data_7I7I
# 
_entry.id   7I7I 
# 
_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   7I7I         pdb_00007i7i 10.2210/pdb7i7i/pdb 
WWPDB D_1001408413 ?            ?                   
# 
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                        7I7I 
_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 '(1R,2S)-2-(methylsulfanyl)cyclohexyl (3S)-3-carbamoylpiperidine-1-carboxylate' 300.417   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                      65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                            78.133    1   ?         ? ? ? 
5 water       nat water                                                                           18.015    365 ?         ? ? ? 
# 
_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 '(1R,2S)-2-(methylsulfanyl)cyclohexyl (3S)-3-carbamoylpiperidine-1-carboxylate' A1B5O 
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 
A1B5O non-polymer         . '(1R,2S)-2-(methylsulfanyl)cyclohexyl (3S)-3-carbamoylpiperidine-1-carboxylate' ? 'C14 H24 N2 O3 S' 
300.417 
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        A1B5O 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B5O 
_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 A1B5O 1   201 201 A1B5O LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 3 ZN    1   201 1   ZN    ZN  C . 
F 4 DMS   1   202 1   DMS   DMS C . 
G 5 HOH   1   301 221 HOH   HOH A . 
G 5 HOH   2   302 373 HOH   HOH A . 
G 5 HOH   3   303 219 HOH   HOH A . 
G 5 HOH   4   304 358 HOH   HOH A . 
G 5 HOH   5   305 55  HOH   HOH A . 
G 5 HOH   6   306 329 HOH   HOH A . 
G 5 HOH   7   307 182 HOH   HOH A . 
G 5 HOH   8   308 343 HOH   HOH A . 
G 5 HOH   9   309 163 HOH   HOH A . 
G 5 HOH   10  310 154 HOH   HOH A . 
G 5 HOH   11  311 282 HOH   HOH A . 
G 5 HOH   12  312 226 HOH   HOH A . 
G 5 HOH   13  313 146 HOH   HOH A . 
G 5 HOH   14  314 105 HOH   HOH A . 
G 5 HOH   15  315 43  HOH   HOH A . 
G 5 HOH   16  316 120 HOH   HOH A . 
G 5 HOH   17  317 210 HOH   HOH A . 
G 5 HOH   18  318 136 HOH   HOH A . 
G 5 HOH   19  319 98  HOH   HOH A . 
G 5 HOH   20  320 42  HOH   HOH A . 
G 5 HOH   21  321 264 HOH   HOH A . 
G 5 HOH   22  322 158 HOH   HOH A . 
G 5 HOH   23  323 106 HOH   HOH A . 
G 5 HOH   24  324 183 HOH   HOH A . 
G 5 HOH   25  325 56  HOH   HOH A . 
G 5 HOH   26  326 115 HOH   HOH A . 
G 5 HOH   27  327 138 HOH   HOH A . 
G 5 HOH   28  328 5   HOH   HOH A . 
G 5 HOH   29  329 83  HOH   HOH A . 
G 5 HOH   30  330 18  HOH   HOH A . 
G 5 HOH   31  331 187 HOH   HOH A . 
G 5 HOH   32  332 63  HOH   HOH A . 
G 5 HOH   33  333 19  HOH   HOH A . 
G 5 HOH   34  334 129 HOH   HOH A . 
G 5 HOH   35  335 169 HOH   HOH A . 
G 5 HOH   36  336 243 HOH   HOH A . 
G 5 HOH   37  337 96  HOH   HOH A . 
G 5 HOH   38  338 361 HOH   HOH A . 
G 5 HOH   39  339 279 HOH   HOH A . 
G 5 HOH   40  340 149 HOH   HOH A . 
G 5 HOH   41  341 196 HOH   HOH A . 
G 5 HOH   42  342 168 HOH   HOH A . 
G 5 HOH   43  343 200 HOH   HOH A . 
G 5 HOH   44  344 164 HOH   HOH A . 
G 5 HOH   45  345 205 HOH   HOH A . 
G 5 HOH   46  346 14  HOH   HOH A . 
G 5 HOH   47  347 280 HOH   HOH A . 
G 5 HOH   48  348 102 HOH   HOH A . 
G 5 HOH   49  349 185 HOH   HOH A . 
G 5 HOH   50  350 304 HOH   HOH A . 
G 5 HOH   51  351 124 HOH   HOH A . 
G 5 HOH   52  352 16  HOH   HOH A . 
G 5 HOH   53  353 60  HOH   HOH A . 
G 5 HOH   54  354 47  HOH   HOH A . 
G 5 HOH   55  355 32  HOH   HOH A . 
G 5 HOH   56  356 186 HOH   HOH A . 
G 5 HOH   57  357 276 HOH   HOH A . 
G 5 HOH   58  358 144 HOH   HOH A . 
G 5 HOH   59  359 17  HOH   HOH A . 
G 5 HOH   60  360 224 HOH   HOH A . 
G 5 HOH   61  361 8   HOH   HOH A . 
G 5 HOH   62  362 135 HOH   HOH A . 
G 5 HOH   63  363 325 HOH   HOH A . 
G 5 HOH   64  364 294 HOH   HOH A . 
G 5 HOH   65  365 41  HOH   HOH A . 
G 5 HOH   66  366 303 HOH   HOH A . 
G 5 HOH   67  367 177 HOH   HOH A . 
G 5 HOH   68  368 299 HOH   HOH A . 
G 5 HOH   69  369 167 HOH   HOH A . 
G 5 HOH   70  370 50  HOH   HOH A . 
G 5 HOH   71  371 4   HOH   HOH A . 
G 5 HOH   72  372 107 HOH   HOH A . 
G 5 HOH   73  373 3   HOH   HOH A . 
G 5 HOH   74  374 305 HOH   HOH A . 
G 5 HOH   75  375 29  HOH   HOH A . 
G 5 HOH   76  376 162 HOH   HOH A . 
G 5 HOH   77  377 140 HOH   HOH A . 
G 5 HOH   78  378 216 HOH   HOH A . 
G 5 HOH   79  379 31  HOH   HOH A . 
G 5 HOH   80  380 72  HOH   HOH A . 
G 5 HOH   81  381 310 HOH   HOH A . 
G 5 HOH   82  382 188 HOH   HOH A . 
G 5 HOH   83  383 36  HOH   HOH A . 
G 5 HOH   84  384 184 HOH   HOH A . 
G 5 HOH   85  385 211 HOH   HOH A . 
G 5 HOH   86  386 284 HOH   HOH A . 
G 5 HOH   87  387 97  HOH   HOH A . 
G 5 HOH   88  388 70  HOH   HOH A . 
G 5 HOH   89  389 254 HOH   HOH A . 
G 5 HOH   90  390 51  HOH   HOH A . 
G 5 HOH   91  391 360 HOH   HOH A . 
G 5 HOH   92  392 111 HOH   HOH A . 
G 5 HOH   93  393 222 HOH   HOH A . 
G 5 HOH   94  394 13  HOH   HOH A . 
G 5 HOH   95  395 179 HOH   HOH A . 
G 5 HOH   96  396 290 HOH   HOH A . 
G 5 HOH   97  397 192 HOH   HOH A . 
G 5 HOH   98  398 64  HOH   HOH A . 
G 5 HOH   99  399 27  HOH   HOH A . 
G 5 HOH   100 400 302 HOH   HOH A . 
G 5 HOH   101 401 117 HOH   HOH A . 
G 5 HOH   102 402 166 HOH   HOH A . 
G 5 HOH   103 403 175 HOH   HOH A . 
G 5 HOH   104 404 283 HOH   HOH A . 
G 5 HOH   105 405 38  HOH   HOH A . 
G 5 HOH   106 406 197 HOH   HOH A . 
G 5 HOH   107 407 118 HOH   HOH A . 
G 5 HOH   108 408 225 HOH   HOH A . 
G 5 HOH   109 409 367 HOH   HOH A . 
G 5 HOH   110 410 121 HOH   HOH A . 
G 5 HOH   111 411 88  HOH   HOH A . 
G 5 HOH   112 412 86  HOH   HOH A . 
G 5 HOH   113 413 45  HOH   HOH A . 
G 5 HOH   114 414 127 HOH   HOH A . 
G 5 HOH   115 415 181 HOH   HOH A . 
G 5 HOH   116 416 74  HOH   HOH A . 
G 5 HOH   117 417 207 HOH   HOH A . 
G 5 HOH   118 418 87  HOH   HOH A . 
G 5 HOH   119 419 103 HOH   HOH A . 
G 5 HOH   120 420 159 HOH   HOH A . 
G 5 HOH   121 421 126 HOH   HOH A . 
G 5 HOH   122 422 116 HOH   HOH A . 
G 5 HOH   123 423 77  HOH   HOH A . 
G 5 HOH   124 424 324 HOH   HOH A . 
G 5 HOH   125 425 134 HOH   HOH A . 
G 5 HOH   126 426 71  HOH   HOH A . 
G 5 HOH   127 427 313 HOH   HOH A . 
G 5 HOH   128 428 232 HOH   HOH A . 
G 5 HOH   129 429 293 HOH   HOH A . 
G 5 HOH   130 430 363 HOH   HOH A . 
G 5 HOH   131 431 46  HOH   HOH A . 
G 5 HOH   132 432 287 HOH   HOH A . 
G 5 HOH   133 433 147 HOH   HOH A . 
G 5 HOH   134 434 311 HOH   HOH A . 
G 5 HOH   135 435 212 HOH   HOH A . 
G 5 HOH   136 436 68  HOH   HOH A . 
G 5 HOH   137 437 35  HOH   HOH A . 
G 5 HOH   138 438 227 HOH   HOH A . 
G 5 HOH   139 439 306 HOH   HOH A . 
G 5 HOH   140 440 109 HOH   HOH A . 
G 5 HOH   141 441 132 HOH   HOH A . 
G 5 HOH   142 442 237 HOH   HOH A . 
G 5 HOH   143 443 268 HOH   HOH A . 
G 5 HOH   144 444 307 HOH   HOH A . 
G 5 HOH   145 445 81  HOH   HOH A . 
G 5 HOH   146 446 104 HOH   HOH A . 
G 5 HOH   147 447 59  HOH   HOH A . 
G 5 HOH   148 448 344 HOH   HOH A . 
G 5 HOH   149 449 357 HOH   HOH A . 
G 5 HOH   150 450 318 HOH   HOH A . 
G 5 HOH   151 451 332 HOH   HOH A . 
G 5 HOH   152 452 261 HOH   HOH A . 
G 5 HOH   153 453 326 HOH   HOH A . 
G 5 HOH   154 454 217 HOH   HOH A . 
G 5 HOH   155 455 241 HOH   HOH A . 
G 5 HOH   156 456 160 HOH   HOH A . 
G 5 HOH   157 457 371 HOH   HOH A . 
G 5 HOH   158 458 348 HOH   HOH A . 
G 5 HOH   159 459 334 HOH   HOH A . 
G 5 HOH   160 460 335 HOH   HOH A . 
G 5 HOH   161 461 247 HOH   HOH A . 
G 5 HOH   162 462 277 HOH   HOH A . 
G 5 HOH   163 463 312 HOH   HOH A . 
G 5 HOH   164 464 199 HOH   HOH A . 
G 5 HOH   165 465 242 HOH   HOH A . 
G 5 HOH   166 466 273 HOH   HOH A . 
G 5 HOH   167 467 244 HOH   HOH A . 
G 5 HOH   168 468 271 HOH   HOH A . 
G 5 HOH   169 469 215 HOH   HOH A . 
G 5 HOH   170 470 110 HOH   HOH A . 
G 5 HOH   171 471 255 HOH   HOH A . 
G 5 HOH   172 472 346 HOH   HOH A . 
G 5 HOH   173 473 375 HOH   HOH A . 
G 5 HOH   174 474 339 HOH   HOH A . 
H 5 HOH   1   301 351 HOH   HOH C . 
H 5 HOH   2   302 327 HOH   HOH C . 
H 5 HOH   3   303 89  HOH   HOH C . 
H 5 HOH   4   304 320 HOH   HOH C . 
H 5 HOH   5   305 296 HOH   HOH C . 
H 5 HOH   6   306 278 HOH   HOH C . 
H 5 HOH   7   307 151 HOH   HOH C . 
H 5 HOH   8   308 157 HOH   HOH C . 
H 5 HOH   9   309 266 HOH   HOH C . 
H 5 HOH   10  310 274 HOH   HOH C . 
H 5 HOH   11  311 190 HOH   HOH C . 
H 5 HOH   12  312 246 HOH   HOH C . 
H 5 HOH   13  313 84  HOH   HOH C . 
H 5 HOH   14  314 52  HOH   HOH C . 
H 5 HOH   15  315 369 HOH   HOH C . 
H 5 HOH   16  316 99  HOH   HOH C . 
H 5 HOH   17  317 372 HOH   HOH C . 
H 5 HOH   18  318 300 HOH   HOH C . 
H 5 HOH   19  319 131 HOH   HOH C . 
H 5 HOH   20  320 30  HOH   HOH C . 
H 5 HOH   21  321 364 HOH   HOH C . 
H 5 HOH   22  322 323 HOH   HOH C . 
H 5 HOH   23  323 198 HOH   HOH C . 
H 5 HOH   24  324 165 HOH   HOH C . 
H 5 HOH   25  325 295 HOH   HOH C . 
H 5 HOH   26  326 172 HOH   HOH C . 
H 5 HOH   27  327 82  HOH   HOH C . 
H 5 HOH   28  328 194 HOH   HOH C . 
H 5 HOH   29  329 20  HOH   HOH C . 
H 5 HOH   30  330 39  HOH   HOH C . 
H 5 HOH   31  331 308 HOH   HOH C . 
H 5 HOH   32  332 92  HOH   HOH C . 
H 5 HOH   33  333 251 HOH   HOH C . 
H 5 HOH   34  334 292 HOH   HOH C . 
H 5 HOH   35  335 319 HOH   HOH C . 
H 5 HOH   36  336 49  HOH   HOH C . 
H 5 HOH   37  337 233 HOH   HOH C . 
H 5 HOH   38  338 231 HOH   HOH C . 
H 5 HOH   39  339 85  HOH   HOH C . 
H 5 HOH   40  340 206 HOH   HOH C . 
H 5 HOH   41  341 7   HOH   HOH C . 
H 5 HOH   42  342 189 HOH   HOH C . 
H 5 HOH   43  343 58  HOH   HOH C . 
H 5 HOH   44  344 26  HOH   HOH C . 
H 5 HOH   45  345 9   HOH   HOH C . 
H 5 HOH   46  346 33  HOH   HOH C . 
H 5 HOH   47  347 214 HOH   HOH C . 
H 5 HOH   48  348 291 HOH   HOH C . 
H 5 HOH   49  349 6   HOH   HOH C . 
H 5 HOH   50  350 281 HOH   HOH C . 
H 5 HOH   51  351 137 HOH   HOH C . 
H 5 HOH   52  352 79  HOH   HOH C . 
H 5 HOH   53  353 342 HOH   HOH C . 
H 5 HOH   54  354 69  HOH   HOH C . 
H 5 HOH   55  355 235 HOH   HOH C . 
H 5 HOH   56  356 101 HOH   HOH C . 
H 5 HOH   57  357 148 HOH   HOH C . 
H 5 HOH   58  358 130 HOH   HOH C . 
H 5 HOH   59  359 239 HOH   HOH C . 
H 5 HOH   60  360 153 HOH   HOH C . 
H 5 HOH   61  361 25  HOH   HOH C . 
H 5 HOH   62  362 142 HOH   HOH C . 
H 5 HOH   63  363 170 HOH   HOH C . 
H 5 HOH   64  364 94  HOH   HOH C . 
H 5 HOH   65  365 309 HOH   HOH C . 
H 5 HOH   66  366 90  HOH   HOH C . 
H 5 HOH   67  367 321 HOH   HOH C . 
H 5 HOH   68  368 37  HOH   HOH C . 
H 5 HOH   69  369 176 HOH   HOH C . 
H 5 HOH   70  370 209 HOH   HOH C . 
H 5 HOH   71  371 315 HOH   HOH C . 
H 5 HOH   72  372 44  HOH   HOH C . 
H 5 HOH   73  373 353 HOH   HOH C . 
H 5 HOH   74  374 28  HOH   HOH C . 
H 5 HOH   75  375 314 HOH   HOH C . 
H 5 HOH   76  376 245 HOH   HOH C . 
H 5 HOH   77  377 125 HOH   HOH C . 
H 5 HOH   78  378 23  HOH   HOH C . 
H 5 HOH   79  379 173 HOH   HOH C . 
H 5 HOH   80  380 285 HOH   HOH C . 
H 5 HOH   81  381 22  HOH   HOH C . 
H 5 HOH   82  382 238 HOH   HOH C . 
H 5 HOH   83  383 108 HOH   HOH C . 
H 5 HOH   84  384 48  HOH   HOH C . 
H 5 HOH   85  385 322 HOH   HOH C . 
H 5 HOH   86  386 230 HOH   HOH C . 
H 5 HOH   87  387 253 HOH   HOH C . 
H 5 HOH   88  388 298 HOH   HOH C . 
H 5 HOH   89  389 208 HOH   HOH C . 
H 5 HOH   90  390 258 HOH   HOH C . 
H 5 HOH   91  391 75  HOH   HOH C . 
H 5 HOH   92  392 289 HOH   HOH C . 
H 5 HOH   93  393 73  HOH   HOH C . 
H 5 HOH   94  394 93  HOH   HOH C . 
H 5 HOH   95  395 11  HOH   HOH C . 
H 5 HOH   96  396 78  HOH   HOH C . 
H 5 HOH   97  397 218 HOH   HOH C . 
H 5 HOH   98  398 24  HOH   HOH C . 
H 5 HOH   99  399 65  HOH   HOH C . 
H 5 HOH   100 400 34  HOH   HOH C . 
H 5 HOH   101 401 76  HOH   HOH C . 
H 5 HOH   102 402 359 HOH   HOH C . 
H 5 HOH   103 403 220 HOH   HOH C . 
H 5 HOH   104 404 223 HOH   HOH C . 
H 5 HOH   105 405 2   HOH   HOH C . 
H 5 HOH   106 406 1   HOH   HOH C . 
H 5 HOH   107 407 80  HOH   HOH C . 
H 5 HOH   108 408 267 HOH   HOH C . 
H 5 HOH   109 409 133 HOH   HOH C . 
H 5 HOH   110 410 229 HOH   HOH C . 
H 5 HOH   111 411 112 HOH   HOH C . 
H 5 HOH   112 412 54  HOH   HOH C . 
H 5 HOH   113 413 156 HOH   HOH C . 
H 5 HOH   114 414 250 HOH   HOH C . 
H 5 HOH   115 415 57  HOH   HOH C . 
H 5 HOH   116 416 201 HOH   HOH C . 
H 5 HOH   117 417 352 HOH   HOH C . 
H 5 HOH   118 418 191 HOH   HOH C . 
H 5 HOH   119 419 193 HOH   HOH C . 
H 5 HOH   120 420 139 HOH   HOH C . 
H 5 HOH   121 421 114 HOH   HOH C . 
H 5 HOH   122 422 21  HOH   HOH C . 
H 5 HOH   123 423 155 HOH   HOH C . 
H 5 HOH   124 424 350 HOH   HOH C . 
H 5 HOH   125 425 10  HOH   HOH C . 
H 5 HOH   126 426 365 HOH   HOH C . 
H 5 HOH   127 427 257 HOH   HOH C . 
H 5 HOH   128 428 362 HOH   HOH C . 
H 5 HOH   129 429 316 HOH   HOH C . 
H 5 HOH   130 430 62  HOH   HOH C . 
H 5 HOH   131 431 119 HOH   HOH C . 
H 5 HOH   132 432 128 HOH   HOH C . 
H 5 HOH   133 433 328 HOH   HOH C . 
H 5 HOH   134 434 297 HOH   HOH C . 
H 5 HOH   135 435 95  HOH   HOH C . 
H 5 HOH   136 436 61  HOH   HOH C . 
H 5 HOH   137 437 40  HOH   HOH C . 
H 5 HOH   138 438 272 HOH   HOH C . 
H 5 HOH   139 439 143 HOH   HOH C . 
H 5 HOH   140 440 53  HOH   HOH C . 
H 5 HOH   141 441 178 HOH   HOH C . 
H 5 HOH   142 442 122 HOH   HOH C . 
H 5 HOH   143 443 15  HOH   HOH C . 
H 5 HOH   144 444 171 HOH   HOH C . 
H 5 HOH   145 445 370 HOH   HOH C . 
H 5 HOH   146 446 141 HOH   HOH C . 
H 5 HOH   147 447 202 HOH   HOH C . 
H 5 HOH   148 448 161 HOH   HOH C . 
H 5 HOH   149 449 180 HOH   HOH C . 
H 5 HOH   150 450 240 HOH   HOH C . 
H 5 HOH   151 451 203 HOH   HOH C . 
H 5 HOH   152 452 174 HOH   HOH C . 
H 5 HOH   153 453 152 HOH   HOH C . 
H 5 HOH   154 454 368 HOH   HOH C . 
H 5 HOH   155 455 123 HOH   HOH C . 
H 5 HOH   156 456 330 HOH   HOH C . 
H 5 HOH   157 457 333 HOH   HOH C . 
H 5 HOH   158 458 354 HOH   HOH C . 
H 5 HOH   159 459 286 HOH   HOH C . 
H 5 HOH   160 460 349 HOH   HOH C . 
H 5 HOH   161 461 345 HOH   HOH C . 
