HG13 H  N N 435 
VAL   HG21 H  N N 436 
VAL   HG22 H  N N 437 
VAL   HG23 H  N N 438 
VAL   HXT  H  N N 439 
ZN    ZN   ZN N N 440 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1B3C C   S    sing N N 1   
A1B3C S   C1   sing N N 2   
A1B3C C1  C2   doub Y N 3   
A1B3C C2  C3   sing Y N 4   
A1B3C C3  C4   doub Y N 5   
A1B3C C4  C5   sing Y N 6   
A1B3C C5  C6   doub Y N 7   
A1B3C C1  C6   sing Y N 8   
A1B3C C6  C7   sing N N 9   
A1B3C C7  C8   sing N N 10  
A1B3C O   C8   doub N N 11  
A1B3C C8  N    sing N N 12  
A1B3C N   C9   sing N N 13  
A1B3C C9  C10  sing N N 14  
A1B3C C10 C11  sing N N 15  
A1B3C C11 C12  sing N N 16  
A1B3C C12 C13  sing N N 17  
A1B3C F   C13  sing N N 18  
A1B3C C13 F1   sing N N 19  
A1B3C C14 C12  sing N N 20  
A1B3C N   C14  sing N N 21  
A1B3C C4  H6   sing N N 22  
A1B3C C5  H7   sing N N 23  
A1B3C C7  H8   sing N N 24  
A1B3C C7  H9   sing N N 25  
A1B3C C10 H12  sing N N 26  
A1B3C C10 H13  sing N N 27  
A1B3C C13 H16  sing N N 28  
A1B3C C12 H    sing N N 29  
A1B3C C11 H14  sing N N 30  
A1B3C C11 H15  sing N N 31  
A1B3C C9  H11  sing N N 32  
A1B3C C9  H10  sing N N 33  
A1B3C C14 H17  sing N N 34  
A1B3C C14 H18  sing N N 35  
A1B3C C   H1   sing N N 36  
A1B3C C   H2   sing N N 37  
A1B3C C   H3   sing N N 38  
A1B3C C3  H5   sing N N 39  
A1B3C C2  H4   sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
DMS   S   O    doub N N 123 
DMS   S   C1   sing N N 124 
DMS   S   C2   sing N N 125 
DMS   C1  H11  sing N N 126 
DMS   C1  H12  sing N N 127 
DMS   C1  H13  sing N N 128 
DMS   C2  H21  sing N N 129 
DMS   C2  H22  sing N N 130 
DMS   C2  H23  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I4V 
_atom_sites.fract_transf_matrix[1][1]   0.011528 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000952 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017533 
_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]   0.015455 
_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  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.723 8.043   24.860 1.00 16.24  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.967 8.133   24.061 1.00 15.60  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.106 6.932   23.124 1.00 15.79  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.387 5.932   23.287 1.00 16.45  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.163 8.189   25.018 1.00 18.73  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.236 6.982   25.748 1.00 22.53  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.029 7.010   22.175 1.00 14.13  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.260 5.893   21.268 1.00 13.24  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.664 6.373   19.881 1.00 11.71  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.367 7.494   19.495 1.00 13.58  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.342 5.540   19.157 1.00 10.78  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.818 5.887   17.804 1.00 11.25  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.786 4.665   16.909 1.00 11.25  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.682 3.522   17.389 1.00 12.07  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.269 6.409   17.920 1.00 13.39  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.857 4.905   15.608 1.00 11.04  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.086 3.861   14.601 1.00 10.34  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.543 3.944   14.204 1.00 11.08  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.040 5.052   13.902 1.00 11.10  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.211 4.069   13.338 1.00 9.99   ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.737 4.230   13.683 1.00 12.03  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.412 2.887   12.360 1.00 12.03  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.937 4.780   12.475 1.00 13.09  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.251 2.811   14.161 1.00 10.85  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.651 2.795   13.760 1.00 11.80  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.786 1.969   12.489 1.00 12.33  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.749 0.719   12.556 1.00 13.42  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.538 2.209   14.895 1.00 13.56  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.593 3.097   16.112 1.00 13.05  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.485 4.173   16.179 1.00 14.05  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.768 2.869   17.201 1.00 14.58  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.498 5.045   17.271 1.00 14.67  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.776 3.729   18.306 1.00 15.57  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.634 4.826   18.319 1.00 15.54  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.661 5.695   19.404 1.00 18.52  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.809 2.626   11.339 1.00 12.45  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.889 2.001   10.026 1.00 12.65  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.123 2.479   9.294  1.00 13.84  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.374 3.697   9.251  1.00 13.24  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.593 2.262   9.182  1.00 14.15  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.256 3.746   9.060  1.00 15.61  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.724 1.646   7.802  1.00 16.00  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.978 1.566   8.805  1.00 15.27  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.234 1.999   8.172  1.00 16.34  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.059 2.875   9.105  1.00 14.99  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.178 2.574   10.294 1.00 15.01  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.538 4.022   8.596  1.00 14.33  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.234 4.999   9.442  1.00 13.52  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.329 6.189   9.749  1.00 13.57  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.820 7.333   9.880  1.00 13.90  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.584 5.461   8.867  1.00 15.24  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.658 4.405   8.967  1.00 19.89  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.405 4.317   9.963  1.00 22.12  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.690 3.540   7.995  1.00 18.15  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.049 5.907   9.990  1.00 12.11  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.096 6.944   10.350 1.00 12.30  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.425 6.616   11.688 1.00 11.41  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.157 5.433   12.004 1.00 12.30  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.973 7.033   9.282  1.00 13.18  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.478 7.436   7.909  1.00 13.65  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.138 8.651   7.711  1.00 15.29  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.304 6.602   6.810  1.00 16.00  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.605 9.026   6.458  1.00 15.95  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.703 7.005   5.539  1.00 17.36  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.361 8.212   5.373  1.00 17.76  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.809 8.638   4.135  1.00 21.75  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.075 7.667   12.433 1.00 10.63  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.281 7.601   13.661 1.00 10.92  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.055 8.472   13.421 1.00 10.47  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.211 9.678   13.129 1.00 11.09  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.102 8.158   14.850 1.00 12.14  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.334 8.465   16.117 1.00 12.72  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.265 8.848   17.290 1.00 13.59  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.706 9.918   18.133 1.00 14.86  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.043 9.715   19.266 1.00 16.00  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.741 8.470   19.655 1.00 16.99  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.571 10.748  19.961 1.00 16.13  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.856 7.870   13.474 1.00 10.41  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.583 8.601   13.261 1.00 10.01  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.916 8.811   14.589 1.00 10.84  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.635 7.815   15.287 1.00 11.30  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.650 7.815   12.322 1.00 10.58  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.419 8.678   11.991 1.00 11.37  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.345 7.328   11.051 1.00 11.81  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.673 10.067  14.950 1.00 9.94   ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.064 10.414  16.252 0.50 10.22  ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.106 10.379  16.262 0.50 12.01  ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.964 11.398  16.081 1.00 10.67  ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.804 12.042  15.000 1.00 11.97  ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.081 11.020  17.272 0.50 9.58   ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.269 10.963  17.153 0.50 15.11  ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 23.000 9.942   17.797 0.50 11.75  ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.848 11.256  18.574 0.50 15.36  ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.818 12.266  16.679 0.50 6.68   ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.469 10.049  17.173 0.50 17.61  ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.139 11.571  17.123 1.00 10.35  ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.135 12.642  17.077 1.00 11.08  ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.938 13.975  17.097 1.00 11.86  ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.865 14.145  17.908 1.00 11.79  ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.287 12.638  18.342 1.00 11.32  ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.419 11.396  18.447 1.00 11.85  ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.812 10.379  19.057 1.00 13.09  ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.235 11.461  17.836 1.00 12.50  ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.565 14.911  16.217 1.00 11.48  ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.312 16.202  16.182 1.00 11.81  ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.283 16.880  17.527 1.00 13.45  ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.300 17.434  17.959 1.00 14.26  ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.708 17.083  15.093 1.00 12.52  ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.481 18.405  14.869 1.00 12.95  ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.734 19.262  13.856 1.00 14.85  ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.481 20.466  13.406 1.00 16.28  ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.474 21.618  14.060 1.00 18.60  ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.882 21.718  15.243 1.00 19.19  ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 20.064 22.693  13.532 1.00 19.87  ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.133 16.767  18.245 1.00 13.01  ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 18.029 17.460  19.527 1.00 15.19  ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.876 16.856  20.652 1.00 15.90  ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 19.025 17.490  21.712 1.00 17.90  ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.560 17.628  19.962 1.00 16.62  ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.876 16.385  20.466 1.00 15.41  ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.257 15.493  19.601 1.00 15.13  ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.685 15.961  21.740 1.00 17.14  ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.702 14.547  20.388 1.00 15.49  ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 14.939 14.794  21.672 1.00 17.28  ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.420 15.636  20.441 1.00 15.63  ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.297 14.954  21.395 1.00 14.42  ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.757 14.889  20.944 1.00 16.11  ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.589 14.288  21.600 1.00 17.32  ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.786 13.572  21.741 1.00 14.27  ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.380 13.571  22.329 1.00 14.91  ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.921 12.118  22.571 1.00 15.51  ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.331 14.362  23.675 1.00 16.83  ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 22.097 15.546  19.802 1.00 14.92  ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.478 15.519  19.292 1.00 14.31  ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.453 16.176  20.259 1.00 16.07  ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 24.126 17.175  20.910 1.00 16.27  ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.539 16.220  17.937 1.00 14.59  ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.621 15.553  20.392 1.00 15.58  ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.675 16.050  21.307 1.00 14.58  ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.605 17.035  20.570 1.00 15.78  ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.545 17.193  19.327 1.00 14.97  ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.543 14.865  21.790 1.00 17.04  ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.266 14.328  20.668 1.00 17.08  ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.736 13.744  22.461 1.00 17.90  ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.533 17.703  21.313 1.00 15.95  ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.514 18.567  20.685 1.00 15.93  ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.363 17.755  19.711 1.00 15.82  ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.642 18.240  18.613 1.00 15.85  ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.442 19.223  21.751 1.00 16.80  ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.709 19.855  21.132 1.00 23.06  ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.668 21.042  20.407 1.00 27.14  ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.970 19.338  21.023 1.00 27.40  ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.915 21.305  20.029 1.00 27.61  ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.739 20.277  20.320 1.00 29.83  ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.733 16.492  20.082 1.00 15.32  ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.530 15.706  19.155 1.00 15.30  ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.759 15.425  17.854 1.00 13.50  ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.345 15.455  16.778 1.00 14.63  ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 31.990 14.385  19.794 1.00 17.45  ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.947 13.645  18.880 1.00 24.49  ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.099 14.072  18.688 1.00 28.65  ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.478 12.557  18.224 1.00 26.18  ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.427 15.178  17.951 1.00 13.70  ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.632 15.006  16.737 1.00 12.48  ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.693 16.267  15.830 1.00 12.29  ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.914 16.165  14.624 1.00 12.82  ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.169 14.725  17.080 1.00 13.31  ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.914 13.364  17.685 1.00 14.31  ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.560 12.379  17.223 1.00 15.21  ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 26.066 13.281  18.618 1.00 14.45  ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.484 17.450  16.428 1.00 12.04  ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.520 18.702  15.655 1.00 12.20  ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.930 18.974  15.082 1.00 12.81  ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.008 19.534  13.987 1.00 13.53  ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 28.072 19.883  16.534 1.00 13.02  ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.574 19.938  16.669 1.00 13.09  ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.830 19.641  17.772 1.00 14.93  ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.644 20.406  15.677 1.00 13.71  ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.487 19.893  17.531 1.00 14.58  ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.345 20.326  16.230 1.00 13.88  ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.790 20.858  14.359 1.00 15.45  ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.201 20.722  15.508 1.00 15.68  ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.664 21.189  13.640 1.00 15.95  ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.410 21.189  14.217 1.00 16.61  ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 30.993 18.557  15.785 1.00 12.76  ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.354 18.764  15.306 1.00 13.23  ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.774 17.765  14.232 1.00 14.29  ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.806 17.925  13.596 1.00 15.61  ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.305 18.732  16.492 1.00 14.81  ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 31.970 16.698  14.025 1.00 13.87  ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.256 15.649  13.009 1.00 14.22  ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 30.978 15.474  12.175 1.00 13.87  ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.594 14.354  11.819 1.00 13.71  ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.655 14.306  13.708 1.00 15.28  ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 33.995 14.500  14.373 1.00 16.64  ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.039 14.438  13.703 1.00 19.78  ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 34.012 14.803  15.683 1.00 17.83  ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.329 16.563  11.835 1.00 13.19  ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.048 16.519  11.155 1.00 12.17  ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.103 16.087  9.719  1.00 13.60  ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.934 16.592  8.937  1.00 14.99  ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.460 17.936  11.236 1.00 12.87  ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.074 18.095  10.648 1.00 13.37  ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.041 17.331  11.489 1.00 13.88  ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.631 19.575  10.626 1.00 15.73  ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.172 15.216  9.311  1.00 12.91  ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.006 14.805  7.925  1.00 13.24  ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.751 15.507  7.348  1.00 13.03  ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.793 16.073  6.243  1.00 14.98  ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.891 13.273  7.825  1.00 12.64  ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.507 12.870  6.379  1.00 15.07  ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.198 12.590  8.274  1.00 14.67  ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.605 15.481  8.075  1.00 12.54  ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.345 16.018  7.569  1.00 12.96  ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.397 16.226  8.725  1.00 13.15  ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.435 15.452  9.716  1.00 12.28  ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.738 15.003  6.551  1.00 14.27  ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.338 15.278  6.110  1.00 14.94  ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.935 16.125  5.115  1.00 17.67  ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.148 14.678  6.640  1.00 14.66  ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.569 16.063  4.976  1.00 18.84  ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.059 15.173  5.893  1.00 16.94  ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.894 13.739  7.647  1.00 15.54  ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.734 14.734  6.110  1.00 17.93  ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.595 13.289  7.835  1.00 16.57  ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.530 13.824  7.118  1.00 18.00  ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.567 17.257  8.665  1.00 13.71  ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.555 17.461  9.684  1.00 14.06  ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.331 18.088  9.066  1.00 15.51  ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.447 18.899  8.133  1.00 16.06  ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.056 18.279  10.872 1.00 15.53  ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.675 19.646  10.509 1.00 16.45  ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.724 20.830  10.313 1.00 17.22  ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.073 21.790  9.570  1.00 18.73  ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.616 20.811  10.892 1.00 17.16  ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.172 17.813  9.638  1.00 14.29  ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.906 18.361  9.172  1.00 14.50  ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.945 18.543  10.341 1.00 13.72  ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.421 17.560  10.890 1.00 14.09  ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.310 17.450  8.064  1.00 16.78  ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.042 17.964  7.429  1.00 20.04  ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.221 18.551  8.144  1.00 22.66  ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.833 17.700  6.232  1.00 24.79  ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.735 19.799  10.750 1.00 14.72  ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.876 20.140  11.869 0.50 15.29  ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.891 20.072  11.897 0.50 16.33  ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.432 19.699  11.634 1.00 16.31  ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.793 19.192  12.562 1.00 17.18  ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.936 21.645  12.119 0.50 15.65  ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 16.042 21.523  12.334 0.50 19.83  ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 14.976 22.025  13.091 0.50 15.15  ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.621 22.355  11.273 0.50 25.56  ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.931 19.834  10.397 1.00 16.74  ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.546 19.426  10.118 1.00 16.86  ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.302 17.952  10.313 1.00 16.50  ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.154 17.567  10.550 1.00 17.54  ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.103 19.829  8.712  1.00 20.20  ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.668 19.011  7.705  1.00 25.44  ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.353 17.121  10.242 1.00 14.52  ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.253 15.666  10.447 1.00 14.73  ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.744 15.206  11.825 1.00 13.91  ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.646 14.001  12.143 1.00 13.54  ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.111 14.933  9.379  1.00 15.11  ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.583 15.134  7.955  1.00 17.61  ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.460 14.449  6.928  1.00 16.92  ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.369 12.979  7.050  1.00 14.05  ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.543 12.141  6.037  1.00 15.85  ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.811 12.606  4.815  1.00 17.87  ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.392 10.824  6.216  1.00 15.55  ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.296 16.103  12.641 1.00 13.04  ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.944 15.769  13.896 1.00 12.39  ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 16.082 14.756  13.726 1.00 11.86  ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.316 13.932  14.621 1.00 12.21  ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.943 15.290  14.975 1.00 13.44  ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.561 15.053  16.338 1.00 13.88  ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.416 15.889  16.787 1.00 14.72  ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.178 14.061  17.015 1.00 14.61  ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.878 14.875  12.643 1.00 11.56  ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.986 13.925  12.429 1.00 10.87  ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.326 14.648  12.299 1.00 11.09  ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.410 15.755  11.711 1.00 12.10  ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.749 13.135  11.145 1.00 11.73  ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.661 12.029  11.200 1.00 12.91  ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.575 11.285  9.876  1.00 13.96  ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.934 11.001  12.324 1.00 13.49  ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.369 13.979  12.757 1.00 10.59  ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.744 14.441  12.543 1.00 10.73  ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.582 13.201  12.384 1.00 10.27  ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.401 12.177  13.088 1.00 10.55  ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.215 15.291  13.735 1.00 11.13  ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.649 15.848  13.643 1.00 11.29  ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.721 17.210  14.349 1.00 13.23  ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.653 14.914  14.305 1.00 11.39  ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.550 13.274  11.472 1.00 10.45  ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.498 12.185  11.190 1.00 10.00  ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.919 12.690  11.345 1.00 10.15  ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.248 13.750  10.769 1.00 11.51  ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.270 11.595  9.766  1.00 10.71  ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.297 10.502  9.477  1.00 12.14  ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.829 11.058  9.613  1.00 12.17  ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.727 12.005  12.143 1.00 10.54  ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.147 12.332  12.319 1.00 10.59  ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 29.004 11.166  11.861 1.00 11.84  ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.531 10.025  11.633 1.00 11.69  ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.425 12.709  13.767 1.00 12.03  ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.085 11.631  14.632 1.00 12.92  ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.295 11.435  11.657 1.00 12.60  ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.238 10.409  11.215 1.00 13.72  ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.863 9.681   12.406 1.00 15.70  ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 32.041 10.293  13.492 1.00 17.62  ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.307 11.031  10.319 1.00 16.24  ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 33.016 12.008  11.059 1.00 19.61  ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.201 8.374   12.223 1.00 15.54  ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.786 7.573   13.289 1.00 17.02  ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.128 7.008   12.843 1.00 19.30  ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.349 6.771   11.651 1.00 18.38  ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.841 6.382   13.658 1.00 17.78  ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.734 5.485   12.552 1.00 18.54  ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.447 6.830   14.045 1.00 18.60  ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 34.975 6.710   13.822 1.00 20.45  ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.256 6.085   13.530 1.00 22.13  ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 36.046 4.575   13.308 1.00 22.07  ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.575 4.013   12.332 1.00 23.83  ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.274 6.409   14.657 1.00 26.50  ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.774 5.914   15.885 1.00 31.57  ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.507 7.878   14.796 1.00 27.35  ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.217 3.948   14.163 1.00 22.36  ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.944 2.504   14.073 1.00 23.56  ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.732 2.207   13.165 1.00 22.14  ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.795 2.993   13.144 1.00 20.90  ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.639 1.962   15.458 1.00 26.18  ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.715 1.070   12.475 1.00 20.77  ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.586 0.669   11.628 1.00 21.09  ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.480 0.071   12.482 1.00 20.75  ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.759 -0.697  13.397 1.00 21.86  ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 33.010 -0.340  10.561 1.00 23.44  ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.868 0.292   9.464  1.00 29.71  ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.205 -0.722  8.430  1.00 36.18  ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.047 -1.610  8.662  1.00 35.08  ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.525 -0.630  7.292  1.00 38.51  ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.229 0.412   12.177 1.00 16.85  ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.079 -0.117  12.905 1.00 16.28  ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.477 -1.374  12.296 1.00 15.63  ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.762 -1.740  11.145 1.00 17.14  ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.513 -1.951  13.059 1.00 15.05  ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 26.913 -3.240  12.679 1.00 15.55  ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.472 -3.171  12.214 1.00 15.08  ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 24.932 -4.205  11.813 1.00 15.90  ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.066 -4.257  13.818 1.00 16.24  ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.778 -4.655  14.223 1.00 20.20  ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.816 -2.026  12.378 1.00 13.84  ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.426 -1.919  11.952 1.00 12.83  ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.338 -1.862  10.435 1.00 14.83  ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.226 -1.284  9.783  1.00 16.81  ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.782 -0.663  12.572 1.00 12.67  ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.678 -0.722  14.082 1.00 13.78  ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.320 -1.833  14.623 1.00 14.40  ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.901 0.327   14.740 1.00 14.38  ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.291 -2.398  9.875  1.00 15.87  ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 21.983 -2.366  8.425  1.00 17.65  ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.658 -1.599  8.260  1.00 16.35  ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.747 -1.747  9.078  1.00 17.62  ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 21.860 -3.798  7.891  1.00 24.17  ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 23.203 -4.349  7.845  1.00 28.95  ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 21.156 -3.879  6.531  1.00 28.30  ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.544 -0.769  7.206  1.00 15.11  ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.317 0.006   7.003  1.00 13.81  ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.344 -0.744  6.091  1.00 13.93  ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.721 -1.289  5.027  1.00 15.32  ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.653 1.374   6.352  1.00 14.18  ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.756 2.119   7.151  1.00 15.34  ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.367 2.249   6.248  1.00 13.83  ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.400 2.445   8.631  1.00 16.35  ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.094 -0.780  6.479  1.00 12.66  ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 16.009 -1.361  5.670  1.00 13.25  ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.735 -0.490  4.420  1.00 13.56  ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.761 0.754   4.479  1.00 14.25  ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.733 -1.403  6.484  1.00 13.32  ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.488 -1.161  3.260  1.00 15.46  ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.139 -0.448  2.030  1.00 17.63  ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 13.827 -1.092  1.559  1.00 19.23  ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 13.854 -2.044  0.770  1.00 20.79  ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.297 -0.551  1.007  1.00 19.26  ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.676 -0.024  1.490  1.00 18.72  ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.696 1.479   1.852  1.00 17.05  ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 19.035 1.918   2.307  1.00 16.15  ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.257 3.062   2.941  1.00 16.68  ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.272 3.936   3.116  1.00 15.62  ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.484 3.357   3.391  1.00 18.10  ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 12.702 -0.518  1.989  1.00 19.13  ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.348 -1.132  1.901  1.00 18.40  ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.247 -0.126  2.217  1.00 19.11  ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.470 1.008   2.626  1.00 21.12  ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.301 -2.303  2.888  1.00 18.22  ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.282 -1.780  4.624  1.00 17.71  ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 8.952  -0.615  2.138  1.00 22.01  ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 7.787  0.178   2.551  1.00 23.95  ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 7.020  -0.583  3.645  1.00 22.58  ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 5.795  -0.404  3.753  1.00 22.74  ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 6.857  0.552   1.366  1.00 30.08  ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.235  -0.639  0.677  1.00 37.26  ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 6.572  -1.799  1.055  1.00 38.03  ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 5.415  -0.427  -0.259 1.00 41.73  ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 7.715  -1.381  4.511  1.00 19.47  ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 7.019  -2.053  5.637  1.00 17.57  ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.295  -1.007  6.501  1.00 17.95  ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 6.770  0.123   6.709  1.00 17.82  ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 7.998  -2.824  6.532  1.00 18.48  ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 8.746  -4.311  5.793  1.00 19.05  ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.176  -1.435  7.034  1.00 16.18  ? 59  GLN   A N   1 
ATOM   411  C  CA  . GLN   A 1 53  ? 4.386  -0.701  8.005  1.00 15.86  ? 59  GLN   A CA  1 
ATOM   412  C  C   . GLN   A 1 53  ? 4.187  -1.506  9.271  1.00 14.11  ? 59  GLN   A C   1 
ATOM   413  O  O   . GLN   A 1 53  ? 3.351  -1.150  10.079 1.00 14.92  ? 59  GLN   A O   1 
ATOM   414  C  CB  . GLN   A 1 53  ? 3.031  -0.217  7.463  1.00 18.44  ? 59  GLN   A CB  1 
ATOM   415  C  CG  . GLN   A 1 53  ? 3.148  0.900   6.437  1.00 21.86  ? 59  GLN   A CG  1 
ATOM   416  C  CD  . GLN   A 1 53  ? 1.755  1.433   6.082  1.00 25.51  ? 59  GLN   A CD  1 
ATOM   417  O  OE1 . GLN   A 1 53  ? 1.255  1.267   4.959  1.00 28.89  ? 59  GLN   A OE1 1 
ATOM   418  N  NE2 . GLN   A 1 53  ? 1.051  2.091   7.009  1.00 22.48  ? 59  GLN   A NE2 1 
ATOM   419  N  N   . THR   A 1 54  ? 4.955  -2.616  9.475  1.00 12.75  ? 60  THR   A N   1 
ATOM   420  C  CA  . THR   A 1 54  ? 4.964  -3.322  10.758 1.00 12.90  ? 60  THR   A CA  1 
ATOM   421  C  C   . THR   A 1 54  ? 6.432  -3.590  11.138 1.00 12.23  ? 60  THR   A C   1 
ATOM   422  O  O   . THR   A 1 54  ? 7.289  -3.780  10.255 1.00 13.86  ? 60  THR   A O   1 
ATOM   423  C  CB  . THR   A 1 54  ? 4.202  -4.606  10.736 1.00 16.22  ? 60  THR   A CB  1 
ATOM   424  O  OG1 . THR   A 1 54  ? 4.808  -5.527  9.866  1.00 22.28  ? 60  THR   A OG1 1 
ATOM   425  C  CG2 . THR   A 1 54  ? 2.775  -4.433  10.317 1.00 16.17  ? 60  THR   A CG2 1 
ATOM   426  N  N   . GLY   A 1 55  ? 6.701  -3.533  12.425 1.00 11.31  ? 61  GLY   A N   1 
ATOM   427  C  CA  . GLY   A 1 55  ? 8.068  -3.740  12.891 1.00 11.47  ? 61  GLY   A CA  1 
ATOM   428  C  C   . GLY   A 1 55  ? 8.083  -3.790  14.392 1.00 10.51  ? 61  GLY   A C   1 
ATOM   429  O  O   . GLY   A 1 55  ? 7.052  -4.043  15.010 1.00 11.09  ? 61  GLY   A O   1 
ATOM   430  N  N   . VAL   A 1 56  ? 9.253  -3.585  14.995 1.00 9.71   ? 62  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 56  ? 9.435  -3.676  16.444 1.00 8.92   ? 62  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 56  ? 10.294 -2.514  16.861 1.00 9.49   ? 62  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 56  ? 11.288 -2.212  16.196 1.00 10.40  ? 62  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 56  ? 10.142 -5.027  16.769 1.00 10.78  ? 62  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 56  ? 10.515 -5.111  18.249 1.00 13.43  ? 62  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 56  ? 9.240  -6.213  16.396 1.00 11.10  ? 62  VAL   A CG2 1 
ATOM   437  N  N   . TYR   A 1 57  ? 9.926  -1.827  17.956 1.00 9.78   ? 63  TYR   A N   1 
ATOM   438  C  CA  . TYR   A 1 57  ? 10.782 -0.742  18.468 1.00 9.66   ? 63  TYR   A CA  1 
ATOM   439  C  C   . TYR   A 1 57  ? 11.218 -0.956  19.899 1.00 10.44  ? 63  TYR   A C   1 
ATOM   440  O  O   . TYR   A 1 57  ? 10.526 -1.629  20.669 1.00 10.65  ? 63  TYR   A O   1 
ATOM   441  C  CB  . TYR   A 1 57  ? 10.096 0.658   18.328 1.00 10.36  ? 63  TYR   A CB  1 
ATOM   442  C  CG  . TYR   A 1 57  ? 9.130  1.052   19.417 1.00 9.84   ? 63  TYR   A CG  1 
ATOM   443  C  CD1 . TYR   A 1 57  ? 7.845  0.529   19.453 1.00 11.53  ? 63  TYR   A CD1 1 
ATOM   444  C  CD2 . TYR   A 1 57  ? 9.499  1.949   20.417 1.00 10.61  ? 63  TYR   A CD2 1 
ATOM   445  C  CE1 . TYR   A 1 57  ? 6.949  0.889   20.459 1.00 12.36  ? 63  TYR   A CE1 1 
ATOM   446  C  CE2 . TYR   A 1 57  ? 8.596  2.348   21.404 1.00 11.67  ? 63  TYR   A CE2 1 
ATOM   447  C  CZ  . TYR   A 1 57  ? 7.333  1.802   21.424 1.00 13.23  ? 63  TYR   A CZ  1 
ATOM   448  O  OH  . TYR   A 1 57  ? 6.399  2.140   22.400 1.00 15.88  ? 63  TYR   A OH  1 
ATOM   449  N  N   . TYR   A 1 58  ? 12.355 -0.363  20.280 1.00 9.68   ? 64  TYR   A N   1 
ATOM   450  C  CA  . TYR   A 1 58  ? 12.805 -0.419  21.666 1.00 9.59   ? 64  TYR   A CA  1 
ATOM   451  C  C   . TYR   A 1 58  ? 12.351 0.805   22.472 1.00 9.46   ? 64  TYR   A C   1 
ATOM   452  O  O   . TYR   A 1 58  ? 12.594 1.956   22.090 1.00 10.09  ? 64  TYR   A O   1 
ATOM   453  C  CB  . TYR   A 1 58  ? 14.364 -0.486  21.706 1.00 10.85  ? 64  TYR   A CB  1 
ATOM   454  C  CG  . TYR   A 1 58  ? 14.841 -0.633  23.142 1.00 11.00  ? 64  TYR   A CG  1 
ATOM   455  C  CD1 . TYR   A 1 58  ? 14.517 -1.748  23.888 1.00 11.27  ? 64  TYR   A CD1 1 
ATOM   456  C  CD2 . TYR   A 1 58  ? 15.582 0.377   23.760 1.00 11.36  ? 64  TYR   A CD2 1 
ATOM   457  C  CE1 . TYR   A 1 58  ? 14.879 -1.843  25.228 1.00 13.01  ? 64  TYR   A CE1 1 
ATOM   458  C  CE2 . TYR   A 1 58  ? 15.977 0.279   25.085 1.00 12.70  ? 64  TYR   A CE2 1 
ATOM   459  C  CZ  . TYR   A 1 58  ? 15.649 -0.848  25.796 1.00 13.16  ? 64  TYR   A CZ  1 
ATOM   460  O  OH  . TYR   A 1 58  ? 16.036 -0.956  27.133 1.00 16.48  ? 64  TYR   A OH  1 
ATOM   461  N  N   . CYS   A 1 59  ? 11.734 0.493   23.613 1.00 9.80   ? 65  CYS   A N   1 
ATOM   462  C  CA  . CYS   A 1 59  ? 11.229 1.510   24.561 1.00 10.16  ? 65  CYS   A CA  1 
ATOM   463  C  C   . CYS   A 1 59  ? 12.046 1.486   25.856 1.00 11.20  ? 65  CYS   A C   1 
ATOM   464  O  O   . CYS   A 1 59  ? 11.858 0.568   26.692 1.00 11.60  ? 65  CYS   A O   1 
ATOM   465  C  CB  . CYS   A 1 59  ? 9.770  1.211   24.842 1.00 11.05  ? 65  CYS   A CB  1 
ATOM   466  S  SG  . CYS   A 1 59  ? 9.015  2.327   26.068 1.00 12.31  ? 65  CYS   A SG  1 
ATOM   467  N  N   . SER   A 1 60  ? 12.972 2.433   26.024 1.00 11.15  ? 66  SER   A N   1 
ATOM   468  C  CA  . SER   A 1 60  ? 13.852 2.410   27.195 1.00 12.26  ? 66  SER   A CA  1 
ATOM   469  C  C   . SER   A 1 60  ? 13.104 2.608   28.528 1.00 12.31  ? 66  SER   A C   1 
ATOM   470  O  O   . SER   A 1 60  ? 13.505 2.026   29.547 1.00 14.05  ? 66  SER   A O   1 
ATOM   471  C  CB  . SER   A 1 60  ? 14.972 3.434   27.002 1.00 14.10  ? 66  SER   A CB  1 
ATOM   472  O  OG  . SER   A 1 60  ? 14.530 4.769   27.160 1.00 16.61  ? 66  SER   A OG  1 
ATOM   473  N  N   . SER   A 1 61  ? 11.972 3.355   28.509 1.00 11.46  ? 67  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 61  ? 11.174 3.550   29.725 1.00 12.01  ? 67  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 61  ? 10.362 2.337   30.158 1.00 12.29  ? 67  SER   A C   1 
ATOM   476  O  O   . SER   A 1 61  ? 9.727  2.371   31.201 1.00 13.24  ? 67  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 61  ? 10.260 4.764   29.615 1.00 13.13  ? 67  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 61  ? 9.306  4.577   28.604 1.00 14.08  ? 67  SER   A OG  1 
ATOM   479  N  N   . ARG   A 1 62  ? 10.438 1.238   29.377 1.00 12.75  ? 68  ARG   A N   1 
ATOM   480  C  CA  . ARG   A 1 62  ? 9.836  -0.046  29.779 1.00 12.95  ? 68  ARG   A CA  1 
ATOM   481  C  C   . ARG   A 1 62  ? 10.872 -1.188  29.709 1.00 14.24  ? 68  ARG   A C   1 
ATOM   482  O  O   . ARG   A 1 62  ? 10.533 -2.345  29.993 1.00 14.32  ? 68  ARG   A O   1 
ATOM   483  C  CB  . ARG   A 1 62  ? 8.664  -0.356  28.828 1.00 14.05  ? 68  ARG   A CB  1 
ATOM   484  C  CG  . ARG   A 1 62  ? 7.503  0.617   28.986 1.00 14.24  ? 68  ARG   A CG  1 
ATOM   485  C  CD  . ARG   A 1 62  ? 6.761  0.311   30.269 1.00 14.03  ? 68  ARG   A CD  1 
ATOM   486  N  NE  . ARG   A 1 62  ? 5.606  1.204   30.427 1.00 16.17  ? 68  ARG   A NE  1 
ATOM   487  C  CZ  . ARG   A 1 62  ? 5.632  2.376   31.053 1.00 14.82  ? 68  ARG   A CZ  1 
ATOM   488  N  NH1 . ARG   A 1 62  ? 6.769  2.828   31.599 1.00 16.49  ? 68  ARG   A NH1 1 
ATOM   489  N  NH2 . ARG   A 1 62  ? 4.510  3.109   31.164 1.00 17.20  ? 68  ARG   A NH2 1 
ATOM   490  N  N   . ARG   A 1 63  ? 12.104 -0.915  29.272 1.00 13.67  ? 69  ARG   A N   1 
ATOM   491  C  CA  . ARG   A 1 63  ? 13.110 -1.977  28.960 1.00 14.90  ? 69  ARG   A CA  1 
ATOM   492  C  C   . ARG   A 1 63  ? 12.508 -3.087  28.082 1.00 16.96  ? 69  ARG   A C   1 
ATOM   493  O  O   . ARG   A 1 63  ? 12.684 -4.300  28.349 1.00 19.22  ? 69  ARG   A O   1 
ATOM   494  C  CB  . ARG   A 1 63  ? 13.751 -2.610  30.205 1.00 17.79  ? 69  ARG   A CB  1 
ATOM   495  C  CG  . ARG   A 1 63  ? 14.674 -1.688  30.857 1.00 19.14  ? 69  ARG   A CG  1 
ATOM   496  C  CD  . ARG   A 1 63  ? 15.496 -2.497  31.869 1.00 19.77  ? 69  ARG   A CD  1 
ATOM   497  N  NE  . ARG   A 1 63  ? 16.258 -1.564  32.659 1.00 21.21  ? 69  ARG   A NE  1 
ATOM   498  C  CZ  . ARG   A 1 63  ? 15.940 -1.175  33.891 1.00 18.99  ? 69  ARG   A CZ  1 
ATOM   499  N  NH1 . ARG   A 1 63  ? 14.862 -1.676  34.501 1.00 19.58  ? 69  ARG   A NH1 1 
ATOM   500  N  NH2 . ARG   A 1 63  ? 16.690 -0.280  34.521 1.00 20.70  ? 69  ARG   A NH2 1 
ATOM   501  N  N   . LYS   A 1 64  ? 11.765 -2.702  27.080 1.00 13.97  ? 70  LYS   A N   1 
ATOM   502  C  CA  . LYS   A 1 64  ? 11.052 -3.697  26.272 1.00 14.64  ? 70  LYS   A CA  1 
ATOM   503  C  C   . LYS   A 1 64  ? 11.036 -3.314  24.833 1.00 13.23  ? 70  LYS   A C   1 
ATOM   504  O  O   . LYS   A 1 64  ? 10.940 -2.126  24.485 1.00 13.22  ? 70  LYS   A O   1 
ATOM   505  C  CB  . LYS   A 1 64  ? 9.600  -3.812  26.803 1.00 18.73  ? 70  LYS   A CB  1 
ATOM   506  C  CG  . LYS   A 1 64  ? 9.465  -4.799  27.984 1.00 28.38  ? 70  LYS   A CG  1 
ATOM   507  C  CD  . LYS   A 1 64  ? 8.021  -5.125  28.304 1.00 37.17  ? 70  LYS   A CD  1 
ATOM   508  C  CE  . LYS   A 1 64  ? 7.915  -6.073  29.491 1.00 43.19  ? 70  LYS   A CE  1 
ATOM   509  N  NZ  . LYS   A 1 64  ? 8.434  -5.475  30.754 1.00 47.15  ? 70  LYS   A NZ  1 
ATOM   510  N  N   . HIS   A 1 65  ? 11.006 -4.323  23.972 1.00 12.05  ? 71  HIS   A N   1 
ATOM   511  C  CA  . HIS   A 1 65  ? 10.772 -4.183  22.539 1.00 11.40  ? 71  HIS   A CA  1 
ATOM   512  C  C   . HIS   A 1 65  ? 9.334  -4.523  22.259 1.00 13.01  ? 71  HIS   A C   1 
ATOM   513  O  O   . HIS   A 1 65  ? 8.838  -5.583  22.700 1.00 16.06  ? 71  HIS   A O   1 
ATOM   514  C  CB  . HIS   A 1 65  ? 11.696 -5.149  21.743 1.00 10.71  ? 71  HIS   A CB  1 
ATOM   515  C  CG  . HIS   A 1 65  ? 13.163 -4.816  21.855 1.00 12.37  ? 71  HIS   A CG  1 
ATOM   516  N  ND1 . HIS   A 1 65  ? 13.867 -4.125  20.885 1.00 15.85  ? 71  HIS   A ND1 1 
ATOM   517  C  CD2 . HIS   A 1 65  ? 14.022 -5.126  22.853 1.00 12.07  ? 71  HIS   A CD2 1 
ATOM   518  C  CE1 . HIS   A 1 65  ? 15.145 -4.078  21.308 1.00 13.74  ? 71  HIS   A CE1 1 
ATOM   519  N  NE2 . HIS   A 1 65  ? 15.256 -4.639  22.474 1.00 15.63  ? 71  HIS   A NE2 1 
ATOM   520  N  N   . TYR   A 1 66  ? 8.642  -3.658  21.501 1.00 10.99  ? 72  TYR   A N   1 
ATOM   521  C  CA  . TYR   A 1 66  ? 7.209  -3.833  21.233 1.00 11.21  ? 72  TYR   A CA  1 
ATOM   522  C  C   . TYR   A 1 66  ? 6.951  -3.941  19.751 1.00 11.13  ? 72  TYR   A C   1 
ATOM   523  O  O   . TYR   A 1 66  ? 7.467  -3.115  18.980 1.00 10.74  ? 72  TYR   A O   1 
ATOM   524  C  CB  . TYR   A 1 66  ? 6.393  -2.595  21.715 1.00 12.02  ? 72  TYR   A CB  1 
ATOM   525  C  CG  . TYR   A 1 66  ? 6.318  -2.428  23.224 1.00 13.62  ? 72  TYR   A CG  1 
ATOM   526  C  CD1 . TYR   A 1 66  ? 5.468  -3.226  23.997 1.00 15.30  ? 72  TYR   A CD1 1 
ATOM   527  C  CD2 . TYR   A 1 66  ? 7.068  -1.459  23.868 1.00 13.32  ? 72  TYR   A CD2 1 
ATOM   528  C  CE1 . TYR   A 1 66  ? 5.357  -3.041  25.368 1.00 15.90  ? 72  TYR   A CE1 1 
ATOM   529  C  CE2 . TYR   A 1 66  ? 6.967  -1.259  25.244 1.00 14.94  ? 72  TYR   A CE2 1 
ATOM   530  C  CZ  . TYR   A 1 66  ? 6.109  -2.055  25.993 1.00 16.05  ? 72  TYR   A CZ  1 
ATOM   531  O  OH  . TYR   A 1 66  ? 6.011  -1.860  27.366 1.00 18.42  ? 72  TYR   A OH  1 
ATOM   532  N  N   . PRO   A 1 67  ? 6.129  -4.903  19.338 1.00 10.73  ? 73  PRO   A N   1 
ATOM   533  C  CA  . PRO   A 1 67  ? 5.712  -4.953  17.933 1.00 11.15  ? 73  PRO   A CA  1 
ATOM   534  C  C   . PRO   A 1 67  ? 4.669  -3.854  17.675 1.00 11.72  ? 73  PRO   A C   1 
ATOM   535  O  O   . PRO   A 1 67  ? 3.745  -3.666  18.503 1.00 14.56  ? 73  PRO   A O   1 
ATOM   536  C  CB  . PRO   A 1 67  ? 5.063  -6.345  17.770 1.00 13.11  ? 73  PRO   A CB  1 
ATOM   537  C  CG  . PRO   A 1 67  ? 4.672  -6.753  19.165 1.00 14.58  ? 73  PRO   A CG  1 
ATOM   538  C  CD  . PRO   A 1 67  ? 5.593  -6.024  20.148 1.00 11.69  ? 73  PRO   A CD  1 
ATOM   539  N  N   . VAL   A 1 68  ? 4.796  -3.183  16.554 1.00 10.31  ? 74  VAL   A N   1 
ATOM   540  C  CA  . VAL   A 1 68  ? 3.888  -2.062  16.197 1.00 12.00  ? 74  VAL   A CA  1 
ATOM   541  C  C   . VAL   A 1 68  ? 3.553  -2.046  14.741 1.00 12.01  ? 74  VAL   A C   1 
ATOM   542  O  O   . VAL   A 1 68  ? 4.332  -2.430  13.891 1.00 12.57  ? 74  VAL   A O   1 
ATOM   543  C  CB  . VAL   A 1 68  ? 4.486  -0.685  16.576 1.00 14.81  ? 74  VAL   A CB  1 
ATOM   544  C  CG1 . VAL   A 1 68  ? 4.435  -0.465  18.093 1.00 16.43  ? 74  VAL   A CG1 1 
ATOM   545  C  CG2 . VAL   A 1 68  ? 5.878  -0.501  16.006 1.00 15.41  ? 74  VAL   A CG2 1 
ATOM   546  N  N   . SER   A 1 69  ? 2.355  -1.497  14.425 1.00 11.98  ? 75  SER   A N   1 
ATOM   547  C  CA  . SER   A 1 69  ? 1.961  -1.076  13.083 1.00 12.56  ? 75  SER   A CA  1 
ATOM   548  C  C   . SER   A 1 69  ? 2.208  0.440   13.028 1.00 11.80  ? 75  SER   A C   1 
ATOM   549  O  O   . SER   A 1 69  ? 1.848  1.137   14.008 1.00 13.19  ? 75  SER   A O   1 
ATOM   550  C  CB  . SER   A 1 69  ? 0.464  -1.301  12.919 1.00 15.10  ? 75  SER   A CB  1 
ATOM   551  O  OG  . SER   A 1 69  ? 0.264  -2.700  12.899 1.00 23.36  ? 75  SER   A OG  1 
ATOM   552  N  N   . PHE   A 1 70  ? 2.773  0.962   11.963 1.00 12.40  ? 76  PHE   A N   1 
ATOM   553  C  CA  . PHE   A 1 70  ? 3.084  2.379   11.886 1.00 12.82  ? 76  PHE   A CA  1 
ATOM   554  C  C   . PHE   A 1 70  ? 2.699  2.966   10.561 1.00 13.78  ? 76  PHE   A C   1 
ATOM   555  O  O   . PHE   A 1 70  ? 2.622  2.258   9.554  1.00 14.26  ? 76  PHE   A O   1 
ATOM   556  C  CB  . PHE   A 1 70  ? 4.593  2.637   12.249 1.00 13.06  ? 76  PHE   A CB  1 
ATOM   557  C  CG  . PHE   A 1 70  ? 5.606  1.837   11.445 1.00 12.53  ? 76  PHE   A CG  1 
ATOM   558  C  CD1 . PHE   A 1 70  ? 6.020  0.574   11.859 1.00 12.11  ? 76  PHE   A CD1 1 
ATOM   559  C  CD2 . PHE   A 1 70  ? 6.181  2.364   10.297 1.00 12.70  ? 76  PHE   A CD2 1 
ATOM   560  C  CE1 . PHE   A 1 70  ? 6.971  -0.143  11.118 1.00 12.31  ? 76  PHE   A CE1 1 
ATOM   561  C  CE2 . PHE   A 1 70  ? 7.108  1.626   9.543  1.00 13.07  ? 76  PHE   A CE2 1 
ATOM   562  C  CZ  . PHE   A 1 70  ? 7.488  0.374   9.959  1.00 12.78  ? 76  PHE   A CZ  1 
ATOM   563  N  N   . SER   A 1 71  ? 2.431  4.275   10.543 1.00 14.10  ? 77  SER   A N   1 
ATOM   564  C  CA  . SER   A 1 71  ? 2.013  4.952   9.327  1.00 14.47  ? 77  SER   A CA  1 
ATOM   565  C  C   . SER   A 1 71  ? 3.175  5.179   8.368  1.00 14.44  ? 77  SER   A C   1 
ATOM   566  O  O   . SER   A 1 71  ? 4.348  5.050   8.750  1.00 14.82  ? 77  SER   A O   1 
ATOM   567  C  CB  . SER   A 1 71  ? 1.295  6.274   9.675  1.00 16.07  ? 77  SER   A CB  1 
ATOM   568  O  OG  . SER   A 1 71  ? 2.168  7.167   10.351 1.00 18.19  ? 77  SER   A OG  1 
ATOM   569  N  N   . LYS   A 1 72  ? 2.895  5.525   7.112  1.00 15.37  ? 78  LYS   A N   1 
ATOM   570  C  CA  . LYS   A 1 72  ? 3.946  5.846   6.152  1.00 15.76  ? 78  LYS   A CA  1 
ATOM   571  C  C   . LYS   A 1 72  ? 4.580  7.186   6.490  1.00 16.81  ? 78  LYS   A C   1 
ATOM   572  O  O   . LYS   A 1 72  ? 3.898  8.049   7.040  1.00 18.04  ? 78  LYS   A O   1 
ATOM   573  C  CB  . LYS   A 1 72  ? 3.362  5.874   4.735  1.00 19.07  ? 78  LYS   A CB  1 
ATOM   574  C  CG  . LYS   A 1 72  ? 2.912  4.502   4.295  1.00 21.05  ? 78  LYS   A CG  1 
ATOM   575  C  CD  . LYS   A 1 72  ? 2.531  4.471   2.820  1.00 28.12  ? 78  LYS   A CD  1 
ATOM   576  C  CE  . LYS   A 1 72  ? 2.147  3.073   2.420  1.00 33.55  ? 78  LYS   A CE  1 
ATOM   577  N  NZ  . LYS   A 1 72  ? 2.232  2.887   0.943  1.00 38.03  ? 78  LYS   A NZ  1 
ATOM   578  N  N   . PRO   A 1 73  ? 5.847  7.426   6.151  1.00 16.35  ? 79  PRO   A N   1 
ATOM   579  C  CA  . PRO   A 1 73  ? 6.491  8.715   6.494  1.00 16.89  ? 79  PRO   A CA  1 
ATOM   580  C  C   . PRO   A 1 73  ? 5.708  9.900   5.932  1.00 18.09  ? 79  PRO   A C   1 
ATOM   581  O  O   . PRO   A 1 73  ? 5.334  9.897   4.758  1.00 20.42  ? 79  PRO   A O   1 
ATOM   582  C  CB  . PRO   A 1 73  ? 7.895  8.604   5.878  1.00 19.11  ? 79  PRO   A CB  1 
ATOM   583  C  CG  . PRO   A 1 73  ? 8.108  7.178   5.569  1.00 22.03  ? 79  PRO   A CG  1 
ATOM   584  C  CD  . PRO   A 1 73  ? 6.772  6.490   5.466  1.00 17.79  ? 79  PRO   A CD  1 
ATOM   585  N  N   . SER   A 1 74  ? 5.418  10.866  6.793  1.00 17.38  ? 80  SER   A N   1 
ATOM   586  C  CA  . SER   A 1 74  ? 4.530  11.975  6.435  1.00 19.50  ? 80  SER   A CA  1 
ATOM   587  C  C   . SER   A 1 74  ? 4.919  13.244  7.184  1.00 17.99  ? 80  SER   A C   1 
ATOM   588  O  O   . SER   A 1 74  ? 5.753  13.229  8.097  1.00 16.45  ? 80  SER   A O   1 
ATOM   589  C  CB  . SER   A 1 74  ? 3.068  11.634  6.820  1.00 24.47  ? 80  SER   A CB  1 
ATOM   590  O  OG  . SER   A 1 74  ? 2.675  10.306  6.536  1.00 33.14  ? 80  SER   A OG  1 
ATOM   591  N  N   . LEU   A 1 75  ? 4.215  14.347  6.833  1.00 19.63  ? 81  LEU   A N   1 
ATOM   592  C  CA  . LEU   A 1 75  ? 4.407  15.640  7.439  1.00 21.46  ? 81  LEU   A CA  1 
ATOM   593  C  C   . LEU   A 1 75  ? 3.308  15.739  8.517  1.00 22.68  ? 81  LEU   A C   1 
ATOM   594  O  O   . LEU   A 1 75  ? 2.098  15.809  8.175  1.00 24.94  ? 81  LEU   A O   1 
ATOM   595  C  CB  . LEU   A 1 75  ? 4.216  16.721  6.332  1.00 22.57  ? 81  LEU   A CB  1 
ATOM   596  C  CG  . LEU   A 1 75  ? 4.477  18.127  6.759  1.00 26.88  ? 81  LEU   A CG  1 