H 5 HOH   162 462 262 HOH   HOH C . 
H 5 HOH   163 463 204 HOH   HOH C . 
H 5 HOH   164 464 366 HOH   HOH C . 
H 5 HOH   165 465 248 HOH   HOH C . 
H 5 HOH   166 466 265 HOH   HOH C . 
H 5 HOH   167 467 213 HOH   HOH C . 
H 5 HOH   168 468 331 HOH   HOH C . 
H 5 HOH   169 469 269 HOH   HOH C . 
H 5 HOH   170 470 195 HOH   HOH C . 
H 5 HOH   171 471 338 HOH   HOH C . 
H 5 HOH   172 472 67  HOH   HOH C . 
H 5 HOH   173 473 256 HOH   HOH C . 
H 5 HOH   174 474 355 HOH   HOH C . 
H 5 HOH   175 475 336 HOH   HOH C . 
H 5 HOH   176 476 234 HOH   HOH C . 
H 5 HOH   177 477 340 HOH   HOH C . 
H 5 HOH   178 478 270 HOH   HOH C . 
H 5 HOH   179 479 317 HOH   HOH C . 
H 5 HOH   180 480 374 HOH   HOH C . 
H 5 HOH   181 481 260 HOH   HOH C . 
H 5 HOH   182 482 91  HOH   HOH C . 
H 5 HOH   183 483 145 HOH   HOH C . 
H 5 HOH   184 484 263 HOH   HOH C . 
H 5 HOH   185 485 249 HOH   HOH C . 
H 5 HOH   186 486 341 HOH   HOH C . 
H 5 HOH   187 487 150 HOH   HOH C . 
H 5 HOH   188 488 347 HOH   HOH C . 
H 5 HOH   189 489 113 HOH   HOH C . 
H 5 HOH   190 490 337 HOH   HOH C . 
H 5 HOH   191 491 236 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           7I7I 
_cell.length_a           86.450 
_cell.length_b           57.480 
_cell.length_c           64.650 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.70 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I7I 
_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          7I7I 
_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   51.16 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-02-20 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92204 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92204 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I7I 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             37.59 
_reflns.d_resolution_high            1.29 
_reflns.number_obs                   75650 
_reflns.percent_possible_obs         95.3 
_reflns.pdbx_Rmerge_I_obs            0.085 
_reflns.pdbx_netI_over_sigmaI        14.4 
_reflns.pdbx_redundancy              5.6 
_reflns.pdbx_Rrim_I_all              0.093 
_reflns.pdbx_Rpim_I_all              0.037 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     425296 
_reflns.pdbx_chi_squared             0.90 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.29 
_reflns_shell.d_res_low                   1.32 
_reflns_shell.number_measured_all         9958 
_reflns_shell.number_unique_obs           3771 
_reflns_shell.Rmerge_I_obs                0.988 
_reflns_shell.pdbx_chi_squared            1.02 
_reflns_shell.pdbx_redundancy             2.6 
_reflns_shell.percent_possible_obs        64.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.1 
_reflns_shell.pdbx_Rrim_I_all             1.255 
_reflns_shell.pdbx_Rpim_I_all             0.753 
_reflns_shell.pdbx_CC_half                0.392 
_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                                 7I7I 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     75650 
_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                             37.59 
_refine.ls_d_res_high                            1.290 
_refine.ls_percent_reflns_obs                    95.3 
_refine.ls_R_factor_obs                          0.1876 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1866 
_refine.ls_R_factor_R_free                       0.2054 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  3782 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.960 
_refine.correlation_coeff_Fo_to_Fc_free          0.957 
_refine.B_iso_mean                               18.43 
_refine.aniso_B[1][1]                            -1.43360 
_refine.aniso_B[2][2]                            -0.36290 
_refine.aniso_B[3][3]                            1.79650 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -2.26760 
_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   0.049 
_refine.pdbx_overall_SU_R_Blow_DPI               0.051 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.052 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I7I 
_refine_analyze.Luzzati_coordinate_error_obs    0.17 
_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         26 
_refine_hist.number_atoms_solvent             365 
_refine_hist.number_atoms_total               2557 
_refine_hist.d_res_high                       1.290 
_refine_hist.d_res_low                        37.59 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.012 ? 2.00  2262 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.08  ? 2.00  3081 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  765  '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  396  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2262 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.79  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.82 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  281  '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  2114 '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                       1.29 
_refine_ls_shell.d_res_low                        1.30 
_refine_ls_shell.number_reflns_R_work             1435 
_refine_ls_shell.R_factor_R_work                  0.3696 
_refine_ls_shell.percent_reflns_obs               61.28 
_refine_ls_shell.R_factor_R_free                  0.4264 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.16 
_refine_ls_shell.number_reflns_R_free             78 
_refine_ls_shell.number_reflns_all                1513 
_refine_ls_shell.R_factor_all                     0.3723 
# 
_struct.entry_id                  7I7I 
_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-0038434-001 (A71EV2A-x5231)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I7I 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I7I A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I7I C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P6  AA6 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P7  AA7 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P8  AA8 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P9  AA9 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P10 AB1 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P11 AB2 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.349 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.320 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.262 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.105 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.339 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.300 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 E ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.124 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 110.7 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 105.9 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.4 ? 
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_555 106.0 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 103.8 ? 
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_555 113.7 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.9 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.4 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 118.2 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 106.1 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.1 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.6 ? 
# 
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 ? THR A 120 ? GLY A 119 THR A 126 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7I7I 
_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 C HOH 332 ? ? O C HOH 429 ? ? 1.94 
2 1 O A HOH 394 ? ? O A HOH 450 ? ? 2.02 
3 1 O C HOH 362 ? ? O C HOH 388 ? ? 2.11 
4 1 O C HOH 375 ? ? O C HOH 393 ? ? 2.12 
5 1 O A HOH 360 ? ? O A HOH 424 ? ? 2.15 
6 1 O A HOH 350 ? ? O C HOH 483 ? ? 2.18 
7 1 O C HOH 402 ? ? O C HOH 456 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     427 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     435 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_455 
_pdbx_validate_symm_contact.dist              1.89 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1  1 C  A SER 105 ? ? O   A SER 105 ? ? 1.055 1.229 -0.174 0.019 N 
2  1 CB A GLU 106 ? ? CG  A GLU 106 ? ? 1.640 1.517 0.123  0.019 N 
3  1 CD A GLU 106 ? ? OE2 A GLU 106 ? ? 1.174 1.252 -0.078 0.011 N 
4  1 CA A GLU 106 ? ? C   A GLU 106 ? ? 1.686 1.525 0.161  0.026 N 
5  1 C  A GLU 106 ? ? O   A GLU 106 ? ? 1.075 1.229 -0.154 0.019 N 
6  1 N  A PRO 107 ? ? CA  A PRO 107 ? ? 1.302 1.468 -0.166 0.017 N 
7  1 CA A PRO 107 ? ? CB  A PRO 107 ? ? 1.655 1.531 0.124  0.020 N 
8  1 CD A PRO 107 ? ? N   A PRO 107 ? ? 1.570 1.474 0.096  0.014 N 
9  1 C  A PRO 107 ? ? O   A PRO 107 ? ? 0.766 1.228 -0.462 0.020 N 
10 1 CA A GLY 108 ? ? C   A GLY 108 ? ? 1.365 1.514 -0.149 0.016 N 
11 1 C  A GLY 108 ? ? N   A ASP 109 ? ? 1.512 1.336 0.176  0.023 Y 
12 1 N  A ASP 109 ? ? CA  A ASP 109 ? ? 1.604 1.459 0.145  0.020 N 
13 1 CA A ASP 109 ? ? CB  A ASP 109 ? ? 1.687 1.535 0.152  0.022 N 
14 1 C  A ASP 109 ? ? O   A ASP 109 ? ? 1.364 1.229 0.135  0.019 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C  A GLY 103 ? ? N  A HIS 104 ? ? CA  A HIS 104 ? ? 104.88 121.70 -16.82 2.50 Y 
2 1 C  A GLU 106 ? ? N  A PRO 107 ? ? CD  A PRO 107 ? ? 114.28 128.40 -14.12 2.10 Y 
3 1 CA A PRO 107 ? ? N  A PRO 107 ? ? CD  A PRO 107 ? ? 120.16 111.70 8.46   1.40 N 
4 1 C  A GLY 108 ? ? N  A ASP 109 ? ? CA  A ASP 109 ? ? 105.14 121.70 -16.56 2.50 Y 
5 1 CB A ASP 109 ? ? CG A ASP 109 ? ? OD1 A ASP 109 ? ? 110.96 118.30 -7.34  0.90 N 
6 1 CB A ASP 109 ? ? CG A ASP 109 ? ? OD2 A ASP 109 ? ? 123.98 118.30 5.68   0.90 N 
7 1 CB A CYS 110 ? ? CA A CYS 110 ? ? C   A CYS 110 ? ? 121.97 111.50 10.47  1.20 N 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             GLY 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              108 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   12.38 
# 
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 14.7810 8.1833   14.2939 -0.0135 -0.0179 -0.0084 0.0139 -0.0178 -0.0023 0.9595 0.5959 0.5850 
0.4856 -0.3179 -0.1509 -0.0204 0.0131 0.0758 0.0126 0.0256 0.0003 -0.0074 -0.0360 -0.0052 
'X-RAY DIFFRACTION' 2 ? refined 25.6406 -20.3214 17.6363 -0.0242 -0.0130 0.0065  0.0062 -0.0141 0.0122  0.5177 0.8829 0.2297 
0.0992 -0.0850 -0.1119 0.0133  0.0147 0.1085 0.0082 0.0228 0.0485 0.0420  0.0188  -0.0361 
# 
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 
A1B5O N1   N  N N 1   
A1B5O C4   C  N N 2   
A1B5O C5   C  N N 3   
A1B5O C6   C  N R 4   
A1B5O C7   C  N N 5   
A1B5O C8   C  N N 6   
A1B5O C10  C  N N 7   
A1B5O C13  C  N N 8   
A1B5O O2   O  N N 9   
A1B5O C12  C  N N 10  
A1B5O C11  C  N S 11  
A1B5O C9   C  N N 12  
A1B5O N    N  N N 13  
A1B5O O1   O  N N 14  
A1B5O O    O  N N 15  
A1B5O C1   C  N R 16  
A1B5O S    S  N N 17  
A1B5O C    C  N N 18  
A1B5O C3   C  N N 19  
A1B5O C2   C  N N 20  
A1B5O H21  H  N N 21  
A1B5O H20  H  N N 22  
A1B5O H11  H  N N 23  
A1B5O H10  H  N N 24  
A1B5O H13  H  N N 25  
A1B5O H12  H  N N 26  
A1B5O H1   H  N N 27  
A1B5O H14  H  N N 28  
A1B5O H15  H  N N 29  
A1B5O H18  H  N N 30  
A1B5O H19  H  N N 31  
A1B5O H22  H  N N 32  
A1B5O H23  H  N N 33  
A1B5O H2   H  N N 34  
A1B5O H16  H  N N 35  
A1B5O H17  H  N N 36  
A1B5O H    H  N N 37  
A1B5O H4   H  N N 38  
A1B5O H5   H  N N 39  
A1B5O H3   H  N N 40  
A1B5O H9   H  N N 41  
A1B5O H8   H  N N 42  
A1B5O H7   H  N N 43  
A1B5O H6   H  N N 44  
ALA   N    N  N N 45  
ALA   CA   C  N S 46  
ALA   C    C  N N 47  
ALA   O    O  N N 48  
ALA   CB   C  N N 49  
ALA   OXT  O  N N 50  
ALA   H    H  N N 51  
ALA   H2   H  N N 52  
ALA   HA   H  N N 53  
ALA   HB1  H  N N 54  
ALA   HB2  H  N N 55  
ALA   HB3  H  N N 56  
ALA   HXT  H  N N 57  
ARG   N    N  N N 58  
ARG   CA   C  N S 59  
ARG   C    C  N N 60  
ARG   O    O  N N 61  
ARG   CB   C  N N 62  
ARG   CG   C  N N 63  
ARG   CD   C  N N 64  
ARG   NE   N  N N 65  
ARG   CZ   C  N N 66  
ARG   NH1  N  N N 67  
ARG   NH2  N  N N 68  
ARG   OXT  O  N N 69  
ARG   H    H  N N 70  
ARG   H2   H  N N 71  
ARG   HA   H  N N 72  
ARG   HB2  H  N N 73  
ARG   HB3  H  N N 74  
ARG   HG2  H  N N 75  
ARG   HG3  H  N N 76  
ARG   HD2  H  N N 77  
ARG   HD3  H  N N 78  
ARG   HE   H  N N 79  
ARG   HH11 H  N N 80  
ARG   HH12 H  N N 81  
ARG   HH21 H  N N 82  
ARG   HH22 H  N N 83  
ARG   HXT  H  N N 84  
ASN   N    N  N N 85  
ASN   CA   C  N S 86  
ASN   C    C  N N 87  
ASN   O    O  N N 88  
ASN   CB   C  N N 89  
ASN   CG   C  N N 90  
ASN   OD1  O  N N 91  
ASN   ND2  N  N N 92  
ASN   OXT  O  N N 93  
ASN   H    H  N N 94  
ASN   H2   H  N N 95  
ASN   HA   H  N N 96  
ASN   HB2  H  N N 97  
ASN   HB3  H  N N 98  
ASN   HD21 H  N N 99  
ASN   HD22 H  N N 100 
ASN   HXT  H  N N 101 
ASP   N    N  N N 102 
ASP   CA   C  N S 103 
ASP   C    C  N N 104 
ASP   O    O  N N 105 
ASP   CB   C  N N 106 
ASP   CG   C  N N 107 
ASP   OD1  O  N N 108 
ASP   OD2  O  N N 109 
ASP   OXT  O  N N 110 
ASP   H    H  N N 111 
ASP   H2   H  N N 112 
ASP   HA   H  N N 113 
ASP   HB2  H  N N 114 
ASP   HB3  H  N N 115 
ASP   HD2  H  N N 116 
ASP   HXT  H  N N 117 
CYS   N    N  N N 118 
CYS   CA   C  N R 119 
CYS   C    C  N N 120 
CYS   O    O  N N 121 
CYS   CB   C  N N 122 
CYS   SG   S  N N 123 
CYS   OXT  O  N N 124 
CYS   H    H  N N 125 
CYS   H2   H  N N 126 
CYS   HA   H  N N 127 
CYS   HB2  H  N N 128 
CYS   HB3  H  N N 129 
CYS   HG   H  N N 130 
CYS   HXT  H  N N 131 
DMS   S    S  N N 132 
DMS   O    O  N N 133 
DMS   C1   C  N N 134 
DMS   C2   C  N N 135 
DMS   H11  H  N N 136 
DMS   H12  H  N N 137 
DMS   H13  H  N N 138 
DMS   H21  H  N N 139 
DMS   H22  H  N N 140 
DMS   H23  H  N N 141 
GLN   N    N  N N 142 
GLN   CA   C  N S 143 
GLN   C    C  N N 144 
GLN   O    O  N N 145 
GLN   CB   C  N N 146 
GLN   CG   C  N N 147 
GLN   CD   C  N N 148 
GLN   OE1  O  N N 149 
GLN   NE2  N  N N 150 
GLN   OXT  O  N N 151 
GLN   H    H  N N 152 
GLN   H2   H  N N 153 
GLN   HA   H  N N 154 
GLN   HB2  H  N N 155 
GLN   HB3  H  N N 156 
GLN   HG2  H  N N 157 
GLN   HG3  H  N N 158 
GLN   HE21 H  N N 159 
GLN   HE22 H  N N 160 
GLN   HXT  H  N N 161 
GLU   N    N  N N 162 
GLU   CA   C  N S 163 
GLU   C    C  N N 164 
GLU   O    O  N N 165 
GLU   CB   C  N N 166 
GLU   CG   C  N N 167 
GLU   CD   C  N N 168 
GLU   OE1  O  N N 169 
GLU   OE2  O  N N 170 
GLU   OXT  O  N N 171 
GLU   H    H  N N 172 
GLU   H2   H  N N 173 
GLU   HA   H  N N 174 
GLU   HB2  H  N N 175 
GLU   HB3  H  N N 176 
GLU   HG2  H  N N 177 
GLU   HG3  H  N N 178 
GLU   HE2  H  N N 179 
GLU   HXT  H  N N 180 
GLY   N    N  N N 181 
GLY   CA   C  N N 182 
GLY   C    C  N N 183 
GLY   O    O  N N 184 
GLY   OXT  O  N N 185 
GLY   H    H  N N 186 
GLY   H2   H  N N 187 
GLY   HA2  H  N N 188 
GLY   HA3  H  N N 189 
GLY   HXT  H  N N 190 
HIS   N    N  N N 191 
HIS   CA   C  N S 192 
HIS   C    C  N N 193 
HIS   O    O  N N 194 
HIS   CB   C  N N 195 
HIS   CG   C  Y N 196 
HIS   ND1  N  Y N 197 
HIS   CD2  C  Y N 198 
HIS   CE1  C  Y N 199 
HIS   NE2  N  Y N 200 
HIS   OXT  O  N N 201 
HIS   H    H  N N 202 
HIS   H2   H  N N 203 
HIS   HA   H  N N 204 
HIS   HB2  H  N N 205 
HIS   HB3  H  N N 206 
HIS   HD1  H  N N 207 
HIS   HD2  H  N N 208 
HIS   HE1  H  N N 209 
HIS   HE2  H  N N 210 
HIS   HXT  H  N N 211 
HOH   O    O  N N 212 
HOH   H1   H  N N 213 
HOH   H2   H  N N 214 
ILE   N    N  N N 215 
ILE   CA   C  N S 216 
ILE   C    C  N N 217 
ILE   O    O  N N 218 
ILE   CB   C  N S 219 
ILE   CG1  C  N N 220 
ILE   CG2  C  N N 221 
ILE   CD1  C  N N 222 
ILE   OXT  O  N N 223 
ILE   H    H  N N 224 
ILE   H2   H  N N 225 
ILE   HA   H  N N 226 
ILE   HB   H  N N 227 
ILE   HG12 H  N N 228 
ILE   HG13 H  N N 229 
ILE   HG21 H  N N 230 
ILE   HG22 H  N N 231 
ILE   HG23 H  N N 232 
ILE   HD11 H  N N 233 
ILE   HD12 H  N N 234 
ILE   HD13 H  N N 235 
ILE   HXT  H  N N 236 
LEU   N    N  N N 237 
LEU   CA   C  N S 238 
LEU   C    C  N N 239 
LEU   O    O  N N 240 
LEU   CB   C  N N 241 
LEU   CG   C  N N 242 
LEU   CD1  C  N N 243 
LEU   CD2  C  N N 244 
LEU   OXT  O  N N 245 
LEU   H    H  N N 246 
LEU   H2   H  N N 247 
LEU   HA   H  N N 248 
LEU   HB2  H  N N 249 
LEU   HB3  H  N N 250 
LEU   HG   H  N N 251 
LEU   HD11 H  N N 252 
LEU   HD12 H  N N 253 
LEU   HD13 H  N N 254 
LEU   HD21 H  N N 255 
LEU   HD22 H  N N 256 
LEU   HD23 H  N N 257 
LEU   HXT  H  N N 258 
LYS   N    N  N N 259 
LYS   CA   C  N S 260 
LYS   C    C  N N 261 
LYS   O    O  N N 262 
LYS   CB   C  N N 263 
LYS   CG   C  N N 264 
LYS   CD   C  N N 265 
LYS   CE   C  N N 266 
LYS   NZ   N  N N 267 
LYS   OXT  O  N N 268 
LYS   H    H  N N 269 
LYS   H2   H  N N 270 
LYS   HA   H  N N 271 
LYS   HB2  H  N N 272 
LYS   HB3  H  N N 273 
LYS   HG2  H  N N 274 
LYS   HG3  H  N N 275 
LYS   HD2  H  N N 276 
LYS   HD3  H  N N 277 
LYS   HE2  H  N N 278 
LYS   HE3  H  N N 279 
LYS   HZ1  H  N N 280 
LYS   HZ2  H  N N 281 
LYS   HZ3  H  N N 282 
LYS   HXT  H  N N 283 
MET   N    N  N N 284 
MET   CA   C  N S 285 
MET   C    C  N N 286 