ATOM   597  C  CD1 . LEU   A 1 75  ? 5.930  18.330  7.101  1.00 27.60  ? 81  LEU   A CD1 1 
ATOM   598  C  CD2 . LEU   A 1 75  ? 4.106  19.123  5.624  1.00 27.99  ? 81  LEU   A CD2 1 
ATOM   599  N  N   . ILE   A 1 76  ? 3.675  15.685  9.796  1.00 21.73  ? 82  ILE   A N   1 
ATOM   600  C  CA  . ILE   A 1 76  ? 2.776  15.640  10.954 1.00 23.60  ? 82  ILE   A CA  1 
ATOM   601  C  C   . ILE   A 1 76  ? 3.023  16.809  11.892 1.00 23.94  ? 82  ILE   A C   1 
ATOM   602  O  O   . ILE   A 1 76  ? 4.198  17.156  12.176 1.00 22.40  ? 82  ILE   A O   1 
ATOM   603  C  CB  . ILE   A 1 76  ? 3.056  14.332  11.740 1.00 25.77  ? 82  ILE   A CB  1 
ATOM   604  C  CG1 . ILE   A 1 76  ? 2.896  13.034  10.865 1.00 29.40  ? 82  ILE   A CG1 1 
ATOM   605  C  CG2 . ILE   A 1 76  ? 2.252  14.248  13.065 1.00 27.53  ? 82  ILE   A CG2 1 
ATOM   606  C  CD1 . ILE   A 1 76  ? 1.461  12.535  10.679 1.00 32.77  ? 82  ILE   A CD1 1 
ATOM   607  N  N   . PHE   A 1 77  ? 1.950  17.405  12.427 1.00 25.16  ? 83  PHE   A N   1 
ATOM   608  C  CA  . PHE   A 1 77  ? 2.070  18.472  13.404 1.00 25.19  ? 83  PHE   A CA  1 
ATOM   609  C  C   . PHE   A 1 77  ? 2.428  17.841  14.753 1.00 26.80  ? 83  PHE   A C   1 
ATOM   610  O  O   . PHE   A 1 77  ? 1.811  16.860  15.192 1.00 29.44  ? 83  PHE   A O   1 
ATOM   611  C  CB  . PHE   A 1 77  ? 0.734  19.272  13.526 1.00 26.44  ? 83  PHE   A CB  1 
ATOM   612  C  CG  . PHE   A 1 77  ? 0.946  20.561  14.259 1.00 28.99  ? 83  PHE   A CG  1 
ATOM   613  C  CD1 . PHE   A 1 77  ? 1.636  21.604  13.669 1.00 31.65  ? 83  PHE   A CD1 1 
ATOM   614  C  CD2 . PHE   A 1 77  ? 0.538  20.697  15.578 1.00 31.89  ? 83  PHE   A CD2 1 
ATOM   615  C  CE1 . PHE   A 1 77  ? 1.863  22.787  14.360 1.00 34.20  ? 83  PHE   A CE1 1 
ATOM   616  C  CE2 . PHE   A 1 77  ? 0.749  21.883  16.260 1.00 33.21  ? 83  PHE   A CE2 1 
ATOM   617  C  CZ  . PHE   A 1 77  ? 1.388  22.929  15.641 1.00 34.24  ? 83  PHE   A CZ  1 
ATOM   618  N  N   . VAL   A 1 78  ? 3.525  18.331  15.364 1.00 24.17  ? 84  VAL   A N   1 
ATOM   619  C  CA  . VAL   A 1 78  ? 3.985  17.834  16.654 1.00 22.71  ? 84  VAL   A CA  1 
ATOM   620  C  C   . VAL   A 1 78  ? 3.886  18.991  17.671 1.00 22.32  ? 84  VAL   A C   1 
ATOM   621  O  O   . VAL   A 1 78  ? 4.382  20.066  17.373 1.00 22.92  ? 84  VAL   A O   1 
ATOM   622  C  CB  . VAL   A 1 78  ? 5.448  17.317  16.527 1.00 21.21  ? 84  VAL   A CB  1 
ATOM   623  C  CG1 . VAL   A 1 78  ? 5.942  16.795  17.891 1.00 21.78  ? 84  VAL   A CG1 1 
ATOM   624  C  CG2 . VAL   A 1 78  ? 5.508  16.193  15.471 1.00 21.36  ? 84  VAL   A CG2 1 
ATOM   625  N  N   . GLU   A 1 79  ? 3.351  18.718  18.868 1.00 22.44  ? 85  GLU   A N   1 
ATOM   626  C  CA  . GLU   A 1 79  ? 3.225  19.726  19.922 1.00 24.15  ? 85  GLU   A CA  1 
ATOM   627  C  C   . GLU   A 1 79  ? 4.588  20.173  20.426 1.00 24.32  ? 85  GLU   A C   1 
ATOM   628  O  O   . GLU   A 1 79  ? 5.583  19.460  20.300 1.00 23.84  ? 85  GLU   A O   1 
ATOM   629  C  CB  . GLU   A 1 79  ? 2.406  19.169  21.103 1.00 28.68  ? 85  GLU   A CB  1 
ATOM   630  C  CG  . GLU   A 1 79  ? 0.927  18.966  20.777 1.00 35.72  ? 85  GLU   A CG  1 
ATOM   631  C  CD  . GLU   A 1 79  ? 0.242  20.211  20.244 1.00 45.71  ? 85  GLU   A CD  1 
ATOM   632  O  OE1 . GLU   A 1 79  ? 0.347  21.280  20.891 1.00 46.56  ? 85  GLU   A OE1 1 
ATOM   633  O  OE2 . GLU   A 1 79  ? -0.375 20.127  19.158 1.00 51.24  ? 85  GLU   A OE2 1 
ATOM   634  N  N   . ALA   A 1 80  ? 4.617  21.355  21.044 1.00 25.47  ? 86  ALA   A N   1 
ATOM   635  C  CA  . ALA   A 1 80  ? 5.825  21.931  21.624 1.00 27.23  ? 86  ALA   A CA  1 
ATOM   636  C  C   . ALA   A 1 80  ? 6.410  21.027  22.664 1.00 29.65  ? 86  ALA   A C   1 
ATOM   637  O  O   . ALA   A 1 80  ? 5.697  20.317  23.393 1.00 30.51  ? 86  ALA   A O   1 
ATOM   638  C  CB  . ALA   A 1 80  ? 5.512  23.276  22.262 1.00 28.41  ? 86  ALA   A CB  1 
ATOM   639  N  N   . SER   A 1 81  ? 7.740  20.951  22.664 1.00 30.10  ? 87  SER   A N   1 
ATOM   640  C  CA  . SER   A 1 81  ? 8.481  20.173  23.651 1.00 30.57  ? 87  SER   A CA  1 
ATOM   641  C  C   . SER   A 1 81  ? 9.590  21.110  24.213 1.00 31.54  ? 87  SER   A C   1 
ATOM   642  O  O   . SER   A 1 81  ? 9.657  22.262  23.793 1.00 31.63  ? 87  SER   A O   1 
ATOM   643  C  CB  . SER   A 1 81  ? 9.125  18.967  22.983 1.00 30.86  ? 87  SER   A CB  1 
ATOM   644  O  OG  . SER   A 1 81  ? 10.132 19.393  22.072 1.00 28.98  ? 87  SER   A OG  1 
ATOM   645  N  N   . GLU   A 1 82  ? 10.571 20.570  24.919 1.00 32.60  ? 88  GLU   A N   1 
ATOM   646  C  CA  . GLU   A 1 82  ? 11.606 21.561  25.366 1.00 32.44  ? 88  GLU   A CA  1 
ATOM   647  C  C   . GLU   A 1 82  ? 12.648 21.745  24.254 1.00 27.35  ? 88  GLU   A C   1 
ATOM   648  O  O   . GLU   A 1 82  ? 13.413 22.676  24.306 1.00 26.82  ? 88  GLU   A O   1 
ATOM   649  C  CB  . GLU   A 1 82  ? 12.149 21.244  26.769 1.00 37.94  ? 88  GLU   A CB  1 
ATOM   650  C  CG  . GLU   A 1 82  ? 13.388 20.388  26.758 1.00 44.42  ? 88  GLU   A CG  1 
ATOM   651  C  CD  . GLU   A 1 82  ? 13.247 19.208  27.694 1.00 55.08  ? 88  GLU   A CD  1 
ATOM   652  O  OE1 . GLU   A 1 82  ? 14.170 18.978  28.500 1.00 56.47  ? 88  GLU   A OE1 1 
ATOM   653  O  OE2 . GLU   A 1 82  ? 12.199 18.547  27.623 1.00 59.56  ? 88  GLU   A OE2 1 
ATOM   654  N  N   . TYR   A 1 83  ? 12.569 20.901  23.224 1.00 24.35  ? 89  TYR   A N   1 
ATOM   655  C  CA  . TYR   A 1 83  ? 13.552 20.984  22.118 1.00 21.35  ? 89  TYR   A CA  1 
ATOM   656  C  C   . TYR   A 1 83  ? 13.077 21.685  20.867 1.00 20.80  ? 89  TYR   A C   1 
ATOM   657  O  O   . TYR   A 1 83  ? 13.888 22.199  20.077 1.00 20.45  ? 89  TYR   A O   1 
ATOM   658  C  CB  . TYR   A 1 83  ? 14.003 19.579  21.746 1.00 21.67  ? 89  TYR   A CB  1 
ATOM   659  C  CG  . TYR   A 1 83  ? 14.616 18.886  22.933 1.00 21.99  ? 89  TYR   A CG  1 
ATOM   660  C  CD1 . TYR   A 1 83  ? 15.909 19.182  23.340 1.00 24.23  ? 89  TYR   A CD1 1 
ATOM   661  C  CD2 . TYR   A 1 83  ? 13.875 18.008  23.708 1.00 25.09  ? 89  TYR   A CD2 1 
ATOM   662  C  CE1 . TYR   A 1 83  ? 16.494 18.524  24.411 1.00 26.30  ? 89  TYR   A CE1 1 
ATOM   663  C  CE2 . TYR   A 1 83  ? 14.453 17.333  24.776 1.00 26.84  ? 89  TYR   A CE2 1 
ATOM   664  C  CZ  . TYR   A 1 83  ? 15.745 17.631  25.157 1.00 28.40  ? 89  TYR   A CZ  1 
ATOM   665  O  OH  . TYR   A 1 83  ? 16.322 16.957  26.211 1.00 31.72  ? 89  TYR   A OH  1 
ATOM   666  N  N   . TYR   A 1 84  ? 11.750 21.688  20.657 1.00 22.19  ? 90  TYR   A N   1 
ATOM   667  C  CA  . TYR   A 1 84  ? 11.224 22.341  19.463 1.00 22.08  ? 90  TYR   A CA  1 
ATOM   668  C  C   . TYR   A 1 84  ? 9.895  23.016  19.831 1.00 23.38  ? 90  TYR   A C   1 
ATOM   669  O  O   . TYR   A 1 84  ? 9.144  22.458  20.652 1.00 23.85  ? 90  TYR   A O   1 
ATOM   670  C  CB  . TYR   A 1 84  ? 10.902 21.309  18.346 1.00 20.98  ? 90  TYR   A CB  1 
ATOM   671  C  CG  . TYR   A 1 84  ? 12.083 20.548  17.761 1.00 18.43  ? 90  TYR   A CG  1 
ATOM   672  C  CD1 . TYR   A 1 84  ? 13.017 21.178  16.943 1.00 17.93  ? 90  TYR   A CD1 1 
ATOM   673  C  CD2 . TYR   A 1 84  ? 12.267 19.204  18.037 1.00 17.86  ? 90  TYR   A CD2 1 
ATOM   674  C  CE1 . TYR   A 1 84  ? 14.080 20.466  16.382 1.00 17.16  ? 90  TYR   A CE1 1 
ATOM   675  C  CE2 . TYR   A 1 84  ? 13.332 18.491  17.508 1.00 17.85  ? 90  TYR   A CE2 1 
ATOM   676  C  CZ  . TYR   A 1 84  ? 14.259 19.146  16.732 1.00 16.10  ? 90  TYR   A CZ  1 
ATOM   677  O  OH  . TYR   A 1 84  ? 15.325 18.440  16.244 1.00 16.13  ? 90  TYR   A OH  1 
ATOM   678  N  N   . PRO   A 1 85  ? 9.557  24.094  19.127 1.00 24.57  ? 91  PRO   A N   1 
ATOM   679  C  CA  . PRO   A 1 85  ? 8.201  24.684  19.286 1.00 25.43  ? 91  PRO   A CA  1 
ATOM   680  C  C   . PRO   A 1 85  ? 7.221  23.726  18.583 1.00 26.12  ? 91  PRO   A C   1 
ATOM   681  O  O   . PRO   A 1 85  ? 7.643  22.800  17.833 1.00 25.03  ? 91  PRO   A O   1 
ATOM   682  C  CB  . PRO   A 1 85  ? 8.318  26.011  18.506 1.00 27.61  ? 91  PRO   A CB  1 
ATOM   683  C  CG  . PRO   A 1 85  ? 9.324  25.711  17.411 1.00 28.72  ? 91  PRO   A CG  1 
ATOM   684  C  CD  . PRO   A 1 85  ? 10.341 24.798  18.080 1.00 25.08  ? 91  PRO   A CD  1 
ATOM   685  N  N   . ALA   A 1 86  ? 5.913  23.967  18.712 1.00 27.59  ? 92  ALA   A N   1 
ATOM   686  C  CA  . ALA   A 1 86  ? 4.910  23.187  17.987 1.00 27.81  ? 92  ALA   A CA  1 
ATOM   687  C  C   . ALA   A 1 86  ? 5.153  23.491  16.485 1.00 27.97  ? 92  ALA   A C   1 
ATOM   688  O  O   . ALA   A 1 86  ? 5.409  24.639  16.117 1.00 30.33  ? 92  ALA   A O   1 
ATOM   689  C  CB  . ALA   A 1 86  ? 3.512  23.636  18.416 1.00 27.95  ? 92  ALA   A CB  1 
ATOM   690  N  N   . ARG   A 1 87  ? 5.221  22.442  15.662 1.00 27.00  ? 93  ARG   A N   1 
ATOM   691  C  CA  . ARG   A 1 87  ? 5.590  22.625  14.260 1.00 26.14  ? 93  ARG   A CA  1 
ATOM   692  C  C   . ARG   A 1 87  ? 5.268  21.358  13.485 1.00 25.74  ? 93  ARG   A C   1 
ATOM   693  O  O   . ARG   A 1 87  ? 4.966  20.336  14.072 1.00 26.93  ? 93  ARG   A O   1 
ATOM   694  C  CB  . ARG   A 1 87  ? 7.113  22.886  14.149 1.00 25.78  ? 93  ARG   A CB  1 
ATOM   695  C  CG  . ARG   A 1 87  ? 7.933  21.566  14.455 1.00 27.42  ? 93  ARG   A CG  1 
ATOM   696  C  CD  . ARG   A 1 87  ? 9.378  21.799  14.609 1.00 26.16  ? 93  ARG   A CD  1 
ATOM   697  N  NE  . ARG   A 1 87  ? 10.314 20.702  14.265 1.00 27.38  ? 93  ARG   A NE  1 
ATOM   698  C  CZ  . ARG   A 1 87  ? 10.392 19.467  14.725 1.00 29.80  ? 93  ARG   A CZ  1 
ATOM   699  N  NH1 . ARG   A 1 87  ? 9.429  18.976  15.520 1.00 29.77  ? 93  ARG   A NH1 1 
ATOM   700  N  NH2 . ARG   A 1 87  ? 11.392 18.672  14.333 1.00 22.35  ? 93  ARG   A NH2 1 
ATOM   701  N  N   . TYR   A 1 88  ? 5.422  21.432  12.160 1.00 26.66  ? 94  TYR   A N   1 
ATOM   702  C  CA  . TYR   A 1 88  ? 5.300  20.276  11.309 1.00 26.39  ? 94  TYR   A CA  1 
ATOM   703  C  C   . TYR   A 1 88  ? 6.658  19.600  11.221 1.00 23.68  ? 94  TYR   A C   1 
ATOM   704  O  O   . TYR   A 1 88  ? 7.669  20.258  10.957 1.00 25.12  ? 94  TYR   A O   1 
ATOM   705  C  CB  . TYR   A 1 88  ? 4.868  20.691  9.912  1.00 27.59  ? 94  TYR   A CB  1 
ATOM   706  C  CG  . TYR   A 1 88  ? 3.384  20.994  9.849  1.00 28.68  ? 94  TYR   A CG  1 
ATOM   707  C  CD1 . TYR   A 1 88  ? 2.450  19.975  9.741  1.00 29.34  ? 94  TYR   A CD1 1 
ATOM   708  C  CD2 . TYR   A 1 88  ? 2.909  22.293  9.980  1.00 29.71  ? 94  TYR   A CD2 1 
ATOM   709  C  CE1 . TYR   A 1 88  ? 1.086  20.238  9.726  1.00 31.49  ? 94  TYR   A CE1 1 
ATOM   710  C  CE2 . TYR   A 1 88  ? 1.545  22.564  9.989  1.00 31.44  ? 94  TYR   A CE2 1 
ATOM   711  C  CZ  . TYR   A 1 88  ? 0.639  21.529  9.870  1.00 32.41  ? 94  TYR   A CZ  1 
ATOM   712  O  OH  . TYR   A 1 88  ? -0.708 21.758  9.844  1.00 35.73  ? 94  TYR   A OH  1 
ATOM   713  N  N   . GLN   A 1 89  ? 6.689  18.268  11.499 1.00 20.32  ? 95  GLN   A N   1 
ATOM   714  C  CA  . GLN   A 1 89  ? 7.921  17.466  11.398 1.00 18.61  ? 95  GLN   A CA  1 
ATOM   715  C  C   . GLN   A 1 89  ? 7.749  16.566  10.172 1.00 18.18  ? 95  GLN   A C   1 
ATOM   716  O  O   . GLN   A 1 89  ? 6.670  15.975  9.973  1.00 18.49  ? 95  GLN   A O   1 
ATOM   717  C  CB  . GLN   A 1 89  ? 8.170  16.660  12.674 1.00 18.84  ? 95  GLN   A CB  1 
ATOM   718  C  CG  . GLN   A 1 89  ? 9.409  15.783  12.588 1.00 17.39  ? 95  GLN   A CG  1 
ATOM   719  C  CD  . GLN   A 1 89  ? 9.946  15.343  13.948 1.00 16.83  ? 95  GLN   A CD  1 
ATOM   720  O  OE1 . GLN   A 1 89  ? 9.889  16.057  14.972 1.00 19.43  ? 95  GLN   A OE1 1 
ATOM   721  N  NE2 . GLN   A 1 89  ? 10.506 14.153  13.982 1.00 15.22  ? 95  GLN   A NE2 1 
ATOM   722  N  N   . SER   A 1 90  ? 8.763  16.509  9.299  1.00 16.35  ? 96  SER   A N   1 
ATOM   723  C  CA  . SER   A 1 90  ? 8.657  15.729  8.094  1.00 15.96  ? 96  SER   A CA  1 
ATOM   724  C  C   . SER   A 1 90  ? 9.246  14.323  8.275  1.00 15.22  ? 96  SER   A C   1 
ATOM   725  O  O   . SER   A 1 90  ? 10.028 14.079  9.210  1.00 15.58  ? 96  SER   A O   1 
ATOM   726  C  CB  . SER   A 1 90  ? 9.345  16.461  6.945  1.00 19.07  ? 96  SER   A CB  1 
ATOM   727  O  OG  . SER   A 1 90  ? 10.722 16.569  7.250  1.00 20.88  ? 96  SER   A OG  1 
ATOM   728  N  N   . HIS   A 1 91  ? 8.855  13.418  7.353  1.00 15.88  ? 97  HIS   A N   1 
ATOM   729  C  CA  . HIS   A 1 91  ? 9.360  12.042  7.296  1.00 15.36  ? 97  HIS   A CA  1 
ATOM   730  C  C   . HIS   A 1 91  ? 9.095  11.328  8.644  1.00 13.15  ? 97  HIS   A C   1 
ATOM   731  O  O   . HIS   A 1 91  ? 9.941  10.505  9.073  1.00 14.57  ? 97  HIS   A O   1 
ATOM   732  C  CB  . HIS   A 1 91  ? 10.890 12.025  6.931  1.00 16.28  ? 97  HIS   A CB  1 
ATOM   733  C  CG  . HIS   A 1 91  ? 11.182 12.607  5.560  1.00 17.12  ? 97  HIS   A CG  1 
ATOM   734  N  ND1 . HIS   A 1 91  ? 11.301 11.790  4.452  1.00 19.46  ? 97  HIS   A ND1 1 
ATOM   735  C  CD2 . HIS   A 1 91  ? 11.315 13.902  5.171  1.00 20.14  ? 97  HIS   A CD2 1 
ATOM   736  C  CE1 . HIS   A 1 91  ? 11.548 12.609  3.419  1.00 20.24  ? 97  HIS   A CE1 1 
ATOM   737  N  NE2 . HIS   A 1 91  ? 11.556 13.885  3.805  1.00 21.55  ? 97  HIS   A NE2 1 
ATOM   738  N  N   . LEU   A 1 92  ? 7.971  11.590  9.282  1.00 13.07  ? 98  LEU   A N   1 
ATOM   739  C  CA  . LEU   A 1 92  ? 7.641  11.031  10.591 1.00 13.58  ? 98  LEU   A CA  1 
ATOM   740  C  C   . LEU   A 1 92  ? 6.562  9.951   10.413 1.00 13.78  ? 98  LEU   A C   1 
ATOM   741  O  O   . LEU   A 1 92  ? 5.638  10.106  9.613  1.00 14.79  ? 98  LEU   A O   1 
ATOM   742  C  CB  . LEU   A 1 92  ? 7.100  12.168  11.494 1.00 15.18  ? 98  LEU   A CB  1 
ATOM   743  C  CG  . LEU   A 1 92  ? 6.814  11.765  12.965 1.00 17.32  ? 98  LEU   A CG  1 
ATOM   744  C  CD1 . LEU   A 1 92  ? 8.088  11.454  13.681 1.00 17.26  ? 98  LEU   A CD1 1 
ATOM   745  C  CD2 . LEU   A 1 92  ? 6.077  12.886  13.725 1.00 19.74  ? 98  LEU   A CD2 1 
ATOM   746  N  N   . MET   A 1 93  ? 6.707  8.864   11.175 1.00 13.61  ? 99  MET   A N   1 
ATOM   747  C  CA  . MET   A 1 93  ? 5.722  7.751   11.146 1.00 13.72  ? 99  MET   A CA  1 
ATOM   748  C  C   . MET   A 1 93  ? 5.142  7.603   12.554 1.00 14.05  ? 99  MET   A C   1 
ATOM   749  O  O   . MET   A 1 93  ? 5.902  7.632   13.528 1.00 14.21  ? 99  MET   A O   1 
ATOM   750  C  CB  . MET   A 1 93  ? 6.486  6.471   10.782 1.00 14.23  ? 99  MET   A CB  1 
ATOM   751  C  CG  . MET   A 1 93  ? 7.130  6.565   9.404  1.00 14.45  ? 99  MET   A CG  1 
ATOM   752  S  SD  . MET   A 1 93  ? 8.235  5.210   8.961  1.00 18.08  ? 99  MET   A SD  1 
ATOM   753  C  CE  . MET   A 1 93  ? 9.544  5.466   10.191 1.00 21.50  ? 99  MET   A CE  1 
ATOM   754  N  N   . LEU   A 1 94  ? 3.827  7.413   12.694 1.00 13.05  ? 100 LEU   A N   1 
ATOM   755  C  CA  . LEU   A 1 94  ? 3.228  7.274   14.012 1.00 13.89  ? 100 LEU   A CA  1 
ATOM   756  C  C   . LEU   A 1 94  ? 2.727  5.856   14.274 1.00 12.87  ? 100 LEU   A C   1 
ATOM   757  O  O   . LEU   A 1 94  ? 2.285  5.139   13.349 1.00 14.20  ? 100 LEU   A O   1 
ATOM   758  C  CB  . LEU   A 1 94  ? 2.003  8.223   14.199 1.00 16.03  ? 100 LEU   A CB  1 
ATOM   759  C  CG  . LEU   A 1 94  ? 2.271  9.699   14.201 1.00 21.11  ? 100 LEU   A CG  1 
ATOM   760  C  CD1 . LEU   A 1 94  ? 0.978  10.502  14.469 1.00 21.93  ? 100 LEU   A CD1 1 
ATOM   761  C  CD2 . LEU   A 1 94  ? 3.276  10.117  15.269 1.00 23.75  ? 100 LEU   A CD2 1 
ATOM   762  N  N   . ALA   A 1 95  ? 2.790  5.449   15.522 1.00 12.97  ? 101 ALA   A N   1 
ATOM   763  C  CA  . ALA   A 1 95  ? 2.247  4.163   15.986 1.00 12.01  ? 101 ALA   A CA  1 
ATOM   764  C  C   . ALA   A 1 95  ? 1.631  4.369   17.379 1.00 11.86  ? 101 ALA   A C   1 
ATOM   765  O  O   . ALA   A 1 95  ? 1.911  5.370   18.085 1.00 12.75  ? 101 ALA   A O   1 
ATOM   766  C  CB  . ALA   A 1 95  ? 3.365  3.093   16.103 1.00 12.42  ? 101 ALA   A CB  1 
ATOM   767  N  N   . VAL   A 1 96  ? 0.826  3.399   17.813 1.00 12.41  ? 102 VAL   A N   1 
ATOM   768  C  CA  . VAL   A 1 96  ? 0.300  3.382   19.147 1.00 11.89  ? 102 VAL   A CA  1 
ATOM   769  C  C   . VAL   A 1 96  ? 1.342  2.654   20.040 1.00 13.88  ? 102 VAL   A C   1 
ATOM   770  O  O   . VAL   A 1 96  ? 1.670  1.517   19.778 1.00 15.56  ? 102 VAL   A O   1 
ATOM   771  C  CB  . VAL   A 1 96  ? -1.048 2.651   19.168 1.00 12.61  ? 102 VAL   A CB  1 
ATOM   772  C  CG1 . VAL   A 1 96  ? -1.551 2.497   20.614 1.00 13.88  ? 102 VAL   A CG1 1 
ATOM   773  C  CG2 . VAL   A 1 96  ? -2.064 3.398   18.290 1.00 12.45  ? 102 VAL   A CG2 1 
ATOM   774  N  N   . GLY   A 1 97  ? 1.879  3.407   20.980 1.00 14.61  ? 103 GLY   A N   1 
ATOM   775  C  CA  . GLY   A 1 97  ? 2.921  2.800   21.815 1.00 15.29  ? 103 GLY   A CA  1 
ATOM   776  C  C   . GLY   A 1 97  ? 3.327  3.748   22.891 1.00 15.88  ? 103 GLY   A C   1 
ATOM   777  O  O   . GLY   A 1 97  ? 3.056  4.936   22.779 1.00 17.59  ? 103 GLY   A O   1 
ATOM   778  N  N   . HIS   A 1 98  ? 3.857  3.138   23.960 1.00 18.35  ? 104 HIS   A N   1 
ATOM   779  C  CA  . HIS   A 1 98  ? 4.386  3.980   25.046 1.00 19.49  ? 104 HIS   A CA  1 
ATOM   780  C  C   . HIS   A 1 98  ? 5.671  4.738   24.660 1.00 17.22  ? 104 HIS   A C   1 
ATOM   781  O  O   . HIS   A 1 98  ? 6.609  4.135   24.108 1.00 17.41  ? 104 HIS   A O   1 
ATOM   782  C  CB  . HIS   A 1 98  ? 4.562  3.154   26.347 1.00 20.94  ? 104 HIS   A CB  1 
ATOM   783  C  CG  . HIS   A 1 98  ? 5.051  4.038   27.432 1.00 21.70  ? 104 HIS   A CG  1 
ATOM   784  N  ND1 . HIS   A 1 98  ? 4.236  4.972   28.018 1.00 22.08  ? 104 HIS   A ND1 1 
ATOM   785  C  CD2 . HIS   A 1 98  ? 6.277  4.212   27.961 1.00 21.89  ? 104 HIS   A CD2 1 
ATOM   786  C  CE1 . HIS   A 1 98  ? 4.923  5.657   28.899 1.00 21.87  ? 104 HIS   A CE1 1 
ATOM   787  N  NE2 . HIS   A 1 98  ? 6.175  5.206   28.887 1.00 21.07  ? 104 HIS   A NE2 1 
ATOM   788  N  N   . SER   A 1 99  ? 5.726  6.028   24.914 1.00 17.17  ? 105 SER   A N   1 
ATOM   789  C  CA  . SER   A 1 99  ? 6.932  6.836   24.670 1.00 18.47  ? 105 SER   A CA  1 
ATOM   790  C  C   . SER   A 1 99  ? 7.052  7.892   25.802 1.00 21.46  ? 105 SER   A C   1 
ATOM   791  O  O   . SER   A 1 99  ? 5.970  8.246   26.298 1.00 23.32  ? 105 SER   A O   1 
ATOM   792  C  CB  . SER   A 1 99  ? 6.910  7.451   23.244 1.00 19.87  ? 105 SER   A CB  1 
ATOM   793  O  OG  . SER   A 1 99  ? 8.130  8.083   22.899 1.00 21.83  ? 105 SER   A OG  1 
ATOM   794  N  N   . GLU   A 1 100 ? 8.258  8.342   26.160 1.00 17.41  ? 106 GLU   A N   1 
ATOM   795  C  CA  . GLU   A 1 100 ? 8.613  9.455   27.091 1.00 16.94  ? 106 GLU   A CA  1 
ATOM   796  C  C   . GLU   A 1 100 ? 9.837  10.129  26.453 1.00 18.57  ? 106 GLU   A C   1 
ATOM   797  O  O   . GLU   A 1 100 ? 10.484 9.492   25.646 1.00 16.91  ? 106 GLU   A O   1 
ATOM   798  C  CB  . GLU   A 1 100 ? 8.970  8.976   28.497 1.00 17.89  ? 106 GLU   A CB  1 
ATOM   799  C  CG  . GLU   A 1 100 ? 7.849  8.195   29.165 1.00 20.89  ? 106 GLU   A CG  1 
ATOM   800  C  CD  . GLU   A 1 100 ? 8.081  7.607   30.553 1.00 25.38  ? 106 GLU   A CD  1 
ATOM   801  O  OE1 . GLU   A 1 100 ? 8.970  8.090   31.276 1.00 29.63  ? 106 GLU   A OE1 1 
ATOM   802  O  OE2 . GLU   A 1 100 ? 7.353  6.670   30.913 1.00 23.79  ? 106 GLU   A OE2 1 
ATOM   803  N  N   . PRO   A 1 101 ? 10.205 11.391  26.780 1.00 18.93  ? 107 PRO   A N   1 
ATOM   804  C  CA  . PRO   A 1 101 ? 11.275 12.115  26.062 1.00 17.93  ? 107 PRO   A CA  1 
ATOM   805  C  C   . PRO   A 1 101 ? 12.588 11.344  25.952 1.00 18.36  ? 107 PRO   A C   1 
ATOM   806  O  O   . PRO   A 1 101 ? 13.181 11.345  24.888 1.00 17.96  ? 107 PRO   A O   1 
ATOM   807  C  CB  . PRO   A 1 101 ? 11.399 13.395  26.913 1.00 19.89  ? 107 PRO   A CB  1 
ATOM   808  C  CG  . PRO   A 1 101 ? 10.005 13.626  27.405 1.00 21.59  ? 107 PRO   A CG  1 
ATOM   809  C  CD  . PRO   A 1 101 ? 9.551  12.237  27.790 1.00 20.02  ? 107 PRO   A CD  1 
ATOM   810  N  N   . GLY   A 1 102 ? 12.975 10.668  27.022 1.00 16.48  ? 108 GLY   A N   1 
ATOM   811  C  CA  . GLY   A 1 102 ? 14.240 9.905   27.053 1.00 16.48  ? 108 GLY   A CA  1 
ATOM   812  C  C   . GLY   A 1 102 ? 14.204 8.657   26.184 1.00 13.92  ? 108 GLY   A C   1 
ATOM   813  O  O   . GLY   A 1 102 ? 15.217 8.035   26.055 1.00 14.57  ? 108 GLY   A O   1 
ATOM   814  N  N   . ASP   A 1 103 ? 13.026 8.319   25.648 1.00 13.24  ? 109 ASP   A N   1 
ATOM   815  C  CA  . ASP   A 1 103 ? 12.914 7.156   24.729 1.00 12.52  ? 109 ASP   A CA  1 
ATOM   816  C  C   . ASP   A 1 103 ? 13.444 7.555   23.344 1.00 12.79  ? 109 ASP   A C   1 
ATOM   817  O  O   . ASP   A 1 103 ? 13.658 6.653   22.538 1.00 11.91  ? 109 ASP   A O   1 
ATOM   818  C  CB  . ASP   A 1 103 ? 11.478 6.625   24.682 1.00 12.57  ? 109 ASP   A CB  1 
ATOM   819  C  CG  . ASP   A 1 103 ? 11.082 5.846   25.920 1.00 13.33  ? 109 ASP   A CG  1 
ATOM   820  O  OD1 . ASP   A 1 103 ? 11.961 5.196   26.493 1.00 13.96  ? 109 ASP   A OD1 1 
ATOM   821  O  OD2 . ASP   A 1 103 ? 9.896  5.919   26.298 1.00 13.87  ? 109 ASP   A OD2 1 
ATOM   822  N  N   . CYS   A 1 104 ? 13.612 8.845   23.076 1.00 12.46  ? 110 CYS   A N   1 
ATOM   823  C  CA  . CYS   A 1 104 ? 14.167 9.171   21.737 1.00 13.04  ? 110 CYS   A CA  1 
ATOM   824  C  C   . CYS   A 1 104 ? 15.514 8.465   21.497 1.00 12.04  ? 110 CYS   A C   1 
ATOM   825  O  O   . CYS   A 1 104 ? 16.329 8.391   22.420 1.00 12.67  ? 110 CYS   A O   1 
ATOM   826  C  CB  . CYS   A 1 104 ? 14.344 10.675  21.567 1.00 13.38  ? 110 CYS   A CB  1 
ATOM   827  S  SG  . CYS   A 1 104 ? 12.751 11.534  21.478 1.00 15.20  ? 110 CYS   A SG  1 
ATOM   828  N  N   . GLY   A 1 105 ? 15.664 7.923   20.287 1.00 10.44  ? 111 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 105 ? 16.861 7.220   19.910 1.00 11.02  ? 111 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 105 ? 16.684 5.722   19.839 1.00 10.32  ? 111 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 105 ? 17.540 5.032   19.263 1.00 11.48  ? 111 GLY   A O   1 
ATOM   832  N  N   . GLY   A 1 106 ? 15.618 5.190   20.439 1.00 10.81  ? 112 GLY   A N   1 
ATOM   833  C  CA  . GLY   A 1 106 ? 15.347 3.764   20.346 1.00 10.56  ? 112 GLY   A CA  1 
ATOM   834  C  C   . GLY   A 1 106 ? 15.115 3.343   18.891 1.00 9.76   ? 112 GLY   A C   1 
ATOM   835  O  O   . GLY   A 1 106 ? 14.417 4.065   18.139 1.00 10.06  ? 112 GLY   A O   1 
ATOM   836  N  N   . ILE   A 1 107 ? 15.617 2.187   18.469 1.00 9.64   ? 113 ILE   A N   1 
ATOM   837  C  CA  . ILE   A 1 107 ? 15.453 1.768   17.069 1.00 9.66   ? 113 ILE   A CA  1 
ATOM   838  C  C   . ILE   A 1 107 ? 14.110 1.120   16.797 1.00 9.10   ? 113 ILE   A C   1 
ATOM   839  O  O   . ILE   A 1 107 ? 13.647 0.288   17.596 1.00 10.06  ? 113 ILE   A O   1 
ATOM   840  C  CB  . ILE   A 1 107 ? 16.607 0.788   16.732 1.00 10.14  ? 113 ILE   A CB  1 
ATOM   841  C  CG1 . ILE   A 1 107 ? 17.902 1.654   16.449 1.00 12.26  ? 113 ILE   A CG1 1 
ATOM   842  C  CG2 . ILE   A 1 107 ? 16.310 -0.076  15.472 1.00 10.58  ? 113 ILE   A CG2 1 
ATOM   843  C  CD1 . ILE   A 1 107 ? 19.143 0.810   16.305 1.00 15.49  ? 113 ILE   A CD1 1 
ATOM   844  N  N   . LEU   A 1 108 ? 13.526 1.465   15.650 1.00 8.45   ? 114 LEU   A N   1 
ATOM   845  C  CA  . LEU   A 1 108 ? 12.428 0.748   15.011 1.00 8.95   ? 114 LEU   A CA  1 
ATOM   846  C  C   . LEU   A 1 108 ? 13.038 -0.091  13.881 1.00 9.07   ? 114 LEU   A C   1 
ATOM   847  O  O   . LEU   A 1 108 ? 13.805 0.451   13.059 1.00 9.40   ? 114 LEU   A O   1 
ATOM   848  C  CB  . LEU   A 1 108 ? 11.439 1.769   14.414 1.00 9.60   ? 114 LEU   A CB  1 
ATOM   849  C  CG  . LEU   A 1 108 ? 10.321 1.158   13.526 1.00 10.01  ? 114 LEU   A CG  1 
ATOM   850  C  CD1 . LEU   A 1 108 ? 9.327  0.328   14.375 1.00 11.23  ? 114 LEU   A CD1 1 
ATOM   851  C  CD2 . LEU   A 1 108 ? 9.543  2.279   12.772 1.00 12.30  ? 114 LEU   A CD2 1 
ATOM   852  N  N   . ARG   A 1 109 ? 12.716 -1.383  13.841 1.00 9.66   ? 115 ARG   A N   1 
ATOM   853  C  CA  . ARG   A 1 109 ? 13.282 -2.284  12.796 1.00 10.03  ? 115 ARG   A CA  1 
ATOM   854  C  C   . ARG   A 1 109 ? 12.192 -3.166  12.235 1.00 10.74  ? 115 ARG   A C   1 
ATOM   855  O  O   . ARG   A 1 109 ? 11.202 -3.479  12.908 1.00 10.45  ? 115 ARG   A O   1 
ATOM   856  C  CB  . ARG   A 1 109 ? 14.427 -3.120  13.398 1.00 11.24  ? 115 ARG   A CB  1 
ATOM   857  C  CG  . ARG   A 1 109 ? 13.952 -4.104  14.480 1.00 11.49  ? 115 ARG   A CG  1 
ATOM   858  C  CD  . ARG   A 1 109 ? 15.209 -4.825  15.018 1.00 13.50  ? 115 ARG   A CD  1 
ATOM   859  N  NE  . ARG   A 1 109 ? 16.000 -3.963  15.881 1.00 14.13  ? 115 ARG   A NE  1 
ATOM   860  C  CZ  . ARG   A 1 109 ? 17.315 -3.761  15.805 1.00 14.76  ? 115 ARG   A CZ  1 
ATOM   861  N  NH1 . ARG   A 1 109 ? 18.009 -4.183  14.741 1.00 15.61  ? 115 ARG   A NH1 1 
ATOM   862  N  NH2 . ARG   A 1 109 ? 17.931 -3.030  16.721 1.00 15.29  ? 115 ARG   A NH2 1 
ATOM   863  N  N   . CYS   A 1 110 ? 12.405 -3.619  11.014 1.00 13.48  ? 116 CYS   A N   1 
ATOM   864  C  CA  . CYS   A 1 110 ? 11.470 -4.541  10.317 1.00 15.51  ? 116 CYS   A CA  1 
ATOM   865  C  C   . CYS   A 1 110 ? 12.298 -5.732  9.898  1.00 17.24  ? 116 CYS   A C   1 
ATOM   866  O  O   . CYS   A 1 110 ? 13.495 -5.861  10.220 1.00 17.16  ? 116 CYS   A O   1 
ATOM   867  C  CB  . CYS   A 1 110 ? 10.814 -3.838  9.125  1.00 15.45  ? 116 CYS   A CB  1 
ATOM   868  S  SG  . CYS   A 1 110 ? 11.984 -3.490  7.766  1.00 15.34  ? 116 CYS   A SG  1 
ATOM   869  N  N   . GLN   A 1 111 ? 11.652 -6.641  9.103  1.00 18.47  ? 117 GLN   A N   1 
ATOM   870  C  CA  . GLN   A 1 111 ? 12.378 -7.801  8.601  1.00 20.79  ? 117 GLN   A CA  1 
ATOM   871  C  C   . GLN   A 1 111 ? 13.612 -7.449  7.743  1.00 22.56  ? 117 GLN   A C   1 
ATOM   872  O  O   . GLN   A 1 111 ? 14.533 -8.274  7.603  1.00 25.92  ? 117 GLN   A O   1 
ATOM   873  C  CB  . GLN   A 1 111 ? 11.440 -8.751  7.797  1.00 24.64  ? 117 GLN   A CB  1 
ATOM   874  C  CG  . GLN   A 1 111 ? 10.901 -8.123  6.525  1.00 27.05  ? 117 GLN   A CG  1 
ATOM   875  C  CD  . GLN   A 1 111 ? 10.000 -9.071  5.760  1.00 34.81  ? 117 GLN   A CD  1 
ATOM   876  O  OE1 . GLN   A 1 111 ? 8.764  -8.969  5.818  1.00 37.46  ? 117 GLN   A OE1 1 
ATOM   877  N  NE2 . GLN   A 1 111 ? 10.607 -9.999  5.030  1.00 33.78  ? 117 GLN   A NE2 1 
ATOM   878  N  N   . HIS   A 1 112 ? 13.668 -6.245  7.174  1.00 19.19  ? 118 HIS   A N   1 
ATOM   879  C  CA  . HIS   A 1 112 ? 14.782 -5.835  6.273  1.00 18.74  ? 118 HIS   A CA  1 
ATOM   880  C  C   . HIS   A 1 112 ? 15.939 -5.117  6.967  1.00 18.66  ? 118 HIS   A C   1 
ATOM   881  O  O   . HIS   A 1 112 ? 16.981 -4.855  6.347  1.00 21.26  ? 118 HIS   A O   1 
ATOM   882  C  CB  . HIS   A 1 112 ? 14.219 -4.956  5.137  1.00 19.52  ? 118 HIS   A CB  1 
ATOM   883  C  CG  . HIS   A 1 112 ? 13.068 -5.616  4.397  1.00 21.84  ? 118 HIS   A CG  1 
ATOM   884  N  ND1 . HIS   A 1 112 ? 11.727 -5.238  4.583  1.00 21.39  ? 118 HIS   A ND1 1 
ATOM   885  C  CD2 . HIS   A 1 112 ? 13.107 -6.579  3.435  1.00 24.87  ? 118 HIS   A CD2 1 
ATOM   886  C  CE1 . HIS   A 1 112 ? 11.009 -6.018  3.778  1.00 26.05  ? 118 HIS   A CE1 1 
ATOM   887  N  NE2 . HIS   A 1 112 ? 11.798 -6.835  3.072  1.00 27.34  ? 118 HIS   A NE2 1 
ATOM   888  N  N   . GLY   A 1 113 ? 15.731 -4.678  8.224  1.00 15.75  ? 119 GLY   A N   1 
ATOM   889  C  CA  . GLY   A 1 113 ? 16.772 -3.934  8.928  1.00 15.15  ? 119 GLY   A CA  1 
ATOM   890  C  C   . GLY   A 1 113 ? 16.196 -2.743  9.699  1.00 12.93  ? 119 GLY   A C   1 
ATOM   891  O  O   . GLY   A 1 113 ? 15.006 -2.715  10.022 1.00 13.06  ? 119 GLY   A O   1 
ATOM   892  N  N   . VAL   A 1 114 ? 17.060 -1.740  9.979  1.00 12.13  ? 120 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 114 ? 16.629 -0.546  10.755 1.00 11.48  ? 120 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 114 ? 15.798 0.379   9.890  1.00 10.51  ? 120 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 114 ? 16.210 0.727   8.758  1.00 11.36  ? 120 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 114 ? 17.870 0.193   11.306 1.00 11.43  ? 120 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 114 ? 17.458 1.524   11.978 1.00 12.67  ? 120 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 114 ? 18.635 -0.709  12.284 1.00 12.95  ? 120 VAL   A CG2 1 
ATOM   899  N  N   . VAL   A 1 115 ? 14.644 0.780   10.410 1.00 10.20  ? 121 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 115 ? 13.712 1.646   9.715  1.00 11.13  ? 121 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 115 ? 13.871 3.100   10.146 1.00 10.78  ? 121 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 115 ? 13.726 4.044   9.345  1.00 11.53  ? 121 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 115 ? 12.256 1.171   10.014 1.00 11.89  ? 121 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 115 ? 11.170 2.166   9.517  1.00 13.79  ? 121 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 115 ? 11.993 -0.220  9.481  1.00 13.50  ? 121 VAL   A CG2 1 
ATOM   906  N  N   . GLY   A 1 116 ? 14.079 3.323   11.448 1.00 11.07  ? 122 GLY   A N   1 
ATOM   907  C  CA  . GLY   A 1 116 ? 14.162 4.692   11.982 1.00 11.42  ? 122 GLY   A CA  1 
ATOM   908  C  C   . GLY   A 1 116 ? 14.391 4.704   13.477 1.00 10.69  ? 122 GLY   A C   1 
ATOM   909  O  O   . GLY   A 1 116 ? 14.703 3.640   14.064 1.00 10.60  ? 122 GLY   A O   1 
ATOM   910  N  N   . ILE   A 1 117 ? 14.264 5.881   14.095 1.00 10.33  ? 123 ILE   A N   1 
ATOM   911  C  CA  . ILE   A 1 117 ? 14.501 6.004   15.553 1.00 9.57   ? 123 ILE   A CA  1 
ATOM   912  C  C   . ILE   A 1 117 ? 13.355 6.772   16.188 1.00 9.23   ? 123 ILE   A C   1 
ATOM   913  O  O   . ILE   A 1 117 ? 12.763 7.661   15.533 1.00 10.54  ? 123 ILE   A O   1 
ATOM   914  C  CB  . ILE   A 1 117 ? 15.851 6.705   15.911 1.00 10.22  ? 123 ILE   A CB  1 
ATOM   915  C  CG1 . ILE   A 1 117 ? 16.000 8.028   15.175 1.00 11.81  ? 123 ILE   A CG1 1 
ATOM   916  C  CG2 . ILE   A 1 117 ? 16.996 5.729   15.706 1.00 11.84  ? 123 ILE   A CG2 1 
ATOM   917  C  CD1 . ILE   A 1 117 ? 17.267 8.827   15.694 1.00 13.12  ? 123 ILE   A CD1 1 
ATOM   918  N  N   . VAL   A 1 118 ? 13.057 6.487   17.446 1.00 9.71   ? 124 VAL   A N   1 
ATOM   919  C  CA  . VAL   A 1 118 ? 12.009 7.229   18.164 1.00 10.07  ? 124 VAL   A CA  1 
ATOM   920  C  C   . VAL   A 1 118 ? 12.396 8.720   18.185 1.00 10.42  ? 124 VAL   A C   1 
ATOM   921  O  O   . VAL   A 1 118 ? 13.568 9.082   18.463 1.00 10.57  ? 124 VAL   A O   1 
ATOM   922  C  CB  . VAL   A 1 118 ? 11.913 6.718   19.606 1.00 10.87  ? 124 VAL   A CB  1 
ATOM   923  C  CG1 . VAL   A 1 118 ? 10.937 7.590   20.445 1.00 11.56  ? 124 VAL   A CG1 1 
ATOM   924  C  CG2 . VAL   A 1 118 ? 11.459 5.249   19.663 1.00 11.56  ? 124 VAL   A CG2 1 
ATOM   925  N  N   . SER   A 1 119 ? 11.431 9.585   17.873 1.00 10.76  ? 125 SER   A N   1 
ATOM   926  C  CA  . SER   A 1 119 ? 11.630 11.040  17.845 1.00 12.08  ? 125 SER   A CA  1 
ATOM   927  C  C   . SER   A 1 119 ? 10.543 11.804  18.590 1.00 13.79  ? 125 SER   A C   1 
ATOM   928  O  O   . SER   A 1 119 ? 10.841 12.920  19.073 1.00 15.81  ? 125 SER   A O   1 
ATOM   929  C  CB  . SER   A 1 119 ? 11.766 11.497  16.403 1.00 12.74  ? 125 SER   A CB  1 
ATOM   930  O  OG  . SER   A 1 119 ? 11.825 12.905  16.218 1.00 15.35  ? 125 SER   A OG  1 
ATOM   931  N  N   . THR   A 1 120 ? 9.289  11.271  18.663 1.00 13.85  ? 126 THR   A N   1 
ATOM   932  C  CA  . THR   A 1 120 ? 8.202  12.035  19.317 1.00 15.02  ? 126 THR   A CA  1 
ATOM   933  C  C   . THR   A 1 120 ? 7.413  11.094  20.229 1.00 16.72  ? 126 THR   A C   1 
ATOM   934  O  O   . THR   A 1 120 ? 7.463  9.859   20.063 1.00 15.19  ? 126 THR   A O   1 
ATOM   935  C  CB  . THR   A 1 120 ? 7.278  12.729  18.255 1.00 16.26  ? 126 THR   A CB  1 
ATOM   936  O  OG1 . THR   A 1 120 ? 6.445  11.756  17.604 1.00 17.70  ? 126 THR   A OG1 1 
ATOM   937  C  CG2 . THR   A 1 120 ? 8.024  13.562  17.255 1.00 16.95  ? 126 THR   A CG2 1 
ATOM   938  N  N   . GLY   A 1 121 ? 6.625  11.665  21.154 1.00 18.67  ? 127 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 121 ? 5.797  10.852  22.026 1.00 22.06  ? 127 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 121 ? 4.678  11.666  22.669 1.00 26.44  ? 127 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 121 ? 4.615  12.884  22.510 1.00 28.72  ? 127 GLY   A O   1 
ATOM   942  N  N   . GLY   A 1 122 ? 3.896  10.957  23.460 1.00 27.87  ? 128 GLY   A N   1 
ATOM   943  C  CA  . GLY   A 1 122 ? 2.804  11.481  24.277 1.00 29.15  ? 128 GLY   A CA  1 
ATOM   944  C  C   . GLY   A 1 122 ? 1.466  10.939  23.852 1.00 31.85  ? 128 GLY   A C   1 
ATOM   945  O  O   . GLY   A 1 122 ? 1.296  10.499  22.717 1.00 31.55  ? 128 GLY   A O   1 
ATOM   946  N  N   . ASN   A 1 123 ? 0.471  11.037  24.730 1.00 32.39  ? 129 ASN   A N   1 
ATOM   947  C  CA  . ASN   A 1 123 ? -0.904 10.663  24.392 1.00 32.69  ? 129 ASN   A CA  1 
ATOM   948  C  C   . ASN   A 1 123 ? -1.042 9.197   23.936 1.00 30.14  ? 129 ASN   A C   1 
ATOM   949  O  O   . ASN   A 1 123 ? -2.014 8.850   23.256 1.00 30.29  ? 129 ASN   A O   1 
ATOM   950  C  CB  . ASN   A 1 123 ? -1.495 11.658  23.347 1.00 33.88  ? 129 ASN   A CB  1 
ATOM   951  C  CG  . ASN   A 1 123 ? -1.516 13.102  23.816 1.00 37.84  ? 129 ASN   A CG  1 
ATOM   952  O  OD1 . ASN   A 1 123 ? -1.391 13.396  25.010 1.00 39.72  ? 129 ASN   A OD1 1 
ATOM   953  N  ND2 . ASN   A 1 123 ? -1.713 14.031  22.893 1.00 37.03  ? 129 ASN   A ND2 1 
ATOM   954  N  N   . GLY   A 1 124 ? -0.132 8.323   24.355 1.00 26.61  ? 130 GLY   A N   1 
ATOM   955  C  CA  . GLY   A 1 124 ? -0.180 6.926   23.980 1.00 22.61  ? 130 GLY   A CA  1 
ATOM   956  C  C   . GLY   A 1 124 ? 0.273  6.666   22.522 1.00 17.63  ? 130 GLY   A C   1 
ATOM   957  O  O   . GLY   A 1 124 ? 0.060  5.592   22.011 1.00 17.86  ? 130 GLY   A O   1 
ATOM   958  N  N   . LEU   A 1 125 ? 0.934  7.622   21.917 1.00 16.90  ? 131 LEU   A N   1 
ATOM   959  C  CA  . LEU   A 1 125 ? 1.506  7.499   20.566 1.00 15.87  ? 131 LEU   A CA  1 
ATOM   960  C  C   . LEU   A 1 125 ? 3.028  7.598   20.621 1.00 16.51  ? 131 LEU   A C   1 
ATOM   961  O  O   . LEU   A 1 125 ? 3.597  8.226   21.548 1.00 20.01  ? 131 LEU   A O   1 
ATOM   962  C  CB  . LEU   A 1 125 ? 1.003  8.638   19.692 1.00 16.47  ? 131 LEU   A CB  1 
ATOM   963  C  CG  . LEU   A 1 125 ? -0.539 8.617   19.493 1.00 17.25  ? 131 LEU   A CG  1 
ATOM   964  C  CD1 . LEU   A 1 125 ? -1.039 9.998   19.093 1.00 19.85  ? 131 LEU   A CD1 1 
ATOM   965  C  CD2 . LEU   A 1 125 ? -0.942 7.512   18.509 1.00 16.84  ? 131 LEU   A CD2 1 
ATOM   966  N  N   . VAL   A 1 126 ? 3.675  6.956   19.666 1.00 12.99  ? 132 VAL   A N   1 
ATOM   967  C  CA  . VAL   A 1 126 ? 5.133  7.083   19.538 1.00 12.88  ? 132 VAL   A CA  1 
ATOM   968  C  C   . VAL   A 1 126 ? 5.365  7.466   18.061 1.00 12.68  ? 132 VAL   A C   1 
ATOM   969  O  O   . VAL   A 1 126 ? 4.752  6.881   17.165 1.00 13.64  ? 132 VAL   A O   1 
ATOM   970  C  CB  . VAL   A 1 126 ? 5.839  5.761   19.963 1.00 13.04  ? 132 VAL   A CB  1 
ATOM   971  C  CG1 . VAL   A 1 126 ? 5.277  4.517   19.252 1.00 13.90  ? 132 VAL   A CG1 1 
ATOM   972  C  CG2 . VAL   A 1 126 ? 7.360  5.877   19.775 1.00 12.93  ? 132 VAL   A CG2 1 
ATOM   973  N  N   . GLY   A 1 127 ? 6.269  8.405   17.802 1.00 12.43  ? 133 GLY   A N   1 
ATOM   974  C  CA  . GLY   A 1 127 ? 6.617  8.785   16.442 1.00 12.48  ? 133 GLY   A CA  1 
ATOM   975  C  C   . GLY   A 1 127 ? 8.073  8.479   16.138 1.00 12.76  ? 133 GLY   A C   1 
ATOM   976  O  O   . GLY   A 1 127 ? 8.944  8.617   17.017 1.00 13.56  ? 133 GLY   A O   1 
ATOM   977  N  N   . PHE   A 1 128 ? 8.306  8.003   14.939 1.00 11.58  ? 134 PHE   A N   1 
ATOM   978  C  CA  . PHE   A 1 128 ? 9.655  7.583   14.493 1.00 11.56  ? 134 PHE   A CA  1 
ATOM   979  C  C   . PHE   A 1 128 ? 10.106 8.413   13.308 1.00 11.93  ? 134 PHE   A C   1 
ATOM   980  O  O   . PHE   A 1 128 ? 9.342  8.583   12.340 1.00 12.23  ? 134 PHE   A O   1 
ATOM   981  C  CB  . PHE   A 1 128 ? 9.617  6.097   14.057 1.00 11.24  ? 134 PHE   A CB  1 
ATOM   982  C  CG  . PHE   A 1 128 ? 8.999  5.164   15.080 1.00 11.04  ? 134 PHE   A CG  1 
ATOM   983  C  CD1 . PHE   A 1 128 ? 9.748  4.672   16.148 1.00 10.61  ? 134 PHE   A CD1 1 
ATOM   984  C  CD2 . PHE   A 1 128 ? 7.669  4.784   14.971 1.00 12.18  ? 134 PHE   A CD2 1 
ATOM   985  C  CE1 . PHE   A 1 128 ? 9.177  3.790   17.066 1.00 10.76  ? 134 PHE   A CE1 1 
ATOM   986  C  CE2 . PHE   A 1 128 ? 7.109  3.909   15.885 1.00 12.32  ? 134 PHE   A CE2 1 
ATOM   987  C  CZ  . PHE   A 1 128 ? 7.869  3.423   16.936 1.00 11.34  ? 134 PHE   A CZ  1 
ATOM   988  N  N   . ALA   A 1 129 ? 11.364 8.868   13.369 1.00 11.36  ? 135 ALA   A N   1 
ATOM   989  C  CA  . ALA   A 1 129 ? 12.001 9.546   12.221 1.00 11.84  ? 135 ALA   A CA  1 
ATOM   990  C  C   . ALA   A 1 129 ? 12.482 8.481   11.250 1.00 11.26  ? 135 ALA   A C   1 
ATOM   991  O  O   . ALA   A 1 129 ? 13.361 7.674   11.611 1.00 11.92  ? 135 ALA   A O   1 
ATOM   992  C  CB  . ALA   A 1 129 ? 13.144 10.408  12.726 1.00 11.32  ? 135 ALA   A CB  1 
ATOM   993  N  N   . ASP   A 1 130 ? 11.932 8.434   10.024 1.00 11.38  ? 136 ASP   A N   1 
ATOM   994  C  CA  . ASP   A 1 130 ? 12.344 7.429   9.051  1.00 12.10  ? 136 ASP   A CA  1 
ATOM   995  C  C   . ASP   A 1 130 ? 13.754 7.732   8.551  1.00 12.36  ? 136 ASP   A C   1 
ATOM   996  O  O   . ASP   A 1 130 ? 14.141 8.902   8.400  1.00 13.03  ? 136 ASP   A O   1 
ATOM   997  C  CB  . ASP   A 1 130 ? 11.398 7.536   7.839  1.00 14.22  ? 136 ASP   A CB  1 
ATOM   998  C  CG  . ASP   A 1 130 ? 11.641 6.526   6.762  1.00 18.38  ? 136 ASP   A CG  1 
ATOM   999  O  OD1 . ASP   A 1 130 ? 11.715 5.317   7.076  1.00 17.75  ? 136 ASP   A OD1 1 
ATOM   1000 O  OD2 . ASP   A 1 130 ? 11.885 6.959   5.595  1.00 22.65  ? 136 ASP   A OD2 1 
ATOM   1001 N  N   . VAL   A 1 131 ? 14.517 6.674   8.232  1.00 11.44  ? 137 VAL   A N   1 
ATOM   1002 C  CA  . VAL   A 1 131 ? 15.836 6.813   7.595  1.00 11.76  ? 137 VAL   A CA  1 
ATOM   1003 C  C   . VAL   A 1 131 ? 15.941 5.997   6.304  1.00 11.78  ? 137 VAL   A C   1 
ATOM   1004 O  O   . VAL   A 1 131 ? 17.016 5.994   5.673  1.00 11.54  ? 137 VAL   A O   1 
ATOM   1005 C  CB  . VAL   A 1 131 ? 16.992 6.434   8.536  1.00 11.59  ? 137 VAL   A CB  1 
ATOM   1006 C  CG1 . VAL   A 1 131 ? 17.055 7.366   9.767  1.00 12.42  ? 137 VAL   A CG1 1 
ATOM   1007 C  CG2 . VAL   A 1 131 ? 17.028 4.958   8.951  1.00 12.17  ? 137 VAL   A CG2 1 
ATOM   1008 N  N   . ARG   A 1 132 ? 14.869 5.313   5.880  1.00 11.81  ? 138 ARG   A N   1 
ATOM   1009 C  CA  . ARG   A 1 132 ? 14.950 4.393   4.727  1.00 12.07  ? 138 ARG   A CA  1 
ATOM   1010 C  C   . ARG   A 1 132 ? 15.213 5.101   3.405  1.00 13.73  ? 138 ARG   A C   1 
ATOM   1011 O  O   . ARG   A 1 132 ? 15.677 4.446   2.444  1.00 14.90  ? 138 ARG   A O   1 
ATOM   1012 C  CB  . ARG   A 1 132 ? 13.685 3.532   4.625  1.00 12.23  ? 138 ARG   A CB  1 
ATOM   1013 C  CG  . ARG   A 1 132 ? 13.539 2.570   5.841  1.00 12.28  ? 138 ARG   A CG  1 
ATOM   1014 C  CD  . ARG   A 1 132 ? 12.228 1.809   5.699  1.00 13.41  ? 138 ARG   A CD  1 
ATOM   1015 N  NE  . ARG   A 1 132 ? 11.097 2.733   5.939  1.00 13.76  ? 138 ARG   A NE  1 
ATOM   1016 C  CZ  . ARG   A 1 132 ? 9.821  2.360   6.037  1.00 15.30  ? 138 ARG   A CZ  1 
ATOM   1017 N  NH1 . ARG   A 1 132 ? 9.469  1.117   5.753  1.00 16.13  ? 138 ARG   A NH1 1 
ATOM   1018 N  NH2 . ARG   A 1 132 ? 8.893  3.249   6.374  1.00 17.17  ? 138 ARG   A NH2 1 
ATOM   1019 N  N   . ASP   A 1 133 ? 14.890 6.405   3.290  1.00 13.17  ? 139 ASP   A N   1 
ATOM   1020 C  CA  . ASP   A 1 133 ? 15.155 7.129   2.052  1.00 14.58  ? 139 ASP   A CA  1 
ATOM   1021 C  C   . ASP   A 1 133 ? 16.594 7.634   1.971  1.00 14.44  ? 139 ASP   A C   1 
ATOM   1022 O  O   . ASP   A 1 133 ? 16.983 8.137   0.915  1.00 16.41  ? 139 ASP   A O   1 
ATOM   1023 C  CB  . ASP   A 1 133 ? 14.165 8.325   1.950  1.00 16.79  ? 139 ASP   A CB  1 
ATOM   1024 C  CG  . ASP   A 1 133 ? 14.391 9.363   3.039  1.00 19.74  ? 139 ASP   A CG  1 
ATOM   1025 O  OD1 . ASP   A 1 133 ? 14.536 8.977   4.218  1.00 18.31  ? 139 ASP   A OD1 1 
ATOM   1026 O  OD2 . ASP   A 1 133 ? 14.383 10.569  2.731  1.00 22.59  ? 139 ASP   A OD2 1 
ATOM   1027 N  N   . LEU   A 1 134 ? 17.402 7.559   3.060  1.00 13.19  ? 140 LEU   A N   1 
ATOM   1028 C  CA  . LEU   A 1 134 ? 18.784 8.099   3.076  1.00 12.94  ? 140 LEU   A CA  1 
ATOM   1029 C  C   . LEU   A 1 134 ? 19.730 7.055   2.515  1.00 13.37  ? 140 LEU   A C   1 
ATOM   1030 O  O   . LEU   A 1 134 ? 20.423 6.341   3.248  1.00 13.73  ? 140 LEU   A O   1 
ATOM   1031 C  CB  . LEU   A 1 134 ? 19.130 8.496   4.531  1.00 12.75  ? 140 LEU   A CB  1 
ATOM   1032 C  CG  . LEU   A 1 134 ? 18.184 9.537   5.189  1.00 14.16  ? 140 LEU   A CG  1 
ATOM   1033 C  CD1 . LEU   A 1 134 ? 18.579 9.764   6.652  1.00 14.99  ? 140 LEU   A CD1 1 
ATOM   1034 C  CD2 . LEU   A 1 134 ? 18.184 10.862  4.441  1.00 16.82  ? 140 LEU   A CD2 1 
ATOM   1035 N  N   . LEU   A 1 135 ? 19.721 6.942   1.173  1.00 13.51  ? 141 LEU   A N   1 
ATOM   1036 C  CA  . LEU   A 1 135 ? 20.458 5.836   0.541  1.00 14.62  ? 141 LEU   A CA  1 
ATOM   1037 C  C   . LEU   A 1 135 ? 21.949 5.923   0.718  1.00 15.13  ? 141 LEU   A C   1 
ATOM   1038 O  O   . LEU   A 1 135 ? 22.651 4.888   0.747  1.00 16.42  ? 141 LEU   A O   1 
ATOM   1039 C  CB  . LEU   A 1 135 ? 20.106 5.711   -0.990 1.00 15.88  ? 141 LEU   A CB  1 
ATOM   1040 C  CG  . LEU   A 1 135 ? 18.600 5.733   -1.279 1.00 17.24  ? 141 LEU   A CG  1 
ATOM   1041 C  CD1 . LEU   A 1 135 ? 18.353 5.424   -2.769 1.00 19.64  ? 141 LEU   A CD1 1 
ATOM   1042 C  CD2 . LEU   A 1 135 ? 17.803 4.702   -0.455 1.00 18.58  ? 141 LEU   A CD2 1 
ATOM   1043 N  N   . TRP   A 1 136 ? 22.450 7.160   0.891  1.00 13.54  ? 142 TRP   A N   1 
ATOM   1044 C  CA  . TRP   A 1 136 ? 23.873 7.396   1.050  1.00 13.84  ? 142 TRP   A CA  1 
ATOM   1045 C  C   . TRP   A 1 136 ? 24.424 6.822   2.347  1.00 14.50  ? 142 TRP   A C   1 
ATOM   1046 O  O   . TRP   A 1 136 ? 25.649 6.669   2.467  1.00 16.33  ? 142 TRP   A O   1 
ATOM   1047 C  CB  . TRP   A 1 136 ? 24.170 8.909   0.931  1.00 14.70  ? 142 TRP   A CB  1 
ATOM   1048 C  CG  . TRP   A 1 136 ? 23.358 9.746   1.881  1.00 13.48  ? 142 TRP   A CG  1 
ATOM   1049 C  CD1 . TRP   A 1 136 ? 22.221 10.435  1.588  1.00 14.78  ? 142 TRP   A CD1 1 
ATOM   1050 C  CD2 . TRP   A 1 136 ? 23.699 10.074  3.239  1.00 13.78  ? 142 TRP   A CD2 1 
ATOM   1051 N  NE1 . TRP   A 1 136 ? 21.774 11.104  2.715  1.00 15.63  ? 142 TRP   A NE1 1 
ATOM   1052 C  CE2 . TRP   A 1 136 ? 22.681 10.907  3.734  1.00 14.48  ? 142 TRP   A CE2 1 
ATOM   1053 C  CE3 . TRP   A 1 136 ? 24.769 9.748   4.074  1.00 14.59  ? 142 TRP   A CE3 1 
ATOM   1054 C  CZ2 . TRP   A 1 136 ? 22.714 11.429  5.041  1.00 16.01  ? 142 TRP   A CZ2 1 
ATOM   1055 C  CZ3 . TRP   A 1 136 ? 24.811 10.267  5.363  1.00 16.84  ? 142 TRP   A CZ3 1 
ATOM   1056 C  CH2 . TRP   A 1 136 ? 23.802 11.110  5.821  1.00 16.30  ? 142 TRP   A CH2 1 
ATOM   1057 N  N   . LEU   A 1 137 ? 23.566 6.466   3.328  1.00 13.46  ? 143 LEU   A N   1 
ATOM   1058 C  CA  . LEU   A 1 137 ? 24.079 5.817   4.560  1.00 15.15  ? 143 LEU   A CA  1 
ATOM   1059 C  C   . LEU   A 1 137 ? 24.775 4.493   4.236  1.00 16.65  ? 143 LEU   A C   1 
ATOM   1060 O  O   . LEU   A 1 137 ? 25.612 4.039   5.041  1.00 18.39  ? 143 LEU   A O   1 
ATOM   1061 C  CB  . LEU   A 1 137 ? 22.935 5.552   5.549  1.00 14.94  ? 143 LEU   A CB  1 
ATOM   1062 C  CG  . LEU   A 1 137 ? 22.380 6.792   6.249  1.00 14.15  ? 143 LEU   A CG  1 
ATOM   1063 C  CD1 . LEU   A 1 137 ? 21.123 6.426   7.020  1.00 15.25  ? 143 LEU   A CD1 1 
ATOM   1064 C  CD2 . LEU   A 1 137 ? 23.452 7.413   7.215  1.00 14.37  ? 143 LEU   A CD2 1 
ATOM   1065 N  N   . ASP   A 1 138 ? 24.438 3.857   3.075  1.00 19.34  ? 144 ASP   A N   1 
ATOM   1066 C  CA  . ASP   A 1 138 ? 24.997 2.541   2.672  1.00 22.51  ? 144 ASP   A CA  1 
ATOM   1067 C  C   . ASP   A 1 138 ? 26.343 2.611   1.976  1.00 27.36  ? 144 ASP   A C   1 
ATOM   1068 O  O   . ASP   A 1 138 ? 26.858 1.564   1.557  1.00 28.76  ? 144 ASP   A O   1 
ATOM   1069 C  CB  . ASP   A 1 138 ? 24.023 1.800   1.701  1.00 23.10  ? 144 ASP   A CB  1 
ATOM   1070 C  CG  . ASP   A 1 138 ? 22.662 1.484   2.234  1.00 26.77  ? 144 ASP   A CG  1 
ATOM   1071 O  OD1 . ASP   A 1 138 ? 22.481 1.564   3.466  1.00 28.51  ? 144 ASP   A OD1 1 
ATOM   1072 O  OD2 . ASP   A 1 138 ? 21.751 1.153   1.417  1.00 34.19  ? 144 ASP   A OD2 1 
ATOM   1073 N  N   . GLU   A 1 139 ? 26.918 3.811   1.788  1.00 29.02  ? 145 GLU   A N   1 
ATOM   1074 C  CA  . GLU   A 1 139 ? 28.202 3.925   1.070  1.00 32.92  ? 145 GLU   A CA  1 
ATOM   1075 C  C   . GLU   A 1 139 ? 29.074 5.075   1.584  1.00 35.54  ? 145 GLU   A C   1 
ATOM   1076 O  O   . GLU   A 1 139 ? 28.623 5.856   2.423  1.00 36.11  ? 145 GLU   A O   1 
ATOM   1077 C  CB  . GLU   A 1 139 ? 27.866 4.161   -0.413 1.00 37.13  ? 145 GLU   A CB  1 
ATOM   1078 C  CG  . GLU   A 1 139 ? 27.098 5.456   -0.611 1.00 45.04  ? 145 GLU   A CG  1 
ATOM   1079 C  CD  . GLU   A 1 139 ? 26.208 5.526   -1.836 1.00 54.13  ? 145 GLU   A CD  1 
ATOM   1080 O  OE1 . GLU   A 1 139 ? 25.727 6.641   -2.149 1.00 55.16  ? 145 GLU   A OE1 1 
ATOM   1081 O  OE2 . GLU   A 1 139 ? 25.987 4.473   -2.480 1.00 58.05  ? 145 GLU   A OE2 1 
ATOM   1082 N  N   . GLU   A 1 140 ? 30.302 5.216   1.029  1.00 37.81  ? 146 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 140 ? 31.236 6.341   1.234  1.00 40.43  ? 146 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 140 ? 31.285 6.827   2.680  1.00 42.26  ? 146 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 140 ? 31.906 7.841   3.001  1.00 42.69  ? 146 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 140 ? 30.846 7.464   0.233  1.00 43.59  ? 146 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 140 ? 31.301 8.890   0.515  1.00 50.45  ? 146 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 140 ? 32.766 9.211   0.268  1.00 59.47  ? 146 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 140 ? 33.276 10.156  0.913  1.00 61.36  ? 146 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 140 ? 33.406 8.520   -0.561 1.00 61.54  ? 146 GLU   A OE2 1 
ATOM   1091 N  N   . SER   B 1 1   ? 21.932 -21.281 7.666  1.00 17.43  ? 7   SER   C N   1 
ATOM   1092 C  CA  . SER   B 1 1   ? 20.799 -21.052 8.596  1.00 16.62  ? 7   SER   C CA  1 
ATOM   1093 C  C   . SER   B 1 1   ? 20.754 -22.158 9.682  1.00 17.25  ? 7   SER   C C   1 
ATOM   1094 O  O   . SER   B 1 1   ? 21.412 -23.203 9.543  1.00 18.87  ? 7   SER   C O   1 
ATOM   1095 C  CB  . SER   B 1 1   ? 19.489 -21.064 7.809  1.00 20.42  ? 7   SER   C CB  1 
ATOM   1096 O  OG  . SER   B 1 1   ? 19.320 -22.342 7.234  1.00 24.19  ? 7   SER   C OG  1 
ATOM   1097 N  N   . GLY   B 1 2   ? 19.991 -21.923 10.744 1.00 16.55  ? 8   GLY   C N   1 
ATOM   1098 C  CA  . GLY   B 1 2   ? 19.829 -22.924 11.792 1.00 15.43  ? 8   GLY   C CA  1 
ATOM   1099 C  C   . GLY   B 1 2   ? 19.553 -22.317 13.143 1.00 14.34  ? 8   GLY   C C   1 
ATOM   1100 O  O   . GLY   B 1 2   ? 19.946 -21.186 13.407 1.00 15.41  ? 8   GLY   C O   1 
ATOM   1101 N  N   . ALA   B 1 3   ? 18.893 -23.063 14.018 1.00 13.61  ? 9   ALA   C N   1 
ATOM   1102 C  CA  . ALA   B 1 3   ? 18.567 -22.581 15.366 1.00 13.53  ? 9   ALA   C CA  1 
ATOM   1103 C  C   . ALA   B 1 3   ? 18.679 -23.713 16.397 1.00 12.50  ? 9   ALA   C C   1 
ATOM   1104 O  O   . ALA   B 1 3   ? 18.749 -24.897 16.010 1.00 13.70  ? 9   ALA   C O   1 
ATOM   1105 C  CB  . ALA   B 1 3   ? 17.121 -22.043 15.375 1.00 16.58  ? 9   ALA   C CB  1 
ATOM   1106 N  N   . ILE   B 1 4   ? 18.701 -23.347 17.672 1.00 12.54  ? 10  ILE   C N   1 
ATOM   1107 C  CA  . ILE   B 1 4   ? 18.617 -24.285 18.787 1.00 12.74  ? 10  ILE   C CA  1 
ATOM   1108 C  C   . ILE   B 1 4   ? 17.206 -24.100 19.397 1.00 12.30  ? 10  ILE   C C   1 
ATOM   1109 O  O   . ILE   B 1 4   ? 16.778 -22.946 19.609 1.00 13.61  ? 10  ILE   C O   1 
ATOM   1110 C  CB  . ILE   B 1 4   ? 19.643 -23.962 19.869 1.00 12.32  ? 10  ILE   C CB  1 
ATOM   1111 C  CG1 . ILE   B 1 4   ? 21.073 -23.843 19.287 1.00 13.38  ? 10  ILE   C CG1 1 
ATOM   1112 C  CG2 . ILE   B 1 4   ? 19.588 -25.049 20.965 1.00 14.64  ? 10  ILE   C CG2 1 
ATOM   1113 C  CD1 . ILE   B 1 4   ? 22.040 -23.242 20.313 1.00 13.73  ? 10  ILE   C CD1 1 
ATOM   1114 N  N   . TYR   B 1 5   ? 16.506 -25.195 19.689 1.00 12.82  ? 11  TYR   C N   1 
ATOM   1115 C  CA  . TYR   B 1 5   ? 15.150 -25.144 20.266 1.00 13.46  ? 11  TYR   C CA  1 
ATOM   1116 C  C   . TYR   B 1 5   ? 15.215 -25.828 21.633 1.00 14.80  ? 11  TYR   C C   1 
ATOM   1117 O  O   . TYR   B 1 5   ? 15.304 -27.057 21.702 1.00 16.00  ? 11  TYR   C O   1 
ATOM   1118 C  CB  . TYR   B 1 5   ? 14.097 -25.837 19.347 1.00 14.03  ? 11  TYR   C CB  1 
ATOM   1119 C  CG  . TYR   B 1 5   ? 13.906 -25.070 18.049 1.00 15.26  ? 11  TYR   C CG  1 
ATOM   1120 C  CD1 . TYR   B 1 5   ? 13.077 -23.952 17.991 1.00 15.13  ? 11  TYR   C CD1 1 
ATOM   1121 C  CD2 . TYR   B 1 5   ? 14.627 -25.400 16.909 1.00 15.90  ? 11  TYR   C CD2 1 
ATOM   1122 C  CE1 . TYR   B 1 5   ? 12.950 -23.214 16.828 1.00 16.66  ? 11  TYR   C CE1 1 
ATOM   1123 C  CE2 . TYR   B 1 5   ? 14.504 -24.675 15.736 1.00 17.71  ? 11  TYR   C CE2 1 
ATOM   1124 C  CZ  . TYR   B 1 5   ? 13.652 -23.590 15.696 1.00 17.19  ? 11  TYR   C CZ  1 
ATOM   1125 O  OH  . TYR   B 1 5   ? 13.585 -22.862 14.523 1.00 19.03  ? 11  TYR   C OH  1 
ATOM   1126 N  N   . VAL   B 1 6   ? 15.266 -25.080 22.724 1.00 15.46  ? 12  VAL   C N   1 
ATOM   1127 C  CA  . VAL   B 1 6   ? 15.348 -25.621 24.087 1.00 16.05  ? 12  VAL   C CA  1 
ATOM   1128 C  C   . VAL   B 1 6   ? 14.215 -25.014 24.928 1.00 15.98  ? 12  VAL   C C   1 
ATOM   1129 O  O   . VAL   B 1 6   ? 14.032 -23.795 24.918 1.00 15.06  ? 12  VAL   C O   1 
ATOM   1130 C  CB  . VAL   B 1 6   ? 16.761 -25.334 24.698 1.00 16.88  ? 12  VAL   C CB  1 
ATOM   1131 C  CG1 . VAL   B 1 6   ? 17.134 -23.838 24.643 1.00 16.64  ? 12  VAL   C CG1 1 
ATOM   1132 C  CG2 . VAL   B 1 6   ? 16.809 -25.823 26.130 1.00 18.62  ? 12  VAL   C CG2 1 
ATOM   1133 N  N   . GLY   B 1 7   ? 13.383 -25.847 25.590 1.00 16.87  ? 13  GLY   C N   1 
ATOM   1134 C  CA  . GLY   B 1 7   ? 12.277 -25.311 26.368 1.00 16.51  ? 13  GLY   C CA  1 
ATOM   1135 C  C   . GLY   B 1 7   ? 11.346 -24.478 25.496 1.00 16.82  ? 13  GLY   C C   1 
ATOM   1136 O  O   . GLY   B 1 7   ? 11.078 -24.856 24.345 1.00 18.25  ? 13  GLY   C O   1 
ATOM   1137 N  N   . ASN   B 1 8   ? 11.005 -23.287 25.954 1.00 17.06  ? 14  ASN   C N   1 
ATOM   1138 C  CA  . ASN   B 1 8   ? 10.221 -22.361 25.127 1.00 17.33  ? 14  ASN   C CA  1 
ATOM   1139 C  C   . ASN   B 1 8   ? 11.092 -21.255 24.554 1.00 16.25  ? 14  ASN   C C   1 
ATOM   1140 O  O   . ASN   B 1 8   ? 10.631 -20.125 24.376 1.00 16.41  ? 14  ASN   C O   1 
ATOM   1141 C  CB  . ASN   B 1 8   ? 8.977  -21.787 25.850 1.00 20.55  ? 14  ASN   C CB  1 
ATOM   1142 C  CG  . ASN   B 1 8   ? 7.894  -22.839 25.996 1.00 26.70  ? 14  ASN   C CG  1 
ATOM   1143 O  OD1 . ASN   B 1 8   ? 7.029  -22.995 25.129 1.00 29.20  ? 14  ASN   C OD1 1 
ATOM   1144 N  ND2 . ASN   B 1 8   ? 8.011  -23.640 27.030 1.00 28.69  ? 14  ASN   C ND2 1 
ATOM   1145 N  N   . TYR   B 1 9   ? 12.316 -21.617 24.155 1.00 14.31  ? 15  TYR   C N   1 
ATOM   1146 C  CA  . TYR   B 1 9   ? 13.263 -20.640 23.574 1.00 13.57  ? 15  TYR   C CA  1 
ATOM   1147 C  C   . TYR   B 1 9   ? 13.741 -21.120 22.208 1.00 13.19  ? 15  TYR   C C   1 
ATOM   1148 O  O   . TYR   B 1 9   ? 13.920 -22.327 21.997 1.00 14.55  ? 15  TYR   C O   1 
ATOM   1149 C  CB  . TYR   B 1 9   ? 14.514 -20.501 24.486 1.00 14.58  ? 15  TYR   C CB  1 
ATOM   1150 C  CG  . TYR   B 1 9   ? 14.190 -19.979 25.880 1.00 15.66  ? 15  TYR   C CG  1 
ATOM   1151 C  CD1 . TYR   B 1 9   ? 13.627 -18.717 26.060 1.00 17.91  ? 15  TYR   C CD1 1 
ATOM   1152 C  CD2 . TYR   B 1 9   ? 14.475 -20.738 27.015 1.00 18.22  ? 15  TYR   C CD2 1 
ATOM   1153 C  CE1 . TYR   B 1 9   ? 13.349 -18.233 27.341 1.00 20.93  ? 15  TYR   C CE1 1 
ATOM   1154 C  CE2 . TYR   B 1 9   ? 14.243 -20.237 28.297 1.00 21.69  ? 15  TYR   C CE2 1 
ATOM   1155 C  CZ  . TYR   B 1 9   ? 13.666 -18.993 28.446 1.00 24.38  ? 15  TYR   C CZ  1 
ATOM   1156 O  OH  . TYR   B 1 9   ? 13.401 -18.470 29.698 1.00 29.88  ? 15  TYR   C OH  1 
ATOM   1157 N  N   . ARG   B 1 10  ? 14.001 -20.163 21.297 1.00 12.51  ? 16  ARG   C N   1 
ATOM   1158 C  CA  . ARG   B 1 10  ? 14.629 -20.385 19.993 1.00 12.23  ? 16  ARG   C CA  1 
ATOM   1159 C  C   . ARG   B 1 10  ? 15.884 -19.508 19.981 1.00 12.21  ? 16  ARG   C C   1 
ATOM   1160 O  O   . ARG   B 1 10  ? 15.800 -18.280 20.197 1.00 12.93  ? 16  ARG   C O   1 
ATOM   1161 C  CB  . ARG   B 1 10  ? 13.665 -19.928 18.859 1.00 13.23  ? 16  ARG   C CB  1 
ATOM   1162 C  CG  . ARG   B 1 10  ? 14.288 -19.763 17.468 1.00 14.74  ? 16  ARG   C CG  1 
ATOM   1163 C  CD  . ARG   B 1 10  ? 13.204 -19.473 16.419 1.00 15.14  ? 16  ARG   C CD  1 
ATOM   1164 N  NE  . ARG   B 1 10  ? 13.660 -18.524 15.385 1.00 16.00  ? 16  ARG   C NE  1 
ATOM   1165 C  CZ  . ARG   B 1 10  ? 14.182 -18.827 14.189 1.00 17.09  ? 16  ARG   C CZ  1 
ATOM   1166 N  NH1 . ARG   B 1 10  ? 14.456 -20.100 13.865 1.00 17.11  ? 16  ARG   C NH1 1 
ATOM   1167 N  NH2 . ARG   B 1 10  ? 14.528 -17.859 13.345 1.00 17.59  ? 16  ARG   C NH2 1 
ATOM   1168 N  N   . VAL   B 1 11  ? 17.049 -20.118 19.756 1.00 11.64  ? 17  VAL   C N   1 
ATOM   1169 C  CA  . VAL   B 1 11  ? 18.356 -19.400 19.721 1.00 11.63  ? 17  VAL   C CA  1 
ATOM   1170 C  C   . VAL   B 1 11  ? 18.826 -19.344 18.315 1.00 11.82  ? 17  VAL   C C   1 
ATOM   1171 O  O   . VAL   B 1 11  ? 18.986 -20.416 17.661 1.00 12.39  ? 17  VAL   C O   1 
ATOM   1172 C  CB  . VAL   B 1 11  ? 19.417 -20.110 20.597 1.00 12.81  ? 17  VAL   C CB  1 
ATOM   1173 C  CG1 . VAL   B 1 11  ? 20.673 -19.255 20.675 1.00 14.63  ? 17  VAL   C CG1 1 
ATOM   1174 C  CG2 . VAL   B 1 11  ? 18.879 -20.481 21.990 1.00 14.48  ? 17  VAL   C CG2 1 
ATOM   1175 N  N   . VAL   B 1 12  ? 19.072 -18.132 17.797 1.00 11.23  ? 18  VAL   C N   1 
ATOM   1176 C  CA  A VAL   B 1 12  ? 19.522 -17.940 16.404 0.50 11.61  ? 18  VAL   C CA  1 
ATOM   1177 C  CA  B VAL   B 1 12  ? 19.477 -17.973 16.404 0.50 13.37  ? 18  VAL   C CA  1 
ATOM   1178 C  C   . VAL   B 1 12  ? 20.651 -16.943 16.324 1.00 12.07  ? 18  VAL   C C   1 
ATOM   1179 O  O   . VAL   B 1 12  ? 20.914 -16.192 17.305 1.00 11.98  ? 18  VAL   C O   1 
ATOM   1180 C  CB  A VAL   B 1 12  ? 18.375 -17.417 15.471 0.50 11.09  ? 18  VAL   C CB  1 
ATOM   1181 C  CB  B VAL   B 1 12  ? 18.202 -17.454 15.630 0.50 16.90  ? 18  VAL   C CB  1 
ATOM   1182 C  CG1 A VAL   B 1 12  ? 17.397 -18.548 15.178 0.50 12.48  ? 18  VAL   C CG1 1 
ATOM   1183 C  CG1 B VAL   B 1 12  ? 18.448 -17.314 14.149 0.50 17.42  ? 18  VAL   C CG1 1 