MET   O    O  N N 287 
MET   CB   C  N N 288 
MET   CG   C  N N 289 
MET   SD   S  N N 290 
MET   CE   C  N N 291 
MET   OXT  O  N N 292 
MET   H    H  N N 293 
MET   H2   H  N N 294 
MET   HA   H  N N 295 
MET   HB2  H  N N 296 
MET   HB3  H  N N 297 
MET   HG2  H  N N 298 
MET   HG3  H  N N 299 
MET   HE1  H  N N 300 
MET   HE2  H  N N 301 
MET   HE3  H  N N 302 
MET   HXT  H  N N 303 
PHE   N    N  N N 304 
PHE   CA   C  N S 305 
PHE   C    C  N N 306 
PHE   O    O  N N 307 
PHE   CB   C  N N 308 
PHE   CG   C  Y N 309 
PHE   CD1  C  Y N 310 
PHE   CD2  C  Y N 311 
PHE   CE1  C  Y N 312 
PHE   CE2  C  Y N 313 
PHE   CZ   C  Y N 314 
PHE   OXT  O  N N 315 
PHE   H    H  N N 316 
PHE   H2   H  N N 317 
PHE   HA   H  N N 318 
PHE   HB2  H  N N 319 
PHE   HB3  H  N N 320 
PHE   HD1  H  N N 321 
PHE   HD2  H  N N 322 
PHE   HE1  H  N N 323 
PHE   HE2  H  N N 324 
PHE   HZ   H  N N 325 
PHE   HXT  H  N N 326 
PRO   N    N  N N 327 
PRO   CA   C  N S 328 
PRO   C    C  N N 329 
PRO   O    O  N N 330 
PRO   CB   C  N N 331 
PRO   CG   C  N N 332 
PRO   CD   C  N N 333 
PRO   OXT  O  N N 334 
PRO   H    H  N N 335 
PRO   HA   H  N N 336 
PRO   HB2  H  N N 337 
PRO   HB3  H  N N 338 
PRO   HG2  H  N N 339 
PRO   HG3  H  N N 340 
PRO   HD2  H  N N 341 
PRO   HD3  H  N N 342 
PRO   HXT  H  N N 343 
SER   N    N  N N 344 
SER   CA   C  N S 345 
SER   C    C  N N 346 
SER   O    O  N N 347 
SER   CB   C  N N 348 
SER   OG   O  N N 349 
SER   OXT  O  N N 350 
SER   H    H  N N 351 
SER   H2   H  N N 352 
SER   HA   H  N N 353 
SER   HB2  H  N N 354 
SER   HB3  H  N N 355 
SER   HG   H  N N 356 
SER   HXT  H  N N 357 
THR   N    N  N N 358 
THR   CA   C  N S 359 
THR   C    C  N N 360 
THR   O    O  N N 361 
THR   CB   C  N R 362 
THR   OG1  O  N N 363 
THR   CG2  C  N N 364 
THR   OXT  O  N N 365 
THR   H    H  N N 366 
THR   H2   H  N N 367 
THR   HA   H  N N 368 
THR   HB   H  N N 369 
THR   HG1  H  N N 370 
THR   HG21 H  N N 371 
THR   HG22 H  N N 372 
THR   HG23 H  N N 373 
THR   HXT  H  N N 374 
TRP   N    N  N N 375 
TRP   CA   C  N S 376 
TRP   C    C  N N 377 
TRP   O    O  N N 378 
TRP   CB   C  N N 379 
TRP   CG   C  Y N 380 
TRP   CD1  C  Y N 381 
TRP   CD2  C  Y N 382 
TRP   NE1  N  Y N 383 
TRP   CE2  C  Y N 384 
TRP   CE3  C  Y N 385 
TRP   CZ2  C  Y N 386 
TRP   CZ3  C  Y N 387 
TRP   CH2  C  Y N 388 
TRP   OXT  O  N N 389 
TRP   H    H  N N 390 
TRP   H2   H  N N 391 
TRP   HA   H  N N 392 
TRP   HB2  H  N N 393 
TRP   HB3  H  N N 394 
TRP   HD1  H  N N 395 
TRP   HE1  H  N N 396 
TRP   HE3  H  N N 397 
TRP   HZ2  H  N N 398 
TRP   HZ3  H  N N 399 
TRP   HH2  H  N N 400 
TRP   HXT  H  N N 401 
TYR   N    N  N N 402 
TYR   CA   C  N S 403 
TYR   C    C  N N 404 
TYR   O    O  N N 405 
TYR   CB   C  N N 406 
TYR   CG   C  Y N 407 
TYR   CD1  C  Y N 408 
TYR   CD2  C  Y N 409 
TYR   CE1  C  Y N 410 
TYR   CE2  C  Y N 411 
TYR   CZ   C  Y N 412 
TYR   OH   O  N N 413 
TYR   OXT  O  N N 414 
TYR   H    H  N N 415 
TYR   H2   H  N N 416 
TYR   HA   H  N N 417 
TYR   HB2  H  N N 418 
TYR   HB3  H  N N 419 
TYR   HD1  H  N N 420 
TYR   HD2  H  N N 421 
TYR   HE1  H  N N 422 
TYR   HE2  H  N N 423 
TYR   HH   H  N N 424 
TYR   HXT  H  N N 425 
VAL   N    N  N N 426 
VAL   CA   C  N S 427 
VAL   C    C  N N 428 
VAL   O    O  N N 429 
VAL   CB   C  N N 430 
VAL   CG1  C  N N 431 
VAL   CG2  C  N N 432 
VAL   OXT  O  N N 433 
VAL   H    H  N N 434 
VAL   H2   H  N N 435 
VAL   HA   H  N N 436 
VAL   HB   H  N N 437 
VAL   HG11 H  N N 438 
VAL   HG12 H  N N 439 
VAL   HG13 H  N N 440 
VAL   HG21 H  N N 441 
VAL   HG22 H  N N 442 
VAL   HG23 H  N N 443 
VAL   HXT  H  N N 444 
ZN    ZN   ZN N N 445 
# 
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 
A1B5O C   S    sing N N 1   
A1B5O S   C1   sing N N 2   
A1B5O C1  C2   sing N N 3   
A1B5O C2  C3   sing N N 4   
A1B5O C3  C4   sing N N 5   
A1B5O C4  C5   sing N N 6   
A1B5O C5  C6   sing N N 7   
A1B5O C1  C6   sing N N 8   
A1B5O C6  O    sing N N 9   
A1B5O O   C7   sing N N 10  
A1B5O O1  C7   doub N N 11  
A1B5O C7  N    sing N N 12  
A1B5O N   C8   sing N N 13  
A1B5O C8  C9   sing N N 14  
A1B5O C9  C10  sing N N 15  
A1B5O C10 C11  sing N N 16  
A1B5O C11 C12  sing N N 17  
A1B5O N1  C12  sing N N 18  
A1B5O C12 O2   doub N N 19  
A1B5O C13 C11  sing N N 20  
A1B5O N   C13  sing N N 21  
A1B5O N1  H21  sing N N 22  
A1B5O N1  H20  sing N N 23  
A1B5O C4  H11  sing N N 24  
A1B5O C4  H10  sing N N 25  
A1B5O C5  H13  sing N N 26  
A1B5O C5  H12  sing N N 27  
A1B5O C6  H1   sing N N 28  
A1B5O C8  H14  sing N N 29  
A1B5O C8  H15  sing N N 30  
A1B5O C10 H18  sing N N 31  
A1B5O C10 H19  sing N N 32  
A1B5O C13 H22  sing N N 33  
A1B5O C13 H23  sing N N 34  
A1B5O C11 H2   sing N N 35  
A1B5O C9  H16  sing N N 36  
A1B5O C9  H17  sing N N 37  
A1B5O C1  H    sing N N 38  
A1B5O C   H4   sing N N 39  
A1B5O C   H5   sing N N 40  
A1B5O C   H3   sing N N 41  
A1B5O C3  H9   sing N N 42  
A1B5O C3  H8   sing N N 43  
A1B5O C2  H7   sing N N 44  
A1B5O C2  H6   sing N N 45  
ALA   N   CA   sing N N 46  
ALA   N   H    sing N N 47  
ALA   N   H2   sing N N 48  
ALA   CA  C    sing N N 49  
ALA   CA  CB   sing N N 50  
ALA   CA  HA   sing N N 51  
ALA   C   O    doub N N 52  
ALA   C   OXT  sing N N 53  
ALA   CB  HB1  sing N N 54  
ALA   CB  HB2  sing N N 55  
ALA   CB  HB3  sing N N 56  
ALA   OXT HXT  sing N N 57  
ARG   N   CA   sing N N 58  
ARG   N   H    sing N N 59  
ARG   N   H2   sing N N 60  
ARG   CA  C    sing N N 61  
ARG   CA  CB   sing N N 62  
ARG   CA  HA   sing N N 63  
ARG   C   O    doub N N 64  
ARG   C   OXT  sing N N 65  
ARG   CB  CG   sing N N 66  
ARG   CB  HB2  sing N N 67  
ARG   CB  HB3  sing N N 68  
ARG   CG  CD   sing N N 69  
ARG   CG  HG2  sing N N 70  
ARG   CG  HG3  sing N N 71  
ARG   CD  NE   sing N N 72  
ARG   CD  HD2  sing N N 73  
ARG   CD  HD3  sing N N 74  
ARG   NE  CZ   sing N N 75  
ARG   NE  HE   sing N N 76  
ARG   CZ  NH1  sing N N 77  
ARG   CZ  NH2  doub N N 78  
ARG   NH1 HH11 sing N N 79  
ARG   NH1 HH12 sing N N 80  
ARG   NH2 HH21 sing N N 81  
ARG   NH2 HH22 sing N N 82  
ARG   OXT HXT  sing N N 83  
ASN   N   CA   sing N N 84  
ASN   N   H    sing N N 85  
ASN   N   H2   sing N N 86  
ASN   CA  C    sing N N 87  
ASN   CA  CB   sing N N 88  
ASN   CA  HA   sing N N 89  
ASN   C   O    doub N N 90  
ASN   C   OXT  sing N N 91  
ASN   CB  CG   sing N N 92  
ASN   CB  HB2  sing N N 93  
ASN   CB  HB3  sing N N 94  
ASN   CG  OD1  doub N N 95  
ASN   CG  ND2  sing N N 96  
ASN   ND2 HD21 sing N N 97  
ASN   ND2 HD22 sing N N 98  
ASN   OXT HXT  sing N N 99  
ASP   N   CA   sing N N 100 
ASP   N   H    sing N N 101 
ASP   N   H2   sing N N 102 
ASP   CA  C    sing N N 103 
ASP   CA  CB   sing N N 104 
ASP   CA  HA   sing N N 105 
ASP   C   O    doub N N 106 
ASP   C   OXT  sing N N 107 
ASP   CB  CG   sing N N 108 
ASP   CB  HB2  sing N N 109 
ASP   CB  HB3  sing N N 110 
ASP   CG  OD1  doub N N 111 
ASP   CG  OD2  sing N N 112 
ASP   OD2 HD2  sing N N 113 
ASP   OXT HXT  sing N N 114 
CYS   N   CA   sing N N 115 
CYS   N   H    sing N N 116 
CYS   N   H2   sing N N 117 
CYS   CA  C    sing N N 118 
CYS   CA  CB   sing N N 119 
CYS   CA  HA   sing N N 120 
CYS   C   O    doub N N 121 
CYS   C   OXT  sing N N 122 
CYS   CB  SG   sing N N 123 
CYS   CB  HB2  sing N N 124 
CYS   CB  HB3  sing N N 125 
CYS   SG  HG   sing N N 126 
CYS   OXT HXT  sing N N 127 
DMS   S   O    doub N N 128 
DMS   S   C1   sing N N 129 
DMS   S   C2   sing N N 130 
DMS   C1  H11  sing N N 131 
DMS   C1  H12  sing N N 132 
DMS   C1  H13  sing N N 133 
DMS   C2  H21  sing N N 134 
DMS   C2  H22  sing N N 135 
DMS   C2  H23  sing N N 136 
GLN   N   CA   sing N N 137 
GLN   N   H    sing N N 138 
GLN   N   H2   sing N N 139 
GLN   CA  C    sing N N 140 
GLN   CA  CB   sing N N 141 
GLN   CA  HA   sing N N 142 
GLN   C   O    doub N N 143 
GLN   C   OXT  sing N N 144 
GLN   CB  CG   sing N N 145 
GLN   CB  HB2  sing N N 146 
GLN   CB  HB3  sing N N 147 
GLN   CG  CD   sing N N 148 
GLN   CG  HG2  sing N N 149 
GLN   CG  HG3  sing N N 150 
GLN   CD  OE1  doub N N 151 
GLN   CD  NE2  sing N N 152 
GLN   NE2 HE21 sing N N 153 
GLN   NE2 HE22 sing N N 154 
GLN   OXT HXT  sing N N 155 
GLU   N   CA   sing N N 156 
GLU   N   H    sing N N 157 
GLU   N   H2   sing N N 158 
GLU   CA  C    sing N N 159 
GLU   CA  CB   sing N N 160 
GLU   CA  HA   sing N N 161 
GLU   C   O    doub N N 162 
GLU   C   OXT  sing N N 163 
GLU   CB  CG   sing N N 164 
GLU   CB  HB2  sing N N 165 
GLU   CB  HB3  sing N N 166 
GLU   CG  CD   sing N N 167 
GLU   CG  HG2  sing N N 168 
GLU   CG  HG3  sing N N 169 
GLU   CD  OE1  doub N N 170 
GLU   CD  OE2  sing N N 171 
GLU   OE2 HE2  sing N N 172 
GLU   OXT HXT  sing N N 173 
GLY   N   CA   sing N N 174 
GLY   N   H    sing N N 175 
GLY   N   H2   sing N N 176 
GLY   CA  C    sing N N 177 
GLY   CA  HA2  sing N N 178 
GLY   CA  HA3  sing N N 179 
GLY   C   O    doub N N 180 
GLY   C   OXT  sing N N 181 
GLY   OXT HXT  sing N N 182 
HIS   N   CA   sing N N 183 
HIS   N   H    sing N N 184 
HIS   N   H2   sing N N 185 
HIS   CA  C    sing N N 186 
HIS   CA  CB   sing N N 187 
HIS   CA  HA   sing N N 188 
HIS   C   O    doub N N 189 
HIS   C   OXT  sing N N 190 
HIS   CB  CG   sing N N 191 
HIS   CB  HB2  sing N N 192 
HIS   CB  HB3  sing N N 193 
HIS   CG  ND1  sing Y N 194 
HIS   CG  CD2  doub Y N 195 
HIS   ND1 CE1  doub Y N 196 
HIS   ND1 HD1  sing N N 197 
HIS   CD2 NE2  sing Y N 198 
HIS   CD2 HD2  sing N N 199 
HIS   CE1 NE2  sing Y N 200 
HIS   CE1 HE1  sing N N 201 
HIS   NE2 HE2  sing N N 202 
HIS   OXT HXT  sing N N 203 
HOH   O   H1   sing N N 204 
HOH   O   H2   sing N N 205 
ILE   N   CA   sing N N 206 
ILE   N   H    sing N N 207 
ILE   N   H2   sing N N 208 
ILE   CA  C    sing N N 209 
ILE   CA  CB   sing N N 210 
ILE   CA  HA   sing N N 211 
ILE   C   O    doub N N 212 
ILE   C   OXT  sing N N 213 
ILE   CB  CG1  sing N N 214 
ILE   CB  CG2  sing N N 215 
ILE   CB  HB   sing N N 216 
ILE   CG1 CD1  sing N N 217 
ILE   CG1 HG12 sing N N 218 
ILE   CG1 HG13 sing N N 219 
ILE   CG2 HG21 sing N N 220 
ILE   CG2 HG22 sing N N 221 
ILE   CG2 HG23 sing N N 222 
ILE   CD1 HD11 sing N N 223 
ILE   CD1 HD12 sing N N 224 
ILE   CD1 HD13 sing N N 225 
ILE   OXT HXT  sing N N 226 
LEU   N   CA   sing N N 227 
LEU   N   H    sing N N 228 
LEU   N   H2   sing N N 229 
LEU   CA  C    sing N N 230 
LEU   CA  CB   sing N N 231 
LEU   CA  HA   sing N N 232 
LEU   C   O    doub N N 233 
LEU   C   OXT  sing N N 234 
LEU   CB  CG   sing N N 235 
LEU   CB  HB2  sing N N 236 
LEU   CB  HB3  sing N N 237 
LEU   CG  CD1  sing N N 238 
LEU   CG  CD2  sing N N 239 
LEU   CG  HG   sing N N 240 
LEU   CD1 HD11 sing N N 241 
LEU   CD1 HD12 sing N N 242 
LEU   CD1 HD13 sing N N 243 
LEU   CD2 HD21 sing N N 244 
LEU   CD2 HD22 sing N N 245 
LEU   CD2 HD23 sing N N 246 
LEU   OXT HXT  sing N N 247 
LYS   N   CA   sing N N 248 
LYS   N   H    sing N N 249 
LYS   N   H2   sing N N 250 
LYS   CA  C    sing N N 251 
LYS   CA  CB   sing N N 252 
LYS   CA  HA   sing N N 253 
LYS   C   O    doub N N 254 
LYS   C   OXT  sing N N 255 
LYS   CB  CG   sing N N 256 
LYS   CB  HB2  sing N N 257 
LYS   CB  HB3  sing N N 258 
LYS   CG  CD   sing N N 259 
LYS   CG  HG2  sing N N 260 
LYS   CG  HG3  sing N N 261 
LYS   CD  CE   sing N N 262 
LYS   CD  HD2  sing N N 263 
LYS   CD  HD3  sing N N 264 
LYS   CE  NZ   sing N N 265 
LYS   CE  HE2  sing N N 266 
LYS   CE  HE3  sing N N 267 
LYS   NZ  HZ1  sing N N 268 
LYS   NZ  HZ2  sing N N 269 
LYS   NZ  HZ3  sing N N 270 
LYS   OXT HXT  sing N N 271 
MET   N   CA   sing N N 272 
MET   N   H    sing N N 273 
MET   N   H2   sing N N 274 
MET   CA  C    sing N N 275 
MET   CA  CB   sing N N 276 
MET   CA  HA   sing N N 277 
MET   C   O    doub N N 278 
MET   C   OXT  sing N N 279 
MET   CB  CG   sing N N 280 
MET   CB  HB2  sing N N 281 
MET   CB  HB3  sing N N 282 
MET   CG  SD   sing N N 283 
MET   CG  HG2  sing N N 284 
MET   CG  HG3  sing N N 285 
MET   SD  CE   sing N N 286 
MET   CE  HE1  sing N N 287 
MET   CE  HE2  sing N N 288 
MET   CE  HE3  sing N N 289 
MET   OXT HXT  sing N N 290 
PHE   N   CA   sing N N 291 
PHE   N   H    sing N N 292 
PHE   N   H2   sing N N 293 
PHE   CA  C    sing N N 294 
PHE   CA  CB   sing N N 295 
PHE   CA  HA   sing N N 296 
PHE   C   O    doub N N 297 
PHE   C   OXT  sing N N 298 
PHE   CB  CG   sing N N 299 
PHE   CB  HB2  sing N N 300 
PHE   CB  HB3  sing N N 301 
PHE   CG  CD1  doub Y N 302 
PHE   CG  CD2  sing Y N 303 
PHE   CD1 CE1  sing Y N 304 
PHE   CD1 HD1  sing N N 305 
PHE   CD2 CE2  doub Y N 306 
PHE   CD2 HD2  sing N N 307 
PHE   CE1 CZ   doub Y N 308 
PHE   CE1 HE1  sing N N 309 
PHE   CE2 CZ   sing Y N 310 
PHE   CE2 HE2  sing N N 311 
PHE   CZ  HZ   sing N N 312 
PHE   OXT HXT  sing N N 313 
PRO   N   CA   sing N N 314 
PRO   N   CD   sing N N 315 
PRO   N   H    sing N N 316 
PRO   CA  C    sing N N 317 
PRO   CA  CB   sing N N 318 
PRO   CA  HA   sing N N 319 
PRO   C   O    doub N N 320 
PRO   C   OXT  sing N N 321 
PRO   CB  CG   sing N N 322 
PRO   CB  HB2  sing N N 323 
PRO   CB  HB3  sing N N 324 
PRO   CG  CD   sing N N 325 
PRO   CG  HG2  sing N N 326 
PRO   CG  HG3  sing N N 327 
PRO   CD  HD2  sing N N 328 
PRO   CD  HD3  sing N N 329 
PRO   OXT HXT  sing N N 330 
SER   N   CA   sing N N 331 
SER   N   H    sing N N 332 
SER   N   H2   sing N N 333 
SER   CA  C    sing N N 334 
SER   CA  CB   sing N N 335 
SER   CA  HA   sing N N 336 
SER   C   O    doub N N 337 
SER   C   OXT  sing N N 338 
SER   CB  OG   sing N N 339 
SER   CB  HB2  sing N N 340 
SER   CB  HB3  sing N N 341 
SER   OG  HG   sing N N 342 
SER   OXT HXT  sing N N 343 
THR   N   CA   sing N N 344 
THR   N   H    sing N N 345 
THR   N   H2   sing N N 346 
THR   CA  C    sing N N 347 
THR   CA  CB   sing N N 348 
THR   CA  HA   sing N N 349 
THR   C   O    doub N N 350 
THR   C   OXT  sing N N 351 
THR   CB  OG1  sing N N 352 
THR   CB  CG2  sing N N 353 
THR   CB  HB   sing N N 354 
THR   OG1 HG1  sing N N 355 
THR   CG2 HG21 sing N N 356 
THR   CG2 HG22 sing N N 357 
THR   CG2 HG23 sing N N 358 
THR   OXT HXT  sing N N 359 
TRP   N   CA   sing N N 360 
TRP   N   H    sing N N 361 
TRP   N   H2   sing N N 362 
TRP   CA  C    sing N N 363 
TRP   CA  CB   sing N N 364 
TRP   CA  HA   sing N N 365 
TRP   C   O    doub N N 366 
TRP   C   OXT  sing N N 367 
TRP   CB  CG   sing N N 368 
TRP   CB  HB2  sing N N 369 
TRP   CB  HB3  sing N N 370 
TRP   CG  CD1  doub Y N 371 
TRP   CG  CD2  sing Y N 372 
TRP   CD1 NE1  sing Y N 373 
TRP   CD1 HD1  sing N N 374 
TRP   CD2 CE2  doub Y N 375 
TRP   CD2 CE3  sing Y N 376 
TRP   NE1 CE2  sing Y N 377 
TRP   NE1 HE1  sing N N 378 
TRP   CE2 CZ2  sing Y N 379 
TRP   CE3 CZ3  doub Y N 380 
TRP   CE3 HE3  sing N N 381 
TRP   CZ2 CH2  doub Y N 382 
TRP   CZ2 HZ2  sing N N 383 
TRP   CZ3 CH2  sing Y N 384 
TRP   CZ3 HZ3  sing N N 385 
TRP   CH2 HH2  sing N N 386 
TRP   OXT HXT  sing N N 387 
TYR   N   CA   sing N N 388 
TYR   N   H    sing N N 389 
TYR   N   H2   sing N N 390 
TYR   CA  C    sing N N 391 
TYR   CA  CB   sing N N 392 
TYR   CA  HA   sing N N 393 
TYR   C   O    doub N N 394 
TYR   C   OXT  sing N N 395 
TYR   CB  CG   sing N N 396 
TYR   CB  HB2  sing N N 397 
TYR   CB  HB3  sing N N 398 
TYR   CG  CD1  doub Y N 399 
TYR   CG  CD2  sing Y N 400 
TYR   CD1 CE1  sing Y N 401 
TYR   CD1 HD1  sing N N 402 
TYR   CD2 CE2  doub Y N 403 
TYR   CD2 HD2  sing N N 404 
TYR   CE1 CZ   doub Y N 405 
TYR   CE1 HE1  sing N N 406 
TYR   CE2 CZ   sing Y N 407 
TYR   CE2 HE2  sing N N 408 
TYR   CZ  OH   sing N N 409 
TYR   OH  HH   sing N N 410 
TYR   OXT HXT  sing N N 411 
VAL   N   CA   sing N N 412 
VAL   N   H    sing N N 413 
VAL   N   H2   sing N N 414 
VAL   CA  C    sing N N 415 
VAL   CA  CB   sing N N 416 
VAL   CA  HA   sing N N 417 
VAL   C   O    doub N N 418 
VAL   C   OXT  sing N N 419 
VAL   CB  CG1  sing N N 420 
VAL   CB  CG2  sing N N 421 
VAL   CB  HB   sing N N 422 
VAL   CG1 HG11 sing N N 423 
VAL   CG1 HG12 sing N N 424 
VAL   CG1 HG13 sing N N 425 
VAL   CG2 HG21 sing N N 426 
VAL   CG2 HG22 sing N N 427 
VAL   CG2 HG23 sing N N 428 
VAL   OXT HXT  sing N N 429 
# 
_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                    7I7I 
_atom_sites.fract_transf_matrix[1][1]   0.011567 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000951 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017397 