ATOM   1184 C  CG2 A VAL   B 1 12  ? 17.727 -16.115 16.020 0.50 8.25   ? 18  VAL   C CG2 1 
ATOM   1185 C  CG2 B VAL   B 1 12  ? 17.011 -18.382 15.851 0.50 19.72  ? 18  VAL   C CG2 1 
ATOM   1186 N  N   . ASN   B 1 13  ? 21.346 -16.901 15.181 1.00 11.18  ? 19  ASN   C N   1 
ATOM   1187 C  CA  . ASN   B 1 13  ? 22.338 -15.855 14.977 1.00 11.39  ? 19  ASN   C CA  1 
ATOM   1188 C  C   . ASN   B 1 13  ? 21.528 -14.504 14.927 1.00 11.93  ? 19  ASN   C C   1 
ATOM   1189 O  O   . ASN   B 1 13  ? 20.526 -14.420 14.213 1.00 11.88  ? 19  ASN   C O   1 
ATOM   1190 C  CB  . ASN   B 1 13  ? 23.046 -15.999 13.630 1.00 12.27  ? 19  ASN   C CB  1 
ATOM   1191 C  CG  . ASN   B 1 13  ? 23.903 -17.267 13.537 1.00 11.99  ? 19  ASN   C CG  1 
ATOM   1192 O  OD1 . ASN   B 1 13  ? 23.443 -18.335 13.094 1.00 12.99  ? 19  ASN   C OD1 1 
ATOM   1193 N  ND2 . ASN   B 1 13  ? 25.151 -17.152 13.983 1.00 12.57  ? 19  ASN   C ND2 1 
ATOM   1194 N  N   . ARG   B 1 14  ? 22.037 -13.477 15.625 1.00 11.44  ? 20  ARG   C N   1 
ATOM   1195 C  CA  . ARG   B 1 14  ? 21.309 -12.189 15.632 1.00 11.91  ? 20  ARG   C CA  1 
ATOM   1196 C  C   . ARG   B 1 14  ? 21.147 -11.647 14.209 1.00 13.25  ? 20  ARG   C C   1 
ATOM   1197 O  O   . ARG   B 1 14  ? 20.077 -11.109 13.867 1.00 13.51  ? 20  ARG   C O   1 
ATOM   1198 C  CB  . ARG   B 1 14  ? 22.047 -11.192 16.502 1.00 12.09  ? 20  ARG   C CB  1 
ATOM   1199 C  CG  . ARG   B 1 14  ? 21.233 -9.862  16.731 1.00 12.72  ? 20  ARG   C CG  1 
ATOM   1200 C  CD  . ARG   B 1 14  ? 22.108 -8.912  17.529 1.00 13.10  ? 20  ARG   C CD  1 
ATOM   1201 N  NE  . ARG   B 1 14  ? 21.430 -7.648  17.961 1.00 13.34  ? 20  ARG   C NE  1 
ATOM   1202 C  CZ  . ARG   B 1 14  ? 21.318 -6.565  17.207 1.00 13.21  ? 20  ARG   C CZ  1 
ATOM   1203 N  NH1 . ARG   B 1 14  ? 21.712 -6.582  15.940 1.00 14.56  ? 20  ARG   C NH1 1 
ATOM   1204 N  NH2 . ARG   B 1 14  ? 20.827 -5.447  17.716 1.00 13.96  ? 20  ARG   C NH2 1 
ATOM   1205 N  N   . HIS   B 1 15  ? 22.172 -11.852 13.348 1.00 12.55  ? 21  HIS   C N   1 
ATOM   1206 C  CA  . HIS   B 1 15  ? 22.081 -11.321 11.980 1.00 12.83  ? 21  HIS   C CA  1 
ATOM   1207 C  C   . HIS   B 1 15  ? 21.085 -12.048 11.079 1.00 14.11  ? 21  HIS   C C   1 
ATOM   1208 O  O   . HIS   B 1 15  ? 20.773 -11.521 10.015 1.00 16.12  ? 21  HIS   C O   1 
ATOM   1209 C  CB  . HIS   B 1 15  ? 23.476 -11.223 11.314 1.00 14.12  ? 21  HIS   C CB  1 
ATOM   1210 C  CG  . HIS   B 1 15  ? 24.073 -12.537 10.869 1.00 13.09  ? 21  HIS   C CG  1 
ATOM   1211 N  ND1 . HIS   B 1 15  ? 24.783 -13.373 11.758 1.00 13.99  ? 21  HIS   C ND1 1 
ATOM   1212 C  CD2 . HIS   B 1 15  ? 24.083 -13.104 9.641  1.00 14.25  ? 21  HIS   C CD2 1 
ATOM   1213 C  CE1 . HIS   B 1 15  ? 25.192 -14.411 11.007 1.00 14.69  ? 21  HIS   C CE1 1 
ATOM   1214 N  NE2 . HIS   B 1 15  ? 24.786 -14.286 9.743  1.00 14.02  ? 21  HIS   C NE2 1 
ATOM   1215 N  N   . LEU   B 1 16  ? 20.545 -13.184 11.517 1.00 12.42  ? 22  LEU   C N   1 
ATOM   1216 C  CA  . LEU   B 1 16  ? 19.527 -13.961 10.780 1.00 13.64  ? 22  LEU   C CA  1 
ATOM   1217 C  C   . LEU   B 1 16  ? 18.149 -13.900 11.451 1.00 14.37  ? 22  LEU   C C   1 
ATOM   1218 O  O   . LEU   B 1 16  ? 17.216 -14.610 11.025 1.00 15.10  ? 22  LEU   C O   1 
ATOM   1219 C  CB  . LEU   B 1 16  ? 19.989 -15.404 10.573 1.00 13.39  ? 22  LEU   C CB  1 
ATOM   1220 C  CG  . LEU   B 1 16  ? 21.286 -15.555 9.778  1.00 13.88  ? 22  LEU   C CG  1 
ATOM   1221 C  CD1 . LEU   B 1 16  ? 21.741 -17.016 9.712  1.00 14.73  ? 22  LEU   C CD1 1 
ATOM   1222 C  CD2 . LEU   B 1 16  ? 21.180 -14.955 8.370  1.00 14.56  ? 22  LEU   C CD2 1 
ATOM   1223 N  N   . ALA   B 1 17  ? 18.009 -13.128 12.569 1.00 14.64  ? 23  ALA   C N   1 
ATOM   1224 C  CA  . ALA   B 1 17  ? 16.721 -13.058 13.271 1.00 14.12  ? 23  ALA   C CA  1 
ATOM   1225 C  C   . ALA   B 1 17  ? 15.608 -12.505 12.375 1.00 14.94  ? 23  ALA   C C   1 
ATOM   1226 O  O   . ALA   B 1 17  ? 15.849 -11.576 11.580 1.00 15.77  ? 23  ALA   C O   1 
ATOM   1227 C  CB  . ALA   B 1 17  ? 16.866 -12.201 14.539 1.00 15.25  ? 23  ALA   C CB  1 
ATOM   1228 N  N   . THR   B 1 18  ? 14.417 -13.072 12.534 1.00 14.94  ? 24  THR   C N   1 
ATOM   1229 C  CA  . THR   B 1 18  ? 13.263 -12.663 11.756 1.00 15.29  ? 24  THR   C CA  1 
ATOM   1230 C  C   . THR   B 1 18  ? 12.444 -11.595 12.525 1.00 15.23  ? 24  THR   C C   1 
ATOM   1231 O  O   . THR   B 1 18  ? 12.678 -11.296 13.697 1.00 15.87  ? 24  THR   C O   1 
ATOM   1232 C  CB  . THR   B 1 18  ? 12.338 -13.889 11.480 1.00 16.70  ? 24  THR   C CB  1 
ATOM   1233 O  OG1 . THR   B 1 18  ? 11.816 -14.306 12.712 1.00 17.09  ? 24  THR   C OG1 1 
ATOM   1234 C  CG2 . THR   B 1 18  ? 13.081 -15.081 10.776 1.00 18.00  ? 24  THR   C CG2 1 
ATOM   1235 N  N   . HIS   B 1 19  ? 11.422 -10.996 11.828 1.00 16.45  ? 25  HIS   C N   1 
ATOM   1236 C  CA  . HIS   B 1 19  ? 10.504 -10.072 12.507 1.00 17.47  ? 25  HIS   C CA  1 
ATOM   1237 C  C   . HIS   B 1 19  ? 9.807  -10.830 13.638 1.00 15.90  ? 25  HIS   C C   1 
ATOM   1238 O  O   . HIS   B 1 19  ? 9.708  -10.260 14.721 1.00 17.05  ? 25  HIS   C O   1 
ATOM   1239 C  CB  . HIS   B 1 19  ? 9.395  -9.577  11.528 1.00 18.75  ? 25  HIS   C CB  1 
ATOM   1240 C  CG  . HIS   B 1 19  ? 8.240  -8.885  12.227 1.00 19.55  ? 25  HIS   C CG  1 
ATOM   1241 N  ND1 . HIS   B 1 19  ? 8.375  -7.617  12.776 1.00 22.59  ? 25  HIS   C ND1 1 
ATOM   1242 C  CD2 . HIS   B 1 19  ? 7.032  -9.377  12.576 1.00 21.19  ? 25  HIS   C CD2 1 
ATOM   1243 C  CE1 . HIS   B 1 19  ? 7.190  -7.320  13.306 1.00 22.21  ? 25  HIS   C CE1 1 
ATOM   1244 N  NE2 . HIS   B 1 19  ? 6.355  -8.368  13.250 1.00 21.71  ? 25  HIS   C NE2 1 
ATOM   1245 N  N   . ASN   B 1 20  ? 9.394  -12.095 13.429 1.00 16.51  ? 26  ASN   C N   1 
ATOM   1246 C  CA  . ASN   B 1 20  ? 8.755  -12.822 14.522 1.00 17.38  ? 26  ASN   C CA  1 
ATOM   1247 C  C   . ASN   B 1 20  ? 9.671  -12.989 15.726 1.00 16.04  ? 26  ASN   C C   1 
ATOM   1248 O  O   . ASN   B 1 20  ? 9.250  -12.903 16.874 1.00 15.39  ? 26  ASN   C O   1 
ATOM   1249 C  CB  . ASN   B 1 20  ? 8.224  -14.201 14.070 1.00 19.32  ? 26  ASN   C CB  1 
ATOM   1250 C  CG  . ASN   B 1 20  ? 7.420  -14.890 15.175 1.00 26.51  ? 26  ASN   C CG  1 
ATOM   1251 O  OD1 . ASN   B 1 20  ? 6.301  -14.450 15.492 1.00 29.25  ? 26  ASN   C OD1 1 
ATOM   1252 N  ND2 . ASN   B 1 20  ? 7.991  -15.930 15.830 1.00 27.37  ? 26  ASN   C ND2 1 
ATOM   1253 N  N   . ASP   B 1 21  ? 11.000 -13.199 15.469 1.00 14.66  ? 27  ASP   C N   1 
ATOM   1254 C  CA  . ASP   B 1 21  ? 11.934 -13.285 16.571 1.00 14.41  ? 27  ASP   C CA  1 
ATOM   1255 C  C   . ASP   B 1 21  ? 11.984 -11.981 17.387 1.00 14.18  ? 27  ASP   C C   1 
ATOM   1256 O  O   . ASP   B 1 21  ? 11.909 -11.995 18.611 1.00 15.34  ? 27  ASP   C O   1 
ATOM   1257 C  CB  . ASP   B 1 21  ? 13.340 -13.611 16.068 1.00 13.94  ? 27  ASP   C CB  1 
ATOM   1258 C  CG  . ASP   B 1 21  ? 13.541 -15.026 15.571 1.00 14.97  ? 27  ASP   C CG  1 
ATOM   1259 O  OD1 . ASP   B 1 21  ? 12.964 -15.954 16.182 1.00 17.03  ? 27  ASP   C OD1 1 
ATOM   1260 O  OD2 . ASP   B 1 21  ? 14.262 -15.195 14.550 1.00 15.37  ? 27  ASP   C OD2 1 
ATOM   1261 N  N   . TRP   B 1 22  ? 12.087 -10.833 16.682 1.00 14.29  ? 28  TRP   C N   1 
ATOM   1262 C  CA  . TRP   B 1 22  ? 12.131 -9.548  17.354 1.00 14.87  ? 28  TRP   C CA  1 
ATOM   1263 C  C   . TRP   B 1 22  ? 10.792 -9.213  18.063 1.00 14.63  ? 28  TRP   C C   1 
ATOM   1264 O  O   . TRP   B 1 22  ? 10.810 -8.593  19.133 1.00 15.20  ? 28  TRP   C O   1 
ATOM   1265 C  CB  . TRP   B 1 22  ? 12.501 -8.446  16.381 1.00 15.02  ? 28  TRP   C CB  1 
ATOM   1266 C  CG  . TRP   B 1 22  ? 13.987 -8.399  16.100 1.00 14.90  ? 28  TRP   C CG  1 
ATOM   1267 C  CD1 . TRP   B 1 22  ? 14.649 -8.891  15.013 1.00 15.36  ? 28  TRP   C CD1 1 
ATOM   1268 C  CD2 . TRP   B 1 22  ? 14.994 -7.828  16.959 1.00 13.23  ? 28  TRP   C CD2 1 
ATOM   1269 N  NE1 . TRP   B 1 22  ? 16.007 -8.613  15.117 1.00 15.10  ? 28  TRP   C NE1 1 
ATOM   1270 C  CE2 . TRP   B 1 22  ? 16.233 -7.944  16.295 1.00 14.33  ? 28  TRP   C CE2 1 
ATOM   1271 C  CE3 . TRP   B 1 22  ? 14.944 -7.125  18.172 1.00 15.99  ? 28  TRP   C CE3 1 
ATOM   1272 C  CZ2 . TRP   B 1 22  ? 17.399 -7.401  16.798 1.00 14.79  ? 28  TRP   C CZ2 1 
ATOM   1273 C  CZ3 . TRP   B 1 22  ? 16.120 -6.602  18.677 1.00 16.83  ? 28  TRP   C CZ3 1 
ATOM   1274 C  CH2 . TRP   B 1 22  ? 17.326 -6.746  17.988 1.00 16.43  ? 28  TRP   C CH2 1 
ATOM   1275 N  N   . ALA   B 1 23  ? 9.671  -9.689  17.518 1.00 14.50  ? 29  ALA   C N   1 
ATOM   1276 C  CA  . ALA   B 1 23  ? 8.344  -9.453  18.119 1.00 15.39  ? 29  ALA   C CA  1 
ATOM   1277 C  C   . ALA   B 1 23  ? 8.086  -10.349 19.339 1.00 17.19  ? 29  ALA   C C   1 
ATOM   1278 O  O   . ALA   B 1 23  ? 7.112  -10.146 20.058 1.00 18.55  ? 29  ALA   C O   1 
ATOM   1279 C  CB  . ALA   B 1 23  ? 7.253  -9.706  17.081 1.00 16.45  ? 29  ALA   C CB  1 
ATOM   1280 N  N   . ASN   B 1 24  ? 8.945  -11.380 19.569 1.00 16.98  ? 30  ASN   C N   1 
ATOM   1281 C  CA  . ASN   B 1 24  ? 8.842  -12.293 20.709 1.00 15.94  ? 30  ASN   C CA  1 
ATOM   1282 C  C   . ASN   B 1 24  ? 10.232 -12.360 21.365 1.00 15.86  ? 30  ASN   C C   1 
ATOM   1283 O  O   . ASN   B 1 24  ? 10.644 -13.429 21.800 1.00 15.40  ? 30  ASN   C O   1 
ATOM   1284 C  CB  . ASN   B 1 24  ? 8.380  -13.672 20.206 1.00 17.60  ? 30  ASN   C CB  1 
ATOM   1285 C  CG  . ASN   B 1 24  ? 6.966  -13.622 19.698 1.00 18.50  ? 30  ASN   C CG  1 
ATOM   1286 O  OD1 . ASN   B 1 24  ? 5.997  -13.641 20.504 1.00 21.05  ? 30  ASN   C OD1 1 
ATOM   1287 N  ND2 . ASN   B 1 24  ? 6.801  -13.493 18.387 1.00 19.06  ? 30  ASN   C ND2 1 
ATOM   1288 N  N   . LEU   B 1 25  ? 10.914 -11.236 21.497 1.00 16.29  ? 31  LEU   C N   1 
ATOM   1289 C  CA  . LEU   B 1 25  ? 12.293 -11.219 21.986 1.00 15.38  ? 31  LEU   C CA  1 
ATOM   1290 C  C   . LEU   B 1 25  ? 12.428 -11.543 23.459 1.00 16.72  ? 31  LEU   C C   1 
ATOM   1291 O  O   . LEU   B 1 25  ? 11.670 -11.025 24.291 1.00 17.60  ? 31  LEU   C O   1 
ATOM   1292 C  CB  . LEU   B 1 25  ? 12.851 -9.815  21.728 1.00 15.95  ? 31  LEU   C CB  1 
ATOM   1293 C  CG  . LEU   B 1 25  ? 14.317 -9.643  22.095 1.00 16.69  ? 31  LEU   C CG  1 
ATOM   1294 C  CD1 . LEU   B 1 25  ? 15.223 -10.509 21.182 1.00 16.76  ? 31  LEU   C CD1 1 
ATOM   1295 C  CD2 . LEU   B 1 25  ? 14.736 -8.200  21.966 1.00 18.00  ? 31  LEU   C CD2 1 
ATOM   1296 N  N   . VAL   B 1 26  ? 13.415 -12.368 23.796 1.00 15.35  ? 32  VAL   C N   1 
ATOM   1297 C  CA  . VAL   B 1 26  ? 13.757 -12.627 25.190 1.00 16.39  ? 32  VAL   C CA  1 
ATOM   1298 C  C   . VAL   B 1 26  ? 15.095 -11.923 25.530 1.00 16.43  ? 32  VAL   C C   1 
ATOM   1299 O  O   . VAL   B 1 26  ? 15.208 -11.246 26.565 1.00 18.24  ? 32  VAL   C O   1 
ATOM   1300 C  CB  . VAL   B 1 26  ? 13.894 -14.144 25.427 1.00 16.53  ? 32  VAL   C CB  1 
ATOM   1301 C  CG1 . VAL   B 1 26  ? 14.458 -14.436 26.832 1.00 18.20  ? 32  VAL   C CG1 1 
ATOM   1302 C  CG2 . VAL   B 1 26  ? 12.550 -14.861 25.223 1.00 16.59  ? 32  VAL   C CG2 1 
ATOM   1303 N  N   . TRP   B 1 27  ? 16.124 -12.057 24.666 1.00 14.98  ? 33  TRP   C N   1 
ATOM   1304 C  CA  . TRP   B 1 27  ? 17.445 -11.495 24.936 1.00 14.92  ? 33  TRP   C CA  1 
ATOM   1305 C  C   . TRP   B 1 27  ? 18.230 -11.431 23.619 1.00 15.01  ? 33  TRP   C C   1 
ATOM   1306 O  O   . TRP   B 1 27  ? 18.039 -12.296 22.740 1.00 15.15  ? 33  TRP   C O   1 
ATOM   1307 C  CB  . TRP   B 1 27  ? 18.182 -12.374 25.973 1.00 15.94  ? 33  TRP   C CB  1 
ATOM   1308 C  CG  . TRP   B 1 27  ? 19.647 -12.096 26.154 1.00 16.69  ? 33  TRP   C CG  1 
ATOM   1309 C  CD1 . TRP   B 1 27  ? 20.224 -11.146 26.954 1.00 18.97  ? 33  TRP   C CD1 1 
ATOM   1310 C  CD2 . TRP   B 1 27  ? 20.731 -12.788 25.511 1.00 15.46  ? 33  TRP   C CD2 1 
ATOM   1311 N  NE1 . TRP   B 1 27  ? 21.613 -11.241 26.887 1.00 19.44  ? 33  TRP   C NE1 1 
ATOM   1312 C  CE2 . TRP   B 1 27  ? 21.942 -12.252 26.017 1.00 16.86  ? 33  TRP   C CE2 1 
ATOM   1313 C  CE3 . TRP   B 1 27  ? 20.797 -13.826 24.565 1.00 15.31  ? 33  TRP   C CE3 1 
ATOM   1314 C  CZ2 . TRP   B 1 27  ? 23.200 -12.738 25.629 1.00 16.26  ? 33  TRP   C CZ2 1 
ATOM   1315 C  CZ3 . TRP   B 1 27  ? 22.047 -14.328 24.227 1.00 16.72  ? 33  TRP   C CZ3 1 
ATOM   1316 C  CH2 . TRP   B 1 27  ? 23.217 -13.741 24.697 1.00 16.66  ? 33  TRP   C CH2 1 
ATOM   1317 N  N   . GLU   B 1 28  ? 19.080 -10.431 23.465 1.00 14.69  ? 34  GLU   C N   1 
ATOM   1318 C  CA  . GLU   B 1 28  ? 19.937 -10.337 22.299 1.00 16.13  ? 34  GLU   C CA  1 
ATOM   1319 C  C   . GLU   B 1 28  ? 21.223 -9.660  22.647 1.00 15.93  ? 34  GLU   C C   1 
ATOM   1320 O  O   . GLU   B 1 28  ? 21.240 -8.769  23.530 1.00 15.82  ? 34  GLU   C O   1 
ATOM   1321 C  CB  . GLU   B 1 28  ? 19.247 -9.658  21.104 1.00 16.51  ? 34  GLU   C CB  1 
ATOM   1322 C  CG  . GLU   B 1 28  ? 18.693 -8.266  21.371 1.00 17.04  ? 34  GLU   C CG  1 
ATOM   1323 C  CD  . GLU   B 1 28  ? 19.663 -7.102  21.289 1.00 19.11  ? 34  GLU   C CD  1 
ATOM   1324 O  OE1 . GLU   B 1 28  ? 19.394 -6.073  21.962 1.00 22.14  ? 34  GLU   C OE1 1 
ATOM   1325 O  OE2 . GLU   B 1 28  ? 20.691 -7.191  20.570 1.00 17.96  ? 34  GLU   C OE2 1 
ATOM   1326 N  N   . ASP   B 1 29  ? 22.309 -10.014 21.931 1.00 14.34  ? 35  ASP   C N   1 
ATOM   1327 C  CA  . ASP   B 1 29  ? 23.608 -9.381  22.157 1.00 14.64  ? 35  ASP   C CA  1 
ATOM   1328 C  C   . ASP   B 1 29  ? 24.382 -9.331  20.827 1.00 14.29  ? 35  ASP   C C   1 
ATOM   1329 O  O   . ASP   B 1 29  ? 24.815 -10.378 20.329 1.00 13.76  ? 35  ASP   C O   1 
ATOM   1330 C  CB  . ASP   B 1 29  ? 24.340 -10.182 23.251 1.00 15.42  ? 35  ASP   C CB  1 
ATOM   1331 C  CG  . ASP   B 1 29  ? 25.679 -9.600  23.647 1.00 18.68  ? 35  ASP   C CG  1 
ATOM   1332 O  OD1 . ASP   B 1 29  ? 26.409 -9.116  22.757 1.00 20.09  ? 35  ASP   C OD1 1 
ATOM   1333 O  OD2 . ASP   B 1 29  ? 26.061 -9.726  24.833 1.00 22.99  ? 35  ASP   C OD2 1 
ATOM   1334 N  N   . SER   B 1 30  ? 24.526 -8.134  20.245 1.00 14.34  ? 36  SER   C N   1 
ATOM   1335 C  CA  A SER   B 1 30  ? 25.230 -7.953  18.986 0.50 14.34  ? 36  SER   C CA  1 
ATOM   1336 C  CA  B SER   B 1 30  ? 25.209 -8.024  18.970 0.50 14.79  ? 36  SER   C CA  1 
ATOM   1337 C  C   . SER   B 1 30  ? 26.694 -8.398  19.086 1.00 14.55  ? 36  SER   C C   1 
ATOM   1338 O  O   . SER   B 1 30  ? 27.212 -9.014  18.135 1.00 14.19  ? 36  SER   C O   1 
ATOM   1339 C  CB  A SER   B 1 30  ? 25.181 -6.490  18.549 0.50 14.93  ? 36  SER   C CB  1 
ATOM   1340 C  CB  B SER   B 1 30  ? 25.036 -6.639  18.372 0.50 16.99  ? 36  SER   C CB  1 
ATOM   1341 O  OG  A SER   B 1 30  ? 26.092 -6.216  17.491 0.50 15.22  ? 36  SER   C OG  1 
ATOM   1342 O  OG  B SER   B 1 30  ? 25.559 -5.696  19.285 0.50 18.46  ? 36  SER   C OG  1 
ATOM   1343 N  N   . SER   B 1 31  ? 27.354 -8.134  20.236 1.00 14.50  ? 37  SER   C N   1 
ATOM   1344 C  CA  . SER   B 1 31  ? 28.772 -8.522  20.347 1.00 15.56  ? 37  SER   C CA  1 
ATOM   1345 C  C   . SER   B 1 31  ? 28.955 -10.038 20.301 1.00 14.41  ? 37  SER   C C   1 
ATOM   1346 O  O   . SER   B 1 31  ? 30.053 -10.480 19.937 1.00 15.22  ? 37  SER   C O   1 
ATOM   1347 C  CB  . SER   B 1 31  ? 29.414 -7.981  21.610 1.00 19.03  ? 37  SER   C CB  1 
ATOM   1348 O  OG  . SER   B 1 31  ? 28.993 -8.678  22.762 1.00 24.34  ? 37  SER   C OG  1 
ATOM   1349 N  N   . ARG   B 1 32  ? 27.905 -10.825 20.626 1.00 13.49  ? 38  ARG   C N   1 
ATOM   1350 C  CA  . ARG   B 1 32  ? 27.990 -12.293 20.568 1.00 13.30  ? 38  ARG   C CA  1 
ATOM   1351 C  C   . ARG   B 1 32  ? 27.350 -12.866 19.293 1.00 13.06  ? 38  ARG   C C   1 
ATOM   1352 O  O   . ARG   B 1 32  ? 27.400 -14.078 19.072 1.00 12.24  ? 38  ARG   C O   1 
ATOM   1353 C  CB  . ARG   B 1 32  ? 27.260 -12.901 21.786 1.00 15.29  ? 38  ARG   C CB  1 
ATOM   1354 C  CG  . ARG   B 1 32  ? 27.909 -12.515 23.128 1.00 15.75  ? 38  ARG   C CG  1 
ATOM   1355 C  CD  . ARG   B 1 32  ? 27.170 -13.113 24.316 1.00 14.84  ? 38  ARG   C CD  1 
ATOM   1356 N  NE  . ARG   B 1 32  ? 27.224 -14.597 24.350 1.00 13.67  ? 38  ARG   C NE  1 
ATOM   1357 C  CZ  . ARG   B 1 32  ? 27.177 -15.334 25.463 1.00 13.27  ? 38  ARG   C CZ  1 
ATOM   1358 N  NH1 . ARG   B 1 32  ? 27.075 -14.755 26.648 1.00 14.81  ? 38  ARG   C NH1 1 
ATOM   1359 N  NH2 . ARG   B 1 32  ? 27.324 -16.656 25.398 1.00 14.58  ? 38  ARG   C NH2 1 
ATOM   1360 N  N   . ASP   B 1 33  ? 26.695 -12.034 18.465 1.00 11.80  ? 39  ASP   C N   1 
ATOM   1361 C  CA  . ASP   B 1 33  ? 25.895 -12.487 17.336 1.00 11.61  ? 39  ASP   C CA  1 
ATOM   1362 C  C   . ASP   B 1 33  ? 24.808 -13.474 17.785 1.00 11.70  ? 39  ASP   C C   1 
ATOM   1363 O  O   . ASP   B 1 33  ? 24.499 -14.399 17.007 1.00 11.85  ? 39  ASP   C O   1 
ATOM   1364 C  CB  . ASP   B 1 33  ? 26.749 -13.109 16.225 1.00 11.95  ? 39  ASP   C CB  1 
ATOM   1365 C  CG  . ASP   B 1 33  ? 25.964 -13.431 14.950 1.00 13.01  ? 39  ASP   C CG  1 
ATOM   1366 O  OD1 . ASP   B 1 33  ? 25.058 -12.630 14.569 1.00 13.70  ? 39  ASP   C OD1 1 
ATOM   1367 O  OD2 . ASP   B 1 33  ? 26.287 -14.444 14.288 1.00 12.61  ? 39  ASP   C OD2 1 
ATOM   1368 N  N   . LEU   B 1 34  ? 24.135 -13.230 18.932 1.00 11.05  ? 40  LEU   C N   1 
ATOM   1369 C  CA  . LEU   B 1 34  ? 23.051 -14.133 19.362 1.00 11.22  ? 40  LEU   C CA  1 
ATOM   1370 C  C   . LEU   B 1 34  ? 21.747 -13.379 19.628 1.00 12.14  ? 40  LEU   C C   1 
ATOM   1371 O  O   . LEU   B 1 34  ? 21.764 -12.217 20.086 1.00 12.57  ? 40  LEU   C O   1 
ATOM   1372 C  CB  . LEU   B 1 34  ? 23.447 -14.837 20.675 1.00 12.29  ? 40  LEU   C CB  1 
ATOM   1373 C  CG  . LEU   B 1 34  ? 24.523 -15.950 20.558 1.00 12.46  ? 40  LEU   C CG  1 
ATOM   1374 C  CD1 . LEU   B 1 34  ? 24.787 -16.556 21.975 1.00 13.85  ? 40  LEU   C CD1 1 
ATOM   1375 C  CD2 . LEU   B 1 34  ? 24.089 -17.063 19.607 1.00 13.48  ? 40  LEU   C CD2 1 
ATOM   1376 N  N   . LEU   B 1 35  ? 20.640 -14.064 19.400 1.00 11.27  ? 41  LEU   C N   1 
ATOM   1377 C  CA  . LEU   B 1 35  ? 19.333 -13.539 19.759 1.00 11.58  ? 41  LEU   C CA  1 
ATOM   1378 C  C   . LEU   B 1 35  ? 18.494 -14.766 20.147 1.00 12.12  ? 41  LEU   C C   1 
ATOM   1379 O  O   . LEU   B 1 35  ? 18.596 -15.840 19.524 1.00 12.77  ? 41  LEU   C O   1 
ATOM   1380 C  CB  . LEU   B 1 35  ? 18.687 -12.807 18.549 1.00 12.15  ? 41  LEU   C CB  1 
ATOM   1381 C  CG  . LEU   B 1 35  ? 17.286 -12.218 18.806 1.00 12.54  ? 41  LEU   C CG  1 
ATOM   1382 C  CD1 . LEU   B 1 35  ? 17.116 -10.908 18.028 1.00 14.94  ? 41  LEU   C CD1 1 
ATOM   1383 C  CD2 . LEU   B 1 35  ? 16.197 -13.247 18.419 1.00 13.86  ? 41  LEU   C CD2 1 
ATOM   1384 N  N   . VAL   B 1 36  ? 17.694 -14.607 21.207 1.00 12.35  ? 42  VAL   C N   1 
ATOM   1385 C  CA  . VAL   B 1 36  ? 16.786 -15.628 21.721 1.00 12.44  ? 42  VAL   C CA  1 
ATOM   1386 C  C   . VAL   B 1 36  ? 15.358 -15.087 21.708 1.00 12.36  ? 42  VAL   C C   1 
ATOM   1387 O  O   . VAL   B 1 36  ? 15.143 -13.955 22.211 1.00 13.71  ? 42  VAL   C O   1 
ATOM   1388 C  CB  . VAL   B 1 36  ? 17.200 -16.068 23.140 1.00 13.40  ? 42  VAL   C CB  1 
ATOM   1389 C  CG1 . VAL   B 1 36  ? 16.224 -17.112 23.686 1.00 14.99  ? 42  VAL   C CG1 1 
ATOM   1390 C  CG2 . VAL   B 1 36  ? 18.650 -16.627 23.145 1.00 13.92  ? 42  VAL   C CG2 1 
ATOM   1391 N  N   . SER   B 1 37  ? 14.434 -15.842 21.139 1.00 12.66  ? 43  SER   C N   1 
ATOM   1392 C  CA  . SER   B 1 37  ? 13.014 -15.491 21.111 1.00 12.85  ? 43  SER   C CA  1 
ATOM   1393 C  C   . SER   B 1 37  ? 12.214 -16.595 21.799 1.00 14.00  ? 43  SER   C C   1 
ATOM   1394 O  O   . SER   B 1 37  ? 12.709 -17.700 22.063 1.00 14.43  ? 43  SER   C O   1 
ATOM   1395 C  CB  . SER   B 1 37  ? 12.533 -15.282 19.679 1.00 13.39  ? 43  SER   C CB  1 
ATOM   1396 O  OG  . SER   B 1 37  ? 12.707 -16.446 18.887 1.00 15.50  ? 43  SER   C OG  1 
ATOM   1397 N  N   . SER   B 1 38  ? 10.986 -16.266 22.198 1.00 14.76  ? 44  SER   C N   1 
ATOM   1398 C  CA  . SER   B 1 38  ? 10.094 -17.236 22.859 1.00 15.98  ? 44  SER   C CA  1 
ATOM   1399 C  C   . SER   B 1 38  ? 9.287  -18.025 21.829 1.00 17.95  ? 44  SER   C C   1 
ATOM   1400 O  O   . SER   B 1 38  ? 8.974  -17.522 20.741 1.00 19.38  ? 44  SER   C O   1 
ATOM   1401 C  CB  . SER   B 1 38  ? 9.188  -16.512 23.854 1.00 18.63  ? 44  SER   C CB  1 
ATOM   1402 O  OG  . SER   B 1 38  ? 8.351  -15.608 23.151 1.00 23.03  ? 44  SER   C OG  1 
ATOM   1403 N  N   . THR   B 1 39  ? 8.934  -19.282 22.165 1.00 17.71  ? 45  THR   C N   1 
ATOM   1404 C  CA  . THR   B 1 39  ? 8.191  -20.164 21.257 1.00 18.69  ? 45  THR   C CA  1 
ATOM   1405 C  C   . THR   B 1 39  ? 6.901  -20.617 21.958 1.00 21.52  ? 45  THR   C C   1 
ATOM   1406 O  O   . THR   B 1 39  ? 6.845  -20.699 23.180 1.00 21.37  ? 45  THR   C O   1 
ATOM   1407 C  CB  . THR   B 1 39  ? 9.050  -21.422 20.898 1.00 19.28  ? 45  THR   C CB  1 
ATOM   1408 O  OG1 . THR   B 1 39  ? 9.288  -22.182 22.082 1.00 20.76  ? 45  THR   C OG1 1 
ATOM   1409 C  CG2 . THR   B 1 39  ? 10.409 -21.068 20.262 1.00 19.79  ? 45  THR   C CG2 1 
ATOM   1410 N  N   . THR   B 1 40  ? 5.908  -20.980 21.159 1.00 23.69  ? 46  THR   C N   1 
ATOM   1411 C  CA  . THR   B 1 40  ? 4.662  -21.524 21.718 1.00 25.66  ? 46  THR   C CA  1 
ATOM   1412 C  C   . THR   B 1 40  ? 4.882  -22.998 22.069 1.00 25.93  ? 46  THR   C C   1 
ATOM   1413 O  O   . THR   B 1 40  ? 4.482  -23.454 23.156 1.00 28.56  ? 46  THR   C O   1 
ATOM   1414 C  CB  . THR   B 1 40  ? 3.499  -21.282 20.745 1.00 30.86  ? 46  THR   C CB  1 
ATOM   1415 O  OG1 . THR   B 1 40  ? 3.808  -21.916 19.503 1.00 35.23  ? 46  THR   C OG1 1 
ATOM   1416 C  CG2 . THR   B 1 40  ? 3.291  -19.817 20.478 1.00 30.55  ? 46  THR   C CG2 1 
ATOM   1417 N  N   . ALA   B 1 41  ? 5.544  -23.750 21.167 1.00 23.98  ? 47  ALA   C N   1 
ATOM   1418 C  CA  . ALA   B 1 41  ? 5.796  -25.172 21.377 1.00 24.73  ? 47  ALA   C CA  1 
ATOM   1419 C  C   . ALA   B 1 41  ? 7.114  -25.427 22.115 1.00 22.49  ? 47  ALA   C C   1 
ATOM   1420 O  O   . ALA   B 1 41  ? 8.055  -24.670 21.939 1.00 21.75  ? 47  ALA   C O   1 
ATOM   1421 C  CB  . ALA   B 1 41  ? 5.846  -25.867 20.024 1.00 26.17  ? 47  ALA   C CB  1 
ATOM   1422 N  N   . GLN   B 1 42  ? 7.210  -26.489 22.902 1.00 22.47  ? 48  GLN   C N   1 
ATOM   1423 C  CA  . GLN   B 1 42  ? 8.443  -26.850 23.591 1.00 23.11  ? 48  GLN   C CA  1 
ATOM   1424 C  C   . GLN   B 1 42  ? 9.408  -27.502 22.620 1.00 22.44  ? 48  GLN   C C   1 
ATOM   1425 O  O   . GLN   B 1 42  ? 9.014  -28.282 21.740 1.00 24.10  ? 48  GLN   C O   1 
ATOM   1426 C  CB  . GLN   B 1 42  ? 8.165  -27.780 24.781 1.00 28.10  ? 48  GLN   C CB  1 
ATOM   1427 C  CG  . GLN   B 1 42  ? 7.552  -27.027 25.952 1.00 37.27  ? 48  GLN   C CG  1 
ATOM   1428 C  CD  . GLN   B 1 42  ? 7.495  -27.955 27.129 1.00 47.83  ? 48  GLN   C CD  1 
ATOM   1429 O  OE1 . GLN   B 1 42  ? 6.713  -28.910 27.160 1.00 51.75  ? 48  GLN   C OE1 1 
ATOM   1430 N  NE2 . GLN   B 1 42  ? 8.349  -27.725 28.110 1.00 50.61  ? 48  GLN   C NE2 1 
ATOM   1431 N  N   . GLY   B 1 43  ? 10.672 -27.166 22.806 1.00 19.52  ? 49  GLY   C N   1 
ATOM   1432 C  CA  . GLY   B 1 43  ? 11.787 -27.690 22.025 1.00 19.69  ? 49  GLY   C CA  1 
ATOM   1433 C  C   . GLY   B 1 43  ? 12.446 -28.818 22.780 1.00 19.00  ? 49  GLY   C C   1 
ATOM   1434 O  O   . GLY   B 1 43  ? 12.224 -28.987 23.985 1.00 21.12  ? 49  GLY   C O   1 
ATOM   1435 N  N   . CYS   B 1 44  ? 13.279 -29.572 22.073 1.00 17.79  ? 50  CYS   C N   1 
ATOM   1436 C  CA  . CYS   B 1 44  ? 13.869 -30.781 22.617 1.00 18.90  ? 50  CYS   C CA  1 
ATOM   1437 C  C   . CYS   B 1 44  ? 15.372 -30.817 22.670 1.00 18.50  ? 50  CYS   C C   1 
ATOM   1438 O  O   . CYS   B 1 44  ? 15.926 -31.875 23.048 1.00 21.55  ? 50  CYS   C O   1 
ATOM   1439 C  CB  . CYS   B 1 44  ? 13.338 -31.985 21.841 1.00 19.18  ? 50  CYS   C CB  1 
ATOM   1440 S  SG  . CYS   B 1 44  ? 11.530 -32.139 21.906 1.00 26.52  ? 50  CYS   C SG  1 
ATOM   1441 N  N   . ASP   B 1 45  ? 16.065 -29.768 22.247 1.00 15.49  ? 51  ASP   C N   1 
ATOM   1442 C  CA  . ASP   B 1 45  ? 17.529 -29.774 22.275 1.00 15.33  ? 51  ASP   C CA  1 
ATOM   1443 C  C   . ASP   B 1 45  ? 17.955 -29.581 23.744 1.00 16.11  ? 51  ASP   C C   1 
ATOM   1444 O  O   . ASP   B 1 45  ? 17.250 -28.902 24.538 1.00 18.68  ? 51  ASP   C O   1 
ATOM   1445 C  CB  . ASP   B 1 45  ? 18.091 -28.609 21.425 1.00 15.65  ? 51  ASP   C CB  1 
ATOM   1446 C  CG  . ASP   B 1 45  ? 17.895 -28.771 19.935 1.00 19.28  ? 51  ASP   C CG  1 
ATOM   1447 O  OD1 . ASP   B 1 45  ? 17.867 -29.916 19.457 1.00 20.45  ? 51  ASP   C OD1 1 
ATOM   1448 O  OD2 . ASP   B 1 45  ? 17.776 -27.735 19.221 1.00 17.65  ? 51  ASP   C OD2 1 
ATOM   1449 N  N   . THR   B 1 46  ? 19.070 -30.191 24.096 1.00 14.86  ? 52  THR   C N   1 
ATOM   1450 C  CA  . THR   B 1 46  ? 19.662 -30.017 25.423 1.00 14.91  ? 52  THR   C CA  1 
ATOM   1451 C  C   . THR   B 1 46  ? 20.931 -29.185 25.258 1.00 13.88  ? 52  THR   C C   1 
ATOM   1452 O  O   . THR   B 1 46  ? 21.757 -29.494 24.359 1.00 14.59  ? 52  THR   C O   1 
ATOM   1453 C  CB  . THR   B 1 46  ? 20.044 -31.383 26.002 1.00 17.23  ? 52  THR   C CB  1 
ATOM   1454 O  OG1 . THR   B 1 46  ? 18.838 -32.169 26.174 1.00 19.60  ? 52  THR   C OG1 1 
ATOM   1455 C  CG2 . THR   B 1 46  ? 20.768 -31.250 27.362 1.00 19.40  ? 52  THR   C CG2 1 
ATOM   1456 N  N   . ILE   B 1 47  ? 21.104 -28.134 26.092 1.00 14.08  ? 53  ILE   C N   1 
ATOM   1457 C  CA  . ILE   B 1 47  ? 22.317 -27.317 26.015 1.00 13.61  ? 53  ILE   C CA  1 
ATOM   1458 C  C   . ILE   B 1 47  ? 23.405 -27.997 26.872 1.00 13.43  ? 53  ILE   C C   1 
ATOM   1459 O  O   . ILE   B 1 47  ? 23.158 -28.464 27.996 1.00 14.86  ? 53  ILE   C O   1 
ATOM   1460 C  CB  . ILE   B 1 47  ? 22.059 -25.926 26.619 1.00 14.48  ? 53  ILE   C CB  1 
ATOM   1461 C  CG1 . ILE   B 1 47  ? 20.859 -25.245 25.974 1.00 14.99  ? 53  ILE   C CG1 1 
ATOM   1462 C  CG2 . ILE   B 1 47  ? 23.329 -25.069 26.519 1.00 15.79  ? 53  ILE   C CG2 1 
ATOM   1463 C  CD1 . ILE   B 1 47  ? 21.043 -25.081 24.430 1.00 17.46  ? 53  ILE   C CD1 1 
ATOM   1464 N  N   . ALA   B 1 48  ? 24.606 -28.070 26.324 1.00 12.07  ? 54  ALA   C N   1 
ATOM   1465 C  CA  . ALA   B 1 48  ? 25.743 -28.634 27.078 1.00 12.00  ? 54  ALA   C CA  1 
ATOM   1466 C  C   . ALA   B 1 48  ? 26.105 -27.712 28.253 1.00 12.12  ? 54  ALA   C C   1 
ATOM   1467 O  O   . ALA   B 1 48  ? 26.076 -26.478 28.102 1.00 12.39  ? 54  ALA   C O   1 
ATOM   1468 C  CB  . ALA   B 1 48  ? 26.936 -28.738 26.154 1.00 11.98  ? 54  ALA   C CB  1 
ATOM   1469 N  N   . ARG   B 1 49  ? 26.467 -28.313 29.408 1.00 11.96  ? 55  ARG   C N   1 
ATOM   1470 C  CA  . ARG   B 1 49  ? 26.926 -27.556 30.573 1.00 12.20  ? 55  ARG   C CA  1 
ATOM   1471 C  C   . ARG   B 1 49  ? 28.243 -28.220 30.949 1.00 12.34  ? 55  ARG   C C   1 
ATOM   1472 O  O   . ARG   B 1 49  ? 28.277 -29.254 31.630 1.00 13.99  ? 55  ARG   C O   1 
ATOM   1473 C  CB  . ARG   B 1 49  ? 25.887 -27.605 31.710 1.00 13.18  ? 55  ARG   C CB  1 
ATOM   1474 C  CG  . ARG   B 1 49  ? 24.521 -27.035 31.296 1.00 12.99  ? 55  ARG   C CG  1 
ATOM   1475 C  CD  . ARG   B 1 49  ? 24.544 -25.550 30.898 1.00 14.12  ? 55  ARG   C CD  1 
ATOM   1476 N  NE  . ARG   B 1 49  ? 23.177 -25.111 30.542 1.00 14.51  ? 55  ARG   C NE  1 
ATOM   1477 C  CZ  . ARG   B 1 49  ? 22.921 -24.002 29.844 1.00 14.26  ? 55  ARG   C CZ  1 
ATOM   1478 N  NH1 . ARG   B 1 49  ? 23.898 -23.183 29.506 1.00 14.39  ? 55  ARG   C NH1 1 
ATOM   1479 N  NH2 . ARG   B 1 49  ? 21.664 -23.701 29.484 1.00 15.58  ? 55  ARG   C NH2 1 
ATOM   1480 N  N   . CYS   B 1 50  ? 29.331 -27.658 30.435 1.00 11.81  ? 56  CYS   C N   1 
ATOM   1481 C  CA  . CYS   B 1 50  ? 30.662 -28.291 30.458 1.00 12.03  ? 56  CYS   C CA  1 
ATOM   1482 C  C   . CYS   B 1 50  ? 31.717 -27.317 29.944 1.00 12.36  ? 56  CYS   C C   1 
ATOM   1483 O  O   . CYS   B 1 50  ? 31.407 -26.220 29.491 1.00 13.35  ? 56  CYS   C O   1 
ATOM   1484 C  CB  . CYS   B 1 50  ? 30.625 -29.521 29.532 1.00 11.67  ? 56  CYS   C CB  1 
ATOM   1485 S  SG  . CYS   B 1 50  ? 30.467 -29.094 27.753 1.00 12.44  ? 56  CYS   C SG  1 
ATOM   1486 N  N   . ASP   B 1 51  ? 33.008 -27.781 29.977 1.00 14.05  ? 57  ASP   C N   1 
ATOM   1487 C  CA  . ASP   B 1 51  ? 34.134 -27.059 29.387 1.00 14.98  ? 57  ASP   C CA  1 
ATOM   1488 C  C   . ASP   B 1 51  ? 34.787 -27.936 28.295 1.00 14.33  ? 57  ASP   C C   1 
ATOM   1489 O  O   . ASP   B 1 51  ? 35.994 -27.784 28.041 1.00 15.52  ? 57  ASP   C O   1 
ATOM   1490 C  CB  . ASP   B 1 51  ? 35.161 -26.632 30.445 1.00 17.26  ? 57  ASP   C CB  1 
ATOM   1491 C  CG  . ASP   B 1 51  ? 35.805 -27.762 31.191 1.00 21.83  ? 57  ASP   C CG  1 
ATOM   1492 O  OD1 . ASP   B 1 51  ? 35.504 -28.919 30.895 1.00 20.80  ? 57  ASP   C OD1 1 
ATOM   1493 O  OD2 . ASP   B 1 51  ? 36.710 -27.479 32.046 1.00 28.26  ? 57  ASP   C OD2 1 
ATOM   1494 N  N   . CYS   B 1 52  ? 34.000 -28.793 27.577 1.00 13.09  ? 58  CYS   C N   1 
ATOM   1495 C  CA  . CYS   B 1 52  ? 34.591 -29.546 26.454 1.00 12.95  ? 58  CYS   C CA  1 
ATOM   1496 C  C   . CYS   B 1 52  ? 35.255 -28.629 25.434 1.00 12.13  ? 58  CYS   C C   1 
ATOM   1497 O  O   . CYS   B 1 52  ? 34.812 -27.494 25.198 1.00 12.40  ? 58  CYS   C O   1 
ATOM   1498 C  CB  . CYS   B 1 52  ? 33.530 -30.384 25.723 1.00 12.94  ? 58  CYS   C CB  1 
ATOM   1499 S  SG  . CYS   B 1 52  ? 32.883 -31.798 26.659 1.00 13.35  ? 58  CYS   C SG  1 
ATOM   1500 N  N   . GLN   B 1 53  ? 36.308 -29.145 24.822 1.00 11.85  ? 59  GLN   C N   1 
ATOM   1501 C  CA  . GLN   B 1 53  ? 36.981 -28.513 23.694 1.00 12.75  ? 59  GLN   C CA  1 
ATOM   1502 C  C   . GLN   B 1 53  ? 37.052 -29.454 22.518 1.00 11.35  ? 59  GLN   C C   1 
ATOM   1503 O  O   . GLN   B 1 53  ? 37.825 -29.233 21.565 1.00 11.96  ? 59  GLN   C O   1 
ATOM   1504 C  CB  . GLN   B 1 53  ? 38.410 -28.052 24.045 1.00 13.98  ? 59  GLN   C CB  1 
ATOM   1505 C  CG  . GLN   B 1 53  ? 38.396 -26.811 24.975 1.00 17.59  ? 59  GLN   C CG  1 
ATOM   1506 C  CD  . GLN   B 1 53  ? 39.779 -26.240 25.160 1.00 19.58  ? 59  GLN   C CD  1 
ATOM   1507 O  OE1 . GLN   B 1 53  ? 40.301 -26.280 26.293 1.00 22.07  ? 59  GLN   C OE1 1 
ATOM   1508 N  NE2 . GLN   B 1 53  ? 40.413 -25.721 24.088 1.00 18.20  ? 59  GLN   C NE2 1 
ATOM   1509 N  N   . THR   B 1 54  ? 36.260 -30.556 22.512 1.00 11.14  ? 60  THR   C N   1 
ATOM   1510 C  CA  . THR   B 1 54  ? 36.162 -31.402 21.307 1.00 12.20  ? 60  THR   C CA  1 
ATOM   1511 C  C   . THR   B 1 54  ? 34.669 -31.665 21.065 1.00 12.15  ? 60  THR   C C   1 
ATOM   1512 O  O   . THR   B 1 54  ? 33.883 -31.786 22.008 1.00 12.78  ? 60  THR   C O   1 
ATOM   1513 C  CB  . THR   B 1 54  ? 36.897 -32.696 21.373 1.00 15.54  ? 60  THR   C CB  1 
ATOM   1514 O  OG1 . THR   B 1 54  ? 36.355 -33.458 22.396 1.00 18.74  ? 60  THR   C OG1 1 
ATOM   1515 C  CG2 . THR   B 1 54  ? 38.358 -32.503 21.659 1.00 15.70  ? 60  THR   C CG2 1 
ATOM   1516 N  N   . GLY   B 1 55  ? 34.279 -31.742 19.781 1.00 10.62  ? 61  GLY   C N   1 
ATOM   1517 C  CA  . GLY   B 1 55  ? 32.866 -31.955 19.462 1.00 10.99  ? 61  GLY   C CA  1 
ATOM   1518 C  C   . GLY   B 1 55  ? 32.727 -32.147 17.970 1.00 10.46  ? 61  GLY   C C   1 
ATOM   1519 O  O   . GLY   B 1 55  ? 33.719 -32.469 17.298 1.00 11.17  ? 61  GLY   C O   1 
ATOM   1520 N  N   . VAL   B 1 56  ? 31.502 -32.034 17.483 1.00 9.95   ? 62  VAL   C N   1 
ATOM   1521 C  CA  . VAL   B 1 56  ? 31.213 -32.244 16.051 1.00 9.40   ? 62  VAL   C CA  1 
ATOM   1522 C  C   . VAL   B 1 56  ? 30.319 -31.116 15.620 1.00 9.48   ? 62  VAL   C C   1 
ATOM   1523 O  O   . VAL   B 1 56  ? 29.370 -30.801 16.317 1.00 10.68  ? 62  VAL   C O   1 
ATOM   1524 C  CB  . VAL   B 1 56  ? 30.466 -33.613 15.872 1.00 10.00  ? 62  VAL   C CB  1 
ATOM   1525 C  CG1 . VAL   B 1 56  ? 29.999 -33.800 14.422 1.00 12.03  ? 62  VAL   C CG1 1 
ATOM   1526 C  CG2 . VAL   B 1 56  ? 31.393 -34.787 16.285 1.00 11.41  ? 62  VAL   C CG2 1 
ATOM   1527 N  N   . TYR   B 1 57  ? 30.579 -30.513 14.444 1.00 9.64   ? 63  TYR   C N   1 
ATOM   1528 C  CA  . TYR   B 1 57  ? 29.698 -29.453 13.930 1.00 8.92   ? 63  TYR   C CA  1 
ATOM   1529 C  C   . TYR   B 1 57  ? 29.128 -29.796 12.569 1.00 10.46  ? 63  TYR   C C   1 
ATOM   1530 O  O   . TYR   B 1 57  ? 29.800 -30.499 11.798 1.00 10.64  ? 63  TYR   C O   1 
ATOM   1531 C  CB  . TYR   B 1 57  ? 30.383 -28.047 13.920 1.00 9.80   ? 63  TYR   C CB  1 
ATOM   1532 C  CG  . TYR   B 1 57  ? 31.252 -27.733 12.706 1.00 10.01  ? 63  TYR   C CG  1 
ATOM   1533 C  CD1 . TYR   B 1 57  ? 32.536 -28.238 12.598 1.00 11.04  ? 63  TYR   C CD1 1 
ATOM   1534 C  CD2 . TYR   B 1 57  ? 30.784 -26.894 11.687 1.00 9.58   ? 63  TYR   C CD2 1 
ATOM   1535 C  CE1 . TYR   B 1 57  ? 33.348 -27.921 11.512 1.00 11.64  ? 63  TYR   C CE1 1 
ATOM   1536 C  CE2 . TYR   B 1 57  ? 31.596 -26.564 10.593 1.00 10.81  ? 63  TYR   C CE2 1 
ATOM   1537 C  CZ  . TYR   B 1 57  ? 32.865 -27.087 10.515 1.00 11.22  ? 63  TYR   C CZ  1 
ATOM   1538 O  OH  . TYR   B 1 57  ? 33.740 -26.791 9.465  1.00 13.80  ? 63  TYR   C OH  1 
ATOM   1539 N  N   . TYR   B 1 58  ? 27.970 -29.226 12.271 1.00 9.66   ? 64  TYR   C N   1 
ATOM   1540 C  CA  . TYR   B 1 58  ? 27.362 -29.392 10.934 1.00 9.88   ? 64  TYR   C CA  1 
ATOM   1541 C  C   . TYR   B 1 58  ? 27.765 -28.240 10.016 1.00 10.85  ? 64  TYR   C C   1 
ATOM   1542 O  O   . TYR   B 1 58  ? 27.517 -27.060 10.330 1.00 11.32  ? 64  TYR   C O   1 
ATOM   1543 C  CB  . TYR   B 1 58  ? 25.829 -29.487 11.023 1.00 11.27  ? 64  TYR   C CB  1 
ATOM   1544 C  CG  . TYR   B 1 58  ? 25.234 -29.764 9.654  1.00 12.72  ? 64  TYR   C CG  1 
ATOM   1545 C  CD1 . TYR   B 1 58  ? 25.576 -30.909 8.944  1.00 13.34  ? 64  TYR   C CD1 1 
ATOM   1546 C  CD2 . TYR   B 1 58  ? 24.394 -28.850 9.043  1.00 13.05  ? 64  TYR   C CD2 1 
ATOM   1547 C  CE1 . TYR   B 1 58  ? 25.076 -31.150 7.654  1.00 14.07  ? 64  TYR   C CE1 1 
ATOM   1548 C  CE2 . TYR   B 1 58  ? 23.856 -29.107 7.766  1.00 13.72  ? 64  TYR   C CE2 1 
ATOM   1549 C  CZ  . TYR   B 1 58  ? 24.220 -30.254 7.098  1.00 13.79  ? 64  TYR   C CZ  1 
ATOM   1550 O  OH  . TYR   B 1 58  ? 23.750 -30.490 5.803  1.00 17.35  ? 64  TYR   C OH  1 
ATOM   1551 N  N   . CYS   B 1 59  ? 28.286 -28.603 8.842  1.00 10.43  ? 65  CYS   C N   1 
ATOM   1552 C  CA  . CYS   B 1 59  ? 28.664 -27.638 7.788  1.00 10.53  ? 65  CYS   C CA  1 
ATOM   1553 C  C   . CYS   B 1 59  ? 27.739 -27.807 6.563  1.00 11.35  ? 65  CYS   C C   1 
ATOM   1554 O  O   . CYS   B 1 59  ? 27.892 -28.764 5.778  1.00 12.08  ? 65  CYS   C O   1 
ATOM   1555 C  CB  . CYS   B 1 59  ? 30.101 -27.923 7.401  1.00 10.89  ? 65  CYS   C CB  1 
ATOM   1556 S  SG  . CYS   B 1 59  ? 30.717 -26.872 6.050  1.00 13.17  ? 65  CYS   C SG  1 
ATOM   1557 N  N   . SER   B 1 60  ? 26.750 -26.931 6.444  1.00 12.47  ? 66  SER   C N   1 
ATOM   1558 C  CA  . SER   B 1 60  ? 25.764 -27.067 5.371  1.00 13.83  ? 66  SER   C CA  1 
ATOM   1559 C  C   . SER   B 1 60  ? 26.387 -26.957 3.971  1.00 14.10  ? 66  SER   C C   1 
ATOM   1560 O  O   . SER   B 1 60  ? 25.974 -27.724 3.071  1.00 15.59  ? 66  SER   C O   1 
ATOM   1561 C  CB  . SER   B 1 60  ? 24.637 -26.077 5.601  1.00 17.73  ? 66  SER   C CB  1 
ATOM   1562 O  OG  . SER   B 1 60  ? 25.040 -24.746 5.367  1.00 26.67  ? 66  SER   C OG  1 
ATOM   1563 N  N   . SER   B 1 61  ? 27.436 -26.121 3.816  1.00 12.87  ? 67  SER   C N   1 
ATOM   1564 C  CA  . SER   B 1 61  ? 28.107 -25.986 2.498  1.00 13.87  ? 67  SER   C CA  1 
ATOM   1565 C  C   . SER   B 1 61  ? 28.929 -27.174 2.074  1.00 15.05  ? 67  SER   C C   1 
ATOM   1566 O  O   . SER   B 1 61  ? 29.428 -27.193 0.955  1.00 17.07  ? 67  SER   C O   1 
ATOM   1567 C  CB  . SER   B 1 61  ? 28.970 -24.739 2.434  1.00 15.66  ? 67  SER   C CB  1 
ATOM   1568 O  OG  . SER   B 1 61  ? 30.048 -24.818 3.351  1.00 16.30  ? 67  SER   C OG  1 
ATOM   1569 N  N   . ARG   B 1 62  ? 29.039 -28.212 2.935  1.00 13.65  ? 68  ARG   C N   1 
ATOM   1570 C  CA  . ARG   B 1 62  ? 29.674 -29.481 2.553  1.00 14.04  ? 68  ARG   C CA  1 
ATOM   1571 C  C   . ARG   B 1 62  ? 28.732 -30.674 2.779  1.00 14.61  ? 68  ARG   C C   1 
ATOM   1572 O  O   . ARG   B 1 62  ? 29.135 -31.828 2.572  1.00 15.89  ? 68  ARG   C O   1 
ATOM   1573 C  CB  . ARG   B 1 62  ? 30.940 -29.692 3.386  1.00 14.70  ? 68  ARG   C CB  1 
ATOM   1574 C  CG  . ARG   B 1 62  ? 32.007 -28.631 3.126  1.00 17.44  ? 68  ARG   C CG  1 
ATOM   1575 C  CD  . ARG   B 1 62  ? 32.671 -28.895 1.796  1.00 17.41  ? 68  ARG   C CD  1 
ATOM   1576 N  NE  . ARG   B 1 62  ? 33.736 -27.912 1.554  1.00 19.48  ? 68  ARG   C NE  1 
ATOM   1577 C  CZ  . ARG   B 1 62  ? 33.571 -26.746 0.956  1.00 21.55  ? 68  ARG   C CZ  1 
ATOM   1578 N  NH1 . ARG   B 1 62  ? 32.388 -26.411 0.451  1.00 22.44  ? 68  ARG   C NH1 1 
ATOM   1579 N  NH2 . ARG   B 1 62  ? 34.618 -25.940 0.747  1.00 23.99  ? 68  ARG   C NH2 1 
ATOM   1580 N  N   . ARG   B 1 63  ? 27.505 -30.416 3.289  1.00 15.05  ? 69  ARG   C N   1 
ATOM   1581 C  CA  . ARG   B 1 63  ? 26.565 -31.489 3.733  1.00 16.22  ? 69  ARG   C CA  1 
ATOM   1582 C  C   . ARG   B 1 63  ? 27.257 -32.516 4.600  1.00 17.34  ? 69  ARG   C C   1 
ATOM   1583 O  O   . ARG   B 1 63  ? 27.119 -33.735 4.404  1.00 19.33  ? 69  ARG   C O   1 
ATOM   1584 C  CB  . ARG   B 1 63  ? 25.890 -32.177 2.533  1.00 17.31  ? 69  ARG   C CB  1 
ATOM   1585 C  CG  . ARG   B 1 63  ? 24.920 -31.280 1.833  1.00 22.90  ? 69  ARG   C CG  1 
ATOM   1586 C  CD  . ARG   B 1 63  ? 23.871 -32.151 1.185  1.00 34.31  ? 69  ARG   C CD  1 
ATOM   1587 N  NE  . ARG   B 1 63  ? 22.877 -31.305 0.541  1.00 40.89  ? 69  ARG   C NE  1 
ATOM   1588 C  CZ  . ARG   B 1 63  ? 22.842 -31.049 -0.760 1.00 46.70  ? 69  ARG   C CZ  1 
ATOM   1589 N  NH1 . ARG   B 1 63  ? 23.724 -31.614 -1.581 1.00 47.13  ? 69  ARG   C NH1 1 
ATOM   1590 N  NH2 . ARG   B 1 63  ? 21.892 -30.272 -1.261 1.00 47.64  ? 69  ARG   C NH2 1 
ATOM   1591 N  N   . LYS   B 1 64  ? 28.063 -32.026 5.564  1.00 14.29  ? 70  LYS   C N   1 
ATOM   1592 C  CA  . LYS   B 1 64  ? 28.848 -32.956 6.371  1.00 14.74  ? 70  LYS   C CA  1 
ATOM   1593 C  C   . LYS   B 1 64  ? 28.958 -32.485 7.795  1.00 13.43  ? 70  LYS   C C   1 
ATOM   1594 O  O   . LYS   B 1 64  ? 29.004 -31.270 8.059  1.00 13.66  ? 70  LYS   C O   1 
ATOM   1595 C  CB  . LYS   B 1 64  ? 30.264 -33.024 5.769  1.00 19.70  ? 70  LYS   C CB  1 
ATOM   1596 C  CG  . LYS   B 1 64  ? 30.386 -34.071 4.645  1.00 30.59  ? 70  LYS   C CG  1 
ATOM   1597 C  CD  . LYS   B 1 64  ? 31.843 -34.381 4.288  1.00 39.04  ? 70  LYS   C CD  1 
ATOM   1598 C  CE  . LYS   B 1 64  ? 31.950 -35.397 3.182  1.00 45.04  ? 70  LYS   C CE  1 
ATOM   1599 N  NZ  . LYS   B 1 64  ? 31.372 -34.901 1.910  1.00 50.03  ? 70  LYS   C NZ  1 
ATOM   1600 N  N   . HIS   B 1 65  ? 29.078 -33.439 8.700  1.00 12.14  ? 71  HIS   C N   1 
ATOM   1601 C  CA  . HIS   B 1 65  ? 29.393 -33.177 10.115 1.00 11.98  ? 71  HIS   C CA  1 
ATOM   1602 C  C   . HIS   B 1 65  ? 30.858 -33.464 10.301 1.00 13.92  ? 71  HIS   C C   1 
ATOM   1603 O  O   . HIS   B 1 65  ? 31.349 -34.563 9.932  1.00 17.35  ? 71  HIS   C O   1 
ATOM   1604 C  CB  . HIS   B 1 65  ? 28.567 -34.076 11.045 1.00 12.18  ? 71  HIS   C CB  1 
ATOM   1605 C  CG  . HIS   B 1 65  ? 27.094 -33.801 11.005 1.00 11.30  ? 71  HIS   C CG  1 
ATOM   1606 N  ND1 . HIS   B 1 65  ? 26.438 -33.044 11.956 1.00 14.69  ? 71  HIS   C ND1 1 
ATOM   1607 C  CD2 . HIS   B 1 65  ? 26.190 -34.230 10.092 1.00 11.75  ? 71  HIS   C CD2 1 
ATOM   1608 C  CE1 . HIS   B 1 65  ? 25.143 -33.054 11.612 1.00 12.09  ? 71  HIS   C CE1 1 
ATOM   1609 N  NE2 . HIS   B 1 65  ? 24.943 -33.772 10.524 1.00 15.13  ? 71  HIS   C NE2 1 
ATOM   1610 N  N   . TYR   B 1 66  ? 31.615 -32.524 10.898 1.00 11.02  ? 72  TYR   C N   1 
ATOM   1611 C  CA  . TYR   B 1 66  ? 33.054 -32.717 11.076 1.00 11.04  ? 72  TYR   C CA  1 
ATOM   1612 C  C   . TYR   B 1 66  ? 33.427 -32.739 12.551 1.00 11.15  ? 72  TYR   C C   1 
ATOM   1613 O  O   . TYR   B 1 66  ? 32.981 -31.861 13.319 1.00 10.92  ? 72  TYR   C O   1 
ATOM   1614 C  CB  . TYR   B 1 66  ? 33.802 -31.487 10.485 1.00 12.02  ? 72  TYR   C CB  1 
ATOM   1615 C  CG  . TYR   B 1 66  ? 33.759 -31.392 8.967  1.00 12.77  ? 72  TYR   C CG  1 
ATOM   1616 C  CD1 . TYR   B 1 66  ? 34.608 -32.151 8.181  1.00 15.93  ? 72  TYR   C CD1 1 
ATOM   1617 C  CD2 . TYR   B 1 66  ? 32.940 -30.469 8.328  1.00 14.29  ? 72  TYR   C CD2 1 
ATOM   1618 C  CE1 . TYR   B 1 66  ? 34.621 -32.020 6.790  1.00 16.65  ? 72  TYR   C CE1 1 
ATOM   1619 C  CE2 . TYR   B 1 66  ? 32.935 -30.334 6.943  1.00 15.22  ? 72  TYR   C CE2 1 
ATOM   1620 C  CZ  . TYR   B 1 66  ? 33.775 -31.121 6.183  1.00 15.87  ? 72  TYR   C CZ  1 
ATOM   1621 O  OH  . TYR   B 1 66  ? 33.756 -30.922 4.810  1.00 18.59  ? 72  TYR   C OH  1 
ATOM   1622 N  N   . PRO   B 1 67  ? 34.246 -33.696 12.953 1.00 11.07  ? 73  PRO   C N   1 
ATOM   1623 C  CA  . PRO   B 1 67  ? 34.771 -33.667 14.333 1.00 10.70  ? 73  PRO   C CA  1 
ATOM   1624 C  C   . PRO   B 1 67  ? 35.882 -32.611 14.432 1.00 11.85  ? 73  PRO   C C   1 
ATOM   1625 O  O   . PRO   B 1 67  ? 36.747 -32.526 13.545 1.00 14.86  ? 73  PRO   C O   1 
ATOM   1626 C  CB  . PRO   B 1 67  ? 35.353 -35.080 14.537 1.00 12.72  ? 73  PRO   C CB  1 
ATOM   1627 C  CG  . PRO   B 1 67  ? 35.585 -35.613 13.189 1.00 15.33  ? 73  PRO   C CG  1 
ATOM   1628 C  CD  . PRO   B 1 67  ? 34.731 -34.887 12.188 1.00 11.98  ? 73  PRO   C CD  1 
ATOM   1629 N  N   . VAL   B 1 68  ? 35.851 -31.820 15.491 1.00 10.76  ? 74  VAL   C N   1 
ATOM   1630 C  CA  . VAL   B 1 68  ? 36.794 -30.698 15.641 1.00 11.67  ? 74  VAL   C CA  1 
ATOM   1631 C  C   . VAL   B 1 68  ? 37.210 -30.532 17.074 1.00 11.17  ? 74  VAL   C C   1 
ATOM   1632 O  O   . VAL   B 1 68  ? 36.464 -30.813 18.016 1.00 11.50  ? 74  VAL   C O   1 
ATOM   1633 C  CB  . VAL   B 1 68  ? 36.201 -29.330 15.151 1.00 12.82  ? 74  VAL   C CB  1 
ATOM   1634 C  CG1 . VAL   B 1 68  ? 36.134 -29.241 13.611 1.00 14.91  ? 74  VAL   C CG1 1 
ATOM   1635 C  CG2 . VAL   B 1 68  ? 34.855 -29.042 15.809 1.00 13.73  ? 74  VAL   C CG2 1 
ATOM   1636 N  N   . SER   B 1 69  ? 38.428 -29.981 17.261 1.00 11.42  ? 75  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 69  ? 38.884 -29.381 18.511 1.00 11.74  ? 75  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 69  ? 38.600 -27.885 18.404 1.00 11.17  ? 75  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 69  ? 38.753 -27.259 17.310 1.00 11.99  ? 75  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 69  ? 40.395 -29.546 18.631 1.00 14.39  ? 75  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 69  ? 40.641 -30.928 18.769 1.00 19.53  ? 75  SER   C OG  1 
ATOM   1642 N  N   . PHE   B 1 70  ? 38.125 -27.268 19.482 1.00 10.14  ? 76  PHE   C N   1 
ATOM   1643 C  CA  . PHE   B 1 70  ? 37.772 -25.850 19.443 1.00 10.63  ? 76  PHE   C CA  1 
ATOM   1644 C  C   . PHE   B 1 70  ? 38.266 -25.125 20.687 1.00 10.95  ? 76  PHE   C C   1 
ATOM   1645 O  O   . PHE   B 1 70  ? 38.428 -25.737 21.742 1.00 11.64  ? 76  PHE   C O   1 
ATOM   1646 C  CB  . PHE   B 1 70  ? 36.242 -25.608 19.181 1.00 11.58  ? 76  PHE   C CB  1 
ATOM   1647 C  CG  . PHE   B 1 70  ? 35.335 -26.321 20.174 1.00 11.12  ? 76  PHE   C CG  1 
ATOM   1648 C  CD1 . PHE   B 1 70  ? 34.920 -27.628 19.956 1.00 11.11  ? 76  PHE   C CD1 1 
ATOM   1649 C  CD2 . PHE   B 1 70  ? 34.891 -25.671 21.317 1.00 11.84  ? 76  PHE   C CD2 1 
ATOM   1650 C  CE1 . PHE   B 1 70  ? 34.083 -28.268 20.883 1.00 10.79  ? 76  PHE   C CE1 1 
ATOM   1651 C  CE2 . PHE   B 1 70  ? 34.050 -26.325 22.237 1.00 11.50  ? 76  PHE   C CE2 1 
ATOM   1652 C  CZ  . PHE   B 1 70  ? 33.679 -27.623 22.034 1.00 11.20  ? 76  PHE   C CZ  1 
ATOM   1653 N  N   . SER   B 1 71  ? 38.521 -23.835 20.556 1.00 10.81  ? 77  SER   C N   1 
ATOM   1654 C  CA  . SER   B 1 71  ? 39.097 -23.058 21.637 1.00 11.68  ? 77  SER   C CA  1 
ATOM   1655 C  C   . SER   B 1 71  ? 38.113 -22.689 22.721 1.00 13.04  ? 77  SER   C C   1 
ATOM   1656 O  O   . SER   B 1 71  ? 36.912 -22.912 22.605 1.00 14.71  ? 77  SER   C O   1 
ATOM   1657 C  CB  . SER   B 1 71  ? 39.826 -21.834 21.092 1.00 12.26  ? 77  SER   C CB  1 
ATOM   1658 O  OG  . SER   B 1 71  ? 38.922 -20.957 20.433 1.00 15.08  ? 77  SER   C OG  1 
ATOM   1659 N  N   . LYS   B 1 72  ? 38.592 -22.101 23.820 1.00 14.66  ? 78  LYS   C N   1 
ATOM   1660 C  CA  . LYS   B 1 72  ? 37.713 -21.671 24.916 1.00 14.54  ? 78  LYS   C CA  1 
ATOM   1661 C  C   . LYS   B 1 72  ? 37.019 -20.351 24.521 1.00 14.91  ? 78  LYS   C C   1 
ATOM   1662 O  O   . LYS   B 1 72  ? 37.611 -19.549 23.783 1.00 15.88  ? 78  LYS   C O   1 
ATOM   1663 C  CB  . LYS   B 1 72  ? 38.565 -21.447 26.183 1.00 18.86  ? 78  LYS   C CB  1 
ATOM   1664 C  CG  . LYS   B 1 72  ? 39.287 -22.702 26.608 1.00 24.51  ? 78  LYS   C CG  1 
ATOM   1665 C  CD  . LYS   B 1 72  ? 39.613 -22.728 28.116 1.00 35.66  ? 78  LYS   C CD  1 
ATOM   1666 C  CE  . LYS   B 1 72  ? 39.700 -24.162 28.638 1.00 42.86  ? 78  LYS   C CE  1 
ATOM   1667 N  NZ  . LYS   B 1 72  ? 39.677 -24.227 30.133 1.00 47.12  ? 78  LYS   C NZ  1 
ATOM   1668 N  N   . PRO   B 1 73  ? 35.781 -20.093 24.972 1.00 14.02  ? 79  PRO   C N   1 
ATOM   1669 C  CA  . PRO   B 1 73  ? 35.063 -18.849 24.546 1.00 14.70  ? 79  PRO   C CA  1 
ATOM   1670 C  C   . PRO   B 1 73  ? 35.838 -17.601 24.916 1.00 14.98  ? 79  PRO   C C   1 
ATOM   1671 O  O   . PRO   B 1 73  ? 36.298 -17.476 26.076 1.00 17.31  ? 79  PRO   C O   1 
ATOM   1672 C  CB  . PRO   B 1 73  ? 33.743 -18.885 25.310 1.00 16.80  ? 79  PRO   C CB  1 
ATOM   1673 C  CG  . PRO   B 1 73  ? 33.614 -20.313 25.826 1.00 19.09  ? 79  PRO   C CG  1 
ATOM   1674 C  CD  . PRO   B 1 73  ? 34.983 -20.952 25.883 1.00 15.80  ? 79  PRO   C CD  1 
ATOM   1675 N  N   . SER   B 1 74  ? 36.076 -16.711 23.940 1.00 13.88  ? 80  SER   C N   1 
ATOM   1676 C  CA  . SER   B 1 74  ? 36.946 -15.556 24.149 1.00 15.50  ? 80  SER   C CA  1 
ATOM   1677 C  C   . SER   B 1 74  ? 36.529 -14.380 23.271 1.00 15.15  ? 80  SER   C C   1 
ATOM   1678 O  O   . SER   B 1 74  ? 35.662 -14.517 22.414 1.00 14.79  ? 80  SER   C O   1 
ATOM   1679 C  CB  . SER   B 1 74  ? 38.382 -15.923 23.770 1.00 18.14  ? 80  SER   C CB  1 
ATOM   1680 O  OG  . SER   B 1 74  ? 38.843 -17.101 24.427 1.00 24.44  ? 80  SER   C OG  1 
ATOM   1681 N  N   . LEU   B 1 75  ? 37.205 -13.223 23.471 1.00 15.75  ? 81  LEU   C N   1 
ATOM   1682 C  CA  . LEU   B 1 75  ? 36.996 -12.012 22.678 1.00 16.28  ? 81  LEU   C CA  1 
ATOM   1683 C  C   . LEU   B 1 75  ? 38.018 -12.064 21.516 1.00 16.90  ? 81  LEU   C C   1 
ATOM   1684 O  O   . LEU   B 1 75  ? 39.256 -11.987 21.775 1.00 20.13  ? 81  LEU   C O   1 
ATOM   1685 C  CB  . LEU   B 1 75  ? 37.241 -10.780 23.597 1.00 18.25  ? 81  LEU   C CB  1 
ATOM   1686 C  CG  . LEU   B 1 75  ? 37.017 -9.433  22.935 1.00 20.87  ? 81  LEU   C CG  1 
ATOM   1687 C  CD1 . LEU   B 1 75  ? 35.531 -9.218  22.663 1.00 20.26  ? 81  LEU   C CD1 1 
ATOM   1688 C  CD2 . LEU   B 1 75  ? 37.491 -8.288  23.895 1.00 23.66  ? 81  LEU   C CD2 1 
ATOM   1689 N  N   . ILE   B 1 76  ? 37.561 -12.272 20.283 1.00 17.77  ? 82  ILE   C N   1 
ATOM   1690 C  CA  . ILE   B 1 76  ? 38.393 -12.524 19.103 1.00 19.35  ? 82  ILE   C CA  1 
ATOM   1691 C  C   . ILE   B 1 76  ? 38.119 -11.466 18.041 1.00 19.05  ? 82  ILE   C C   1 
ATOM   1692 O  O   . ILE   B 1 76  ? 36.937 -11.140 17.794 1.00 17.96  ? 82  ILE   C O   1 
ATOM   1693 C  CB  . ILE   B 1 76  ? 38.036 -13.925 18.518 1.00 22.06  ? 82  ILE   C CB  1 
ATOM   1694 C  CG1 . ILE   B 1 76  ? 38.259 -15.100 19.529 1.00 24.96  ? 82  ILE   C CG1 1 
ATOM   1695 C  CG2 . ILE   B 1 76  ? 38.733 -14.216 17.167 1.00 24.46  ? 82  ILE   C CG2 1 
ATOM   1696 C  CD1 . ILE   B 1 76  ? 39.671 -15.605 19.676 1.00 27.00  ? 82  ILE   C CD1 1 
ATOM   1697 N  N   . PHE   B 1 77  ? 39.200 -10.954 17.382 1.00 19.07  ? 83  PHE   C N   1 
ATOM   1698 C  CA  . PHE   B 1 77  ? 39.009 -10.018 16.277 1.00 18.97  ? 83  PHE   C CA  1 
ATOM   1699 C  C   . PHE   B 1 77  ? 38.607 -10.882 15.061 1.00 19.78  ? 83  PHE   C C   1 
ATOM   1700 O  O   . PHE   B 1 77  ? 39.276 -11.880 14.728 1.00 22.74  ? 83  PHE   C O   1 
ATOM   1701 C  CB  . PHE   B 1 77  ? 40.299 -9.219  15.978 1.00 18.98  ? 83  PHE   C CB  1 
ATOM   1702 C  CG  . PHE   B 1 77  ? 40.026 -8.066  15.025 1.00 20.71  ? 83  PHE   C CG  1 
ATOM   1703 C  CD1 . PHE   B 1 77  ? 39.311 -6.954  15.439 1.00 22.33  ? 83  PHE   C CD1 1 
ATOM   1704 C  CD2 . PHE   B 1 77  ? 40.390 -8.147  13.684 1.00 22.66  ? 83  PHE   C CD2 1 
ATOM   1705 C  CE1 . PHE   B 1 77  ? 39.006 -5.914  14.542 1.00 23.21  ? 83  PHE   C CE1 1 
ATOM   1706 C  CE2 . PHE   B 1 77  ? 40.090 -7.109  12.797 1.00 23.29  ? 83  PHE   C CE2 1 
ATOM   1707 C  CZ  . PHE   B 1 77  ? 39.434 -5.989  13.235 1.00 23.00  ? 83  PHE   C CZ  1 
ATOM   1708 N  N   . VAL   B 1 78  ? 37.494 -10.515 14.413 1.00 16.73  ? 84  VAL   C N   1 
ATOM   1709 C  CA  . VAL   B 1 78  ? 36.991 -11.250 13.257 1.00 16.53  ? 84  VAL   C CA  1 
ATOM   1710 C  C   . VAL   B 1 78  ? 37.082 -10.317 12.045 1.00 16.09  ? 84  VAL   C C   1 
ATOM   1711 O  O   . VAL   B 1 78  ? 36.625 -9.177  12.138 1.00 16.88  ? 84  VAL   C O   1 
ATOM   1712 C  CB  . VAL   B 1 78  ? 35.502 -11.674 13.542 1.00 16.55  ? 84  VAL   C CB  1 
ATOM   1713 C  CG1 . VAL   B 1 78  ? 34.943 -12.438 12.353 1.00 16.66  ? 84  VAL   C CG1 1 
ATOM   1714 C  CG2 . VAL   B 1 78  ? 35.397 -12.525 14.815 1.00 17.71  ? 84  VAL   C CG2 1 
ATOM   1715 N  N   . GLU   B 1 79  ? 37.610 -10.795 10.905 1.00 15.70  ? 85  GLU   C N   1 
ATOM   1716 C  CA  . GLU   B 1 79  ? 37.650 -9.987  9.680  1.00 16.28  ? 85  GLU   C CA  1 
ATOM   1717 C  C   . GLU   B 1 79  ? 36.238 -9.734  9.135  1.00 15.97  ? 85  GLU   C C   1 
ATOM   1718 O  O   . GLU   B 1 79  ? 35.269 -10.415 9.498  1.00 15.31  ? 85  GLU   C O   1 
ATOM   1719 C  CB  . GLU   B 1 79  ? 38.479 -10.703 8.590  1.00 18.85  ? 85  GLU   C CB  1 
ATOM   1720 C  CG  . GLU   B 1 79  ? 39.971 -10.776 8.914  1.00 23.86  ? 85  GLU   C CG  1 
ATOM   1721 C  CD  . GLU   B 1 79  ? 40.595 -9.404  9.145  1.00 34.55  ? 85  GLU   C CD  1 
ATOM   1722 O  OE1 . GLU   B 1 79  ? 40.384 -8.489  8.312  1.00 39.30  ? 85  GLU   C OE1 1 
ATOM   1723 O  OE2 . GLU   B 1 79  ? 41.279 -9.231  10.181 1.00 38.97  ? 85  GLU   C OE2 1 
ATOM   1724 N  N   . ALA   B 1 80  ? 36.113 -8.738  8.262  1.00 16.68  ? 86  ALA   C N   1 
ATOM   1725 C  CA  . ALA   B 1 80  ? 34.824 -8.395  7.681  1.00 17.53  ? 86  ALA   C CA  1 
ATOM   1726 C  C   . ALA   B 1 80  ? 34.214 -9.581  6.947  1.00 17.22  ? 86  ALA   C C   1 
ATOM   1727 O  O   . ALA   B 1 80  ? 34.946 -10.384 6.360  1.00 19.81  ? 86  ALA   C O   1 
ATOM   1728 C  CB  . ALA   B 1 80  ? 35.023 -7.248  6.693  1.00 19.06  ? 86  ALA   C CB  1 
ATOM   1729 N  N   . SER   B 1 81  ? 32.920 -9.757  7.106  1.00 15.88  ? 87  SER   C N   1 
ATOM   1730 C  CA  . SER   B 1 81  ? 32.194 -10.778 6.411  1.00 16.80  ? 87  SER   C CA  1 
ATOM   1731 C  C   . SER   B 1 81  ? 31.077 -10.099 5.608  1.00 17.99  ? 87  SER   C C   1 
ATOM   1732 O  O   . SER   B 1 81  ? 30.913 -8.864  5.650  1.00 18.64  ? 87  SER   C O   1 
ATOM   1733 C  CB  . SER   B 1 81  ? 31.596 -11.765 7.422  1.00 16.11  ? 87  SER   C CB  1 
ATOM   1734 O  OG  . SER   B 1 81  ? 30.549 -11.107 8.138  1.00 15.81  ? 87  SER   C OG  1 
ATOM   1735 N  N   . GLU   B 1 82  ? 30.245 -10.917 4.965  1.00 19.18  ? 88  GLU   C N   1 
ATOM   1736 C  CA  . GLU   B 1 82  ? 29.137 -10.297 4.219  1.00 20.58  ? 88  GLU   C CA  1 
ATOM   1737 C  C   . GLU   B 1 82  ? 28.059 -9.674  5.141  1.00 19.51  ? 88  GLU   C C   1 
ATOM   1738 O  O   . GLU   B 1 82  ? 27.263 -8.835  4.683  1.00 21.25  ? 88  GLU   C O   1 
ATOM   1739 C  CB  . GLU   B 1 82  ? 28.561 -11.293 3.217  1.00 25.98  ? 88  GLU   C CB  1 
ATOM   1740 C  CG  . GLU   B 1 82  ? 27.607 -12.306 3.774  1.00 34.49  ? 88  GLU   C CG  1 
ATOM   1741 C  CD  . GLU   B 1 82  ? 26.944 -13.130 2.684  1.00 41.27  ? 88  GLU   C CD  1 
ATOM   1742 O  OE1 . GLU   B 1 82  ? 27.597 -13.369 1.639  1.00 41.75  ? 88  GLU   C OE1 1 
ATOM   1743 O  OE2 . GLU   B 1 82  ? 25.773 -13.535 2.881  1.00 41.82  ? 88  GLU   C OE2 1 
ATOM   1744 N  N   . TYR   B 1 83  ? 28.089 -10.002 6.433  1.00 17.09  ? 89  TYR   C N   1 
ATOM   1745 C  CA  . TYR   B 1 83  ? 27.056 -9.535  7.347  1.00 15.91  ? 89  TYR   C CA  1 
ATOM   1746 C  C   . TYR   B 1 83  ? 27.566 -8.709  8.551  1.00 17.60  ? 89  TYR   C C   1 
ATOM   1747 O  O   . TYR   B 1 83  ? 26.721 -8.138  9.245  1.00 17.90  ? 89  TYR   C O   1 
ATOM   1748 C  CB  . TYR   B 1 83  ? 26.188 -10.745 7.819  1.00 15.30  ? 89  TYR   C CB  1 
ATOM   1749 C  CG  . TYR   B 1 83  ? 27.019 -11.942 8.294  1.00 14.80  ? 89  TYR   C CG  1 
ATOM   1750 C  CD1 . TYR   B 1 83  ? 27.482 -12.910 7.395  1.00 15.38  ? 89  TYR   C CD1 1 
ATOM   1751 C  CD2 . TYR   B 1 83  ? 27.400 -12.065 9.620  1.00 15.19  ? 89  TYR   C CD2 1 
ATOM   1752 C  CE1 . TYR   B 1 83  ? 28.226 -14.014 7.832  1.00 15.38  ? 89  TYR   C CE1 1 
ATOM   1753 C  CE2 . TYR   B 1 83  ? 28.180 -13.130 10.063 1.00 15.14  ? 89  TYR   C CE2 1 
ATOM   1754 C  CZ  . TYR   B 1 83  ? 28.590 -14.120 9.174  1.00 14.83  ? 89  TYR   C CZ  1 
ATOM   1755 O  OH  . TYR   B 1 83  ? 29.422 -15.153 9.584  1.00 15.95  ? 89  TYR   C OH  1 
ATOM   1756 N  N   . TYR   B 1 84  ? 28.876 -8.580  8.811  1.00 15.45  ? 90  TYR   C N   1 
ATOM   1757 C  CA  . TYR   B 1 84  ? 29.413 -7.683  9.848  1.00 15.39  ? 90  TYR   C CA  1 
ATOM   1758 C  C   . TYR   B 1 84  ? 30.734 -7.072  9.323  1.00 15.92  ? 90  TYR   C C   1 
ATOM   1759 O  O   . TYR   B 1 84  ? 31.460 -7.696  8.552  1.00 16.17  ? 90  TYR   C O   1 
ATOM   1760 C  CB  . TYR   B 1 84  ? 29.773 -8.421  11.180 1.00 14.45  ? 90  TYR   C CB  1 
ATOM   1761 C  CG  . TYR   B 1 84  ? 28.601 -8.840  12.037 1.00 13.97  ? 90  TYR   C CG  1 
ATOM   1762 C  CD1 . TYR   B 1 84  ? 27.678 -7.907  12.524 1.00 14.69  ? 90  TYR   C CD1 1 
ATOM   1763 C  CD2 . TYR   B 1 84  ? 28.392 -10.156 12.337 1.00 14.34  ? 90  TYR   C CD2 1 
ATOM   1764 C  CE1 . TYR   B 1 84  ? 26.601 -8.299  13.333 1.00 15.09  ? 90  TYR   C CE1 1 
ATOM   1765 C  CE2 . TYR   B 1 84  ? 27.321 -10.563 13.128 1.00 14.18  ? 90  TYR   C CE2 1 
ATOM   1766 C  CZ  . TYR   B 1 84  ? 26.442 -9.634  13.661 1.00 14.22  ? 90  TYR   C CZ  1 
ATOM   1767 O  OH  . TYR   B 1 84  ? 25.366 -10.029 14.455 1.00 13.97  ? 90  TYR   C OH  1 
ATOM   1768 N  N   . PRO   B 1 85  ? 31.086 -5.858  9.774  1.00 16.47  ? 91  PRO   C N   1 
ATOM   1769 C  CA  . PRO   B 1 85  ? 32.434 -5.329  9.478  1.00 16.16  ? 91  PRO   C CA  1 
ATOM   1770 C  C   . PRO   B 1 85  ? 33.463 -6.102  10.333 1.00 15.94  ? 91  PRO   C C   1 
ATOM   1771 O  O   . PRO   B 1 85  ? 33.114 -6.905  11.241 1.00 15.99  ? 91  PRO   C O   1 
ATOM   1772 C  CB  . PRO   B 1 85  ? 32.315 -3.861  9.950  1.00 17.38  ? 91  PRO   C CB  1 
ATOM   1773 C  CG  . PRO   B 1 85  ? 31.410 -3.962  11.117 1.00 17.27  ? 91  PRO   C CG  1 
ATOM   1774 C  CD  . PRO   B 1 85  ? 30.344 -5.009  10.740 1.00 17.62  ? 91  PRO   C CD  1 
ATOM   1775 N  N   . ALA   B 1 86  ? 34.752 -5.822  10.120 1.00 16.15  ? 92  ALA   C N   1 
ATOM   1776 C  CA  . ALA   B 1 86  ? 35.804 -6.357  10.962 1.00 18.21  ? 92  ALA   C CA  1 
ATOM   1777 C  C   . ALA   B 1 86  ? 35.601 -5.777  12.377 1.00 18.97  ? 92  ALA   C C   1 
ATOM   1778 O  O   . ALA   B 1 86  ? 35.305 -4.571  12.516 1.00 20.12  ? 92  ALA   C O   1 
ATOM   1779 C  CB  . ALA   B 1 86  ? 37.162 -5.912  10.399 1.00 18.62  ? 92  ALA   C CB  1 
ATOM   1780 N  N   . ARG   B 1 87  ? 35.615 -6.653  13.405 1.00 17.55  ? 93  ARG   C N   1 
ATOM   1781 C  CA  . ARG   B 1 87  ? 35.289 -6.192  14.755 1.00 17.87  ? 93  ARG   C CA  1 
ATOM   1782 C  C   . ARG   B 1 87  ? 35.694 -7.282  15.756 1.00 17.48  ? 93  ARG   C C   1 
ATOM   1783 O  O   . ARG   B 1 87  ? 35.936 -8.420  15.369 1.00 16.71  ? 93  ARG   C O   1 
ATOM   1784 C  CB  . ARG   B 1 87  ? 33.759 -5.938  14.888 1.00 18.04  ? 93  ARG   C CB  1 
ATOM   1785 C  CG  . ARG   B 1 87  ? 32.957 -7.263  14.824 1.00 16.59  ? 93  ARG   C CG  1 
ATOM   1786 C  CD  . ARG   B 1 87  ? 31.476 -7.008  14.798 1.00 16.81  ? 93  ARG   C CD  1 
ATOM   1787 N  NE  . ARG   B 1 87  ? 30.772 -8.264  15.081 1.00 16.13  ? 93  ARG   C NE  1 
ATOM   1788 C  CZ  . ARG   B 1 87  ? 29.706 -8.435  15.831 1.00 17.04  ? 93  ARG   C CZ  1 
ATOM   1789 N  NH1 . ARG   B 1 87  ? 29.097 -7.388  16.393 1.00 18.75  ? 93  ARG   C NH1 1 
ATOM   1790 N  NH2 . ARG   B 1 87  ? 29.263 -9.660  16.086 1.00 17.41  ? 93  ARG   C NH2 1 
ATOM   1791 N  N   . TYR   B 1 88  ? 35.652 -6.949  17.053 1.00 18.60  ? 94  TYR   C N   1 
ATOM   1792 C  CA  . TYR   B 1 88  ? 35.805 -7.953  18.095 1.00 19.56  ? 94  TYR   C CA  1 
ATOM   1793 C  C   . TYR   B 1 88  ? 34.431 -8.604  18.364 1.00 17.21  ? 94  TYR   C C   1 
ATOM   1794 O  O   . TYR   B 1 88  ? 33.428 -7.904  18.481 1.00 19.32  ? 94  TYR   C O   1 
ATOM   1795 C  CB  . TYR   B 1 88  ? 36.265 -7.312  19.414 1.00 22.08  ? 94  TYR   C CB  1 
ATOM   1796 C  CG  . TYR   B 1 88  ? 37.727 -6.964  19.369 1.00 24.76  ? 94  TYR   C CG  1 
ATOM   1797 C  CD1 . TYR   B 1 88  ? 38.691 -7.922  19.616 1.00 26.10  ? 94  TYR   C CD1 1 
ATOM   1798 C  CD2 . TYR   B 1 88  ? 38.147 -5.681  19.004 1.00 26.19  ? 94  TYR   C CD2 1 
ATOM   1799 C  CE1 . TYR   B 1 88  ? 40.051 -7.615  19.525 1.00 27.62  ? 94  TYR   C CE1 1 
ATOM   1800 C  CE2 . TYR   B 1 88  ? 39.487 -5.371  18.890 1.00 27.15  ? 94  TYR   C CE2 1 
ATOM   1801 C  CZ  . TYR   B 1 88  ? 40.437 -6.328  19.179 1.00 28.15  ? 94  TYR   C CZ  1 
ATOM   1802 O  OH  . TYR   B 1 88  ? 41.764 -5.952  19.079 1.00 30.84  ? 94  TYR   C OH  1 
ATOM   1803 N  N   . GLN   B 1 89  ? 34.394 -9.930  18.431 1.00 15.24  ? 95  GLN   C N   1 
ATOM   1804 C  CA  . GLN   B 1 89  ? 33.182 -10.675 18.779 1.00 14.36  ? 95  GLN   C CA  1 
ATOM   1805 C  C   . GLN   B 1 89  ? 33.492 -11.399 20.086 1.00 13.97  ? 95  GLN   C C   1 
ATOM   1806 O  O   . GLN   B 1 89  ? 34.584 -12.013 20.229 1.00 14.87  ? 95  GLN   C O   1 
ATOM   1807 C  CB  . GLN   B 1 89  ? 32.814 -11.620 17.625 1.00 15.16  ? 95  GLN   C CB  1 
ATOM   1808 C  CG  . GLN   B 1 89  ? 31.561 -12.436 17.923 1.00 16.19  ? 95  GLN   C CG  1 
ATOM   1809 C  CD  . GLN   B 1 89  ? 30.863 -12.984 16.701 1.00 13.79  ? 95  GLN   C CD  1 
ATOM   1810 O  OE1 . GLN   B 1 89  ? 30.843 -12.389 15.603 1.00 15.68  ? 95  GLN   C OE1 1 
ATOM   1811 N  NE2 . GLN   B 1 89  ? 30.289 -14.156 16.876 1.00 13.71  ? 95  GLN   C NE2 1 
ATOM   1812 N  N   . SER   B 1 90  ? 32.584 -11.366 21.033 1.00 13.34  ? 96  SER   C N   1 
ATOM   1813 C  CA  . SER   B 1 90  ? 32.773 -12.003 22.320 1.00 14.14  ? 96  SER   C CA  1 
ATOM   1814 C  C   . SER   B 1 90  ? 32.177 -13.416 22.379 1.00 12.76  ? 96  SER   C C   1 
ATOM   1815 O  O   . SER   B 1 90  ? 31.327 -13.774 21.566 1.00 12.90  ? 96  SER   C O   1 
ATOM   1816 C  CB  . SER   B 1 90  ? 32.228 -11.121 23.450 1.00 15.51  ? 96  SER   C CB  1 
ATOM   1817 O  OG  . SER   B 1 90  ? 30.829 -11.076 23.336 1.00 15.96  ? 96  SER   C OG  1 
ATOM   1818 N  N   . HIS   B 1 91  ? 32.629 -14.196 23.368 1.00 13.10  ? 97  HIS   C N   1 
ATOM   1819 C  CA  . HIS   B 1 91  ? 32.132 -15.556 23.641 1.00 12.89  ? 97  HIS   C CA  1 
ATOM   1820 C  C   . HIS   B 1 91  ? 32.255 -16.434 22.375 1.00 12.34  ? 97  HIS   C C   1 
ATOM   1821 O  O   . HIS   B 1 91  ? 31.353 -17.242 22.117 1.00 12.68  ? 97  HIS   C O   1 
ATOM   1822 C  CB  . HIS   B 1 91  ? 30.674 -15.510 24.183 1.00 13.47  ? 97  HIS   C CB  1 
ATOM   1823 C  CG  . HIS   B 1 91  ? 30.565 -14.773 25.505 1.00 14.79  ? 97  HIS   C CG  1 
ATOM   1824 N  ND1 . HIS   B 1 91  ? 30.555 -15.443 26.707 1.00 17.44  ? 97  HIS   C ND1 1 
ATOM   1825 C  CD2 . HIS   B 1 91  ? 30.465 -13.437 25.746 1.00 15.77  ? 97  HIS   C CD2 1 
ATOM   1826 C  CE1 . HIS   B 1 91  ? 30.429 -14.510 27.652 1.00 18.52  ? 97  HIS   C CE1 1 
ATOM   1827 N  NE2 . HIS   B 1 91  ? 30.382 -13.285 27.119 1.00 18.25  ? 97  HIS   C NE2 1 
ATOM   1828 N  N   . LEU   B 1 92  ? 33.342 -16.269 21.623 1.00 11.89  ? 98  LEU   C N   1 
ATOM   1829 C  CA  . LEU   B 1 92  ? 33.529 -16.971 20.364 1.00 11.40  ? 98  LEU   C CA  1 
ATOM   1830 C  C   . LEU   B 1 92  ? 34.619 -18.037 20.545 1.00 11.55  ? 98  LEU   C C   1 
ATOM   1831 O  O   . LEU   B 1 92  ? 35.598 -17.821 21.263 1.00 12.60  ? 98  LEU   C O   1 
ATOM   1832 C  CB  . LEU   B 1 92  ? 33.991 -15.944 19.297 1.00 13.44  ? 98  LEU   C CB  1 
ATOM   1833 C  CG  . LEU   B 1 92  ? 34.105 -16.515 17.882 1.00 14.65  ? 98  LEU   C CG  1 
ATOM   1834 C  CD1 . LEU   B 1 92  ? 32.739 -16.864 17.324 1.00 14.80  ? 98  LEU   C CD1 1 
ATOM   1835 C  CD2 . LEU   B 1 92  ? 34.802 -15.508 16.930 1.00 16.03  ? 98  LEU   C CD2 1 
ATOM   1836 N  N   . MET   B 1 93  ? 34.409 -19.198 19.913 1.00 10.92  ? 99  MET   C N   1 
ATOM   1837 C  CA  . MET   B 1 93  ? 35.365 -20.324 19.966 1.00 10.32  ? 99  MET   C CA  1 
ATOM   1838 C  C   . MET   B 1 93  ? 35.772 -20.622 18.530 1.00 11.45  ? 99  MET   C C   1 
ATOM   1839 O  O   . MET   B 1 93  ? 34.898 -20.661 17.660 1.00 12.92  ? 99  MET   C O   1 
ATOM   1840 C  CB  . MET   B 1 93  ? 34.625 -21.562 20.551 1.00 12.14  ? 99  MET   C CB  1 
ATOM   1841 C  CG  . MET   B 1 93  ? 34.150 -21.298 21.974 1.00 13.34  ? 99  MET   C CG  1 
ATOM   1842 S  SD  . MET   B 1 93  ? 33.137 -22.609 22.590 1.00 15.06  ? 99  MET   C SD  1 
ATOM   1843 C  CE  . MET   B 1 93  ? 31.672 -22.446 21.484 1.00 15.77  ? 99  MET   C CE  1 
ATOM   1844 N  N   . LEU   B 1 94  ? 37.038 -20.895 18.258 1.00 11.21  ? 100 LEU   C N   1 
ATOM   1845 C  CA  . LEU   B 1 94  ? 37.491 -21.176 16.904 1.00 11.65  ? 100 LEU   C CA  1 
ATOM   1846 C  C   . LEU   B 1 94  ? 37.936 -22.638 16.757 1.00 11.06  ? 100 LEU   C C   1 
ATOM   1847 O  O   . LEU   B 1 94  ? 38.465 -23.244 17.701 1.00 12.19  ? 100 LEU   C O   1 
ATOM   1848 C  CB  . LEU   B 1 94  ? 38.744 -20.336 16.511 1.00 12.59  ? 100 LEU   C CB  1 
ATOM   1849 C  CG  . LEU   B 1 94  ? 38.574 -18.831 16.454 1.00 14.92  ? 100 LEU   C CG  1 
ATOM   1850 C  CD1 . LEU   B 1 94  ? 39.883 -18.158 16.058 1.00 18.53  ? 100 LEU   C CD1 1 
ATOM   1851 C  CD2 . LEU   B 1 94  ? 37.422 -18.393 15.492 1.00 15.91  ? 100 LEU   C CD2 1 
ATOM   1852 N  N   . ALA   B 1 95  ? 37.767 -23.157 15.559 1.00 11.35  ? 101 ALA   C N   1 
ATOM   1853 C  CA  . ALA   B 1 95  ? 38.310 -24.448 15.147 1.00 11.34  ? 101 ALA   C CA  1 
ATOM   1854 C  C   . ALA   B 1 95  ? 38.896 -24.320 13.707 1.00 11.18  ? 101 ALA   C C   1 
ATOM   1855 O  O   . ALA   B 1 95  ? 38.530 -23.394 12.959 1.00 11.41  ? 101 ALA   C O   1 
ATOM   1856 C  CB  . ALA   B 1 95  ? 37.226 -25.545 15.149 1.00 12.05  ? 101 ALA   C CB  1 
ATOM   1857 N  N   . VAL   B 1 96  ? 39.764 -25.247 13.312 1.00 11.69  ? 102 VAL   C N   1 
ATOM   1858 C  CA  . VAL   B 1 96  ? 40.233 -25.318 11.948 1.00 12.91  ? 102 VAL   C CA  1 
ATOM   1859 C  C   . VAL   B 1 96  ? 39.163 -26.066 11.132 1.00 13.17  ? 102 VAL   C C   1 
ATOM   1860 O  O   . VAL   B 1 96  ? 38.822 -27.235 11.446 1.00 14.15  ? 102 VAL   C O   1 
ATOM   1861 C  CB  . VAL   B 1 96  ? 41.612 -26.027 11.922 1.00 13.85  ? 102 VAL   C CB  1 
ATOM   1862 C  CG1 . VAL   B 1 96  ? 42.062 -26.185 10.481 1.00 16.08  ? 102 VAL   C CG1 1 
ATOM   1863 C  CG2 . VAL   B 1 96  ? 42.631 -25.241 12.747 1.00 14.58  ? 102 VAL   C CG2 1 
ATOM   1864 N  N   . GLY   B 1 97  ? 38.585 -25.384 10.160 1.00 14.18  ? 103 GLY   C N   1 
ATOM   1865 C  CA  . GLY   B 1 97  ? 37.506 -25.991 9.386  1.00 14.61  ? 103 GLY   C CA  1 
ATOM   1866 C  C   . GLY   B 1 97  ? 36.845 -25.019 8.462  1.00 14.23  ? 103 GLY   C C   1 
ATOM   1867 O  O   . GLY   B 1 97  ? 37.161 -23.813 8.457  1.00 16.68  ? 103 GLY   C O   1 
ATOM   1868 N  N   . HIS   B 1 98  ? 35.967 -25.554 7.622  1.00 14.80  ? 104 HIS   C N   1 
ATOM   1869 C  CA  . HIS   B 1 98  ? 35.287 -24.762 6.627  1.00 14.44  ? 104 HIS   C CA  1 
ATOM   1870 C  C   . HIS   B 1 98  ? 34.001 -24.071 7.147  1.00 13.41  ? 104 HIS   C C   1 
ATOM   1871 O  O   . HIS   B 1 98  ? 33.162 -24.725 7.815  1.00 13.16  ? 104 HIS   C O   1 
ATOM   1872 C  CB  . HIS   B 1 98  ? 34.951 -25.635 5.432  1.00 16.19  ? 104 HIS   C CB  1 
ATOM   1873 C  CG  . HIS   B 1 98  ? 34.408 -24.838 4.304  1.00 17.88  ? 104 HIS   C CG  1 
ATOM   1874 N  ND1 . HIS   B 1 98  ? 35.195 -23.900 3.629  1.00 20.79  ? 104 HIS   C ND1 1 
ATOM   1875 C  CD2 . HIS   B 1 98  ? 33.135 -24.786 3.828  1.00 19.06  ? 104 HIS   C CD2 1 
ATOM   1876 C  CE1 . HIS   B 1 98  ? 34.372 -23.325 2.759  1.00 22.39  ? 104 HIS   C CE1 1 
ATOM   1877 N  NE2 . HIS   B 1 98  ? 33.128 -23.844 2.831  1.00 22.27  ? 104 HIS   C NE2 1 
ATOM   1878 N  N   . SER   B 1 99  ? 33.774 -22.808 6.780  1.00 13.96  ? 105 SER   C N   1 
ATOM   1879 C  CA  . SER   B 1 99  ? 32.553 -22.065 7.172  1.00 14.21  ? 105 SER   C CA  1 
ATOM   1880 C  C   . SER   B 1 99  ? 32.325 -20.898 6.182  1.00 15.46  ? 105 SER   C C   1 
ATOM   1881 O  O   . SER   B 1 99  ? 33.206 -20.024 6.036  1.00 17.74  ? 105 SER   C O   1 
ATOM   1882 C  CB  . SER   B 1 99  ? 32.784 -21.492 8.565  1.00 15.66  ? 105 SER   C CB  1 
ATOM   1883 O  OG  . SER   B 1 99  ? 31.679 -20.664 8.930  1.00 15.63  ? 105 SER   C OG  1 
ATOM   1884 N  N   . GLU   B 1 100 ? 31.240 -20.926 5.502  1.00 15.77  ? 106 GLU   C N   1 
ATOM   1885 C  CA  . GLU   B 1 100 ? 30.796 -19.839 4.595  1.00 16.42  ? 106 GLU   C CA  1 
ATOM   1886 C  C   . GLU   B 1 100 ? 29.618 -19.156 5.260  1.00 14.81  ? 106 GLU   C C   1 
ATOM   1887 O  O   . GLU   B 1 100 ? 29.031 -19.689 6.206  1.00 14.32  ? 106 GLU   C O   1 
ATOM   1888 C  CB  . GLU   B 1 100 ? 30.290 -20.480 3.298  1.00 19.78  ? 106 GLU   C CB  1 
ATOM   1889 C  CG  . GLU   B 1 100 ? 31.406 -21.113 2.533  1.00 28.14  ? 106 GLU   C CG  1 
ATOM   1890 C  CD  . GLU   B 1 100 ? 30.946 -21.869 1.316  1.00 30.71  ? 106 GLU   C CD  1 
ATOM   1891 O  OE1 . GLU   B 1 100 ? 29.813 -21.642 0.826  1.00 37.01  ? 106 GLU   C OE1 1 
ATOM   1892 O  OE2 . GLU   B 1 100 ? 31.771 -22.662 0.827  1.00 32.61  ? 106 GLU   C OE2 1 
ATOM   1893 N  N   . PRO   B 1 101 ? 29.191 -17.958 4.790  1.00 15.37  ? 107 PRO   C N   1 
ATOM   1894 C  CA  . PRO   B 1 101 ? 28.055 -17.298 5.453  1.00 15.08  ? 107 PRO   C CA  1 
ATOM   1895 C  C   . PRO   B 1 101 ? 26.815 -18.177 5.608  1.00 15.12  ? 107 PRO   C C   1 
ATOM   1896 O  O   . PRO   B 1 101 ? 26.190 -18.098 6.679  1.00 15.40  ? 107 PRO   C O   1 
ATOM   1897 C  CB  . PRO   B 1 101 ? 27.773 -16.070 4.538  1.00 17.59  ? 107 PRO   C CB  1 
ATOM   1898 C  CG  . PRO   B 1 101 ? 29.059 -15.781 3.958  1.00 20.84  ? 107 PRO   C CG  1 
ATOM   1899 C  CD  . PRO   B 1 101 ? 29.811 -17.080 3.761  1.00 17.37  ? 107 PRO   C CD  1 
ATOM   1900 N  N   . GLY   B 1 102 ? 26.493 -19.015 4.604  1.00 14.68  ? 108 GLY   C N   1 
ATOM   1901 C  CA  . GLY   B 1 102 ? 25.279 -19.840 4.681  1.00 14.62  ? 108 GLY   C CA  1 
ATOM   1902 C  C   . GLY   B 1 102 ? 25.364 -20.925 5.748  1.00 14.25  ? 108 GLY   C C   1 
ATOM   1903 O  O   . GLY   B 1 102 ? 24.380 -21.617 6.027  1.00 15.31  ? 108 GLY   C O   1 
ATOM   1904 N  N   . ASP   B 1 103 ? 26.573 -21.191 6.283  1.00 12.59  ? 109 ASP   C N   1 
ATOM   1905 C  CA  . ASP   B 1 103 ? 26.757 -22.201 7.322  1.00 11.78  ? 109 ASP   C CA  1 
ATOM   1906 C  C   . ASP   B 1 103 ? 26.360 -21.713 8.688  1.00 11.68  ? 109 ASP   C C   1 
ATOM   1907 O  O   . ASP   B 1 103 ? 26.242 -22.498 9.645  1.00 11.51  ? 109 ASP   C O   1 
ATOM   1908 C  CB  . ASP   B 1 103 ? 28.236 -22.659 7.356  1.00 12.17  ? 109 ASP   C CB  1 
ATOM   1909 C  CG  . ASP   B 1 103 ? 28.553 -23.433 6.118  1.00 14.78  ? 109 ASP   C CG  1 
ATOM   1910 O  OD1 . ASP   B 1 103 ? 27.699 -24.217 5.682  1.00 15.53  ? 109 ASP   C OD1 1 
ATOM   1911 O  OD2 . ASP   B 1 103 ? 29.681 -23.283 5.600  1.00 15.43  ? 109 ASP   C OD2 1 
ATOM   1912 N  N   . CYS   B 1 104 ? 26.170 -20.373 8.886  1.00 10.60  ? 110 CYS   C N   1 
ATOM   1913 C  CA  . CYS   B 1 104 ? 25.744 -19.854 10.183 1.00 11.24  ? 110 CYS   C CA  1 
ATOM   1914 C  C   . CYS   B 1 104 ? 24.498 -20.555 10.674 1.00 11.56  ? 110 CYS   C C   1 
ATOM   1915 O  O   . CYS   B 1 104 ? 23.553 -20.766 9.911  1.00 13.08  ? 110 CYS   C O   1 
ATOM   1916 C  CB  . CYS   B 1 104 ? 25.529 -18.337 10.114 1.00 12.06  ? 110 CYS   C CB  1 
ATOM   1917 S  SG  . CYS   B 1 104 ? 27.069 -17.385 10.003 1.00 13.93  ? 110 CYS   C SG  1 
ATOM   1918 N  N   . GLY   B 1 105 ? 24.512 -20.915 11.939 1.00 9.99   ? 111 GLY   C N   1 
ATOM   1919 C  CA  . GLY   B 1 105 ? 23.375 -21.571 12.583 1.00 11.37  ? 111 GLY   C CA  1 
ATOM   1920 C  C   . GLY   B 1 105 ? 23.580 -23.073 12.713 1.00 11.33  ? 111 GLY   C C   1 
ATOM   1921 O  O   . GLY   B 1 105 ? 22.796 -23.727 13.422 1.00 12.38  ? 111 GLY   C O   1 
ATOM   1922 N  N   . GLY   B 1 106 ? 24.613 -23.654 12.052 1.00 10.87  ? 112 GLY   C N   1 
ATOM   1923 C  CA  . GLY   B 1 106 ? 24.908 -25.083 12.212 1.00 11.90  ? 112 GLY   C CA  1 
ATOM   1924 C  C   . GLY   B 1 106 ? 25.290 -25.377 13.661 1.00 10.68  ? 112 GLY   C C   1 
ATOM   1925 O  O   . GLY   B 1 106 ? 26.027 -24.583 14.286 1.00 10.83  ? 112 GLY   C O   1 
ATOM   1926 N  N   . ILE   B 1 107 ? 24.858 -26.511 14.185 1.00 9.96   ? 113 ILE   C N   1 
ATOM   1927 C  CA  . ILE   B 1 107 ? 25.121 -26.832 15.577 1.00 10.28  ? 113 ILE   C CA  1 
ATOM   1928 C  C   . ILE   B 1 107 ? 26.495 -27.469 15.762 1.00 9.91   ? 113 ILE   C C   1 
ATOM   1929 O  O   . ILE   B 1 107 ? 26.899 -28.321 14.992 1.00 9.96   ? 113 ILE   C O   1 
ATOM   1930 C  CB  . ILE   B 1 107 ? 23.989 -27.811 16.084 1.00 12.48  ? 113 ILE   C CB  1 
ATOM   1931 C  CG1 . ILE   B 1 107 ? 22.760 -26.859 16.530 1.00 16.17  ? 113 ILE   C CG1 1 
ATOM   1932 C  CG2 . ILE   B 1 107 ? 24.450 -28.667 17.291 1.00 12.99  ? 113 ILE   C CG2 1 
ATOM   1933 C  CD1 . ILE   B 1 107 ? 21.423 -27.575 16.862 1.00 20.68  ? 113 ILE   C CD1 1 
ATOM   1934 N  N   . LEU   B 1 108 ? 27.172 -27.043 16.840 1.00 8.75   ? 114 LEU   C N   1 
ATOM   1935 C  CA  . LEU   B 1 108 ? 28.341 -27.711 17.416 1.00 9.01   ? 114 LEU   C CA  1 
ATOM   1936 C  C   . LEU   B 1 108 ? 27.837 -28.469 18.668 1.00 9.19   ? 114 LEU   C C   1 
ATOM   1937 O  O   . LEU   B 1 108 ? 27.206 -27.873 19.534 1.00 9.35   ? 114 LEU   C O   1 
ATOM   1938 C  CB  . LEU   B 1 108 ? 29.382 -26.655 17.814 1.00 9.37   ? 114 LEU   C CB  1 
ATOM   1939 C  CG  . LEU   B 1 108 ? 30.592 -27.173 18.618 1.00 10.15  ? 114 LEU   C CG  1 
ATOM   1940 C  CD1 . LEU   B 1 108 ? 31.464 -28.091 17.763 1.00 11.84  ? 114 LEU   C CD1 1 
ATOM   1941 C  CD2 . LEU   B 1 108 ? 31.427 -25.991 19.139 1.00 11.93  ? 114 LEU   C CD2 1 
ATOM   1942 N  N   . ARG   B 1 109 ? 28.124 -29.767 18.738 1.00 9.26   ? 115 ARG   C N   1 
ATOM   1943 C  CA  . ARG   B 1 109 ? 27.643 -30.602 19.875 1.00 9.96   ? 115 ARG   C CA  1 
ATOM   1944 C  C   . ARG   B 1 109 ? 28.802 -31.417 20.433 1.00 10.26  ? 115 ARG   C C   1 
ATOM   1945 O  O   . ARG   B 1 109 ? 29.715 -31.832 19.716 1.00 11.21  ? 115 ARG   C O   1 
ATOM   1946 C  CB  . ARG   B 1 109 ? 26.505 -31.518 19.400 1.00 13.15  ? 115 ARG   C CB  1 
ATOM   1947 C  CG  . ARG   B 1 109 ? 26.971 -32.522 18.361 1.00 16.57  ? 115 ARG   C CG  1 
ATOM   1948 C  CD  . ARG   B 1 109 ? 25.826 -33.417 17.895 1.00 21.53  ? 115 ARG   C CD  1 
ATOM   1949 N  NE  . ARG   B 1 109 ? 24.983 -32.676 16.958 1.00 25.24  ? 115 ARG   C NE  1 
ATOM   1950 C  CZ  . ARG   B 1 109 ? 23.663 -32.630 17.017 1.00 32.78  ? 115 ARG   C CZ  1 
ATOM   1951 N  NH1 . ARG   B 1 109 ? 23.014 -33.290 17.967 1.00 35.19  ? 115 ARG   C NH1 1 
ATOM   1952 N  NH2 . ARG   B 1 109 ? 22.976 -31.932 16.118 1.00 35.11  ? 115 ARG   C NH2 1 
ATOM   1953 N  N   . CYS   B 1 110 ? 28.719 -31.676 21.733 1.00 10.49  ? 116 CYS   C N   1 
ATOM   1954 C  CA  . CYS   B 1 110 ? 29.689 -32.558 22.447 1.00 11.32  ? 116 CYS   C CA  1 
ATOM   1955 C  C   . CYS   B 1 110 ? 28.822 -33.647 23.115 1.00 12.56  ? 116 CYS   C C   1 
ATOM   1956 O  O   . CYS   B 1 110 ? 27.587 -33.744 22.908 1.00 12.87  ? 116 CYS   C O   1 
ATOM   1957 C  CB  . CYS   B 1 110 ? 30.490 -31.773 23.481 1.00 11.33  ? 116 CYS   C CB  1 
ATOM   1958 S  SG  . CYS   B 1 110 ? 29.446 -31.119 24.842 1.00 11.78  ? 116 CYS   C SG  1 
ATOM   1959 N  N   . GLN   B 1 111 ? 29.462 -34.502 23.955 1.00 13.23  ? 117 GLN   C N   1 
ATOM   1960 C  CA  . GLN   B 1 111 ? 28.697 -35.548 24.643 1.00 15.00  ? 117 GLN   C CA  1 
ATOM   1961 C  C   . GLN   B 1 111 ? 27.617 -34.999 25.574 1.00 15.85  ? 117 GLN   C C   1 
ATOM   1962 O  O   . GLN   B 1 111 ? 26.661 -35.731 25.922 1.00 17.39  ? 117 GLN   C O   1 
ATOM   1963 C  CB  . GLN   B 1 111 ? 29.629 -36.489 25.462 1.00 16.09  ? 117 GLN   C CB  1 
ATOM   1964 C  CG  . GLN   B 1 111 ? 30.327 -35.783 26.615 1.00 18.42  ? 117 GLN   C CG  1 
ATOM   1965 C  CD  . GLN   B 1 111 ? 31.248 -36.688 27.401 1.00 29.91  ? 117 GLN   C CD  1 
ATOM   1966 O  OE1 . GLN   B 1 111 ? 32.462 -36.710 27.182 1.00 33.71  ? 117 GLN   C OE1 1 
ATOM   1967 N  NE2 . GLN   B 1 111 ? 30.675 -37.404 28.346 1.00 30.77  ? 117 GLN   C NE2 1 
ATOM   1968 N  N   . HIS   B 1 112 ? 27.703 -33.709 25.982 1.00 13.26  ? 118 HIS   C N   1 
ATOM   1969 C  CA  . HIS   B 1 112 ? 26.713 -33.151 26.914 1.00 14.10  ? 118 HIS   C CA  1 
ATOM   1970 C  C   . HIS   B 1 112 ? 25.537 -32.449 26.253 1.00 13.79  ? 118 HIS   C C   1 
ATOM   1971 O  O   . HIS   B 1 112 ? 24.603 -32.048 26.952 1.00 15.33  ? 118 HIS   C O   1 
ATOM   1972 C  CB  . HIS   B 1 112 ? 27.425 -32.192 27.885 1.00 14.08  ? 118 HIS   C CB  1 
ATOM   1973 C  CG  . HIS   B 1 112 ? 28.621 -32.817 28.566 1.00 12.94  ? 118 HIS   C CG  1 
ATOM   1974 N  ND1 . HIS   B 1 112 ? 29.939 -32.542 28.185 1.00 12.83  ? 118 HIS   C ND1 1 
ATOM   1975 C  CD2 . HIS   B 1 112 ? 28.653 -33.644 29.646 1.00 16.29  ? 118 HIS   C CD2 1 
ATOM   1976 C  CE1 . HIS   B 1 112 ? 30.710 -33.255 29.007 1.00 14.16  ? 118 HIS   C CE1 1 
ATOM   1977 N  NE2 . HIS   B 1 112 ? 29.973 -33.908 29.904 1.00 17.56  ? 118 HIS   C NE2 1 
ATOM   1978 N  N   . GLY   B 1 113 ? 25.628 -32.210 24.945 1.00 12.91  ? 119 GLY   C N   1 
ATOM   1979 C  CA  . GLY   B 1 113 ? 24.565 -31.520 24.220 1.00 13.20  ? 119 GLY   C CA  1 
ATOM   1980 C  C   . GLY   B 1 113 ? 25.108 -30.447 23.297 1.00 11.83  ? 119 GLY   C C   1 
ATOM   1981 O  O   . GLY   B 1 113 ? 26.239 -30.527 22.805 1.00 11.49  ? 119 GLY   C O   1 
ATOM   1982 N  N   . VAL   B 1 114 ? 24.257 -29.438 23.028 1.00 11.44  ? 120 VAL   C N   1 
ATOM   1983 C  CA  . VAL   B 1 114 ? 24.588 -28.363 22.099 1.00 11.08  ? 120 VAL   C CA  1 
ATOM   1984 C  C   . VAL   B 1 114 ? 25.514 -27.373 22.789 1.00 11.36  ? 120 VAL   C C   1 
ATOM   1985 O  O   . VAL   B 1 114 ? 25.207 -26.811 23.847 1.00 12.01  ? 120 VAL   C O   1 
ATOM   1986 C  CB  . VAL   B 1 114 ? 23.297 -27.662 21.611 1.00 12.00  ? 120 VAL   C CB  1 
ATOM   1987 C  CG1 . VAL   B 1 114 ? 23.655 -26.450 20.735 1.00 13.40  ? 120 VAL   C CG1 1 
ATOM   1988 C  CG2 . VAL   B 1 114 ? 22.383 -28.652 20.870 1.00 13.20  ? 120 VAL   C CG2 1 
ATOM   1989 N  N   . VAL   B 1 115 ? 26.667 -27.116 22.175 1.00 9.44   ? 121 VAL   C N   1 
ATOM   1990 C  CA  . VAL   B 1 115 ? 27.681 -26.180 22.687 1.00 10.63  ? 121 VAL   C CA  1 
ATOM   1991 C  C   . VAL   B 1 115 ? 27.472 -24.764 22.158 1.00 11.38  ? 121 VAL   C C   1 
ATOM   1992 O  O   . VAL   B 1 115 ? 27.708 -23.774 22.875 1.00 11.39  ? 121 VAL   C O   1 
ATOM   1993 C  CB  . VAL   B 1 115 ? 29.087 -26.712 22.272 1.00 10.75  ? 121 VAL   C CB  1 
ATOM   1994 C  CG1 . VAL   B 1 115 ? 30.169 -25.713 22.639 1.00 12.32  ? 121 VAL   C CG1 1 
ATOM   1995 C  CG2 . VAL   B 1 115 ? 29.346 -28.096 22.879 1.00 12.15  ? 121 VAL   C CG2 1 
ATOM   1996 N  N   . GLY   B 1 116 ? 27.087 -24.667 20.888 1.00 10.64  ? 122 GLY   C N   1 
ATOM   1997 C  CA  . GLY   B 1 116 ? 26.917 -23.364 20.256 1.00 11.98  ? 122 GLY   C CA  1 
ATOM   1998 C  C   . GLY   B 1 116 ? 26.566 -23.528 18.790 1.00 10.30  ? 122 GLY   C C   1 
ATOM   1999 O  O   . GLY   B 1 116 ? 26.252 -24.645 18.337 1.00 10.96  ? 122 GLY   C O   1 
ATOM   2000 N  N   . ILE   B 1 117 ? 26.562 -22.370 18.053 1.00 9.76   ? 123 ILE   C N   1 
ATOM   2001 C  CA  . ILE   B 1 117 ? 26.196 -22.404 16.638 1.00 9.92   ? 123 ILE   C CA  1 
ATOM   2002 C  C   . ILE   B 1 117 ? 27.256 -21.669 15.825 1.00 9.75   ? 123 ILE   C C   1 
ATOM   2003 O  O   . ILE   B 1 117 ? 27.888 -20.707 16.299 1.00 10.94  ? 123 ILE   C O   1 
ATOM   2004 C  CB  . ILE   B 1 117 ? 24.775 -21.764 16.373 1.00 11.17  ? 123 ILE   C CB  1 
ATOM   2005 C  CG1 . ILE   B 1 117 ? 24.663 -20.379 17.045 1.00 12.28  ? 123 ILE   C CG1 1 
ATOM   2006 C  CG2 . ILE   B 1 117 ? 23.661 -22.715 16.786 1.00 12.17  ? 123 ILE   C CG2 1 
ATOM   2007 C  CD1 . ILE   B 1 117 ? 23.348 -19.566 16.576 1.00 12.70  ? 123 ILE   C CD1 1 
ATOM   2008 N  N   . VAL   B 1 118 ? 27.428 -22.102 14.567 1.00 9.49   ? 124 VAL   C N   1 
ATOM   2009 C  CA  . VAL   B 1 118 ? 28.365 -21.398 13.670 1.00 9.76   ? 124 VAL   C CA  1 
ATOM   2010 C  C   . VAL   B 1 118 ? 27.981 -19.919 13.569 1.00 10.45  ? 124 VAL   C C   1 
ATOM   2011 O  O   . VAL   B 1 118 ? 26.789 -19.583 13.352 1.00 10.04  ? 124 VAL   C O   1 
ATOM   2012 C  CB  . VAL   B 1 118 ? 28.356 -22.060 12.279 1.00 10.03  ? 124 VAL   C CB  1 
ATOM   2013 C  CG1 . VAL   B 1 118 ? 29.217 -21.294 11.293 1.00 10.72  ? 124 VAL   C CG1 1 
ATOM   2014 C  CG2 . VAL   B 1 118 ? 28.809 -23.522 12.342 1.00 11.25  ? 124 VAL   C CG2 1 
ATOM   2015 N  N   . SER   B 1 119 ? 29.000 -19.052 13.664 1.00 10.09  ? 125 SER   C N   1 
ATOM   2016 C  CA  . SER   B 1 119 ? 28.788 -17.596 13.535 1.00 10.57  ? 125 SER   C CA  1 
ATOM   2017 C  C   . SER   B 1 119 ? 29.798 -16.908 12.624 1.00 11.89  ? 125 SER   C C   1 
ATOM   2018 O  O   . SER   B 1 119 ? 29.468 -15.822 12.096 1.00 11.74  ? 125 SER   C O   1 
ATOM   2019 C  CB  . SER   B 1 119 ? 28.809 -16.997 14.941 1.00 12.17  ? 125 SER   C CB  1 
ATOM   2020 O  OG  . SER   B 1 119 ? 28.721 -15.563 14.915 1.00 13.04  ? 125 SER   C OG  1 
ATOM   2021 N  N   . THR   B 1 120 ? 31.061 -17.437 12.521 1.00 11.37  ? 126 THR   C N   1 
ATOM   2022 C  CA  . THR   B 1 120 ? 32.092 -16.771 11.717 1.00 11.39  ? 126 THR   C CA  1 
ATOM   2023 C  C   . THR   B 1 120 ? 32.785 -17.779 10.806 1.00 10.60  ? 126 THR   C C   1 
ATOM   2024 O  O   . THR   B 1 120 ? 32.728 -19.002 11.045 1.00 10.97  ? 126 THR   C O   1 
ATOM   2025 C  CB  . THR   B 1 120 ? 33.158 -16.047 12.599 1.00 11.97  ? 126 THR   C CB  1 
ATOM   2026 O  OG1 . THR   B 1 120 ? 34.009 -17.007 13.243 1.00 12.79  ? 126 THR   C OG1 1 
ATOM   2027 C  CG2 . THR   B 1 120 ? 32.555 -15.124 13.615 1.00 13.67  ? 126 THR   C CG2 1 
ATOM   2028 N  N   . GLY   B 1 121 ? 33.479 -17.278 9.799  1.00 12.01  ? 127 GLY   C N   1 
ATOM   2029 C  CA  . GLY   B 1 121 ? 34.259 -18.131 8.899  1.00 14.24  ? 127 GLY   C CA  1 
ATOM   2030 C  C   . GLY   B 1 121 ? 35.288 -17.352 8.129  1.00 17.82  ? 127 GLY   C C   1 
ATOM   2031 O  O   . GLY   B 1 121 ? 35.190 -16.148 8.012  1.00 21.61  ? 127 GLY   C O   1 
ATOM   2032 N  N   . GLY   B 1 122 ? 36.149 -18.066 7.450  1.00 21.18  ? 128 GLY   C N   1 
ATOM   2033 C  CA  . GLY   B 1 122 ? 37.221 -17.430 6.676  1.00 23.30  ? 128 GLY   C CA  1 
ATOM   2034 C  C   . GLY   B 1 122 ? 38.612 -17.817 7.181  1.00 22.91  ? 128 GLY   C C   1 
ATOM   2035 O  O   . GLY   B 1 122 ? 38.812 -18.228 8.323  1.00 22.23  ? 128 GLY   C O   1 
ATOM   2036 N  N   . ASN   B 1 123 ? 39.628 -17.635 6.319  1.00 21.86  ? 129 ASN   C N   1 
ATOM   2037 C  CA  . ASN   B 1 123 ? 41.036 -17.982 6.613  1.00 22.19  ? 129 ASN   C CA  1 
ATOM   2038 C  C   . ASN   B 1 123 ? 41.164 -19.443 7.088  1.00 20.20  ? 129 ASN   C C   1 
ATOM   2039 O  O   . ASN   B 1 123 ? 42.134 -19.768 7.786  1.00 23.37  ? 129 ASN   C O   1 
ATOM   2040 C  CB  . ASN   B 1 123 ? 41.687 -17.013 7.649  1.00 27.76  ? 129 ASN   C CB  1 
ATOM   2041 C  CG  . ASN   B 1 123 ? 42.664 -15.957 7.099  1.00 35.30  ? 129 ASN   C CG  1 
ATOM   2042 O  OD1 . ASN   B 1 123 ? 43.131 -16.010 5.951  1.00 36.99  ? 129 ASN   C OD1 1 
ATOM   2043 N  ND2 . ASN   B 1 123 ? 42.992 -14.938 7.901  1.00 38.24  ? 129 ASN   C ND2 1 
ATOM   2044 N  N   . GLY   B 1 124 ? 40.264 -20.337 6.655  1.00 18.19  ? 130 GLY   C N   1 
ATOM   2045 C  CA  . GLY   B 1 124 ? 40.343 -21.747 7.071  1.00 17.40  ? 130 GLY   C CA  1 
ATOM   2046 C  C   . GLY   B 1 124 ? 39.947 -22.024 8.510  1.00 15.47  ? 130 GLY   C C   1 
ATOM   2047 O  O   . GLY   B 1 124 ? 40.222 -23.104 9.025  1.00 15.62  ? 130 GLY   C O   1 
ATOM   2048 N  N   . LEU   B 1 125 ? 39.278 -21.067 9.147  1.00 14.17  ? 131 LEU   C N   1 
ATOM   2049 C  CA  . LEU   B 1 125 ? 38.808 -21.222 10.507 1.00 13.67  ? 131 LEU   C CA  1 
ATOM   2050 C  C   . LEU   B 1 125 ? 37.270 -21.121 10.514 1.00 13.87  ? 131 LEU   C C   1 
ATOM   2051 O  O   . LEU   B 1 125 ? 36.632 -20.465 9.634  1.00 16.33  ? 131 LEU   C O   1 
ATOM   2052 C  CB  . LEU   B 1 125 ? 39.393 -20.121 11.406 1.00 15.99  ? 131 LEU   C CB  1 
ATOM   2053 C  CG  . LEU   B 1 125 ? 40.940 -20.109 11.493 1.00 18.16  ? 131 LEU   C CG  1 
ATOM   2054 C  CD1 . LEU   B 1 125 ? 41.478 -18.721 11.879 1.00 22.86  ? 131 LEU   C CD1 1 
ATOM   2055 C  CD2 . LEU   B 1 125 ? 41.454 -21.240 12.349 1.00 18.30  ? 131 LEU   C CD2 1 
ATOM   2056 N  N   . VAL   B 1 126 ? 36.677 -21.758 11.483 1.00 10.94  ? 132 VAL   C N   1 
ATOM   2057 C  CA  . VAL   B 1 126 ? 35.222 -21.663 11.736 1.00 10.47  ? 132 VAL   C CA  1 
ATOM   2058 C  C   . VAL   B 1 126 ? 35.067 -21.185 13.181 1.00 10.51  ? 132 VAL   C C   1 
ATOM   2059 O  O   . VAL   B 1 126 ? 35.730 -21.703 14.095 1.00 10.73  ? 132 VAL   C O   1 
ATOM   2060 C  CB  . VAL   B 1 126 ? 34.493 -23.006 11.487 1.00 10.90  ? 132 VAL   C CB  1 
ATOM   2061 C  CG1 . VAL   B 1 126 ? 35.132 -24.182 12.171 1.00 13.00  ? 132 VAL   C CG1 1 
ATOM   2062 C  CG2 . VAL   B 1 126 ? 32.981 -22.918 11.833 1.00 12.20  ? 132 VAL   C CG2 1 
ATOM   2063 N  N   . GLY   B 1 127 ? 34.186 -20.212 13.392 1.00 10.61  ? 133 GLY   C N   1 
ATOM   2064 C  CA  . GLY   B 1 127 ? 33.939 -19.707 14.745 1.00 10.62  ? 133 GLY   C CA  1 
ATOM   2065 C  C   . GLY   B 1 127 ? 32.510 -20.021 15.177 1.00 10.53  ? 133 GLY   C C   1 
ATOM   2066 O  O   . GLY   B 1 127 ? 31.559 -19.899 14.375 1.00 10.88  ? 133 GLY   C O   1 
ATOM   2067 N  N   . PHE   B 1 128 ? 32.379 -20.394 16.429 1.00 9.80   ? 134 PHE   C N   1 
ATOM   2068 C  CA  . PHE   B 1 128 ? 31.097 -20.774 17.070 1.00 9.77   ? 134 PHE   C CA  1 
ATOM   2069 C  C   . PHE   B 1 128 ? 30.780 -19.822 18.183 1.00 9.96   ? 134 PHE   C C   1 
ATOM   2070 O  O   . PHE   B 1 128 ? 31.630 -19.580 19.063 1.00 10.95  ? 134 PHE   C O   1 
ATOM   2071 C  CB  . PHE   B 1 128 ? 31.155 -22.215 17.635 1.00 10.23  ? 134 PHE   C CB  1 
ATOM   2072 C  CG  . PHE   B 1 128 ? 31.693 -23.233 16.635 1.00 9.94   ? 134 PHE   C CG  1 
ATOM   2073 C  CD1 . PHE   B 1 128 ? 30.852 -23.824 15.699 1.00 10.53  ? 134 PHE   C CD1 1 
ATOM   2074 C  CD2 . PHE   B 1 128 ? 33.041 -23.590 16.633 1.00 10.81  ? 134 PHE   C CD2 1 
ATOM   2075 C  CE1 . PHE   B 1 128 ? 31.334 -24.787 14.825 1.00 10.53  ? 134 PHE   C CE1 1 
ATOM   2076 C  CE2 . PHE   B 1 128 ? 33.528 -24.558 15.738 1.00 11.36  ? 134 PHE   C CE2 1 
ATOM   2077 C  CZ  . PHE   B 1 128 ? 32.681 -25.141 14.837 1.00 11.13  ? 134 PHE   C CZ  1 
ATOM   2078 N  N   . ALA   B 1 129 ? 29.511 -19.357 18.210 1.00 10.38  ? 135 ALA   C N   1 
ATOM   2079 C  CA  . ALA   B 1 129 ? 29.016 -18.545 19.327 1.00 10.39  ? 135 ALA   C CA  1 
ATOM   2080 C  C   . ALA   B 1 129 ? 28.619 -19.528 20.462 1.00 11.41  ? 135 ALA   C C   1 
ATOM   2081 O  O   . ALA   B 1 129 ? 27.710 -20.366 20.294 1.00 11.10  ? 135 ALA   C O   1 
ATOM   2082 C  CB  . ALA   B 1 129 ? 27.793 -17.755 18.876 1.00 11.29  ? 135 ALA   C CB  1 
ATOM   2083 N  N   . ASP   B 1 130 ? 29.317 -19.449 21.608 1.00 10.67  ? 136 ASP   C N   1 
ATOM   2084 C  CA  . ASP   B 1 130 ? 29.022 -20.342 22.732 1.00 11.02  ? 136 ASP   C CA  1 
ATOM   2085 C  C   . ASP   B 1 130 ? 27.677 -19.990 23.336 1.00 11.68  ? 136 ASP   C C   1 
ATOM   2086 O  O   . ASP   B 1 130 ? 27.297 -18.807 23.419 1.00 12.15  ? 136 ASP   C O   1 
ATOM   2087 C  CB  . ASP   B 1 130 ? 30.106 -20.122 23.811 1.00 12.66  ? 136 ASP   C CB  1 
ATOM   2088 C  CG  . ASP   B 1 130 ? 29.992 -21.039 25.004 1.00 15.83  ? 136 ASP   C CG  1 
ATOM   2089 O  OD1 . ASP   B 1 130 ? 29.867 -22.250 24.811 1.00 14.97  ? 136 ASP   C OD1 1 
ATOM   2090 O  OD2 . ASP   B 1 130 ? 29.921 -20.513 26.140 1.00 18.80  ? 136 ASP   C OD2 1 
ATOM   2091 N  N   . VAL   B 1 131 ? 26.978 -21.004 23.847 1.00 11.57  ? 137 VAL   C N   1 
ATOM   2092 C  CA  . VAL   B 1 131 ? 25.721 -20.825 24.609 1.00 11.80  ? 137 VAL   C CA  1 
ATOM   2093 C  C   . VAL   B 1 131 ? 25.770 -21.508 25.971 1.00 12.73  ? 137 VAL   C C   1 
ATOM   2094 O  O   . VAL   B 1 131 ? 24.793 -21.433 26.721 1.00 12.83  ? 137 VAL   C O   1 
ATOM   2095 C  CB  . VAL   B 1 131 ? 24.445 -21.286 23.849 1.00 12.64  ? 137 VAL   C CB  1 
ATOM   2096 C  CG1 . VAL   B 1 131 ? 24.260 -20.456 22.560 1.00 12.82  ? 137 VAL   C CG1 1 
ATOM   2097 C  CG2 . VAL   B 1 131 ? 24.481 -22.763 23.522 1.00 12.67  ? 137 VAL   C CG2 1 
ATOM   2098 N  N   . ARG   B 1 132 ? 26.898 -22.151 26.325 1.00 12.23  ? 138 ARG   C N   1 
ATOM   2099 C  CA  . ARG   B 1 132 ? 26.975 -22.935 27.590 1.00 12.04  ? 138 ARG   C CA  1 
ATOM   2100 C  C   . ARG   B 1 132 ? 26.914 -22.107 28.840 1.00 12.55  ? 138 ARG   C C   1 
ATOM   2101 O  O   . ARG   B 1 132 ? 26.601 -22.681 29.898 1.00 14.22  ? 138 ARG   C O   1 
ATOM   2102 C  CB  . ARG   B 1 132 ? 28.239 -23.799 27.572 1.00 10.98  ? 138 ARG   C CB  1 
ATOM   2103 C  CG  . ARG   B 1 132 ? 28.219 -24.861 26.440 1.00 11.78  ? 138 ARG   C CG  1 
ATOM   2104 C  CD  . ARG   B 1 132 ? 29.537 -25.625 26.476 1.00 12.25  ? 138 ARG   C CD  1 
ATOM   2105 N  NE  . ARG   B 1 132 ? 30.638 -24.729 26.084 1.00 11.78  ? 138 ARG   C NE  1 
ATOM   2106 C  CZ  . ARG   B 1 132 ? 31.886 -25.121 25.928 1.00 12.59  ? 138 ARG   C CZ  1 
ATOM   2107 N  NH1 . ARG   B 1 132 ? 32.258 -26.362 26.276 1.00 12.60  ? 138 ARG   C NH1 1 
ATOM   2108 N  NH2 . ARG   B 1 132 ? 32.793 -24.277 25.444 1.00 13.02  ? 138 ARG   C NH2 1 
ATOM   2109 N  N   . ASP   B 1 133 ? 27.211 -20.819 28.765 1.00 12.62  ? 139 ASP   C N   1 
ATOM   2110 C  CA  . ASP   B 1 133 ? 27.152 -19.947 29.936 1.00 13.08  ? 139 ASP   C CA  1 
ATOM   2111 C  C   . ASP   B 1 133 ? 25.723 -19.404 30.162 1.00 14.50  ? 139 ASP   C C   1 
ATOM   2112 O  O   . ASP   B 1 133 ? 25.500 -18.768 31.209 1.00 15.61  ? 139 ASP   C O   1 
ATOM   2113 C  CB  . ASP   B 1 133 ? 28.126 -18.752 29.789 1.00 14.56  ? 139 ASP   C CB  1 
ATOM   2114 C  CG  . ASP   B 1 133 ? 27.771 -17.831 28.643 1.00 17.30  ? 139 ASP   C CG  1 
ATOM   2115 O  OD1 . ASP   B 1 133 ? 27.429 -18.330 27.564 1.00 16.46  ? 139 ASP   C OD1 1 
ATOM   2116 O  OD2 . ASP   B 1 133 ? 27.784 -16.570 28.846 1.00 20.45  ? 139 ASP   C OD2 1 
ATOM   2117 N  N   . LEU   B 1 134 ? 24.776 -19.608 29.207 1.00 13.83  ? 140 LEU   C N   1 
ATOM   2118 C  CA  . LEU   B 1 134 ? 23.410 -19.027 29.310 1.00 13.33  ? 140 LEU   C CA  1 
ATOM   2119 C  C   . LEU   B 1 134 ? 22.549 -19.997 30.082 1.00 14.34  ? 140 LEU   C C   1 
ATOM   2120 O  O   . LEU   B 1 134 ? 21.749 -20.744 29.527 1.00 14.02  ? 140 LEU   C O   1 
ATOM   2121 C  CB  . LEU   B 1 134 ? 22.869 -18.792 27.888 1.00 13.18  ? 140 LEU   C CB  1 
ATOM   2122 C  CG  . LEU   B 1 134 ? 23.710 -17.815 27.023 1.00 13.55  ? 140 LEU   C CG  1 
ATOM   2123 C  CD1 . LEU   B 1 134 ? 23.139 -17.732 25.574 1.00 14.95  ? 140 LEU   C CD1 1 
ATOM   2124 C  CD2 . LEU   B 1 134 ? 23.812 -16.423 27.658 1.00 15.93  ? 140 LEU   C CD2 1 
ATOM   2125 N  N   . LEU   B 1 135 ? 22.764 -20.034 31.417 1.00 14.86  ? 141 LEU   C N   1 
ATOM   2126 C  CA  . LEU   B 1 135 ? 22.125 -21.080 32.247 1.00 15.51  ? 141 LEU   C CA  1 
ATOM   2127 C  C   . LEU   B 1 135 ? 20.614 -20.987 32.281 1.00 15.76  ? 141 LEU   C C   1 
ATOM   2128 O  O   . LEU   B 1 135 ? 19.920 -22.000 32.492 1.00 16.63  ? 141 LEU   C O   1 
ATOM   2129 C  CB  . LEU   B 1 135 ? 22.699 -21.108 33.684 1.00 15.83  ? 141 LEU   C CB  1 
ATOM   2130 C  CG  . LEU   B 1 135 ? 24.245 -21.115 33.763 1.00 16.43  ? 141 LEU   C CG  1 
ATOM   2131 C  CD1 . LEU   B 1 135 ? 24.756 -21.147 35.233 1.00 17.86  ? 141 LEU   C CD1 1 
ATOM   2132 C  CD2 . LEU   B 1 135 ? 24.908 -22.247 32.954 1.00 16.98  ? 141 LEU   C CD2 1 
ATOM   2133 N  N   . TRP   B 1 136 ? 20.093 -19.769 32.099 1.00 15.19  ? 142 TRP   C N   1 
ATOM   2134 C  CA  . TRP   B 1 136 ? 18.655 -19.524 32.134 1.00 15.73  ? 142 TRP   C CA  1 
ATOM   2135 C  C   . TRP   B 1 136 ? 17.930 -20.198 30.977 1.00 16.47  ? 142 TRP   C C   1 
ATOM   2136 O  O   . TRP   B 1 136 ? 16.697 -20.350 31.054 1.00 18.51  ? 142 TRP   C O   1 
ATOM   2137 C  CB  . TRP   B 1 136 ? 18.385 -18.010 32.128 1.00 16.42  ? 142 TRP   C CB  1 
ATOM   2138 C  CG  . TRP   B 1 136 ? 19.079 -17.261 31.033 1.00 16.46  ? 142 TRP   C CG  1 
ATOM   2139 C  CD1 . TRP   B 1 136 ? 20.257 -16.583 31.116 1.00 17.29  ? 142 TRP   C CD1 1 
ATOM   2140 C  CD2 . TRP   B 1 136 ? 18.567 -17.019 29.704 1.00 16.38  ? 142 TRP   C CD2 1 
ATOM   2141 N  NE1 . TRP   B 1 136 ? 20.549 -15.987 29.893 1.00 17.50  ? 142 TRP   C NE1 1 
ATOM   2142 C  CE2 . TRP   B 1 136 ? 19.524 -16.244 29.015 1.00 16.63  ? 142 TRP   C CE2 1 
ATOM   2143 C  CE3 . TRP   B 1 136 ? 17.411 -17.404 29.042 1.00 16.11  ? 142 TRP   C CE3 1 
ATOM   2144 C  CZ2 . TRP   B 1 136 ? 19.339 -15.837 27.675 1.00 17.25  ? 142 TRP   C CZ2 1 
ATOM   2145 C  CZ3 . TRP   B 1 136 ? 17.212 -16.996 27.731 1.00 17.01  ? 142 TRP   C CZ3 1 
ATOM   2146 C  CH2 . TRP   B 1 136 ? 18.173 -16.226 27.062 1.00 17.43  ? 142 TRP   C CH2 1 
ATOM   2147 N  N   . LEU   B 1 137 ? 18.631 -20.659 29.921 1.00 15.92  ? 143 LEU   C N   1 
ATOM   2148 C  CA  . LEU   B 1 137 ? 17.954 -21.407 28.853 1.00 16.26  ? 143 LEU   C CA  1 
ATOM   2149 C  C   . LEU   B 1 137 ? 17.332 -22.710 29.400 1.00 19.47  ? 143 LEU   C C   1 
ATOM   2150 O  O   . LEU   B 1 137 ? 16.410 -23.251 28.782 1.00 20.72  ? 143 LEU   C O   1 
ATOM   2151 C  CB  . LEU   B 1 137 ? 18.917 -21.746 27.709 1.00 15.18  ? 143 LEU   C CB  1 
ATOM   2152 C  CG  . LEU   B 1 137 ? 19.352 -20.557 26.835 1.00 14.48  ? 143 LEU   C CG  1 
ATOM   2153 C  CD1 . LEU   B 1 137 ? 20.526 -20.977 25.923 1.00 15.48  ? 143 LEU   C CD1 1 
ATOM   2154 C  CD2 . LEU   B 1 137 ? 18.188 -20.036 25.972 1.00 16.39  ? 143 LEU   C CD2 1 
ATOM   2155 N  N   . ASP   B 1 138 ? 17.851 -23.232 30.558 1.00 18.08  ? 144 ASP   C N   1 
ATOM   2156 C  CA  . ASP   B 1 138 ? 17.400 -24.507 31.160 1.00 19.73  ? 144 ASP   C CA  1 
ATOM   2157 C  C   . ASP   B 1 138 ? 16.149 -24.371 32.028 1.00 22.41  ? 144 ASP   C C   1 
ATOM   2158 O  O   . ASP   B 1 138 ? 15.728 -25.382 32.614 1.00 23.66  ? 144 ASP   C O   1 
ATOM   2159 C  CB  . ASP   B 1 138 ? 18.501 -25.159 32.031 1.00 18.83  ? 144 ASP   C CB  1 
ATOM   2160 C  CG  . ASP   B 1 138 ? 19.753 -25.562 31.278 1.00 20.65  ? 144 ASP   C CG  1 
ATOM   2161 O  OD1 . ASP   B 1 138 ? 19.725 -25.582 30.032 1.00 20.71  ? 144 ASP   C OD1 1 
ATOM   2162 O  OD2 . ASP   B 1 138 ? 20.767 -25.846 31.943 1.00 24.70  ? 144 ASP   C OD2 1 
ATOM   2163 N  N   . GLU   B 1 139 ? 15.580 -23.178 32.156 1.00 23.45  ? 145 GLU   C N   1 
ATOM   2164 C  CA  . GLU   B 1 139 ? 14.411 -22.970 33.028 1.00 28.00  ? 145 GLU   C CA  1 
ATOM   2165 C  C   . GLU   B 1 139 ? 13.467 -21.852 32.539 1.00 31.73  ? 145 GLU   C C   1 
ATOM   2166 O  O   . GLU   B 1 139 ? 13.784 -21.160 31.580 1.00 32.04  ? 145 GLU   C O   1 
ATOM   2167 C  CB  . GLU   B 1 139 ? 14.950 -22.610 34.426 1.00 33.18  ? 145 GLU   C CB  1 
ATOM   2168 C  CG  . GLU   B 1 139 ? 15.730 -21.307 34.403 1.00 42.01  ? 145 GLU   C CG  1 
ATOM   2169 C  CD  . GLU   B 1 139 ? 16.775 -21.116 35.483 1.00 53.68  ? 145 GLU   C CD  1 
ATOM   2170 O  OE1 . GLU   B 1 139 ? 17.295 -19.983 35.608 1.00 57.05  ? 145 GLU   C OE1 1 
ATOM   2171 O  OE2 . GLU   B 1 139 ? 17.065 -22.094 36.209 1.00 56.60  ? 145 GLU   C OE2 1 
ATOM   2172 N  N   . GLU   B 1 140 ? 12.333 -21.626 33.260 1.00 34.84  ? 146 GLU   C N   1 
ATOM   2173 C  CA  . GLU   B 1 140 ? 11.407 -20.482 33.091 1.00 37.70  ? 146 GLU   C CA  1 
ATOM   2174 C  C   . GLU   B 1 140 ? 11.150 -20.124 31.639 1.00 39.87  ? 146 GLU   C C   1 
ATOM   2175 O  O   . GLU   B 1 140 ? 10.470 -19.151 31.326 1.00 41.19  ? 146 GLU   C O   1 
ATOM   2176 C  CB  . GLU   B 1 140 ? 11.972 -19.293 33.907 1.00 40.85  ? 146 GLU   C CB  1 
ATOM   2177 C  CG  . GLU   B 1 140 ? 11.530 -17.871 33.567 1.00 49.43  ? 146 GLU   C CG  1 
ATOM   2178 C  CD  . GLU   B 1 140 ? 10.137 -17.451 33.991 1.00 58.34  ? 146 GLU   C CD  1 
ATOM   2179 O  OE1 . GLU   B 1 140 ? 9.584  -16.537 33.338 1.00 61.32  ? 146 GLU   C OE1 1 
ATOM   2180 O  OE2 . GLU   B 1 140 ? 9.598  -18.029 34.962 1.00 61.40  ? 146 GLU   C OE2 1 
HETATM 2181 C  C4  . A1B3C C 2 .   ? 5.989  13.292  25.627 1.00 42.26  ? 201 A1B3C A C4  1 
HETATM 2182 C  C5  . A1B3C C 2 .   ? 6.670  14.144  24.779 1.00 41.66  ? 201 A1B3C A C5  1 
HETATM 2183 C  C6  . A1B3C C 2 .   ? 7.732  13.689  24.003 1.00 40.45  ? 201 A1B3C A C6  1 
HETATM 2184 C  C7  . A1B3C C 2 .   ? 8.687  14.693  23.413 1.00 38.60  ? 201 A1B3C A C7  1 
HETATM 2185 C  C8  . A1B3C C 2 .   ? 8.359  15.011  21.969 1.00 35.28  ? 201 A1B3C A C8  1 
HETATM 2186 C  C10 . A1B3C C 2 .   ? 11.554 16.486  21.459 1.00 35.46  ? 201 A1B3C A C10 1 
HETATM 2187 C  C13 . A1B3C C 2 .   ? 10.269 16.037  17.911 1.00 34.28  ? 201 A1B3C A C13 1 
HETATM 2188 F  F1  . A1B3C C 2 .   ? 10.057 17.361  17.658 1.00 35.78  ? 201 A1B3C A F1  1 
HETATM 2189 F  F   . A1B3C C 2 .   ? 11.455 15.740  17.338 1.00 31.90  ? 201 A1B3C A F   1 
HETATM 2190 C  C12 . A1B3C C 2 .   ? 10.354 15.810  19.336 1.00 34.97  ? 201 A1B3C A C12 1 
HETATM 2191 C  C11 . A1B3C C 2 .   ? 11.490 16.635  19.950 1.00 35.63  ? 201 A1B3C A C11 1 
HETATM 2192 C  C9  . A1B3C C 2 .   ? 10.186 16.717  22.085 1.00 36.31  ? 201 A1B3C A C9  1 
HETATM 2193 C  C14 . A1B3C C 2 .   ? 9.043  16.219  19.970 1.00 34.77  ? 201 A1B3C A C14 1 
HETATM 2194 N  N   . A1B3C C 2 .   ? 9.146  15.936  21.399 1.00 35.83  ? 201 A1B3C A N   1 
HETATM 2195 O  O   . A1B3C C 2 .   ? 7.415  14.516  21.390 1.00 31.06  ? 201 A1B3C A O   1 
HETATM 2196 C  C1  . A1B3C C 2 .   ? 8.016  12.320  23.998 1.00 40.28  ? 201 A1B3C A C1  1 
HETATM 2197 S  S   . A1B3C C 2 .   ? 9.054  11.757  22.674 1.00 38.62  ? 201 A1B3C A S   1 
HETATM 2198 C  C   . A1B3C C 2 .   ? 9.807  10.269  23.254 1.00 37.54  ? 201 A1B3C A C   1 
HETATM 2199 C  C3  . A1B3C C 2 .   ? 6.350  11.979  25.702 1.00 42.04  ? 201 A1B3C A C3  1 
HETATM 2200 C  C2  . A1B3C C 2 .   ? 7.348  11.481  24.876 1.00 41.41  ? 201 A1B3C A C2  1 
HETATM 2201 ZN ZN  . ZN    D 3 .   ? 10.944 -3.737  5.779  1.00 18.66  2 202 ZN    A ZN  1 
HETATM 2202 S  S   . DMS   E 4 .   ? 19.722 -1.616  24.185 1.00 89.40  ? 203 DMS   A S   1 
HETATM 2203 O  O   . DMS   E 4 .   ? 20.028 -0.157  23.998 1.00 89.36  ? 203 DMS   A O   1 
HETATM 2204 C  C1  . DMS   E 4 .   ? 18.380 -2.049  23.044 1.00 89.30  ? 203 DMS   A C1  1 
HETATM 2205 C  C2  . DMS   E 4 .   ? 21.015 -2.571  23.343 1.00 89.44  ? 203 DMS   A C2  1 
HETATM 2206 ZN ZN  . ZN    F 3 .   ? 30.645 -31.188 26.777 1.00 12.59  2 201 ZN    C ZN  1 
HETATM 2207 S  S   . DMS   G 4 .   ? 21.050 -32.493 10.170 1.00 64.24  ? 202 DMS   C S   1 
HETATM 2208 O  O   . DMS   G 4 .   ? 21.778 -32.842 8.910  1.00 64.66  ? 202 DMS   C O   1 
HETATM 2209 C  C1  . DMS   G 4 .   ? 22.227 -32.377 11.552 1.00 64.34  ? 202 DMS   C C1  1 
HETATM 2210 C  C2  . DMS   G 4 .   ? 20.748 -30.701 10.074 1.00 64.05  ? 202 DMS   C C2  1 
HETATM 2211 S  S   . DMS   H 4 .   ? 27.608 -4.983  7.187  1.00 104.98 ? 203 DMS   C S   1 
HETATM 2212 O  O   . DMS   H 4 .   ? 27.103 -4.471  8.505  1.00 104.94 ? 203 DMS   C O   1 
HETATM 2213 C  C1  . DMS   H 4 .   ? 26.219 -4.979  6.023  1.00 104.99 ? 203 DMS   C C1  1 
HETATM 2214 C  C2  . DMS   H 4 .   ? 28.525 -3.639  6.389  1.00 105.02 ? 203 DMS   C C2  1 
HETATM 2215 O  O   . HOH   I 5 .   ? 12.234 16.573  28.352 1.00 30.00  ? 301 HOH   A O   1 
HETATM 2216 O  O   . HOH   I 5 .   ? 35.408 -3.843  7.987  1.00 23.10  ? 302 HOH   A O   1 
HETATM 2217 O  O   . HOH   I 5 .   ? 11.233 8.993   4.402  1.00 23.02  ? 303 HOH   A O   1 
HETATM 2218 O  O   . HOH   I 5 .   ? 2.055  22.824  21.772 1.00 31.83  ? 304 HOH   A O   1 
HETATM 2219 O  O   . HOH   I 5 .   ? 27.768 8.099   1.580  1.00 32.89  ? 305 HOH   A O   1 
HETATM 2220 O  O   . HOH   I 5 .   ? 8.752  -3.040  0.584  1.00 34.14  ? 306 HOH   A O   1 
HETATM 2221 O  O   . HOH   I 5 .   ? 37.487 14.976  14.198 1.00 44.51  ? 307 HOH   A O   1 
HETATM 2222 O  O   . HOH   I 5 .   ? 30.495 10.494  15.517 1.00 29.56  ? 308 HOH   A O   1 
HETATM 2223 O  O   . HOH   I 5 .   ? 12.419 22.218  13.055 1.00 34.91  ? 309 HOH   A O   1 
HETATM 2224 O  O   . HOH   I 5 .   ? 10.571 10.108  31.440 1.00 25.34  ? 310 HOH   A O   1 
HETATM 2225 O  O   . HOH   I 5 .   ? 35.468 7.935   9.623  1.00 48.41  ? 311 HOH   A O   1 
HETATM 2226 O  O   . HOH   I 5 .   ? 6.100  2.319   5.491  1.00 25.89  ? 312 HOH   A O   1 
HETATM 2227 O  O   . HOH   I 5 .   ? 5.555  17.864  24.250 1.00 49.07  ? 313 HOH   A O   1 
HETATM 2228 O  O   . HOH   I 5 .   ? 29.544 22.231  19.470 1.00 27.49  ? 314 HOH   A O   1 
HETATM 2229 O  O   . HOH   I 5 .   ? 23.426 21.683  7.329  1.00 24.19  ? 315 HOH   A O   1 
HETATM 2230 O  O   . HOH   I 5 .   ? 17.467 0.945   28.265 1.00 24.93  ? 316 HOH   A O   1 
HETATM 2231 O  O   . HOH   I 5 .   ? 3.008  9.508   9.048  1.00 27.30  ? 317 HOH   A O   1 
HETATM 2232 O  O   . HOH   I 5 .   ? 28.118 3.211   4.876  1.00 33.58  ? 318 HOH   A O   1 
HETATM 2233 O  O   . HOH   I 5 .   ? 13.883 2.939   1.214  1.00 19.00  ? 319 HOH   A O   1 
HETATM 2234 O  O   . HOH   I 5 .   ? 7.464  20.169  17.600 1.00 24.53  ? 320 HOH   A O   1 
HETATM 2235 O  O   . HOH   I 5 .   ? 33.850 -2.305  13.691 1.00 32.38  ? 321 HOH   A O   1 
HETATM 2236 O  O   . HOH   I 5 .   ? 36.758 2.445   10.181 1.00 37.22  ? 322 HOH   A O   1 
HETATM 2237 O  O   . HOH   I 5 .   ? 21.914 2.333   -0.973 1.00 33.72  ? 323 HOH   A O   1 
HETATM 2238 O  O   . HOH   I 5 .   ? 19.386 10.050  19.705 1.00 12.90  ? 324 HOH   A O   1 
HETATM 2239 O  O   . HOH   I 5 .   ? 0.408  -0.826  19.491 1.00 21.19  ? 325 HOH   A O   1 
HETATM 2240 O  O   . HOH   I 5 .   ? 10.840 5.744   3.442  1.00 23.08  ? 326 HOH   A O   1 
HETATM 2241 O  O   . HOH   I 5 .   ? 23.304 11.747  22.106 1.00 33.68  ? 327 HOH   A O   1 
HETATM 2242 O  O   . HOH   I 5 .   ? -0.054 1.326   15.915 1.00 12.64  ? 328 HOH   A O   1 
HETATM 2243 O  O   . HOH   I 5 .   ? 4.717  -3.645  28.933 1.00 29.55  ? 329 HOH   A O   1 
HETATM 2244 O  O   . HOH   I 5 .   ? 4.209  9.371   28.028 1.00 43.39  ? 330 HOH   A O   1 
HETATM 2245 O  O   . HOH   I 5 .   ? 3.843  -8.068  9.816  1.00 47.76  ? 331 HOH   A O   1 
HETATM 2246 O  O   . HOH   I 5 .   ? 33.786 14.133  9.546  1.00 30.75  ? 332 HOH   A O   1 
HETATM 2247 O  O   . HOH   I 5 .   ? 2.640  -2.833  20.847 1.00 24.40  ? 333 HOH   A O   1 
HETATM 2248 O  O   . HOH   I 5 .   ? 14.024 13.796  24.038 1.00 22.74  ? 334 HOH   A O   1 
HETATM 2249 O  O   . HOH   I 5 .   ? 20.954 -4.163  14.199 1.00 16.09  ? 335 HOH   A O   1 
HETATM 2250 O  O   . HOH   I 5 .   ? 4.234  0.426   24.053 1.00 19.00  ? 336 HOH   A O   1 
HETATM 2251 O  O   . HOH   I 5 .   ? 24.978 5.066   21.475 1.00 31.59  ? 337 HOH   A O   1 
HETATM 2252 O  O   . HOH   I 5 .   ? 16.653 3.845   23.702 1.00 16.42  ? 338 HOH   A O   1 
HETATM 2253 O  O   . HOH   I 5 .   ? 8.432  24.718  23.861 1.00 30.74  ? 339 HOH   A O   1 
HETATM 2254 O  O   . HOH   I 5 .   ? 16.963 -3.455  27.799 1.00 33.44  ? 340 HOH   A O   1 
HETATM 2255 O  O   . HOH   I 5 .   ? 10.726 17.103  25.789 1.00 30.88  ? 341 HOH   A O   1 
HETATM 2256 O  O   . HOH   I 5 .   ? 13.788 3.963   23.562 1.00 12.09  ? 342 HOH   A O   1 
HETATM 2257 O  O   . HOH   I 5 .   ? 16.061 -6.750  10.726 1.00 34.48  ? 343 HOH   A O   1 
HETATM 2258 O  O   . HOH   I 5 .   ? 22.640 0.828   17.445 1.00 15.27  ? 344 HOH   A O   1 
HETATM 2259 O  O   . HOH   I 5 .   ? 28.908 3.348   12.635 1.00 16.06  ? 345 HOH   A O   1 
HETATM 2260 O  O   . HOH   I 5 .   ? 14.288 -10.844 8.620  1.00 39.83  ? 346 HOH   A O   1 
HETATM 2261 O  O   . HOH   I 5 .   ? 5.635  16.645  21.630 1.00 33.15  ? 347 HOH   A O   1 
HETATM 2262 O  O   . HOH   I 5 .   ? 11.277 12.747  11.316 1.00 15.67  ? 348 HOH   A O   1 
HETATM 2263 O  O   . HOH   I 5 .   ? 29.442 11.855  21.207 1.00 32.36  ? 349 HOH   A O   1 
HETATM 2264 O  O   . HOH   I 5 .   ? 3.954  12.823  18.273 1.00 29.61  ? 350 HOH   A O   1 
HETATM 2265 O  O   . HOH   I 5 .   ? 29.899 11.528  18.533 1.00 26.23  ? 351 HOH   A O   1 
HETATM 2266 O  O   . HOH   I 5 .   ? 6.614  -6.935  23.716 1.00 23.68  ? 352 HOH   A O   1 
HETATM 2267 O  O   . HOH   I 5 .   ? 18.410 21.881  9.547  1.00 19.28  ? 353 HOH   A O   1 
HETATM 2268 O  O   . HOH   I 5 .   ? 15.252 14.370  26.371 1.00 32.24  ? 354 HOH   A O   1 
HETATM 2269 O  O   . HOH   I 5 .   ? 17.614 19.971  17.033 1.00 17.55  ? 355 HOH   A O   1 
HETATM 2270 O  O   . HOH   I 5 .   ? 26.848 -1.222  8.781  1.00 24.08  ? 356 HOH   A O   1 
HETATM 2271 O  O   . HOH   I 5 .   ? 32.736 16.529  9.180  1.00 30.51  ? 357 HOH   A O   1 
HETATM 2272 O  O   . HOH   I 5 .   ? 21.852 4.885   24.794 1.00 39.52  ? 358 HOH   A O   1 
HETATM 2273 O  O   . HOH   I 5 .   ? 3.216  20.862  24.608 1.00 49.82  ? 359 HOH   A O   1 
HETATM 2274 O  O   . HOH   I 5 .   ? 17.399 -4.997  12.114 1.00 35.69  ? 360 HOH   A O   1 
HETATM 2275 O  O   . HOH   I 5 .   ? 31.193 -2.464  15.523 1.00 40.31  ? 361 HOH   A O   1 
HETATM 2276 O  O   . HOH   I 5 .   ? 30.958 -0.616  6.117  1.00 60.86  ? 362 HOH   A O   1 
HETATM 2277 O  O   . HOH   I 5 .   ? 31.633 19.922  11.706 1.00 20.45  ? 363 HOH   A O   1 
HETATM 2278 O  O   . HOH   I 5 .   ? 30.528 2.915   14.832 1.00 22.77  ? 364 HOH   A O   1 
HETATM 2279 O  O   . HOH   I 5 .   ? 33.686 11.082  15.660 1.00 36.25  ? 365 HOH   A O   1 
HETATM 2280 O  O   . HOH   I 5 .   ? 12.318 11.123  29.741 1.00 21.73  ? 366 HOH   A O   1 
HETATM 2281 O  O   . HOH   I 5 .   ? 20.747 -2.578  16.864 1.00 14.85  ? 367 HOH   A O   1 
HETATM 2282 O  O   . HOH   I 5 .   ? 25.318 17.803  4.544  1.00 34.94  ? 368 HOH   A O   1 
HETATM 2283 O  O   . HOH   I 5 .   ? 19.456 2.935   19.363 1.00 18.17  ? 369 HOH   A O   1 
HETATM 2284 O  O   . HOH   I 5 .   ? 13.204 11.430  9.306  1.00 13.87  ? 370 HOH   A O   1 
HETATM 2285 O  O   . HOH   I 5 .   ? 28.921 15.846  4.367  1.00 31.11  ? 371 HOH   A O   1 
HETATM 2286 O  O   . HOH   I 5 .   ? 36.537 17.873  14.409 1.00 29.31  ? 372 HOH   A O   1 
HETATM 2287 O  O   . HOH   I 5 .   ? 9.639  3.968   33.561 1.00 14.00  ? 373 HOH   A O   1 
HETATM 2288 O  O   . HOH   I 5 .   ? 31.041 15.571  22.763 1.00 24.77  ? 374 HOH   A O   1 
HETATM 2289 O  O   . HOH   I 5 .   ? 30.141 -1.405  8.666  1.00 32.09  ? 375 HOH   A O   1 
HETATM 2290 O  O   . HOH   I 5 .   ? 2.536  16.034  19.470 1.00 35.36  ? 376 HOH   A O   1 
HETATM 2291 O  O   . HOH   I 5 .   ? 14.459 -2.445  17.960 1.00 17.80  ? 377 HOH   A O   1 
HETATM 2292 O  O   . HOH   I 5 .   ? 17.110 6.046   26.909 1.00 27.51  ? 378 HOH   A O   1 
HETATM 2293 O  O   . HOH   I 5 .   ? 25.524 19.560  21.732 1.00 26.00  ? 379 HOH   A O   1 
HETATM 2294 O  O   . HOH   I 5 .   ? 11.583 -7.032  24.778 1.00 26.10  ? 380 HOH   A O   1 
HETATM 2295 O  O   . HOH   I 5 .   ? 35.263 10.700  12.310 1.00 43.99  ? 381 HOH   A O   1 
HETATM 2296 O  O   . HOH   I 5 .   ? 17.844 10.584  26.225 1.00 26.93  ? 382 HOH   A O   1 
HETATM 2297 O  O   . HOH   I 5 .   ? 0.201  5.915   6.144  1.00 25.40  ? 383 HOH   A O   1 
HETATM 2298 O  O   . HOH   I 5 .   ? 9.154  3.544   3.077  1.00 26.35  ? 384 HOH   A O   1 
HETATM 2299 O  O   . HOH   I 5 .   ? 5.525  5.383   32.752 1.00 23.98  ? 385 HOH   A O   1 
HETATM 2300 O  O   . HOH   I 5 .   ? 23.297 -6.591  11.950 1.00 30.18  ? 386 HOH   A O   1 
HETATM 2301 O  O   . HOH   I 5 .   ? 24.227 -3.444  16.093 1.00 36.15  ? 387 HOH   A O   1 
HETATM 2302 O  O   . HOH   I 5 .   ? 27.201 -1.316  15.870 1.00 23.60  ? 388 HOH   A O   1 
HETATM 2303 O  O   . HOH   I 5 .   ? 3.874  -3.814  6.008  1.00 26.57  ? 389 HOH   A O   1 
HETATM 2304 O  O   . HOH   I 5 .   ? 6.007  3.103   6.616  1.00 27.49  ? 390 HOH   A O   1 
HETATM 2305 O  O   . HOH   I 5 .   ? 30.372 4.561   5.750  1.00 23.75  ? 391 HOH   A O   1 
HETATM 2306 O  O   . HOH   I 5 .   ? 8.417  19.167  19.718 1.00 28.02  ? 392 HOH   A O   1 
HETATM 2307 O  O   . HOH   I 5 .   ? 22.799 -0.641  5.347  1.00 22.99  ? 393 HOH   A O   1 
HETATM 2308 O  O   . HOH   I 5 .   ? 36.275 -0.326  12.606 1.00 34.62  ? 394 HOH   A O   1 
HETATM 2309 O  O   . HOH   I 5 .   ? 34.025 18.659  10.776 1.00 26.74  ? 395 HOH   A O   1 
HETATM 2310 O  O   . HOH   I 5 .   ? 5.027  8.220   2.382  1.00 32.76  ? 396 HOH   A O   1 
HETATM 2311 O  O   . HOH   I 5 .   ? 1.449  11.734  27.397 1.00 46.28  ? 397 HOH   A O   1 
HETATM 2312 O  O   . HOH   I 5 .   ? 11.591 17.979  4.837  1.00 35.98  ? 398 HOH   A O   1 
HETATM 2313 O  O   . HOH   I 5 .   ? 18.041 17.751  4.309  1.00 36.26  ? 399 HOH   A O   1 
HETATM 2314 O  O   . HOH   I 5 .   ? 3.318  7.714   24.419 1.00 26.55  ? 400 HOH   A O   1 
HETATM 2315 O  O   . HOH   I 5 .   ? 15.407 15.247  3.689  1.00 29.91  ? 401 HOH   A O   1 
HETATM 2316 O  O   . HOH   I 5 .   ? 32.041 8.757   7.621  1.00 23.19  ? 402 HOH   A O   1 
HETATM 2317 O  O   . HOH   I 5 .   ? 28.002 17.512  24.200 1.00 24.26  ? 403 HOH   A O   1 
HETATM 2318 O  O   . HOH   I 5 .   ? 18.552 2.017   22.675 1.00 33.53  ? 404 HOH   A O   1 
HETATM 2319 O  O   . HOH   I 5 .   ? 14.251 24.301  18.047 1.00 39.59  ? 405 HOH   A O   1 
HETATM 2320 O  O   . HOH   I 5 .   ? 5.265  26.485  20.111 1.00 29.70  ? 406 HOH   A O   1 
HETATM 2321 O  O   . HOH   I 5 .   ? 16.522 21.198  19.193 1.00 27.54  ? 407 HOH   A O   1 
HETATM 2322 O  O   . HOH   I 5 .   ? 32.172 2.031   5.953  1.00 37.27  ? 408 HOH   A O   1 
HETATM 2323 O  O   . HOH   I 5 .   ? 7.327  14.002  4.884  1.00 23.62  ? 409 HOH   A O   1 
HETATM 2324 O  O   . HOH   I 5 .   ? 17.486 0.641   20.174 1.00 18.03  ? 410 HOH   A O   1 
HETATM 2325 O  O   . HOH   I 5 .   ? 4.622  -5.615  14.362 1.00 44.43  ? 411 HOH   A O   1 
HETATM 2326 O  O   . HOH   I 5 .   ? 16.591 -3.865  2.721  1.00 29.89  ? 412 HOH   A O   1 
HETATM 2327 O  O   . HOH   I 5 .   ? -1.309 16.011  20.716 1.00 44.66  ? 413 HOH   A O   1 
HETATM 2328 O  O   . HOH   I 5 .   ? 25.068 10.493  22.885 1.00 38.44  ? 414 HOH   A O   1 
HETATM 2329 O  O   . HOH   I 5 .   ? 19.282 16.739  26.464 1.00 40.91  ? 415 HOH   A O   1 
HETATM 2330 O  O   . HOH   I 5 .   ? 34.939 16.666  19.888 1.00 48.82  ? 416 HOH   A O   1 
HETATM 2331 O  O   . HOH   I 5 .   ? 8.491  -6.430  9.614  1.00 29.03  ? 417 HOH   A O   1 
HETATM 2332 O  O   . HOH   I 5 .   ? 33.969 5.229   16.685 1.00 33.04  ? 418 HOH   A O   1 
HETATM 2333 O  O   . HOH   I 5 .   ? 7.166  26.410  14.457 1.00 40.37  ? 419 HOH   A O   1 
HETATM 2334 O  O   . HOH   I 5 .   ? 22.395 19.461  19.636 1.00 30.73  ? 420 HOH   A O   1 
HETATM 2335 O  O   . HOH   I 5 .   ? 1.388  5.162   27.085 1.00 32.97  ? 421 HOH   A O   1 
HETATM 2336 O  O   . HOH   I 5 .   ? 3.431  -0.219  21.495 1.00 21.10  ? 422 HOH   A O   1 
HETATM 2337 O  O   . HOH   I 5 .   ? 36.006 15.102  10.928 1.00 40.60  ? 423 HOH   A O   1 
HETATM 2338 O  O   . HOH   I 5 .   ? 2.129  14.501  17.040 1.00 31.18  ? 424 HOH   A O   1 
HETATM 2339 O  O   . HOH   I 5 .   ? 0.535  -1.212  16.814 1.00 17.54  ? 425 HOH   A O   1 
HETATM 2340 O  O   . HOH   I 5 .   ? 31.034 19.405  9.080  1.00 38.97  ? 426 HOH   A O   1 
HETATM 2341 O  O   . HOH   I 5 .   ? 19.783 13.326  2.198  1.00 31.90  ? 427 HOH   A O   1 
HETATM 2342 O  O   . HOH   I 5 .   ? 0.443  -1.339  9.255  1.00 37.89  ? 428 HOH   A O   1 
HETATM 2343 O  O   . HOH   I 5 .   ? 6.180  23.936  10.631 1.00 41.80  ? 429 HOH   A O   1 
HETATM 2344 O  O   . HOH   I 5 .   ? 34.123 7.711   16.553 1.00 33.76  ? 430 HOH   A O   1 
HETATM 2345 O  O   . HOH   I 5 .   ? 19.843 -4.231  10.821 1.00 35.14  ? 431 HOH   A O   1 
HETATM 2346 O  O   . HOH   I 5 .   ? 35.786 11.924  17.356 1.00 48.39  ? 432 HOH   A O   1 
HETATM 2347 O  O   . HOH   I 5 .   ? 19.391 21.465  6.888  1.00 36.38  ? 433 HOH   A O   1 
HETATM 2348 O  O   . HOH   I 5 .   ? 22.719 3.412   20.847 1.00 20.25  ? 434 HOH   A O   1 
HETATM 2349 O  O   . HOH   I 5 .   ? 23.250 19.133  6.354  1.00 18.42  ? 435 HOH   A O   1 
HETATM 2350 O  O   . HOH   I 5 .   ? 15.715 21.461  7.358  1.00 30.38  ? 436 HOH   A O   1 
HETATM 2351 O  O   . HOH   I 5 .   ? 23.465 8.250   21.700 1.00 23.96  ? 437 HOH   A O   1 
HETATM 2352 O  O   . HOH   I 5 .   ? 8.358  6.474   33.861 1.00 20.84  ? 438 HOH   A O   1 
HETATM 2353 O  O   . HOH   I 5 .   ? 17.162 -2.451  19.679 1.00 19.92  ? 439 HOH   A O   1 
HETATM 2354 O  O   . HOH   I 5 .   ? 21.071 9.934   21.961 1.00 16.80  ? 440 HOH   A O   1 
HETATM 2355 O  O   . HOH   I 5 .   ? 36.624 16.066  16.822 1.00 38.44  ? 441 HOH   A O   1 
HETATM 2356 O  O   . HOH   I 5 .   ? 17.749 24.472  10.422 1.00 34.62  ? 442 HOH   A O   1 
HETATM 2357 O  O   . HOH   I 5 .   ? 15.237 -4.830  0.455  1.00 39.33  ? 443 HOH   A O   1 
HETATM 2358 O  O   . HOH   I 5 .   ? 19.457 9.320   -0.866 1.00 29.28  ? 444 HOH   A O   1 
HETATM 2359 O  O   . HOH   I 5 .   ? 6.039  -3.549  31.473 1.00 31.99  ? 445 HOH   A O   1 
HETATM 2360 O  O   . HOH   I 5 .   ? 21.344 -4.979  11.649 1.00 33.23  ? 446 HOH   A O   1 
HETATM 2361 O  O   . HOH   I 5 .   ? 7.357  -4.530  2.678  1.00 36.80  ? 447 HOH   A O   1 
HETATM 2362 O  O   . HOH   I 5 .   ? -1.348 -2.985  15.759 1.00 29.26  ? 448 HOH   A O   1 