_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]   0.015520 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.380 8.213   24.746 1.00 16.87 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.619 8.361   23.984 1.00 16.71 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 18.817 7.129   23.093 1.00 16.30 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.136 6.104   23.280 1.00 16.77 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 19.810 8.517   24.928 1.00 20.41 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 19.935 7.338   25.699 1.00 24.62 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.714 7.221   22.111 1.00 14.36 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.013 6.084   21.239 1.00 13.01 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.463 6.536   19.860 1.00 12.03 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.177 7.667   19.455 1.00 13.50 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.141 5.659   19.153 1.00 10.95 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.663 5.996   17.833 1.00 11.59 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.672 4.780   16.917 1.00 11.53 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.573 3.645   17.386 1.00 13.18 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.100 6.516   17.995 1.00 12.81 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.735 5.016   15.608 1.00 10.30 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 21.984 3.943   14.645 1.00 10.35 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.456 4.043   14.285 1.00 11.13 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 23.937 5.146   13.955 1.00 11.61 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.152 4.106   13.357 1.00 10.80 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.630 4.242   13.653 1.00 11.69 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.416 2.918   12.418 1.00 11.34 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.874 4.826   12.409 1.00 12.38 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.184 2.891   14.254 1.00 11.09 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.599 2.886   13.862 1.00 12.16 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.724 2.039   12.591 1.00 11.91 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.732 0.799   12.650 1.00 12.31 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.478 2.316   14.992 1.00 13.19 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.494 3.216   16.211 1.00 13.19 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.320 4.334   16.268 1.00 13.78 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.636 2.989   17.279 1.00 13.91 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.317 5.182   17.375 1.00 13.58 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.629 3.832   18.392 1.00 14.85 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.460 4.937   18.422 1.00 14.42 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.453 5.804   19.508 1.00 15.94 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.808 2.695   11.439 1.00 12.63 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.924 2.058   10.135 1.00 12.84 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.156 2.555   9.444  1.00 13.88 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.377 3.755   9.365  1.00 13.13 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.629 2.273   9.275  1.00 14.74 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.236 3.758   9.182  1.00 15.85 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.827 1.678   7.888  1.00 15.84 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.024 1.644   8.993  1.00 14.95 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.264 2.072   8.352  1.00 14.48 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.076 2.968   9.289  1.00 13.92 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.168 2.666   10.494 1.00 14.42 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.520 4.136   8.772  1.00 14.03 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.198 5.124   9.612  1.00 14.27 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.277 6.306   9.903  1.00 13.16 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.750 7.448   10.024 1.00 13.84 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.542 5.568   9.019  1.00 15.44 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.598 4.488   9.152  1.00 19.63 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.368 4.438   10.113 1.00 22.46 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.636 3.588   8.209  1.00 17.86 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 28.985 5.996   10.142 1.00 12.04 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.014 7.032   10.465 1.00 11.71 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.338 6.716   11.802 1.00 11.63 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.064 5.543   12.115 1.00 12.40 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.923 7.084   9.361  1.00 12.31 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.438 7.472   7.995  1.00 13.16 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.094 8.680   7.792  1.00 14.59 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.267 6.630   6.903  1.00 14.58 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.555 9.050   6.531  1.00 15.87 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.669 7.020   5.629  1.00 15.44 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.324 8.222   5.453  1.00 16.03 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.785 8.614   4.193  1.00 19.60 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 26.943 7.784   12.525 1.00 11.33 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.147 7.703   13.745 1.00 11.28 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 24.924 8.568   13.466 1.00 11.29 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.068 9.774   13.169 1.00 11.43 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 26.971 8.239   14.958 1.00 12.06 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.140 8.613   16.197 1.00 12.60 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.059 8.981   17.381 1.00 13.40 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.506 10.046  18.218 1.00 14.12 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 25.821 9.851   19.335 1.00 16.96 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.561 8.614   19.754 1.00 17.28 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.358 10.891  20.024 1.00 16.10 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.736 7.951   13.501 1.00 10.47 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.474 8.663   13.219 1.00 9.53  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.759 8.888   14.534 1.00 10.78 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.446 7.897   15.226 1.00 11.56 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.545 7.850   12.283 1.00 10.61 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.336 8.712   11.874 1.00 11.76 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.265 7.351   11.034 1.00 10.95 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.488 10.145  14.886 1.00 9.56  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 20.810 10.492  16.150 1.00 9.95  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 19.683 11.454  15.918 1.00 10.88 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.568 12.064  14.845 1.00 11.58 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 21.824 11.144  17.148 1.00 11.35 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 22.811 10.112  17.611 1.00 14.01 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 22.533 12.382  16.555 1.00 12.84 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 18.844 11.668  16.963 1.00 11.02 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 17.843 12.725  16.887 1.00 11.34 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 18.622 14.031  16.911 1.00 12.12 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 19.509 14.209  17.761 1.00 11.93 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 16.963 12.687  18.140 1.00 11.39 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.120 11.444  18.226 1.00 11.20 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 16.529 10.456  18.878 1.00 13.17 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 14.967 11.475  17.583 1.00 11.96 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.289 14.949  15.993 1.00 10.54 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 18.995 16.243  15.964 1.00 11.07 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 18.899 16.937  17.320 1.00 12.71 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 19.873 17.517  17.776 1.00 12.90 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.396 17.122  14.845 1.00 11.05 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.209 18.422  14.597 1.00 12.23 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.432 19.301  13.617 1.00 12.44 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.191 20.490  13.177 1.00 14.53 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.176 21.660  13.809 1.00 17.34 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.575 21.778  14.980 1.00 18.70 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.785 22.725  13.273 1.00 18.66 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 17.748 16.832  17.993 1.00 13.03 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 17.566 17.543  19.258 1.00 13.87 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 18.390 16.966  20.414 1.00 14.49 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 18.482 17.605  21.473 1.00 14.77 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.064 17.690  19.605 1.00 13.17 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 15.394 16.452  20.154 1.00 12.75 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 14.788 15.540  19.309 1.00 13.58 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 15.130 16.095  21.447 1.00 13.08 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 14.281 14.589  20.091 1.00 13.87 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 14.430 14.894  21.396 1.00 12.96 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 18.960 15.766  20.254 1.00 13.64 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 19.818 15.134  21.259 1.00 13.46 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 21.288 15.054  20.833 1.00 14.22 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 22.101 14.448  21.529 1.00 15.07 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 19.309 13.738  21.614 1.00 13.45 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 17.872 13.713  22.110 1.00 15.44 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 17.437 12.284  22.385 1.00 16.13 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 17.707 14.530  23.434 1.00 16.44 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 21.655 15.687  19.683 1.00 13.59 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.040 15.630  19.230 1.00 13.46 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 23.990 16.268  20.239 1.00 14.98 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 23.657 17.306  20.843 1.00 15.65 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.164 16.315  17.869 1.00 13.32 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 25.157 15.668  20.398 1.00 13.58 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 26.183 16.198  21.319 1.00 14.58 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.091 17.198  20.603 1.00 15.23 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.059 17.321  19.357 1.00 14.41 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 27.059 15.032  21.838 1.00 16.28 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 27.836 14.505  20.741 1.00 17.10 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 26.261 13.924  22.504 1.00 17.92 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 27.982 17.876  21.371 1.00 15.52 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 28.948 18.742  20.751 1.00 14.84 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 29.880 17.975  19.812 1.00 15.20 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.182 18.456  18.703 1.00 15.13 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 29.743 19.522  21.806 1.00 16.79 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.623 20.499  21.128 1.00 26.31 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.081 21.509  20.347 1.00 30.91 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 31.956 20.503  20.992 1.00 28.98 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 31.114 22.153  19.834 1.00 31.77 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 32.261 21.590  20.190 1.00 30.80 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.259 16.740  20.184 1.00 14.40 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.109 15.946  19.312 1.00 15.42 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.402 15.622  17.993 1.00 14.40 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.031 15.618  16.936 1.00 14.26 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 31.566 14.632  19.962 1.00 17.99 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 32.595 13.926  19.126 1.00 26.29 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 33.750 14.389  19.020 1.00 30.19 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.175 12.848  18.439 1.00 28.23 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.071 15.375  18.023 1.00 13.43 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.313 15.141  16.787 1.00 13.36 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.392 16.401  15.873 1.00 12.25 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.646 16.282  14.672 1.00 12.54 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 26.826 14.875  17.095 1.00 12.67 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 26.571 13.510  17.693 1.00 14.40 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.254 12.541  17.275 1.00 13.88 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 25.717 13.413  18.605 1.00 14.12 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.162 17.587  16.435 1.00 12.60 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.242 18.816  15.648 1.00 12.83 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.638 19.103  15.107 1.00 13.67 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.751 19.659  14.006 1.00 14.01 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.726 20.016  16.487 1.00 12.74 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.224 20.096  16.579 1.00 13.39 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.423 19.780  17.646 1.00 14.13 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.343 20.534  15.537 1.00 13.68 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.097 19.993  17.320 1.00 14.24 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.021 20.415  16.015 1.00 13.86 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.546 20.956  14.218 1.00 15.58 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 22.918 20.834  15.252 1.00 15.22 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.456 21.298  13.454 1.00 16.05 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.167 21.238  13.964 1.00 16.49 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.688 18.724  15.857 1.00 13.25 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.070 18.922  15.433 1.00 13.91 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.524 17.904  14.387 1.00 15.46 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.550 18.091  13.762 1.00 16.63 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 32.979 18.905  16.668 1.00 15.34 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.719 16.842  14.163 1.00 13.97 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.057 15.797  13.165 1.00 13.71 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.825 15.582  12.282 1.00 13.42 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.474 14.456  11.945 1.00 13.33 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.412 14.484  13.908 1.00 15.54 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.744 14.651  14.595 1.00 18.62 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.795 14.588  13.949 1.00 20.09 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.729 14.977  15.897 1.00 18.49 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.165 16.673  11.901 1.00 13.11 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.888 16.647  11.209 1.00 12.37 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.970 16.181  9.778  1.00 12.96 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.833 16.665  9.018  1.00 14.83 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.272 18.083  11.249 1.00 12.34 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.901 18.221  10.615 1.00 13.61 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.850 17.421  11.402 1.00 13.43 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.436 19.687  10.568 1.00 14.96 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 28.058 15.272  9.368  1.00 12.74 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.915 14.874  7.981  1.00 13.46 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.673 15.560  7.377  1.00 14.24 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.743 16.101  6.266  1.00 14.88 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.818 13.335  7.869  1.00 13.07 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.480 12.912  6.428  1.00 14.26 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 29.102 12.664  8.381  1.00 14.01 