HETATM 2363 O  O   . HOH   I 5 .   ? 25.538 -1.017  16.620 1.00 35.89  ? 449 HOH   A O   1 
HETATM 2364 O  O   . HOH   I 5 .   ? 11.625 15.147  23.768 1.00 29.85  ? 450 HOH   A O   1 
HETATM 2365 O  O   . HOH   I 5 .   ? 0.995  3.352   26.040 1.00 39.05  ? 451 HOH   A O   1 
HETATM 2366 O  O   . HOH   I 5 .   ? 13.813 -6.626  25.704 1.00 46.14  ? 452 HOH   A O   1 
HETATM 2367 O  O   . HOH   I 5 .   ? 21.472 19.692  4.366  1.00 37.41  ? 453 HOH   A O   1 
HETATM 2368 O  O   . HOH   I 5 .   ? 6.519  3.465   3.319  1.00 41.21  ? 454 HOH   A O   1 
HETATM 2369 O  O   . HOH   I 5 .   ? 8.714  12.099  31.663 1.00 42.01  ? 455 HOH   A O   1 
HETATM 2370 O  O   . HOH   I 5 .   ? 7.079  21.404  27.047 1.00 48.12  ? 456 HOH   A O   1 
HETATM 2371 O  O   . HOH   I 5 .   ? 23.802 0.996   19.848 1.00 28.54  ? 457 HOH   A O   1 
HETATM 2372 O  O   . HOH   I 5 .   ? 9.506  8.028   2.375  1.00 38.64  ? 458 HOH   A O   1 
HETATM 2373 O  O   . HOH   I 5 .   ? 30.351 7.012   17.913 1.00 31.37  ? 459 HOH   A O   1 
HETATM 2374 O  O   . HOH   I 5 .   ? -2.762 0.204   7.625  1.00 48.20  ? 460 HOH   A O   1 
HETATM 2375 O  O   . HOH   I 5 .   ? 31.322 4.477   16.943 1.00 26.54  ? 461 HOH   A O   1 
HETATM 2376 O  O   . HOH   I 5 .   ? 21.340 11.263  24.533 1.00 34.31  ? 462 HOH   A O   1 
HETATM 2377 O  O   . HOH   I 5 .   ? 12.466 -5.132  33.059 1.00 31.76  ? 463 HOH   A O   1 
HETATM 2378 O  O   . HOH   I 5 .   ? 37.854 -4.562  6.831  1.00 32.73  ? 464 HOH   A O   1 
HETATM 2379 O  O   . HOH   I 5 .   ? 21.281 -1.057  18.967 1.00 28.95  ? 465 HOH   A O   1 
HETATM 2380 O  O   . HOH   I 5 .   ? 27.505 10.484  0.245  1.00 49.51  ? 466 HOH   A O   1 
HETATM 2381 O  O   . HOH   I 5 .   ? 8.246  16.788  26.236 1.00 39.03  ? 467 HOH   A O   1 
HETATM 2382 O  O   . HOH   I 5 .   ? 26.588 0.318   19.753 1.00 49.74  ? 468 HOH   A O   1 
HETATM 2383 O  O   . HOH   J 5 .   ? 27.654 -20.759 1.299  1.00 37.86  ? 301 HOH   C O   1 
HETATM 2384 O  O   . HOH   J 5 .   ? 17.608 -33.275 24.112 1.00 42.73  ? 302 HOH   C O   1 
HETATM 2385 O  O   . HOH   J 5 .   ? 38.392 -7.338  7.140  1.00 22.87  ? 303 HOH   C O   1 
HETATM 2386 O  O   . HOH   J 5 .   ? 38.500 -27.455 28.594 1.00 46.10  ? 304 HOH   C O   1 
HETATM 2387 O  O   . HOH   J 5 .   ? 38.916 -18.659 21.624 1.00 25.03  ? 305 HOH   C O   1 
HETATM 2388 O  O   . HOH   J 5 .   ? 16.253 -16.167 9.191  1.00 37.40  ? 306 HOH   C O   1 
HETATM 2389 O  O   . HOH   J 5 .   ? 31.051 -32.579 0.777  1.00 40.28  ? 307 HOH   C O   1 
HETATM 2390 O  O   . HOH   J 5 .   ? 26.029 -35.603 2.920  1.00 42.35  ? 308 HOH   C O   1 
HETATM 2391 O  O   . HOH   J 5 .   ? 27.071 -7.809  2.266  1.00 48.63  ? 309 HOH   C O   1 
HETATM 2392 O  O   . HOH   J 5 .   ? 17.864 -6.011  24.107 1.00 26.43  ? 310 HOH   C O   1 
HETATM 2393 O  O   . HOH   J 5 .   ? 24.668 -5.978  15.283 1.00 27.21  ? 311 HOH   C O   1 
HETATM 2394 O  O   . HOH   J 5 .   ? 19.718 -4.095  20.243 1.00 21.73  ? 312 HOH   C O   1 
HETATM 2395 O  O   . HOH   J 5 .   ? 22.930 -5.919  21.160 1.00 19.83  ? 313 HOH   C O   1 
HETATM 2396 O  O   . HOH   J 5 .   ? 30.784 -18.149 26.971 1.00 17.95  ? 314 HOH   C O   1 
HETATM 2397 O  O   . HOH   J 5 .   ? 20.789 -18.721 12.887 1.00 13.12  ? 315 HOH   C O   1 
HETATM 2398 O  O   . HOH   J 5 .   ? 36.231 -26.187 34.322 1.00 34.35  ? 316 HOH   C O   1 
HETATM 2399 O  O   . HOH   J 5 .   ? 42.638 -11.237 11.285 1.00 30.53  ? 317 HOH   C O   1 
HETATM 2400 O  O   . HOH   J 5 .   ? 18.726 -32.389 19.991 1.00 38.78  ? 318 HOH   C O   1 
HETATM 2401 O  O   . HOH   J 5 .   ? 18.631 -8.853  13.810 1.00 28.97  ? 319 HOH   C O   1 
HETATM 2402 O  O   . HOH   J 5 .   ? 17.905 -27.547 16.550 1.00 18.33  ? 320 HOH   C O   1 
HETATM 2403 O  O   . HOH   J 5 .   ? 24.429 -9.338  26.930 1.00 44.31  ? 321 HOH   C O   1 
HETATM 2404 O  O   . HOH   J 5 .   ? 36.111 -17.658 11.693 1.00 27.25  ? 322 HOH   C O   1 
HETATM 2405 O  O   . HOH   J 5 .   ? 10.269 -17.523 18.371 1.00 25.54  ? 323 HOH   C O   1 
HETATM 2406 O  O   . HOH   J 5 .   ? 14.811 -23.918 12.358 1.00 29.96  ? 324 HOH   C O   1 
HETATM 2407 O  O   . HOH   J 5 .   ? 21.815 -26.248 34.403 1.00 28.06  ? 325 HOH   C O   1 
HETATM 2408 O  O   . HOH   J 5 .   ? 16.803 -9.405  27.745 1.00 36.75  ? 326 HOH   C O   1 
HETATM 2409 O  O   . HOH   J 5 .   ? 37.195 -18.794 28.270 1.00 28.03  ? 327 HOH   C O   1 
HETATM 2410 O  O   . HOH   J 5 .   ? 37.414 -31.890 10.993 1.00 24.74  ? 328 HOH   C O   1 
HETATM 2411 O  O   . HOH   J 5 .   ? 40.584 -27.225 15.303 1.00 12.07  ? 329 HOH   C O   1 
HETATM 2412 O  O   . HOH   J 5 .   ? 32.517 -23.747 29.208 1.00 17.55  ? 330 HOH   C O   1 
HETATM 2413 O  O   . HOH   J 5 .   ? 28.238 -5.036  18.687 1.00 43.25  ? 331 HOH   C O   1 
HETATM 2414 O  O   . HOH   J 5 .   ? 36.361 -2.492  11.102 1.00 34.09  ? 332 HOH   C O   1 
HETATM 2415 O  O   . HOH   J 5 .   ? 37.322 -10.515 5.025  1.00 37.22  ? 333 HOH   C O   1 
HETATM 2416 O  O   . HOH   J 5 .   ? 14.777 -18.661 32.053 1.00 38.49  ? 334 HOH   C O   1 
HETATM 2417 O  O   . HOH   J 5 .   ? 25.906 -37.868 24.394 1.00 31.76  ? 335 HOH   C O   1 
HETATM 2418 O  O   . HOH   J 5 .   ? 40.195 -29.554 11.980 1.00 23.16  ? 336 HOH   C O   1 
HETATM 2419 O  O   . HOH   J 5 .   ? 24.756 -15.729 7.399  1.00 18.10  ? 337 HOH   C O   1 
HETATM 2420 O  O   . HOH   J 5 .   ? 26.084 -25.225 8.858  1.00 12.68  ? 338 HOH   C O   1 
HETATM 2421 O  O   . HOH   J 5 .   ? 13.968 -24.410 29.319 1.00 31.95  ? 339 HOH   C O   1 
HETATM 2422 O  O   . HOH   J 5 .   ? 30.992 -21.530 28.470 1.00 16.96  ? 340 HOH   C O   1 
HETATM 2423 O  O   . HOH   J 5 .   ? 9.264  -8.079  21.360 1.00 24.34  ? 341 HOH   C O   1 
HETATM 2424 O  O   . HOH   J 5 .   ? 26.380 -15.260 30.835 1.00 30.65  ? 342 HOH   C O   1 
HETATM 2425 O  O   . HOH   J 5 .   ? 29.950 -15.259 19.677 1.00 15.04  ? 343 HOH   C O   1 
HETATM 2426 O  O   . HOH   J 5 .   ? 41.774 -13.719 10.078 1.00 36.21  ? 344 HOH   C O   1 
HETATM 2427 O  O   . HOH   J 5 .   ? 3.338  -12.860 20.299 1.00 40.29  ? 345 HOH   C O   1 
HETATM 2428 O  O   . HOH   J 5 .   ? 9.895  -8.915  23.936 1.00 26.82  ? 346 HOH   C O   1 
HETATM 2429 O  O   . HOH   J 5 .   ? 23.057 -32.662 20.675 1.00 34.02  ? 347 HOH   C O   1 
HETATM 2430 O  O   . HOH   J 5 .   ? 17.556 -23.948 8.663  1.00 34.94  ? 348 HOH   C O   1 
HETATM 2431 O  O   . HOH   J 5 .   ? 11.919 -24.271 21.759 1.00 17.72  ? 349 HOH   C O   1 
HETATM 2432 O  O   . HOH   J 5 .   ? 20.822 -25.640 13.868 1.00 19.18  ? 350 HOH   C O   1 
HETATM 2433 O  O   . HOH   J 5 .   ? 29.606 -31.398 32.815 1.00 24.80  ? 351 HOH   C O   1 
HETATM 2434 O  O   . HOH   J 5 .   ? 10.509 -16.889 15.107 1.00 31.35  ? 352 HOH   C O   1 
HETATM 2435 O  O   . HOH   J 5 .   ? 23.938 -8.165  9.510  1.00 20.13  ? 353 HOH   C O   1 
HETATM 2436 O  O   . HOH   J 5 .   ? 35.285 -32.782 3.388  1.00 31.03  ? 354 HOH   C O   1 
HETATM 2437 O  O   . HOH   J 5 .   ? 22.125 -21.322 4.377  1.00 37.12  ? 355 HOH   C O   1 
HETATM 2438 O  O   . HOH   J 5 .   ? 31.101 -6.072  5.944  1.00 38.75  ? 356 HOH   C O   1 
HETATM 2439 O  O   . HOH   J 5 .   ? 36.376 -21.285 6.951  1.00 23.22  ? 357 HOH   C O   1 
HETATM 2440 O  O   . HOH   J 5 .   ? 32.096 -10.431 13.861 1.00 17.41  ? 358 HOH   C O   1 
HETATM 2441 O  O   . HOH   J 5 .   ? 14.640 -28.809 25.598 1.00 31.25  ? 359 HOH   C O   1 
HETATM 2442 O  O   . HOH   J 5 .   ? 35.242 -13.148 8.791  1.00 18.82  ? 360 HOH   C O   1 
HETATM 2443 O  O   . HOH   J 5 .   ? 41.444 -24.990 7.315  1.00 30.70  ? 361 HOH   C O   1 
HETATM 2444 O  O   . HOH   J 5 .   ? 11.139 -21.647 13.804 1.00 38.83  ? 362 HOH   C O   1 
HETATM 2445 O  O   . HOH   J 5 .   ? 34.164 -33.705 24.163 1.00 34.21  ? 363 HOH   C O   1 
HETATM 2446 O  O   . HOH   J 5 .   ? 22.065 -28.409 4.900  1.00 25.32  ? 364 HOH   C O   1 
HETATM 2447 O  O   . HOH   J 5 .   ? 34.788 -34.943 18.148 1.00 28.46  ? 365 HOH   C O   1 
HETATM 2448 O  O   . HOH   J 5 .   ? 29.832 -13.081 13.046 1.00 14.35  ? 366 HOH   C O   1 
HETATM 2449 O  O   . HOH   J 5 .   ? 19.247 -27.697 28.202 1.00 19.29  ? 367 HOH   C O   1 
HETATM 2450 O  O   . HOH   J 5 .   ? 7.197  -30.412 22.210 1.00 36.06  ? 368 HOH   C O   1 
HETATM 2451 O  O   . HOH   J 5 .   ? 18.749 -11.448 8.022  1.00 43.31  ? 369 HOH   C O   1 
HETATM 2452 O  O   . HOH   J 5 .   ? 36.097 -28.638 2.964  1.00 43.32  ? 370 HOH   C O   1 
HETATM 2453 O  O   . HOH   J 5 .   ? 22.960 -33.204 5.445  1.00 29.53  ? 371 HOH   C O   1 
HETATM 2454 O  O   . HOH   J 5 .   ? 6.811  -9.277  22.756 1.00 33.63  ? 372 HOH   C O   1 
HETATM 2455 O  O   . HOH   J 5 .   ? 13.161 -11.225 28.554 1.00 37.02  ? 373 HOH   C O   1 
HETATM 2456 O  O   . HOH   J 5 .   ? 42.090 -12.193 14.365 1.00 41.88  ? 374 HOH   C O   1 
HETATM 2457 O  O   . HOH   J 5 .   ? 22.975 -8.512  14.092 1.00 15.77  ? 375 HOH   C O   1 
HETATM 2458 O  O   . HOH   J 5 .   ? 20.178 -32.123 15.564 1.00 49.40  ? 376 HOH   C O   1 
HETATM 2459 O  O   . HOH   J 5 .   ? 27.165 -35.631 20.801 1.00 23.68  ? 377 HOH   C O   1 
HETATM 2460 O  O   . HOH   J 5 .   ? 32.173 -34.632 24.859 1.00 27.24  ? 378 HOH   C O   1 
HETATM 2461 O  O   . HOH   J 5 .   ? 39.404 -33.506 13.957 1.00 41.92  ? 379 HOH   C O   1 
HETATM 2462 O  O   . HOH   J 5 .   ? 3.896  -8.260  14.716 1.00 26.23  ? 380 HOH   C O   1 
HETATM 2463 O  O   . HOH   J 5 .   ? 13.235 -29.609 19.208 1.00 30.70  ? 381 HOH   C O   1 
HETATM 2464 O  O   . HOH   J 5 .   ? 22.794 -7.455  25.549 1.00 44.50  ? 382 HOH   C O   1 
HETATM 2465 O  O   . HOH   J 5 .   ? 4.290  -10.446 19.643 1.00 29.87  ? 383 HOH   C O   1 
HETATM 2466 O  O   . HOH   J 5 .   ? 28.976 -36.189 7.880  1.00 19.21  ? 384 HOH   C O   1 
HETATM 2467 O  O   . HOH   J 5 .   ? 29.915 -15.868 30.641 1.00 33.55  ? 385 HOH   C O   1 
HETATM 2468 O  O   . HOH   J 5 .   ? 22.237 -13.725 29.332 1.00 38.60  ? 386 HOH   C O   1 
HETATM 2469 O  O   . HOH   J 5 .   ? 14.826 -18.366 10.527 1.00 36.64  ? 387 HOH   C O   1 
HETATM 2470 O  O   . HOH   J 5 .   ? 37.917 -31.236 25.979 1.00 29.83  ? 388 HOH   C O   1 
HETATM 2471 O  O   . HOH   J 5 .   ? 22.279 -23.745 6.213  1.00 32.49  ? 389 HOH   C O   1 
HETATM 2472 O  O   . HOH   J 5 .   ? 23.242 -25.372 9.015  1.00 20.24  ? 390 HOH   C O   1 
HETATM 2473 O  O   . HOH   J 5 .   ? 37.941 -23.484 4.418  1.00 40.69  ? 391 HOH   C O   1 
HETATM 2474 O  O   . HOH   J 5 .   ? 10.693 -16.949 12.390 1.00 32.78  ? 392 HOH   C O   1 
HETATM 2475 O  O   . HOH   J 5 .   ? 11.481 -22.520 28.700 1.00 25.88  ? 393 HOH   C O   1 
HETATM 2476 O  O   . HOH   J 5 .   ? 5.937  -16.909 22.228 1.00 38.92  ? 394 HOH   C O   1 
HETATM 2477 O  O   . HOH   J 5 .   ? 38.541 -13.536 10.872 1.00 36.41  ? 395 HOH   C O   1 
HETATM 2478 O  O   . HOH   J 5 .   ? 10.059 -24.900 19.861 1.00 21.34  ? 396 HOH   C O   1 
HETATM 2479 O  O   . HOH   J 5 .   ? 10.975 -6.426  13.237 1.00 21.96  ? 397 HOH   C O   1 
HETATM 2480 O  O   . HOH   J 5 .   ? 33.012 -9.824  11.215 1.00 14.39  ? 398 HOH   C O   1 
HETATM 2481 O  O   . HOH   J 5 .   ? 28.152 -16.343 22.147 1.00 13.37  ? 399 HOH   C O   1 
HETATM 2482 O  O   . HOH   J 5 .   ? 8.813  -13.285 10.846 1.00 22.51  ? 400 HOH   C O   1 
HETATM 2483 O  O   . HOH   J 5 .   ? 31.297 -12.149 10.744 1.00 14.34  ? 401 HOH   C O   1 
HETATM 2484 O  O   . HOH   J 5 .   ? 24.591 -13.771 5.524  1.00 36.11  ? 402 HOH   C O   1 
HETATM 2485 O  O   . HOH   J 5 .   ? 26.715 -12.062 27.676 1.00 28.22  ? 403 HOH   C O   1 
HETATM 2486 O  O   . HOH   J 5 .   ? 23.035 -28.184 12.662 1.00 20.19  ? 404 HOH   C O   1 
HETATM 2487 O  O   . HOH   J 5 .   ? 27.063 -19.057 1.755  1.00 25.19  ? 405 HOH   C O   1 
HETATM 2488 O  O   . HOH   J 5 .   ? 36.719 -16.154 12.625 1.00 29.92  ? 406 HOH   C O   1 
HETATM 2489 O  O   . HOH   J 5 .   ? 38.855 -16.635 3.696  1.00 40.46  ? 407 HOH   C O   1 
HETATM 2490 O  O   . HOH   J 5 .   ? 26.444 -31.216 14.903 1.00 18.86  ? 408 HOH   C O   1 
HETATM 2491 O  O   . HOH   J 5 .   ? 31.204 -35.762 31.785 1.00 38.32  ? 409 HOH   C O   1 
HETATM 2492 O  O   . HOH   J 5 .   ? 23.806 -3.373  19.077 1.00 35.08  ? 410 HOH   C O   1 
HETATM 2493 O  O   . HOH   J 5 .   ? 31.551 -13.467 4.395  1.00 32.70  ? 411 HOH   C O   1 
HETATM 2494 O  O   . HOH   J 5 .   ? 43.299 -25.355 23.826 1.00 28.51  ? 412 HOH   C O   1 
HETATM 2495 O  O   . HOH   J 5 .   ? 26.622 -6.066  22.175 1.00 29.64  ? 413 HOH   C O   1 
HETATM 2496 O  O   . HOH   J 5 .   ? 34.363 -13.458 25.610 1.00 19.83  ? 414 HOH   C O   1 
HETATM 2497 O  O   . HOH   J 5 .   ? 10.827 -11.863 9.094  1.00 29.64  ? 415 HOH   C O   1 
HETATM 2498 O  O   . HOH   J 5 .   ? 34.659 -23.360 -0.657 1.00 35.09  ? 416 HOH   C O   1 
HETATM 2499 O  O   . HOH   J 5 .   ? 26.052 -31.037 30.916 1.00 17.16  ? 417 HOH   C O   1 
HETATM 2500 O  O   . HOH   J 5 .   ? 35.635 -24.652 24.783 1.00 19.12  ? 418 HOH   C O   1 
HETATM 2501 O  O   . HOH   J 5 .   ? 38.916 -14.571 13.583 1.00 31.74  ? 419 HOH   C O   1 
HETATM 2502 O  O   . HOH   J 5 .   ? 20.346 -23.686 34.878 1.00 30.41  ? 420 HOH   C O   1 
HETATM 2503 O  O   . HOH   J 5 .   ? 21.715 -18.895 5.934  1.00 26.75  ? 421 HOH   C O   1 
HETATM 2504 O  O   . HOH   J 5 .   ? 30.181 -10.410 27.842 1.00 42.82  ? 422 HOH   C O   1 
HETATM 2505 O  O   . HOH   J 5 .   ? 35.813 -28.522 7.828  1.00 18.80  ? 423 HOH   C O   1 
HETATM 2506 O  O   . HOH   J 5 .   ? 38.924 -13.034 25.903 1.00 27.62  ? 424 HOH   C O   1 
HETATM 2507 O  O   . HOH   J 5 .   ? 37.011 -29.228 10.159 1.00 20.65  ? 425 HOH   C O   1 
HETATM 2508 O  O   . HOH   J 5 .   ? 36.501 -32.384 25.184 1.00 37.37  ? 426 HOH   C O   1 
HETATM 2509 O  O   . HOH   J 5 .   ? 23.426 -28.112 1.522  1.00 33.95  ? 427 HOH   C O   1 
HETATM 2510 O  O   . HOH   J 5 .   ? 9.791  -18.467 26.740 1.00 29.58  ? 428 HOH   C O   1 
HETATM 2511 O  O   . HOH   J 5 .   ? 20.247 -19.698 36.126 1.00 35.76  ? 429 HOH   C O   1 
HETATM 2512 O  O   . HOH   J 5 .   ? 15.288 -29.951 17.901 1.00 46.48  ? 430 HOH   C O   1 
HETATM 2513 O  O   . HOH   J 5 .   ? 4.612  -27.962 23.299 1.00 35.52  ? 431 HOH   C O   1 
HETATM 2514 O  O   . HOH   J 5 .   ? 17.216 -25.252 12.802 1.00 23.62  ? 432 HOH   C O   1 
HETATM 2515 O  O   . HOH   J 5 .   ? 30.401 -17.974 8.464  1.00 24.44  ? 433 HOH   C O   1 
HETATM 2516 O  O   . HOH   J 5 .   ? 32.857 -14.332 9.534  1.00 14.60  ? 434 HOH   C O   1 
HETATM 2517 O  O   . HOH   J 5 .   ? 20.423 -32.211 22.287 1.00 30.03  ? 435 HOH   C O   1 
HETATM 2518 O  O   . HOH   J 5 .   ? 33.576 -33.048 0.941  1.00 35.64  ? 436 HOH   C O   1 
HETATM 2519 O  O   . HOH   J 5 .   ? 16.434 -20.506 11.589 1.00 23.84  ? 437 HOH   C O   1 
HETATM 2520 O  O   . HOH   J 5 .   ? 18.880 -19.096 10.931 1.00 18.54  ? 438 HOH   C O   1 
HETATM 2521 O  O   . HOH   J 5 .   ? 41.713 -12.503 18.131 1.00 24.92  ? 439 HOH   C O   1 
HETATM 2522 O  O   . HOH   J 5 .   ? 18.606 -8.307  25.611 1.00 21.33  ? 440 HOH   C O   1 
HETATM 2523 O  O   . HOH   J 5 .   ? 34.929 -4.061  17.750 1.00 29.18  ? 441 HOH   C O   1 
HETATM 2524 O  O   . HOH   J 5 .   ? 40.088 -29.872 14.695 1.00 16.85  ? 442 HOH   C O   1 
HETATM 2525 O  O   . HOH   J 5 .   ? 4.018  -12.785 17.323 1.00 35.98  ? 443 HOH   C O   1 
HETATM 2526 O  O   . HOH   J 5 .   ? 6.491  -22.877 18.336 1.00 33.01  ? 444 HOH   C O   1 
HETATM 2527 O  O   . HOH   J 5 .   ? 6.849  -17.193 18.534 1.00 42.99  ? 445 HOH   C O   1 
HETATM 2528 O  O   . HOH   J 5 .   ? 37.867 -20.638 4.730  1.00 32.72  ? 446 HOH   C O   1 
HETATM 2529 O  O   . HOH   J 5 .   ? 34.114 -15.617 27.257 1.00 33.47  ? 447 HOH   C O   1 
HETATM 2530 O  O   . HOH   J 5 .   ? 33.902 -35.980 8.850  1.00 35.00  ? 448 HOH   C O   1 
HETATM 2531 O  O   . HOH   J 5 .   ? 36.607 -24.805 27.262 1.00 37.05  ? 449 HOH   C O   1 
HETATM 2532 O  O   . HOH   J 5 .   ? 35.131 -13.599 6.159  1.00 33.01  ? 450 HOH   C O   1 
HETATM 2533 O  O   . HOH   J 5 .   ? 23.273 -17.562 33.343 1.00 23.19  ? 451 HOH   C O   1 
HETATM 2534 O  O   . HOH   J 5 .   ? 9.741  -24.544 29.551 1.00 43.33  ? 452 HOH   C O   1 
HETATM 2535 O  O   . HOH   J 5 .   ? 6.705  -18.846 25.794 1.00 51.85  ? 453 HOH   C O   1 
HETATM 2536 O  O   . HOH   J 5 .   ? 6.686  -20.135 18.148 1.00 34.07  ? 454 HOH   C O   1 
HETATM 2537 O  O   . HOH   J 5 .   ? 37.374 -14.341 9.552  1.00 30.49  ? 455 HOH   C O   1 
HETATM 2538 O  O   . HOH   J 5 .   ? 40.722 -28.632 28.486 1.00 51.33  ? 456 HOH   C O   1 
HETATM 2539 O  O   . HOH   J 5 .   ? 31.659 -15.684 7.179  1.00 27.45  ? 457 HOH   C O   1 
HETATM 2540 O  O   . HOH   J 5 .   ? 5.945  -12.148 23.514 1.00 52.14  ? 458 HOH   C O   1 
HETATM 2541 O  O   . HOH   J 5 .   ? 24.275 -16.520 3.324  1.00 37.88  ? 459 HOH   C O   1 
HETATM 2542 O  O   . HOH   J 5 .   ? 39.714 -14.264 8.530  1.00 35.49  ? 460 HOH   C O   1 
HETATM 2543 O  O   . HOH   J 5 .   ? 23.776 -15.717 31.542 1.00 33.35  ? 461 HOH   C O   1 
HETATM 2544 O  O   . HOH   J 5 .   ? 8.844  -19.223 16.792 1.00 33.35  ? 462 HOH   C O   1 
HETATM 2545 O  O   . HOH   J 5 .   ? 26.184 -35.341 7.501  1.00 24.63  ? 463 HOH   C O   1 
HETATM 2546 O  O   . HOH   J 5 .   ? 21.092 -17.523 34.748 1.00 29.29  ? 464 HOH   C O   1 
HETATM 2547 O  O   . HOH   J 5 .   ? 22.944 -16.721 5.465  1.00 37.92  ? 465 HOH   C O   1 
HETATM 2548 O  O   . HOH   J 5 .   ? 12.105 -18.662 10.585 1.00 49.92  ? 466 HOH   C O   1 
HETATM 2549 O  O   . HOH   J 5 .   ? 21.475 -26.843 10.492 1.00 34.18  ? 467 HOH   C O   1 
HETATM 2550 O  O   . HOH   J 5 .   ? 37.126 -29.079 5.556  1.00 41.74  ? 468 HOH   C O   1 
HETATM 2551 O  O   . HOH   J 5 .   ? 43.216 -20.750 4.079  1.00 52.11  ? 469 HOH   C O   1 
HETATM 2552 O  O   . HOH   J 5 .   ? 16.481 -27.584 14.211 1.00 31.95  ? 470 HOH   C O   1 
HETATM 2553 O  O   . HOH   J 5 .   ? 40.495 -15.173 11.071 1.00 34.43  ? 471 HOH   C O   1 
HETATM 2554 O  O   . HOH   J 5 .   ? 18.608 -26.082 10.226 1.00 36.64  ? 472 HOH   C O   1 
HETATM 2555 O  O   . HOH   J 5 .   ? 41.482 -15.233 13.827 1.00 38.62  ? 473 HOH   C O   1 
HETATM 2556 O  O   . HOH   J 5 .   ? 32.582 -19.455 29.316 1.00 34.41  ? 474 HOH   C O   1 
HETATM 2557 O  O   . HOH   J 5 .   ? 18.164 -17.867 8.401  1.00 32.38  ? 475 HOH   C O   1 
HETATM 2558 O  O   . HOH   J 5 .   ? 18.700 -4.229  25.847 1.00 42.40  ? 476 HOH   C O   1 
HETATM 2559 O  O   . HOH   J 5 .   ? 25.099 -35.344 0.313  1.00 56.21  ? 477 HOH   C O   1 
HETATM 2560 O  O   . HOH   J 5 .   ? 16.990 -28.939 28.934 1.00 37.48  ? 478 HOH   C O   1 
HETATM 2561 O  O   . HOH   J 5 .   ? 38.095 -31.666 4.987  1.00 43.25  ? 479 HOH   C O   1 
HETATM 2562 O  O   . HOH   J 5 .   ? 22.797 -11.873 6.016  1.00 39.05  ? 480 HOH   C O   1 
HETATM 2563 O  O   . HOH   J 5 .   ? 35.213 -23.122 29.079 1.00 30.44  ? 481 HOH   C O   1 
HETATM 2564 O  O   . HOH   J 5 .   ? 9.088  -23.544 17.673 1.00 31.16  ? 482 HOH   C O   1 
HETATM 2565 O  O   . HOH   J 5 .   ? 37.169 -23.080 -1.687 1.00 32.59  ? 483 HOH   C O   1 
HETATM 2566 O  O   . HOH   J 5 .   ? 3.255  -8.674  22.124 1.00 44.56  ? 484 HOH   C O   1 
HETATM 2567 O  O   . HOH   J 5 .   ? 35.582 -20.576 29.613 1.00 41.09  ? 485 HOH   C O   1 
HETATM 2568 O  O   . HOH   J 5 .   ? 39.266 -2.615  10.811 1.00 39.90  ? 486 HOH   C O   1 
HETATM 2569 O  O   . HOH   J 5 .   ? 19.394 -17.618 5.771  1.00 37.62  ? 487 HOH   C O   1 
HETATM 2570 O  O   . HOH   J 5 .   ? 19.551 -15.198 34.733 1.00 39.71  ? 488 HOH   C O   1 
HETATM 2571 O  O   . HOH   J 5 .   ? 6.064  -24.272 15.102 1.00 49.92  ? 489 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   ? 0.2159 0.2062 0.1950 -0.0127 -0.0069 -0.0139 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2053 0.1969 0.1904 -0.0109 -0.0103 -0.0110 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2043 0.1985 0.1971 -0.0055 -0.0133 -0.0055 7   SER   A C   
4    O O   . SER   A 1   ? 0.2123 0.2080 0.2047 -0.0042 -0.0137 -0.0035 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2449 0.2416 0.2253 -0.0183 -0.0146 -0.0094 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2913 0.2945 0.2702 -0.0206 -0.0193 -0.0039 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1810 0.1754 0.1804 -0.0030 -0.0146 -0.0037 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1668 0.1627 0.1735 0.0011  -0.0157 0.0002  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1463 0.1401 0.1586 0.0043  -0.0139 -0.0008 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1714 0.1623 0.1824 0.0047  -0.0115 -0.0037 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1318 0.1271 0.1508 0.0061  -0.0145 0.0018  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1366 0.1306 0.1602 0.0079  -0.0125 0.0008  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1350 0.1289 0.1635 0.0096  -0.0103 0.0018  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1446 0.1389 0.1752 0.0100  -0.0106 0.0040  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1616 0.1577 0.1893 0.0065  -0.0145 0.0020  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1322 0.1251 0.1622 0.0100  -0.0077 0.0000  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1221 0.1142 0.1564 0.0099  -0.0041 -0.0006 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1287 0.1216 0.1708 0.0101  -0.0033 -0.0001 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1289 0.1227 0.1702 0.0095  -0.0044 -0.0007 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1192 0.1114 0.1488 0.0081  -0.0015 -0.0030 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1468 0.1400 0.1703 0.0080  -0.0026 -0.0026 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1447 0.1355 0.1769 0.0061  0.0034  -0.0051 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1603 0.1564 0.1805 0.0059  -0.0015 -0.0025 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1231 0.1155 0.1738 0.0111  -0.0009 0.0013  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1314 0.1251 0.1921 0.0117  0.0008  0.0022  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1378 0.1282 0.2026 0.0106  0.0083  -0.0015 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1505 0.1380 0.2216 0.0115  0.0123  -0.0011 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1489 0.1462 0.2200 0.0136  -0.0020 0.0084  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1428 0.1445 0.2086 0.0123  -0.0090 0.0114  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1542 0.1593 0.2204 0.0107  -0.0116 0.0118  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1641 0.1663 0.2237 0.0115  -0.0123 0.0132  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1632 0.1714 0.2227 0.0078  -0.0169 0.0130  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1777 0.1835 0.2304 0.0086  -0.0175 0.0145  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1765 0.1849 0.2289 0.0064  -0.0194 0.0139  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2159 0.2271 0.2604 0.0020  -0.0234 0.0139  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1409 0.1312 0.2010 0.0079  0.0106  -0.0053 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1440 0.1318 0.2048 0.0046  0.0182  -0.0101 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1566 0.1458 0.2234 0.0038  0.0209  -0.0113 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1492 0.1416 0.2124 0.0034  0.0166  -0.0101 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1674 0.1555 0.2148 -0.0001 0.0186  -0.0132 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1868 0.1789 0.2273 -0.0006 0.0131  -0.0112 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.1918 0.1783 0.2377 -0.0059 0.0266  -0.0188 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1719 0.1587 0.2495 0.0037  0.0285  -0.0134 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1824 0.1711 0.2674 0.0031  0.0316  -0.0144 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1616 0.1556 0.2524 0.0067  0.0242  -0.0085 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1592 0.1550 0.2561 0.0104  0.0198  -0.0031 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1536 0.1504 0.2406 0.0046  0.0223  -0.0092 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1408 0.1424 0.2306 0.0064  0.0154  -0.0046 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1462 0.1474 0.2222 0.0050  0.0091  -0.0044 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1502 0.1535 0.2244 0.0040  0.0057  -0.0034 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1586 0.1637 0.2569 0.0054  0.0178  -0.0047 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2106 0.2176 0.3275 0.0083  0.0229  -0.0025 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2333 0.2459 0.3613 0.0111  0.0187  0.0041  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.1886 0.1914 0.3096 0.0071  0.0323  -0.0073 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1313 0.1299 0.1991 0.0052  0.0080  -0.0051 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1374 0.1353 0.1948 0.0047  0.0034  -0.0045 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1269 0.1243 0.1823 0.0069  -0.0005 -0.0023 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1373 0.1340 0.1959 0.0082  0.0010  -0.0017 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1517 0.1485 0.2005 0.0020  0.0056  -0.0067 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1576 0.1557 0.2055 -0.0019 0.0090  -0.0086 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1778 0.1772 0.2261 -0.0026 0.0071  -0.0074 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1879 0.1860 0.2339 -0.0058 0.0147  -0.0120 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1859 0.1870 0.2330 -0.0067 0.0101  -0.0087 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2054 0.2056 0.2487 -0.0109 0.0179  -0.0139 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2095 0.2115 0.2537 -0.0111 0.0153  -0.0118 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2602 0.2648 0.3016 -0.0165 0.0182  -0.0131 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1190 0.1162 0.1688 0.0067  -0.0045 -0.0015 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1244 0.1209 0.1697 0.0074  -0.0075 -0.0005 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1222 0.1159 0.1597 0.0072  -0.0072 -0.0020 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1309 0.1234 0.1671 0.0062  -0.0072 -0.0025 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1387 0.1377 0.1850 0.0059  -0.0115 0.0013  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1487 0.1469 0.1877 0.0046  -0.0140 0.0011  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1582 0.1607 0.1973 0.0008  -0.0179 0.0030  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1786 0.1779 0.2082 -0.0026 -0.0182 -0.0003 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.1950 0.1946 0.2183 -0.0049 -0.0193 -0.0006 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2058 0.2086 0.2310 -0.0034 -0.0210 0.0028  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2007 0.1964 0.2158 -0.0087 -0.0177 -0.0049 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1229 0.1159 0.1569 0.0080  -0.0064 -0.0022 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1198 0.1116 0.1491 0.0083  -0.0059 -0.0022 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1318 0.1221 0.1578 0.0090  -0.0072 -0.0025 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1378 0.1288 0.1627 0.0093  -0.0080 -0.0023 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1269 0.1207 0.1544 0.0077  -0.0041 -0.0018 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1372 0.1322 0.1626 0.0080  -0.0041 0.0002  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1414 0.1367 0.1708 0.0052  -0.0017 -0.0028 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1218 0.1094 0.1465 0.0089  -0.0066 -0.0033 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1273 0.1125 0.1483 0.0084  -0.0062 -0.0050 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1501 0.1353 0.1711 0.0084  -0.0063 -0.0050 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1337 0.1161 0.1557 0.0100  -0.0030 -0.0050 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1488 0.1313 0.1749 0.0113  -0.0019 -0.0026 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1205 0.1042 0.1393 0.0050  -0.0073 -0.0072 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.1902 0.1744 0.2096 0.0050  -0.0076 -0.0069 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1462 0.1346 0.1655 0.0034  -0.0110 -0.0053 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.1959 0.1782 0.2094 0.0021  -0.0070 -0.0096 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.0838 0.0647 0.1051 0.0041  -0.0060 -0.0079 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2194 0.2082 0.2416 0.0040  -0.0110 -0.0047 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1313 0.1114 0.1506 0.0098  -0.0010 -0.0070 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1404 0.1170 0.1635 0.0118  0.0035  -0.0070 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1515 0.1224 0.1765 0.0103  0.0060  -0.0090 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1531 0.1218 0.1730 0.0063  0.0053  -0.0129 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1454 0.1196 0.1651 0.0109  0.0066  -0.0103 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1511 0.1303 0.1688 0.0120  0.0047  -0.0085 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1680 0.1494 0.1801 0.0097  0.0015  -0.0093 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1567 0.1384 0.1799 0.0152  0.0065  -0.0052 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1449 0.1141 0.1774 0.0130  0.0086  -0.0058 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1503 0.1130 0.1853 0.0115  0.0115  -0.0075 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.1749 0.1299 0.2061 0.0083  0.0167  -0.0142 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.1878 0.1390 0.2151 0.0038  0.0172  -0.0183 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1560 0.1182 0.2013 0.0152  0.0140  -0.0015 20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1626 0.1178 0.2118 0.0140  0.0172  -0.0021 20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.1824 0.1378 0.2439 0.0180  0.0197  0.0058  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.2010 0.1503 0.2673 0.0170  0.0222  0.0069  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.2325 0.1709 0.3034 0.0167  0.0296  0.0032  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2424 0.1746 0.3120 0.0164  0.0353  -0.0030 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2485 0.1814 0.3250 0.0160  0.0320  0.0053  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.1697 0.1232 0.2013 0.0095  0.0206  -0.0159 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.2014 0.1470 0.2289 0.0052  0.0272  -0.0235 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.2140 0.1618 0.2284 -0.0021 0.0237  -0.0287 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.2434 0.1852 0.2517 -0.0083 0.0288  -0.0357 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.2184 0.1615 0.2514 0.0084  0.0339  -0.0241 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.2027 0.1526 0.2302 0.0084  0.0307  -0.0238 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.1950 0.1531 0.2266 0.0132  0.0258  -0.0168 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.2280 0.1773 0.2459 0.0035  0.0322  -0.0295 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.2006 0.1621 0.2259 0.0117  0.0247  -0.0187 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.2276 0.1843 0.2448 0.0061  0.0283  -0.0259 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.2090 0.1653 0.2195 -0.0021 0.0156  -0.0250 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.1953 0.1562 0.1962 -0.0085 0.0108  -0.0269 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.2153 0.1801 0.2166 -0.0106 0.0054  -0.0246 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.2304 0.2011 0.2267 -0.0154 0.0005  -0.0239 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.1921 0.1597 0.1903 -0.0074 0.0067  -0.0241 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.2016 0.1664 0.1986 -0.0064 0.0119  -0.0266 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.2078 0.1795 0.2021 -0.0053 0.0072  -0.0231 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.2304 0.1899 0.2191 -0.0141 0.0177  -0.0343 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.1988 0.1611 0.2071 -0.0072 0.0063  -0.0226 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.1893 0.1555 0.1990 -0.0089 0.0019  -0.0206 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.2141 0.1793 0.2173 -0.0172 0.0020  -0.0248 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.2203 0.1781 0.2196 -0.0213 0.0078  -0.0305 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.1913 0.1545 0.2086 -0.0047 0.0037  -0.0180 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.2053 0.1788 0.2080 -0.0202 -0.0042 -0.0219 24  THR   A N   
139  C CA  . THR   A 18  ? 0.1938 0.1699 0.1902 -0.0295 -0.0058 -0.0244 24  THR   A CA  
140  C C   . THR   A 18  ? 0.2087 0.1820 0.2088 -0.0307 -0.0047 -0.0251 24  THR   A C   
141  O O   . THR   A 18  ? 0.1967 0.1675 0.2045 -0.0243 -0.0036 -0.0227 24  THR   A O   
142  C CB  . THR   A 18  ? 0.2206 0.2093 0.2175 -0.0320 -0.0137 -0.0185 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.2162 0.2094 0.2234 -0.0263 -0.0167 -0.0131 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2311 0.2235 0.2253 -0.0307 -0.0157 -0.0162 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.2124 0.1871 0.2065 -0.0401 -0.0052 -0.0282 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.2116 0.1848 0.2090 -0.0422 -0.0047 -0.0286 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.2039 0.1862 0.2108 -0.0370 -0.0104 -0.0215 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.2035 0.1824 0.2163 -0.0334 -0.0087 -0.0206 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.2247 0.2006 0.2131 -0.0549 -0.0054 -0.0326 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.3018 0.2800 0.2943 -0.0577 -0.0069 -0.0314 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.3566 0.3234 0.3514 -0.0566 -0.0007 -0.0351 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.3510 0.3421 0.3479 -0.0601 -0.0140 -0.0255 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.3596 0.3322 0.3574 -0.0602 -0.0040 -0.0329 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.3819 0.3695 0.3819 -0.0618 -0.0120 -0.0269 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.1931 0.1866 0.2024 -0.0365 -0.0165 -0.0160 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.1868 0.1877 0.2069 -0.0314 -0.0201 -0.0099 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.1641 0.1592 0.1897 -0.0224 -0.0167 -0.0095 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.1758 0.1721 0.2081 -0.0196 -0.0163 -0.0077 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.2087 0.2215 0.2330 -0.0318 -0.0260 -0.0034 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.2910 0.3109 0.3287 -0.0270 -0.0279 0.0023  26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.3404 0.3656 0.3826 -0.0303 -0.0295 0.0040  26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.3103 0.3296 0.3548 -0.0195 -0.0268 0.0048  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.1695 0.1592 0.1917 -0.0187 -0.0142 -0.0110 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1541 0.1398 0.1804 -0.0119 -0.0114 -0.0101 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1532 0.1325 0.1811 -0.0116 -0.0078 -0.0116 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1578 0.1385 0.1907 -0.0088 -0.0075 -0.0091 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1672 0.1488 0.1898 -0.0090 -0.0093 -0.0113 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.1781 0.1654 0.2002 -0.0080 -0.0124 -0.0090 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1856 0.1786 0.2137 -0.0060 -0.0149 -0.0053 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.1824 0.1677 0.1987 -0.0092 -0.0116 -0.0109 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1540 0.1261 0.1775 -0.0153 -0.0044 -0.0155 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1574 0.1225 0.1837 -0.0151 -0.0004 -0.0162 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1628 0.1319 0.1919 -0.0180 -0.0026 -0.0149 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.1714 0.1380 0.2047 -0.0161 -0.0009 -0.0129 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.1725 0.1277 0.1946 -0.0190 0.0051  -0.0216 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.1748 0.1243 0.1982 -0.0145 0.0095  -0.0219 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.2004 0.1484 0.2185 -0.0160 0.0113  -0.0255 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.1815 0.1269 0.2127 -0.0084 0.0128  -0.0179 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.1961 0.1388 0.2191 -0.0105 0.0161  -0.0245 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.1847 0.1265 0.2163 -0.0057 0.0166  -0.0190 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.2012 0.1468 0.2392 -0.0055 0.0127  -0.0127 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.2053 0.1445 0.2458 0.0003  0.0201  -0.0143 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.2056 0.1493 0.2511 -0.0002 0.0154  -0.0076 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.2143 0.1548 0.2619 0.0027  0.0192  -0.0081 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1603 0.1367 0.1880 -0.0228 -0.0066 -0.0152 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.1631 0.1447 0.1947 -0.0257 -0.0087 -0.0136 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.1716 0.1604 0.2111 -0.0208 -0.0106 -0.0092 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.1854 0.1781 0.2296 -0.0222 -0.0111 -0.0078 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.1821 0.1705 0.2103 -0.0333 -0.0123 -0.0144 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1653 0.1555 0.2061 -0.0157 -0.0109 -0.0075 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1658 0.1613 0.2133 -0.0118 -0.0110 -0.0046 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1635 0.1545 0.2090 -0.0078 -0.0083 -0.0046 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1599 0.1536 0.2073 -0.0049 -0.0080 -0.0035 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.1750 0.1783 0.2273 -0.0108 -0.0140 -0.0021 30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.1885 0.1991 0.2447 -0.0154 -0.0172 -0.0001 30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2240 0.2394 0.2881 -0.0156 -0.0168 0.0015  30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.2049 0.2171 0.2554 -0.0202 -0.0203 -0.0004 30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1580 0.1427 0.2006 -0.0079 -0.0061 -0.0051 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1462 0.1284 0.1878 -0.0047 -0.0043 -0.0034 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1623 0.1485 0.2059 -0.0044 -0.0035 -0.0010 31  LEU   A C   
201  O O   . LEU   A 25  ? 0.1788 0.1662 0.2244 -0.0067 -0.0029 -0.0004 31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1578 0.1324 0.1987 -0.0050 -0.0018 -0.0032 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1643 0.1373 0.2065 -0.0017 -0.0001 0.0003  31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1714 0.1445 0.2113 0.0008  -0.0003 -0.0009 31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.1955 0.1609 0.2412 -0.0014 0.0034  0.0019  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1533 0.1417 0.1956 -0.0025 -0.0033 0.0001  32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1562 0.1487 0.1982 -0.0040 -0.0019 0.0018  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1541 0.1462 0.1946 -0.0036 -0.0019 0.0063  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1780 0.1725 0.2187 -0.0063 -0.0015 0.0098  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1476 0.1434 0.1892 -0.0036 -0.0011 -0.0002 32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1780 0.1778 0.2167 -0.0070 0.0011  0.0007  32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1711 0.1685 0.2179 -0.0034 -0.0006 -0.0026 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1489 0.1388 0.1889 -0.0006 -0.0023 0.0072  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1532 0.1445 0.1946 0.0003  -0.0023 0.0128  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1567 0.1435 0.1995 0.0042  -0.0015 0.0122  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1471 0.1325 0.1870 0.0052  -0.0019 0.0077  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1684 0.1676 0.2063 -0.0023 -0.0030 0.0148  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1748 0.1785 0.2143 -0.0020 -0.0039 0.0216  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.2067 0.2152 0.2494 -0.0040 -0.0049 0.0295  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1708 0.1762 0.2099 0.0003  -0.0044 0.0222  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2189 0.2330 0.2641 -0.0031 -0.0061 0.0356  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.1962 0.2083 0.2390 -0.0005 -0.0056 0.0308  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1837 0.1865 0.2203 0.0025  -0.0040 0.0172  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.2068 0.2236 0.2508 0.0009  -0.0064 0.0340  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.1955 0.2019 0.2321 0.0037  -0.0045 0.0196  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.2101 0.2232 0.2507 0.0031  -0.0056 0.0277  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1627 0.1473 0.2109 0.0062  -0.0001 0.0170  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1677 0.1482 0.2185 0.0097  0.0021  0.0163  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1824 0.1659 0.2412 0.0120  0.0030  0.0247  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.1870 0.1723 0.2510 0.0112  0.0029  0.0311  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.1894 0.1602 0.2405 0.0100  0.0053  0.0108  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.2013 0.1664 0.2572 0.0090  0.0078  0.0124  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.2090 0.1696 0.2755 0.0122  0.0121  0.0182  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2270 0.1856 0.2992 0.0116  0.0132  0.0229  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.2075 0.1666 0.2779 0.0154  0.0149  0.0188  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1659 0.1502 0.2271 0.0150  0.0042  0.0256  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1636 0.1522 0.2351 0.0178  0.0052  0.0347  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1538 0.1373 0.2303 0.0219  0.0097  0.0324  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1593 0.1455 0.2305 0.0221  0.0087  0.0291  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1889 0.1909 0.2577 0.0148  0.0004  0.0409  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2237 0.2341 0.3037 0.0165  -0.0001 0.0528  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2547 0.2612 0.3449 0.0216  0.0039  0.0548  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2804 0.3023 0.3591 0.0122  -0.0042 0.0601  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1658 0.1410 0.2525 0.0250  0.0155  0.0336  36  SER   A N   
245  C CA  A SER   A 30  ? 0.1732 0.1418 0.2658 0.0284  0.0220  0.0304  36  SER   A CA  
246  C CA  B SER   A 30  ? 0.1867 0.1553 0.2784 0.0283  0.0218  0.0301  36  SER   A CA  
247  C C   . SER   A 30  ? 0.1805 0.1585 0.2808 0.0316  0.0213  0.0379  36  SER   A C   
248  O O   . SER   A 30  ? 0.1926 0.1693 0.2906 0.0327  0.0236  0.0331  36  SER   A O   
249  C CB  A SER   A 30  ? 0.1777 0.1350 0.2820 0.0307  0.0298  0.0311  36  SER   A CB  
250  C CB  B SER   A 30  ? 0.2319 0.1882 0.3335 0.0301  0.0298  0.0287  36  SER   A CB  
251  O OG  A SER   A 30  ? 0.1708 0.1217 0.2830 0.0340  0.0377  0.0285  36  SER   A OG  
252  O OG  B SER   A 30  ? 0.2983 0.2583 0.4147 0.0330  0.0302  0.0407  36  SER   A OG  
253  N N   . SER   A 31  ? 0.1796 0.1684 0.2881 0.0321  0.0175  0.0500  37  SER   A N   
254  C CA  . SER   A 31  ? 0.1746 0.1748 0.2913 0.0343  0.0161  0.0584  37  SER   A CA  
255  C C   . SER   A 31  ? 0.1723 0.1792 0.2756 0.0312  0.0116  0.0536  37  SER   A C   
256  O O   . SER   A 31  ? 0.1817 0.1949 0.2900 0.0331  0.0121  0.0569  37  SER   A O   
257  C CB  . SER   A 31  ? 0.2091 0.2222 0.3362 0.0336  0.0118  0.0736  37  SER   A CB  
258  O OG  . SER   A 31  ? 0.2766 0.2991 0.3908 0.0270  0.0043  0.0745  37  SER   A OG  
259  N N   . ARG   A 32  ? 0.1527 0.1582 0.2406 0.0266  0.0078  0.0460  38  ARG   A N   
260  C CA  . ARG   A 32  ? 0.1580 0.1680 0.2337 0.0236  0.0044  0.0408  38  ARG   A CA  
261  C C   . ARG   A 32  ? 0.1538 0.1539 0.2209 0.0240  0.0068  0.0295  38  ARG   A C   
262  O O   . ARG   A 32  ? 0.1512 0.1538 0.2095 0.0221  0.0046  0.0255  38  ARG   A O   
263  C CB  . ARG   A 32  ? 0.1643 0.1798 0.2299 0.0179  -0.0007 0.0405  38  ARG   A CB  
264  C CG  . ARG   A 32  ? 0.1902 0.2184 0.2604 0.0147  -0.0042 0.0516  38  ARG   A CG  
265  C CD  . ARG   A 32  ? 0.1837 0.2163 0.2429 0.0077  -0.0076 0.0497  38  ARG   A CD  
266  N NE  . ARG   A 32  ? 0.1502 0.1849 0.1986 0.0041  -0.0085 0.0433  38  ARG   A NE  
267  C CZ  . ARG   A 32  ? 0.1735 0.2155 0.2133 -0.0032 -0.0105 0.0429  38  ARG   A CZ  
268  N NH1 . ARG   A 32  ? 0.1968 0.2460 0.2364 -0.0084 -0.0124 0.0488  38  ARG   A NH1 
269  N NH2 . ARG   A 32  ? 0.1723 0.2146 0.2038 -0.0062 -0.0101 0.0369  38  ARG   A NH2 
270  N N   . ASP   A 33  ? 0.1457 0.1351 0.2147 0.0255  0.0113  0.0245  39  ASP   A N   
271  C CA  . ASP   A 33  ? 0.1432 0.1246 0.2029 0.0239  0.0129  0.0146  39  ASP   A CA  
272  C C   . ASP   A 33  ? 0.1396 0.1228 0.1882 0.0202  0.0077  0.0108  39  ASP   A C   
273  O O   . ASP   A 33  ? 0.1470 0.1289 0.1880 0.0186  0.0068  0.0054  39  ASP   A O   
274  C CB  . ASP   A 33  ? 0.1570 0.1379 0.2156 0.0251  0.0157  0.0114  39  ASP   A CB  
275  C CG  . ASP   A 33  ? 0.1683 0.1421 0.2171 0.0222  0.0173  0.0021  39  ASP   A CG  
276  O OD1 . ASP   A 33  ? 0.1820 0.1480 0.2293 0.0202  0.0200  -0.0024 39  ASP   A OD1 
277  O OD2 . ASP   A 33  ? 0.1789 0.1552 0.2212 0.0210  0.0159  -0.0005 39  ASP   A OD2 
278  N N   . LEU   A 34  ? 0.1349 0.1208 0.1835 0.0185  0.0049  0.0135  40  LEU   A N   
279  C CA  . LEU   A 34  ? 0.1282 0.1157 0.1689 0.0154  0.0014  0.0100  40  LEU   A CA  
280  C C   . LEU   A 34  ? 0.1325 0.1156 0.1731 0.0138  0.0015  0.0079  40  LEU   A C   
281  O O   . LEU   A 34  ? 0.1441 0.1255 0.1903 0.0143  0.0030  0.0114  40  LEU   A O   
282  C CB  . LEU   A 34  ? 0.1367 0.1328 0.1761 0.0133  -0.0014 0.0141  40  LEU   A CB  
283  C CG  . LEU   A 34  ? 0.1508 0.1523 0.1876 0.0130  -0.0023 0.0150  40  LEU   A CG  
284  C CD1 . LEU   A 34  ? 0.1624 0.1719 0.1960 0.0087  -0.0043 0.0178  40  LEU   A CD1 
285  C CD2 . LEU   A 34  ? 0.1613 0.1592 0.1923 0.0130  -0.0024 0.0089  40  LEU   A CD2 
286  N N   . LEU   A 35  ? 0.1283 0.1105 0.1636 0.0117  -0.0003 0.0034  41  LEU   A N   
287  C CA  . LEU   A 35  ? 0.1307 0.1111 0.1659 0.0095  -0.0009 0.0018  41  LEU   A CA  
288  C C   . LEU   A 35  ? 0.1244 0.1088 0.1569 0.0080  -0.0034 0.0002  41  LEU   A C   
289  O O   . LEU   A 35  ? 0.1284 0.1140 0.1584 0.0083  -0.0044 -0.0013 41  LEU   A O   
290  C CB  . LEU   A 35  ? 0.1384 0.1121 0.1723 0.0082  0.0010  -0.0024 41  LEU   A CB  
291  C CG  . LEU   A 35  ? 0.1410 0.1133 0.1748 0.0052  0.0002  -0.0042 41  LEU   A CG  
292  C CD1 . LEU   A 35  ? 0.1681 0.1323 0.2022 0.0034  0.0041  -0.0072 41  LEU   A CD1 
293  C CD2 . LEU   A 35  ? 0.1422 0.1182 0.1726 0.0028  -0.0031 -0.0064 41  LEU   A CD2 
294  N N   . VAL   A 36  ? 0.1255 0.1119 0.1596 0.0063  -0.0038 0.0008  42  VAL   A N   
295  C CA  . VAL   A 36  ? 0.1186 0.1082 0.1530 0.0050  -0.0046 -0.0006 42  VAL   A CA  
296  C C   . VAL   A 36  ? 0.1198 0.1089 0.1568 0.0033  -0.0051 -0.0018 42  VAL   A C   
297  O O   . VAL   A 36  ? 0.1372 0.1249 0.1752 0.0021  -0.0044 -0.0009 42  VAL   A O   
298  C CB  . VAL   A 36  ? 0.1264 0.1202 0.1604 0.0032  -0.0033 0.0007  42  VAL   A CB  
299  C CG1 . VAL   A 36  ? 0.1432 0.1387 0.1795 0.0020  -0.0019 -0.0017 42  VAL   A CG1 
300  C CG2 . VAL   A 36  ? 0.1451 0.1410 0.1763 0.0037  -0.0032 0.0023  42  VAL   A CG2 
301  N N   . SER   A 37  ? 0.1237 0.1145 0.1624 0.0031  -0.0066 -0.0029 43  SER   A N   
302  C CA  . SER   A 37  ? 0.1224 0.1151 0.1649 0.0011  -0.0077 -0.0030 43  SER   A CA  
303  C C   . SER   A 37  ? 0.1345 0.1317 0.1835 0.0016  -0.0069 -0.0023 43  SER   A C   
304  O O   . SER   A 37  ? 0.1321 0.1299 0.1823 0.0032  -0.0054 -0.0023 43  SER   A O   
305  C CB  . SER   A 37  ? 0.1415 0.1339 0.1817 -0.0008 -0.0102 -0.0037 43  SER   A CB  
306  O OG  . SER   A 37  ? 0.1520 0.1468 0.1919 0.0001  -0.0120 -0.0027 43  SER   A OG  
307  N N   . SER   A 38  ? 0.1413 0.1415 0.1958 0.0000  -0.0070 -0.0018 44  SER   A N   
308  C CA  . SER   A 38  ? 0.1510 0.1555 0.2149 0.0008  -0.0050 -0.0009 44  SER   A CA  
309  C C   . SER   A 38  ? 0.1721 0.1814 0.2429 0.0017  -0.0080 0.0025  44  SER   A C   
310  O O   . SER   A 38  ? 0.1968 0.2080 0.2646 -0.0005 -0.0124 0.0039  44  SER   A O   
311  C CB  . SER   A 38  ? 0.1809 0.1873 0.2488 -0.0014 -0.0031 -0.0015 44  SER   A CB  
312  O OG  . SER   A 38  ? 0.2231 0.2312 0.2909 -0.0036 -0.0067 -0.0004 44  SER   A OG  
313  N N   . THR   A 39  ? 0.1661 0.1776 0.2466 0.0042  -0.0054 0.0042  45  THR   A N   
314  C CA  . THR   A 39  ? 0.1798 0.1971 0.2698 0.0054  -0.0083 0.0097  45  THR   A CA  
315  C C   . THR   A 39  ? 0.2015 0.2242 0.3078 0.0067  -0.0053 0.0127  45  THR   A C   
316  O O   . THR   A 39  ? 0.1895 0.2094 0.2995 0.0073  0.0011  0.0091  45  THR   A O   
317  C CB  . THR   A 39  ? 0.1904 0.2049 0.2802 0.0081  -0.0072 0.0106  45  THR   A CB  
318  O OG1 . THR   A 39  ? 0.1996 0.2103 0.2946 0.0100  -0.0001 0.0078  45  THR   A OG1 
319  C CG2 . THR   A 39  ? 0.2072 0.2170 0.2825 0.0072  -0.0093 0.0077  45  THR   A CG2 
320  N N   . THR   A 40  ? 0.2098 0.2409 0.3265 0.0068  -0.0095 0.0197  46  THR   A N   
321  C CA  . THR   A 40  ? 0.2224 0.2601 0.3584 0.0088  -0.0067 0.0244  46  THR   A CA  
322  C C   . THR   A 40  ? 0.2185 0.2532 0.3667 0.0136  -0.0007 0.0261  46  THR   A C   
323  O O   . THR   A 40  ? 0.2377 0.2704 0.3975 0.0157  0.0075  0.0240  46  THR   A O   
324  C CB  . THR   A 40  ? 0.2711 0.3211 0.4147 0.0062  -0.0142 0.0329  46  THR   A CB  
325  O OG1 . THR   A 40  ? 0.3348 0.3882 0.4763 0.0058  -0.0198 0.0384  46  THR   A OG1 
326  C CG2 . THR   A 40  ? 0.2854 0.3368 0.4169 0.0006  -0.0184 0.0298  46  THR   A CG2 
327  N N   . ALA   A 41  ? 0.2238 0.2572 0.3684 0.0148  -0.0037 0.0290  47  ALA   A N   
328  C CA  . ALA   A 41  ? 0.2366 0.2663 0.3925 0.0190  0.0020  0.0310  47  ALA   A CA  
329  C C   . ALA   A 41  ? 0.2265 0.2447 0.3700 0.0188  0.0083  0.0216  47  ALA   A C   
330  O O   . ALA   A 41  ? 0.2180 0.2328 0.3435 0.0161  0.0051  0.0169  47  ALA   A O   
331  C CB  . ALA   A 41  ? 0.2673 0.3021 0.4252 0.0195  -0.0047 0.0394  47  ALA   A CB  
332  N N   . GLN   A 42  ? 0.2078 0.2202 0.3613 0.0211  0.0174  0.0194  48  GLN   A N   
333  C CA  . GLN   A 42  ? 0.2190 0.2217 0.3607 0.0193  0.0236  0.0109  48  GLN   A CA  
334  C C   . GLN   A 42  ? 0.2176 0.2178 0.3529 0.0202  0.0202  0.0131  48  GLN   A C   
335  O O   . GLN   A 42  ? 0.2268 0.2298 0.3742 0.0233  0.0184  0.0208  48  GLN   A O   
336  C CB  . GLN   A 42  ? 0.2466 0.2434 0.4005 0.0198  0.0361  0.0063  48  GLN   A CB  
337  C CG  . GLN   A 42  ? 0.3250 0.3230 0.4807 0.0174  0.0411  0.0015  48  GLN   A CG  
338  C CD  . GLN   A 42  ? 0.4057 0.3969 0.5720 0.0166  0.0549  -0.0045 48  GLN   A CD  
339  O OE1 . GLN   A 42  ? 0.3843 0.3757 0.5728 0.0210  0.0608  -0.0001 48  GLN   A OE1 
340  N NE2 . GLN   A 42  ? 0.4422 0.4276 0.5933 0.0106  0.0606  -0.0142 48  GLN   A NE2 
341  N N   . GLY   A 43  ? 0.1758 0.1714 0.2930 0.0173  0.0193  0.0073  49  GLY   A N   
342  C CA  . GLY   A 43  ? 0.1718 0.1649 0.2818 0.0176  0.0166  0.0085  49  GLY   A CA  
343  C C   . GLY   A 43  ? 0.1655 0.1508 0.2774 0.0172  0.0251  0.0044  49  GLY   A C   
344  O O   . GLY   A 43  ? 0.1851 0.1660 0.3003 0.0153  0.0340  -0.0015 49  GLY   A O   
345  N N   . CYS   A 44  ? 0.1604 0.1439 0.2676 0.0177  0.0226  0.0065  50  CYS   A N   
346  C CA  . CYS   A 44  ? 0.1684 0.1443 0.2781 0.0170  0.0305  0.0033  50  CYS   A CA  
347  C C   . CYS   A 44  ? 0.1695 0.1422 0.2613 0.0125  0.0308  -0.0031 50  CYS   A C   
348  O O   . CYS   A 44  ? 0.1820 0.1482 0.2739 0.0104  0.0378  -0.0068 50  CYS   A O   
349  C CB  . CYS   A 44  ? 0.1728 0.1487 0.2954 0.0209  0.0292  0.0117  50  CYS   A CB  
350  S SG  . CYS   A 44  ? 0.2126 0.1933 0.3616 0.0261  0.0306  0.0211  50  CYS   A SG  
351  N N   . ASP   A 45  ? 0.1569 0.1341 0.2349 0.0110  0.0236  -0.0035 51  ASP   A N   
352  C CA  . ASP   A 45  ? 0.1493 0.1255 0.2126 0.0071  0.0234  -0.0078 51  ASP   A CA  
353  C C   . ASP   A 45  ? 0.1770 0.1517 0.2348 0.0015  0.0298  -0.0147 51  ASP   A C   
354  O O   . ASP   A 45  ? 0.2005 0.1767 0.2614 0.0009  0.0314  -0.0161 51  ASP   A O   
355  C CB  . ASP   A 45  ? 0.1489 0.1305 0.2021 0.0077  0.0148  -0.0055 51  ASP   A CB  
356  C CG  . ASP   A 45  ? 0.1617 0.1452 0.2166 0.0108  0.0089  0.0002  51  ASP   A CG  
357  O OD1 . ASP   A 45  ? 0.1694 0.1504 0.2275 0.0115  0.0104  0.0021  51  ASP   A OD1 
358  O OD2 . ASP   A 45  ? 0.1689 0.1564 0.2211 0.0117  0.0032  0.0025  51  ASP   A OD2 
359  N N   . THR   A 46  ? 0.1938 0.1665 0.2428 -0.0034 0.0332  -0.0188 52  THR   A N   
360  C CA  . THR   A 46  ? 0.2191 0.1922 0.2594 -0.0113 0.0386  -0.0252 52  THR   A CA  
361  C C   . THR   A 46  ? 0.2049 0.1847 0.2315 -0.0146 0.0323  -0.0238 52  THR   A C   
362  O O   . THR   A 46  ? 0.2217 0.2024 0.2454 -0.0126 0.0282  -0.0210 52  THR   A O   
363  C CB  . THR   A 46  ? 0.3035 0.2691 0.3456 -0.0161 0.0490  -0.0312 52  THR   A CB  
364  O OG1 . THR   A 46  ? 0.3608 0.3208 0.4184 -0.0128 0.0561  -0.0322 52  THR   A OG1 
365  C CG2 . THR   A 46  ? 0.3597 0.3270 0.3884 -0.0269 0.0539  -0.0380 52  THR   A CG2 
366  N N   . ILE   A 47  ? 0.1899 0.1751 0.2090 -0.0197 0.0316  -0.0250 53  ILE   A N   
367  C CA  . ILE   A 47  ? 0.1741 0.1671 0.1835 -0.0225 0.0256  -0.0218 53  ILE   A CA  
368  C C   . ILE   A 47  ? 0.1780 0.1735 0.1776 -0.0321 0.0295  -0.0254 53  ILE   A C   
369  O O   . ILE   A 47  ? 0.1973 0.1912 0.1935 -0.0399 0.0367  -0.0313 53  ILE   A O   
370  C CB  . ILE   A 47  ? 0.1775 0.1765 0.1850 -0.0233 0.0219  -0.0190 53  ILE   A CB  
371  C CG1 . ILE   A 47  ? 0.1900 0.1863 0.2064 -0.0155 0.0190  -0.0165 53  ILE   A CG1 
372  C CG2 . ILE   A 47  ? 0.1722 0.1798 0.1736 -0.0246 0.0155  -0.0134 53  ILE   A CG2 
373  C CD1 . ILE   A 47  ? 0.2021 0.1974 0.2218 -0.0082 0.0133  -0.0123 53  ILE   A CD1 
374  N N   . ALA   A 48  ? 0.1621 0.1620 0.1569 -0.0325 0.0254  -0.0223 54  ALA   A N   
375  C CA  . ALA   A 48  ? 0.1713 0.1763 0.1560 -0.0425 0.0274  -0.0243 54  ALA   A CA  
376  C C   . ALA   A 48  ? 0.1740 0.1900 0.1513 -0.0505 0.0250  -0.0218 54  ALA   A C   
377  O O   . ALA   A 48  ? 0.1798 0.2015 0.1599 -0.0462 0.0188  -0.0154 54  ALA   A O   
378  C CB  . ALA   A 48  ? 0.1712 0.1803 0.1545 -0.0400 0.0223  -0.0197 54  ALA   A CB  
379  N N   . ARG   A 49  ? 0.2003 0.2193 0.1679 -0.0631 0.0303  -0.0269 55  ARG   A N   
380  C CA  . ARG   A 49  ? 0.2264 0.2579 0.1854 -0.0729 0.0276  -0.0236 55  ARG   A CA  
381  C C   . ARG   A 49  ? 0.2473 0.2874 0.1959 -0.0839 0.0274  -0.0234 55  ARG   A C   
382  O O   . ARG   A 49  ? 0.2708 0.3090 0.2102 -0.0958 0.0349  -0.0314 55  ARG   A O   
383  C CB  . ARG   A 49  ? 0.2493 0.2773 0.2052 -0.0797 0.0348  -0.0304 55  ARG   A CB  
384  C CG  . ARG   A 49  ? 0.2415 0.2612 0.2087 -0.0693 0.0357  -0.0310 55  ARG   A CG  
385  C CD  . ARG   A 49  ? 0.2165 0.2424 0.1891 -0.0613 0.0263  -0.0214 55  ARG   A CD  
386  N NE  . ARG   A 49  ? 0.2043 0.2226 0.1866 -0.0528 0.0275  -0.0226 55  ARG   A NE  
387  C CZ  . ARG   A 49  ? 0.2085 0.2278 0.1973 -0.0442 0.0210  -0.0163 55  ARG   A CZ  
388  N NH1 . ARG   A 49  ? 0.1928 0.2198 0.1809 -0.0425 0.0139  -0.0084 55  ARG   A NH1 
389  N NH2 . ARG   A 49  ? 0.2259 0.2388 0.2230 -0.0377 0.0222  -0.0178 55  ARG   A NH2 
390  N N   . CYS   A 50  ? 0.2421 0.2922 0.1925 -0.0807 0.0192  -0.0143 56  CYS   A N   
391  C CA  . CYS   A 50  ? 0.2323 0.2909 0.1759 -0.0883 0.0177  -0.0125 56  CYS   A CA  
392  C C   . CYS   A 50  ? 0.2349 0.3073 0.1839 -0.0838 0.0081  0.0000  56  CYS   A C   
393  O O   . CYS   A 50  ? 0.2568 0.3303 0.2152 -0.0740 0.0033  0.0067  56  CYS   A O   
394  C CB  . CYS   A 50  ? 0.2336 0.2791 0.1795 -0.0837 0.0227  -0.0192 56  CYS   A CB  
395  S SG  . CYS   A 50  ? 0.2247 0.2638 0.1844 -0.0655 0.0174  -0.0138 56  CYS   A SG  
396  N N   . ASP   A 51  ? 0.2699 0.3524 0.2142 -0.0906 0.0059  0.0031  57  ASP   A N   
397  C CA  . ASP   A 51  ? 0.2875 0.3831 0.2395 -0.0857 -0.0020 0.0151  57  ASP   A CA  
398  C C   . ASP   A 51  ? 0.2710 0.3617 0.2252 -0.0810 -0.0011 0.0130  57  ASP   A C   
399  O O   . ASP   A 51  ? 0.2679 0.3716 0.2247 -0.0823 -0.0058 0.0209  57  ASP   A O   
400  C CB  . ASP   A 51  ? 0.3596 0.4769 0.3064 -0.0986 -0.0073 0.0246  57  ASP   A CB  
401  C CG  . ASP   A 51  ? 0.4533 0.5766 0.3857 -0.1148 -0.0042 0.0193  57  ASP   A CG  
402  O OD1 . ASP   A 51  ? 0.4698 0.5785 0.3966 -0.1160 0.0032  0.0073  57  ASP   A OD1 
403  O OD2 . ASP   A 51  ? 0.5051 0.6481 0.4322 -0.1272 -0.0090 0.0273  57  ASP   A OD2 
404  N N   . CYS   A 52  ? 0.2372 0.3104 0.1921 -0.0749 0.0045  0.0038  58  CYS   A N   
405  C CA  . CYS   A 52  ? 0.2139 0.2825 0.1713 -0.0699 0.0049  0.0026  58  CYS   A CA  
406  C C   . CYS   A 52  ? 0.2128 0.2881 0.1810 -0.0595 -0.0012 0.0120  58  CYS   A C   
407  O O   . CYS   A 52  ? 0.2088 0.2835 0.1850 -0.0515 -0.0038 0.0162  58  CYS   A O   
408  C CB  . CYS   A 52  ? 0.2308 0.2807 0.1905 -0.0630 0.0105  -0.0057 58  CYS   A CB  
409  S SG  . CYS   A 52  ? 0.2448 0.2831 0.1957 -0.0735 0.0208  -0.0178 58  CYS   A SG  
410  N N   . GLN   A 53  ? 0.1886 0.2689 0.1573 -0.0600 -0.0024 0.0142  59  GLN   A N   
411  C CA  . GLN   A 53  ? 0.1795 0.2643 0.1586 -0.0507 -0.0060 0.0211  59  GLN   A CA  
412  C C   . GLN   A 53  ? 0.1608 0.2355 0.1398 -0.0459 -0.0034 0.0162  59  GLN   A C   
413  O O   . GLN   A 53  ? 0.1675 0.2465 0.1530 -0.0405 -0.0052 0.0206  59  GLN   A O   
414  C CB  . GLN   A 53  ? 0.2043 0.3090 0.1874 -0.0554 -0.0108 0.0317  59  GLN   A CB  
415  C CG  . GLN   A 53  ? 0.2422 0.3587 0.2298 -0.0574 -0.0148 0.0403  59  GLN   A CG  
416  C CD  . GLN   A 53  ? 0.2787 0.4161 0.2746 -0.0602 -0.0199 0.0532  59  GLN   A CD  
417  O OE1 . GLN   A 53  ? 0.3180 0.4712 0.3086 -0.0723 -0.0231 0.0587  59  GLN   A OE1 
418  N NE2 . GLN   A 53  ? 0.2350 0.3745 0.2447 -0.0500 -0.0207 0.0591  59  GLN   A NE2 
419  N N   . THR   A 54  ? 0.1502 0.2114 0.1228 -0.0478 0.0014  0.0074  60  THR   A N   
420  C CA  . THR   A 54  ? 0.1553 0.2060 0.1290 -0.0423 0.0035  0.0039  60  THR   A CA  
421  C C   . THR   A 54  ? 0.1514 0.1870 0.1263 -0.0375 0.0067  -0.0017 60  THR   A C   
422  O O   . THR   A 54  ? 0.1742 0.2061 0.1464 -0.0415 0.0096  -0.0054 60  THR   A O   
423  C CB  . THR   A 54  ? 0.1996 0.2503 0.1664 -0.0500 0.0062  0.0007  60  THR   A CB  
424  O OG1 . THR   A 54  ? 0.2808 0.3253 0.2404 -0.0585 0.0114  -0.0060 60  THR   A OG1 
425  C CG2 . THR   A 54  ? 0.1937 0.2610 0.1596 -0.0560 0.0029  0.0066  60  THR   A CG2 
426  N N   . GLY   A 55  ? 0.1407 0.1692 0.1200 -0.0294 0.0061  -0.0015 61  GLY   A N   
427  C CA  . GLY   A 55  ? 0.1457 0.1623 0.1280 -0.0247 0.0081  -0.0047 61  GLY   A CA  
428  C C   . GLY   A 55  ? 0.1339 0.1458 0.1194 -0.0182 0.0067  -0.0033 61  GLY   A C   
429  O O   . GLY   A 55  ? 0.1407 0.1561 0.1245 -0.0187 0.0058  -0.0018 61  GLY   A O   
430  N N   . VAL   A 56  ? 0.1249 0.1298 0.1145 -0.0130 0.0063  -0.0037 62  VAL   A N   
431  C CA  . VAL   A 56  ? 0.1155 0.1166 0.1070 -0.0085 0.0047  -0.0020 62  VAL   A CA  
432  C C   . VAL   A 56  ? 0.1217 0.1223 0.1166 -0.0036 0.0021  -0.0008 62  VAL   A C   
433  O O   . VAL   A 56  ? 0.1330 0.1315 0.1307 -0.0030 0.0026  -0.0018 62  VAL   A O   
434  C CB  . VAL   A 56  ? 0.1412 0.1337 0.1348 -0.0092 0.0076  -0.0029 62  VAL   A CB  
435  C CG1 . VAL   A 56  ? 0.1748 0.1649 0.1707 -0.0054 0.0048  0.0004  62  VAL   A CG1 
436  C CG2 . VAL   A 56  ? 0.1469 0.1383 0.1366 -0.0148 0.0111  -0.0048 62  VAL   A CG2 
437  N N   . TYR   A 57  ? 0.1249 0.1274 0.1193 -0.0008 -0.0001 0.0007  63  TYR   A N   
438  C CA  . TYR   A 57  ? 0.1231 0.1243 0.1198 0.0025  -0.0019 0.0009  63  TYR   A CA  
439  C C   . TYR   A 57  ? 0.1342 0.1328 0.1295 0.0031  -0.0035 0.0019  63  TYR   A C   
440  O O   . TYR   A 57  ? 0.1378 0.1369 0.1301 0.0016  -0.0035 0.0027  63  TYR   A O   
441  C CB  . TYR   A 57  ? 0.1300 0.1358 0.1278 0.0043  -0.0019 0.0012  63  TYR   A CB  
442  C CG  . TYR   A 57  ? 0.1232 0.1310 0.1196 0.0050  -0.0012 0.0012  63  TYR   A CG  
443  C CD1 . TYR   A 57  ? 0.1435 0.1558 0.1388 0.0034  -0.0001 0.0022  63  TYR   A CD1 
444  C CD2 . TYR   A 57  ? 0.1339 0.1392 0.1298 0.0063  -0.0009 -0.0002 63  TYR   A CD2 
445  C CE1 . TYR   A 57  ? 0.1536 0.1678 0.1483 0.0040  0.0015  0.0018  63  TYR   A CE1 
446  C CE2 . TYR   A 57  ? 0.1474 0.1540 0.1419 0.0062  0.0014  -0.0014 63  TYR   A CE2 
447  C CZ  . TYR   A 57  ? 0.1658 0.1768 0.1601 0.0053  0.0027  -0.0003 63  TYR   A CZ  
448  O OH  . TYR   A 57  ? 0.1992 0.2117 0.1927 0.0050  0.0058  -0.0017 63  TYR   A OH  
449  N N   . TYR   A 58  ? 0.1246 0.1215 0.1218 0.0045  -0.0053 0.0023  64  TYR   A N   
450  C CA  . TYR   A 58  ? 0.1243 0.1210 0.1192 0.0034  -0.0076 0.0039  64  TYR   A CA  
451  C C   . TYR   A 58  ? 0.1236 0.1219 0.1141 0.0027  -0.0072 0.0015  64  TYR   A C   
452  O O   . TYR   A 58  ? 0.1313 0.1290 0.1232 0.0040  -0.0062 -0.0005 64  TYR   A O   
453  C CB  . TYR   A 58  ? 0.1391 0.1344 0.1388 0.0040  -0.0099 0.0063  64  TYR   A CB  
454  C CG  . TYR   A 58  ? 0.1410 0.1386 0.1383 0.0013  -0.0133 0.0097  64  TYR   A CG  
455  C CD1 . TYR   A 58  ? 0.1445 0.1429 0.1409 -0.0004 -0.0144 0.0135  64  TYR   A CD1 
456  C CD2 . TYR   A 58  ? 0.1457 0.1453 0.1407 -0.0005 -0.0155 0.0093  64  TYR   A CD2 
457  C CE1 . TYR   A 58  ? 0.1663 0.1686 0.1594 -0.0042 -0.0181 0.0176  64  TYR   A CE1 
458  C CE2 . TYR   A 58  ? 0.1628 0.1662 0.1537 -0.0049 -0.0190 0.0125  64  TYR   A CE2 
459  C CZ  . TYR   A 58  ? 0.1682 0.1735 0.1584 -0.0068 -0.0206 0.0172  64  TYR   A CZ  
460  O OH  . TYR   A 58  ? 0.2100 0.2208 0.1954 -0.0125 -0.0248 0.0216  64  TYR   A OH  
461  N N   . CYS   A 59  ? 0.1292 0.1289 0.1144 0.0000  -0.0073 0.0017  65  CYS   A N   
462  C CA  . CYS   A 59  ? 0.1352 0.1356 0.1153 -0.0021 -0.0053 -0.0016 65  CYS   A CA  
463  C C   . CYS   A 59  ? 0.1500 0.1514 0.1242 -0.0070 -0.0081 -0.0006 65  CYS   A C   
464  O O   . CYS   A 59  ? 0.1556 0.1592 0.1259 -0.0102 -0.0100 0.0024  65  CYS   A O   
465  C CB  . CYS   A 59  ? 0.1465 0.1489 0.1244 -0.0026 -0.0024 -0.0027 65  CYS   A CB  
466  S SG  . CYS   A 59  ? 0.1643 0.1668 0.1368 -0.0056 0.0025  -0.0078 65  CYS   A SG  
467  N N   . SER   A 60  ? 0.1498 0.1504 0.1233 -0.0084 -0.0087 -0.0022 66  SER   A N   
468  C CA  . SER   A 60  ? 0.1648 0.1685 0.1325 -0.0146 -0.0123 -0.0003 66  SER   A CA  
469  C C   . SER   A 60  ? 0.1684 0.1738 0.1257 -0.0212 -0.0101 -0.0034 66  SER   A C   
470  O O   . SER   A 60  ? 0.1907 0.2010 0.1422 -0.0273 -0.0141 0.0006  66  SER   A O   
471  C CB  . SER   A 60  ? 0.1880 0.1908 0.1569 -0.0155 -0.0131 -0.0020 66  SER   A CB  
472  O OG  . SER   A 60  ? 0.2222 0.2213 0.1875 -0.0168 -0.0077 -0.0091 66  SER   A OG  
473  N N   . SER   A 61  ? 0.1590 0.1614 0.1149 -0.0201 -0.0036 -0.0097 67  SER   A N   
474  C CA  . SER   A 61  ? 0.1689 0.1722 0.1153 -0.0265 0.0003  -0.0138 67  SER   A CA  
475  C C   . SER   A 61  ? 0.1721 0.1789 0.1159 -0.0276 -0.0012 -0.0102 67  SER   A C   
476  O O   . SER   A 61  ? 0.1864 0.1949 0.1219 -0.0336 0.0017  -0.0131 67  SER   A O   
477  C CB  . SER   A 61  ? 0.1840 0.1825 0.1323 -0.0248 0.0091  -0.0215 67  SER   A CB  
478  O OG  . SER   A 61  ? 0.1929 0.1911 0.1508 -0.0171 0.0112  -0.0200 67  SER   A OG  
479  N N   . ARG   A 62  ? 0.1754 0.1830 0.1260 -0.0227 -0.0052 -0.0041 68  ARG   A N   
480  C CA  . ARG   A 62  ? 0.1776 0.1880 0.1263 -0.0241 -0.0071 0.0003  68  ARG   A CA  
481  C C   . ARG   A 62  ? 0.1921 0.2041 0.1447 -0.0240 -0.0137 0.0088  68  ARG   A C   
482  O O   . ARG   A 62  ? 0.1926 0.2060 0.1454 -0.0249 -0.0154 0.0137  68  ARG   A O   
483  C CB  . ARG   A 62  ? 0.1902 0.1990 0.1447 -0.0185 -0.0036 -0.0010 68  ARG   A CB  
484  C CG  . ARG   A 62  ? 0.1930 0.2016 0.1466 -0.0182 0.0032  -0.0073 68  ARG   A CG  
485  C CD  . ARG   A 62  ? 0.1923 0.2036 0.1370 -0.0245 0.0052  -0.0088 68  ARG   A CD  
486  N NE  . ARG   A 62  ? 0.2192 0.2301 0.1652 -0.0238 0.0132  -0.0150 68  ARG   A NE  
487  C CZ  . ARG   A 62  ? 0.2039 0.2125 0.1468 -0.0269 0.0189  -0.0214 68  ARG   A CZ  
488  N NH1 . ARG   A 62  ? 0.2277 0.2347 0.1639 -0.0320 0.0168  -0.0228 68  ARG   A NH1 
489  N NH2 . ARG   A 62  ? 0.2329 0.2407 0.1800 -0.0255 0.0274  -0.0265 68  ARG   A NH2 
490  N N   . ARG   A 63  ? 0.1832 0.1950 0.1411 -0.0223 -0.0167 0.0110  69  ARG   A N   
491  C CA  . ARG   A 63  ? 0.1956 0.2083 0.1621 -0.0202 -0.0214 0.0193  69  ARG   A CA  
492  C C   . ARG   A 63  ? 0.2209 0.2295 0.1941 -0.0152 -0.0193 0.0209  69  ARG   A C   
493  O O   . ARG   A 63  ? 0.2480 0.2570 0.2253 -0.0157 -0.0214 0.0277  69  ARG   A O   
494  C CB  . ARG   A 63  ? 0.2310 0.2502 0.1947 -0.0265 -0.0270 0.0276  69  ARG   A CB  
495  C CG  . ARG   A 63  ? 0.2480 0.2722 0.2069 -0.0321 -0.0300 0.0276  69  ARG   A CG  
496  C CD  . ARG   A 63  ? 0.2528 0.2858 0.2125 -0.0380 -0.0371 0.0390  69  ARG   A CD  
497  N NE  . ARG   A 63  ? 0.2715 0.3111 0.2233 -0.0461 -0.0401 0.0385  69  ARG   A NE  
498  C CZ  . ARG   A 63  ? 0.2464 0.2915 0.1835 -0.0567 -0.0408 0.0367  69  ARG   A CZ  
499  N NH1 . ARG   A 63  ? 0.2564 0.3015 0.1861 -0.0597 -0.0388 0.0357  69  ARG   A NH1 
500  N NH2 . ARG   A 63  ? 0.2688 0.3197 0.1981 -0.0652 -0.0430 0.0352  69  ARG   A NH2 
501  N N   . LYS   A 64  ? 0.1836 0.1888 0.1582 -0.0114 -0.0151 0.0151  70  LYS   A N   
502  C CA  . LYS   A 64  ? 0.1918 0.1941 0.1703 -0.0089 -0.0127 0.0154  70  LYS   A CA  
503  C C   . LYS   A 64  ? 0.1733 0.1728 0.1566 -0.0048 -0.0100 0.0117  70  LYS   A C   
504  O O   . LYS   A 64  ? 0.1732 0.1735 0.1556 -0.0035 -0.0088 0.0077  70  LYS   A O   
505  C CB  . LYS   A 64  ? 0.2454 0.2495 0.2169 -0.0114 -0.0104 0.0130  70  LYS   A CB  
506  C CG  . LYS   A 64  ? 0.3682 0.3743 0.3358 -0.0158 -0.0127 0.0183  70  LYS   A CG  
507  C CD  . LYS   A 64  ? 0.4809 0.4885 0.4430 -0.0180 -0.0099 0.0160  70  LYS   A CD  
508  C CE  . LYS   A 64  ? 0.5578 0.5676 0.5154 -0.0231 -0.0124 0.0217  70  LYS   A CE  
509  N NZ  . LYS   A 64  ? 0.6089 0.6235 0.5590 -0.0285 -0.0152 0.0230  70  LYS   A NZ  
510  N N   . HIS   A 65  ? 0.1577 0.1540 0.1460 -0.0036 -0.0082 0.0127  71  HIS   A N   
511  C CA  . HIS   A 65  ? 0.1492 0.1439 0.1402 -0.0019 -0.0052 0.0090  71  HIS   A CA  
512  C C   . HIS   A 65  ? 0.1702 0.1668 0.1572 -0.0038 -0.0029 0.0070  71  HIS   A C   
513  O O   . HIS   A 65  ? 0.2097 0.2051 0.1952 -0.0061 -0.0022 0.0087  71  HIS   A O   
514  C CB  . HIS   A 65  ? 0.1397 0.1291 0.1382 -0.0011 -0.0034 0.0104  71  HIS   A CB  
515  C CG  . HIS   A 65  ? 0.1589 0.1476 0.1637 0.0012  -0.0055 0.0130  71  HIS   A CG  
516  N ND1 . HIS   A 65  ? 0.2020 0.1901 0.2102 0.0030  -0.0045 0.0104  71  HIS   A ND1 
517  C CD2 . HIS   A 65  ? 0.1534 0.1431 0.1622 0.0012  -0.0087 0.0189  71  HIS   A CD2 
518  C CE1 . HIS   A 65  ? 0.1731 0.1613 0.1877 0.0044  -0.0068 0.0143  71  HIS   A CE1 
519  N NE2 . HIS   A 65  ? 0.1963 0.1861 0.2115 0.0033  -0.0096 0.0198  71  HIS   A NE2 
520  N N   . TYR   A 66  ? 0.1437 0.1441 0.1299 -0.0032 -0.0017 0.0043  72  TYR   A N   
521  C CA  . TYR   A 66  ? 0.1457 0.1507 0.1294 -0.0053 0.0000  0.0034  72  TYR   A CA  
522  C C   . TYR   A 66  ? 0.1436 0.1506 0.1287 -0.0068 0.0015  0.0023  72  TYR   A C   
523  O O   . TYR   A 66  ? 0.1374 0.1454 0.1252 -0.0052 0.0011  0.0018  72  TYR   A O   
524  C CB  . TYR   A 66  ? 0.1543 0.1647 0.1376 -0.0037 0.0003  0.0028  72  TYR   A CB  
525  C CG  . TYR   A 66  ? 0.1761 0.1859 0.1555 -0.0043 0.0001  0.0026  72  TYR   A CG  
526  C CD1 . TYR   A 66  ? 0.1982 0.2096 0.1736 -0.0072 0.0007  0.0033  72  TYR   A CD1 
527  C CD2 . TYR   A 66  ? 0.1730 0.1811 0.1518 -0.0032 -0.0005 0.0014  72  TYR   A CD2 
528  C CE1 . TYR   A 66  ? 0.2074 0.2191 0.1778 -0.0091 0.0008  0.0029  72  TYR   A CE1 
529  C CE2 . TYR   A 66  ? 0.1953 0.2036 0.1686 -0.0058 -0.0002 0.0005  72  TYR   A CE2 
530  C CZ  . TYR   A 66  ? 0.2102 0.2206 0.1792 -0.0089 0.0004  0.0013  72  TYR   A CZ  
531  O OH  . TYR   A 66  ? 0.2421 0.2533 0.2043 -0.0128 0.0010  0.0002  72  TYR   A OH  
532  N N   . PRO   A 67  ? 0.1389 0.1473 0.1215 -0.0110 0.0033  0.0019  73  PRO   A N   
533  C CA  . PRO   A 67  ? 0.1429 0.1557 0.1250 -0.0148 0.0046  0.0008  73  PRO   A CA  
534  C C   . PRO   A 67  ? 0.1460 0.1695 0.1298 -0.0140 0.0031  0.0032  73  PRO   A C   
535  O O   . PRO   A 67  ? 0.1805 0.2082 0.1647 -0.0129 0.0029  0.0046  73  PRO   A O   
536  C CB  . PRO   A 67  ? 0.1696 0.1808 0.1477 -0.0206 0.0072  -0.0005 73  PRO   A CB  
537  C CG  . PRO   A 67  ? 0.1892 0.1985 0.1662 -0.0190 0.0065  0.0012  73  PRO   A CG  
538  C CD  . PRO   A 67  ? 0.1528 0.1589 0.1324 -0.0134 0.0042  0.0026  73  PRO   A CD  
539  N N   . VAL   A 68  ? 0.1258 0.1541 0.1117 -0.0148 0.0024  0.0041  74  VAL   A N   
540  C CA  . VAL   A 68  ? 0.1419 0.1812 0.1327 -0.0136 0.0009  0.0084  74  VAL   A CA  
541  C C   . VAL   A 68  ? 0.1394 0.1874 0.1295 -0.0193 0.0000  0.0107  74  VAL   A C   
542  O O   . VAL   A 68  ? 0.1489 0.1935 0.1352 -0.0231 0.0007  0.0080  74  VAL   A O   
543  C CB  . VAL   A 68  ? 0.1763 0.2135 0.1730 -0.0069 0.0003  0.0094  74  VAL   A CB  
544  C CG1 . VAL   A 68  ? 0.1983 0.2307 0.1953 -0.0029 0.0014  0.0078  74  VAL   A CG1 
545  C CG2 . VAL   A 68  ? 0.1862 0.2170 0.1822 -0.0063 -0.0002 0.0074  74  VAL   A CG2 
546  N N   . SER   A 69  ? 0.1331 0.1941 0.1279 -0.0203 -0.0016 0.0164  75  SER   A N   
547  C CA  . SER   A 69  ? 0.1358 0.2091 0.1323 -0.0254 -0.0039 0.0216  75  SER   A CA  
548  C C   . SER   A 69  ? 0.1218 0.1978 0.1286 -0.0184 -0.0052 0.0266  75  SER   A C   
549  O O   . SER   A 69  ? 0.1374 0.2121 0.1518 -0.0114 -0.0039 0.0280  75  SER   A O   
550  C CB  . SER   A 69  ? 0.1624 0.2501 0.1612 -0.0298 -0.0052 0.0270  75  SER   A CB  
551  O OG  . SER   A 69  ? 0.2714 0.3560 0.2602 -0.0372 -0.0035 0.0220  75  SER   A OG  
552  N N   . PHE   A 70  ? 0.1283 0.2074 0.1355 -0.0206 -0.0068 0.0289  76  PHE   A N   
553  C CA  . PHE   A 70  ? 0.1299 0.2101 0.1472 -0.0142 -0.0076 0.0337  76  PHE   A CA  
554  C C   . PHE   A 70  ? 0.1358 0.2304 0.1573 -0.0189 -0.0110 0.0425  76  PHE   A C   
555  O O   . PHE   A 70  ? 0.1424 0.2438 0.1555 -0.0285 -0.0127 0.0426  76  PHE   A O   
556  C CB  . PHE   A 70  ? 0.1388 0.2041 0.1531 -0.0099 -0.0061 0.0272  76  PHE   A CB  
557  C CG  . PHE   A 70  ? 0.1371 0.1974 0.1418 -0.0159 -0.0058 0.0221  76  PHE   A CG  
558  C CD1 . PHE   A 70  ? 0.1372 0.1886 0.1342 -0.0183 -0.0035 0.0150  76  PHE   A CD1 
559  C CD2 . PHE   A 70  ? 0.1380 0.2021 0.1426 -0.0190 -0.0071 0.0243  76  PHE   A CD2 
560  C CE1 . PHE   A 70  ? 0.1438 0.1896 0.1343 -0.0233 -0.0015 0.0100  76  PHE   A CE1 
561  C CE2 . PHE   A 70  ? 0.1471 0.2062 0.1432 -0.0250 -0.0055 0.0187  76  PHE   A CE2 
562  C CZ  . PHE   A 70  ? 0.1487 0.1985 0.1385 -0.0269 -0.0021 0.0113  76  PHE   A CZ  
563  N N   . SER   A 71  ? 0.1337 0.2334 0.1686 -0.0129 -0.0117 0.0503  77  SER   A N   
564  C CA  . SER   A 71  ? 0.1309 0.2461 0.1726 -0.0168 -0.0155 0.0613  77  SER   A CA  
565  C C   . SER   A 71  ? 0.1338 0.2459 0.1690 -0.0207 -0.0169 0.0598  77  SER   A C   
566  O O   . SER   A 71  ? 0.1456 0.2427 0.1746 -0.0179 -0.0144 0.0508  77  SER   A O   
567  C CB  . SER   A 71  ? 0.1426 0.2638 0.2041 -0.0083 -0.0148 0.0712  77  SER   A CB  
568  O OG  . SER   A 71  ? 0.1727 0.2794 0.2390 0.0002  -0.0111 0.0670  77  SER   A OG  
569  N N   . LYS   A 72  ? 0.1400 0.2671 0.1768 -0.0276 -0.0210 0.0691  78  LYS   A N   
570  C CA  . LYS   A 72  ? 0.1475 0.2729 0.1786 -0.0318 -0.0222 0.0685  78  LYS   A CA  
571  C C   . LYS   A 72  ? 0.1593 0.2771 0.2022 -0.0219 -0.0211 0.0714  78  LYS   A C   
572  O O   . LYS   A 72  ? 0.1689 0.2894 0.2271 -0.0141 -0.0204 0.0785  78  LYS   A O   
573  C CB  . LYS   A 72  ? 0.1833 0.3290 0.2124 -0.0435 -0.0273 0.0789  78  LYS   A CB  
574  C CG  . LYS   A 72  ? 0.2113 0.3630 0.2255 -0.0558 -0.0274 0.0738  78  LYS   A CG  
575  C CD  . LYS   A 72  ? 0.2962 0.4678 0.3043 -0.0703 -0.0323 0.0824  78  LYS   A CD  
576  C CE  . LYS   A 72  ? 0.3692 0.5447 0.3609 -0.0839 -0.0310 0.0752  78  LYS   A CE  
577  N NZ  . LYS   A 72  ? 0.4255 0.6149 0.4047 -0.1007 -0.0336 0.0780  78  LYS   A NZ  
578  N N   . PRO   A 73  ? 0.1585 0.2670 0.1958 -0.0222 -0.0201 0.0663  79  PRO   A N   
579  C CA  . PRO   A 73  ? 0.1645 0.2650 0.2124 -0.0134 -0.0187 0.0684  79  PRO   A CA  
580  C C   . PRO   A 73  ? 0.1697 0.2836 0.2338 -0.0115 -0.0214 0.0837  79  PRO   A C   
581  O O   . PRO   A 73  ? 0.1944 0.3240 0.2575 -0.0198 -0.0260 0.0929  79  PRO   A O   
582  C CB  . PRO   A 73  ? 0.1985 0.2915 0.2361 -0.0174 -0.0183 0.0618  79  PRO   A CB  
583  C CG  . PRO   A 73  ? 0.2408 0.3328 0.2633 -0.0258 -0.0175 0.0533  79  PRO   A CG  
584  C CD  . PRO   A 73  ? 0.1834 0.2876 0.2048 -0.0309 -0.0193 0.0575  79  PRO   A CD  
585  N N   . SER   A 74  ? 0.1577 0.2658 0.2370 -0.0013 -0.0182 0.0866  80  SER   A N   
586  C CA  . SER   A 74  ? 0.1739 0.2940 0.2731 0.0023  -0.0192 0.1020  80  SER   A CA  
587  C C   . SER   A 74  ? 0.1545 0.2612 0.2677 0.0128  -0.0136 0.1016  80  SER   A C   
588  O O   . SER   A 74  ? 0.1430 0.2324 0.2495 0.0167  -0.0092 0.0891  80  SER   A O   
589  C CB  . SER   A 74  ? 0.2299 0.3614 0.3383 0.0035  -0.0193 0.1081  80  SER   A CB  
590  O OG  . SER   A 74  ? 0.3419 0.4815 0.4358 -0.0055 -0.0226 0.1045  80  SER   A OG  
591  N N   . LEU   A 75  ? 0.1652 0.2809 0.2995 0.0171  -0.0134 0.1162  81  LEU   A N   
592  C CA  . LEU   A 75  ? 0.1869 0.2908 0.3376 0.0266  -0.0068 0.1175  81  LEU   A CA  
593  C C   . LEU   A 75  ? 0.1982 0.3007 0.3627 0.0336  -0.0007 0.1174  81  LEU   A C   
594  O O   . LEU   A 75  ? 0.2164 0.3353 0.3960 0.0342  -0.0024 0.1305  81  LEU   A O   
595  C CB  . LEU   A 75  ? 0.1913 0.3071 0.3592 0.0267  -0.0098 0.1352  81  LEU   A CB  
596  C CG  . LEU   A 75  ? 0.2439 0.3473 0.4302 0.0357  -0.0027 0.1379  81  LEU   A CG  
597  C CD1 . LEU   A 75  ? 0.2641 0.3484 0.4363 0.0355  0.0001  0.1241  81  LEU   A CD1 
598  C CD2 . LEU   A 75  ? 0.2465 0.3643 0.4526 0.0357  -0.0062 0.1586  81  LEU   A CD2 
599  N N   . ILE   A 76  ? 0.1939 0.2789 0.3529 0.0380  0.0062  0.1033  82  ILE   A N   
600  C CA  . ILE   A 76  ? 0.2161 0.2973 0.3833 0.0432  0.0131  0.0994  82  ILE   A CA  
601  C C   . ILE   A 76  ? 0.2220 0.2864 0.4012 0.0507  0.0235  0.0944  82  ILE   A C   
602  O O   . ILE   A 76  ? 0.2106 0.2603 0.3802 0.0502  0.0255  0.0850  82  ILE   A O   
603  C CB  . ILE   A 76  ? 0.2530 0.3279 0.3981 0.0391  0.0121  0.0850  82  ILE   A CB  
604  C CG1 . ILE   A 76  ? 0.2993 0.3880 0.4299 0.0304  0.0031  0.0872  82  ILE   A CG1 
605  C CG2 . ILE   A 76  ? 0.2754 0.3448 0.4258 0.0434  0.0196  0.0790  82  ILE   A CG2 
606  C CD1 . ILE   A 76  ? 0.3337 0.4393 0.4722 0.0289  0.0010  0.0960  82  ILE   A CD1 
607  N N   . PHE   A 77  ? 0.2300 0.2958 0.4301 0.0570  0.0311  0.0995  83  PHE   A N   
608  C CA  . PHE   A 77  ? 0.2322 0.2809 0.4439 0.0633  0.0433  0.0929  83  PHE   A CA  
609  C C   . PHE   A 77  ? 0.2635 0.2986 0.4563 0.0609  0.0479  0.0747  83  PHE   A C   
610  O O   . PHE   A 77  ? 0.2975 0.3386 0.4826 0.0588  0.0461  0.0715  83  PHE   A O   
611  C CB  . PHE   A 77  ? 0.2356 0.2907 0.4782 0.0709  0.0514  0.1046  83  PHE   A CB  
612  C CG  . PHE   A 77  ? 0.2691 0.3059 0.5265 0.0769  0.0651  0.0995  83  PHE   A CG  
613  C CD1 . PHE   A 77  ? 0.3019 0.3322 0.5685 0.0789  0.0665  0.1048  83  PHE   A CD1 
614  C CD2 . PHE   A 77  ? 0.3091 0.3338 0.5689 0.0792  0.0772  0.0878  83  PHE   A CD2 
615  C CE1 . PHE   A 77  ? 0.3360 0.3477 0.6156 0.0835  0.0802  0.0989  83  PHE   A CE1 
616  C CE2 . PHE   A 77  ? 0.3277 0.3343 0.5999 0.0832  0.0912  0.0815  83  PHE   A CE2 
617  C CZ  . PHE   A 77  ? 0.3394 0.3394 0.6223 0.0856  0.0929  0.0872  83  PHE   A CZ  
618  N N   . VAL   A 78  ? 0.2392 0.2569 0.4223 0.0599  0.0525  0.0630  84  VAL   A N   
619  C CA  . VAL   A 78  ? 0.2309 0.2363 0.3957 0.0564  0.0563  0.0467  84  VAL   A CA  
620  C C   . VAL   A 78  ? 0.2275 0.2173 0.4033 0.0596  0.0707  0.0394  84  VAL   A C   
621  O O   . VAL   A 78  ? 0.2346 0.2164 0.4200 0.0618  0.0750  0.0413  84  VAL   A O   
622  C CB  . VAL   A 78  ? 0.2212 0.2212 0.3633 0.0505  0.0489  0.0389  84  VAL   A CB  
623  C CG1 . VAL   A 78  ? 0.2380 0.2275 0.3619 0.0461  0.0519  0.0239  84  VAL   A CG1 
624  C CG2 . VAL   A 78  ? 0.2216 0.2358 0.3542 0.0470  0.0368  0.0455  84  VAL   A CG2 
625  N N   . GLU   A 79  ? 0.2319 0.2168 0.4039 0.0585  0.0780  0.0301  85  GLU   A N   
626  C CA  . GLU   A 79  ? 0.2560 0.2255 0.4360 0.0596  0.0932  0.0209  85  GLU   A CA  
627  C C   . GLU   A 79  ? 0.2686 0.2228 0.4326 0.0541  0.0953  0.0089  85  GLU   A C   
628  O O   . GLU   A 79  ? 0.2688 0.2245 0.4124 0.0488  0.0852  0.0053  85  GLU   A O   
629  C CB  . GLU   A 79  ? 0.3151 0.2840 0.4904 0.0576  0.0997  0.0124  85  GLU   A CB  
630  C CG  . GLU   A 79  ? 0.3930 0.3756 0.5885 0.0636  0.1011  0.0236  85  GLU   A CG  
631  C CD  . GLU   A 79  ? 0.5087 0.4914 0.7366 0.0720  0.1103  0.0346  85  GLU   A CD  
632  O OE1 . GLU   A 79  ? 0.5215 0.4884 0.7590 0.0735  0.1245  0.0273  85  GLU   A OE1 
633  O OE2 . GLU   A 79  ? 0.5682 0.5668 0.8120 0.0766  0.1033  0.0510  85  GLU   A OE2 
634  N N   . ALA   A 80  ? 0.2849 0.2242 0.4588 0.0548  0.1093  0.0023  86  ALA   A N   
635  C CA  . ALA   A 80  ? 0.3169 0.2411 0.4768 0.0484  0.1134  -0.0098 86  ALA   A CA  
636  C C   . ALA   A 80  ? 0.3571 0.2797 0.4897 0.0392  0.1096  -0.0224 86  ALA   A C   
637  O O   . ALA   A 80  ? 0.3685 0.2953 0.4956 0.0374  0.1111  -0.0262 86  ALA   A O   
638  C CB  . ALA   A 80  ? 0.3319 0.2398 0.5076 0.0498  0.1317  -0.0162 86  ALA   A CB  
639  N N   . SER   A 81  ? 0.3698 0.2886 0.4851 0.0331  0.1031  -0.0274 87  SER   A N   
640  C CA  . SER   A 81  ? 0.3844 0.3025 0.4745 0.0235  0.0988  -0.0379 87  SER   A CA  
641  C C   . SER   A 81  ? 0.4042 0.3086 0.4855 0.0162  0.1049  -0.0483 87  SER   A C   
642  O O   . SER   A 81  ? 0.4036 0.2991 0.4992 0.0194  0.1127  -0.0470 87  SER   A O   
643  C CB  . SER   A 81  ? 0.3882 0.3183 0.4661 0.0230  0.0825  -0.0318 87  SER   A CB  
644  O OG  . SER   A 81  ? 0.3643 0.2933 0.4434 0.0238  0.0771  -0.0276 87  SER   A OG  
645  N N   . GLU   A 82  ? 0.4253 0.3295 0.4837 0.0060  0.1002  -0.0569 88  GLU   A N   
646  C CA  . GLU   A 82  ? 0.4297 0.3229 0.4798 -0.0019 0.1048  -0.0655 88  GLU   A CA  
647  C C   . GLU   A 82  ? 0.3637 0.2591 0.4164 0.0010  0.0957  -0.0582 88  GLU   A C   
648  O O   . GLU   A 82  ? 0.3607 0.2466 0.4118 -0.0034 0.1004  -0.0633 88  GLU   A O   
649  C CB  . GLU   A 82  ? 0.5075 0.4000 0.5340 -0.0153 0.1043  -0.0767 88  GLU   A CB  
650  C CG  . GLU   A 82  ? 0.5898 0.4961 0.6019 -0.0175 0.0887  -0.0718 88  GLU   A CG  
651  C CD  . GLU   A 82  ? 0.7289 0.6394 0.7244 -0.0267 0.0885  -0.0781 88  GLU   A CD  
652  O OE1 . GLU   A 82  ? 0.7529 0.6571 0.7356 -0.0383 0.0953  -0.0888 88  GLU   A OE1 
653  O OE2 . GLU   A 82  ? 0.7828 0.7031 0.7773 -0.0231 0.0816  -0.0724 88  GLU   A OE2 
654  N N   . TYR   A 83  ? 0.3199 0.2271 0.3781 0.0084  0.0842  -0.0464 89  TYR   A N   
655  C CA  . TYR   A 83  ? 0.2805 0.1909 0.3399 0.0104  0.0755  -0.0398 89  TYR   A CA  
656  C C   . TYR   A 83  ? 0.2667 0.1773 0.3464 0.0193  0.0771  -0.0294 89  TYR   A C   
657  O O   . TYR   A 83  ? 0.2618 0.1709 0.3443 0.0198  0.0740  -0.0257 89  TYR   A O   
658  C CB  . TYR   A 83  ? 0.2838 0.2072 0.3324 0.0100  0.0616  -0.0350 89  TYR   A CB  
659  C CG  . TYR   A 83  ? 0.2937 0.2184 0.3236 0.0010  0.0587  -0.0429 89  TYR   A CG  
660  C CD1 . TYR   A 83  ? 0.3267 0.2484 0.3457 -0.0067 0.0567  -0.0481 89  TYR   A CD1 
661  C CD2 . TYR   A 83  ? 0.3334 0.2628 0.3571 -0.0005 0.0583  -0.0448 89  TYR   A CD2 
662  C CE1 . TYR   A 83  ? 0.3569 0.2825 0.3597 -0.0157 0.0528  -0.0532 89  TYR   A CE1 
663  C CE2 . TYR   A 83  ? 0.3603 0.2925 0.3672 -0.0093 0.0546  -0.0502 89  TYR   A CE2 
664  C CZ  . TYR   A 83  ? 0.3840 0.3145 0.3808 -0.0171 0.0521  -0.0542 89  TYR   A CZ  
665  O OH  . TYR   A 83  ? 0.4295 0.3651 0.4107 -0.0264 0.0475  -0.0576 89  TYR   A OH  
666  N N   . TYR   A 84  ? 0.2782 0.1922 0.3729 0.0261  0.0813  -0.0234 90  TYR   A N   
667  C CA  . TYR   A 84  ? 0.2688 0.1855 0.3845 0.0342  0.0821  -0.0112 90  TYR   A CA  
668  C C   . TYR   A 84  ? 0.2804 0.1924 0.4156 0.0396  0.0948  -0.0097 90  TYR   A C   
669  O O   . TYR   A 84  ? 0.2869 0.2008 0.4185 0.0386  0.0980  -0.0144 90  TYR   A O   
670  C CB  . TYR   A 84  ? 0.2490 0.1824 0.3656 0.0379  0.0695  0.0007  90  TYR   A CB  
671  C CG  . TYR   A 84  ? 0.2199 0.1593 0.3211 0.0339  0.0576  0.0011  90  TYR   A CG  
672  C CD1 . TYR   A 84  ? 0.2137 0.1509 0.3168 0.0335  0.0550  0.0044  90  TYR   A CD1 
673  C CD2 . TYR   A 84  ? 0.2152 0.1621 0.3012 0.0306  0.0497  -0.0018 90  TYR   A CD2 
674  C CE1 . TYR   A 84  ? 0.2062 0.1491 0.2967 0.0300  0.0451  0.0046  90  TYR   A CE1 
675  C CE2 . TYR   A 84  ? 0.2173 0.1691 0.2918 0.0275  0.0403  -0.0014 90  TYR   A CE2 
676  C CZ  . TYR   A 84  ? 0.1952 0.1447 0.2718 0.0270  0.0385  0.0011  90  TYR   A CZ  
677  O OH  . TYR   A 84  ? 0.1974 0.1517 0.2637 0.0239  0.0304  0.0010  90  TYR   A OH  
678  N N   . PRO   A 85  ? 0.2894 0.1977 0.4466 0.0457  0.1008  -0.0012 91  PRO   A N   
679  C CA  . PRO   A 85  ? 0.2928 0.1994 0.4740 0.0527  0.1124  0.0037  91  PRO   A CA  
680  C C   . PRO   A 85  ? 0.2930 0.2186 0.4807 0.0577  0.1028  0.0164  91  PRO   A C   
681  O O   . PRO   A 85  ? 0.2792 0.2173 0.4547 0.0558  0.0887  0.0216  91  PRO   A O   
682  C CB  . PRO   A 85  ? 0.3155 0.2150 0.5186 0.0578  0.1185  0.0123  91  PRO   A CB  
683  C CG  . PRO   A 85  ? 0.3302 0.2377 0.5233 0.0560  0.1042  0.0192  91  PRO   A CG  
684  C CD  . PRO   A 85  ? 0.2943 0.2011 0.4576 0.0471  0.0971  0.0061  91  PRO   A CD  
685  N N   . ALA   A 86  ? 0.3036 0.2325 0.5122 0.0639  0.1107  0.0223  92  ALA   A N   
686  C CA  . ALA   A 86  ? 0.2970 0.2452 0.5145 0.0682  0.1022  0.0358  92  ALA   A CA  
687  C C   . ALA   A 86  ? 0.2920 0.2505 0.5202 0.0712  0.0929  0.0521  92  ALA   A C   
688  O O   . ALA   A 86  ? 0.3194 0.2700 0.5632 0.0744  0.0989  0.0569  92  ALA   A O   
689  C CB  . ALA   A 86  ? 0.2903 0.2391 0.5326 0.0747  0.1143  0.0400  92  ALA   A CB  
690  N N   . ARG   A 87  ? 0.2782 0.2528 0.4950 0.0686  0.0786  0.0589  93  ARG   A N   
691  C CA  . ARG   A 87  ? 0.2623 0.2471 0.4838 0.0688  0.0691  0.0724  93  ARG   A CA  
692  C C   . ARG   A 87  ? 0.2544 0.2585 0.4653 0.0654  0.0558  0.0794  93  ARG   A C   
693  O O   . ARG   A 87  ? 0.2726 0.2798 0.4706 0.0628  0.0537  0.0722  93  ARG   A O   
694  C CB  . ARG   A 87  ? 0.2670 0.2407 0.4719 0.0640  0.0665  0.0642  93  ARG   A CB  
695  C CG  . ARG   A 87  ? 0.2970 0.2726 0.4723 0.0568  0.0575  0.0528  93  ARG   A CG  
696  C CD  . ARG   A 87  ? 0.2898 0.2542 0.4501 0.0521  0.0566  0.0433  93  ARG   A CD  
697  N NE  . ARG   A 87  ? 0.3105 0.2806 0.4492 0.0464  0.0457  0.0394  93  ARG   A NE  
698  C CZ  . ARG   A 87  ? 0.3452 0.3194 0.4678 0.0429  0.0408  0.0330  93  ARG   A CZ  
699  N NH1 . ARG   A 87  ? 0.3439 0.3198 0.4674 0.0441  0.0440  0.0303  93  ARG   A NH1 
700  N NH2 . ARG   A 87  ? 0.2550 0.2323 0.3620 0.0382  0.0327  0.0300  93  ARG   A NH2 
701  N N   . TYR   A 88  ? 0.2605 0.2769 0.4755 0.0642  0.0471  0.0926  94  TYR   A N   
702  C CA  . TYR   A 88  ? 0.2556 0.2892 0.4579 0.0587  0.0349  0.0979  94  TYR   A CA  
703  C C   . TYR   A 88  ? 0.2319 0.2594 0.4082 0.0521  0.0290  0.0864  94  TYR   A C   
704  O O   . TYR   A 88  ? 0.2537 0.2728 0.4277 0.0513  0.0295  0.0845  94  TYR   A O   
705  C CB  . TYR   A 88  ? 0.2601 0.3106 0.4776 0.0587  0.0286  0.1173  94  TYR   A CB  
706  C CG  . TYR   A 88  ? 0.2612 0.3244 0.5041 0.0641  0.0314  0.1315  94  TYR   A CG  
707  C CD1 . TYR   A 88  ? 0.2653 0.3445 0.5049 0.0613  0.0260  0.1353  94  TYR   A CD1 
708  C CD2 . TYR   A 88  ? 0.2664 0.3248 0.5377 0.0721  0.0406  0.1405  94  TYR   A CD2 
709  C CE1 . TYR   A 88  ? 0.2801 0.3723 0.5441 0.0662  0.0286  0.1486  94  TYR   A CE1 
710  C CE2 . TYR   A 88  ? 0.2757 0.3460 0.5730 0.0778  0.0441  0.1539  94  TYR   A CE2 
711  C CZ  . TYR   A 88  ? 0.2834 0.3713 0.5769 0.0748  0.0377  0.1580  94  TYR   A CZ  
712  O OH  . TYR   A 88  ? 0.3121 0.4139 0.6318 0.0800  0.0405  0.1721  94  TYR   A OH  
713  N N   . GLN   A 89  ? 0.1944 0.2257 0.3520 0.0475  0.0241  0.0786  95  GLN   A N   
714  C CA  . GLN   A 89  ? 0.1817 0.2088 0.3168 0.0415  0.0186  0.0688  95  GLN   A CA  
715  C C   . GLN   A 89  ? 0.1731 0.2165 0.3012 0.0357  0.0093  0.0763  95  GLN   A C   
716  O O   . GLN   A 89  ? 0.1718 0.2276 0.3033 0.0348  0.0069  0.0823  95  GLN   A O   
717  C CB  . GLN   A 89  ? 0.1925 0.2104 0.3131 0.0403  0.0210  0.0546  95  GLN   A CB  
718  C CG  . GLN   A 89  ? 0.1818 0.1965 0.2824 0.0348  0.0157  0.0462  95  GLN   A CG  
719  C CD  . GLN   A 89  ? 0.1825 0.1859 0.2711 0.0338  0.0187  0.0332  95  GLN   A CD  
720  O OE1 . GLN   A 89  ? 0.2174 0.2109 0.3098 0.0359  0.0258  0.0277  95  GLN   A OE1 
721  N NE2 . GLN   A 89  ? 0.1664 0.1715 0.2405 0.0297  0.0136  0.0282  95  GLN   A NE2 
722  N N   . SER   A 90  ? 0.1527 0.1970 0.2716 0.0310  0.0046  0.0764  96  SER   A N   
723  C CA  . SER   A 90  ? 0.1454 0.2043 0.2566 0.0239  -0.0029 0.0824  96  SER   A CA  
724  C C   . SER   A 90  ? 0.1437 0.2000 0.2346 0.0185  -0.0054 0.0708  96  SER   A C   
725  O O   . SER   A 90  ? 0.1552 0.1985 0.2382 0.0202  -0.0025 0.0593  96  SER   A O   
726  C CB  . SER   A 90  ? 0.1829 0.2454 0.2964 0.0210  -0.0059 0.0898  96  SER   A CB  
727  O OG  . SER   A 90  ? 0.2138 0.2625 0.3173 0.0207  -0.0041 0.0790  96  SER   A OG  
728  N N   . HIS   A 91  ? 0.1501 0.2197 0.2337 0.0113  -0.0105 0.0746  97  HIS   A N   
729  C CA  . HIS   A 91  ? 0.1499 0.2178 0.2159 0.0052  -0.0120 0.0649  97  HIS   A CA  
730  C C   . HIS   A 91  ? 0.1260 0.1854 0.1883 0.0089  -0.0089 0.0558  97  HIS   A C   
731  O O   . HIS   A 91  ? 0.1507 0.2014 0.2016 0.0074  -0.0081 0.0457  97  HIS   A O   
732  C CB  . HIS   A 91  ? 0.1676 0.2270 0.2242 0.0025  -0.0119 0.0578  97  HIS   A CB  
733  C CG  . HIS   A 91  ? 0.1747 0.2431 0.2326 -0.0028 -0.0150 0.0661  97  HIS   A CG  
734  N ND1 . HIS   A 91  ? 0.2050 0.2826 0.2517 -0.0127 -0.0179 0.0663  97  HIS   A ND1 
735  C CD2 . HIS   A 91  ? 0.2090 0.2784 0.2779 0.0000  -0.0153 0.0746  97  HIS   A CD2 
736  C CE1 . HIS   A 91  ? 0.2114 0.2963 0.2614 -0.0162 -0.0203 0.0748  97  HIS   A CE1 
737  N NE2 . HIS   A 91  ? 0.2248 0.3051 0.2888 -0.0084 -0.0191 0.0806  97  HIS   A NE2 
738  N N   . LEU   A 92  ? 0.1207 0.1831 0.1930 0.0133  -0.0070 0.0598  98  LEU   A N   
739  C CA  . LEU   A 92  ? 0.1305 0.1856 0.1998 0.0165  -0.0037 0.0520  98  LEU   A CA  
740  C C   . LEU   A 92  ? 0.1306 0.1967 0.1964 0.0123  -0.0060 0.0543  98  LEU   A C   
741  O O   . LEU   A 92  ? 0.1362 0.2165 0.2093 0.0099  -0.0087 0.0646  98  LEU   A O   
742  C CB  . LEU   A 92  ? 0.1477 0.1975 0.2315 0.0241  0.0019  0.0539  98  LEU   A CB  
743  C CG  . LEU   A 92  ? 0.1789 0.2202 0.2592 0.0267  0.0064  0.0451  98  LEU   A CG  
744  C CD1 . LEU   A 92  ? 0.1865 0.2152 0.2541 0.0255  0.0070  0.0342  98  LEU   A CD1 
745  C CD2 . LEU   A 92  ? 0.2054 0.2431 0.3014 0.0330  0.0135  0.0473  98  LEU   A CD2 
746  N N   . MET   A 93  ? 0.1341 0.1940 0.1890 0.0109  -0.0052 0.0454  99  MET   A N   
747  C CA  . MET   A 93  ? 0.1343 0.2025 0.1846 0.0066  -0.0066 0.0460  99  MET   A CA  
748  C C   . MET   A 93  ? 0.1397 0.2021 0.1922 0.0113  -0.0029 0.0417  99  MET   A C   
749  O O   . MET   A 93  ? 0.1473 0.1973 0.1954 0.0142  -0.0003 0.0339  99  MET   A O   
750  C CB  . MET   A 93  ? 0.1470 0.2116 0.1822 0.0001  -0.0081 0.0387  99  MET   A CB  
751  C CG  . MET   A 93  ? 0.1494 0.2188 0.1807 -0.0059 -0.0106 0.0412  99  MET   A CG  
752  S SD  . MET   A 93  ? 0.2029 0.2650 0.2190 -0.0129 -0.0095 0.0313  99  MET   A SD  
753  C CE  . MET   A 93  ? 0.2516 0.2968 0.2685 -0.0050 -0.0069 0.0235  99  MET   A CE  
754  N N   . LEU   A 94  ? 0.1216 0.1938 0.1803 0.0113  -0.0026 0.0467  100 LEU   A N   
755  C CA  . LEU   A 94  ? 0.1333 0.2007 0.1939 0.0151  0.0016  0.0425  100 LEU   A CA  
756  C C   . LEU   A 94  ? 0.1229 0.1931 0.1732 0.0101  0.0001  0.0390  100 LEU   A C   
757  O O   . LEU   A 94  ? 0.1376 0.2180 0.1840 0.0039  -0.0035 0.0428  100 LEU   A O   
758  C CB  . LEU   A 94  ? 0.1517 0.2271 0.2304 0.0201  0.0049  0.0507  100 LEU   A CB  
759  C CG  . LEU   A 94  ? 0.2128 0.2837 0.3054 0.0263  0.0088  0.0542  100 LEU   A CG  
760  C CD1 . LEU   A 94  ? 0.2139 0.2923 0.3270 0.0317  0.0137  0.0622  100 LEU   A CD1 
761  C CD2 . LEU   A 94  ? 0.2540 0.3076 0.3408 0.0291  0.0136  0.0434  100 LEU   A CD2 
762  N N   . ALA   A 95  ? 0.1288 0.1901 0.1739 0.0118  0.0031  0.0319  101 ALA   A N   
763  C CA  . ALA   A 95  ? 0.1190 0.1816 0.1557 0.0078  0.0026  0.0287  101 ALA   A CA  
764  C C   . ALA   A 95  ? 0.1173 0.1762 0.1570 0.0115  0.0073  0.0257  101 ALA   A C   
765  O O   . ALA   A 95  ? 0.1291 0.1812 0.1742 0.0161  0.0114  0.0234  101 ALA   A O   
766  C CB  . ALA   A 95  ? 0.1321 0.1849 0.1550 0.0043  0.0011  0.0216  101 ALA   A CB  
767  N N   . VAL   A 96  ? 0.1245 0.1870 0.1599 0.0084  0.0074  0.0248  102 VAL   A N   
768  C CA  . VAL   A 96  ? 0.1190 0.1781 0.1545 0.0102  0.0118  0.0210  102 VAL   A CA  
769  C C   . VAL   A 96  ? 0.1528 0.1998 0.1746 0.0081  0.0112  0.0134  102 VAL   A C   
770  O O   . VAL   A 96  ? 0.1774 0.2232 0.1905 0.0041  0.0079  0.0123  102 VAL   A O   
771  C CB  . VAL   A 96  ? 0.1240 0.1937 0.1613 0.0074  0.0118  0.0244  102 VAL   A CB  
772  C CG1 . VAL   A 96  ? 0.1422 0.2077 0.1774 0.0081  0.0166  0.0195  102 VAL   A CG1 
773  C CG2 . VAL   A 96  ? 0.1121 0.1961 0.1650 0.0092  0.0117  0.0339  102 VAL   A CG2 
774  N N   . GLY   A 97  ? 0.1650 0.2040 0.1863 0.0105  0.0147  0.0089  103 GLY   A N   
775  C CA  . GLY   A 97  ? 0.1805 0.2103 0.1900 0.0080  0.0134  0.0035  103 GLY   A CA  
776  C C   . GLY   A 97  ? 0.1902 0.2133 0.1998 0.0094  0.0176  -0.0010 103 GLY   A C   
777  O O   . GLY   A 97  ? 0.2089 0.2317 0.2276 0.0127  0.0220  -0.0008 103 GLY   A O   
778  N N   . HIS   A 98  ? 0.2270 0.2443 0.2260 0.0058  0.0166  -0.0051 104 HIS   A N   
779  C CA  . HIS   A 98  ? 0.2446 0.2559 0.2401 0.0044  0.0203  -0.0103 104 HIS   A CA  
780  C C   . HIS   A 98  ? 0.2173 0.2235 0.2133 0.0054  0.0185  -0.0111 104 HIS   A C   
781  O O   . HIS   A 98  ? 0.2210 0.2267 0.2139 0.0050  0.0127  -0.0088 104 HIS   A O   
782  C CB  . HIS   A 98  ? 0.2675 0.2774 0.2508 -0.0015 0.0190  -0.0127 104 HIS   A CB  
783  C CG  . HIS   A 98  ? 0.2805 0.2858 0.2581 -0.0053 0.0234  -0.0186 104 HIS   A CG  
784  N ND1 . HIS   A 98  ? 0.2845 0.2889 0.2655 -0.0056 0.0319  -0.0232 104 HIS   A ND1 
785  C CD2 . HIS   A 98  ? 0.2868 0.2887 0.2564 -0.0097 0.0208  -0.0206 104 HIS   A CD2 
786  C CE1 . HIS   A 98  ? 0.2861 0.2854 0.2593 -0.0108 0.0348  -0.0289 104 HIS   A CE1 
787  N NE2 . HIS   A 98  ? 0.2788 0.2773 0.2444 -0.0138 0.0275  -0.0271 104 HIS   A NE2 
788  N N   . SER   A 99  ? 0.2170 0.2185 0.2168 0.0064  0.0237  -0.0146 105 SER   A N   
789  C CA  . SER   A 99  ? 0.2349 0.2316 0.2352 0.0070  0.0225  -0.0156 105 SER   A CA  
790  C C   . SER   A 99  ? 0.2751 0.2652 0.2748 0.0048  0.0300  -0.0222 105 SER   A C   
791  O O   . SER   A 99  ? 0.2959 0.2843 0.3059 0.0082  0.0372  -0.0230 105 SER   A O   
792  C CB  . SER   A 99  ? 0.2480 0.2472 0.2597 0.0125  0.0213  -0.0104 105 SER   A CB  
793  O OG  . SER   A 99  ? 0.2739 0.2683 0.2871 0.0132  0.0207  -0.0112 105 SER   A OG  
794  N N   . GLU   A 100 ? 0.2286 0.2152 0.2175 -0.0012 0.0287  -0.0263 106 GLU   A N   
795  C CA  . GLU   A 100 ? 0.2262 0.2059 0.2114 -0.0057 0.0354  -0.0337 106 GLU   A CA  
796  C C   . GLU   A 100 ? 0.2474 0.2233 0.2348 -0.0048 0.0330  -0.0333 106 GLU   A C   
797  O O   . GLU   A 100 ? 0.2246 0.2038 0.2142 -0.0017 0.0256  -0.0276 106 GLU   A O   
798  C CB  . GLU   A 100 ? 0.2431 0.2237 0.2128 -0.0152 0.0341  -0.0377 106 GLU   A CB  
799  C CG  . GLU   A 100 ? 0.2808 0.2651 0.2479 -0.0166 0.0367  -0.0382 106 GLU   A CG  
800  C CD  . GLU   A 100 ? 0.3420 0.3290 0.2934 -0.0266 0.0346  -0.0405 106 GLU   A CD  
801  O OE1 . GLU   A 100 ? 0.3994 0.3849 0.3415 -0.0341 0.0336  -0.0437 106 GLU   A OE1 
802  O OE2 . GLU   A 100 ? 0.3214 0.3129 0.2698 -0.0277 0.0338  -0.0387 106 GLU   A OE2 
803  N N   . PRO   A 101 ? 0.2544 0.2228 0.2421 -0.0075 0.0400  -0.0394 107 PRO   A N   
804  C CA  . PRO   A 101 ? 0.2418 0.2067 0.2329 -0.0061 0.0379  -0.0384 107 PRO   A CA  
805  C C   . PRO   A 101 ? 0.2481 0.2175 0.2319 -0.0088 0.0279  -0.0350 107 PRO   A C   
806  O O   . PRO   A 101 ? 0.2406 0.2113 0.2306 -0.0041 0.0233  -0.0301 107 PRO   A O   
807  C CB  . PRO   A 101 ? 0.2706 0.2262 0.2588 -0.0118 0.0476  -0.0474 107 PRO   A CB  
808  C CG  . PRO   A 101 ? 0.2913 0.2446 0.2845 -0.0105 0.0572  -0.0509 107 PRO   A CG  
809  C CD  . PRO   A 101 ? 0.2706 0.2326 0.2574 -0.0114 0.0515  -0.0477 107 PRO   A CD  
810  N N   . GLY   A 102 ? 0.2273 0.1999 0.1989 -0.0163 0.0244  -0.0365 108 GLY   A N   
811  C CA  . GLY   A 102 ? 0.2273 0.2052 0.1938 -0.0193 0.0153  -0.0322 108 GLY   A CA  
812  C C   . GLY   A 102 ? 0.1913 0.1748 0.1630 -0.0135 0.0085  -0.0245 108 GLY   A C   
813  O O   . GLY   A 102 ? 0.1984 0.1856 0.1697 -0.0143 0.0019  -0.0202 108 GLY   A O   
814  N N   . ASP   A 103 ? 0.1805 0.1647 0.1578 -0.0080 0.0105  -0.0228 109 ASP   A N   
815  C CA  . ASP   A 103 ? 0.1684 0.1568 0.1504 -0.0034 0.0054  -0.0167 109 ASP   A CA  
816  C C   . ASP   A 103 ? 0.1694 0.1569 0.1597 0.0016  0.0041  -0.0142 109 ASP   A C   
817  O O   . ASP   A 103 ? 0.1564 0.1467 0.1495 0.0039  0.0002  -0.0101 109 ASP   A O   
818  C CB  . ASP   A 103 ? 0.1675 0.1581 0.1519 -0.0007 0.0079  -0.0158 109 ASP   A CB  
819  C CG  . ASP   A 103 ? 0.1793 0.1720 0.1550 -0.0058 0.0076  -0.0168 109 ASP   A CG  
820  O OD1 . ASP   A 103 ? 0.1886 0.1834 0.1586 -0.0098 0.0025  -0.0145 109 ASP   A OD1 
821  O OD2 . ASP   A 103 ? 0.1861 0.1792 0.1618 -0.0058 0.0124  -0.0190 109 ASP   A OD2 
822  N N   . CYS   A 104 ? 0.1654 0.1486 0.1593 0.0026  0.0079  -0.0168 110 CYS   A N   
823  C CA  . CYS   A 104 ? 0.1705 0.1535 0.1715 0.0064  0.0063  -0.0139 110 CYS   A CA  
824  C C   . CYS   A 104 ? 0.1577 0.1429 0.1569 0.0049  0.0004  -0.0116 110 CYS   A C   
825  O O   . CYS   A 104 ? 0.1673 0.1529 0.1612 0.0006  -0.0018 -0.0127 110 CYS   A O   
826  C CB  . CYS   A 104 ? 0.1753 0.1527 0.1801 0.0067  0.0112  -0.0168 110 CYS   A CB  
827  S SG  . CYS   A 104 ? 0.1959 0.1713 0.2105 0.0112  0.0189  -0.0165 110 CYS   A SG  
828  N N   . GLY   A 105 ? 0.1351 0.1226 0.1391 0.0081  -0.0017 -0.0081 111 GLY   A N   
829  C CA  . GLY   A 105 ? 0.1416 0.1307 0.1465 0.0075  -0.0056 -0.0061 111 GLY   A CA  
830  C C   . GLY   A 105 ? 0.1318 0.1236 0.1367 0.0077  -0.0076 -0.0035 111 GLY   A C   
831  O O   . GLY   A 105 ? 0.1451 0.1377 0.1536 0.0082  -0.0092 -0.0016 111 GLY   A O   
832  N N   . GLY   A 106 ? 0.1388 0.1315 0.1404 0.0072  -0.0068 -0.0036 112 GLY   A N   
833  C CA  . GLY   A 106 ? 0.1351 0.1294 0.1368 0.0072  -0.0079 -0.0013 112 GLY   A CA  
834  C C   . GLY   A 106 ? 0.1235 0.1183 0.1289 0.0088  -0.0066 -0.0007 112 GLY   A C   
835  O O   . GLY   A 106 ? 0.1265 0.1227 0.1329 0.0098  -0.0050 -0.0011 112 GLY   A O   
836  N N   . ILE   A 107 ? 0.1215 0.1156 0.1293 0.0084  -0.0067 0.0005  113 ILE   A N   
837  C CA  . ILE   A 107 ? 0.1210 0.1154 0.1306 0.0079  -0.0045 -0.0002 113 ILE   A CA  
838  C C   . ILE   A 107 ? 0.1142 0.1108 0.1206 0.0063  -0.0030 -0.0004 113 ILE   A C   
839  O O   . ILE   A 107 ? 0.1273 0.1231 0.1318 0.0057  -0.0031 0.0002  113 ILE   A O   
840  C CB  . ILE   A 107 ? 0.1264 0.1179 0.1411 0.0077  -0.0034 0.0001  113 ILE   A CB  
841  C CG1 . ILE   A 107 ? 0.1519 0.1433 0.1708 0.0089  -0.0043 0.0002  113 ILE   A CG1 
842  C CG2 . ILE   A 107 ? 0.1322 0.1227 0.1470 0.0052  0.0007  -0.0020 113 ILE   A CG2 
843  C CD1 . ILE   A 107 ? 0.1909 0.1803 0.2175 0.0095  -0.0030 0.0014  113 ILE   A CD1 
844  N N   . LEU   A 108 ? 0.1050 0.1051 0.1108 0.0048  -0.0019 -0.0006 114 LEU   A N   
845  C CA  . LEU   A 108 ? 0.1112 0.1148 0.1139 0.0013  -0.0005 -0.0005 114 LEU   A CA  
846  C C   . LEU   A 108 ? 0.1136 0.1152 0.1159 -0.0025 0.0024  -0.0029 114 LEU   A C   
847  O O   . LEU   A 108 ? 0.1171 0.1189 0.1210 -0.0030 0.0029  -0.0035 114 LEU   A O   
848  C CB  . LEU   A 108 ? 0.1168 0.1278 0.1201 0.0011  -0.0014 0.0022  114 LEU   A CB  
849  C CG  . LEU   A 108 ? 0.1207 0.1386 0.1210 -0.0041 -0.0008 0.0034  114 LEU   A CG  
850  C CD1 . LEU   A 108 ? 0.1368 0.1552 0.1347 -0.0047 -0.0004 0.0032  114 LEU   A CD1 
851  C CD2 . LEU   A 108 ? 0.1455 0.1728 0.1490 -0.0044 -0.0025 0.0085  114 LEU   A CD2 
852  N N   . ARG   A 109 ? 0.1226 0.1217 0.1229 -0.0057 0.0051  -0.0047 115 ARG   A N   
853  C CA  . ARG   A 109 ? 0.1285 0.1240 0.1286 -0.0103 0.0100  -0.0084 115 ARG   A CA  
854  C C   . ARG   A 109 ? 0.1388 0.1365 0.1328 -0.0169 0.0127  -0.0103 115 ARG   A C   
855  O O   . ARG   A 109 ? 0.1352 0.1350 0.1270 -0.0169 0.0112  -0.0087 115 ARG   A O   
856  C CB  . ARG   A 109 ? 0.1444 0.1314 0.1513 -0.0073 0.0126  -0.0092 115 ARG   A CB  
857  C CG  . ARG   A 109 ? 0.1484 0.1321 0.1561 -0.0062 0.0126  -0.0075 115 ARG   A CG  
858  C CD  . ARG   A 109 ? 0.1729 0.1498 0.1903 -0.0028 0.0147  -0.0059 115 ARG   A CD  
859  N NE  . ARG   A 109 ? 0.1788 0.1581 0.2001 0.0020  0.0095  -0.0020 115 ARG   A NE  
860  C CZ  . ARG   A 109 ? 0.1846 0.1625 0.2139 0.0045  0.0098  -0.0007 115 ARG   A CZ  
861  N NH1 . ARG   A 109 ? 0.1948 0.1690 0.2293 0.0032  0.0156  -0.0039 115 ARG   A NH1 
862  N NH2 . ARG   A 109 ? 0.1895 0.1706 0.2211 0.0075  0.0046  0.0032  115 ARG   A NH2 
863  N N   . CYS   A 110 ? 0.1747 0.1720 0.1656 -0.0236 0.0172  -0.0143 116 CYS   A N   
864  C CA  . CYS   A 110 ? 0.2021 0.2014 0.1856 -0.0325 0.0208  -0.0174 116 CYS   A CA  
865  C C   . CYS   A 110 ? 0.2271 0.2157 0.2123 -0.0361 0.0293  -0.0237 116 CYS   A C   
866  O O   . CYS   A 110 ? 0.2258 0.2066 0.2194 -0.0307 0.0317  -0.0244 116 CYS   A O   
867  C CB  . CYS   A 110 ? 0.1997 0.2106 0.1765 -0.0397 0.0187  -0.0160 116 CYS   A CB  
868  S SG  . CYS   A 110 ? 0.1992 0.2092 0.1745 -0.0446 0.0225  -0.0198 116 CYS   A SG  
869  N N   . GLN   A 111 ? 0.2452 0.2336 0.2229 -0.0462 0.0347  -0.0286 117 GLN   A N   
870  C CA  . GLN   A 111 ? 0.2778 0.2547 0.2574 -0.0507 0.0450  -0.0360 117 GLN   A CA  
871  C C   . GLN   A 111 ? 0.3001 0.2741 0.2828 -0.0516 0.0494  -0.0396 117 GLN   A C   
872  O O   . GLN   A 111 ? 0.3441 0.3068 0.3339 -0.0515 0.0583  -0.0446 117 GLN   A O   
873  C CB  . GLN   A 111 ? 0.3300 0.3074 0.2988 -0.0637 0.0509  -0.0419 117 GLN   A CB  
874  C CG  . GLN   A 111 ? 0.3602 0.3502 0.3172 -0.0744 0.0490  -0.0428 117 GLN   A CG  
875  C CD  . GLN   A 111 ? 0.4620 0.4536 0.4071 -0.0889 0.0546  -0.0487 117 GLN   A CD  
876  O OE1 . GLN   A 111 ? 0.4941 0.4967 0.4327 -0.0932 0.0491  -0.0447 117 GLN   A OE1 
877  N NE2 . GLN   A 111 ? 0.4532 0.4342 0.3960 -0.0971 0.0663  -0.0585 117 GLN   A NE2 
878  N N   . HIS   A 112 ? 0.2556 0.2393 0.2344 -0.0523 0.0439  -0.0369 118 HIS   A N   
879  C CA  . HIS   A 112 ? 0.2497 0.2321 0.2301 -0.0543 0.0478  -0.0403 118 HIS   A CA  
880  C C   . HIS   A 112 ? 0.2458 0.2252 0.2379 -0.0430 0.0445  -0.0363 118 HIS   A C   
881  O O   . HIS   A 112 ? 0.2783 0.2556 0.2738 -0.0435 0.0482  -0.0390 118 HIS   A O   
882  C CB  . HIS   A 112 ? 0.2590 0.2544 0.2283 -0.0631 0.0440  -0.0390 118 HIS   A CB  
883  C CG  . HIS   A 112 ? 0.2906 0.2917 0.2473 -0.0762 0.0463  -0.0420 118 HIS   A CG  
884  N ND1 . HIS   A 112 ? 0.2827 0.2959 0.2342 -0.0780 0.0385  -0.0355 118 HIS   A ND1 
885  C CD2 . HIS   A 112 ? 0.3331 0.3302 0.2817 -0.0889 0.0561  -0.0511 118 HIS   A CD2 
886  C CE1 . HIS   A 112 ? 0.3442 0.3611 0.2846 -0.0916 0.0429  -0.0402 118 HIS   A CE1 
887  N NE2 . HIS   A 112 ? 0.3648 0.3717 0.3022 -0.0990 0.0537  -0.0501 118 HIS   A NE2 
888  N N   . GLY   A 113 ? 0.2068 0.1876 0.2040 -0.0337 0.0371  -0.0297 119 GLY   A N   
889  C CA  . GLY   A 113 ? 0.1964 0.1759 0.2031 -0.0246 0.0333  -0.0258 119 GLY   A CA  
890  C C   . GLY   A 113 ? 0.1665 0.1533 0.1715 -0.0193 0.0238  -0.0194 119 GLY   A C   
891  O O   . GLY   A 113 ? 0.1684 0.1598 0.1681 -0.0204 0.0205  -0.0172 119 GLY   A O   
892  N N   . VAL   A 114 ? 0.1544 0.1422 0.1644 -0.0140 0.0202  -0.0167 120 VAL   A N   
893  C CA  . VAL   A 114 ? 0.1446 0.1375 0.1540 -0.0092 0.0129  -0.0116 120 VAL   A CA  
894  C C   . VAL   A 114 ? 0.1316 0.1327 0.1350 -0.0129 0.0104  -0.0098 120 VAL   A C   
895  O O   . VAL   A 114 ? 0.1421 0.1457 0.1436 -0.0172 0.0121  -0.0110 120 VAL   A O   
896  C CB  . VAL   A 114 ? 0.1424 0.1332 0.1587 -0.0037 0.0107  -0.0099 120 VAL   A CB  
897  C CG1 . VAL   A 114 ? 0.1572 0.1520 0.1722 -0.0002 0.0049  -0.0062 120 VAL   A CG1 
898  C CG2 . VAL   A 114 ? 0.1609 0.1463 0.1849 0.0000  0.0119  -0.0091 120 VAL   A CG2 
899  N N   . VAL   A 115 ? 0.1267 0.1326 0.1281 -0.0115 0.0067  -0.0062 121 VAL   A N   
900  C CA  . VAL   A 115 ? 0.1363 0.1515 0.1350 -0.0142 0.0039  -0.0022 121 VAL   A CA  
901  C C   . VAL   A 115 ? 0.1298 0.1463 0.1336 -0.0084 0.0003  0.0019  121 VAL   A C   
902  O O   . VAL   A 115 ? 0.1369 0.1594 0.1418 -0.0099 -0.0013 0.0058  121 VAL   A O   
903  C CB  . VAL   A 115 ? 0.1452 0.1655 0.1409 -0.0162 0.0028  -0.0002 121 VAL   A CB  
904  C CG1 . VAL   A 115 ? 0.1651 0.1969 0.1619 -0.0174 -0.0008 0.0065  121 VAL   A CG1 
905  C CG2 . VAL   A 115 ? 0.1680 0.1871 0.1577 -0.0235 0.0069  -0.0046 121 VAL   A CG2 
906  N N   . GLY   A 116 ? 0.1340 0.1454 0.1411 -0.0025 -0.0007 0.0017  122 GLY   A N   
907  C CA  . GLY   A 116 ? 0.1371 0.1482 0.1486 0.0022  -0.0027 0.0043  122 GLY   A CA  
908  C C   . GLY   A 116 ? 0.1294 0.1350 0.1417 0.0063  -0.0030 0.0026  122 GLY   A C   
909  O O   . GLY   A 116 ? 0.1300 0.1322 0.1406 0.0059  -0.0026 0.0004  122 GLY   A O   
910  N N   . ILE   A 117 ? 0.1243 0.1288 0.1394 0.0094  -0.0034 0.0037  123 ILE   A N   
911  C CA  . ILE   A 117 ? 0.1166 0.1165 0.1307 0.0113  -0.0035 0.0014  123 ILE   A CA  
912  C C   . ILE   A 117 ? 0.1113 0.1122 0.1271 0.0132  -0.0018 0.0023  123 ILE   A C   
913  O O   . ILE   A 117 ? 0.1253 0.1290 0.1462 0.0145  -0.0007 0.0054  123 ILE   A O   
914  C CB  . ILE   A 117 ? 0.1259 0.1215 0.1410 0.0118  -0.0041 -0.0003 123 ILE   A CB  
915  C CG1 . ILE   A 117 ? 0.1447 0.1402 0.1637 0.0128  -0.0032 0.0011  123 ILE   A CG1 
916  C CG2 . ILE   A 117 ? 0.1467 0.1413 0.1618 0.0106  -0.0052 -0.0010 123 ILE   A CG2 
917  C CD1 . ILE   A 117 ? 0.1627 0.1536 0.1821 0.0126  -0.0035 -0.0011 123 ILE   A CD1 
918  N N   . VAL   A 118 ? 0.1192 0.1179 0.1318 0.0131  -0.0012 0.0001  124 VAL   A N   
919  C CA  . VAL   A 118 ? 0.1231 0.1216 0.1377 0.0145  0.0020  -0.0003 124 VAL   A CA  
920  C C   . VAL   A 118 ? 0.1274 0.1219 0.1467 0.0161  0.0047  -0.0012 124 VAL   A C   
921  O O   . VAL   A 118 ? 0.1315 0.1217 0.1483 0.0148  0.0039  -0.0038 124 VAL   A O   
922  C CB  . VAL   A 118 ? 0.1361 0.1324 0.1445 0.0126  0.0025  -0.0036 124 VAL   A CB  
923  C CG1 . VAL   A 118 ? 0.1447 0.1395 0.1550 0.0133  0.0076  -0.0057 124 VAL   A CG1 
924  C CG2 . VAL   A 118 ? 0.1450 0.1444 0.1497 0.0111  0.0004  -0.0024 124 VAL   A CG2 
925  N N   . SER   A 119 ? 0.1284 0.1246 0.1557 0.0188  0.0081  0.0015  125 SER   A N   
926  C CA  . SER   A 119 ? 0.1445 0.1358 0.1786 0.0208  0.0121  0.0014  125 SER   A CA  
927  C C   . SER   A 119 ? 0.1646 0.1537 0.2055 0.0230  0.0189  0.0004  125 SER   A C   
928  O O   . SER   A 119 ? 0.1918 0.1732 0.2357 0.0233  0.0242  -0.0030 125 SER   A O   
929  C CB  . SER   A 119 ? 0.1491 0.1446 0.1902 0.0224  0.0101  0.0076  125 SER   A CB  
930  O OG  . SER   A 119 ? 0.1805 0.1719 0.2307 0.0248  0.0141  0.0093  125 SER   A OG  
931  N N   . THR   A 120 ? 0.1623 0.1575 0.2063 0.0243  0.0197  0.0032  126 THR   A N   
932  C CA  . THR   A 120 ? 0.1746 0.1681 0.2279 0.0269  0.0274  0.0026  126 THR   A CA  
933  C C   . THR   A 120 ? 0.1974 0.1935 0.2445 0.0250  0.0281  -0.0003 126 THR   A C   
934  O O   . THR   A 120 ? 0.1791 0.1801 0.2180 0.0226  0.0222  0.0006  126 THR   A O   
935  C CB  . THR   A 120 ? 0.1824 0.1827 0.2526 0.0318  0.0288  0.0122  126 THR   A CB  
936  O OG1 . THR   A 120 ? 0.1966 0.2088 0.2673 0.0313  0.0239  0.0184  126 THR   A OG1 
937  C CG2 . THR   A 120 ? 0.1897 0.1888 0.2657 0.0331  0.0272  0.0166  126 THR   A CG2 
938  N N   . GLY   A 121 ? 0.2217 0.2143 0.2736 0.0258  0.0361  -0.0038 127 GLY   A N   
939  C CA  . GLY   A 121 ? 0.2654 0.2608 0.3120 0.0237  0.0376  -0.0065 127 GLY   A CA  
940  C C   . GLY   A 121 ? 0.3177 0.3113 0.3758 0.0262  0.0479  -0.0082 127 GLY   A C   
941  O O   . GLY   A 121 ? 0.3442 0.3326 0.4143 0.0295  0.0547  -0.0078 127 GLY   A O   
942  N N   . GLY   A 122 ? 0.3362 0.3328 0.3898 0.0240  0.0497  -0.0106 128 GLY   A N   
943  C CA  . GLY   A 122 ? 0.3499 0.3451 0.4126 0.0253  0.0604  -0.0136 128 GLY   A CA  
944  C C   . GLY   A 122 ? 0.3765 0.3834 0.4501 0.0288  0.0597  -0.0060 128 GLY   A C   
945  O O   . GLY   A 122 ? 0.3684 0.3846 0.4458 0.0308  0.0519  0.0027  128 GLY   A O   
946  N N   . ASN   A 123 ? 0.3815 0.3886 0.4608 0.0290  0.0684  -0.0091 129 ASN   A N   
947  C CA  . ASN   A 123 ? 0.3769 0.3962 0.4690 0.0323  0.0689  -0.0015 129 ASN   A CA  
948  C C   . ASN   A 123 ? 0.3452 0.3743 0.4255 0.0290  0.0578  0.0025  129 ASN   A C   
949  O O   . ASN   A 123 ? 0.3398 0.3811 0.4301 0.0311  0.0552  0.0109  129 ASN   A O   
950  C CB  . ASN   A 123 ? 0.3816 0.4072 0.4983 0.0399  0.0711  0.0093  129 ASN   A CB  
951  C CG  . ASN   A 123 ? 0.4302 0.4454 0.5620 0.0439  0.0838  0.0060  129 ASN   A CG  
952  O OD1 . ASN   A 123 ? 0.4596 0.4641 0.5855 0.0408  0.0934  -0.0052 129 ASN   A OD1 
953  N ND2 . ASN   A 123 ? 0.4123 0.4306 0.5642 0.0502  0.0848  0.0157  129 ASN   A ND2 
954  N N   . GLY   A 124 ? 0.3088 0.3330 0.3691 0.0233  0.0521  -0.0032 130 GLY   A N   
955  C CA  . GLY   A 124 ? 0.2594 0.2903 0.3092 0.0199  0.0432  -0.0002 130 GLY   A CA  
956  C C   . GLY   A 124 ? 0.1941 0.2304 0.2453 0.0210  0.0346  0.0070  130 GLY   A C   
957  O O   . GLY   A 124 ? 0.1967 0.2395 0.2425 0.0183  0.0287  0.0101  130 GLY   A O   
958  N N   . LEU   A 125 ? 0.1839 0.2168 0.2415 0.0241  0.0348  0.0087  131 LEU   A N   
959  C CA  . LEU   A 125 ? 0.1692 0.2064 0.2274 0.0243  0.0276  0.0146  131 LEU   A CA  
960  C C   . LEU   A 125 ? 0.1842 0.2113 0.2319 0.0227  0.0250  0.0095  131 LEU   A C   
961  O O   . LEU   A 125 ? 0.2327 0.2503 0.2773 0.0225  0.0294  0.0030  131 LEU   A O   
962  C CB  . LEU   A 125 ? 0.1687 0.2118 0.2453 0.0292  0.0298  0.0228  131 LEU   A CB  
963  C CG  . LEU   A 125 ? 0.1695 0.2255 0.2604 0.0312  0.0320  0.0305  131 LEU   A CG  
964  C CD1 . LEU   A 125 ? 0.1940 0.2531 0.3070 0.0374  0.0373  0.0381  131 LEU   A CD1 
965  C CD2 . LEU   A 125 ? 0.1617 0.2305 0.2477 0.0268  0.0238  0.0367  131 LEU   A CD2 
966  N N   . VAL   A 126 ? 0.1406 0.1701 0.1828 0.0207  0.0182  0.0120  132 VAL   A N   
967  C CA  . VAL   A 126 ? 0.1442 0.1659 0.1793 0.0197  0.0156  0.0086  132 VAL   A CA  
968  C C   . VAL   A 126 ? 0.1377 0.1647 0.1792 0.0207  0.0123  0.0149  132 VAL   A C   
969  O O   . VAL   A 126 ? 0.1464 0.1828 0.1892 0.0188  0.0091  0.0202  132 VAL   A O   
970  C CB  . VAL   A 126 ? 0.1519 0.1704 0.1734 0.0155  0.0115  0.0047  132 VAL   A CB  
971  C CG1 . VAL   A 126 ? 0.1612 0.1868 0.1799 0.0127  0.0079  0.0079  132 VAL   A CG1 
972  C CG2 . VAL   A 126 ? 0.1542 0.1663 0.1709 0.0147  0.0088  0.0023  132 VAL   A CG2 
973  N N   . GLY   A 127 ? 0.1356 0.1571 0.1798 0.0224  0.0129  0.0143  133 GLY   A N   
974  C CA  . GLY   A 127 ? 0.1331 0.1592 0.1819 0.0225  0.0097  0.0202  133 GLY   A CA  
975  C C   . GLY   A 127 ? 0.1417 0.1619 0.1814 0.0201  0.0064  0.0163  133 GLY   A C   
976  O O   . GLY   A 127 ? 0.1564 0.1679 0.1909 0.0201  0.0077  0.0102  133 GLY   A O   
977  N N   . PHE   A 128 ? 0.1254 0.1514 0.1631 0.0173  0.0025  0.0197  134 PHE   A N   
978  C CA  . PHE   A 128 ? 0.1292 0.1506 0.1595 0.0147  0.0001  0.0162  134 PHE   A CA  
979  C C   . PHE   A 128 ? 0.1313 0.1558 0.1663 0.0144  -0.0012 0.0207  134 PHE   A C   
980  O O   . PHE   A 128 ? 0.1303 0.1645 0.1700 0.0128  -0.0027 0.0276  134 PHE   A O   
981  C CB  . PHE   A 128 ? 0.1267 0.1513 0.1491 0.0100  -0.0021 0.0148  134 PHE   A CB  
982  C CG  . PHE   A 128 ? 0.1260 0.1492 0.1442 0.0096  -0.0013 0.0119  134 PHE   A CG  