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.516 15.519  8.065  1.00 13.10 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 24.264 16.017  7.512  1.00 13.09 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.292 16.233  8.631  1.00 12.97 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.329 15.473  9.606  1.00 13.45 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.692 14.998  6.489  1.00 14.08 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 22.290 15.250  6.012  1.00 14.72 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.892 16.089  5.008  1.00 17.05 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 21.091 14.638  6.525  1.00 14.72 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 20.516 16.008  4.847  1.00 19.00 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 20.004 15.135  5.776  1.00 17.11 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.840 13.707  7.526  1.00 14.83 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.691 14.664  5.960  1.00 17.21 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.553 13.238  7.695  1.00 15.44 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.483 13.754  6.958  1.00 16.06 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.457 17.278  8.552  1.00 13.98 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.407 17.491  9.547  1.00 14.47 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 20.178 18.106  8.911  1.00 15.47 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 20.285 18.859  7.942  1.00 15.39 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.887 18.309  10.734 1.00 15.21 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.488 19.675  10.367 1.00 14.60 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.518 20.830  10.112 1.00 17.35 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.872 21.779  9.363  1.00 18.15 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.401 20.818  10.681 1.00 16.71 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.994 17.821  9.455  1.00 13.15 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.757 18.361  8.909  1.00 13.32 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.791 18.535  10.058 1.00 13.86 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.279 17.547  10.606 1.00 13.61 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 17.194 17.411  7.817  1.00 15.71 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.973 17.914  7.104  1.00 19.24 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 15.174 18.602  7.737  1.00 22.17 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.799 17.575  5.910  1.00 22.04 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.535 19.783  10.457 1.00 13.56 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.637 20.078  11.560 0.50 14.32 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.640 20.043  11.577 0.50 14.60 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.199 19.638  11.257 1.00 14.57 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.482 19.168  12.171 1.00 14.24 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.695 21.576  11.879 0.50 16.28 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.729 21.507  12.008 0.50 17.47 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.638 21.989  12.726 0.50 18.53 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.366 22.345  10.929 0.50 21.17 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.765 19.770  9.985  1.00 14.18 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.398 19.344  9.639  1.00 14.69 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.176 17.851  9.814  1.00 14.60 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.038 17.448  9.919  1.00 15.28 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 12.016 19.764  8.221  1.00 16.15 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.617 18.966  7.216  1.00 20.85 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.234 17.038  9.849  1.00 12.58 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.099 15.592  10.055 1.00 12.06 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.544 15.152  11.469 1.00 11.68 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.478 13.958  11.787 1.00 11.40 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.970 14.852  9.033  1.00 12.61 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.434 14.994  7.595  1.00 13.14 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.317 14.276  6.564  1.00 12.73 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.252 12.826  6.724  1.00 12.73 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.441 11.956  5.742  1.00 14.18 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.673 12.382  4.499  1.00 15.72 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.334 10.647  5.971  1.00 12.50 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.118 16.073  12.288 1.00 11.18 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.714 15.726  13.583 1.00 10.65 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 15.844 14.736  13.460 1.00 11.41 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.056 13.924  14.347 1.00 11.06 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.690 15.246  14.631 1.00 11.92 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.264 15.043  16.023 1.00 12.35 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.066 15.907  16.476 1.00 12.55 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 13.859 14.037  16.702 1.00 11.86 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.664 14.874  12.393 1.00 10.60 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.779 13.946  12.219 1.00 10.47 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.123 14.646  12.118 1.00 11.43 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.203 15.756  11.550 1.00 11.69 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.588 13.115  10.939 1.00 10.85 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.509 12.002  10.968 1.00 11.19 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.466 11.264  9.620  1.00 12.72 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.786 11.031  12.111 1.00 11.73 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.158 13.999  12.626 1.00 10.62 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.526 14.472  12.455 1.00 10.95 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.420 13.260  12.313 1.00 11.39 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.234 12.241  12.997 1.00 11.75 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 21.974 15.349  13.650 1.00 10.63 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.428 15.924  13.612 1.00 11.95 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.500 17.316  14.288 1.00 13.18 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.463 14.964  14.240 1.00 10.98 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.399 13.327  11.384 1.00 11.16 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.344 12.245  11.184 1.00 10.46 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.757 12.768  11.353 1.00 11.13 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.087 13.822  10.779 1.00 12.20 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.164 11.636  9.775  1.00 10.65 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.220 10.562  9.531  1.00 12.44 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.747 11.062  9.577  1.00 11.71 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.562 12.105  12.185 1.00 10.95 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.965 12.454  12.404 1.00 11.01 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.878 11.288  11.955 1.00 12.51 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.414 10.145  11.743 1.00 12.15 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.207 12.835  13.865 1.00 12.14 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 27.877 11.774  14.746 1.00 13.56 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.176 11.568  11.809 1.00 13.41 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.112 10.534  11.382 1.00 14.13 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.731 9.813   12.594 1.00 15.05 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 31.891 10.421  13.682 1.00 16.67 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.199 11.150  10.506 1.00 16.79 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.915 12.126  11.245 1.00 18.99 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.077 8.514   12.409 1.00 15.18 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.669 7.713   13.481 1.00 16.70 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.010 7.139   13.050 1.00 18.24 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.245 6.925   11.845 1.00 18.38 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 31.740 6.540   13.864 1.00 17.29 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 31.638 5.627   12.770 1.00 18.56 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.335 7.009   14.209 1.00 17.44 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 34.858 6.822   14.035 1.00 19.39 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.135 6.189   13.715 1.00 21.31 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 35.918 4.680   13.524 1.00 21.94 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.456 4.099   12.575 1.00 23.55 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.177 6.498   14.814 1.00 24.67 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 36.670 6.032   16.059 1.00 29.41 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.437 7.979   14.951 1.00 25.53 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.120 4.057   14.400 1.00 21.47 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 34.867 2.611   14.276 1.00 22.39 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 33.660 2.313   13.375 1.00 21.19 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 32.709 3.103   13.328 1.00 20.69 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 34.626 2.007   15.654 1.00 25.01 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 33.655 1.162   12.710 1.00 20.50 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 32.542 0.731   11.869 1.00 20.74 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.422 0.171   12.711 1.00 19.66 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 31.665 -0.542  13.699 1.00 20.64 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.013 -0.318  10.852 1.00 23.90 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.890 0.292   9.746  1.00 30.06 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 34.312 -0.754  8.742  1.00 35.21 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 35.125 -1.630  9.027  1.00 34.55 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 33.755 -0.692  7.540  1.00 37.70 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.189 0.519   12.341 1.00 16.41 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.005 0.061   13.052 1.00 16.24 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.444 -1.222  12.488 1.00 15.07 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 28.754 -1.606  11.366 1.00 15.76 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 27.508 -1.829  13.243 1.00 14.08 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 26.934 -3.129  12.841 1.00 15.44 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 25.504 -3.119  12.416 1.00 15.54 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 24.969 -4.179  12.054 1.00 16.73 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 27.128 -4.151  13.953 1.00 16.14 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 28.856 -4.564  14.284 1.00 21.41 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 24.850 -1.964  12.460 1.00 13.40 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.456 -1.896  12.036 1.00 12.58 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.375 -1.838  10.512 1.00 13.75 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.238 -1.241  9.842  1.00 15.40 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 22.784 -0.663  12.648 1.00 12.73 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 22.664 -0.694  14.168 1.00 14.60 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 22.343 -1.782  14.718 1.00 15.00 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 22.847 0.378   14.813 1.00 13.77 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.345 -2.433  9.968  1.00 14.01 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.092 -2.338  8.505  1.00 15.45 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.781 -1.597  8.328  1.00 14.99 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.858 -1.799  9.130  1.00 16.07 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.981 -3.723  7.881  1.00 18.97 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 20.919 -4.391  8.501  1.00 25.31 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 23.267 -4.539  8.063  1.00 19.14 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.676 -0.742  7.298  1.00 14.08 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.443 -0.013  7.067  1.00 13.05 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.492 -0.831  6.183  1.00 13.80 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.891 -1.375  5.130  1.00 13.90 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.729 1.380   6.430  1.00 13.00 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.829 2.171   7.187  1.00 13.64 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.443 2.213   6.264  1.00 13.22 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.428 2.484   8.686  1.00 14.61 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.222 -0.877  6.556  1.00 12.36 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 16.179 -1.509  5.776  1.00 12.32 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.938 -0.679  4.485  1.00 13.61 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.898 0.574   4.481  1.00 12.98 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.867 -1.552  6.571  1.00 13.38 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.774 -1.402  3.360  1.00 13.98 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 15.447 -0.748  2.086  1.00 14.76 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 14.207 -1.505  1.598  1.00 16.79 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 14.294 -2.399  0.740  1.00 17.41 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 16.648 -0.826  1.077  1.00 16.43 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.959 -0.239  1.622  1.00 16.37 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.896 1.288   1.853  1.00 14.22 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 19.167 1.809   2.361  1.00 13.18 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 19.321 2.974   2.978  1.00 15.38 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 18.304 3.804   3.098  1.00 14.64 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.514 3.330   3.469  1.00 16.84 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 13.044 -1.097  2.083  1.00 15.25 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.816 -1.872  1.932  1.00 15.94 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 10.576 -0.989  2.125  1.00 16.67 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.645 0.190   2.438  1.00 17.51 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.818 -2.979  2.985  1.00 15.75 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.656 -2.322  4.667  1.00 15.08 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 9.388  -1.645  2.025  1.00 18.72 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 8.135  -0.963  2.269  1.00 20.29 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 7.381  -1.534  3.462  1.00 20.39 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 6.167  -1.414  3.507  1.00 20.64 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 7.222  -1.035  1.010  1.00 26.12 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 6.835  -2.414  0.540  1.00 36.74 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 7.294  -3.398  1.139  1.00 38.63 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 6.081  -2.515  -0.462 1.00 42.05 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 8.071  -2.100  4.433  1.00 18.55 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.393  -2.631  5.628  1.00 16.83 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.628  -1.539  6.370  1.00 16.67 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 7.124  -0.420  6.533  1.00 17.51 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.391  -3.310  6.560  1.00 17.60 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 9.093  -4.879  5.951  1.00 17.42 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.437  -1.877  6.870  1.00 14.33 ? 59  GLN   A N   1 
ATOM   407  C  CA  A GLN   A 1 53  ? 4.705  -0.964  7.724  0.50 13.88 ? 59  GLN   A CA  1 
ATOM   408  C  CA  B GLN   A 1 53  ? 4.586  -1.005  7.708  0.50 14.26 ? 59  GLN   A CA  1 
ATOM   409  C  C   . GLN   A 1 53  ? 4.316  -1.687  9.071  1.00 13.57 ? 59  GLN   A C   1 