983  C CD1 . PHE   A 128 ? 0.1249 0.1402 0.1381 0.0101  -0.0009 0.0070  134 PHE   A CD1 
984  C CD2 . PHE   A 128 ? 0.1374 0.1684 0.1571 0.0083  -0.0012 0.0152  134 PHE   A CD2 
985  C CE1 . PHE   A 128 ? 0.1284 0.1431 0.1375 0.0092  -0.0004 0.0053  134 PHE   A CE1 
986  C CE2 . PHE   A 128 ? 0.1409 0.1707 0.1565 0.0075  -0.0003 0.0127  134 PHE   A CE2 
987  C CZ  . PHE   A 128 ? 0.1331 0.1544 0.1432 0.0080  0.0001  0.0077  134 PHE   A CZ  
988  N N   . ALA   A 129 ? 0.1270 0.1443 0.1604 0.0150  -0.0010 0.0174  135 ALA   A N   
989  C CA  . ALA   A 129 ? 0.1315 0.1508 0.1676 0.0138  -0.0024 0.0209  135 ALA   A CA  
990  C C   . ALA   A 129 ? 0.1254 0.1484 0.1540 0.0084  -0.0046 0.0197  135 ALA   A C   
991  O O   . ALA   A 129 ? 0.1376 0.1548 0.1604 0.0074  -0.0043 0.0138  135 ALA   A O   
992  C CB  . ALA   A 129 ? 0.1276 0.1379 0.1646 0.0160  -0.0009 0.0172  135 ALA   A CB  
993  N N   . ASP   A 130 ? 0.1235 0.1563 0.1526 0.0042  -0.0064 0.0253  136 ASP   A N   
994  C CA  . ASP   A 130 ? 0.1343 0.1702 0.1551 -0.0027 -0.0070 0.0229  136 ASP   A CA  
995  C C   . ASP   A 130 ? 0.1398 0.1707 0.1590 -0.0037 -0.0064 0.0200  136 ASP   A C   
996  O O   . ASP   A 130 ? 0.1469 0.1769 0.1714 -0.0012 -0.0069 0.0232  136 ASP   A O   
997  C CB  . ASP   A 130 ? 0.1566 0.2061 0.1778 -0.0086 -0.0094 0.0307  136 ASP   A CB  
998  C CG  . ASP   A 130 ? 0.2112 0.2649 0.2224 -0.0180 -0.0091 0.0277  136 ASP   A CG  
999  O OD1 . ASP   A 130 ? 0.2068 0.2559 0.2116 -0.0202 -0.0067 0.0210  136 ASP   A OD1 
1000 O OD2 . ASP   A 130 ? 0.2635 0.3241 0.2731 -0.0236 -0.0104 0.0317  136 ASP   A OD2 
1001 N N   . VAL   A 131 ? 0.1314 0.1591 0.1441 -0.0077 -0.0046 0.0139  137 VAL   A N   
1002 C CA  . VAL   A 131 ? 0.1369 0.1613 0.1486 -0.0097 -0.0032 0.0110  137 VAL   A CA  
1003 C C   . VAL   A 131 ? 0.1379 0.1670 0.1425 -0.0187 -0.0011 0.0089  137 VAL   A C   
1004 O O   . VAL   A 131 ? 0.1361 0.1628 0.1394 -0.0213 0.0011  0.0057  137 VAL   A O   
1005 C CB  . VAL   A 131 ? 0.1375 0.1521 0.1508 -0.0055 -0.0015 0.0052  137 VAL   A CB  
1006 C CG1 . VAL   A 131 ? 0.1479 0.1580 0.1661 0.0011  -0.0031 0.0064  137 VAL   A CG1 
1007 C CG2 . VAL   A 131 ? 0.1470 0.1578 0.1576 -0.0066 0.0010  0.0004  137 VAL   A CG2 
1008 N N   . ARG   A 132 ? 0.1377 0.1736 0.1373 -0.0243 -0.0013 0.0101  138 ARG   A N   
1009 C CA  . ARG   A 132 ? 0.1428 0.1821 0.1337 -0.0347 0.0020  0.0062  138 ARG   A CA  
1010 C C   . ARG   A 132 ? 0.1621 0.2097 0.1499 -0.0418 0.0010  0.0098  138 ARG   A C   
1011 O O   . ARG   A 132 ? 0.1793 0.2275 0.1594 -0.0509 0.0052  0.0045  138 ARG   A O   
1012 C CB  . ARG   A 132 ? 0.1445 0.1901 0.1300 -0.0403 0.0019  0.0067  138 ARG   A CB  
1013 C CG  . ARG   A 132 ? 0.1477 0.1841 0.1348 -0.0350 0.0041  0.0019  138 ARG   A CG  
1014 C CD  . ARG   A 132 ? 0.1615 0.2049 0.1432 -0.0410 0.0037  0.0029  138 ARG   A CD  
1015 N NE  . ARG   A 132 ? 0.1609 0.2145 0.1474 -0.0379 -0.0020 0.0122  138 ARG   A NE  
1016 C CZ  . ARG   A 132 ? 0.1782 0.2399 0.1633 -0.0409 -0.0038 0.0156  138 ARG   A CZ  
1017 N NH1 . ARG   A 132 ? 0.1915 0.2531 0.1682 -0.0488 -0.0007 0.0105  138 ARG   A NH1 
1018 N NH2 . ARG   A 132 ? 0.1965 0.2665 0.1894 -0.0363 -0.0080 0.0243  138 ARG   A NH2 
1019 N N   . ASP   A 133 ? 0.1509 0.2050 0.1445 -0.0387 -0.0039 0.0189  139 ASP   A N   
1020 C CA  . ASP   A 133 ? 0.1667 0.2293 0.1579 -0.0456 -0.0055 0.0239  139 ASP   A CA  
1021 C C   . ASP   A 133 ? 0.1670 0.2214 0.1604 -0.0428 -0.0032 0.0200  139 ASP   A C   
1022 O O   . ASP   A 133 ? 0.1910 0.2513 0.1813 -0.0493 -0.0037 0.0228  139 ASP   A O   
1023 C CB  . ASP   A 133 ? 0.1886 0.2618 0.1877 -0.0431 -0.0115 0.0370  139 ASP   A CB  
1024 C CG  . ASP   A 133 ? 0.2247 0.2895 0.2358 -0.0307 -0.0122 0.0393  139 ASP   A CG  
1025 O OD1 . ASP   A 133 ? 0.2093 0.2639 0.2223 -0.0238 -0.0102 0.0331  139 ASP   A OD1 
1026 O OD2 . ASP   A 133 ? 0.2571 0.3256 0.2756 -0.0286 -0.0147 0.0476  139 ASP   A OD2 
1027 N N   . LEU   A 134 ? 0.1533 0.1956 0.1521 -0.0340 -0.0012 0.0143  140 LEU   A N   
1028 C CA  . LEU   A 134 ? 0.1513 0.1869 0.1535 -0.0311 0.0005  0.0114  140 LEU   A CA  
1029 C C   . LEU   A 134 ? 0.1597 0.1914 0.1569 -0.0367 0.0065  0.0027  140 LEU   A C   
1030 O O   . LEU   A 134 ? 0.1660 0.1891 0.1667 -0.0324 0.0099  -0.0034 140 LEU   A O   
1031 C CB  . LEU   A 134 ? 0.1492 0.1758 0.1593 -0.0205 -0.0005 0.0104  140 LEU   A CB  
1032 C CG  . LEU   A 134 ? 0.1645 0.1928 0.1805 -0.0148 -0.0044 0.0175  140 LEU   A CG  
1033 C CD1 . LEU   A 134 ? 0.1766 0.1954 0.1974 -0.0068 -0.0041 0.0143  140 LEU   A CD1 
1034 C CD2 . LEU   A 134 ? 0.1953 0.2285 0.2152 -0.0158 -0.0066 0.0252  140 LEU   A CD2 
1035 N N   . LEU   A 135 ? 0.1616 0.2006 0.1510 -0.0474 0.0083  0.0025  141 LEU   A N   
1036 C CA  . LEU   A 135 ? 0.1787 0.2139 0.1629 -0.0544 0.0161  -0.0070 141 LEU   A CA  
1037 C C   . LEU   A 135 ? 0.1857 0.2129 0.1764 -0.0502 0.0202  -0.0120 141 LEU   A C   
1038 O O   . LEU   A 135 ? 0.2037 0.2240 0.1962 -0.0511 0.0275  -0.0200 141 LEU   A O   
1039 C CB  . LEU   A 135 ? 0.1952 0.2408 0.1674 -0.0692 0.0179  -0.0068 141 LEU   A CB  
1040 C CG  . LEU   A 135 ? 0.2105 0.2678 0.1767 -0.0748 0.0126  0.0003  141 LEU   A CG  
1041 C CD1 . LEU   A 135 ? 0.2419 0.3100 0.1944 -0.0917 0.0149  -0.0006 141 LEU   A CD1 
1042 C CD2 . LEU   A 135 ? 0.2288 0.2819 0.1951 -0.0720 0.0138  -0.0031 141 LEU   A CD2 
1043 N N   . TRP   A 136 ? 0.1637 0.1915 0.1595 -0.0453 0.0159  -0.0068 142 TRP   A N   
1044 C CA  . TRP   A 136 ? 0.1671 0.1891 0.1695 -0.0417 0.0188  -0.0103 142 TRP   A CA  
1045 C C   . TRP   A 136 ? 0.1753 0.1887 0.1869 -0.0327 0.0200  -0.0135 142 TRP   A C   
1046 O O   . TRP   A 136 ? 0.1976 0.2070 0.2159 -0.0305 0.0236  -0.0170 142 TRP   A O   
1047 C CB  . TRP   A 136 ? 0.1761 0.2010 0.1813 -0.0396 0.0137  -0.0035 142 TRP   A CB  
1048 C CG  . TRP   A 136 ? 0.1594 0.1840 0.1689 -0.0321 0.0073  0.0033  142 TRP   A CG  
1049 C CD1 . TRP   A 136 ? 0.1741 0.2055 0.1819 -0.0334 0.0028  0.0113  142 TRP   A CD1 
1050 C CD2 . TRP   A 136 ? 0.1631 0.1805 0.1800 -0.0229 0.0054  0.0030  142 TRP   A CD2 
1051 N NE1 . TRP   A 136 ? 0.1840 0.2114 0.1986 -0.0249 -0.0006 0.0149  142 TRP   A NE1 
1052 C CE2 . TRP   A 136 ? 0.1708 0.1895 0.1896 -0.0191 0.0010  0.0093  142 TRP   A CE2 
1053 C CE3 . TRP   A 136 ? 0.1736 0.1846 0.1962 -0.0182 0.0072  -0.0016 142 TRP   A CE3 
1054 C CZ2 . TRP   A 136 ? 0.1905 0.2030 0.2148 -0.0116 -0.0007 0.0096  142 TRP   A CZ2 
1055 C CZ3 . TRP   A 136 ? 0.2019 0.2085 0.2293 -0.0114 0.0041  -0.0003 142 TRP   A CZ3 
1056 C CH2 . TRP   A 136 ? 0.1951 0.2019 0.2224 -0.0086 0.0006  0.0045  142 TRP   A CH2 
1057 N N   . LEU   A 137 ? 0.1625 0.1740 0.1750 -0.0277 0.0170  -0.0119 143 LEU   A N   
1058 C CA  . LEU   A 137 ? 0.1834 0.1881 0.2041 -0.0204 0.0179  -0.0141 143 LEU   A CA  
1059 C C   . LEU   A 137 ? 0.2027 0.2032 0.2269 -0.0229 0.0260  -0.0206 143 LEU   A C   
1060 O O   . LEU   A 137 ? 0.2229 0.2189 0.2571 -0.0173 0.0275  -0.0213 143 LEU   A O   
1061 C CB  . LEU   A 137 ? 0.1814 0.1855 0.2008 -0.0165 0.0141  -0.0116 143 LEU   A CB  
1062 C CG  . LEU   A 137 ? 0.1707 0.1765 0.1906 -0.0119 0.0077  -0.0059 143 LEU   A CG  
1063 C CD1 . LEU   A 137 ? 0.1851 0.1912 0.2030 -0.0097 0.0054  -0.0041 143 LEU   A CD1 
1064 C CD2 . LEU   A 137 ? 0.1725 0.1742 0.1994 -0.0063 0.0058  -0.0055 143 LEU   A CD2 
1065 N N   . ASP   A 138 ? 0.2387 0.2407 0.2554 -0.0318 0.0318  -0.0251 144 ASP   A N   
1066 C CA  . ASP   A 138 ? 0.2797 0.2760 0.2997 -0.0353 0.0420  -0.0327 144 ASP   A CA  
1067 C C   . ASP   A 138 ? 0.3396 0.3345 0.3654 -0.0374 0.0485  -0.0368 144 ASP   A C   
1068 O O   . ASP   A 138 ? 0.3578 0.3473 0.3878 -0.0406 0.0586  -0.0436 144 ASP   A O   
1069 C CB  . ASP   A 138 ? 0.2906 0.2888 0.2983 -0.0461 0.0467  -0.0373 144 ASP   A CB  
1070 C CG  . ASP   A 138 ? 0.3383 0.3382 0.3404 -0.0457 0.0421  -0.0345 144 ASP   A CG  
1071 O OD1 . ASP   A 138 ? 0.3590 0.3565 0.3678 -0.0365 0.0370  -0.0303 144 ASP   A OD1 
1072 O OD2 . ASP   A 138 ? 0.4345 0.4392 0.4252 -0.0556 0.0436  -0.0363 144 ASP   A OD2 
1073 N N   . GLU   A 139 ? 0.3590 0.3581 0.3854 -0.0362 0.0440  -0.0331 145 GLU   A N   
1074 C CA  . GLU   A 139 ? 0.4068 0.4054 0.4386 -0.0388 0.0503  -0.0369 145 GLU   A CA  
1075 C C   . GLU   A 139 ? 0.4369 0.4378 0.4757 -0.0327 0.0442  -0.0316 145 GLU   A C   
1076 O O   . GLU   A 139 ? 0.4439 0.4463 0.4818 -0.0275 0.0355  -0.0256 145 GLU   A O   
1077 C CB  . GLU   A 139 ? 0.4629 0.4665 0.4813 -0.0512 0.0541  -0.0404 145 GLU   A CB  
1078 C CG  . GLU   A 139 ? 0.5635 0.5752 0.5724 -0.0532 0.0443  -0.0327 145 GLU   A CG  
1079 C CD  . GLU   A 139 ? 0.6814 0.7003 0.6752 -0.0654 0.0446  -0.0328 145 GLU   A CD  
1080 O OE1 . GLU   A 139 ? 0.6936 0.7205 0.6818 -0.0678 0.0373  -0.0253 145 GLU   A OE1 
1081 O OE2 . GLU   A 139 ? 0.7334 0.7505 0.7216 -0.0729 0.0522  -0.0399 145 GLU   A OE2 
1082 N N   . GLU   A 140 ? 0.4635 0.4645 0.5085 -0.0343 0.0495  -0.0344 146 GLU   A N   
1083 C CA  . GLU   A 140 ? 0.4940 0.4979 0.5444 -0.0311 0.0450  -0.0304 146 GLU   A CA  
1084 C C   . GLU   A 140 ? 0.5151 0.5185 0.5720 -0.0221 0.0365  -0.0243 146 GLU   A C   
1085 O O   . GLU   A 140 ? 0.5188 0.5242 0.5790 -0.0198 0.0321  -0.0209 146 GLU   A O   
1086 C CB  . GLU   A 140 ? 0.5362 0.5455 0.5743 -0.0383 0.0419  -0.0284 146 GLU   A CB  
1087 C CG  . GLU   A 140 ? 0.6219 0.6337 0.6611 -0.0352 0.0343  -0.0223 146 GLU   A CG  
1088 C CD  . GLU   A 140 ? 0.7333 0.7460 0.7805 -0.0352 0.0371  -0.0234 146 GLU   A CD  
1089 O OE1 . GLU   A 140 ? 0.7563 0.7701 0.8050 -0.0326 0.0312  -0.0188 146 GLU   A OE1 
1090 O OE2 . GLU   A 140 ? 0.7579 0.7700 0.8104 -0.0380 0.0457  -0.0291 146 GLU   A OE2 
1091 N N   . SER   B 1   ? 0.2118 0.2219 0.2286 0.0052  -0.0172 0.0346  7   SER   C N   
1092 C CA  . SER   B 1   ? 0.1976 0.2107 0.2231 0.0034  -0.0178 0.0349  7   SER   C CA  
1093 C C   . SER   B 1   ? 0.2062 0.2176 0.2315 0.0018  -0.0178 0.0319  7   SER   C C   
1094 O O   . SER   B 1   ? 0.2303 0.2384 0.2485 0.0018  -0.0184 0.0297  7   SER   C O   
1095 C CB  . SER   B 1   ? 0.2447 0.2596 0.2717 0.0027  -0.0223 0.0371  7   SER   C CB  
1096 O OG  . SER   B 1   ? 0.2958 0.3078 0.3155 0.0018  -0.0263 0.0352  7   SER   C OG  
1097 N N   . GLY   B 2   ? 0.1942 0.2077 0.2270 0.0008  -0.0167 0.0321  8   GLY   C N   
1098 C CA  . GLY   B 2   ? 0.1805 0.1924 0.2132 -0.0003 -0.0162 0.0300  8   GLY   C CA  
1099 C C   . GLY   B 2   ? 0.1641 0.1774 0.2032 -0.0001 -0.0128 0.0300  8   GLY   C C   
1100 O O   . GLY   B 2   ? 0.1763 0.1909 0.2184 0.0011  -0.0104 0.0303  8   GLY   C O   
1101 N N   . ALA   B 3   ? 0.1546 0.1670 0.1955 -0.0010 -0.0122 0.0295  9   ALA   C N   
1102 C CA  . ALA   B 3   ? 0.1519 0.1649 0.1973 -0.0003 -0.0085 0.0295  9   ALA   C CA  
1103 C C   . ALA   B 3   ? 0.1411 0.1510 0.1828 -0.0002 -0.0070 0.0280  9   ALA   C C   
1104 O O   . ALA   B 3   ? 0.1583 0.1660 0.1961 -0.0012 -0.0090 0.0274  9   ALA   C O   
1105 C CB  . ALA   B 3   ? 0.1864 0.2025 0.2411 -0.0011 -0.0083 0.0324  9   ALA   C CB  
1106 N N   . ILE   B 4   ? 0.1416 0.1508 0.1840 0.0013  -0.0035 0.0274  10  ILE   C N   
1107 C CA  . ILE   B 4   ? 0.1463 0.1524 0.1854 0.0020  -0.0013 0.0268  10  ILE   C CA  
1108 C C   . ILE   B 4   ? 0.1378 0.1451 0.1845 0.0017  0.0015  0.0294  10  ILE   C C   
1109 O O   . ILE   B 4   ? 0.1520 0.1614 0.2038 0.0024  0.0032  0.0303  10  ILE   C O   
1110 C CB  . ILE   B 4   ? 0.1435 0.1477 0.1769 0.0046  0.0008  0.0242  10  ILE   C CB  
1111 C CG1 . ILE   B 4   ? 0.1586 0.1627 0.1873 0.0051  -0.0015 0.0218  10  ILE   C CG1 
1112 C CG2 . ILE   B 4   ? 0.1757 0.1763 0.2041 0.0059  0.0030  0.0241  10  ILE   C CG2 
1113 C CD1 . ILE   B 4   ? 0.1643 0.1675 0.1898 0.0074  -0.0003 0.0190  10  ILE   C CD1 
1114 N N   . TYR   B 5   ? 0.1445 0.1502 0.1926 0.0008  0.0023  0.0308  11  TYR   C N   
1115 C CA  . TYR   B 5   ? 0.1493 0.1561 0.2060 0.0005  0.0055  0.0338  11  TYR   C CA  
1116 C C   . TYR   B 5   ? 0.1693 0.1719 0.2212 0.0027  0.0102  0.0339  11  TYR   C C   
1117 O O   . TYR   B 5   ? 0.1863 0.1862 0.2355 0.0021  0.0100  0.0340  11  TYR   C O   
1118 C CB  . TYR   B 5   ? 0.1531 0.1619 0.2182 -0.0026 0.0025  0.0360  11  TYR   C CB  
1119 C CG  . TYR   B 5   ? 0.1659 0.1788 0.2351 -0.0041 -0.0020 0.0363  11  TYR   C CG  
1120 C CD1 . TYR   B 5   ? 0.1601 0.1769 0.2380 -0.0038 -0.0010 0.0387  11  TYR   C CD1 
1121 C CD2 . TYR   B 5   ? 0.1761 0.1885 0.2395 -0.0051 -0.0069 0.0345  11  TYR   C CD2 
1122 C CE1 . TYR   B 5   ? 0.1773 0.1975 0.2582 -0.0046 -0.0050 0.0394  11  TYR   C CE1 
1123 C CE2 . TYR   B 5   ? 0.1973 0.2128 0.2628 -0.0057 -0.0107 0.0352  11  TYR   C CE2 
1124 C CZ  . TYR   B 5   ? 0.1864 0.2060 0.2607 -0.0055 -0.0099 0.0378  11  TYR   C CZ  
1125 O OH  . TYR   B 5   ? 0.2084 0.2308 0.2839 -0.0057 -0.0136 0.0388  11  TYR   C OH  
1126 N N   . VAL   B 6   ? 0.1788 0.1803 0.2283 0.0055  0.0143  0.0336  12  VAL   C N   
1127 C CA  . VAL   B 6   ? 0.1899 0.1870 0.2330 0.0085  0.0190  0.0338  12  VAL   C CA  
1128 C C   . VAL   B 6   ? 0.1871 0.1843 0.2360 0.0101  0.0247  0.0364  12  VAL   C C   
1129 O O   . VAL   B 6   ? 0.1737 0.1729 0.2258 0.0107  0.0253  0.0360  12  VAL   C O   
1130 C CB  . VAL   B 6   ? 0.2051 0.1997 0.2365 0.0113  0.0182  0.0299  12  VAL   C CB  
1131 C CG1 . VAL   B 6   ? 0.2011 0.1977 0.2332 0.0121  0.0174  0.0276  12  VAL   C CG1 
1132 C CG2 . VAL   B 6   ? 0.2314 0.2213 0.2548 0.0149  0.0227  0.0302  12  VAL   C CG2 
1133 N N   . GLY   B 7   ? 0.1981 0.1931 0.2497 0.0107  0.0292  0.0396  13  GLY   C N   
1134 C CA  . GLY   B 7   ? 0.1916 0.1865 0.2493 0.0125  0.0354  0.0426  13  GLY   C CA  
1135 C C   . GLY   B 7   ? 0.1891 0.1895 0.2604 0.0099  0.0339  0.0445  13  GLY   C C   
1136 O O   . GLY   B 7   ? 0.2036 0.2076 0.2823 0.0063  0.0290  0.0451  13  GLY   C O   
1137 N N   . ASN   B 8   ? 0.1913 0.1923 0.2645 0.0120  0.0372  0.0446  14  ASN   C N   
1138 C CA  . ASN   B 8   ? 0.1888 0.1951 0.2745 0.0101  0.0357  0.0464  14  ASN   C CA  
1139 C C   . ASN   B 8   ? 0.1759 0.1837 0.2578 0.0101  0.0316  0.0430  14  ASN   C C   
1140 O O   . ASN   B 8   ? 0.1749 0.1851 0.2634 0.0105  0.0326  0.0438  14  ASN   C O   
1141 C CB  . ASN   B 8   ? 0.2264 0.2331 0.3212 0.0120  0.0426  0.0500  14  ASN   C CB  
1142 C CG  . ASN   B 8   ? 0.3008 0.3082 0.4054 0.0108  0.0457  0.0545  14  ASN   C CG  
1143 O OD1 . ASN   B 8   ? 0.3261 0.3385 0.4447 0.0076  0.0430  0.0572  14  ASN   C OD1 
1144 N ND2 . ASN   B 8   ? 0.3301 0.3323 0.4275 0.0132  0.0508  0.0551  14  ASN   C ND2 
1145 N N   . TYR   B 9   ? 0.1548 0.1614 0.2274 0.0094  0.0270  0.0396  15  TYR   C N   
1146 C CA  . TYR   B 9   ? 0.1461 0.1539 0.2155 0.0093  0.0233  0.0365  15  TYR   C CA  
1147 C C   . TYR   B 9   ? 0.1403 0.1508 0.2102 0.0063  0.0170  0.0362  15  TYR   C C   
1148 O O   . TYR   B 9   ? 0.1589 0.1683 0.2256 0.0050  0.0151  0.0361  15  TYR   C O   
1149 C CB  . TYR   B 9   ? 0.1646 0.1680 0.2214 0.0120  0.0240  0.0322  15  TYR   C CB  
1150 C CG  . TYR   B 9   ? 0.1807 0.1804 0.2340 0.0156  0.0298  0.0317  15  TYR   C CG  
1151 C CD1 . TYR   B 9   ? 0.2070 0.2074 0.2661 0.0167  0.0327  0.0320  15  TYR   C CD1 
1152 C CD2 . TYR   B 9   ? 0.2180 0.2129 0.2613 0.0184  0.0326  0.0308  15  TYR   C CD2 
1153 C CE1 . TYR   B 9   ? 0.2482 0.2444 0.3028 0.0204  0.0383  0.0312  15  TYR   C CE1 
1154 C CE2 . TYR   B 9   ? 0.2652 0.2559 0.3030 0.0223  0.0379  0.0300  15  TYR   C CE2 
1155 C CZ  . TYR   B 9   ? 0.2972 0.2885 0.3406 0.0233  0.0407  0.0300  15  TYR   C CZ  
1156 O OH  . TYR   B 9   ? 0.3705 0.3569 0.4079 0.0275  0.0463  0.0289  15  TYR   C OH  
1157 N N   . ARG   B 10  ? 0.1297 0.1431 0.2026 0.0055  0.0142  0.0358  16  ARG   C N   
1158 C CA  . ARG   B 10  ? 0.1261 0.1413 0.1974 0.0035  0.0087  0.0352  16  ARG   C CA  
1159 C C   . ARG   B 10  ? 0.1279 0.1421 0.1938 0.0048  0.0082  0.0321  16  ARG   C C   
1160 O O   . ARG   B 10  ? 0.1354 0.1504 0.2053 0.0059  0.0102  0.0320  16  ARG   C O   
1161 C CB  . ARG   B 10  ? 0.1339 0.1538 0.2152 0.0017  0.0061  0.0385  16  ARG   C CB  
1162 C CG  . ARG   B 10  ? 0.1531 0.1747 0.2321 0.0006  0.0011  0.0382  16  ARG   C CG  
1163 C CD  . ARG   B 10  ? 0.1538 0.1798 0.2417 -0.0008 -0.0019 0.0417  16  ARG   C CD  
1164 N NE  . ARG   B 10  ? 0.1643 0.1920 0.2517 -0.0002 -0.0042 0.0424  16  ARG   C NE  
1165 C CZ  . ARG   B 10  ? 0.1797 0.2076 0.2619 -0.0008 -0.0085 0.0422  16  ARG   C CZ  
1166 N NH1 . ARG   B 10  ? 0.1828 0.2086 0.2587 -0.0022 -0.0115 0.0405  16  ARG   C NH1 
1167 N NH2 . ARG   B 10  ? 0.1857 0.2149 0.2678 0.0002  -0.0094 0.0435  16  ARG   C NH2 
1168 N N   . VAL   B 11  ? 0.1239 0.1364 0.1819 0.0047  0.0058  0.0296  17  VAL   C N   
1169 C CA  . VAL   B 11  ? 0.1254 0.1372 0.1795 0.0057  0.0051  0.0266  17  VAL   C CA  
1170 C C   . VAL   B 11  ? 0.1269 0.1407 0.1815 0.0044  0.0017  0.0274  17  VAL   C C   
1171 O O   . VAL   B 11  ? 0.1356 0.1488 0.1862 0.0032  -0.0009 0.0276  17  VAL   C O   
1172 C CB  . VAL   B 11  ? 0.1444 0.1528 0.1895 0.0071  0.0051  0.0232  17  VAL   C CB  
1173 C CG1 . VAL   B 11  ? 0.1680 0.1762 0.2116 0.0081  0.0044  0.0201  17  VAL   C CG1 
1174 C CG2 . VAL   B 11  ? 0.1674 0.1730 0.2096 0.0089  0.0085  0.0230  17  VAL   C CG2 
1175 N N   . VAL   B 12  ? 0.1175 0.1330 0.1763 0.0047  0.0019  0.0279  18  VAL   C N   
1176 C CA  A VAL   B 12  ? 0.1217 0.1388 0.1806 0.0040  -0.0006 0.0293  18  VAL   C CA  
1177 C CA  B VAL   B 12  ? 0.1440 0.1611 0.2029 0.0039  -0.0006 0.0293  18  VAL   C CA  
1178 C C   . VAL   B 12  ? 0.1273 0.1442 0.1871 0.0050  0.0005  0.0277  18  VAL   C C   
1179 O O   . VAL   B 12  ? 0.1257 0.1416 0.1878 0.0060  0.0027  0.0255  18  VAL   C O   
1180 C CB  A VAL   B 12  ? 0.1119 0.1321 0.1774 0.0033  -0.0016 0.0333  18  VAL   C CB  
1181 C CB  B VAL   B 12  ? 0.1852 0.2055 0.2514 0.0033  -0.0013 0.0334  18  VAL   C CB  
1182 C CG1 A VAL   B 12  ? 0.1294 0.1502 0.1947 0.0018  -0.0041 0.0348  18  VAL   C CG1 
1183 C CG1 B VAL   B 12  ? 0.1918 0.2134 0.2568 0.0030  -0.0041 0.0354  18  VAL   C CG1 
1184 C CG2 A VAL   B 12  ? 0.0727 0.0943 0.1465 0.0042  0.0016  0.0345  18  VAL   C CG2 
1185 C CG2 B VAL   B 12  ? 0.2201 0.2410 0.2881 0.0021  -0.0022 0.0348  18  VAL   C CG2 
1186 N N   . ASN   B 13  ? 0.1164 0.1338 0.1746 0.0049  -0.0009 0.0287  19  ASN   C N   
1187 C CA  . ASN   B 13  ? 0.1179 0.1354 0.1793 0.0057  0.0007  0.0280  19  ASN   C CA  
1188 C C   . ASN   B 13  ? 0.1213 0.1405 0.1914 0.0061  0.0027  0.0304  19  ASN   C C   
1189 O O   . ASN   B 13  ? 0.1193 0.1404 0.1916 0.0058  0.0019  0.0340  19  ASN   C O   
1190 C CB  . ASN   B 13  ? 0.1299 0.1476 0.1886 0.0060  -0.0003 0.0299  19  ASN   C CB  
1191 C CG  . ASN   B 13  ? 0.1296 0.1455 0.1803 0.0059  -0.0019 0.0278  19  ASN   C CG  
1192 O OD1 . ASN   B 13  ? 0.1445 0.1596 0.1895 0.0053  -0.0041 0.0284  19  ASN   C OD1 
1193 N ND2 . ASN   B 13  ? 0.1372 0.1523 0.1882 0.0065  -0.0008 0.0252  19  ASN   C ND2 
1194 N N   . ARG   B 14  ? 0.1138 0.1322 0.1888 0.0068  0.0051  0.0283  20  ARG   C N   
1195 C CA  . ARG   B 14  ? 0.1166 0.1359 0.2000 0.0073  0.0075  0.0304  20  ARG   C CA  
1196 C C   . ARG   B 14  ? 0.1319 0.1532 0.2185 0.0075  0.0074  0.0351  20  ARG   C C   
1197 O O   . ARG   B 14  ? 0.1330 0.1560 0.2244 0.0079  0.0080  0.0386  20  ARG   C O   
1198 C CB  . ARG   B 14  ? 0.1180 0.1355 0.2059 0.0078  0.0096  0.0267  20  ARG   C CB  
1199 C CG  . ARG   B 14  ? 0.1231 0.1406 0.2197 0.0085  0.0127  0.0282  20  ARG   C CG  
1200 C CD  . ARG   B 14  ? 0.1273 0.1423 0.2281 0.0089  0.0143  0.0238  20  ARG   C CD  
1201 N NE  . ARG   B 14  ? 0.1282 0.1420 0.2368 0.0097  0.0175  0.0240  20  ARG   C NE  
1202 C CZ  . ARG   B 14  ? 0.1234 0.1380 0.2407 0.0100  0.0197  0.0273  20  ARG   C CZ  
1203 N NH1 . ARG   B 14  ? 0.1394 0.1560 0.2578 0.0097  0.0192  0.0313  20  ARG   C NH1 
1204 N NH2 . ARG   B 14  ? 0.1312 0.1439 0.2554 0.0108  0.0228  0.0268  20  ARG   C NH2 
1205 N N   . HIS   B 15  ? 0.1241 0.1451 0.2075 0.0077  0.0068  0.0356  21  HIS   C N   
1206 C CA  . HIS   B 15  ? 0.1268 0.1489 0.2118 0.0086  0.0073  0.0404  21  HIS   C CA  
1207 C C   . HIS   B 15  ? 0.1441 0.1678 0.2241 0.0086  0.0041  0.0438  21  HIS   C C   
1208 O O   . HIS   B 15  ? 0.1688 0.1936 0.2499 0.0098  0.0040  0.0481  21  HIS   C O   
1209 C CB  . HIS   B 15  ? 0.1439 0.1649 0.2276 0.0093  0.0086  0.0404  21  HIS   C CB  
1210 C CG  . HIS   B 15  ? 0.1345 0.1545 0.2084 0.0092  0.0063  0.0393  21  HIS   C CG  
1211 N ND1 . HIS   B 15  ? 0.1474 0.1663 0.2178 0.0083  0.0053  0.0347  21  HIS   C ND1 
1212 C CD2 . HIS   B 15  ? 0.1516 0.1713 0.2184 0.0100  0.0050  0.0422  21  HIS   C CD2 
1213 C CE1 . HIS   B 15  ? 0.1594 0.1773 0.2216 0.0086  0.0038  0.0352  21  HIS   C CE1 
1214 N NE2 . HIS   B 15  ? 0.1517 0.1699 0.2112 0.0096  0.0036  0.0393  21  HIS   C NE2 
1215 N N   . LEU   B 16  ? 0.1243 0.1479 0.1995 0.0074  0.0013  0.0420  22  LEU   C N   
1216 C CA  . LEU   B 16  ? 0.1404 0.1655 0.2122 0.0069  -0.0025 0.0443  22  LEU   C CA  
1217 C C   . LEU   B 16  ? 0.1470 0.1741 0.2251 0.0061  -0.0029 0.0452  22  LEU   C C   
1218 O O   . LEU   B 16  ? 0.1559 0.1846 0.2331 0.0053  -0.0064 0.0467  22  LEU   C O   
1219 C CB  . LEU   B 16  ? 0.1411 0.1643 0.2034 0.0061  -0.0053 0.0419  22  LEU   C CB  
1220 C CG  . LEU   B 16  ? 0.1501 0.1712 0.2059 0.0072  -0.0046 0.0416  22  LEU   C CG  
1221 C CD1 . LEU   B 16  ? 0.1647 0.1834 0.2114 0.0064  -0.0070 0.0389  22  LEU   C CD1 
1222 C CD2 . LEU   B 16  ? 0.1591 0.1808 0.2135 0.0089  -0.0050 0.0460  22  LEU   C CD2 
1223 N N   . ALA   B 17  ? 0.1482 0.1752 0.2329 0.0064  0.0007  0.0439  23  ALA   C N   
1224 C CA  . ALA   B 17  ? 0.1390 0.1676 0.2299 0.0060  0.0013  0.0449  23  ALA   C CA  
1225 C C   . ALA   B 17  ? 0.1461 0.1782 0.2435 0.0065  -0.0002 0.0499  23  ALA   C C   
1226 O O   . ALA   B 17  ? 0.1556 0.1884 0.2552 0.0078  0.0005  0.0526  23  ALA   C O   
1227 C CB  . ALA   B 17  ? 0.1524 0.1793 0.2478 0.0068  0.0058  0.0425  23  ALA   C CB  
1228 N N   . THR   B 18  ? 0.1441 0.1785 0.2452 0.0056  -0.0020 0.0513  24  THR   C N   
1229 C CA  . THR   B 18  ? 0.1448 0.1831 0.2530 0.0060  -0.0043 0.0560  24  THR   C CA  
1230 C C   . THR   B 18  ? 0.1398 0.1796 0.2592 0.0071  0.0001  0.0579  24  THR   C C   
1231 O O   . THR   B 18  ? 0.1484 0.1856 0.2688 0.0074  0.0046  0.0552  24  THR   C O   
1232 C CB  . THR   B 18  ? 0.1619 0.2023 0.2703 0.0042  -0.0091 0.0565  24  THR   C CB  
1233 O OG1 . THR   B 18  ? 0.1655 0.2055 0.2781 0.0033  -0.0062 0.0550  24  THR   C OG1 
1234 C CG2 . THR   B 18  ? 0.1830 0.2212 0.2799 0.0031  -0.0134 0.0541  24  THR   C CG2 
1235 N N   . HIS   B 19  ? 0.1512 0.1950 0.2788 0.0079  -0.0015 0.0627  25  HIS   C N   
1236 C CA  . HIS   B 19  ? 0.1597 0.2051 0.2988 0.0091  0.0027  0.0650  25  HIS   C CA  
1237 C C   . HIS   B 19  ? 0.1389 0.1841 0.2810 0.0079  0.0045  0.0633  25  HIS   C C   
1238 O O   . HIS   B 19  ? 0.1530 0.1962 0.2987 0.0090  0.0100  0.0620  25  HIS   C O   
1239 C CB  . HIS   B 19  ? 0.1714 0.2219 0.3192 0.0101  -0.0004 0.0708  25  HIS   C CB  
1240 C CG  . HIS   B 19  ? 0.1763 0.2292 0.3374 0.0111  0.0034  0.0735  25  HIS   C CG  
1241 N ND1 . HIS   B 19  ? 0.2138 0.2647 0.3800 0.0131  0.0094  0.0739  25  HIS   C ND1 
1242 C CD2 . HIS   B 19  ? 0.1930 0.2494 0.3628 0.0103  0.0027  0.0752  25  HIS   C CD2 
1243 C CE1 . HIS   B 19  ? 0.2043 0.2578 0.3818 0.0138  0.0119  0.0765  25  HIS   C CE1 
1244 N NE2 . HIS   B 19  ? 0.1958 0.2528 0.3763 0.0121  0.0083  0.0775  25  HIS   C NE2 
1245 N N   . ASN   B 20  ? 0.1468 0.1935 0.2871 0.0060  0.0003  0.0630  26  ASN   C N   
1246 C CA  . ASN   B 20  ? 0.1568 0.2030 0.3005 0.0051  0.0029  0.0619  26  ASN   C CA  
1247 C C   . ASN   B 20  ? 0.1444 0.1852 0.2800 0.0055  0.0075  0.0572  26  ASN   C C   
1248 O O   . ASN   B 20  ? 0.1357 0.1749 0.2744 0.0064  0.0125  0.0567  26  ASN   C O   
1249 C CB  . ASN   B 20  ? 0.1807 0.2290 0.3244 0.0026  -0.0025 0.0621  26  ASN   C CB  
1250 C CG  . ASN   B 20  ? 0.2698 0.3178 0.4195 0.0019  0.0010  0.0621  26  ASN   C CG  
1251 O OD1 . ASN   B 20  ? 0.2993 0.3505 0.4614 0.0025  0.0035  0.0655  26  ASN   C OD1 
1252 N ND2 . ASN   B 20  ? 0.2848 0.3289 0.4263 0.0009  0.0021  0.0587  26  ASN   C ND2 
1253 N N   . ASP   B 21  ? 0.1315 0.1693 0.2561 0.0053  0.0060  0.0539  27  ASP   C N   
1254 C CA  . ASP   B 21  ? 0.1325 0.1655 0.2497 0.0059  0.0095  0.0494  27  ASP   C CA  
1255 C C   . ASP   B 21  ? 0.1289 0.1600 0.2500 0.0080  0.0149  0.0486  27  ASP   C C   
1256 O O   . ASP   B 21  ? 0.1450 0.1731 0.2646 0.0091  0.0190  0.0464  27  ASP   C O   
1257 C CB  . ASP   B 21  ? 0.1306 0.1614 0.2376 0.0054  0.0069  0.0464  27  ASP   C CB  
1258 C CG  . ASP   B 21  ? 0.1460 0.1767 0.2463 0.0037  0.0026  0.0456  27  ASP   C CG  
1259 O OD1 . ASP   B 21  ? 0.1721 0.2023 0.2728 0.0028  0.0029  0.0453  27  ASP   C OD1 
1260 O OD2 . ASP   B 21  ? 0.1527 0.1834 0.2477 0.0033  -0.0008 0.0454  27  ASP   C OD2 
1261 N N   . TRP   B 22  ? 0.1282 0.1607 0.2542 0.0089  0.0150  0.0506  28  TRP   C N   
1262 C CA  . TRP   B 22  ? 0.1348 0.1651 0.2653 0.0107  0.0199  0.0498  28  TRP   C CA  
1263 C C   . TRP   B 22  ? 0.1284 0.1597 0.2679 0.0120  0.0240  0.0523  28  TRP   C C   
1264 O O   . TRP   B 22  ? 0.1368 0.1644 0.2765 0.0136  0.0290  0.0499  28  TRP   C O   
1265 C CB  . TRP   B 22  ? 0.1349 0.1663 0.2695 0.0114  0.0194  0.0520  28  TRP   C CB  
1266 C CG  . TRP   B 22  ? 0.1367 0.1655 0.2639 0.0110  0.0182  0.0487  28  TRP   C CG  
1267 C CD1 . TRP   B 22  ? 0.1438 0.1738 0.2658 0.0101  0.0143  0.0496  28  TRP   C CD1 
1268 C CD2 . TRP   B 22  ? 0.1179 0.1423 0.2426 0.0115  0.0210  0.0438  28  TRP   C CD2 
1269 N NE1 . TRP   B 22  ? 0.1429 0.1700 0.2607 0.0101  0.0150  0.0462  28  TRP   C NE1 
1270 C CE2 . TRP   B 22  ? 0.1335 0.1574 0.2536 0.0108  0.0187  0.0425  28  TRP   C CE2 
1271 C CE3 . TRP   B 22  ? 0.1533 0.1742 0.2801 0.0128  0.0252  0.0406  28  TRP   C CE3 
1272 C CZ2 . TRP   B 22  ? 0.1408 0.1614 0.2597 0.0110  0.0202  0.0382  28  TRP   C CZ2 
1273 C CZ3 . TRP   B 22  ? 0.1660 0.1831 0.2902 0.0130  0.0260  0.0357  28  TRP   C CZ3 
1274 C CH2 . TRP   B 22  ? 0.1620 0.1793 0.2831 0.0119  0.0234  0.0346  28  TRP   C CH2 
1275 N N   . ALA   B 23  ? 0.1229 0.1588 0.2692 0.0112  0.0219  0.0567  29  ALA   C N   
1276 C CA  . ALA   B 23  ? 0.1301 0.1678 0.2869 0.0123  0.0259  0.0597  29  ALA   C CA  
1277 C C   . ALA   B 23  ? 0.1551 0.1899 0.3082 0.0124  0.0293  0.0576  29  ALA   C C   
1278 O O   . ALA   B 23  ? 0.1699 0.2048 0.3302 0.0138  0.0341  0.0596  29  ALA   C O   
1279 C CB  . ALA   B 23  ? 0.1380 0.1821 0.3047 0.0113  0.0217  0.0651  29  ALA   C CB  
1280 N N   . ASN   B 24  ? 0.1571 0.1892 0.2989 0.0112  0.0270  0.0539  30  ASN   C N   
1281 C CA  . ASN   B 24  ? 0.1468 0.1757 0.2833 0.0116  0.0302  0.0520  30  ASN   C CA  
1282 C C   . ASN   B 24  ? 0.1520 0.1754 0.2751 0.0123  0.0305  0.0463  30  ASN   C C   
1283 O O   . ASN   B 24  ? 0.1497 0.1709 0.2646 0.0119  0.0297  0.0443  30  ASN   C O   
1284 C CB  . ASN   B 24  ? 0.1663 0.1981 0.3042 0.0091  0.0262  0.0540  30  ASN   C CB  
1285 C CG  . ASN   B 24  ? 0.1710 0.2084 0.3235 0.0084  0.0257  0.0592  30  ASN   C CG  
1286 O OD1 . ASN   B 24  ? 0.2007 0.2382 0.3607 0.0096  0.0310  0.0615  30  ASN   C OD1 
1287 N ND2 . ASN   B 24  ? 0.1750 0.2170 0.3322 0.0069  0.0198  0.0615  30  ASN   C ND2 
1288 N N   . LEU   B 25  ? 0.1588 0.1798 0.2802 0.0136  0.0317  0.0438  31  LEU   C N   
1289 C CA  . LEU   B 25  ? 0.1524 0.1690 0.2628 0.0141  0.0308  0.0382  31  LEU   C CA  
1290 C C   . LEU   B 25  ? 0.1739 0.1853 0.2761 0.0163  0.0347  0.0347  31  LEU   C C   
1291 O O   . LEU   B 25  ? 0.1849 0.1941 0.2898 0.0185  0.0400  0.0353  31  LEU   C O   
1292 C CB  . LEU   B 25  ? 0.1589 0.1746 0.2727 0.0148  0.0314  0.0368  31  LEU   C CB  
1293 C CG  . LEU   B 25  ? 0.1723 0.1843 0.2776 0.0150  0.0299  0.0311  31  LEU   C CG  
1294 C CD1 . LEU   B 25  ? 0.1741 0.1883 0.2746 0.0128  0.0245  0.0309  31  LEU   C CD1 
1295 C CD2 . LEU   B 25  ? 0.1875 0.1981 0.2982 0.0157  0.0313  0.0297  31  LEU   C CD2 
1296 N N   . VAL   B 26  ? 0.1609 0.1699 0.2524 0.0160  0.0322  0.0312  32  VAL   C N   
1297 C CA  . VAL   B 26  ? 0.1793 0.1827 0.2607 0.0186  0.0351  0.0274  32  VAL   C CA  
1298 C C   . VAL   B 26  ? 0.1830 0.1832 0.2581 0.0194  0.0331  0.0215  32  VAL   C C   
1299 O O   . VAL   B 26  ? 0.2088 0.2043 0.2798 0.0220  0.0360  0.0180  32  VAL   C O   
1300 C CB  . VAL   B 26  ? 0.1838 0.1867 0.2578 0.0181  0.0337  0.0278  32  VAL   C CB  
1301 C CG1 . VAL   B 26  ? 0.2110 0.2079 0.2724 0.0212  0.0358  0.0236  32  VAL   C CG1 
1302 C CG2 . VAL   B 26  ? 0.1811 0.1867 0.2625 0.0173  0.0359  0.0332  32  VAL   C CG2 
1303 N N   . TRP   B 27  ? 0.1641 0.1665 0.2386 0.0173  0.0281  0.0203  33  TRP   C N   
1304 C CA  . TRP   B 27  ? 0.1655 0.1654 0.2358 0.0177  0.0258  0.0149  33  TRP   C CA  
1305 C C   . TRP   B 27  ? 0.1639 0.1677 0.2386 0.0151  0.0217  0.0160  33  TRP   C C   
1306 O O   . TRP   B 27  ? 0.1645 0.1715 0.2396 0.0134  0.0196  0.0194  33  TRP   C O   
1307 C CB  . TRP   B 27  ? 0.1838 0.1801 0.2417 0.0193  0.0245  0.0109  33  TRP   C CB  
1308 C CG  . TRP   B 27  ? 0.1951 0.1899 0.2490 0.0193  0.0206  0.0055  33  TRP   C CG  
1309 C CD1 . TRP   B 27  ? 0.2259 0.2170 0.2781 0.0209  0.0206  0.0002  33  TRP   C CD1 
1310 C CD2 . TRP   B 27  ? 0.1795 0.1766 0.2314 0.0176  0.0161  0.0049  33  TRP   C CD2 
1311 N NE1 . TRP   B 27  ? 0.2324 0.2238 0.2824 0.0202  0.0159  -0.0038 33  TRP   C NE1 
1312 C CE2 . TRP   B 27  ? 0.1985 0.1936 0.2483 0.0183  0.0134  -0.0007 33  TRP   C CE2 
1313 C CE3 . TRP   B 27  ? 0.1764 0.1768 0.2283 0.0157  0.0140  0.0083  33  TRP   C CE3 
1314 C CZ2 . TRP   B 27  ? 0.1909 0.1877 0.2393 0.0172  0.0092  -0.0025 33  TRP   C CZ2 
1315 C CZ3 . TRP   B 27  ? 0.1950 0.1963 0.2439 0.0149  0.0101  0.0062  33  TRP   C CZ3 
1316 C CH2 . TRP   B 27  ? 0.1949 0.1948 0.2431 0.0156  0.0080  0.0013  33  TRP   C CH2 
1317 N N   . GLU   B 28  ? 0.1591 0.1621 0.2371 0.0149  0.0208  0.0131  34  GLU   C N   
1318 C CA  . GLU   B 28  ? 0.1750 0.1810 0.2568 0.0130  0.0178  0.0141  34  GLU   C CA  
1319 C C   . GLU   B 28  ? 0.1731 0.1769 0.2552 0.0131  0.0164  0.0090  34  GLU   C C   
1320 O O   . GLU   B 28  ? 0.1725 0.1729 0.2557 0.0145  0.0181  0.0053  34  GLU   C O   
1321 C CB  . GLU   B 28  ? 0.1755 0.1848 0.2668 0.0120  0.0189  0.0193  34  GLU   C CB  
1322 C CG  . GLU   B 28  ? 0.1801 0.1880 0.2795 0.0131  0.0226  0.0195  34  GLU   C CG  
1323 C CD  . GLU   B 28  ? 0.2051 0.2113 0.3098 0.0130  0.0228  0.0166  34  GLU   C CD  
1324 O OE1 . GLU   B 28  ? 0.2431 0.2463 0.3519 0.0142  0.0258  0.0144  34  GLU   C OE1 
1325 O OE2 . GLU   B 28  ? 0.1897 0.1974 0.2952 0.0118  0.0204  0.0163  34  GLU   C OE2 
1326 N N   . ASP   B 29  ? 0.1524 0.1581 0.2344 0.0118  0.0133  0.0087  35  ASP   C N   
1327 C CA  . ASP   B 29  ? 0.1556 0.1602 0.2404 0.0117  0.0117  0.0041  35  ASP   C CA  
1328 C C   . ASP   B 29  ? 0.1482 0.1559 0.2386 0.0101  0.0107  0.0069  35  ASP   C C   
1329 O O   . ASP   B 29  ? 0.1426 0.1520 0.2281 0.0095  0.0086  0.0082  35  ASP   C O   
1330 C CB  . ASP   B 29  ? 0.1694 0.1717 0.2448 0.0128  0.0088  -0.0009 35  ASP   C CB  
1331 C CG  . ASP   B 29  ? 0.2100 0.2113 0.2885 0.0127  0.0062  -0.0064 35  ASP   C CG  
1332 O OD1 . ASP   B 29  ? 0.2243 0.2278 0.3113 0.0112  0.0058  -0.0053 35  ASP   C OD1 
1333 O OD2 . ASP   B 29  ? 0.2678 0.2660 0.3398 0.0143  0.0042  -0.0116 35  ASP   C OD2 
1334 N N   . SER   B 30  ? 0.1455 0.1536 0.2459 0.0096  0.0126  0.0082  36  SER   C N   
1335 C CA  A SER   B 30  ? 0.1429 0.1534 0.2488 0.0086  0.0127  0.0114  36  SER   C CA  
1336 C CA  B SER   B 30  ? 0.1486 0.1592 0.2540 0.0086  0.0126  0.0115  36  SER   C CA  
1337 C C   . SER   B 30  ? 0.1456 0.1564 0.2507 0.0081  0.0101  0.0079  36  SER   C C   
1338 O O   . SER   B 30  ? 0.1408 0.1537 0.2446 0.0077  0.0095  0.0108  36  SER   C O   
1339 C CB  A SER   B 30  ? 0.1466 0.1566 0.2640 0.0085  0.0159  0.0130  36  SER   C CB  
1340 C CB  B SER   B 30  ? 0.1729 0.1835 0.2894 0.0085  0.0159  0.0141  36  SER   C CB  
1341 O OG  A SER   B 30  ? 0.1477 0.1594 0.2711 0.0079  0.0165  0.0155  36  SER   C OG  
1342 O OG  B SER   B 30  ? 0.1905 0.1982 0.3127 0.0085  0.0163  0.0088  36  SER   C OG  
1343 N N   . SER   B 31  ? 0.1457 0.1543 0.2511 0.0084  0.0083  0.0018  37  SER   C N   
1344 C CA  . SER   B 31  ? 0.1584 0.1679 0.2647 0.0080  0.0053  -0.0015 37  SER   C CA  
1345 C C   . SER   B 31  ? 0.1470 0.1577 0.2428 0.0084  0.0029  -0.0007 37  SER   C C   
1346 O O   . SER   B 31  ? 0.1562 0.1685 0.2535 0.0080  0.0014  -0.0012 37  SER   C O   
1347 C CB  . SER   B 31  ? 0.2026 0.2096 0.3108 0.0083  0.0028  -0.0086 37  SER   C CB  
1348 O OG  . SER   B 31  ? 0.2744 0.2792 0.3711 0.0099  0.0007  -0.0119 37  SER   C OG  
1349 N N   . ARG   B 32  ? 0.1388 0.1486 0.2251 0.0091  0.0030  0.0007  38  ARG   C N   
1350 C CA  . ARG   B 32  ? 0.1393 0.1498 0.2162 0.0094  0.0012  0.0016  38  ARG   C CA  
1351 C C   . ARG   B 32  ? 0.1363 0.1486 0.2115 0.0087  0.0025  0.0074  38  ARG   C C   
1352 O O   . ARG   B 32  ? 0.1281 0.1407 0.1961 0.0087  0.0011  0.0085  38  ARG   C O   
1353 C CB  . ARG   B 32  ? 0.1684 0.1764 0.2359 0.0108  0.0005  -0.0005 38  ARG   C CB  
1354 C CG  . ARG   B 32  ? 0.1757 0.1812 0.2415 0.0122  -0.0016 -0.0067 38  ARG   C CG  
1355 C CD  . ARG   B 32  ? 0.1687 0.1711 0.2239 0.0142  -0.0015 -0.0082 38  ARG   C CD  
1356 N NE  . ARG   B 32  ? 0.1568 0.1595 0.2031 0.0148  -0.0027 -0.0065 38  ARG   C NE  
1357 C CZ  . ARG   B 32  ? 0.1560 0.1560 0.1923 0.0171  -0.0037 -0.0086 38  ARG   C CZ  
1358 N NH1 . ARG   B 32  ? 0.1779 0.1746 0.2104 0.0192  -0.0038 -0.0127 38  ARG   C NH1 
1359 N NH2 . ARG   B 32  ? 0.1748 0.1750 0.2044 0.0175  -0.0046 -0.0068 38  ARG   C NH2 
1360 N N   . ASP   B 33  ? 0.1180 0.1313 0.1992 0.0081  0.0049  0.0112  39  ASP   C N   
1361 C CA  . ASP   B 33  ? 0.1158 0.1305 0.1948 0.0077  0.0056  0.0164  39  ASP   C CA  
1362 C C   . ASP   B 33  ? 0.1196 0.1338 0.1913 0.0078  0.0047  0.0170  39  ASP   C C   
1363 O O   . ASP   B 33  ? 0.1226 0.1377 0.1897 0.0073  0.0035  0.0197  39  ASP   C O   
1364 C CB  . ASP   B 33  ? 0.1204 0.1362 0.1973 0.0076  0.0049  0.0184  39  ASP   C CB  
1365 C CG  . ASP   B 33  ? 0.1344 0.1513 0.2085 0.0074  0.0051  0.0235  39  ASP   C CG  
1366 O OD1 . ASP   B 33  ? 0.1415 0.1592 0.2201 0.0075  0.0065  0.0265  39  ASP   C OD1 
1367 O OD2 . ASP   B 33  ? 0.1316 0.1483 0.1993 0.0074  0.0038  0.0244  39  ASP   C OD2 
1368 N N   . LEU   B 34  ? 0.1120 0.1247 0.1833 0.0084  0.0056  0.0150  40  LEU   C N   
1369 C CA  . LEU   B 34  ? 0.1161 0.1283 0.1819 0.0086  0.0056  0.0163  40  LEU   C CA  
1370 C C   . LEU   B 34  ? 0.1260 0.1383 0.1969 0.0089  0.0083  0.0183  40  LEU   C C   
1371 O O   . LEU   B 34  ? 0.1301 0.1414 0.2061 0.0096  0.0102  0.0167  40  LEU   C O   
1372 C CB  . LEU   B 34  ? 0.1330 0.1425 0.1914 0.0098  0.0048  0.0122  40  LEU   C CB  
1373 C CG  . LEU   B 34  ? 0.1373 0.1466 0.1894 0.0097  0.0021  0.0107  40  LEU   C CG  
1374 C CD1 . LEU   B 34  ? 0.1584 0.1649 0.2029 0.0116  0.0015  0.0071  40  LEU   C CD1 
1375 C CD2 . LEU   B 34  ? 0.1510 0.1613 0.2000 0.0086  0.0013  0.0143  40  LEU   C CD2 
1376 N N   . LEU   B 35  ? 0.1149 0.1283 0.1848 0.0084  0.0084  0.0215  41  LEU   C N   
1377 C CA  . LEU   B 35  ? 0.1171 0.1309 0.1921 0.0089  0.0111  0.0237  41  LEU   C CA  
1378 C C   . LEU   B 35  ? 0.1253 0.1388 0.1963 0.0087  0.0111  0.0250  41  LEU   C C   
1379 O O   . LEU   B 35  ? 0.1344 0.1488 0.2018 0.0074  0.0084  0.0262  41  LEU   C O   
1380 C CB  . LEU   B 35  ? 0.1204 0.1375 0.2035 0.0082  0.0111  0.0282  41  LEU   C CB  
1381 C CG  . LEU   B 35  ? 0.1227 0.1408 0.2129 0.0088  0.0139  0.0311  41  LEU   C CG  
1382 C CD1 . LEU   B 35  ? 0.1497 0.1696 0.2484 0.0091  0.0150  0.0339  41  LEU   C CD1 
1383 C CD2 . LEU   B 35  ? 0.1384 0.1590 0.2291 0.0077  0.0123  0.0346  41  LEU   C CD2 
1384 N N   . VAL   B 36  ? 0.1286 0.1405 0.2003 0.0100  0.0144  0.0249  42  VAL   C N   
1385 C CA  . VAL   B 36  ? 0.1305 0.1418 0.2003 0.0102  0.0158  0.0266  42  VAL   C CA  
1386 C C   . VAL   B 36  ? 0.1258 0.1390 0.2047 0.0103  0.0188  0.0304  42  VAL   C C   
1387 O O   . VAL   B 36  ? 0.1420 0.1541 0.2246 0.0119  0.0220  0.0298  42  VAL   C O   
1388 C CB  . VAL   B 36  ? 0.1472 0.1540 0.2080 0.0124  0.0178  0.0232  42  VAL   C CB  
1389 C CG1 . VAL   B 36  ? 0.1680 0.1739 0.2276 0.0127  0.0202  0.0257  42  VAL   C CG1 
1390 C CG2 . VAL   B 36  ? 0.1569 0.1624 0.2096 0.0123  0.0143  0.0196  42  VAL   C CG2 
1391 N N   . SER   B 37  ? 0.1272 0.1432 0.2106 0.0088  0.0177  0.0342  43  SER   C N   
1392 C CA  . SER   B 37  ? 0.1253 0.1439 0.2189 0.0088  0.0203  0.0382  43  SER   C CA  
1393 C C   . SER   B 37  ? 0.1402 0.1578 0.2339 0.0088  0.0225  0.0398  43  SER   C C   
1394 O O   . SER   B 37  ? 0.1489 0.1643 0.2350 0.0084  0.0214  0.0383  43  SER   C O   
1395 C CB  . SER   B 37  ? 0.1279 0.1514 0.2293 0.0069  0.0163  0.0417  43  SER   C CB  
1396 O OG  . SER   B 37  ? 0.1554 0.1801 0.2535 0.0048  0.0116  0.0420  43  SER   C OG  
1397 N N   . SER   B 38  ? 0.1464 0.1653 0.2490 0.0096  0.0266  0.0430  44  SER   C N   
1398 C CA  . SER   B 38  ? 0.1613 0.1795 0.2665 0.0098  0.0298  0.0454  44  SER   C CA  
1399 C C   . SER   B 38  ? 0.1816 0.2045 0.2960 0.0066  0.0258  0.0489  44  SER   C C   
1400 O O   . SER   B 38  ? 0.1958 0.2232 0.3174 0.0052  0.0218  0.0507  44  SER   C O   
1401 C CB  . SER   B 38  ? 0.1935 0.2103 0.3040 0.0125  0.0370  0.0472  44  SER   C CB  
1402 O OG  . SER   B 38  ? 0.2435 0.2650 0.3667 0.0120  0.0367  0.0505  44  SER   C OG  
1403 N N   . THR   B 39  ? 0.1789 0.2007 0.2932 0.0057  0.0265  0.0499  45  THR   C N   
1404 C CA  . THR   B 39  ? 0.1871 0.2128 0.3103 0.0025  0.0222  0.0525  45  THR   C CA  
1405 C C   . THR   B 39  ? 0.2191 0.2454 0.3533 0.0027  0.0274  0.0564  45  THR   C C   
1406 O O   . THR   B 39  ? 0.2197 0.2421 0.3502 0.0053  0.0341  0.0566  45  THR   C O   
1407 C CB  . THR   B 39  ? 0.1986 0.2217 0.3123 0.0007  0.0179  0.0498  45  THR   C CB  
1408 O OG1 . THR   B 39  ? 0.2211 0.2393 0.3282 0.0023  0.0228  0.0491  45  THR   C OG1 
1409 C CG2 . THR   B 39  ? 0.2090 0.2311 0.3118 0.0008  0.0136  0.0461  45  THR   C CG2 
1410 N N   . THR   B 40  ? 0.2405 0.2718 0.3880 -0.0001 0.0239  0.0594  46  THR   C N   
1411 C CA  . THR   B 40  ? 0.2606 0.2932 0.4211 -0.0004 0.0284  0.0635  46  THR   C CA  
1412 C C   . THR   B 40  ? 0.2667 0.2956 0.4229 -0.0017 0.0289  0.0627  46  THR   C C   
1413 O O   . THR   B 40  ? 0.3006 0.3263 0.4582 0.0000  0.0361  0.0648  46  THR   C O   
1414 C CB  . THR   B 40  ? 0.3182 0.3580 0.4963 -0.0028 0.0241  0.0670  46  THR   C CB  
1415 O OG1 . THR   B 40  ? 0.3734 0.4152 0.5499 -0.0061 0.0149  0.0651  46  THR   C OG1 
1416 C CG2 . THR   B 40  ? 0.3118 0.3549 0.4940 -0.0010 0.0245  0.0682  46  THR   C CG2 
1417 N N   . ALA   B 41  ? 0.2441 0.2727 0.3944 -0.0044 0.0217  0.0600  47  ALA   C N   
1418 C CA  . ALA   B 41  ? 0.2561 0.2809 0.4026 -0.0058 0.0215  0.0591  47  ALA   C CA  
1419 C C   . ALA   B 41  ? 0.2357 0.2543 0.3643 -0.0032 0.0240  0.0557  47  ALA   C C   
1420 O O   . ALA   B 41  ? 0.2299 0.2479 0.3484 -0.0019 0.0220  0.0528  47  ALA   C O   
1421 C CB  . ALA   B 41  ? 0.2728 0.2999 0.4216 -0.0097 0.0124  0.0574  47  ALA   C CB  
1422 N N   . GLN   B 42  ? 0.2383 0.2523 0.3632 -0.0026 0.0279  0.0562  48  GLN   C N   
1423 C CA  . GLN   B 42  ? 0.2538 0.2621 0.3621 -0.0001 0.0297  0.0533  48  GLN   C CA  
1424 C C   . GLN   B 42  ? 0.2481 0.2557 0.3489 -0.0023 0.0225  0.0498  48  GLN   C C   
1425 O O   . GLN   B 42  ? 0.2663 0.2753 0.3739 -0.0058 0.0179  0.0500  48  GLN   C O   
1426 C CB  . GLN   B 42  ? 0.3192 0.3226 0.4261 0.0019  0.0368  0.0558  48  GLN   C CB  
1427 C CG  . GLN   B 42  ? 0.4352 0.4374 0.5436 0.0058  0.0452  0.0586  48  GLN   C CG  
1428 C CD  . GLN   B 42  ? 0.5725 0.5689 0.6758 0.0085  0.0523  0.0608  48  GLN   C CD  
1429 O OE1 . GLN   B 42  ? 0.6188 0.6151 0.7325 0.0069  0.0549  0.0644  48  GLN   C OE1 
1430 N NE2 . GLN   B 42  ? 0.6147 0.6061 0.7020 0.0129  0.0554  0.0589  48  GLN   C NE2 
1431 N N   . GLY   B 43  ? 0.2166 0.2216 0.3036 -0.0002 0.0215  0.0464  49  GLY   C N   
1432 C CA  . GLY   B 43  ? 0.2221 0.2258 0.3001 -0.0015 0.0159  0.0429  49  GLY   C CA  
1433 C C   . GLY   B 43  ? 0.2182 0.2165 0.2873 0.0000  0.0184  0.0422  49  GLY   C C   
1434 O O   . GLY   B 43  ? 0.2467 0.2420 0.3138 0.0028  0.0245  0.0440  49  GLY   C O   
1435 N N   . CYS   B 44  ? 0.2055 0.2021 0.2685 -0.0013 0.0139  0.0397  50  CYS   C N   
1436 C CA  . CYS   B 44  ? 0.2236 0.2151 0.2793 -0.0002 0.0156  0.0393  50  CYS   C CA  
1437 C C   . CYS   B 44  ? 0.2237 0.2129 0.2663 0.0018  0.0137  0.0359  50  CYS   C C   
1438 O O   . CYS   B 44  ? 0.2658 0.2508 0.3023 0.0029  0.0147  0.0357  50  CYS   C O   
1439 C CB  . CYS   B 44  ? 0.2252 0.2158 0.2877 -0.0038 0.0128  0.0399  50  CYS   C CB  
1440 S SG  . CYS   B 44  ? 0.3113 0.3046 0.3919 -0.0064 0.0153  0.0442  50  CYS   C SG  
1441 N N   . ASP   B 45  ? 0.1859 0.1777 0.2249 0.0024  0.0109  0.0336  51  ASP   C N   
1442 C CA  . ASP   B 45  ? 0.1880 0.1782 0.2164 0.0042  0.0090  0.0304  51  ASP   C CA  
1443 C C   . ASP   B 45  ? 0.2011 0.1886 0.2223 0.0083  0.0132  0.0303  51  ASP   C C   
1444 O O   . ASP   B 45  ? 0.2328 0.2207 0.2565 0.0098  0.0170  0.0318  51  ASP   C O   
1445 C CB  . ASP   B 45  ? 0.1908 0.1846 0.2192 0.0036  0.0054  0.0283  51  ASP   C CB  
1446 C CG  . ASP   B 45  ? 0.2348 0.2306 0.2670 0.0005  0.0008  0.0281  51  ASP   C CG  
1447 O OD1 . ASP   B 45  ? 0.2507 0.2442 0.2821 -0.0010 -0.0008 0.0280  51  ASP   C OD1 
1448 O OD2 . ASP   B 45  ? 0.2118 0.2112 0.2476 -0.0002 -0.0011 0.0281  51  ASP   C OD2 
1449 N N   . THR   B 46  ? 0.1893 0.1739 0.2014 0.0103  0.0125  0.0286  52  THR   C N   
1450 C CA  . THR   B 46  ? 0.1937 0.1756 0.1971 0.0145  0.0151  0.0278  52  THR   C CA  
1451 C C   . THR   B 46  ? 0.1816 0.1654 0.1803 0.0156  0.0115  0.0240  52  THR   C C   
1452 O O   . THR   B 46  ? 0.1906 0.1753 0.1886 0.0142  0.0078  0.0224  52  THR   C O   
1453 C CB  . THR   B 46  ? 0.2267 0.2041 0.2237 0.0164  0.0168  0.0290  52  THR   C CB  
1454 O OG1 . THR   B 46  ? 0.2554 0.2308 0.2584 0.0153  0.0207  0.0328  52  THR   C OG1 
1455 C CG2 . THR   B 46  ? 0.2588 0.2333 0.2450 0.0214  0.0185  0.0280  52  THR   C CG2 
1456 N N   . ILE   B 47  ? 0.1850 0.1692 0.1809 0.0181  0.0125  0.0224  53  ILE   C N   
1457 C CA  . ILE   B 47  ? 0.1794 0.1652 0.1723 0.0190  0.0090  0.0186  53  ILE   C CA  
1458 C C   . ILE   B 47  ? 0.1814 0.1644 0.1646 0.0224  0.0080  0.0170  53  ILE   C C   
1459 O O   . ILE   B 47  ? 0.2030 0.1823 0.1795 0.0256  0.0110  0.0182  53  ILE   C O   
1460 C CB  . ILE   B 47  ? 0.1898 0.1765 0.1838 0.0204  0.0102  0.0171  53  ILE   C CB  
1461 C CG1 . ILE   B 47  ? 0.1921 0.1815 0.1959 0.0177  0.0119  0.0193  53  ILE   C CG1 
1462 C CG2 . ILE   B 47  ? 0.2061 0.1947 0.1989 0.0209  0.0063  0.0129  53  ILE   C CG2 
1463 C CD1 . ILE   B 47  ? 0.2199 0.2131 0.2305 0.0141  0.0083  0.0194  53  ILE   C CD1 
1464 N N   . ALA   B 48  ? 0.1639 0.1484 0.1462 0.0221  0.0041  0.0147  54  ALA   C N   
1465 C CA  . ALA   B 48  ? 0.1664 0.1489 0.1406 0.0254  0.0024  0.0131  54  ALA   C CA  
1466 C C   . ALA   B 48  ? 0.1698 0.1518 0.1389 0.0288  0.0018  0.0102  54  ALA   C C   
1467 O O   . ALA   B 48  ? 0.1710 0.1553 0.1446 0.0277  0.0008  0.0080  54  ALA   C O   
1468 C CB  . ALA   B 48  ? 0.1645 0.1496 0.1411 0.0242  -0.0014 0.0112  54  ALA   C CB  
1469 N N   . ARG   B 49  ? 0.1722 0.1507 0.1316 0.0329  0.0021  0.0101  55  ARG   C N   
1470 C CA  . ARG   B 49  ? 0.1779 0.1552 0.1305 0.0367  0.0006  0.0067  55  ARG   C CA  
1471 C C   . ARG   B 49  ? 0.1817 0.1588 0.1284 0.0394  -0.0035 0.0051  55  ARG   C C   
1472 O O   . ARG   B 49  ? 0.2066 0.1801 0.1451 0.0426  -0.0021 0.0073  55  ARG   C O   
1473 C CB  . ARG   B 49  ? 0.1943 0.1670 0.1395 0.0398  0.0055  0.0087  55  ARG   C CB  
1474 C CG  . ARG   B 49  ? 0.1891 0.1624 0.1419 0.0371  0.0099  0.0109  55  ARG   C CG  
1475 C CD  . ARG   B 49  ? 0.2001 0.1766 0.1597 0.0351  0.0081  0.0076  55  ARG   C CD  
1476 N NE  . ARG   B 49  ? 0.2024 0.1795 0.1694 0.0329  0.0125  0.0105  55  ARG   C NE  
1477 C CZ  . ARG   B 49  ? 0.1952 0.1756 0.1711 0.0301  0.0118  0.0094  55  ARG   C CZ  
1478 N NH1 . ARG   B 49  ? 0.1953 0.1781 0.1736 0.0293  0.0075  0.0054  55  ARG   C NH1 
1479 N NH2 . ARG   B 49  ? 0.2092 0.1905 0.1924 0.0283  0.0156  0.0125  55  ARG   C NH2 
1480 N N   . CYS   B 50  ? 0.1720 0.1529 0.1238 0.0381  -0.0083 0.0017  56  CYS   C N   
1481 C CA  . CYS   B 50  ? 0.1749 0.1570 0.1251 0.0398  -0.0124 0.0005  56  CYS   C CA  
1482 C C   . CYS   B 50  ? 0.1748 0.1617 0.1332 0.0381  -0.0171 -0.0035 56  CYS   C C   
1483 O O   . CYS   B 50  ? 0.1843 0.1732 0.1497 0.0355  -0.0168 -0.0051 56  CYS   C O   
1484 C CB  . CYS   B 50  ? 0.1696 0.1514 0.1223 0.0380  -0.0105 0.0042  56  CYS   C CB  
1485 S SG  . CYS   B 50  ? 0.1739 0.1597 0.1391 0.0322  -0.0101 0.0047  56  CYS   C SG  
1486 N N   . ASP   B 51  ? 0.1955 0.1842 0.1542 0.0397  -0.0212 -0.0049 57  ASP   C N   
1487 C CA  . ASP   B 51  ? 0.2025 0.1959 0.1709 0.0381  -0.0252 -0.0079 57  ASP   C CA  
1488 C C   . ASP   B 51  ? 0.1917 0.1871 0.1655 0.0366  -0.0248 -0.0055 57  ASP   C C   
1489 O O   . ASP   B 51  ? 0.2037 0.2026 0.1837 0.0368  -0.0282 -0.0073 57  ASP   C O   
1490 C CB  . ASP   B 51  ? 0.2318 0.2263 0.1977 0.0414  -0.0310 -0.0124 57  ASP   C CB  
1491 C CG  . ASP   B 51  ? 0.2930 0.2860 0.2506 0.0457  -0.0333 -0.0115 57  ASP   C CG  
1492 O OD1 . ASP   B 51  ? 0.2818 0.2727 0.2359 0.0461  -0.0300 -0.0073 57  ASP   C OD1 
1493 O OD2 . ASP   B 51  ? 0.3747 0.3689 0.3302 0.0487  -0.0391 -0.0152 57  ASP   C OD2 
1494 N N   . CYS   B 52  ? 0.1773 0.1705 0.1496 0.0349  -0.0205 -0.0016 58  CYS   C N   
1495 C CA  . CYS   B 52  ? 0.1737 0.1680 0.1505 0.0335  -0.0198 0.0003  58  CYS   C CA  
1496 C C   . CYS   B 52  ? 0.1582 0.1569 0.1457 0.0309  -0.0209 -0.0012 58  CYS   C C   
1497 O O   . CYS   B 52  ? 0.1596 0.1597 0.1518 0.0288  -0.0205 -0.0024 58  CYS   C O   
1498 C CB  . CYS   B 52  ? 0.1753 0.1663 0.1499 0.0314  -0.0156 0.0039  58  CYS   C CB  
1499 S SG  . CYS   B 52  ? 0.1858 0.1713 0.1500 0.0343  -0.0131 0.0068  58  CYS   C SG  
1500 N N   . GLN   B 53  ? 0.1528 0.1531 0.1442 0.0313  -0.0217 -0.0008 59  GLN   C N   
1501 C CA  . GLN   B 53  ? 0.1597 0.1635 0.1611 0.0291  -0.0213 -0.0011 59  GLN   C CA  
1502 C C   . GLN   B 53  ? 0.1428 0.1449 0.1437 0.0283  -0.0183 0.0017  59  GLN   C C   
1503 O O   . GLN   B 53  ? 0.1474 0.1518 0.1552 0.0275  -0.0175 0.0021  59  GLN   C O   
1504 C CB  . GLN   B 53  ? 0.1715 0.1795 0.1804 0.0307  -0.0252 -0.0037 59  GLN   C CB  
1505 C CG  . GLN   B 53  ? 0.2157 0.2256 0.2273 0.0309  -0.0286 -0.0075 59  GLN   C CG  
1506 C CD  . GLN   B 53  ? 0.2359 0.2504 0.2576 0.0316  -0.0327 -0.0104 59  GLN   C CD  
1507 O OE1 . GLN   B 53  ? 0.2681 0.2832 0.2873 0.0344  -0.0374 -0.0131 59  GLN   C OE1 
1508 N NE2 . GLN   B 53  ? 0.2135 0.2312 0.2469 0.0296  -0.0311 -0.0097 59  GLN   C NE2 
1509 N N   . THR   B 54  ? 0.1442 0.1420 0.1372 0.0284  -0.0162 0.0039  60  THR   C N   
1510 C CA  . THR   B 54  ? 0.1588 0.1541 0.1507 0.0272  -0.0134 0.0060  60  THR   C CA  
1511 C C   . THR   B 54  ? 0.1609 0.1527 0.1481 0.0250  -0.0114 0.0075  60  THR   C C   
1512 O O   . THR   B 54  ? 0.1708 0.1610 0.1539 0.0255  -0.0114 0.0078  60  THR   C O   
1513 C CB  . THR   B 54  ? 0.2029 0.1959 0.1915 0.0296  -0.0131 0.0070  60  THR   C CB  
1514 O OG1 . THR   B 54  ? 0.2470 0.2368 0.2285 0.0313  -0.0133 0.0077  60  THR   C OG1 
1515 C CG2 . THR   B 54  ? 0.2019 0.1987 0.1961 0.0320  -0.0154 0.0058  60  THR   C CG2 
1516 N N   . GLY   B 55  ? 0.1416 0.1323 0.1296 0.0227  -0.0097 0.0086  61  GLY   C N   
1517 C CA  . GLY   B 55  ? 0.1481 0.1362 0.1334 0.0203  -0.0085 0.0098  61  GLY   C CA  
1518 C C   . GLY   B 55  ? 0.1417 0.1285 0.1270 0.0184  -0.0075 0.0105  61  GLY   C C   
1519 O O   . GLY   B 55  ? 0.1509 0.1372 0.1362 0.0195  -0.0069 0.0104  61  GLY   C O   
1520 N N   . VAL   B 56  ? 0.1359 0.1216 0.1207 0.0160  -0.0073 0.0113  62  VAL   C N   
1521 C CA  . VAL   B 56  ? 0.1300 0.1138 0.1132 0.0143  -0.0070 0.0118  62  VAL   C CA  
1522 C C   . VAL   B 56  ? 0.1289 0.1154 0.1157 0.0123  -0.0076 0.0125  62  VAL   C C   
1523 O O   . VAL   B 56  ? 0.1432 0.1307 0.1320 0.0113  -0.0080 0.0129  62  VAL   C O   
1524 C CB  . VAL   B 56  ? 0.1411 0.1196 0.1195 0.0133  -0.0070 0.0121  62  VAL   C CB  
1525 C CG1 . VAL   B 56  ? 0.1683 0.1445 0.1443 0.0116  -0.0077 0.0120  62  VAL   C CG1 
1526 C CG2 . VAL   B 56  ? 0.1611 0.1363 0.1360 0.0157  -0.0060 0.0117  62  VAL   C CG2 
1527 N N   . TYR   B 57  ? 0.1304 0.1179 0.1180 0.0120  -0.0074 0.0129  63  TYR   C N   
1528 C CA  . TYR   B 57  ? 0.1194 0.1093 0.1102 0.0103  -0.0080 0.0140  63  TYR   C CA  
1529 C C   . TYR   B 57  ? 0.1411 0.1285 0.1277 0.0092  -0.0089 0.0147  63  TYR   C C   
1530 O O   . TYR   B 57  ? 0.1462 0.1304 0.1275 0.0103  -0.0083 0.0142  63  TYR   C O   
1531 C CB  . TYR   B 57  ? 0.1270 0.1212 0.1239 0.0110  -0.0070 0.0143  63  TYR   C CB  
1532 C CG  . TYR   B 57  ? 0.1299 0.1240 0.1265 0.0121  -0.0054 0.0151  63  TYR   C CG  
1533 C CD1 . TYR   B 57  ? 0.1435 0.1367 0.1392 0.0141  -0.0040 0.0145  63  TYR   C CD1 
1534 C CD2 . TYR   B 57  ? 0.1239 0.1190 0.1213 0.0115  -0.0051 0.0170  63  TYR   C CD2 
1535 C CE1 . TYR   B 57  ? 0.1512 0.1441 0.1470 0.0154  -0.0016 0.0158  63  TYR   C CE1 
1536 C CE2 . TYR   B 57  ? 0.1399 0.1345 0.1365 0.0130  -0.0029 0.0183  63  TYR   C CE2 
1537 C CZ  . TYR   B 57  ? 0.1456 0.1391 0.1414 0.0149  -0.0009 0.0177  63  TYR   C CZ  
1538 O OH  . TYR   B 57  ? 0.1788 0.1715 0.1742 0.0168  0.0023  0.0193  63  TYR   C OH  
1539 N N   . TYR   B 58  ? 0.1297 0.1187 0.1185 0.0074  -0.0103 0.0158  64  TYR   C N   
1540 C CA  . TYR   B 58  ? 0.1346 0.1216 0.1192 0.0065  -0.0122 0.0164  64  TYR   C CA  
1541 C C   . TYR   B 58  ? 0.1459 0.1351 0.1313 0.0077  -0.0111 0.0180  64  TYR   C C   
1542 O O   . TYR   B 58  ? 0.1484 0.1416 0.1402 0.0074  -0.0105 0.0193  64  TYR   C O   
1543 C CB  . TYR   B 58  ? 0.1511 0.1387 0.1384 0.0041  -0.0148 0.0170  64  TYR   C CB  
1544 C CG  . TYR   B 58  ? 0.1717 0.1572 0.1543 0.0033  -0.0178 0.0170  64  TYR   C CG  
1545 C CD1 . TYR   B 58  ? 0.1840 0.1641 0.1586 0.0037  -0.0188 0.0152  64  TYR   C CD1 
1546 C CD2 . TYR   B 58  ? 0.1740 0.1624 0.1593 0.0026  -0.0197 0.0188  64  TYR   C CD2 
1547 C CE1 . TYR   B 58  ? 0.1962 0.1737 0.1648 0.0033  -0.0220 0.0147  64  TYR   C CE1 
1548 C CE2 . TYR   B 58  ? 0.1851 0.1714 0.1650 0.0023  -0.0232 0.0187  64  TYR   C CE2 
1549 C CZ  . TYR   B 58  ? 0.1907 0.1714 0.1618 0.0027  -0.0244 0.0165  64  TYR   C CZ  
1550 O OH  . TYR   B 58  ? 0.2390 0.2170 0.2032 0.0028  -0.0283 0.0158  64  TYR   C OH  
1551 N N   . CYS   B 59  ? 0.1440 0.1299 0.1224 0.0090  -0.0108 0.0180  65  CYS   C N   
1552 C CA  . CYS   B 59  ? 0.1452 0.1322 0.1226 0.0106  -0.0093 0.0201  65  CYS   C CA  
1553 C C   . CYS   B 59  ? 0.1588 0.1433 0.1293 0.0103  -0.0123 0.0207  65  CYS   C C   
1554 O O   . CYS   B 59  ? 0.1727 0.1522 0.1340 0.0111  -0.0133 0.0193  65  CYS   C O   
1555 C CB  . CYS   B 59  ? 0.1516 0.1363 0.1257 0.0132  -0.0058 0.0199  65  CYS   C CB  
1556 S SG  . CYS   B 59  ? 0.1812 0.1660 0.1534 0.0159  -0.0024 0.0231  65  CYS   C SG  
1557 N N   . SER   B 60  ? 0.1704 0.1582 0.1451 0.0093  -0.0142 0.0226  66  SER   C N   
1558 C CA  . SER   B 60  ? 0.1901 0.1763 0.1591 0.0089  -0.0182 0.0231  66  SER   C CA  
1559 C C   . SER   B 60  ? 0.1980 0.1807 0.1570 0.0119  -0.0171 0.0242  66  SER   C C   
1560 O O   . SER   B 60  ? 0.2215 0.1999 0.1711 0.0122  -0.0205 0.0228  66  SER   C O   
1561 C CB  . SER   B 60  ? 0.2352 0.2263 0.2123 0.0075  -0.0202 0.0253  66  SER   C CB  
1562 O OG  . SER   B 60  ? 0.3461 0.3401 0.3269 0.0092  -0.0171 0.0283  66  SER   C OG  
1563 N N   . SER   B 61  ? 0.1814 0.1653 0.1422 0.0143  -0.0121 0.0264  67  SER   C N   
1564 C CA  . SER   B 61  ? 0.1986 0.1788 0.1498 0.0178  -0.0097 0.0281  67  SER   C CA  
1565 C C   . SER   B 61  ? 0.2187 0.1929 0.1601 0.0194  -0.0083 0.0257  67  SER   C C   
1566 O O   . SER   B 61  ? 0.2489 0.2190 0.1806 0.0226  -0.0062 0.0269  67  SER   C O   
1567 C CB  . SER   B 61  ? 0.2182 0.2012 0.1756 0.0198  -0.0042 0.0316  67  SER   C CB  
1568 O OG  . SER   B 61  ? 0.2233 0.2078 0.1880 0.0196  -0.0005 0.0305  67  SER   C OG  
1569 N N   . ARG   B 62  ? 0.2009 0.1739 0.1440 0.0175  -0.0093 0.0225  68  ARG   C N   
1570 C CA  . ARG   B 62  ? 0.2110 0.1777 0.1448 0.0188  -0.0085 0.0199  68  ARG   C CA  
1571 C C   . ARG   B 62  ? 0.2202 0.1839 0.1509 0.0161  -0.0137 0.0163  68  ARG   C C   
1572 O O   . ARG   B 62  ? 0.2407 0.1987 0.1643 0.0168  -0.0135 0.0137  68  ARG   C O   
1573 C CB  . ARG   B 62  ? 0.2171 0.1848 0.1568 0.0197  -0.0038 0.0196  68  ARG   C CB  
1574 C CG  . ARG   B 62  ? 0.2494 0.2198 0.1936 0.0223  0.0017  0.0228  68  ARG   C CG  
1575 C CD  . ARG   B 62  ? 0.2546 0.2193 0.1875 0.0261  0.0050  0.0238  68  ARG   C CD  
1576 N NE  . ARG   B 62  ? 0.2781 0.2453 0.2168 0.0287  0.0111  0.0274  68  ARG   C NE  
1577 C CZ  . ARG   B 62  ? 0.3032 0.2724 0.2433 0.0299  0.0129  0.0310  68  ARG   C CZ  
1578 N NH1 . ARG   B 62  ? 0.3163 0.2853 0.2512 0.0291  0.0087  0.0316  68  ARG   C NH1 
1579 N NH2 . ARG   B 62  ? 0.3314 0.3022 0.2778 0.0322  0.0191  0.0343  68  ARG   C NH2 
1580 N N   . ARG   B 63  ? 0.2225 0.1899 0.1597 0.0131  -0.0180 0.0164  69  ARG   C N   
1581 C CA  . ARG   B 63  ? 0.2376 0.2031 0.1757 0.0100  -0.0225 0.0134  69  ARG   C CA  
1582 C C   . ARG   B 63  ? 0.2522 0.2152 0.1915 0.0097  -0.0200 0.0114  69  ARG   C C   
1583 O O   . ARG   B 63  ? 0.2810 0.2385 0.2150 0.0090  -0.0218 0.0085  69  ARG   C O   
1584 C CB  . ARG   B 63  ? 0.2567 0.2167 0.1843 0.0099  -0.0274 0.0112  69  ARG   C CB  
1585 C CG  . ARG   B 63  ? 0.3265 0.2895 0.2541 0.0097  -0.0314 0.0131  69  ARG   C CG  
1586 C CD  . ARG   B 63  ? 0.4739 0.4332 0.3964 0.0079  -0.0383 0.0100  69  ARG   C CD  
1587 N NE  . ARG   B 63  ? 0.5561 0.5187 0.4790 0.0079  -0.0429 0.0119  69  ARG   C NE  
1588 C CZ  . ARG   B 63  ? 0.6347 0.5941 0.5458 0.0107  -0.0453 0.0122  69  ARG   C CZ  
1589 N NH1 . ARG   B 63  ? 0.6471 0.5994 0.5443 0.0137  -0.0433 0.0103  69  ARG   C NH1 
1590 N NH2 . ARG   B 63  ? 0.6448 0.6079 0.5573 0.0107  -0.0498 0.0143  69  ARG   C NH2 
1591 N N   . LYS   B 64  ? 0.2100 0.1768 0.1564 0.0104  -0.0160 0.0128  70  LYS   C N   