ATOM   410  O  O   . GLN   A 1 53  ? 3.452  -1.253  9.833  1.00 14.86 ? 59  GLN   A O   1 
ATOM   411  C  CB  A GLN   A 1 53  ? 3.573  -0.272  6.959  0.50 14.74 ? 59  GLN   A CB  1 
ATOM   412  C  CB  B GLN   A 1 53  ? 3.231  -0.630  7.049  0.50 15.85 ? 59  GLN   A CB  1 
ATOM   413  C  CG  A GLN   A 1 53  ? 4.115  0.559   5.744  0.50 13.98 ? 59  GLN   A CG  1 
ATOM   414  C  CG  B GLN   A 1 53  ? 3.199  0.687   6.220  0.50 17.28 ? 59  GLN   A CG  1 
ATOM   415  C  CD  A GLN   A 1 53  ? 5.022  1.730   6.157  0.50 14.12 ? 59  GLN   A CD  1 
ATOM   416  C  CD  B GLN   A 1 53  ? 1.790  1.209   5.905  0.50 18.38 ? 59  GLN   A CD  1 
ATOM   417  O  OE1 A GLN   A 1 53  ? 5.984  2.141   5.458  0.50 12.73 ? 59  GLN   A OE1 1 
ATOM   418  O  OE1 B GLN   A 1 53  ? 1.272  1.078   4.780  0.50 19.89 ? 59  GLN   A OE1 1 
ATOM   419  N  NE2 A GLN   A 1 53  ? 4.729  2.327   7.302  0.50 13.25 ? 59  GLN   A NE2 1 
ATOM   420  N  NE2 B GLN   A 1 53  ? 1.118  1.822   6.876  0.50 16.34 ? 59  GLN   A NE2 1 
ATOM   421  N  N   . THR   A 1 54  ? 5.038  -2.790  9.370  1.00 12.64 ? 60  THR   A N   1 
ATOM   422  C  CA  . THR   A 1 54  ? 5.005  -3.468  10.641 1.00 12.33 ? 60  THR   A CA  1 
ATOM   423  C  C   . THR   A 1 54  ? 6.451  -3.747  11.064 1.00 12.62 ? 60  THR   A C   1 
ATOM   424  O  O   . THR   A 1 54  ? 7.336  -3.966  10.204 1.00 13.64 ? 60  THR   A O   1 
ATOM   425  C  CB  . THR   A 1 54  ? 4.197  -4.749  10.669 1.00 15.02 ? 60  THR   A CB  1 
ATOM   426  O  OG1 . THR   A 1 54  ? 4.804  -5.712  9.839  1.00 21.00 ? 60  THR   A OG1 1 
ATOM   427  C  CG2 . THR   A 1 54  ? 2.763  -4.559  10.285 1.00 15.18 ? 60  THR   A CG2 1 
ATOM   428  N  N   . GLY   A 1 55  ? 6.706  -3.668  12.337 1.00 10.41 ? 61  GLY   A N   1 
ATOM   429  C  CA  . GLY   A 1 55  ? 8.060  -3.868  12.846 1.00 10.85 ? 61  GLY   A CA  1 
ATOM   430  C  C   . GLY   A 1 55  ? 8.053  -3.861  14.354 1.00 11.16 ? 61  GLY   A C   1 
ATOM   431  O  O   . GLY   A 1 55  ? 7.017  -4.112  14.968 1.00 11.84 ? 61  GLY   A O   1 
ATOM   432  N  N   . VAL   A 1 56  ? 9.260  -3.687  14.940 1.00 10.06 ? 62  VAL   A N   1 
ATOM   433  C  CA  . VAL   A 1 56  ? 9.417  -3.716  16.388 1.00 9.92  ? 62  VAL   A CA  1 
ATOM   434  C  C   . VAL   A 1 56  ? 10.282 -2.554  16.822 1.00 10.03 ? 62  VAL   A C   1 
ATOM   435  O  O   . VAL   A 1 56  ? 11.239 -2.224  16.128 1.00 11.30 ? 62  VAL   A O   1 
ATOM   436  C  CB  . VAL   A 1 56  ? 10.103 -5.060  16.752 1.00 12.33 ? 62  VAL   A CB  1 
ATOM   437  C  CG1 . VAL   A 1 56  ? 10.476 -5.121  18.221 1.00 14.61 ? 62  VAL   A CG1 1 
ATOM   438  C  CG2 . VAL   A 1 56  ? 9.193  -6.257  16.406 1.00 13.20 ? 62  VAL   A CG2 1 
ATOM   439  N  N   . TYR   A 1 57  ? 9.885  -1.834  17.904 1.00 9.41  ? 63  TYR   A N   1 
ATOM   440  C  CA  . TYR   A 1 57  ? 10.731 -0.739  18.380 1.00 9.02  ? 63  TYR   A CA  1 
ATOM   441  C  C   . TYR   A 1 57  ? 11.157 -0.944  19.838 1.00 10.00 ? 63  TYR   A C   1 
ATOM   442  O  O   . TYR   A 1 57  ? 10.451 -1.564  20.628 1.00 10.75 ? 63  TYR   A O   1 
ATOM   443  C  CB  . TYR   A 1 57  ? 10.028 0.652   18.243 1.00 10.22 ? 63  TYR   A CB  1 
ATOM   444  C  CG  . TYR   A 1 57  ? 9.026  1.029   19.342 1.00 9.65  ? 63  TYR   A CG  1 
ATOM   445  C  CD1 . TYR   A 1 57  ? 7.746  0.481   19.358 1.00 10.70 ? 63  TYR   A CD1 1 
ATOM   446  C  CD2 . TYR   A 1 57  ? 9.370  1.931   20.345 1.00 10.94 ? 63  TYR   A CD2 1 
ATOM   447  C  CE1 . TYR   A 1 57  ? 6.829  0.834   20.334 1.00 11.78 ? 63  TYR   A CE1 1 
ATOM   448  C  CE2 . TYR   A 1 57  ? 8.450  2.295   21.321 1.00 11.98 ? 63  TYR   A CE2 1 
ATOM   449  C  CZ  . TYR   A 1 57  ? 7.195  1.736   21.295 1.00 12.75 ? 63  TYR   A CZ  1 
ATOM   450  O  OH  . TYR   A 1 57  ? 6.267  2.036   22.253 1.00 13.86 ? 63  TYR   A OH  1 
ATOM   451  N  N   . TYR   A 1 58  ? 12.286 -0.336  20.205 1.00 9.85  ? 64  TYR   A N   1 
ATOM   452  C  CA  . TYR   A 1 58  ? 12.760 -0.347  21.587 1.00 9.87  ? 64  TYR   A CA  1 
ATOM   453  C  C   . TYR   A 1 58  ? 12.265 0.863   22.374 1.00 9.39  ? 64  TYR   A C   1 
ATOM   454  O  O   . TYR   A 1 58  ? 12.484 2.004   21.995 1.00 10.17 ? 64  TYR   A O   1 
ATOM   455  C  CB  . TYR   A 1 58  ? 14.309 -0.411  21.627 1.00 10.77 ? 64  TYR   A CB  1 
ATOM   456  C  CG  . TYR   A 1 58  ? 14.813 -0.557  23.041 1.00 11.95 ? 64  TYR   A CG  1 
ATOM   457  C  CD1 . TYR   A 1 58  ? 14.509 -1.674  23.787 1.00 12.31 ? 64  TYR   A CD1 1 
ATOM   458  C  CD2 . TYR   A 1 58  ? 15.510 0.482   23.667 1.00 11.93 ? 64  TYR   A CD2 1 
ATOM   459  C  CE1 . TYR   A 1 58  ? 14.890 -1.775  25.125 1.00 13.12 ? 64  TYR   A CE1 1 
ATOM   460  C  CE2 . TYR   A 1 58  ? 15.899 0.396   24.996 1.00 12.29 ? 64  TYR   A CE2 1 
ATOM   461  C  CZ  . TYR   A 1 58  ? 15.631 -0.753  25.698 1.00 12.80 ? 64  TYR   A CZ  1 
ATOM   462  O  OH  . TYR   A 1 58  ? 16.036 -0.852  27.037 1.00 15.32 ? 64  TYR   A OH  1 
ATOM   463  N  N   . CYS   A 1 59  ? 11.642 0.559   23.501 1.00 9.86  ? 65  CYS   A N   1 
ATOM   464  C  CA  . CYS   A 1 59  ? 11.117 1.559   24.445 1.00 11.10 ? 65  CYS   A CA  1 
ATOM   465  C  C   . CYS   A 1 59  ? 11.945 1.549   25.707 1.00 11.42 ? 65  CYS   A C   1 
ATOM   466  O  O   . CYS   A 1 59  ? 11.772 0.664   26.573 1.00 11.89 ? 65  CYS   A O   1 
ATOM   467  C  CB  . CYS   A 1 59  ? 9.667  1.235   24.710 1.00 9.97  ? 65  CYS   A CB  1 
ATOM   468  S  SG  . CYS   A 1 59  ? 8.911  2.341   25.947 1.00 12.27 ? 65  CYS   A SG  1 
ATOM   469  N  N   . SER   A 1 60  ? 12.853 2.537   25.854 1.00 11.84 ? 66  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 60  ? 13.736 2.571   27.022 1.00 12.43 ? 66  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 60  ? 13.021 2.729   28.372 1.00 12.26 ? 66  SER   A C   1 
ATOM   472  O  O   . SER   A 1 60  ? 13.456 2.140   29.375 1.00 13.32 ? 66  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 60  ? 14.794 3.650   26.864 1.00 15.04 ? 66  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 60  ? 14.297 4.966   26.951 1.00 20.74 ? 66  SER   A OG  1 
ATOM   475  N  N   . SER   A 1 61  ? 11.876 3.462   28.387 1.00 11.16 ? 67  SER   A N   1 
ATOM   476  C  CA  . SER   A 1 61  ? 11.096 3.659   29.627 1.00 11.32 ? 67  SER   A CA  1 
ATOM   477  C  C   . SER   A 1 61  ? 10.327 2.435   30.081 1.00 11.49 ? 67  SER   A C   1 
ATOM   478  O  O   . SER   A 1 61  ? 9.761  2.451   31.145 1.00 11.49 ? 67  SER   A O   1 
ATOM   479  C  CB  . SER   A 1 61  ? 10.149 4.849   29.479 1.00 11.68 ? 67  SER   A CB  1 
ATOM   480  O  OG  . SER   A 1 61  ? 9.144  4.613   28.515 1.00 11.25 ? 67  SER   A OG  1 
ATOM   481  N  N   . ARG   A 1 62  ? 10.408 1.348   29.305 1.00 11.47 ? 68  ARG   A N   1 
ATOM   482  C  CA  . ARG   A 1 62  ? 9.841  0.049   29.675 1.00 11.27 ? 68  ARG   A CA  1 
ATOM   483  C  C   . ARG   A 1 62  ? 10.868 -1.079  29.600 1.00 12.98 ? 68  ARG   A C   1 
ATOM   484  O  O   . ARG   A 1 62  ? 10.528 -2.232  29.914 1.00 13.55 ? 68  ARG   A O   1 
ATOM   485  C  CB  . ARG   A 1 62  ? 8.641  -0.289  28.749 1.00 11.39 ? 68  ARG   A CB  1 
ATOM   486  C  CG  . ARG   A 1 62  ? 7.486  0.693   28.902 1.00 11.79 ? 68  ARG   A CG  1 
ATOM   487  C  CD  . ARG   A 1 62  ? 6.700  0.381   30.149 1.00 12.19 ? 68  ARG   A CD  1 
ATOM   488  N  NE  . ARG   A 1 62  ? 5.585  1.310   30.298 1.00 14.71 ? 68  ARG   A NE  1 
ATOM   489  C  CZ  . ARG   A 1 62  ? 5.633  2.462   30.976 1.00 14.18 ? 68  ARG   A CZ  1 
ATOM   490  N  NH1 . ARG   A 1 62  ? 6.781  2.895   31.490 1.00 13.67 ? 68  ARG   A NH1 1 
ATOM   491  N  NH2 . ARG   A 1 62  ? 4.538  3.216   31.104 1.00 15.64 ? 68  ARG   A NH2 1 
ATOM   492  N  N   . ARG   A 1 63  ? 12.087 -0.799  29.138 1.00 13.76 ? 69  ARG   A N   1 
ATOM   493  C  CA  . ARG   A 1 63  ? 13.096 -1.854  28.872 1.00 13.91 ? 69  ARG   A CA  1 
ATOM   494  C  C   . ARG   A 1 63  ? 12.489 -2.991  28.016 1.00 16.33 ? 69  ARG   A C   1 
ATOM   495  O  O   . ARG   A 1 63  ? 12.652 -4.196  28.314 1.00 17.53 ? 69  ARG   A O   1 
ATOM   496  C  CB  . ARG   A 1 63  ? 13.695 -2.457  30.137 1.00 16.09 ? 69  ARG   A CB  1 
ATOM   497  C  CG  . ARG   A 1 63  ? 14.599 -1.494  30.800 1.00 16.23 ? 69  ARG   A CG  1 
ATOM   498  C  CD  . ARG   A 1 63  ? 15.536 -2.303  31.727 1.00 17.74 ? 69  ARG   A CD  1 
ATOM   499  N  NE  . ARG   A 1 63  ? 16.316 -1.354  32.499 1.00 17.58 ? 69  ARG   A NE  1 
ATOM   500  C  CZ  . ARG   A 1 63  ? 16.009 -0.949  33.724 1.00 15.93 ? 69  ARG   A CZ  1 
ATOM   501  N  NH1 . ARG   A 1 63  ? 14.957 -1.465  34.366 1.00 17.99 ? 69  ARG   A NH1 1 
ATOM   502  N  NH2 . ARG   A 1 63  ? 16.769 -0.054  34.339 1.00 17.76 ? 69  ARG   A NH2 1 
ATOM   503  N  N   . LYS   A 1 64  ? 11.754 -2.614  26.988 1.00 14.38 ? 70  LYS   A N   1 
ATOM   504  C  CA  . LYS   A 1 64  ? 11.027 -3.611  26.209 1.00 13.94 ? 70  LYS   A CA  1 
ATOM   505  C  C   . LYS   A 1 64  ? 10.996 -3.288  24.745 1.00 13.14 ? 70  LYS   A C   1 
ATOM   506  O  O   . LYS   A 1 64  ? 10.915 -2.099  24.379 1.00 12.41 ? 70  LYS   A O   1 
ATOM   507  C  CB  . LYS   A 1 64  ? 9.566  -3.654  26.718 1.00 18.06 ? 70  LYS   A CB  1 
ATOM   508  C  CG  . LYS   A 1 64  ? 9.243  -4.810  27.679 1.00 29.86 ? 70  LYS   A CG  1 
ATOM   509  C  CD  . LYS   A 1 64  ? 7.725  -5.081  27.599 1.00 39.11 ? 70  LYS   A CD  1 
ATOM   510  C  CE  . LYS   A 1 64  ? 7.318  -6.548  27.654 1.00 45.07 ? 70  LYS   A CE  1 
ATOM   511  N  NZ  . LYS   A 1 64  ? 7.608  -7.275  26.375 1.00 46.98 ? 70  LYS   A NZ  1 
ATOM   512  N  N   . HIS   A 1 65  ? 11.001 -4.327  23.889 1.00 12.36 ? 71  HIS   A N   1 
ATOM   513  C  CA  . HIS   A 1 65  ? 10.786 -4.163  22.449 1.00 11.94 ? 71  HIS   A CA  1 
ATOM   514  C  C   . HIS   A 1 65  ? 9.303  -4.516  22.171 1.00 14.12 ? 71  HIS   A C   1 
ATOM   515  O  O   . HIS   A 1 65  ? 8.806  -5.565  22.609 1.00 17.38 ? 71  HIS   A O   1 
ATOM   516  C  CB  . HIS   A 1 65  ? 11.685 -5.123  21.667 1.00 11.15 ? 71  HIS   A CB  1 
ATOM   517  C  CG  . HIS   A 1 65  ? 13.141 -4.794  21.792 1.00 12.06 ? 71  HIS   A CG  1 
ATOM   518  N  ND1 . HIS   A 1 65  ? 13.832 -4.109  20.784 1.00 15.37 ? 71  HIS   A ND1 1 
ATOM   519  C  CD2 . HIS   A 1 65  ? 14.010 -5.112  22.774 1.00 11.71 ? 71  HIS   A CD2 1 
ATOM   520  C  CE1 . HIS   A 1 65  ? 15.107 -4.069  21.194 1.00 14.42 ? 71  HIS   A CE1 1 
ATOM   521  N  NE2 . HIS   A 1 65  ? 15.252 -4.643  22.367 1.00 15.67 ? 71  HIS   A NE2 1 
ATOM   522  N  N   . TYR   A 1 66  ? 8.590  -3.628  21.478 1.00 11.33 ? 72  TYR   A N   1 
ATOM   523  C  CA  . TYR   A 1 66  ? 7.167  -3.837  21.179 1.00 11.94 ? 72  TYR   A CA  1 
ATOM   524  C  C   . TYR   A 1 66  ? 6.905  -3.960  19.705 1.00 11.37 ? 72  TYR   A C   1 
ATOM   525  O  O   . TYR   A 1 66  ? 7.409  -3.134  18.933 1.00 10.91 ? 72  TYR   A O   1 
ATOM   526  C  CB  . TYR   A 1 66  ? 6.347  -2.583  21.665 1.00 12.92 ? 72  TYR   A CB  1 
ATOM   527  C  CG  . TYR   A 1 66  ? 6.271  -2.400  23.168 1.00 12.41 ? 72  TYR   A CG  1 
ATOM   528  C  CD1 . TYR   A 1 66  ? 5.472  -3.226  23.948 1.00 13.56 ? 72  TYR   A CD1 1 
ATOM   529  C  CD2 . TYR   A 1 66  ? 7.017  -1.430  23.803 1.00 12.25 ? 72  TYR   A CD2 1 
ATOM   530  C  CE1 . TYR   A 1 66  ? 5.331  -3.018  25.314 1.00 15.05 ? 72  TYR   A CE1 1 
ATOM   531  C  CE2 . TYR   A 1 66  ? 6.914  -1.226  25.183 1.00 13.87 ? 72  TYR   A CE2 1 
ATOM   532  C  CZ  . TYR   A 1 66  ? 6.097  -2.054  25.937 1.00 14.59 ? 72  TYR   A CZ  1 
ATOM   533  O  OH  . TYR   A 1 66  ? 5.985  -1.875  27.313 1.00 16.74 ? 72  TYR   A OH  1 
ATOM   534  N  N   . PRO   A 1 67  ? 6.083  -4.925  19.285 1.00 11.91 ? 73  PRO   A N   1 
ATOM   535  C  CA  . PRO   A 1 67  ? 5.686  -4.971  17.871 1.00 11.88 ? 73  PRO   A CA  1 
ATOM   536  C  C   . PRO   A 1 67  ? 4.658  -3.882  17.576 1.00 12.86 ? 73  PRO   A C   1 
ATOM   537  O  O   . PRO   A 1 67  ? 3.720  -3.689  18.386 1.00 16.03 ? 73  PRO   A O   1 
ATOM   538  C  CB  . PRO   A 1 67  ? 5.030  -6.349  17.700 1.00 13.55 ? 73  PRO   A CB  1 
ATOM   539  C  CG  . PRO   A 1 67  ? 4.632  -6.759  19.090 1.00 16.07 ? 73  PRO   A CG  1 
ATOM   540  C  CD  . PRO   A 1 67  ? 5.491  -6.017  20.095 1.00 12.53 ? 73  PRO   A CD  1 
ATOM   541  N  N   . VAL   A 1 68  ? 4.784  -3.224  16.431 1.00 11.61 ? 74  VAL   A N   1 
ATOM   542  C  CA  . VAL   A 1 68  ? 3.860  -2.146  16.065 1.00 13.05 ? 74  VAL   A CA  1 
ATOM   543  C  C   . VAL   A 1 68  ? 3.539  -2.153  14.604 1.00 11.89 ? 74  VAL   A C   1 
ATOM   544  O  O   . VAL   A 1 68  ? 4.344  -2.550  13.765 1.00 12.49 ? 74  VAL   A O   1 
ATOM   545  C  CB  . VAL   A 1 68  ? 4.428  -0.751  16.423 1.00 15.30 ? 74  VAL   A CB  1 
ATOM   546  C  CG1 . VAL   A 1 68  ? 4.351  -0.505  17.930 1.00 16.28 ? 74  VAL   A CG1 1 
ATOM   547  C  CG2 . VAL   A 1 68  ? 5.862  -0.562  15.908 1.00 15.79 ? 74  VAL   A CG2 1 
ATOM   548  N  N   . SER   A 1 69  ? 2.346  -1.638  14.269 1.00 12.05 ? 75  SER   A N   1 
ATOM   549  C  CA  . SER   A 1 69  ? 1.960  -1.253  12.913 1.00 12.34 ? 75  SER   A CA  1 
ATOM   550  C  C   . SER   A 1 69  ? 2.165  0.264   12.853 1.00 11.98 ? 75  SER   A C   1 
ATOM   551  O  O   . SER   A 1 69  ? 1.732  0.969   13.792 1.00 12.89 ? 75  SER   A O   1 
ATOM   552  C  CB  . SER   A 1 69  ? 0.487  -1.532  12.647 1.00 16.08 ? 75  SER   A CB  1 
ATOM   553  O  OG  . SER   A 1 69  ? 0.284  -2.929  12.647 1.00 25.54 ? 75  SER   A OG  1 
ATOM   554  N  N   . PHE   A 1 70  ? 2.766  0.785   11.771 1.00 11.37 ? 76  PHE   A N   1 
ATOM   555  C  CA  . PHE   A 1 70  ? 3.065  2.209   11.719 1.00 11.97 ? 76  PHE   A CA  1 
ATOM   556  C  C   . PHE   A 1 70  ? 2.659  2.779   10.356 1.00 12.61 ? 76  PHE   A C   1 
ATOM   557  O  O   . PHE   A 1 70  ? 2.630  2.071   9.333  1.00 13.15 ? 76  PHE   A O   1 
ATOM   558  C  CB  . PHE   A 1 70  ? 4.576  2.464   12.046 1.00 12.55 ? 76  PHE   A CB  1 
ATOM   559  C  CG  . PHE   A 1 70  ? 5.597  1.661   11.256 1.00 11.72 ? 76  PHE   A CG  1 
ATOM   560  C  CD1 . PHE   A 1 70  ? 6.029  0.421   11.699 1.00 12.08 ? 76  PHE   A CD1 1 
ATOM   561  C  CD2 . PHE   A 1 70  ? 6.191  2.192   10.131 1.00 11.57 ? 76  PHE   A CD2 1 
ATOM   562  C  CE1 . PHE   A 1 70  ? 6.991  -0.299  10.994 1.00 12.67 ? 76  PHE   A CE1 1 
ATOM   563  C  CE2 . PHE   A 1 70  ? 7.140  1.445   9.412  1.00 11.92 ? 76  PHE   A CE2 1 
ATOM   564  C  CZ  . PHE   A 1 70  ? 7.521  0.210   9.857  1.00 12.48 ? 76  PHE   A CZ  1 
ATOM   565  N  N   . SER   A 1 71  ? 2.345  4.083   10.326 1.00 12.51 ? 77  SER   A N   1 
ATOM   566  C  CA  . SER   A 1 71  ? 1.920  4.752   9.108  1.00 12.98 ? 77  SER   A CA  1 
ATOM   567  C  C   . SER   A 1 71  ? 3.094  5.021   8.154  1.00 12.79 ? 77  SER   A C   1 
ATOM   568  O  O   . SER   A 1 71  ? 4.264  4.923   8.564  1.00 13.12 ? 77  SER   A O   1 
ATOM   569  C  CB  . SER   A 1 71  ? 1.194  6.052   9.467  1.00 15.84 ? 77  SER   A CB  1 
ATOM   570  O  OG  . SER   A 1 71  ? 2.048  6.975   10.137 1.00 15.52 ? 77  SER   A OG  1 
ATOM   571  N  N   . LYS   A 1 72  ? 2.812  5.293   6.909  1.00 13.33 ? 78  LYS   A N   1 
ATOM   572  C  CA  . LYS   A 1 72  ? 3.837  5.605   5.922  1.00 13.43 ? 78  LYS   A CA  1 
ATOM   573  C  C   . LYS   A 1 72  ? 4.449  6.979   6.242  1.00 14.58 ? 78  LYS   A C   1 
ATOM   574  O  O   . LYS   A 1 72  ? 3.779  7.850   6.825  1.00 15.18 ? 78  LYS   A O   1 
ATOM   575  C  CB  . LYS   A 1 72  ? 3.190  5.603   4.529  1.00 15.50 ? 78  LYS   A CB  1 
ATOM   576  C  CG  . LYS   A 1 72  ? 2.878  4.181   4.083  1.00 20.05 ? 78  LYS   A CG  1 
ATOM   577  C  CD  . LYS   A 1 72  ? 2.403  4.153   2.633  1.00 26.62 ? 78  LYS   A CD  1 
ATOM   578  C  CE  . LYS   A 1 72  ? 2.360  2.743   2.088  1.00 33.56 ? 78  LYS   A CE  1 
ATOM   579  N  NZ  . LYS   A 1 72  ? 2.244  2.743   0.601  1.00 37.67 ? 78  LYS   A NZ  1 
ATOM   580  N  N   . PRO   A 1 73  ? 5.713  7.209   5.896  1.00 14.62 ? 79  PRO   A N   1 
ATOM   581  C  CA  . PRO   A 1 73  ? 6.358  8.501   6.205  1.00 14.51 ? 79  PRO   A CA  1 
ATOM   582  C  C   . PRO   A 1 73  ? 5.558  9.674   5.643  1.00 15.21 ? 79  PRO   A C   1 
ATOM   583  O  O   . PRO   A 1 73  ? 5.172  9.644   4.470  1.00 15.96 ? 79  PRO   A O   1 
ATOM   584  C  CB  . PRO   A 1 73  ? 7.760  8.358   5.589  1.00 17.78 ? 79  PRO   A CB  1 
ATOM   585  C  CG  . PRO   A 1 73  ? 7.944  6.901   5.301  1.00 21.03 ? 79  PRO   A CG  1 
ATOM   586  C  CD  . PRO   A 1 73  ? 6.621  6.277   5.174  1.00 15.95 ? 79  PRO   A CD  1 
ATOM   587  N  N   . SER   A 1 74  ? 5.277  10.662  6.486  1.00 14.11 ? 80  SER   A N   1 
ATOM   588  C  CA  . SER   A 1 74  ? 4.404  11.758  6.108  1.00 15.27 ? 80  SER   A CA  1 
ATOM   589  C  C   . SER   A 1 74  ? 4.783  13.026  6.842  1.00 13.85 ? 80  SER   A C   1 
ATOM   590  O  O   . SER   A 1 74  ? 5.610  13.025  7.729  1.00 14.30 ? 80  SER   A O   1 
ATOM   591  C  CB  . SER   A 1 74  ? 2.957  11.411  6.518  1.00 21.88 ? 80  SER   A CB  1 
ATOM   592  O  OG  . SER   A 1 74  ? 2.545  10.102  6.145  1.00 32.52 ? 80  SER   A OG  1 
ATOM   593  N  N   . LEU   A 1 75  ? 4.096  14.129  6.463  1.00 15.83 ? 81  LEU   A N   1 
ATOM   594  C  CA  . LEU   A 1 75  ? 4.264  15.433  7.066  1.00 17.10 ? 81  LEU   A CA  1 
ATOM   595  C  C   . LEU   A 1 75  ? 3.201  15.515  8.170  1.00 18.81 ? 81  LEU   A C   1 
ATOM   596  O  O   . LEU   A 1 75  ? 1.993  15.478  7.882  1.00 19.89 ? 81  LEU   A O   1 
ATOM   597  C  CB  . LEU   A 1 75  ? 4.019  16.481  5.954  1.00 18.58 ? 81  LEU   A CB  1 
ATOM   598  C  CG  . LEU   A 1 75  ? 4.384  17.920  6.264  1.00 20.96 ? 81  LEU   A CG  1 
ATOM   599  C  CD1 . LEU   A 1 75  ? 5.875  18.065  6.490  1.00 20.94 ? 81  LEU   A CD1 1 
ATOM   600  C  CD2 . LEU   A 1 75  ? 4.000  18.836  5.106  1.00 23.44 ? 81  LEU   A CD2 1 
ATOM   601  N  N   . ILE   A 1 76  ? 3.629  15.517  9.428  1.00 17.68 ? 82  ILE   A N   1 
ATOM   602  C  CA  . ILE   A 1 76  ? 2.745  15.472  10.606 1.00 19.80 ? 82  ILE   A CA  1 
ATOM   603  C  C   . ILE   A 1 76  ? 2.976  16.673  11.521 1.00 21.05 ? 82  ILE   A C   1 
ATOM   604  O  O   . ILE   A 1 76  ? 4.129  17.054  11.773 1.00 20.10 ? 82  ILE   A O   1 
ATOM   605  C  CB  . ILE   A 1 76  ? 3.048  14.184  11.382 1.00 22.09 ? 82  ILE   A CB  1 
ATOM   606  C  CG1 . ILE   A 1 76  ? 2.821  12.941  10.456 1.00 24.19 ? 82  ILE   A CG1 1 
ATOM   607  C  CG2 . ILE   A 1 76  ? 2.273  14.149  12.752 1.00 24.09 ? 82  ILE   A CG2 1 
ATOM   608  C  CD1 . ILE   A 1 76  ? 2.595  11.824  10.969 1.00 25.01 ? 82  ILE   A CD1 1 
ATOM   609  N  N   . PHE   A 1 77  ? 1.899  17.255  12.061 1.00 21.58 ? 83  PHE   A N   1 
ATOM   610  C  CA  . PHE   A 1 77  ? 2.041  18.397  12.963 1.00 22.87 ? 83  PHE   A CA  1 
ATOM   611  C  C   . PHE   A 1 77  ? 2.481  17.907  14.332 1.00 23.32 ? 83  PHE   A C   1 
ATOM   612  O  O   . PHE   A 1 77  ? 1.967  16.928  14.879 1.00 24.87 ? 83  PHE   A O   1 
ATOM   613  C  CB  . PHE   A 1 77  ? 0.729  19.193  13.071 1.00 24.56 ? 83  PHE   A CB  1 
ATOM   614  C  CG  . PHE   A 1 77  ? 0.961  20.556  13.677 1.00 27.16 ? 83  PHE   A CG  1 
ATOM   615  C  CD1 . PHE   A 1 77  ? 1.607  21.548  12.959 1.00 29.68 ? 83  PHE   A CD1 1 
ATOM   616  C  CD2 . PHE   A 1 77  ? 0.575  20.825  14.976 1.00 29.34 ? 83  PHE   A CD2 1 
ATOM   617  C  CE1 . PHE   A 1 77  ? 1.827  22.796  13.514 1.00 32.19 ? 83  PHE   A CE1 1 
ATOM   618  C  CE2 . PHE   A 1 77  ? 0.802  22.077  15.537 1.00 29.91 ? 83  PHE   A CE2 1 
ATOM   619  C  CZ  . PHE   A 1 77  ? 1.395  23.061  14.790 1.00 31.55 ? 83  PHE   A CZ  1 
ATOM   620  N  N   . VAL   A 1 78  ? 3.570  18.519  14.837 1.00 20.81 ? 84  VAL   A N   1 
ATOM   621  C  CA  . VAL   A 1 78  ? 4.109  18.165  16.132 1.00 19.80 ? 84  VAL   A CA  1 
ATOM   622  C  C   . VAL   A 1 78  ? 4.053  19.424  17.043 1.00 20.87 ? 84  VAL   A C   1 
ATOM   623  O  O   . VAL   A 1 78  ? 4.533  20.480  16.671 1.00 20.09 ? 84  VAL   A O   1 
ATOM   624  C  CB  . VAL   A 1 78  ? 5.554  17.656  15.984 1.00 18.91 ? 84  VAL   A CB  1 
ATOM   625  C  CG1 . VAL   A 1 78  ? 6.126  17.285  17.358 1.00 19.19 ? 84  VAL   A CG1 1 
ATOM   626  C  CG2 . VAL   A 1 78  ? 5.576  16.442  15.024 1.00 18.61 ? 84  VAL   A CG2 1 
ATOM   627  N  N   . GLU   A 1 79  ? 3.429  19.252  18.198 1.00 22.10 ? 85  GLU   A N   1 
ATOM   628  C  CA  . GLU   A 1 79  ? 3.223  20.329  19.162 1.00 23.62 ? 85  GLU   A CA  1 
ATOM   629  C  C   . GLU   A 1 79  ? 4.544  20.944  19.618 1.00 23.74 ? 85  GLU   A C   1 
ATOM   630  O  O   . GLU   A 1 79  ? 5.550  20.232  19.703 1.00 22.50 ? 85  GLU   A O   1 
ATOM   631  C  CB  . GLU   A 1 79  ? 2.514  19.759  20.394 1.00 25.79 ? 85  GLU   A CB  1 
ATOM   632  C  CG  . GLU   A 1 79  ? 2.010  20.841  21.337 1.00 32.64 ? 85  GLU   A CG  1 
ATOM   633  C  CD  . GLU   A 1 79  ? 1.090  21.862  20.695 1.00 40.07 ? 85  GLU   A CD  1 
ATOM   634  O  OE1 . GLU   A 1 79  ? 1.569  22.967  20.335 1.00 38.70 ? 85  GLU   A OE1 1 
ATOM   635  O  OE2 . GLU   A 1 79  ? -0.108 21.540  20.532 1.00 43.79 ? 85  GLU   A OE2 1 
ATOM   636  N  N   . ALA   A 1 80  ? 4.529  22.256  20.002 1.00 24.49 ? 86  ALA   A N   1 
ATOM   637  C  CA  . ALA   A 1 80  ? 5.720  22.942  20.553 1.00 24.89 ? 86  ALA   A CA  1 
ATOM   638  C  C   . ALA   A 1 80  ? 6.230  22.204  21.742 1.00 23.71 ? 86  ALA   A C   1 
ATOM   639  O  O   . ALA   A 1 80  ? 5.444  21.696  22.545 1.00 24.31 ? 86  ALA   A O   1 
ATOM   640  C  CB  . ALA   A 1 80  ? 5.380  24.357  20.981 1.00 26.08 ? 86  ALA   A CB  1 
ATOM   641  N  N   . SER   A 1 81  ? 7.544  22.090  21.831 1.00 22.08 ? 87  SER   A N   1 
ATOM   642  C  CA  . SER   A 1 81  ? 8.189  21.409  22.947 1.00 21.79 ? 87  SER   A CA  1 
ATOM   643  C  C   . SER   A 1 81  ? 9.356  22.320  23.409 1.00 21.50 ? 87  SER   A C   1 
ATOM   644  O  O   . SER   A 1 81  ? 9.516  23.441  22.905 1.00 22.46 ? 87  SER   A O   1 
ATOM   645  C  CB  . SER   A 1 81  ? 8.745  20.060  22.489 1.00 21.79 ? 87  SER   A CB  1 
ATOM   646  O  OG  . SER   A 1 81  ? 9.783  20.279  21.538 1.00 20.33 ? 87  SER   A OG  1 
ATOM   647  N  N   . GLU   A 1 82  ? 10.189 21.823  24.312 1.00 21.29 ? 88  GLU   A N   1 
ATOM   648  C  CA  . GLU   A 1 82  ? 11.382 22.576  24.726 1.00 21.97 ? 88  GLU   A CA  1 
ATOM   649  C  C   . GLU   A 1 82  ? 12.492 22.481  23.646 1.00 20.45 ? 88  GLU   A C   1 
ATOM   650  O  O   . GLU   A 1 82  ? 13.462 23.217  23.735 1.00 21.09 ? 88  GLU   A O   1 
ATOM   651  C  CB  . GLU   A 1 82  ? 11.889 22.095  26.098 1.00 27.39 ? 88  GLU   A CB  1 
ATOM   652  C  CG  . GLU   A 1 82  ? 12.666 20.799  26.096 1.00 34.84 ? 88  GLU   A CG  1 
ATOM   653  C  CD  . GLU   A 1 82  ? 12.630 20.025  27.401 1.00 46.71 ? 88  GLU   A CD  1 
ATOM   654  O  OE1 . GLU   A 1 82  ? 13.531 20.246  28.245 1.00 50.66 ? 88  GLU   A OE1 1 
ATOM   655  O  OE2 . GLU   A 1 82  ? 11.713 19.188  27.577 1.00 48.31 ? 88  GLU   A OE2 1 
ATOM   656  N  N   . TYR   A 1 83  ? 12.307 21.642  22.574 1.00 19.53 ? 89  TYR   A N   1 
ATOM   657  C  CA  . TYR   A 1 83  ? 13.298 21.478  21.508 1.00 17.44 ? 89  TYR   A CA  1 
ATOM   658  C  C   . TYR   A 1 83  ? 12.941 22.120  20.224 1.00 17.47 ? 89  TYR   A C   1 
ATOM   659  O  O   . TYR   A 1 83  ? 13.845 22.473  19.480 1.00 17.33 ? 89  TYR   A O   1 
ATOM   660  C  CB  . TYR   A 1 83  ? 13.557 19.989  21.279 1.00 17.10 ? 89  TYR   A CB  1 
ATOM   661  C  CG  . TYR   A 1 83  ? 14.130 19.342  22.516 1.00 17.41 ? 89  TYR   A CG  1 
ATOM   662  C  CD1 . TYR   A 1 83  ? 15.456 19.521  22.861 1.00 18.68 ? 89  TYR   A CD1 1 
ATOM   663  C  CD2 . TYR   A 1 83  ? 13.343 18.546  23.333 1.00 22.05 ? 89  TYR   A CD2 1 
ATOM   664  C  CE1 . TYR   A 1 83  ? 16.009 18.883  23.965 1.00 20.79 ? 89  TYR   A CE1 1 
ATOM   665  C  CE2 . TYR   A 1 83  ? 13.867 17.948  24.474 1.00 23.82 ? 89  TYR   A CE2 1 
ATOM   666  C  CZ  . TYR   A 1 83  ? 15.195 18.144  24.802 1.00 24.42 ? 89  TYR   A CZ  1 
ATOM   667  O  OH  . TYR   A 1 83  ? 15.750 17.540  25.906 1.00 28.22 ? 89  TYR   A OH  1 
ATOM   668  N  N   . TYR   A 1 84  ? 11.614 22.273  19.912 1.00 17.71 ? 90  TYR   A N   1 
ATOM   669  C  CA  . TYR   A 1 84  ? 11.221 22.885  18.643 1.00 17.80 ? 90  TYR   A CA  1 
ATOM   670  C  C   . TYR   A 1 84  ? 9.926  23.675  18.861 1.00 19.86 ? 90  TYR   A C   1 
ATOM   671  O  O   . TYR   A 1 84  ? 9.089  23.226  19.643 1.00 20.35 ? 90  TYR   A O   1 
ATOM   672  C  CB  . TYR   A 1 84  ? 10.884 21.808  17.555 1.00 16.87 ? 90  TYR   A CB  1 
ATOM   673  C  CG  . TYR   A 1 84  ? 12.036 20.918  17.125 1.00 14.97 ? 90  TYR   A CG  1 
ATOM   674  C  CD1 . TYR   A 1 84  ? 12.998 21.376  16.247 1.00 14.87 ? 90  TYR   A CD1 1 
ATOM   675  C  CD2 . TYR   A 1 84  ? 12.133 19.600  17.574 1.00 14.77 ? 90  TYR   A CD2 1 
ATOM   676  C  CE1 . TYR   A 1 84  ? 14.030 20.542  15.823 1.00 13.49 ? 90  TYR   A CE1 1 
ATOM   677  C  CE2 . TYR   A 1 84  ? 13.157 18.770  17.166 1.00 14.89 ? 90  TYR   A CE2 1 
ATOM   678  C  CZ  . TYR   A 1 84  ? 14.109 19.254  16.315 1.00 13.28 ? 90  TYR   A CZ  1 
ATOM   679  O  OH  . TYR   A 1 84  ? 15.127 18.449  15.873 1.00 12.57 ? 90  TYR   A OH  1 
ATOM   680  N  N   . PRO   A 1 85  ? 9.656  24.708  18.053 1.00 21.65 ? 91  PRO   A N   1 
ATOM   681  C  CA  . PRO   A 1 85  ? 8.309  25.322  18.091 1.00 23.03 ? 91  PRO   A CA  1 
ATOM   682  C  C   . PRO   A 1 85  ? 7.283  24.384  17.427 1.00 24.11 ? 91  PRO   A C   1 
ATOM   683  O  O   . PRO   A 1 85  ? 7.654  23.396  16.773 1.00 23.01 ? 91  PRO   A O   1 
ATOM   684  C  CB  . PRO   A 1 85  ? 8.503  26.601  17.271 1.00 24.16 ? 91  PRO   A CB  1 
ATOM   685  C  CG  . PRO   A 1 85  ? 9.497  26.228  16.266 1.00 24.53 ? 91  PRO   A CG  1 
ATOM   686  C  CD  . PRO   A 1 85  ? 10.488 25.295  16.986 1.00 21.84 ? 91  PRO   A CD  1 
ATOM   687  N  N   . ALA   A 1 86  ? 5.996  24.717  17.490 1.00 25.33 ? 92  ALA   A N   1 
ATOM   688  C  CA  . ALA   A 1 86  ? 4.943  23.940  16.827 1.00 25.32 ? 92  ALA   A CA  1 
ATOM   689  C  C   . ALA   A 1 86  ? 5.215  23.966  15.340 1.00 24.81 ? 92  ALA   A C   1 
ATOM   690  O  O   . ALA   A 1 86  ? 5.545  25.025  14.795 1.00 25.47 ? 92  ALA   A O   1 
ATOM   691  C  CB  . ALA   A 1 86  ? 3.582  24.593  17.112 1.00 26.43 ? 92  ALA   A CB  1 
ATOM   692  N  N   . ARG   A 1 87  ? 5.249  22.765  14.706 1.00 23.26 ? 93  ARG   A N   1 
ATOM   693  C  CA  . ARG   A 1 87  ? 5.611  22.743  13.305 1.00 22.65 ? 93  ARG   A CA  1 
ATOM   694  C  C   . ARG   A 1 87  ? 5.232  21.407  12.677 1.00 20.68 ? 93  ARG   A C   1 
ATOM   695  O  O   . ARG   A 1 87  ? 4.890  20.462  13.381 1.00 23.25 ? 93  ARG   A O   1 
ATOM   696  C  CB  . ARG   A 1 87  ? 7.158  22.928  13.189 1.00 23.05 ? 93  ARG   A CB  1 
ATOM   697  C  CG  . ARG   A 1 87  ? 7.936  21.621  13.565 1.00 22.67 ? 93  ARG   A CG  1 
ATOM   698  C  CD  . ARG   A 1 87  ? 9.348  21.803  13.956 1.00 19.63 ? 93  ARG   A CD  1 
ATOM   699  N  NE  . ARG   A 1 87  ? 10.267 20.679  13.698 1.00 18.70 ? 93  ARG   A NE  1 
ATOM   700  C  CZ  . ARG   A 1 87  ? 10.314 19.512  14.326 1.00 18.10 ? 93  ARG   A CZ  1 
ATOM   701  N  NH1 . ARG   A 1 87  ? 9.424  19.215  15.284 1.00 18.83 ? 93  ARG   A NH1 1 
ATOM   702  N  NH2 . ARG   A 1 87  ? 11.232 18.620  13.999 1.00 14.93 ? 93  ARG   A NH2 1 
ATOM   703  N  N   . TYR   A 1 88  ? 5.395  21.333  11.341 1.00 19.96 ? 94  TYR   A N   1 
ATOM   704  C  CA  . TYR   A 1 88  ? 5.238  20.083  10.647 1.00 20.25 ? 94  TYR   A CA  1 
ATOM   705  C  C   . TYR   A 1 88  ? 6.604  19.416  10.586 1.00 18.50 ? 94  TYR   A C   1 
ATOM   706  O  O   . TYR   A 1 88  ? 7.586  20.033  10.175 1.00 18.10 ? 94  TYR   A O   1 
ATOM   707  C  CB  . TYR   A 1 88  ? 4.736  20.321  9.216  1.00 21.00 ? 94  TYR   A CB  1 
ATOM   708  C  CG  . TYR   A 1 88  ? 3.273  20.681  9.212  1.00 22.94 ? 94  TYR   A CG  1 
ATOM   709  C  CD1 . TYR   A 1 88  ? 2.298  19.699  9.276  1.00 23.05 ? 94  TYR   A CD1 1 
ATOM   710  C  CD2 . TYR   A 1 88  ? 2.864  22.006  9.282  1.00 24.14 ? 94  TYR   A CD2 1 
ATOM   711  C  CE1 . TYR   A 1 88  ? 0.947  20.025  9.331  1.00 25.13 ? 94  TYR   A CE1 1 
ATOM   712  C  CE2 . TYR   A 1 88  ? 1.517  22.340  9.369  1.00 25.10 ? 94  TYR   A CE2 1 
ATOM   713  C  CZ  . TYR   A 1 88  ? 0.565  21.341  9.437  1.00 26.40 ? 94  TYR   A CZ  1 
ATOM   714  O  OH  . TYR   A 1 88  ? -0.781 21.601  9.511  1.00 30.38 ? 94  TYR   A OH  1 
ATOM   715  N  N   . GLN   A 1 89  ? 6.661  18.132  10.966 1.00 16.23 ? 95  GLN   A N   1 
ATOM   716  C  CA  . GLN   A 1 89  ? 7.875  17.323  10.855 1.00 14.31 ? 95  GLN   A CA  1 
ATOM   717  C  C   . GLN   A 1 89  ? 7.663  16.400  9.671  1.00 13.89 ? 95  GLN   A C   1 
ATOM   718  O  O   . GLN   A 1 89  ? 6.591  15.800  9.559  1.00 14.64 ? 95  GLN   A O   1 
ATOM   719  C  CB  . GLN   A 1 89  ? 8.148  16.566  12.161 1.00 13.95 ? 95  GLN   A CB  1 
ATOM   720  C  CG  . GLN   A 1 89  ? 9.367  15.662  12.062 1.00 13.53 ? 95  GLN   A CG  1 
ATOM   721  C  CD  . GLN   A 1 89  ? 9.884  15.193  13.399 1.00 13.88 ? 95  GLN   A CD  1 
ATOM   722  O  OE1 . GLN   A 1 89  ? 9.928  15.924  14.382 1.00 13.32 ? 95  GLN   A OE1 1 
ATOM   723  N  NE2 . GLN   A 1 89  ? 10.340 13.959  13.461 1.00 12.95 ? 95  GLN   A NE2 1 
ATOM   724  N  N   . SER   A 1 90  ? 8.654  16.304  8.770  1.00 13.64 ? 96  SER   A N   1 
ATOM   725  C  CA  . SER   A 1 90  ? 8.523  15.457  7.602  1.00 14.28 ? 96  SER   A CA  1 
ATOM   726  C  C   . SER   A 1 90  ? 9.123  14.054  7.842  1.00 13.58 ? 96  SER   A C   1 
ATOM   727  O  O   . SER   A 1 90  ? 9.884  13.854  8.797  1.00 13.71 ? 96  SER   A O   1 
ATOM   728  C  CB  . SER   A 1 90  ? 9.176  16.143  6.403  1.00 16.34 ? 96  SER   A CB  1 
ATOM   729  O  OG  . SER   A 1 90  ? 10.567 16.261  6.664  1.00 19.53 ? 96  SER   A OG  1 
ATOM   730  N  N   . HIS   A 1 91  ? 8.713  13.102  6.983  1.00 13.57 ? 97  HIS   A N   1 
ATOM   731  C  CA  . HIS   A 1 91  ? 9.212  11.729  6.996  1.00 12.69 ? 97  HIS   A CA  1 
ATOM   732  C  C   . HIS   A 1 91  ? 8.964  11.070  8.375  1.00 11.94 ? 97  HIS   A C   1 
ATOM   733  O  O   . HIS   A 1 91  ? 9.758  10.224  8.810  1.00 12.74 ? 97  HIS   A O   1 
ATOM   734  C  CB  . HIS   A 1 91  ? 10.735 11.685  6.633  1.00 14.24 ? 97  HIS   A CB  1 
ATOM   735  C  CG  . HIS   A 1 91  ? 11.012 12.210  5.246  1.00 14.92 ? 97  HIS   A CG  1 
ATOM   736  N  ND1 . HIS   A 1 91  ? 11.107 11.351  4.164  1.00 17.78 ? 97  HIS   A ND1 1 
ATOM   737  C  CD2 . HIS   A 1 91  ? 11.222 13.477  4.820  1.00 16.15 ? 97  HIS   A CD2 1 
ATOM   738  C  CE1 . HIS   A 1 91  ? 11.347 12.131  3.102  1.00 18.69 ? 97  HIS   A CE1 1 
ATOM   739  N  NE2 . HIS   A 1 91  ? 11.428 13.411  3.443  1.00 18.33 ? 97  HIS   A NE2 1 
ATOM   740  N  N   . LEU   A 1 92  ? 7.832  11.414  8.993  1.00 11.89 ? 98  LEU   A N   1 
ATOM   741  C  CA  . LEU   A 1 92  ? 7.469  10.905  10.320 1.00 11.85 ? 98  LEU   A CA  1 
ATOM   742  C  C   . LEU   A 1 92  ? 6.393  9.816   10.174 1.00 11.23 ? 98  LEU   A C   1 
ATOM   743  O  O   . LEU   A 1 92  ? 5.478  9.940   9.371  1.00 12.26 ? 98  LEU   A O   1 
ATOM   744  C  CB  . LEU   A 1 92  ? 6.938  12.067  11.208 1.00 12.65 ? 98  LEU   A CB  1 
ATOM   745  C  CG  . LEU   A 1 92  ? 6.631  11.677  12.679 1.00 15.43 ? 98  LEU   A CG  1 
ATOM   746  C  CD1 . LEU   A 1 92  ? 7.870  11.317  13.413 1.00 15.29 ? 98  LEU   A CD1 1 
ATOM   747  C  CD2 . LEU   A 1 92  ? 5.966  12.876  13.445 1.00 17.99 ? 98  LEU   A CD2 1 
ATOM   748  N  N   . MET   A 1 93  ? 6.537  8.716   10.930 1.00 11.39 ? 99  MET   A N   1 
ATOM   749  C  CA  . MET   A 1 93  ? 5.590  7.583   10.902 1.00 11.79 ? 99  MET   A CA  1 
ATOM   750  C  C   . MET   A 1 93  ? 5.023  7.416   12.326 1.00 12.10 ? 99  MET   A C   1 
ATOM   751  O  O   . MET   A 1 93  ? 5.784  7.445   13.300 1.00 13.04 ? 99  MET   A O   1 
ATOM   752  C  CB  . MET   A 1 93  ? 6.381  6.337   10.532 1.00 12.20 ? 99  MET   A CB  1 
ATOM   753  C  CG  . MET   A 1 93  ? 7.023  6.492   9.139  1.00 12.43 ? 99  MET   A CG  1 
ATOM   754  S  SD  . MET   A 1 93  ? 8.029  5.059   8.619  1.00 15.11 ? 99  MET   A SD  1 
ATOM   755  C  CE  . MET   A 1 93  ? 9.332  5.134   9.923  1.00 17.86 ? 99  MET   A CE  1 
ATOM   756  N  N   . LEU   A 1 94  ? 3.703  7.270   12.472 1.00 12.00 ? 100 LEU   A N   1 
ATOM   757  C  CA  . LEU   A 1 94  ? 3.114  7.099   13.795 1.00 13.18 ? 100 LEU   A CA  1 
ATOM   758  C  C   . LEU   A 1 94  ? 2.634  5.687   14.035 1.00 11.72 ? 100 LEU   A C   1 
ATOM   759  O  O   . LEU   A 1 94  ? 2.157  5.016   13.100 1.00 12.48 ? 100 LEU   A O   1 
ATOM   760  C  CB  . LEU   A 1 94  ? 1.906  8.039   13.981 1.00 15.11 ? 100 LEU   A CB  1 
ATOM   761  C  CG  . LEU   A 1 94  ? 2.179  9.517   13.861 1.00 18.11 ? 100 LEU   A CG  1 
ATOM   762  C  CD1 . LEU   A 1 94  ? 0.890  10.310  14.204 1.00 20.75 ? 100 LEU   A CD1 1 
ATOM   763  C  CD2 . LEU   A 1 94  ? 3.255  9.972   14.841 1.00 19.77 ? 100 LEU   A CD2 1 
ATOM   764  N  N   . ALA   A 1 95  ? 2.637  5.281   15.325 1.00 11.74 ? 101 ALA   A N   1 
ATOM   765  C  CA  . ALA   A 1 95  ? 2.108  3.992   15.754 1.00 12.12 ? 101 ALA   A CA  1 
ATOM   766  C  C   . ALA   A 1 95  ? 1.475  4.187   17.134 1.00 11.38 ? 101 ALA   A C   1 
ATOM   767  O  O   . ALA   A 1 95  ? 1.757  5.182   17.822 1.00 12.13 ? 101 ALA   A O   1 
ATOM   768  C  CB  . ALA   A 1 95  ? 3.266  2.977   15.863 1.00 13.51 ? 101 ALA   A CB  1 
ATOM   769  N  N   . VAL   A 1 96  ? 0.675  3.203   17.575 1.00 11.24 ? 102 VAL   A N   1 
ATOM   770  C  CA  . VAL   A 1 96  ? 0.159  3.190   18.919 1.00 12.33 ? 102 VAL   A CA  1 
ATOM   771  C  C   . VAL   A 1 96  ? 1.222  2.443   19.796 1.00 13.92 ? 102 VAL   A C   1 
ATOM   772  O  O   . VAL   A 1 96  ? 1.579  1.310   19.540 1.00 15.43 ? 102 VAL   A O   1 
ATOM   773  C  CB  . VAL   A 1 96  ? -1.177 2.458   18.941 1.00 12.19 ? 102 VAL   A CB  1 
ATOM   774  C  CG1 . VAL   A 1 96  ? -1.650 2.305   20.382 1.00 13.18 ? 102 VAL   A CG1 1 
ATOM   775  C  CG2 . VAL   A 1 96  ? -2.190 3.279   18.120 1.00 11.34 ? 102 VAL   A CG2 1 
ATOM   776  N  N   . GLY   A 1 97  ? 1.718  3.139   20.786 1.00 12.78 ? 103 GLY   A N   1 
ATOM   777  C  CA  . GLY   A 1 97  ? 2.715  2.557   21.684 1.00 13.93 ? 103 GLY   A CA  1 
ATOM   778  C  C   . GLY   A 1 97  ? 3.170  3.562   22.701 1.00 14.14 ? 103 GLY   A C   1 
ATOM   779  O  O   . GLY   A 1 97  ? 2.873  4.756   22.604 1.00 14.52 ? 103 GLY   A O   1 
ATOM   780  N  N   . HIS   A 1 98  ? 3.475  2.879   23.755 1.00 14.39 ? 104 HIS   A N   1 
ATOM   781  C  CA  . HIS   A 1 98  ? 3.993  3.879   24.720 1.00 14.38 ? 104 HIS   A CA  1 
ATOM   782  C  C   . HIS   A 1 98  ? 5.250  4.627   24.268 1.00 14.14 ? 104 HIS   A C   1 
ATOM   783  O  O   . HIS   A 1 98  ? 6.208  3.939   23.769 1.00 12.60 ? 104 HIS   A O   1 
ATOM   784  C  CB  . HIS   A 1 98  ? 4.196  3.202   26.100 1.00 14.93 ? 104 HIS   A CB  1 