1592 C CA  . LYS   B 64  ? 0.2161 0.1807 0.1632 0.0109  -0.0136 0.0113  70  LYS   C CA  
1593 C C   . LYS   B 64  ? 0.1944 0.1643 0.1515 0.0101  -0.0122 0.0124  70  LYS   C C   
1594 O O   . LYS   B 64  ? 0.1936 0.1687 0.1567 0.0102  -0.0113 0.0143  70  LYS   C O   
1595 C CB  . LYS   B 64  ? 0.2816 0.2436 0.2234 0.0144  -0.0093 0.0116  70  LYS   C CB  
1596 C CG  . LYS   B 64  ? 0.4261 0.3804 0.3560 0.0157  -0.0099 0.0094  70  LYS   C CG  
1597 C CD  . LYS   B 64  ? 0.5355 0.4867 0.4612 0.0193  -0.0047 0.0097  70  LYS   C CD  
1598 C CE  . LYS   B 64  ? 0.6185 0.5612 0.5314 0.0209  -0.0049 0.0072  70  LYS   C CE  
1599 N NZ  . LYS   B 64  ? 0.6854 0.6260 0.5895 0.0218  -0.0069 0.0076  70  LYS   C NZ  
1600 N N   . HIS   B 65  ? 0.1783 0.1464 0.1366 0.0096  -0.0119 0.0111  71  HIS   C N   
1601 C CA  . HIS   B 65  ? 0.1727 0.1446 0.1381 0.0097  -0.0103 0.0117  71  HIS   C CA  
1602 C C   . HIS   B 65  ? 0.1978 0.1689 0.1621 0.0125  -0.0073 0.0114  71  HIS   C C   
1603 O O   . HIS   B 65  ? 0.2448 0.2109 0.2035 0.0137  -0.0064 0.0103  71  HIS   C O   
1604 C CB  . HIS   B 65  ? 0.1751 0.1454 0.1423 0.0080  -0.0116 0.0111  71  HIS   C CB  
1605 C CG  . HIS   B 65  ? 0.1623 0.1340 0.1329 0.0051  -0.0144 0.0116  71  HIS   C CG  
1606 N ND1 . HIS   B 65  ? 0.2014 0.1776 0.1791 0.0042  -0.0142 0.0130  71  HIS   C ND1 
1607 C CD2 . HIS   B 65  ? 0.1698 0.1388 0.1379 0.0033  -0.0175 0.0108  71  HIS   C CD2 
1608 C CE1 . HIS   B 65  ? 0.1676 0.1441 0.1478 0.0017  -0.0168 0.0134  71  HIS   C CE1 
1609 N NE2 . HIS   B 65  ? 0.2091 0.1816 0.1842 0.0010  -0.0192 0.0120  71  HIS   C NE2 
1610 N N   . TYR   B 66  ? 0.1574 0.1334 0.1278 0.0137  -0.0057 0.0124  72  TYR   C N   
1611 C CA  . TYR   B 66  ? 0.1572 0.1334 0.1287 0.0164  -0.0031 0.0123  72  TYR   C CA  
1612 C C   . TYR   B 66  ? 0.1560 0.1351 0.1327 0.0169  -0.0035 0.0119  72  TYR   C C   
1613 O O   . TYR   B 66  ? 0.1500 0.1331 0.1317 0.0159  -0.0046 0.0121  72  TYR   C O   
1614 C CB  . TYR   B 66  ? 0.1671 0.1469 0.1428 0.0176  -0.0010 0.0137  72  TYR   C CB  
1615 C CG  . TYR   B 66  ? 0.1796 0.1564 0.1491 0.0183  0.0003  0.0146  72  TYR   C CG  
1616 C CD1 . TYR   B 66  ? 0.2231 0.1955 0.1868 0.0206  0.0029  0.0144  72  TYR   C CD1 
1617 C CD2 . TYR   B 66  ? 0.1984 0.1766 0.1679 0.0171  -0.0008 0.0159  72  TYR   C CD2 
1618 C CE1 . TYR   B 66  ? 0.2357 0.2047 0.1923 0.0219  0.0045  0.0153  72  TYR   C CE1 
1619 C CE2 . TYR   B 66  ? 0.2134 0.1887 0.1760 0.0184  0.0004  0.0170  72  TYR   C CE2 
1620 C CZ  . TYR   B 66  ? 0.2256 0.1960 0.1812 0.0209  0.0030  0.0166  72  TYR   C CZ  
1621 O OH  . TYR   B 66  ? 0.2639 0.2310 0.2114 0.0227  0.0044  0.0178  72  TYR   C OH  
1622 N N   . PRO   B 67  ? 0.1562 0.1331 0.1312 0.0188  -0.0025 0.0114  73  PRO   C N   
1623 C CA  . PRO   B 67  ? 0.1491 0.1290 0.1284 0.0201  -0.0032 0.0111  73  PRO   C CA  
1624 C C   . PRO   B 67  ? 0.1596 0.1446 0.1462 0.0215  -0.0026 0.0112  73  PRO   C C   
1625 O O   . PRO   B 67  ? 0.1973 0.1823 0.1851 0.0228  -0.0004 0.0118  73  PRO   C O   
1626 C CB  . PRO   B 67  ? 0.1775 0.1531 0.1527 0.0221  -0.0022 0.0109  73  PRO   C CB  
1627 C CG  . PRO   B 67  ? 0.2135 0.1848 0.1840 0.0224  -0.0003 0.0108  73  PRO   C CG  
1628 C CD  . PRO   B 67  ? 0.1717 0.1430 0.1405 0.0202  -0.0009 0.0109  73  PRO   C CD  
1629 N N   . VAL   B 68  ? 0.1427 0.1319 0.1344 0.0214  -0.0043 0.0106  74  VAL   C N   
1630 C CA  . VAL   B 68  ? 0.1497 0.1439 0.1500 0.0221  -0.0044 0.0102  74  VAL   C CA  
1631 C C   . VAL   B 68  ? 0.1412 0.1383 0.1448 0.0234  -0.0070 0.0086  74  VAL   C C   
1632 O O   . VAL   B 68  ? 0.1472 0.1430 0.1466 0.0232  -0.0086 0.0081  74  VAL   C O   
1633 C CB  . VAL   B 68  ? 0.1619 0.1588 0.1665 0.0201  -0.0041 0.0107  74  VAL   C CB  
1634 C CG1 . VAL   B 68  ? 0.1898 0.1847 0.1921 0.0197  -0.0014 0.0125  74  VAL   C CG1 
1635 C CG2 . VAL   B 68  ? 0.1742 0.1708 0.1765 0.0182  -0.0058 0.0103  74  VAL   C CG2 
1636 N N   . SER   B 69  ? 0.1404 0.1414 0.1520 0.0247  -0.0076 0.0079  75  SER   C N   
1637 C CA  . SER   B 69  ? 0.1416 0.1464 0.1582 0.0257  -0.0109 0.0058  75  SER   C CA  
1638 C C   . SER   B 69  ? 0.1310 0.1389 0.1545 0.0237  -0.0112 0.0050  75  SER   C C   
1639 O O   . SER   B 69  ? 0.1394 0.1483 0.1678 0.0226  -0.0085 0.0064  75  SER   C O   
1640 C CB  . SER   B 69  ? 0.1717 0.1795 0.1955 0.0279  -0.0117 0.0053  75  SER   C CB  
1641 O OG  . SER   B 69  ? 0.2400 0.2447 0.2575 0.0300  -0.0113 0.0063  75  SER   C OG  
1642 N N   . PHE   B 70  ? 0.1176 0.1266 0.1411 0.0234  -0.0139 0.0029  76  PHE   C N   
1643 C CA  . PHE   B 70  ? 0.1209 0.1322 0.1508 0.0215  -0.0140 0.0020  76  PHE   C CA  
1644 C C   . PHE   B 70  ? 0.1226 0.1365 0.1571 0.0224  -0.0179 -0.0016 76  PHE   C C   
1645 O O   . PHE   B 70  ? 0.1333 0.1464 0.1625 0.0245  -0.0207 -0.0031 76  PHE   C O   
1646 C CB  . PHE   B 70  ? 0.1355 0.1444 0.1600 0.0195  -0.0124 0.0033  76  PHE   C CB  
1647 C CG  . PHE   B 70  ? 0.1337 0.1396 0.1492 0.0202  -0.0135 0.0029  76  PHE   C CG  
1648 C CD1 . PHE   B 70  ? 0.1372 0.1397 0.1451 0.0206  -0.0124 0.0047  76  PHE   C CD1 
1649 C CD2 . PHE   B 70  ? 0.1429 0.1492 0.1578 0.0206  -0.0152 0.0008  76  PHE   C CD2 
1650 C CE1 . PHE   B 70  ? 0.1366 0.1362 0.1373 0.0213  -0.0127 0.0048  76  PHE   C CE1 
1651 C CE2 . PHE   B 70  ? 0.1424 0.1457 0.1489 0.0216  -0.0153 0.0010  76  PHE   C CE2 
1652 C CZ  . PHE   B 70  ? 0.1419 0.1420 0.1418 0.0220  -0.0140 0.0032  76  PHE   C CZ  
1653 N N   . SER   B 71  ? 0.1167 0.1334 0.1609 0.0211  -0.0181 -0.0029 77  SER   C N   
1654 C CA  . SER   B 71  ? 0.1249 0.1441 0.1749 0.0218  -0.0223 -0.0069 77  SER   C CA  
1655 C C   . SER   B 71  ? 0.1452 0.1621 0.1881 0.0220  -0.0241 -0.0092 77  SER   C C   
1656 O O   . SER   B 71  ? 0.1699 0.1839 0.2053 0.0213  -0.0217 -0.0073 77  SER   C O   
1657 C CB  . SER   B 71  ? 0.1263 0.1489 0.1907 0.0202  -0.0217 -0.0076 77  SER   C CB  
1658 O OG  . SER   B 71  ? 0.1617 0.1834 0.2277 0.0181  -0.0183 -0.0060 77  SER   C OG  
1659 N N   . LYS   B 72  ? 0.1645 0.1826 0.2099 0.0231  -0.0285 -0.0135 78  LYS   C N   
1660 C CA  . LYS   B 72  ? 0.1663 0.1817 0.2044 0.0238  -0.0300 -0.0161 78  LYS   C CA  
1661 C C   . LYS   B 72  ? 0.1689 0.1842 0.2132 0.0213  -0.0276 -0.0164 78  LYS   C C   
1662 O O   . LYS   B 72  ? 0.1763 0.1944 0.2327 0.0195  -0.0268 -0.0164 78  LYS   C O   
1663 C CB  . LYS   B 72  ? 0.2207 0.2370 0.2589 0.0262  -0.0361 -0.0211 78  LYS   C CB  
1664 C CG  . LYS   B 72  ? 0.2941 0.3107 0.3266 0.0291  -0.0387 -0.0205 78  LYS   C CG  
1665 C CD  . LYS   B 72  ? 0.4380 0.4535 0.4632 0.0325  -0.0445 -0.0248 78  LYS   C CD  
1666 C CE  . LYS   B 72  ? 0.5338 0.5473 0.5475 0.0360  -0.0452 -0.0226 78  LYS   C CE  
1667 N NZ  . LYS   B 72  ? 0.5922 0.6032 0.5950 0.0399  -0.0499 -0.0260 78  LYS   C NZ  
1668 N N   . PRO   B 73  ? 0.1611 0.1733 0.1983 0.0212  -0.0259 -0.0163 79  PRO   C N   
1669 C CA  . PRO   B 73  ? 0.1676 0.1798 0.2112 0.0190  -0.0232 -0.0161 79  PRO   C CA  
1670 C C   . PRO   B 73  ? 0.1672 0.1810 0.2212 0.0185  -0.0260 -0.0206 79  PRO   C C   
1671 O O   . PRO   B 73  ? 0.1979 0.2109 0.2491 0.0203  -0.0305 -0.0253 79  PRO   C O   
1672 C CB  . PRO   B 73  ? 0.1988 0.2071 0.2325 0.0200  -0.0217 -0.0160 79  PRO   C CB  
1673 C CG  . PRO   B 73  ? 0.2323 0.2387 0.2544 0.0222  -0.0222 -0.0146 79  PRO   C CG  
1674 C CD  . PRO   B 73  ? 0.1894 0.1979 0.2131 0.0235  -0.0258 -0.0159 79  PRO   C CD  
1675 N N   . SER   B 74  ? 0.1485 0.1644 0.2145 0.0161  -0.0237 -0.0192 80  SER   C N   
1676 C CA  . SER   B 74  ? 0.1641 0.1819 0.2429 0.0152  -0.0261 -0.0232 80  SER   C CA  
1677 C C   . SER   B 74  ? 0.1563 0.1743 0.2451 0.0129  -0.0219 -0.0211 80  SER   C C   
1678 O O   . SER   B 74  ? 0.1529 0.1703 0.2388 0.0121  -0.0176 -0.0164 80  SER   C O   
1679 C CB  . SER   B 74  ? 0.1933 0.2150 0.2809 0.0153  -0.0282 -0.0234 80  SER   C CB  
1680 O OG  . SER   B 74  ? 0.2759 0.2976 0.3549 0.0176  -0.0318 -0.0244 80  SER   C OG  
1681 N N   . LEU   B 75  ? 0.1592 0.1783 0.2608 0.0118  -0.0235 -0.0248 81  LEU   C N   
1682 C CA  . LEU   B 75  ? 0.1620 0.1813 0.2752 0.0097  -0.0195 -0.0229 81  LEU   C CA  
1683 C C   . LEU   B 75  ? 0.1647 0.1877 0.2896 0.0087  -0.0172 -0.0193 81  LEU   C C   
1684 O O   . LEU   B 75  ? 0.2016 0.2271 0.3362 0.0086  -0.0204 -0.0223 81  LEU   C O   
1685 C CB  . LEU   B 75  ? 0.1848 0.2027 0.3061 0.0091  -0.0226 -0.0292 81  LEU   C CB  
1686 C CG  . LEU   B 75  ? 0.2139 0.2313 0.3479 0.0071  -0.0184 -0.0278 81  LEU   C CG  
1687 C CD1 . LEU   B 75  ? 0.2096 0.2243 0.3359 0.0073  -0.0140 -0.0242 81  LEU   C CD1 
1688 C CD2 . LEU   B 75  ? 0.2466 0.2624 0.3900 0.0064  -0.0223 -0.0350 81  LEU   C CD2 
1689 N N   . ILE   B 76  ? 0.1762 0.1994 0.2998 0.0083  -0.0120 -0.0131 82  ILE   C N   
1690 C CA  . ILE   B 76  ? 0.1929 0.2186 0.3236 0.0081  -0.0087 -0.0088 82  ILE   C CA  
1691 C C   . ILE   B 76  ? 0.1863 0.2117 0.3260 0.0070  -0.0032 -0.0046 82  ILE   C C   
1692 O O   . ILE   B 76  ? 0.1750 0.1983 0.3090 0.0068  -0.0010 -0.0023 82  ILE   C O   
1693 C CB  . ILE   B 76  ? 0.2320 0.2570 0.3492 0.0094  -0.0074 -0.0049 82  ILE   C CB  
1694 C CG1 . ILE   B 76  ? 0.2720 0.2969 0.3793 0.0109  -0.0123 -0.0082 82  ILE   C CG1 
1695 C CG2 . ILE   B 76  ? 0.2603 0.2869 0.3823 0.0097  -0.0031 0.0001  82  ILE   C CG2 
1696 C CD1 . ILE   B 76  ? 0.2949 0.3226 0.4084 0.0118  -0.0147 -0.0097 82  ILE   C CD1 
1697 N N   . PHE   B 77  ? 0.1809 0.2086 0.3351 0.0065  -0.0007 -0.0030 83  PHE   C N   
1698 C CA  . PHE   B 77  ? 0.1770 0.2042 0.3394 0.0059  0.0054  0.0020  83  PHE   C CA  
1699 C C   . PHE   B 77  ? 0.1913 0.2178 0.3427 0.0074  0.0094  0.0084  83  PHE   C C   
1700 O O   . PHE   B 77  ? 0.2295 0.2571 0.3773 0.0085  0.0094  0.0095  83  PHE   C O   
1701 C CB  . PHE   B 77  ? 0.1698 0.1994 0.3518 0.0051  0.0074  0.0021  83  PHE   C CB  
1702 C CG  . PHE   B 77  ? 0.1891 0.2175 0.3803 0.0046  0.0138  0.0069  83  PHE   C CG  
1703 C CD1 . PHE   B 77  ? 0.2089 0.2353 0.4044 0.0034  0.0138  0.0052  83  PHE   C CD1 
1704 C CD2 . PHE   B 77  ? 0.2129 0.2416 0.4065 0.0059  0.0201  0.0138  83  PHE   C CD2 
1705 C CE1 . PHE   B 77  ? 0.2178 0.2428 0.4213 0.0034  0.0200  0.0103  83  PHE   C CE1 
1706 C CE2 . PHE   B 77  ? 0.2190 0.2463 0.4197 0.0060  0.0263  0.0189  83  PHE   C CE2 
1707 C CZ  . PHE   B 77  ? 0.2140 0.2396 0.4204 0.0047  0.0261  0.0172  83  PHE   C CZ  
1708 N N   . VAL   B 78  ? 0.1551 0.1797 0.3009 0.0076  0.0124  0.0123  84  VAL   C N   
1709 C CA  . VAL   B 78  ? 0.1567 0.1801 0.2913 0.0090  0.0154  0.0178  84  VAL   C CA  
1710 C C   . VAL   B 78  ? 0.1487 0.1717 0.2910 0.0096  0.0216  0.0235  84  VAL   C C   
1711 O O   . VAL   B 78  ? 0.1564 0.1789 0.3061 0.0089  0.0230  0.0240  84  VAL   C O   
1712 C CB  . VAL   B 78  ? 0.1620 0.1837 0.2830 0.0089  0.0131  0.0176  84  VAL   C CB  
1713 C CG1 . VAL   B 78  ? 0.1677 0.1881 0.2773 0.0102  0.0151  0.0227  84  VAL   C CG1 
1714 C CG2 . VAL   B 78  ? 0.1792 0.2008 0.2930 0.0086  0.0077  0.0123  84  VAL   C CG2 
1715 N N   . GLU   B 79  ? 0.1448 0.1675 0.2844 0.0114  0.0255  0.0282  85  GLU   C N   
1716 C CA  . GLU   B 79  ? 0.1508 0.1725 0.2953 0.0127  0.0320  0.0345  85  GLU   C CA  
1717 C C   . GLU   B 79  ? 0.1508 0.1705 0.2854 0.0134  0.0324  0.0379  85  GLU   C C   
1718 O O   . GLU   B 79  ? 0.1466 0.1658 0.2694 0.0130  0.0282  0.0361  85  GLU   C O   
1719 C CB  . GLU   B 79  ? 0.1848 0.2058 0.3255 0.0151  0.0362  0.0386  85  GLU   C CB  
1720 C CG  . GLU   B 79  ? 0.2430 0.2664 0.3970 0.0149  0.0372  0.0367  85  GLU   C CG  
1721 C CD  . GLU   B 79  ? 0.3711 0.3961 0.5455 0.0135  0.0399  0.0367  85  GLU   C CD  
1722 O OE1 . GLU   B 79  ? 0.4302 0.4537 0.6093 0.0144  0.0456  0.0419  85  GLU   C OE1 
1723 O OE2 . GLU   B 79  ? 0.4225 0.4500 0.6084 0.0116  0.0362  0.0313  85  GLU   C OE2 
1724 N N   . ALA   B 80  ? 0.1583 0.1770 0.2985 0.0145  0.0376  0.0432  86  ALA   C N   
1725 C CA  . ALA   B 80  ? 0.1721 0.1894 0.3045 0.0155  0.0380  0.0470  86  ALA   C CA  
1726 C C   . ALA   B 80  ? 0.1747 0.1906 0.2891 0.0172  0.0362  0.0490  86  ALA   C C   
1727 O O   . ALA   B 80  ? 0.2096 0.2246 0.3184 0.0187  0.0377  0.0501  86  ALA   C O   
1728 C CB  . ALA   B 80  ? 0.1890 0.2052 0.3299 0.0173  0.0447  0.0534  86  ALA   C CB  
1729 N N   . SER   B 81  ? 0.1605 0.1762 0.2666 0.0167  0.0325  0.0487  87  SER   C N   
1730 C CA  . SER   B 81  ? 0.1779 0.1923 0.2682 0.0179  0.0301  0.0503  87  SER   C CA  
1731 C C   . SER   B 81  ? 0.1942 0.2080 0.2814 0.0193  0.0309  0.0553  87  SER   C C   
1732 O O   . SER   B 81  ? 0.1987 0.2131 0.2963 0.0194  0.0337  0.0576  87  SER   C O   
1733 C CB  . SER   B 81  ? 0.1710 0.1861 0.2548 0.0158  0.0241  0.0450  87  SER   C CB  
1734 O OG  . SER   B 81  ? 0.1655 0.1817 0.2534 0.0144  0.0221  0.0439  87  SER   C OG  
1735 N N   . GLU   B 82  ? 0.2142 0.2270 0.2878 0.0204  0.0278  0.0567  88  GLU   C N   
1736 C CA  . GLU   B 82  ? 0.2328 0.2455 0.3035 0.0219  0.0276  0.0615  88  GLU   C CA  
1737 C C   . GLU   B 82  ? 0.2161 0.2311 0.2941 0.0198  0.0249  0.0599  88  GLU   C C   
1738 O O   . GLU   B 82  ? 0.2372 0.2527 0.3175 0.0210  0.0257  0.0640  88  GLU   C O   
1739 C CB  . GLU   B 82  ? 0.3072 0.3180 0.3618 0.0237  0.0244  0.0632  88  GLU   C CB  
1740 C CG  . GLU   B 82  ? 0.4170 0.4287 0.4649 0.0215  0.0179  0.0593  88  GLU   C CG  
1741 C CD  . GLU   B 82  ? 0.5084 0.5181 0.5417 0.0232  0.0144  0.0611  88  GLU   C CD  
1742 O OE1 . GLU   B 82  ? 0.5181 0.5248 0.5432 0.0261  0.0169  0.0636  88  GLU   C OE1 
1743 O OE2 . GLU   B 82  ? 0.5159 0.5270 0.5462 0.0218  0.0091  0.0599  88  GLU   C OE2 
1744 N N   . TYR   B 83  ? 0.1838 0.2000 0.2657 0.0171  0.0224  0.0542  89  TYR   C N   
1745 C CA  . TYR   B 83  ? 0.1666 0.1844 0.2537 0.0154  0.0203  0.0524  89  TYR   C CA  
1746 C C   . TYR   B 83  ? 0.1837 0.2018 0.2832 0.0138  0.0220  0.0486  89  TYR   C C   
1747 O O   . TYR   B 83  ? 0.1856 0.2045 0.2899 0.0130  0.0213  0.0476  89  TYR   C O   
1748 C CB  . TYR   B 83  ? 0.1616 0.1799 0.2398 0.0140  0.0150  0.0495  89  TYR   C CB  
1749 C CG  . TYR   B 83  ? 0.1575 0.1749 0.2300 0.0131  0.0133  0.0450  89  TYR   C CG  
1750 C CD1 . TYR   B 83  ? 0.1687 0.1845 0.2312 0.0142  0.0127  0.0460  89  TYR   C CD1 
1751 C CD2 . TYR   B 83  ? 0.1608 0.1786 0.2376 0.0114  0.0125  0.0400  89  TYR   C CD2 
1752 C CE1 . TYR   B 83  ? 0.1706 0.1853 0.2283 0.0136  0.0114  0.0422  89  TYR   C CE1 
1753 C CE2 . TYR   B 83  ? 0.1622 0.1791 0.2340 0.0109  0.0109  0.0363  89  TYR   C CE2 
1754 C CZ  . TYR   B 83  ? 0.1616 0.1772 0.2245 0.0119  0.0105  0.0375  89  TYR   C CZ  
1755 O OH  . TYR   B 83  ? 0.1776 0.1923 0.2363 0.0117  0.0094  0.0343  89  TYR   C OH  
1756 N N   . TYR   B 84  ? 0.1547 0.1724 0.2600 0.0134  0.0242  0.0463  90  TYR   C N   
1757 C CA  . TYR   B 84  ? 0.1497 0.1675 0.2675 0.0120  0.0254  0.0425  90  TYR   C CA  
1758 C C   . TYR   B 84  ? 0.1534 0.1708 0.2806 0.0127  0.0298  0.0442  90  TYR   C C   
1759 O O   . TYR   B 84  ? 0.1582 0.1753 0.2808 0.0139  0.0312  0.0462  90  TYR   C O   
1760 C CB  . TYR   B 84  ? 0.1384 0.1564 0.2544 0.0103  0.0215  0.0355  90  TYR   C CB  
1761 C CG  . TYR   B 84  ? 0.1342 0.1523 0.2442 0.0095  0.0180  0.0330  90  TYR   C CG  
1762 C CD1 . TYR   B 84  ? 0.1417 0.1595 0.2570 0.0092  0.0188  0.0331  90  TYR   C CD1 
1763 C CD2 . TYR   B 84  ? 0.1423 0.1605 0.2418 0.0091  0.0146  0.0310  90  TYR   C CD2 
1764 C CE1 . TYR   B 84  ? 0.1483 0.1662 0.2588 0.0088  0.0164  0.0311  90  TYR   C CE1 
1765 C CE2 . TYR   B 84  ? 0.1419 0.1601 0.2367 0.0085  0.0121  0.0292  90  TYR   C CE2 
1766 C CZ  . TYR   B 84  ? 0.1407 0.1587 0.2411 0.0084  0.0132  0.0292  90  TYR   C CZ  
1767 O OH  . TYR   B 84  ? 0.1388 0.1567 0.2352 0.0081  0.0115  0.0278  90  TYR   C OH  
1768 N N   . PRO   B 85  ? 0.1559 0.1730 0.2971 0.0119  0.0324  0.0432  91  PRO   C N   
1769 C CA  . PRO   B 85  ? 0.1481 0.1650 0.3008 0.0119  0.0364  0.0439  91  PRO   C CA  
1770 C C   . PRO   B 85  ? 0.1446 0.1627 0.2983 0.0105  0.0330  0.0377  91  PRO   C C   
1771 O O   . PRO   B 85  ? 0.1478 0.1663 0.2936 0.0095  0.0280  0.0329  91  PRO   C O   
1772 C CB  . PRO   B 85  ? 0.1590 0.1750 0.3263 0.0110  0.0388  0.0432  91  PRO   C CB  
1773 C CG  . PRO   B 85  ? 0.1590 0.1749 0.3224 0.0096  0.0342  0.0380  91  PRO   C CG  
1774 C CD  . PRO   B 85  ? 0.1685 0.1851 0.3160 0.0106  0.0314  0.0402  91  PRO   C CD  
1775 N N   . ALA   B 86  ? 0.1435 0.1622 0.3080 0.0104  0.0359  0.0379  92  ALA   C N   
1776 C CA  . ALA   B 86  ? 0.1677 0.1879 0.3364 0.0090  0.0327  0.0322  92  ALA   C CA  
1777 C C   . ALA   B 86  ? 0.1752 0.1953 0.3502 0.0069  0.0285  0.0254  92  ALA   C C   
1778 O O   . ALA   B 86  ? 0.1869 0.2057 0.3719 0.0062  0.0306  0.0255  92  ALA   C O   
1779 C CB  . ALA   B 86  ? 0.1679 0.1889 0.3506 0.0093  0.0374  0.0345  92  ALA   C CB  
1780 N N   . ARG   B 87  ? 0.1595 0.1802 0.3270 0.0062  0.0228  0.0197  93  ARG   C N   
1781 C CA  . ARG   B 87  ? 0.1632 0.1829 0.3330 0.0049  0.0188  0.0132  93  ARG   C CA  
1782 C C   . ARG   B 87  ? 0.1604 0.1811 0.3224 0.0048  0.0130  0.0076  93  ARG   C C   
1783 O O   . ARG   B 87  ? 0.1532 0.1750 0.3066 0.0057  0.0123  0.0093  93  ARG   C O   
1784 C CB  . ARG   B 87  ? 0.1687 0.1865 0.3303 0.0052  0.0190  0.0145  93  ARG   C CB  
1785 C CG  . ARG   B 87  ? 0.1558 0.1739 0.3004 0.0062  0.0166  0.0157  93  ARG   C CG  
1786 C CD  . ARG   B 87  ? 0.1610 0.1779 0.2999 0.0066  0.0173  0.0180  93  ARG   C CD  
1787 N NE  . ARG   B 87  ? 0.1571 0.1741 0.2818 0.0070  0.0142  0.0174  93  ARG   C NE  
1788 C CZ  . ARG   B 87  ? 0.1709 0.1870 0.2896 0.0070  0.0126  0.0158  93  ARG   C CZ  
1789 N NH1 . ARG   B 87  ? 0.1911 0.2057 0.3155 0.0068  0.0138  0.0145  93  ARG   C NH1 
1790 N NH2 . ARG   B 87  ? 0.1793 0.1955 0.2866 0.0072  0.0100  0.0153  93  ARG   C NH2 
1791 N N   . TYR   B 88  ? 0.1745 0.1942 0.3380 0.0040  0.0088  0.0010  94  TYR   C N   
1792 C CA  . TYR   B 88  ? 0.1899 0.2098 0.3436 0.0044  0.0033  -0.0039 94  TYR   C CA  
1793 C C   . TYR   B 88  ? 0.1660 0.1840 0.3039 0.0054  0.0027  -0.0029 94  TYR   C C   
1794 O O   . TYR   B 88  ? 0.1934 0.2095 0.3311 0.0053  0.0045  -0.0022 94  TYR   C O   
1795 C CB  . TYR   B 88  ? 0.2200 0.2388 0.3799 0.0037  -0.0012 -0.0116 94  TYR   C CB  
1796 C CG  . TYR   B 88  ? 0.2482 0.2694 0.4232 0.0027  -0.0025 -0.0139 94  TYR   C CG  
1797 C CD1 . TYR   B 88  ? 0.2647 0.2886 0.4383 0.0033  -0.0061 -0.0156 94  TYR   C CD1 
1798 C CD2 . TYR   B 88  ? 0.2606 0.2817 0.4528 0.0012  0.0005  -0.0136 94  TYR   C CD2 
1799 C CE1 . TYR   B 88  ? 0.2778 0.3046 0.4672 0.0024  -0.0072 -0.0173 94  TYR   C CE1 
1800 C CE2 . TYR   B 88  ? 0.2666 0.2903 0.4747 0.0001  -0.0002 -0.0151 94  TYR   C CE2 
1801 C CZ  . TYR   B 88  ? 0.2787 0.3054 0.4857 0.0007  -0.0043 -0.0171 94  TYR   C CZ  
1802 O OH  . TYR   B 88  ? 0.3057 0.3354 0.5308 -0.0005 -0.0049 -0.0185 94  TYR   C OH  
1803 N N   . GLN   B 89  ? 0.1448 0.1634 0.2710 0.0063  0.0007  -0.0024 95  GLN   C N   
1804 C CA  . GLN   B 89  ? 0.1387 0.1557 0.2512 0.0071  -0.0001 -0.0017 95  GLN   C CA  
1805 C C   . GLN   B 89  ? 0.1364 0.1526 0.2416 0.0080  -0.0048 -0.0071 95  GLN   C C   
1806 O O   . GLN   B 89  ? 0.1471 0.1649 0.2532 0.0083  -0.0074 -0.0089 95  GLN   C O   
1807 C CB  . GLN   B 89  ? 0.1511 0.1689 0.2562 0.0075  0.0019  0.0040  95  GLN   C CB  
1808 C CG  . GLN   B 89  ? 0.1686 0.1851 0.2615 0.0079  0.0011  0.0049  95  GLN   C CG  
1809 C CD  . GLN   B 89  ? 0.1399 0.1567 0.2275 0.0080  0.0031  0.0105  95  GLN   C CD  
1810 O OE1 . GLN   B 89  ? 0.1620 0.1795 0.2544 0.0079  0.0060  0.0145  95  GLN   C OE1 
1811 N NE2 . GLN   B 89  ? 0.1426 0.1586 0.2197 0.0083  0.0015  0.0108  95  GLN   C NE2 
1812 N N   . SER   B 90  ? 0.1317 0.1455 0.2298 0.0087  -0.0058 -0.0094 96  SER   C N   
1813 C CA  . SER   B 90  ? 0.1452 0.1574 0.2346 0.0101  -0.0099 -0.0142 96  SER   C CA  
1814 C C   . SER   B 90  ? 0.1323 0.1440 0.2086 0.0113  -0.0100 -0.0117 96  SER   C C   
1815 O O   . SER   B 90  ? 0.1349 0.1468 0.2083 0.0107  -0.0071 -0.0069 96  SER   C O   
1816 C CB  . SER   B 90  ? 0.1640 0.1729 0.2525 0.0108  -0.0106 -0.0187 96  SER   C CB  
1817 O OG  . SER   B 90  ? 0.1719 0.1792 0.2552 0.0111  -0.0071 -0.0154 96  SER   C OG  
1818 N N   . HIS   B 91  ? 0.1394 0.1502 0.2081 0.0129  -0.0136 -0.0151 97  HIS   C N   
1819 C CA  . HIS   B 91  ? 0.1413 0.1509 0.1976 0.0143  -0.0138 -0.0133 97  HIS   C CA  
1820 C C   . HIS   B 91  ? 0.1338 0.1453 0.1900 0.0133  -0.0121 -0.0084 97  HIS   C C   
1821 O O   . HIS   B 91  ? 0.1409 0.1513 0.1898 0.0134  -0.0104 -0.0052 97  HIS   C O   
1822 C CB  . HIS   B 91  ? 0.1520 0.1586 0.2011 0.0150  -0.0114 -0.0122 97  HIS   C CB  
1823 C CG  . HIS   B 91  ? 0.1706 0.1742 0.2172 0.0167  -0.0128 -0.0173 97  HIS   C CG  
1824 N ND1 . HIS   B 91  ? 0.2089 0.2097 0.2443 0.0194  -0.0148 -0.0199 97  HIS   C ND1 
1825 C CD2 . HIS   B 91  ? 0.1811 0.1836 0.2345 0.0162  -0.0122 -0.0201 97  HIS   C CD2 
1826 C CE1 . HIS   B 91  ? 0.2236 0.2216 0.2583 0.0207  -0.0156 -0.0244 97  HIS   C CE1 
1827 N NE2 . HIS   B 91  ? 0.2163 0.2152 0.2621 0.0186  -0.0142 -0.0249 97  HIS   C NE2 
1828 N N   . LEU   B 92  ? 0.1245 0.1386 0.1888 0.0126  -0.0124 -0.0080 98  LEU   C N   
1829 C CA  . LEU   B 92  ? 0.1180 0.1333 0.1820 0.0120  -0.0103 -0.0036 98  LEU   C CA  
1830 C C   . LEU   B 92  ? 0.1205 0.1366 0.1818 0.0133  -0.0127 -0.0047 98  LEU   C C   
1831 O O   . LEU   B 92  ? 0.1319 0.1493 0.1977 0.0141  -0.0157 -0.0084 98  LEU   C O   
1832 C CB  . LEU   B 92  ? 0.1392 0.1565 0.2149 0.0107  -0.0077 -0.0016 98  LEU   C CB  
1833 C CG  . LEU   B 92  ? 0.1548 0.1727 0.2292 0.0105  -0.0049 0.0032  98  LEU   C CG  
1834 C CD1 . LEU   B 92  ? 0.1598 0.1761 0.2265 0.0101  -0.0033 0.0067  98  LEU   C CD1 
1835 C CD2 . LEU   B 92  ? 0.1677 0.1873 0.2539 0.0099  -0.0019 0.0053  98  LEU   C CD2 
1836 N N   . MET   B 93  ? 0.1151 0.1304 0.1693 0.0136  -0.0115 -0.0016 99  MET   C N   
1837 C CA  . MET   B 93  ? 0.1085 0.1241 0.1597 0.0150  -0.0130 -0.0019 99  MET   C CA  
1838 C C   . MET   B 93  ? 0.1218 0.1380 0.1754 0.0146  -0.0100 0.0017  99  MET   C C   
1839 O O   . MET   B 93  ? 0.1419 0.1568 0.1921 0.0136  -0.0075 0.0048  99  MET   C O   
1840 C CB  . MET   B 93  ? 0.1366 0.1493 0.1755 0.0161  -0.0137 -0.0015 99  MET   C CB  
1841 C CG  . MET   B 93  ? 0.1537 0.1650 0.1884 0.0172  -0.0159 -0.0045 99  MET   C CG  
1842 S SD  . MET   B 93  ? 0.1810 0.1885 0.2027 0.0185  -0.0153 -0.0030 99  MET   C SD  
1843 C CE  . MET   B 93  ? 0.1901 0.1968 0.2121 0.0159  -0.0116 0.0011  99  MET   C CE  
1844 N N   . LEU   B 94  ? 0.1165 0.1344 0.1752 0.0155  -0.0101 0.0015  100 LEU   C N   
1845 C CA  . LEU   B 94  ? 0.1215 0.1395 0.1818 0.0156  -0.0066 0.0050  100 LEU   C CA  
1846 C C   . LEU   B 94  ? 0.1169 0.1333 0.1699 0.0172  -0.0067 0.0057  100 LEU   C C   
1847 O O   . LEU   B 94  ? 0.1315 0.1484 0.1832 0.0185  -0.0097 0.0034  100 LEU   C O   
1848 C CB  . LEU   B 94  ? 0.1276 0.1488 0.2017 0.0156  -0.0051 0.0051  100 LEU   C CB  
1849 C CG  . LEU   B 94  ? 0.1534 0.1761 0.2376 0.0141  -0.0041 0.0048  100 LEU   C CG  
1850 C CD1 . LEU   B 94  ? 0.1931 0.2189 0.2920 0.0142  -0.0024 0.0052  100 LEU   C CD1 
1851 C CD2 . LEU   B 94  ? 0.1679 0.1887 0.2479 0.0132  -0.0007 0.0085  100 LEU   C CD2 
1852 N N   . ALA   B 95  ? 0.1228 0.1371 0.1712 0.0173  -0.0035 0.0089  101 ALA   C N   
1853 C CA  . ALA   B 95  ? 0.1254 0.1376 0.1681 0.0189  -0.0026 0.0098  101 ALA   C CA  
1854 C C   . ALA   B 95  ? 0.1227 0.1344 0.1678 0.0197  0.0020  0.0130  101 ALA   C C   
1855 O O   . ALA   B 95  ? 0.1246 0.1366 0.1725 0.0188  0.0043  0.0149  101 ALA   C O   
1856 C CB  . ALA   B 95  ? 0.1399 0.1479 0.1700 0.0186  -0.0033 0.0102  101 ALA   C CB  
1857 N N   . VAL   B 96  ? 0.1301 0.1405 0.1735 0.0216  0.0036  0.0137  102 VAL   C N   
1858 C CA  . VAL   B 96  ? 0.1464 0.1551 0.1892 0.0229  0.0085  0.0168  102 VAL   C CA  
1859 C C   . VAL   B 96  ? 0.1560 0.1595 0.1849 0.0226  0.0091  0.0179  102 VAL   C C   
1860 O O   . VAL   B 96  ? 0.1723 0.1727 0.1927 0.0228  0.0072  0.0166  102 VAL   C O   
1861 C CB  . VAL   B 96  ? 0.1565 0.1659 0.2037 0.0253  0.0102  0.0169  102 VAL   C CB  
1862 C CG1 . VAL   B 96  ? 0.1865 0.1931 0.2314 0.0271  0.0160  0.0203  102 VAL   C CG1 
1863 C CG2 . VAL   B 96  ? 0.1588 0.1739 0.2213 0.0252  0.0086  0.0155  102 VAL   C CG2 
1864 N N   . GLY   B 97  ? 0.1699 0.1723 0.1967 0.0222  0.0112  0.0202  103 GLY   C N   
1865 C CA  . GLY   B 97  ? 0.1811 0.1788 0.1952 0.0218  0.0108  0.0209  103 GLY   C CA  
1866 C C   . GLY   B 97  ? 0.1767 0.1743 0.1899 0.0214  0.0123  0.0235  103 GLY   C C   
1867 O O   . GLY   B 97  ? 0.2033 0.2042 0.2261 0.0213  0.0141  0.0249  103 GLY   C O   
1868 N N   . HIS   B 98  ? 0.1890 0.1825 0.1909 0.0215  0.0115  0.0241  104 HIS   C N   
1869 C CA  . HIS   B 98  ? 0.1856 0.1784 0.1846 0.0216  0.0125  0.0269  104 HIS   C CA  
1870 C C   . HIS   B 98  ? 0.1709 0.1662 0.1724 0.0191  0.0089  0.0266  104 HIS   C C   
1871 O O   . HIS   B 98  ? 0.1689 0.1637 0.1673 0.0172  0.0050  0.0244  104 HIS   C O   
1872 C CB  . HIS   B 98  ? 0.2144 0.2014 0.1994 0.0232  0.0127  0.0274  104 HIS   C CB  
1873 C CG  . HIS   B 98  ? 0.2374 0.2235 0.2183 0.0242  0.0139  0.0306  104 HIS   C CG  
1874 N ND1 . HIS   B 98  ? 0.2726 0.2594 0.2579 0.0266  0.0192  0.0342  104 HIS   C ND1 
1875 C CD2 . HIS   B 98  ? 0.2551 0.2399 0.2291 0.0233  0.0103  0.0310  104 HIS   C CD2 
1876 C CE1 . HIS   B 98  ? 0.2952 0.2809 0.2748 0.0273  0.0188  0.0368  104 HIS   C CE1 
1877 N NE2 . HIS   B 98  ? 0.2963 0.2809 0.2690 0.0253  0.0131  0.0348  104 HIS   C NE2 
1878 N N   . SER   B 99  ? 0.1753 0.1729 0.1823 0.0191  0.0105  0.0293  105 SER   C N   
1879 C CA  . SER   B 99  ? 0.1766 0.1766 0.1867 0.0171  0.0077  0.0295  105 SER   C CA  
1880 C C   . SER   B 99  ? 0.1917 0.1922 0.2036 0.0183  0.0103  0.0336  105 SER   C C   
1881 O O   . SER   B 99  ? 0.2174 0.2195 0.2373 0.0194  0.0144  0.0355  105 SER   C O   
1882 C CB  . SER   B 99  ? 0.1900 0.1938 0.2110 0.0155  0.0070  0.0273  105 SER   C CB  
1883 O OG  . SER   B 99  ? 0.1877 0.1936 0.2125 0.0139  0.0053  0.0278  105 SER   C OG  
1884 N N   . GLU   B 100 ? 0.1984 0.1976 0.2033 0.0182  0.0081  0.0351  106 GLU   C N   
1885 C CA  . GLU   B 100 ? 0.2062 0.2059 0.2117 0.0195  0.0097  0.0393  106 GLU   C CA  
1886 C C   . GLU   B 100 ? 0.1827 0.1857 0.1945 0.0173  0.0067  0.0393  106 GLU   C C   
1887 O O   . GLU   B 100 ? 0.1758 0.1798 0.1886 0.0150  0.0033  0.0362  106 GLU   C O   
1888 C CB  . GLU   B 100 ? 0.2549 0.2504 0.2463 0.0214  0.0081  0.0408  106 GLU   C CB  
1889 C CG  . GLU   B 100 ? 0.3646 0.3560 0.3486 0.0242  0.0118  0.0412  106 GLU   C CG  
1890 C CD  . GLU   B 100 ? 0.4040 0.3904 0.3723 0.0262  0.0098  0.0416  106 GLU   C CD  
1891 O OE1 . GLU   B 100 ? 0.4853 0.4717 0.4490 0.0260  0.0059  0.0428  106 GLU   C OE1 
1892 O OE2 . GLU   B 100 ? 0.4321 0.4143 0.3928 0.0283  0.0123  0.0408  106 GLU   C OE2 
1893 N N   . PRO   B 101 ? 0.1877 0.1923 0.2039 0.0181  0.0082  0.0430  107 PRO   C N   
1894 C CA  . PRO   B 101 ? 0.1808 0.1885 0.2037 0.0162  0.0058  0.0430  107 PRO   C CA  
1895 C C   . PRO   B 101 ? 0.1833 0.1908 0.2003 0.0145  0.0003  0.0413  107 PRO   C C   
1896 O O   . PRO   B 101 ? 0.1841 0.1938 0.2072 0.0124  -0.0013 0.0394  107 PRO   C O   
1897 C CB  . PRO   B 101 ? 0.2115 0.2198 0.2370 0.0182  0.0083  0.0482  107 PRO   C CB  
1898 C CG  . PRO   B 101 ? 0.2531 0.2597 0.2792 0.0204  0.0135  0.0500  107 PRO   C CG  
1899 C CD  . PRO   B 101 ? 0.2131 0.2167 0.2301 0.0210  0.0132  0.0475  107 PRO   C CD  
1900 N N   . GLY   B 102 ? 0.1825 0.1871 0.1882 0.0155  -0.0023 0.0418  108 GLY   C N   
1901 C CA  . GLY   B 102 ? 0.1831 0.1876 0.1849 0.0136  -0.0078 0.0402  108 GLY   C CA  
1902 C C   . GLY   B 102 ? 0.1785 0.1823 0.1805 0.0114  -0.0092 0.0359  108 GLY   C C   
1903 O O   . GLY   B 102 ? 0.1923 0.1962 0.1935 0.0095  -0.0132 0.0345  108 GLY   C O   
1904 N N   . ASP   B 103 ? 0.1575 0.1603 0.1604 0.0118  -0.0062 0.0340  109 ASP   C N   
1905 C CA  . ASP   B 103 ? 0.1476 0.1495 0.1503 0.0103  -0.0072 0.0304  109 ASP   C CA  
1906 C C   . ASP   B 103 ? 0.1423 0.1474 0.1541 0.0087  -0.0071 0.0292  109 ASP   C C   
1907 O O   . ASP   B 103 ? 0.1404 0.1450 0.1521 0.0075  -0.0081 0.0267  109 ASP   C O   
1908 C CB  . ASP   B 103 ? 0.1540 0.1539 0.1544 0.0118  -0.0042 0.0290  109 ASP   C CB  
1909 C CG  . ASP   B 103 ? 0.1921 0.1877 0.1817 0.0135  -0.0042 0.0294  109 ASP   C CG  
1910 O OD1 . ASP   B 103 ? 0.2047 0.1980 0.1874 0.0127  -0.0079 0.0286  109 ASP   C OD1 
1911 O OD2 . ASP   B 103 ? 0.2012 0.1956 0.1895 0.0158  -0.0005 0.0304  109 ASP   C OD2 
1912 N N   . CYS   B 104 ? 0.1249 0.1330 0.1449 0.0088  -0.0053 0.0311  110 CYS   C N   
1913 C CA  . CYS   B 104 ? 0.1297 0.1401 0.1574 0.0076  -0.0050 0.0297  110 CYS   C CA  
1914 C C   . CYS   B 104 ? 0.1340 0.1445 0.1607 0.0059  -0.0078 0.0291  110 CYS   C C   
1915 O O   . CYS   B 104 ? 0.1539 0.1646 0.1786 0.0054  -0.0103 0.0309  110 CYS   C O   
1916 C CB  . CYS   B 104 ? 0.1364 0.1494 0.1725 0.0080  -0.0029 0.0321  110 CYS   C CB  
1917 S SG  . CYS   B 104 ? 0.1581 0.1713 0.1997 0.0095  0.0012  0.0322  110 CYS   C SG  
1918 N N   . GLY   B 105 ? 0.1136 0.1239 0.1419 0.0053  -0.0075 0.0267  111 GLY   C N   
1919 C CA  . GLY   B 105 ? 0.1311 0.1413 0.1597 0.0039  -0.0090 0.0263  111 GLY   C CA  
1920 C C   . GLY   B 105 ? 0.1338 0.1410 0.1558 0.0034  -0.0105 0.0245  111 GLY   C C   
1921 O O   . GLY   B 105 ? 0.1471 0.1537 0.1697 0.0024  -0.0110 0.0241  111 GLY   C O   
1922 N N   . GLY   B 106 ? 0.1308 0.1357 0.1466 0.0043  -0.0106 0.0236  112 GLY   C N   
1923 C CA  . GLY   B 106 ? 0.1471 0.1486 0.1566 0.0041  -0.0115 0.0217  112 GLY   C CA  
1924 C C   . GLY   B 106 ? 0.1312 0.1324 0.1420 0.0046  -0.0100 0.0199  112 GLY   C C   
1925 O O   . GLY   B 106 ? 0.1315 0.1344 0.1455 0.0057  -0.0084 0.0190  112 GLY   C O   
1926 N N   . ILE   B 107 ? 0.1238 0.1227 0.1319 0.0039  -0.0107 0.0191  113 ILE   C N   
1927 C CA  . ILE   B 107 ? 0.1281 0.1262 0.1361 0.0049  -0.0092 0.0179  113 ILE   C CA  
1928 C C   . ILE   B 107 ? 0.1257 0.1219 0.1290 0.0066  -0.0088 0.0161  113 ILE   C C   
1929 O O   . ILE   B 107 ? 0.1286 0.1223 0.1275 0.0067  -0.0094 0.0159  113 ILE   C O   
1930 C CB  . ILE   B 107 ? 0.1568 0.1529 0.1646 0.0036  -0.0093 0.0186  113 ILE   C CB  
1931 C CG1 . ILE   B 107 ? 0.2001 0.1992 0.2150 0.0028  -0.0085 0.0203  113 ILE   C CG1 
1932 C CG2 . ILE   B 107 ? 0.1653 0.1588 0.1695 0.0052  -0.0078 0.0176  113 ILE   C CG2 
1933 C CD1 . ILE   B 107 ? 0.2566 0.2547 0.2746 0.0012  -0.0083 0.0219  113 ILE   C CD1 
1934 N N   . LEU   B 108 ? 0.1102 0.1075 0.1147 0.0083  -0.0078 0.0148  114 LEU   C N   
1935 C CA  . LEU   B 108 ? 0.1151 0.1110 0.1161 0.0102  -0.0078 0.0132  114 LEU   C CA  
1936 C C   . LEU   B 108 ? 0.1192 0.1129 0.1171 0.0110  -0.0072 0.0131  114 LEU   C C   
1937 O O   . LEU   B 108 ? 0.1204 0.1150 0.1201 0.0113  -0.0065 0.0132  114 LEU   C O   
1938 C CB  . LEU   B 108 ? 0.1174 0.1163 0.1225 0.0116  -0.0078 0.0117  114 LEU   C CB  
1939 C CG  . LEU   B 108 ? 0.1281 0.1265 0.1311 0.0139  -0.0085 0.0098  114 LEU   C CG  
1940 C CD1 . LEU   B 108 ? 0.1509 0.1478 0.1513 0.0145  -0.0083 0.0102  114 LEU   C CD1 
1941 C CD2 . LEU   B 108 ? 0.1477 0.1493 0.1564 0.0148  -0.0092 0.0078  114 LEU   C CD2 
1942 N N   . ARG   B 109 ? 0.1227 0.1132 0.1159 0.0117  -0.0072 0.0132  115 ARG   C N   
1943 C CA  . ARG   B 109 ? 0.1337 0.1214 0.1235 0.0128  -0.0060 0.0138  115 ARG   C CA  
1944 C C   . ARG   B 109 ? 0.1396 0.1254 0.1248 0.0155  -0.0062 0.0129  115 ARG   C C   
1945 O O   . ARG   B 109 ? 0.1521 0.1375 0.1364 0.0159  -0.0069 0.0123  115 ARG   C O   
1946 C CB  . ARG   B 109 ? 0.1750 0.1599 0.1648 0.0106  -0.0055 0.0155  115 ARG   C CB  
1947 C CG  . ARG   B 109 ? 0.2202 0.2022 0.2071 0.0100  -0.0064 0.0151  115 ARG   C CG  
1948 C CD  . ARG   B 109 ? 0.2838 0.2628 0.2715 0.0075  -0.0066 0.0161  115 ARG   C CD  
1949 N NE  . ARG   B 109 ? 0.3285 0.3100 0.3204 0.0050  -0.0083 0.0165  115 ARG   C NE  
1950 C CZ  . ARG   B 109 ? 0.4221 0.4043 0.4190 0.0030  -0.0084 0.0179  115 ARG   C CZ  
1951 N NH1 . ARG   B 109 ? 0.4528 0.4331 0.4513 0.0030  -0.0063 0.0192  115 ARG   C NH1 
1952 N NH2 . ARG   B 109 ? 0.4494 0.4343 0.4502 0.0010  -0.0104 0.0183  115 ARG   C NH2 
1953 N N   . CYS   B 110 ? 0.1440 0.1286 0.1260 0.0177  -0.0053 0.0131  116 CYS   C N   
1954 C CA  . CYS   B 110 ? 0.1570 0.1394 0.1339 0.0208  -0.0056 0.0128  116 CYS   C CA  
1955 C C   . CYS   B 110 ? 0.1754 0.1535 0.1485 0.0215  -0.0031 0.0151  116 CYS   C C   
1956 O O   . CYS   B 110 ? 0.1789 0.1558 0.1544 0.0192  -0.0014 0.0167  116 CYS   C O   
1957 C CB  . CYS   B 110 ? 0.1566 0.1415 0.1325 0.0236  -0.0073 0.0108  116 CYS   C CB  
1958 S SG  . CYS   B 110 ? 0.1634 0.1475 0.1366 0.0250  -0.0057 0.0111  116 CYS   C SG  
1959 N N   . GLN   B 111 ? 0.1866 0.1620 0.1542 0.0248  -0.0027 0.0157  117 GLN   C N   
1960 C CA  . GLN   B 111 ? 0.2117 0.1825 0.1758 0.0258  0.0003  0.0184  117 GLN   C CA  
1961 C C   . GLN   B 111 ? 0.2226 0.1932 0.1863 0.0263  0.0027  0.0197  117 GLN   C C   
1962 O O   . GLN   B 111 ? 0.2435 0.2105 0.2069 0.0261  0.0061  0.0225  117 GLN   C O   
1963 C CB  . GLN   B 111 ? 0.2285 0.1966 0.1863 0.0300  0.0005  0.0192  117 GLN   C CB  
1964 C CG  . GLN   B 111 ? 0.2588 0.2290 0.2121 0.0338  -0.0014 0.0178  117 GLN   C CG  
1965 C CD  . GLN   B 111 ? 0.4071 0.3750 0.3542 0.0383  -0.0020 0.0187  117 GLN   C CD  
1966 O OE1 . GLN   B 111 ? 0.4542 0.4244 0.4021 0.0396  -0.0050 0.0171  117 GLN   C OE1 
1967 N NE2 . GLN   B 111 ? 0.4215 0.3851 0.3627 0.0409  0.0011  0.0216  117 GLN   C NE2 
1968 N N   . HIS   B 112 ? 0.1886 0.1626 0.1527 0.0269  0.0014  0.0178  118 HIS   C N   
1969 C CA  . HIS   B 112 ? 0.1999 0.1731 0.1628 0.0279  0.0041  0.0189  118 HIS   C CA  
1970 C C   . HIS   B 112 ? 0.1928 0.1680 0.1633 0.0242  0.0053  0.0196  118 HIS   C C   
1971 O O   . HIS   B 112 ? 0.2124 0.1869 0.1831 0.0249  0.0083  0.0210  118 HIS   C O   
1972 C CB  . HIS   B 112 ? 0.2007 0.1754 0.1588 0.0313  0.0021  0.0162  118 HIS   C CB  
1973 C CG  . HIS   B 112 ? 0.1891 0.1624 0.1400 0.0352  -0.0001 0.0154  118 HIS   C CG  
1974 N ND1 . HIS   B 112 ? 0.1861 0.1626 0.1387 0.0355  -0.0045 0.0125  118 HIS   C ND1 
1975 C CD2 . HIS   B 112 ? 0.2358 0.2050 0.1783 0.0394  0.0017  0.0174  118 HIS   C CD2 
1976 C CE1 . HIS   B 112 ? 0.2059 0.1805 0.1516 0.0396  -0.0057 0.0128  118 HIS   C CE1 
1977 N NE2 . HIS   B 112 ? 0.2527 0.2228 0.1916 0.0422  -0.0021 0.0157  118 HIS   C NE2 
1978 N N   . GLY   B 113 ? 0.1788 0.1567 0.1552 0.0207  0.0030  0.0186  119 GLY   C N   
1979 C CA  . GLY   B 113 ? 0.1791 0.1594 0.1630 0.0174  0.0034  0.0193  119 GLY   C CA  
1980 C C   . GLY   B 113 ? 0.1592 0.1436 0.1469 0.0158  0.0004  0.0171  119 GLY   C C   
1981 O O   . GLY   B 113 ? 0.1550 0.1403 0.1413 0.0162  -0.0019 0.0154  119 GLY   C O   
1982 N N   . VAL   B 114 ? 0.1514 0.1384 0.1448 0.0140  0.0009  0.0176  120 VAL   C N   
1983 C CA  . VAL   B 114 ? 0.1441 0.1348 0.1421 0.0125  -0.0013 0.0162  120 VAL   C CA  
1984 C C   . VAL   B 114 ? 0.1476 0.1398 0.1443 0.0147  -0.0021 0.0136  120 VAL   C C   
1985 O O   . VAL   B 114 ? 0.1565 0.1481 0.1519 0.0164  -0.0006 0.0130  120 VAL   C O   
1986 C CB  . VAL   B 114 ? 0.1526 0.1455 0.1577 0.0101  -0.0005 0.0181  120 VAL   C CB  
1987 C CG1 . VAL   B 114 ? 0.1677 0.1642 0.1772 0.0091  -0.0022 0.0171  120 VAL   C CG1 
1988 C CG2 . VAL   B 114 ? 0.1675 0.1592 0.1750 0.0076  -0.0007 0.0203  120 VAL   C CG2 
1989 N N   . VAL   B 115 ? 0.1224 0.1163 0.1198 0.0146  -0.0044 0.0118  121 VAL   C N   
1990 C CA  . VAL   B 115 ? 0.1366 0.1323 0.1349 0.0163  -0.0059 0.0089  121 VAL   C CA  
1991 C C   . VAL   B 115 ? 0.1427 0.1415 0.1482 0.0147  -0.0059 0.0085  121 VAL   C C   
1992 O O   . VAL   B 115 ? 0.1420 0.1416 0.1492 0.0158  -0.0062 0.0062  121 VAL   C O   
1993 C CB  . VAL   B 115 ? 0.1383 0.1345 0.1355 0.0171  -0.0080 0.0077  121 VAL   C CB  
1994 C CG1 . VAL   B 115 ? 0.1562 0.1550 0.1569 0.0183  -0.0100 0.0047  121 VAL   C CG1 
1995 C CG2 . VAL   B 115 ? 0.1595 0.1526 0.1497 0.0191  -0.0079 0.0083  121 VAL   C CG2 
1996 N N   . GLY   B 116 ? 0.1315 0.1317 0.1410 0.0124  -0.0057 0.0105  122 GLY   C N   
1997 C CA  . GLY   B 116 ? 0.1454 0.1482 0.1617 0.0112  -0.0054 0.0107  122 GLY   C CA  
1998 C C   . GLY   B 116 ? 0.1231 0.1268 0.1413 0.0092  -0.0056 0.0133  122 GLY   C C   
1999 O O   . GLY   B 116 ? 0.1334 0.1354 0.1477 0.0085  -0.0061 0.0145  122 GLY   C O   
2000 N N   . ILE   B 117 ? 0.1135 0.1196 0.1376 0.0084  -0.0053 0.0141  123 ILE   C N   
2001 C CA  . ILE   B 117 ? 0.1151 0.1219 0.1399 0.0071  -0.0056 0.0167  123 ILE   C CA  
2002 C C   . ILE   B 117 ? 0.1115 0.1197 0.1394 0.0076  -0.0052 0.0168  123 ILE   C C   
2003 O O   . ILE   B 117 ? 0.1243 0.1339 0.1574 0.0083  -0.0044 0.0153  123 ILE   C O   
2004 C CB  . ILE   B 117 ? 0.1290 0.1372 0.1582 0.0059  -0.0052 0.0191  123 ILE   C CB  
2005 C CG1 . ILE   B 117 ? 0.1404 0.1503 0.1760 0.0064  -0.0036 0.0185  123 ILE   C CG1 
2006 C CG2 . ILE   B 117 ? 0.1428 0.1497 0.1699 0.0051  -0.0056 0.0200  123 ILE   C CG2 
2007 C CD1 . ILE   B 117 ? 0.1431 0.1550 0.1846 0.0055  -0.0029 0.0215  123 ILE   C CD1 
2008 N N   . VAL   B 118 ? 0.1093 0.1168 0.1343 0.0074  -0.0055 0.0185  124 VAL   C N   
2009 C CA  . VAL   B 118 ? 0.1115 0.1201 0.1394 0.0082  -0.0041 0.0195  124 VAL   C CA  
2010 C C   . VAL   B 118 ? 0.1168 0.1277 0.1524 0.0080  -0.0027 0.0209  124 VAL   C C   
2011 O O   . VAL   B 118 ? 0.1112 0.1227 0.1478 0.0071  -0.0031 0.0228  124 VAL   C O   
2012 C CB  . VAL   B 118 ? 0.1176 0.1243 0.1393 0.0084  -0.0043 0.0215  124 VAL   C CB  
2013 C CG1 . VAL   B 118 ? 0.1253 0.1326 0.1495 0.0097  -0.0020 0.0234  124 VAL   C CG1 
2014 C CG2 . VAL   B 118 ? 0.1364 0.1402 0.1509 0.0088  -0.0053 0.0199  124 VAL   C CG2 
2015 N N   . SER   B 119 ? 0.1098 0.1220 0.1516 0.0086  -0.0011 0.0202  125 SER   C N   
2016 C CA  . SER   B 119 ? 0.1125 0.1264 0.1627 0.0085  0.0007  0.0216  125 SER   C CA  
2017 C C   . SER   B 119 ? 0.1273 0.1419 0.1826 0.0094  0.0033  0.0234  125 SER   C C   
2018 O O   . SER   B 119 ? 0.1233 0.1387 0.1841 0.0095  0.0053  0.0260  125 SER   C O   
2019 C CB  . SER   B 119 ? 0.1309 0.1454 0.1861 0.0082  0.0004  0.0181  125 SER   C CB  
2020 O OG  . SER   B 119 ? 0.1386 0.1542 0.2028 0.0081  0.0023  0.0188  125 SER   C OG  
2021 N N   . THR   B 120 ? 0.1211 0.1353 0.1758 0.0102  0.0039  0.0222  126 THR   C N   
2022 C CA  . THR   B 120 ? 0.1189 0.1338 0.1800 0.0112  0.0071  0.0242  126 THR   C CA  
2023 C C   . THR   B 120 ? 0.1118 0.1250 0.1660 0.0126  0.0082  0.0256  126 THR   C C   
2024 O O   . THR   B 120 ? 0.1197 0.1314 0.1659 0.0126  0.0060  0.0239  126 THR   C O   
2025 C CB  . THR   B 120 ? 0.1220 0.1387 0.1943 0.0109  0.0075  0.0212  126 THR   C CB  
2026 O OG1 . THR   B 120 ? 0.1331 0.1499 0.2031 0.0113  0.0054  0.0181  126 THR   C OG1 
2027 C CG2 . THR   B 120 ? 0.1413 0.1588 0.2193 0.0098  0.0062  0.0188  126 THR   C CG2 
2028 N N   . GLY   B 121 ? 0.1286 0.1416 0.1861 0.0139  0.0120  0.0288  127 GLY   C N   
2029 C CA  . GLY   B 121 ? 0.1595 0.1705 0.2110 0.0158  0.0141  0.0303  127 GLY   C CA  
2030 C C   . GLY   B 121 ? 0.2021 0.2136 0.2614 0.0174  0.0193  0.0334  127 GLY   C C   
2031 O O   . GLY   B 121 ? 0.2468 0.2596 0.3146 0.0172  0.0214  0.0353  127 GLY   C O   
2032 N N   . GLY   B 122 ? 0.2466 0.2563 0.3019 0.0194  0.0219  0.0346  128 GLY   C N   
2033 C CA  . GLY   B 122 ? 0.2708 0.2807 0.3338 0.0213  0.0279  0.0381  128 GLY   C CA  
2034 C C   . GLY   B 122 ? 0.2624 0.2740 0.3339 0.0217  0.0290  0.0361  128 GLY   C C   
2035 O O   . GLY   B 122 ? 0.2522 0.2658 0.3267 0.0202  0.0248  0.0317  128 GLY   C O   
2036 N N   . ASN   B 123 ? 0.2477 0.2588 0.3240 0.0240  0.0350  0.0396  129 ASN   C N   
2037 C CA  . ASN   B 123 ? 0.2481 0.2611 0.3340 0.0248  0.0369  0.0386  129 ASN   C CA  
2038 C C   . ASN   B 123 ? 0.2263 0.2382 0.3029 0.0250  0.0331  0.0352  129 ASN   C C   
2039 O O   . ASN   B 123 ? 0.2627 0.2773 0.3479 0.0250  0.0321  0.0329  129 ASN   C O   
2040 C CB  . ASN   B 123 ? 0.3106 0.3286 0.4157 0.0226  0.0354  0.0361  129 ASN   C CB  
2041 C CG  . ASN   B 123 ? 0.3999 0.4197 0.5214 0.0234  0.0418  0.0397  129 ASN   C CG  
2042 O OD1 . ASN   B 123 ? 0.4227 0.4402 0.5424 0.0262  0.0484  0.0447  129 ASN   C OD1 
2043 N ND2 . ASN   B 123 ? 0.4305 0.4539 0.5685 0.0212  0.0402  0.0375  129 ASN   C ND2 
2044 N N   . GLY   B 124 ? 0.2078 0.2156 0.2677 0.0256  0.0314  0.0351  130 GLY   C N   
2045 C CA  . GLY   B 124 ? 0.2013 0.2073 0.2525 0.0258  0.0283  0.0321  130 GLY   C CA  
2046 C C   . GLY   B 124 ? 0.1755 0.1839 0.2284 0.0234  0.0219  0.0275  130 GLY   C C   
2047 O O   . GLY   B 124 ? 0.1790 0.1866 0.2278 0.0238  0.0197  0.0252  130 GLY   C O   
2048 N N   . LEU   B 125 ? 0.1564 0.1673 0.2148 0.0212  0.0194  0.0264  131 LEU   C N   
2049 C CA  . LEU   B 125 ? 0.1492 0.1619 0.2082 0.0193  0.0139  0.0224  131 LEU   C CA  
2050 C C   . LEU   B 125 ? 0.1552 0.1661 0.2056 0.0178  0.0115  0.0224  131 LEU   C C   
2051 O O   . LEU   B 125 ? 0.1872 0.1972 0.2360 0.0178  0.0136  0.0254  131 LEU   C O   
2052 C CB  . LEU   B 125 ? 0.1721 0.1892 0.2461 0.0182  0.0128  0.0204  131 LEU   C CB  
2053 C CG  . LEU   B 125 ? 0.1948 0.2146 0.2805 0.0194  0.0145  0.0202  131 LEU   C CG  
2054 C CD1 . LEU   B 125 ? 0.2474 0.2710 0.3501 0.0182  0.0152  0.0196  131 LEU   C CD1 
2055 C CD2 . LEU   B 125 ? 0.1975 0.2178 0.2803 0.0201  0.0108  0.0171  131 LEU   C CD2 
2056 N N   . VAL   B 126 ? 0.1198 0.1304 0.1653 0.0167  0.0074  0.0195  132 VAL   C N   
2057 C CA  . VAL   B 126 ? 0.1160 0.1257 0.1559 0.0151  0.0050  0.0193  132 VAL   C CA  
2058 C C   . VAL   B 126 ? 0.1139 0.1259 0.1594 0.0140  0.0021  0.0160  132 VAL   C C   
2059 O O   . VAL   B 126 ? 0.1163 0.1289 0.1626 0.0146  0.0001  0.0133  132 VAL   C O   
2060 C CB  . VAL   B 126 ? 0.1269 0.1329 0.1543 0.0151  0.0033  0.0191  132 VAL   C CB  
2061 C CG1 . VAL   B 126 ? 0.1548 0.1598 0.1792 0.0160  0.0020  0.0169  132 VAL   C CG1 
2062 C CG2 . VAL   B 126 ? 0.1447 0.1503 0.1686 0.0133  0.0008  0.0190  132 VAL   C CG2 
2063 N N   . GLY   B 127 ? 0.1139 0.1269 0.1625 0.0128  0.0018  0.0163  133 GLY   C N   
2064 C CA  . GLY   B 127 ? 0.1123 0.1266 0.1647 0.0120  -0.0007 0.0130  133 GLY   C CA  
2065 C C   . GLY   B 127 ? 0.1140 0.1268 0.1595 0.0111  -0.0022 0.0130  133 GLY   C C   
2066 O O   . GLY   B 127 ? 0.1195 0.1316 0.1624 0.0105  -0.0013 0.0158  133 GLY   C O   
2067 N N   . PHE   B 128 ? 0.1057 0.1180 0.1487 0.0113  -0.0045 0.0101  134 PHE   C N   
2068 C CA  . PHE   B 128 ? 0.1077 0.1185 0.1448 0.0108  -0.0054 0.0100  134 PHE   C CA  
2069 C C   . PHE   B 128 ? 0.1087 0.1200 0.1497 0.0109  -0.0059 0.0076  134 PHE   C C   
2070 O O   . PHE   B 128 ? 0.1202 0.1321 0.1636 0.0118  -0.0075 0.0043  134 PHE   C O   
2071 C CB  . PHE   B 128 ? 0.1171 0.1256 0.1459 0.0117  -0.0068 0.0091  134 PHE   C CB  
2072 C CG  . PHE   B 128 ? 0.1152 0.1225 0.1400 0.0121  -0.0064 0.0106  134 PHE   C CG  
2073 C CD1 . PHE   B 128 ? 0.1249 0.1303 0.1448 0.0111  -0.0059 0.0129  134 PHE   C CD1 
2074 C CD2 . PHE   B 128 ? 0.1255 0.1333 0.1517 0.0134  -0.0065 0.0095  134 PHE   C CD2 
2075 C CE1 . PHE   B 128 ? 0.1273 0.1306 0.1423 0.0117  -0.0054 0.0138  134 PHE   C CE1 
2076 C CE2 . PHE   B 128 ? 0.1345 0.1405 0.1565 0.0141  -0.0055 0.0108  134 PHE   C CE2 
2077 C CZ  . PHE   B 128 ? 0.1346 0.1380 0.1504 0.0133  -0.0049 0.0128  134 PHE   C CZ  
2078 N N   . ALA   B 129 ? 0.1141 0.1251 0.1552 0.0100  -0.0049 0.0091  135 ALA   C N   
2079 C CA  . ALA   B 129 ? 0.1137 0.1243 0.1569 0.0104  -0.0048 0.0069  135 ALA   C CA  
2080 C C   . ALA   B 129 ? 0.1301 0.1384 0.1650 0.0116  -0.0058 0.0054  135 ALA   C C   
2081 O O   . ALA   B 129 ? 0.1281 0.1353 0.1583 0.0111  -0.0051 0.0078  135 ALA   C O   
2082 C CB  . ALA   B 129 ? 0.1236 0.1347 0.1705 0.0093  -0.0029 0.0096  135 ALA   C CB  
2083 N N   . ASP   B 130 ? 0.1217 0.1292 0.1548 0.0132  -0.0075 0.0017  136 ASP   C N   
2084 C CA  . ASP   B 130 ? 0.1299 0.1348 0.1541 0.0150  -0.0081 0.0006  136 ASP   C CA  
2085 C C   . ASP   B 130 ? 0.1393 0.1425 0.1618 0.0152  -0.0057 0.0015  136 ASP   C C   
2086 O O   . ASP   B 130 ? 0.1434 0.1469 0.1712 0.0148  -0.0046 0.0007  136 ASP   C O   
2087 C CB  . ASP   B 130 ? 0.1513 0.1558 0.1741 0.0171  -0.0110 -0.0039 136 ASP   C CB  
2088 C CG  . ASP   B 130 ? 0.1958 0.1973 0.2083 0.0198  -0.0118 -0.0050 136 ASP   C CG  
2089 O OD1 . ASP   B 130 ? 0.1869 0.1875 0.1943 0.0201  -0.0113 -0.0026 136 ASP   C OD1 
2090 O OD2 . ASP   B 130 ? 0.2351 0.2348 0.2443 0.0217  -0.0126 -0.0081 136 ASP   C OD2 
2091 N N   . VAL   B 131 ? 0.1411 0.1419 0.1566 0.0162  -0.0046 0.0030  137 VAL   C N   
2092 C CA  . VAL   B 131 ? 0.1455 0.1442 0.1588 0.0170  -0.0017 0.0041  137 VAL   C CA  
2093 C C   . VAL   B 131 ? 0.1616 0.1567 0.1653 0.0201  -0.0013 0.0027  137 VAL   C C   
2094 O O   . VAL   B 131 ? 0.1646 0.1574 0.1654 0.0215  0.0018  0.0037  137 VAL   C O   
2095 C CB  . VAL   B 131 ? 0.1549 0.1543 0.1710 0.0150  0.0007  0.0085  137 VAL   C CB  
2096 C CG1 . VAL   B 131 ? 0.1532 0.1558 0.1779 0.0125  0.0003  0.0102  137 VAL   C CG1 
2097 C CG2 . VAL   B 131 ? 0.1572 0.1555 0.1689 0.0146  0.0001  0.0104  137 VAL   C CG2 
2098 N N   . ARG   B 132 ? 0.1572 0.1518 0.1558 0.0217  -0.0042 0.0006  138 ARG   C N   
2099 C CA  . ARG   B 132 ? 0.1595 0.1505 0.1476 0.0252  -0.0040 -0.0001 138 ARG   C CA  
2100 C C   . ARG   B 132 ? 0.1684 0.1567 0.1516 0.0282  -0.0039 -0.0034 138 ARG   C C   
2101 O O   . ARG   B 132 ? 0.1940 0.1786 0.1676 0.0314  -0.0023 -0.0030 138 ARG   C O   
2102 C CB  . ARG   B 132 ? 0.1470 0.1384 0.1317 0.0264  -0.0075 -0.0012 138 ARG   C CB  
2103 C CG  . ARG   B 132 ? 0.1560 0.1484 0.1430 0.0241  -0.0069 0.0022  138 ARG   C CG  
2104 C CD  . ARG   B 132 ? 0.1627 0.1556 0.1470 0.0256  -0.0100 0.0010  138 ARG   C CD  
2105 N NE  . ARG   B 132 ? 0.1535 0.1498 0.1445 0.0249  -0.0132 -0.0021 138 ARG   C NE  
2106 C CZ  . ARG   B 132 ? 0.1628 0.1607 0.1549 0.0257  -0.0161 -0.0033 138 ARG   C CZ  
2107 N NH1 . ARG   B 132 ? 0.1657 0.1617 0.1513 0.0278  -0.0166 -0.0022 138 ARG   C NH1 
2108 N NH2 . ARG   B 132 ? 0.1643 0.1656 0.1648 0.0246  -0.0182 -0.0054 138 ARG   C NH2 
2109 N N   . ASP   B 133 ? 0.1668 0.1566 0.1559 0.0273  -0.0054 -0.0067 139 ASP   C N   
2110 C CA  . ASP   B 133 ? 0.1753 0.1620 0.1596 0.0301  -0.0056 -0.0106 139 ASP   C CA  
2111 C C   . ASP   B 133 ? 0.1939 0.1784 0.1788 0.0302  -0.0002 -0.0085 139 ASP   C C   
2112 O O   . ASP   B 133 ? 0.2110 0.1919 0.1902 0.0331  0.0007  -0.0115 139 ASP   C O   
2113 C CB  . ASP   B 133 ? 0.1910 0.1797 0.1824 0.0290  -0.0096 -0.0155 139 ASP   C CB  
2114 C CG  . ASP   B 133 ? 0.2205 0.2124 0.2245 0.0254  -0.0078 -0.0140 139 ASP   C CG  
2115 O OD1 . ASP   B 133 ? 0.2075 0.2020 0.2160 0.0230  -0.0062 -0.0096 139 ASP   C OD1 
2116 O OD2 . ASP   B 133 ? 0.2590 0.2503 0.2679 0.0251  -0.0080 -0.0171 139 ASP   C OD2 
2117 N N   . LEU   B 134 ? 0.1823 0.1690 0.1742 0.0274  0.0030  -0.0037 140 LEU   C N   
2118 C CA  . LEU   B 134 ? 0.1752 0.1608 0.1704 0.0273  0.0080  -0.0013 140 LEU   C CA  
2119 C C   . LEU   B 134 ? 0.1917 0.1739 0.1792 0.0297  0.0121  0.0018  140 LEU   C C   
2120 O O   . LEU   B 134 ? 0.1860 0.1695 0.1772 0.0280  0.0145  0.0064  140 LEU   C O   
2121 C CB  . LEU   B 134 ? 0.1679 0.1580 0.1748 0.0233  0.0087  0.0023  140 LEU   C CB  
2122 C CG  . LEU   B 134 ? 0.1687 0.1621 0.1839 0.0210  0.0055  0.0001  140 LEU   C CG  
2123 C CD1 . LEU   B 134 ? 0.1821 0.1794 0.2068 0.0177  0.0062  0.0044  140 LEU   C CD1 
2124 C CD2 . LEU   B 134 ? 0.1988 0.1904 0.2160 0.0222  0.0059  -0.0039 140 LEU   C CD2 
2125 N N   . LEU   B 135 ? 0.2037 0.1812 0.1798 0.0340  0.0128  -0.0008 141 LEU   C N   
2126 C CA  . LEU   B 135 ? 0.2162 0.1898 0.1834 0.0371  0.0169  0.0024  141 LEU   C CA  
2127 C C   . LEU   B 135 ? 0.2181 0.1908 0.1900 0.0369  0.0236  0.0069  141 LEU   C C   
2128 O O   . LEU   B 135 ? 0.2302 0.2014 0.2002 0.0377  0.0275  0.0113  141 LEU   C O   
2129 C CB  . LEU   B 135 ? 0.2269 0.1951 0.1794 0.0424  0.0161  -0.0012 141 LEU   C CB  
2130 C CG  . LEU   B 135 ? 0.2354 0.2048 0.1840 0.0430  0.0088  -0.0061 141 LEU   C CG  
2131 C CD1 . LEU   B 135 ? 0.2606 0.2245 0.1936 0.0487  0.0073  -0.0099 141 LEU   C CD1 
2132 C CD2 . LEU   B 135 ? 0.2403 0.2131 0.1918 0.0408  0.0059  -0.0038 141 LEU   C CD2 
2133 N N   . TRP   B 136 ? 0.2083 0.1819 0.1871 0.0360  0.0252  0.0059  142 TRP   C N   
2134 C CA  . TRP   B 136 ? 0.2132 0.1864 0.1981 0.0359  0.0315  0.0101  142 TRP   C CA  
2135 C C   . TRP   B 136 ? 0.2172 0.1952 0.2135 0.0318  0.0321  0.0153  142 TRP   C C   
2136 O O   . TRP   B 136 ? 0.2412 0.2191 0.2429 0.0318  0.0373  0.0196  142 TRP   C O   
2137 C CB  . TRP   B 136 ? 0.2201 0.1934 0.2105 0.0359  0.0325  0.0075  142 TRP   C CB  
2138 C CG  . TRP   B 136 ? 0.2160 0.1940 0.2155 0.0321  0.0274  0.0053  142 TRP   C CG  
2139 C CD1 . TRP   B 136 ? 0.2273 0.2050 0.2246 0.0322  0.0226  -0.0002 142 TRP   C CD1 
2140 C CD2 . TRP   B 136 ? 0.2086 0.1920 0.2215 0.0280  0.0270  0.0088  142 TRP   C CD2 
2141 N NE1 . TRP   B 136 ? 0.2246 0.2071 0.2333 0.0284  0.0198  0.0001  142 TRP   C NE1 
2142 C CE2 . TRP   B 136 ? 0.2094 0.1954 0.2269 0.0260  0.0223  0.0056  142 TRP   C CE2 
2143 C CE3 . TRP   B 136 ? 0.2014 0.1877 0.2230 0.0260  0.0298  0.0143  142 TRP   C CE3 
2144 C CZ2 . TRP   B 136 ? 0.2119 0.2027 0.2409 0.0224  0.0210  0.0081  142 TRP   C CZ2 
2145 C CZ3 . TRP   B 136 ? 0.2072 0.1987 0.2402 0.0224  0.0276  0.0164  142 TRP   C CZ3 
2146 C CH2 . TRP   B 136 ? 0.2111 0.2046 0.2468 0.0208  0.0234  0.0135  142 TRP   C CH2 
2147 N N   . LEU   B 137 ? 0.2077 0.1895 0.2078 0.0284  0.0269  0.0151  143 LEU   C N   
2148 C CA  . LEU   B 137 ? 0.2077 0.1932 0.2169 0.0248  0.0268  0.0196  143 LEU   C CA  
2149 C C   . LEU   B 137 ? 0.2504 0.2331 0.2562 0.0260  0.0306  0.0233  143 LEU   C C   
2150 O O   . LEU   B 137 ? 0.2626 0.2475 0.2771 0.0235  0.0320  0.0273  143 LEU   C O   
2151 C CB  . LEU   B 137 ? 0.1923 0.1811 0.2035 0.0217  0.0209  0.0183  143 LEU   C CB  
2152 C CG  . LEU   B 137 ? 0.1799 0.1723 0.1979 0.0196  0.0178  0.0163  143 LEU   C CG  
2153 C CD1 . LEU   B 137 ? 0.1922 0.1866 0.2094 0.0177  0.0126  0.0147  143 LEU   C CD1 
2154 C CD2 . LEU   B 137 ? 0.1991 0.1950 0.2286 0.0172  0.0193  0.0198  143 LEU   C CD2 
2155 N N   . ASP   B 138 ? 0.2386 0.2164 0.2319 0.0301  0.0320  0.0220  144 ASP   C N   
2156 C CA  . ASP   B 138 ? 0.2621 0.2365 0.2509 0.0318  0.0360  0.0257  144 ASP   C CA  
2157 C C   . ASP   B 138 ? 0.2967 0.2681 0.2865 0.0345  0.0438  0.0293  144 ASP   C C   
2158 O O   . ASP   B 138 ? 0.3148 0.2830 0.3013 0.0364  0.0482  0.0329  144 ASP   C O   
2159 C CB  . ASP   B 138 ? 0.2569 0.2271 0.2313 0.0356  0.0344  0.0234  144 ASP   C CB  
2160 C CG  . ASP   B 138 ? 0.2795 0.2522 0.2530 0.0335  0.0276  0.0208  144 ASP   C CG  
2161 O OD1 . ASP   B 138 ? 0.2755 0.2526 0.2586 0.0291  0.0247  0.0213  144 ASP   C OD1 
2162 O OD2 . ASP   B 138 ? 0.3350 0.3053 0.2979 0.0366  0.0252  0.0182  144 ASP   C OD2 
2163 N N   . GLU   B 139 ? 0.3082 0.2803 0.3024 0.0349  0.0461  0.0286  145 GLU   C N   
2164 C CA  . GLU   B 139 ? 0.3665 0.3356 0.3617 0.0379  0.0543  0.0321  145 GLU   C CA  
2165 C C   . GLU   B 139 ? 0.4084 0.3809 0.4162 0.0361  0.0563  0.0331  145 GLU   C C   
2166 O O   . GLU   B 139 ? 0.4086 0.3855 0.4232 0.0329  0.0512  0.0309  145 GLU   C O   
2167 C CB  . GLU   B 139 ? 0.4400 0.4023 0.4185 0.0440  0.0567  0.0290  145 GLU   C CB  
2168 C CG  . GLU   B 139 ? 0.5530 0.5154 0.5278 0.0445  0.0524  0.0228  145 GLU   C CG  
2169 C CD  . GLU   B 139 ? 0.7081 0.6656 0.6661 0.0488  0.0494  0.0176  145 GLU   C CD  
2170 O OE1 . GLU   B 139 ? 0.7519 0.7086 0.7070 0.0496  0.0464  0.0123  145 GLU   C OE1 
2171 O OE2 . GLU   B 139 ? 0.7494 0.7037 0.6973 0.0515  0.0499  0.0189  145 GLU   C OE2 
2172 N N   . GLU   B 140 ? 0.4477 0.4178 0.4584 0.0388  0.0643  0.0367  146 GLU   C N   
2173 C CA  . GLU   B 140 ? 0.4796 0.4518 0.5009 0.0385  0.0676  0.0378  146 GLU   C CA  
2174 C C   . GLU   B 140 ? 0.4996 0.4793 0.5362 0.0330  0.0624  0.0386  146 GLU   C C   
2175 O O   . GLU   B 140 ? 0.5120 0.4943 0.5588 0.0324  0.0643  0.0399  146 GLU   C O   
2176 C CB  . GLU   B 140 ? 0.5248 0.4923 0.5350 0.0425  0.0684  0.0326  146 GLU   C CB  
2177 C CG  . GLU   B 140 ? 0.6297 0.5994 0.6488 0.0416  0.0686  0.0311  146 GLU   C CG  
2178 C CD  . GLU   B 140 ? 0.7400 0.7090 0.7676 0.0435  0.0770  0.0353  146 GLU   C CD  
2179 O OE1 . GLU   B 140 ? 0.7739 0.7454 0.8106 0.0425  0.0770  0.0348  146 GLU   C OE1 
2180 O OE2 . GLU   B 140 ? 0.7803 0.7464 0.8063 0.0462  0.0839  0.0395  146 GLU   C OE2 
2181 C C4  . A1B3C C .   ? 0.5336 0.5006 0.5716 0.0133  0.0659  -0.0337 201 A1B3C A C4  
2182 C C5  . A1B3C C .   ? 0.5247 0.4877 0.5704 0.0166  0.0654  -0.0309 201 A1B3C A C5  
2183 C C6  . A1B3C C .   ? 0.5103 0.4764 0.5501 0.0164  0.0550  -0.0268 201 A1B3C A C6  
2184 C C7  . A1B3C C .   ? 0.4875 0.4474 0.5316 0.0174  0.0556  -0.0266 201 A1B3C A C7  
2185 C C8  . A1B3C C .   ? 0.4386 0.4037 0.4981 0.0248  0.0529  -0.0163 201 A1B3C A C8  
2186 C C10 . A1B3C C .   ? 0.4495 0.3997 0.4982 0.0184  0.0489  -0.0223 201 A1B3C A C10 
2187 C C13 . A1B3C C .   ? 0.4174 0.3911 0.4939 0.0321  0.0366  0.0058  201 A1B3C A C13 
2188 F F1  . A1B3C C .   ? 0.4333 0.4017 0.5244 0.0356  0.0433  0.0088  201 A1B3C A F1  
2189 F F   . A1B3C C .   ? 0.3899 0.3642 0.4580 0.0294  0.0300  0.0055  201 A1B3C A F   
2190 C C12 . A1B3C C .   ? 0.4317 0.3988 0.4980 0.0283  0.0406  -0.0043 201 A1B3C A C12 
2191 C C11 . A1B3C C .   ? 0.4459 0.4019 0.5061 0.0242  0.0443  -0.0121 201 A1B3C A C11 
2192 C C9  . A1B3C C .   ? 0.4581 0.4068 0.5148 0.0207  0.0578  -0.0238 201 A1B3C A C9  
2193 C C14 . A1B3C C .   ? 0.4263 0.3919 0.5029 0.0312  0.0495  -0.0048 201 A1B3C A C14 
2194 N N   . A1B3C C .   ? 0.4459 0.4056 0.5101 0.0258  0.0536  -0.0153 201 A1B3C A N   
2195 O O   . A1B3C C .   ? 0.3796 0.3536 0.4468 0.0287  0.0505  -0.0092 201 A1B3C A O   
2196 C C1  . A1B3C C .   ? 0.5097 0.4829 0.5380 0.0139  0.0454  -0.0246 201 A1B3C A C1  
2197 S S   . A1B3C C .   ? 0.4874 0.4654 0.5146 0.0158  0.0344  -0.0178 201 A1B3C A S   
2198 C C   . A1B3C C .   ? 0.4780 0.4594 0.4892 0.0103  0.0262  -0.0191 201 A1B3C A C   
2199 C C3  . A1B3C C .   ? 0.5329 0.5065 0.5580 0.0101  0.0559  -0.0317 201 A1B3C A C3  
2200 C C2  . A1B3C C .   ? 0.5253 0.5018 0.5464 0.0108  0.0459  -0.0270 201 A1B3C A C2  
# 