ATOM   785  C  CG  . HIS   A 1 98  ? 4.919  4.011   27.159 1.00 14.30 ? 104 HIS   A CG  1 
ATOM   786  N  ND1 . HIS   A 1 98  ? 4.155  5.042   27.791 1.00 15.45 ? 104 HIS   A ND1 1 
ATOM   787  C  CD2 . HIS   A 1 98  ? 6.201  4.201   27.611 1.00 14.06 ? 104 HIS   A CD2 1 
ATOM   788  C  CE1 . HIS   A 1 98  ? 4.887  5.767   28.583 1.00 15.62 ? 104 HIS   A CE1 1 
ATOM   789  N  NE2 . HIS   A 1 98  ? 6.111  5.245   28.567 1.00 14.24 ? 104 HIS   A NE2 1 
ATOM   790  N  N   . SER   A 1 99  ? 5.328  5.880   24.671 1.00 14.36 ? 105 SER   A N   1 
ATOM   791  C  CA  . SER   A 1 99  ? 6.487  6.794   24.571 1.00 14.62 ? 105 SER   A CA  1 
ATOM   792  C  C   . SER   A 1 99  ? 6.327  8.084   25.425 1.00 16.87 ? 105 SER   A C   1 
ATOM   793  O  O   . SER   A 1 99  ? 5.571  8.794   25.232 1.00 19.99 ? 105 SER   A O   1 
ATOM   794  C  CB  . SER   A 1 99  ? 6.694  7.051   23.107 1.00 16.11 ? 105 SER   A CB  1 
ATOM   795  O  OG  . SER   A 1 99  ? 5.828  8.127   22.740 1.00 17.76 ? 105 SER   A OG  1 
ATOM   796  N  N   . GLU   A 1 100 ? 7.416  8.338   26.281 1.00 14.70 ? 106 GLU   A N   1 
ATOM   797  C  CA  . GLU   A 1 100 ? 7.570  9.433   27.216 1.00 16.34 ? 106 GLU   A CA  1 
ATOM   798  C  C   . GLU   A 1 100 ? 9.163  9.983   27.169 1.00 17.44 ? 106 GLU   A C   1 
ATOM   799  O  O   . GLU   A 1 100 ? 9.889  9.453   26.579 1.00 17.88 ? 106 GLU   A O   1 
ATOM   800  C  CB  . GLU   A 1 100 ? 7.349  9.047   28.553 1.00 15.49 ? 106 GLU   A CB  1 
ATOM   801  C  CG  . GLU   A 1 100 ? 8.555  8.228   29.305 1.00 15.97 ? 106 GLU   A CG  1 
ATOM   802  C  CD  . GLU   A 1 100 ? 8.135  7.561   30.635 1.00 14.42 ? 106 GLU   A CD  1 
ATOM   803  O  OE1 . GLU   A 1 100 ? 8.526  8.107   31.718 1.00 18.24 ? 106 GLU   A OE1 1 
ATOM   804  O  OE2 . GLU   A 1 100 ? 7.521  6.561   30.616 1.00 14.67 ? 106 GLU   A OE2 1 
ATOM   805  N  N   . PRO   A 1 101 ? 9.546  11.035  27.801 1.00 20.28 ? 107 PRO   A N   1 
ATOM   806  C  CA  . PRO   A 1 101 ? 10.753 11.524  27.783 1.00 20.49 ? 107 PRO   A CA  1 
ATOM   807  C  C   . PRO   A 1 101 ? 11.776 10.493  28.506 1.00 20.44 ? 107 PRO   A C   1 
ATOM   808  O  O   . PRO   A 1 101 ? 11.639 10.021  29.093 1.00 20.36 ? 107 PRO   A O   1 
ATOM   809  C  CB  . PRO   A 1 101 ? 10.426 12.905  28.635 1.00 21.85 ? 107 PRO   A CB  1 
ATOM   810  C  CG  . PRO   A 1 101 ? 8.964  13.224  28.541 1.00 22.93 ? 107 PRO   A CG  1 
ATOM   811  C  CD  . PRO   A 1 101 ? 8.385  11.826  28.501 1.00 20.79 ? 107 PRO   A CD  1 
ATOM   812  N  N   . GLY   A 1 102 ? 13.016 10.381  27.722 1.00 17.68 ? 108 GLY   A N   1 
ATOM   813  C  CA  . GLY   A 1 102 ? 13.985 9.269   27.878 1.00 17.72 ? 108 GLY   A CA  1 
ATOM   814  C  C   . GLY   A 1 102 ? 14.046 8.581   26.701 1.00 15.24 ? 108 GLY   A C   1 
ATOM   815  O  O   . GLY   A 1 102 ? 14.634 7.421   26.544 1.00 16.22 ? 108 GLY   A O   1 
ATOM   816  N  N   . ASP   A 1 103 ? 12.878 9.009   25.842 1.00 14.69 ? 109 ASP   A N   1 
ATOM   817  C  CA  . ASP   A 1 103 ? 12.801 7.920   24.667 1.00 13.41 ? 109 ASP   A CA  1 
ATOM   818  C  C   . ASP   A 1 103 ? 13.038 8.222   23.205 1.00 12.65 ? 109 ASP   A C   1 
ATOM   819  O  O   . ASP   A 1 103 ? 12.951 7.152   22.363 1.00 12.13 ? 109 ASP   A O   1 
ATOM   820  C  CB  . ASP   A 1 103 ? 11.276 7.200   24.714 1.00 11.94 ? 109 ASP   A CB  1 
ATOM   821  C  CG  . ASP   A 1 103 ? 10.859 6.450   26.001 1.00 12.82 ? 109 ASP   A CG  1 
ATOM   822  O  OD1 . ASP   A 1 103 ? 11.744 5.802   26.414 1.00 12.46 ? 109 ASP   A OD1 1 
ATOM   823  O  OD2 . ASP   A 1 103 ? 9.564  6.266   26.391 1.00 12.20 ? 109 ASP   A OD2 1 
ATOM   824  N  N   . CYS   A 1 104 ? 13.438 9.427   22.870 1.00 11.44 ? 110 CYS   A N   1 
ATOM   825  C  CA  . CYS   A 1 104 ? 13.931 9.420   21.441 1.00 11.80 ? 110 CYS   A CA  1 
ATOM   826  C  C   . CYS   A 1 104 ? 15.318 8.744   21.371 1.00 11.65 ? 110 CYS   A C   1 
ATOM   827  O  O   . CYS   A 1 104 ? 16.201 8.964   22.155 1.00 12.46 ? 110 CYS   A O   1 
ATOM   828  C  CB  . CYS   A 1 104 ? 13.717 10.806  20.998 1.00 12.75 ? 110 CYS   A CB  1 
ATOM   829  S  SG  . CYS   A 1 104 ? 12.020 11.551  21.134 1.00 15.15 ? 110 CYS   A SG  1 
ATOM   830  N  N   . GLY   A 1 105 ? 15.383 8.048   20.165 1.00 11.09 ? 111 GLY   A N   1 
ATOM   831  C  CA  . GLY   A 1 105 ? 16.606 7.352   19.808 1.00 11.72 ? 111 GLY   A CA  1 
ATOM   832  C  C   . GLY   A 1 105 ? 16.458 5.841   19.761 1.00 10.94 ? 111 GLY   A C   1 
ATOM   833  O  O   . GLY   A 1 105 ? 17.320 5.149   19.210 1.00 11.62 ? 111 GLY   A O   1 
ATOM   834  N  N   . GLY   A 1 106 ? 15.379 5.310   20.335 1.00 11.11 ? 112 GLY   A N   1 
ATOM   835  C  CA  . GLY   A 1 106 ? 15.166 3.875   20.257 1.00 10.10 ? 112 GLY   A CA  1 
ATOM   836  C  C   . GLY   A 1 106 ? 14.979 3.414   18.806 1.00 9.46  ? 112 GLY   A C   1 
ATOM   837  O  O   . GLY   A 1 106 ? 14.274 4.087   18.051 1.00 9.76  ? 112 GLY   A O   1 
ATOM   838  N  N   . ILE   A 1 107 ? 15.507 2.253   18.437 1.00 10.01 ? 113 ILE   A N   1 
ATOM   839  C  CA  . ILE   A 1 107 ? 15.370 1.800   17.052 1.00 9.25  ? 113 ILE   A CA  1 
ATOM   840  C  C   . ILE   A 1 107 ? 14.048 1.132   16.754 1.00 9.27  ? 113 ILE   A C   1 
ATOM   841  O  O   . ILE   A 1 107 ? 13.579 0.304   17.534 1.00 9.84  ? 113 ILE   A O   1 
ATOM   842  C  CB  . ILE   A 1 107 ? 16.550 0.873   16.766 1.00 10.52 ? 113 ILE   A CB  1 
ATOM   843  C  CG1 . ILE   A 1 107 ? 17.810 1.732   16.490 1.00 13.11 ? 113 ILE   A CG1 1 
ATOM   844  C  CG2 . ILE   A 1 107 ? 16.296 -0.045  15.524 1.00 11.61 ? 113 ILE   A CG2 1 
ATOM   845  C  CD1 . ILE   A 1 107 ? 19.080 0.868   16.366 1.00 14.99 ? 113 ILE   A CD1 1 
ATOM   846  N  N   . LEU   A 1 108 ? 13.497 1.474   15.582 1.00 8.67  ? 114 LEU   A N   1 
ATOM   847  C  CA  . LEU   A 1 108 ? 12.405 0.721   14.983 1.00 8.68  ? 114 LEU   A CA  1 
ATOM   848  C  C   . LEU   A 1 108 ? 13.056 -0.139  13.862 1.00 8.80  ? 114 LEU   A C   1 
ATOM   849  O  O   . LEU   A 1 108 ? 13.818 0.409   13.038 1.00 9.92  ? 114 LEU   A O   1 
ATOM   850  C  CB  . LEU   A 1 108 ? 11.406 1.715   14.328 1.00 9.86  ? 114 LEU   A CB  1 
ATOM   851  C  CG  . LEU   A 1 108 ? 10.312 1.077   13.423 1.00 10.21 ? 114 LEU   A CG  1 
ATOM   852  C  CD1 . LEU   A 1 108 ? 9.317  0.243   14.283 1.00 11.67 ? 114 LEU   A CD1 1 
ATOM   853  C  CD2 . LEU   A 1 108 ? 9.517  2.170   12.627 1.00 10.84 ? 114 LEU   A CD2 1 
ATOM   854  N  N   . ARG   A 1 109 ? 12.738 -1.410  13.819 1.00 9.55  ? 115 ARG   A N   1 
ATOM   855  C  CA  . ARG   A 1 109 ? 13.325 -2.325  12.837 1.00 10.27 ? 115 ARG   A CA  1 
ATOM   856  C  C   . ARG   A 1 109 ? 12.285 -3.279  12.288 1.00 10.38 ? 115 ARG   A C   1 
ATOM   857  O  O   . ARG   A 1 109 ? 11.236 -3.554  12.897 1.00 11.13 ? 115 ARG   A O   1 
ATOM   858  C  CB  . ARG   A 1 109 ? 14.502 -3.104  13.470 1.00 11.66 ? 115 ARG   A CB  1 
ATOM   859  C  CG  . ARG   A 1 109 ? 14.025 -4.056  14.557 1.00 11.83 ? 115 ARG   A CG  1 
ATOM   860  C  CD  . ARG   A 1 109 ? 15.233 -4.823  15.115 1.00 13.48 ? 115 ARG   A CD  1 
ATOM   861  N  NE  . ARG   A 1 109 ? 16.048 -3.951  15.943 1.00 14.82 ? 115 ARG   A NE  1 
ATOM   862  C  CZ  . ARG   A 1 109 ? 17.339 -3.718  15.775 1.00 14.14 ? 115 ARG   A CZ  1 
ATOM   863  N  NH1 . ARG   A 1 109 ? 17.964 -4.163  14.699 1.00 14.17 ? 115 ARG   A NH1 1 
ATOM   864  N  NH2 . ARG   A 1 109 ? 18.008 -2.976  16.652 1.00 14.84 ? 115 ARG   A NH2 1 
ATOM   865  N  N   . CYS   A 1 110 ? 12.614 -3.843  11.109 1.00 11.52 ? 116 CYS   A N   1 
ATOM   866  C  CA  . CYS   A 1 110 ? 11.811 -4.916  10.500 1.00 15.02 ? 116 CYS   A CA  1 
ATOM   867  C  C   . CYS   A 1 110 ? 12.837 -6.071  10.157 1.00 17.02 ? 116 CYS   A C   1 
ATOM   868  O  O   . CYS   A 1 110 ? 14.003 -6.012  10.545 1.00 17.58 ? 116 CYS   A O   1 
ATOM   869  C  CB  . CYS   A 1 110 ? 11.122 -4.381  9.257  1.00 15.14 ? 116 CYS   A CB  1 
ATOM   870  S  SG  . CYS   A 1 110 ? 12.295 -3.891  7.935  1.00 14.54 ? 116 CYS   A SG  1 
ATOM   871  N  N   . GLN   A 1 111 ? 12.394 -7.152  9.436  1.00 21.40 ? 117 GLN   A N   1 
ATOM   872  C  CA  . GLN   A 1 111 ? 13.323 -8.226  9.067  1.00 23.36 ? 117 GLN   A CA  1 
ATOM   873  C  C   . GLN   A 1 111 ? 14.439 -7.767  8.144  1.00 23.10 ? 117 GLN   A C   1 
ATOM   874  O  O   . GLN   A 1 111 ? 15.483 -8.408  8.112  1.00 25.71 ? 117 GLN   A O   1 
ATOM   875  C  CB  . GLN   A 1 111 ? 12.585 -9.385  8.384  1.00 24.04 ? 117 GLN   A CB  1 
ATOM   876  C  CG  . GLN   A 1 111 ? 11.941 -9.000  7.051  1.00 29.91 ? 117 GLN   A CG  1 
ATOM   877  C  CD  . GLN   A 1 111 ? 10.477 -8.769  7.248  1.00 36.31 ? 117 GLN   A CD  1 
ATOM   878  O  OE1 . GLN   A 1 111 ? 10.040 -8.184  8.259  1.00 37.83 ? 117 GLN   A OE1 1 
ATOM   879  N  NE2 . GLN   A 1 111 ? 9.684  -9.255  6.298  1.00 36.32 ? 117 GLN   A NE2 1 
ATOM   880  N  N   . HIS   A 1 112 ? 14.267 -6.609  7.469  1.00 18.65 ? 118 HIS   A N   1 
ATOM   881  C  CA  . HIS   A 1 112 ? 15.285 -6.099  6.540  1.00 17.74 ? 118 HIS   A CA  1 
ATOM   882  C  C   . HIS   A 1 112 ? 16.353 -5.245  7.189  1.00 17.69 ? 118 HIS   A C   1 
ATOM   883  O  O   . HIS   A 1 112 ? 17.379 -4.967  6.555  1.00 19.32 ? 118 HIS   A O   1 
ATOM   884  C  CB  . HIS   A 1 112 ? 14.620 -5.325  5.398  1.00 16.29 ? 118 HIS   A CB  1 
ATOM   885  C  CG  . HIS   A 1 112 ? 13.567 -6.119  4.705  1.00 18.98 ? 118 HIS   A CG  1 
ATOM   886  N  ND1 . HIS   A 1 112 ? 12.254 -5.828  4.834  1.00 18.34 ? 118 HIS   A ND1 1 
ATOM   887  C  CD2 . HIS   A 1 112 ? 13.687 -7.179  3.868  1.00 21.12 ? 118 HIS   A CD2 1 
ATOM   888  C  CE1 . HIS   A 1 112 ? 11.582 -6.737  4.128  1.00 22.21 ? 118 HIS   A CE1 1 
ATOM   889  N  NE2 . HIS   A 1 112 ? 12.416 -7.561  3.522  1.00 22.11 ? 118 HIS   A NE2 1 
ATOM   890  N  N   . GLY   A 1 113 ? 16.107 -4.773  8.419  1.00 15.54 ? 119 GLY   A N   1 
ATOM   891  C  CA  . GLY   A 1 113 ? 17.081 -3.935  9.075  1.00 14.25 ? 119 GLY   A CA  1 
ATOM   892  C  C   . GLY   A 1 113 ? 16.413 -2.776  9.794  1.00 12.47 ? 119 GLY   A C   1 
ATOM   893  O  O   . GLY   A 1 113 ? 15.215 -2.822  10.096 1.00 13.21 ? 119 GLY   A O   1 
ATOM   894  N  N   . VAL   A 1 114 ? 17.224 -1.736  10.062 1.00 11.07 ? 120 VAL   A N   1 
ATOM   895  C  CA  . VAL   A 1 114 ? 16.720 -0.567  10.800 1.00 10.22 ? 120 VAL   A CA  1 
ATOM   896  C  C   . VAL   A 1 114 ? 15.854 0.322   9.910  1.00 10.03 ? 120 VAL   A C   1 
ATOM   897  O  O   . VAL   A 1 114 ? 16.262 0.668   8.797  1.00 10.66 ? 120 VAL   A O   1 
ATOM   898  C  CB  . VAL   A 1 114 ? 17.907 0.232   11.377 1.00 11.33 ? 120 VAL   A CB  1 
ATOM   899  C  CG1 . VAL   A 1 114 ? 17.414 1.517   12.054 1.00 12.86 ? 120 VAL   A CG1 1 
ATOM   900  C  CG2 . VAL   A 1 114 ? 18.689 -0.618  12.375 1.00 12.51 ? 120 VAL   A CG2 1 
ATOM   901  N  N   . VAL   A 1 115 ? 14.671 0.711   10.387 1.00 9.84  ? 121 VAL   A N   1 
ATOM   902  C  CA  . VAL   A 1 115 ? 13.709 1.514   9.660  1.00 10.94 ? 121 VAL   A CA  1 
ATOM   903  C  C   . VAL   A 1 115 ? 13.831 2.983   10.069 1.00 10.48 ? 121 VAL   A C   1 
ATOM   904  O  O   . VAL   A 1 115 ? 13.690 3.877   9.237  1.00 11.46 ? 121 VAL   A O   1 
ATOM   905  C  CB  . VAL   A 1 115 ? 12.273 0.985   9.946  1.00 11.07 ? 121 VAL   A CB  1 
ATOM   906  C  CG1 . VAL   A 1 115 ? 11.198 1.918   9.344  1.00 11.79 ? 121 VAL   A CG1 1 
ATOM   907  C  CG2 . VAL   A 1 115 ? 12.091 -0.434  9.407  1.00 12.61 ? 121 VAL   A CG2 1 
ATOM   908  N  N   . GLY   A 1 116 ? 14.060 3.250   11.363 1.00 10.37 ? 122 GLY   A N   1 
ATOM   909  C  CA  . GLY   A 1 116 ? 14.131 4.629   11.847 1.00 10.81 ? 122 GLY   A CA  1 
ATOM   910  C  C   . GLY   A 1 116 ? 14.287 4.662   13.362 1.00 10.05 ? 122 GLY   A C   1 
ATOM   911  O  O   . GLY   A 1 116 ? 14.656 3.637   13.961 1.00 9.71  ? 122 GLY   A O   1 
ATOM   912  N  N   . ILE   A 1 117 ? 14.142 5.868   13.960 1.00 9.61  ? 123 ILE   A N   1 
ATOM   913  C  CA  . ILE   A 1 117 ? 14.344 5.998   15.410 1.00 9.53  ? 123 ILE   A CA  1 
ATOM   914  C  C   . ILE   A 1 117 ? 13.187 6.752   16.013 1.00 9.59  ? 123 ILE   A C   1 
ATOM   915  O  O   . ILE   A 1 117 ? 12.579 7.615   15.348 1.00 10.57 ? 123 ILE   A O   1 
ATOM   916  C  CB  . ILE   A 1 117 ? 15.681 6.700   15.811 1.00 10.95 ? 123 ILE   A CB  1 
ATOM   917  C  CG1 . ILE   A 1 117 ? 15.853 8.036   15.027 1.00 11.79 ? 123 ILE   A CG1 1 
ATOM   918  C  CG2 . ILE   A 1 117 ? 16.847 5.758   15.605 1.00 12.31 ? 123 ILE   A CG2 1 
ATOM   919  C  CD1 . ILE   A 1 117 ? 17.088 8.871   15.531 1.00 12.51 ? 123 ILE   A CD1 1 
ATOM   920  N  N   . VAL   A 1 118 ? 12.890 6.485   17.293 1.00 9.93  ? 124 VAL   A N   1 
ATOM   921  C  CA  . VAL   A 1 118 ? 11.829 7.227   17.984 1.00 9.82  ? 124 VAL   A CA  1 
ATOM   922  C  C   . VAL   A 1 118 ? 12.159 8.718   17.983 1.00 10.07 ? 124 VAL   A C   1 
ATOM   923  O  O   . VAL   A 1 118 ? 13.312 9.093   18.311 1.00 10.30 ? 124 VAL   A O   1 
ATOM   924  C  CB  . VAL   A 1 118 ? 11.710 6.739   19.446 1.00 10.44 ? 124 VAL   A CB  1 
ATOM   925  C  CG1 . VAL   A 1 118 ? 10.680 7.588   20.211 1.00 11.78 ? 124 VAL   A CG1 1 
ATOM   926  C  CG2 . VAL   A 1 118 ? 11.280 5.268   19.514 1.00 10.91 ? 124 VAL   A CG2 1 
ATOM   927  N  N   . SER   A 1 119 ? 11.169 9.557   17.612 1.00 10.81 ? 125 SER   A N   1 
ATOM   928  C  CA  . SER   A 1 119 ? 11.357 11.003  17.553 1.00 10.90 ? 125 SER   A CA  1 
ATOM   929  C  C   . SER   A 1 119 ? 10.224 11.757  18.264 1.00 13.14 ? 125 SER   A C   1 
ATOM   930  O  O   . SER   A 1 119 ? 10.466 12.910  18.645 1.00 14.45 ? 125 SER   A O   1 
ATOM   931  C  CB  . SER   A 1 119 ? 11.505 11.422  16.089 1.00 12.37 ? 125 SER   A CB  1 
ATOM   932  O  OG  . SER   A 1 119 ? 11.545 12.835  15.891 1.00 12.26 ? 125 SER   A OG  1 
ATOM   933  N  N   . THR   A 1 120 ? 9.027  11.175  18.410 1.00 12.99 ? 126 THR   A N   1 
ATOM   934  C  CA  . THR   A 1 120 ? 7.917  11.896  19.082 1.00 14.86 ? 126 THR   A CA  1 
ATOM   935  C  C   . THR   A 1 120 ? 7.149  10.926  20.003 1.00 16.87 ? 126 THR   A C   1 
ATOM   936  O  O   . THR   A 1 120 ? 7.291  9.707   19.888 1.00 15.32 ? 126 THR   A O   1 
ATOM   937  C  CB  . THR   A 1 120 ? 6.952  12.566  18.043 1.00 15.90 ? 126 THR   A CB  1 
ATOM   938  O  OG1 . THR   A 1 120 ? 6.144  11.571  17.413 1.00 18.42 ? 126 THR   A OG1 1 
ATOM   939  C  CG2 . THR   A 1 120 ? 7.660  13.386  16.993 1.00 16.76 ? 126 THR   A CG2 1 
ATOM   940  N  N   . GLY   A 1 121 ? 6.362  11.473  20.947 1.00 19.25 ? 127 GLY   A N   1 
ATOM   941  C  CA  . GLY   A 1 121 ? 5.601  10.626  21.863 1.00 20.49 ? 127 GLY   A CA  1 
ATOM   942  C  C   . GLY   A 1 121 ? 4.398  11.344  22.446 1.00 20.88 ? 127 GLY   A C   1 
ATOM   943  O  O   . GLY   A 1 121 ? 3.943  12.363  21.927 1.00 19.94 ? 127 GLY   A O   1 
ATOM   944  N  N   . GLY   A 1 122 ? 3.806  10.673  23.447 1.00 20.92 ? 128 GLY   A N   1 
ATOM   945  C  CA  . GLY   A 1 122 ? 2.671  11.192  24.198 1.00 20.96 ? 128 GLY   A CA  1 
ATOM   946  C  C   . GLY   A 1 122 ? 1.338  10.642  23.736 1.00 21.19 ? 128 GLY   A C   1 
ATOM   947  O  O   . GLY   A 1 122 ? 1.177  10.207  22.593 1.00 21.10 ? 128 GLY   A O   1 
ATOM   948  N  N   . ASN   A 1 123 ? 0.359  10.679  24.637 1.00 21.53 ? 129 ASN   A N   1 
ATOM   949  C  CA  . ASN   A 1 123 ? -1.003 10.321  24.297 1.00 23.03 ? 129 ASN   A CA  1 
ATOM   950  C  C   . ASN   A 1 123 ? -1.178 8.857   23.878 1.00 19.91 ? 129 ASN   A C   1 
ATOM   951  O  O   . ASN   A 1 123 ? -2.196 8.550   23.244 1.00 18.87 ? 129 ASN   A O   1 
ATOM   952  C  CB  . ASN   A 1 123 ? -1.521 11.307  23.203 1.00 26.17 ? 129 ASN   A CB  1 
ATOM   953  C  CG  . ASN   A 1 123 ? -1.623 12.762  23.687 1.00 30.25 ? 129 ASN   A CG  1 
ATOM   954  O  OD1 . ASN   A 1 123 ? -1.713 13.026  24.881 1.00 30.92 ? 129 ASN   A OD1 1 
ATOM   955  N  ND2 . ASN   A 1 123 ? -1.632 13.731  22.778 1.00 31.35 ? 129 ASN   A ND2 1 
ATOM   956  N  N   . GLY   A 1 124 ? -0.260 7.959   24.243 1.00 18.21 ? 130 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 124 ? -0.347 6.589   23.798 1.00 16.38 ? 130 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 124 ? 0.081  6.414   22.339 1.00 13.69 ? 130 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 124 ? -0.140 5.354   21.780 1.00 14.55 ? 130 GLY   A O   1 
ATOM   960  N  N   . LEU   A 1 125 ? 0.789  7.411   21.771 1.00 12.35 ? 131 LEU   A N   1 
ATOM   961  C  CA  . LEU   A 1 125 ? 1.332  7.346   20.411 1.00 12.44 ? 131 LEU   A CA  1 
ATOM   962  C  C   . LEU   A 1 125 ? 2.838  7.418   20.473 1.00 12.09 ? 131 LEU   A C   1 
ATOM   963  O  O   . LEU   A 1 125 ? 3.427  7.967   21.435 1.00 13.56 ? 131 LEU   A O   1 
ATOM   964  C  CB  . LEU   A 1 125 ? 0.839  8.553   19.589 1.00 12.37 ? 131 LEU   A CB  1 
ATOM   965  C  CG  . LEU   A 1 125 ? -0.666 8.541   19.304 1.00 13.63 ? 131 LEU   A CG  1 
ATOM   966  C  CD1 . LEU   A 1 125 ? -1.119 9.934   18.872 1.00 16.68 ? 131 LEU   A CD1 1 
ATOM   967  C  CD2 . LEU   A 1 125 ? -1.041 7.447   18.250 1.00 13.68 ? 131 LEU   A CD2 1 
ATOM   968  N  N   . VAL   A 1 126 ? 3.466  6.847   19.455 1.00 10.60 ? 132 VAL   A N   1 
ATOM   969  C  CA  . VAL   A 1 126 ? 4.919  6.931   19.312 1.00 10.84 ? 132 VAL   A CA  1 
ATOM   970  C  C   . VAL   A 1 126 ? 5.210  7.297   17.825 1.00 11.50 ? 132 VAL   A C   1 
ATOM   971  O  O   . VAL   A 1 126 ? 4.590  6.725   16.919 1.00 12.35 ? 132 VAL   A O   1 
ATOM   972  C  CB  . VAL   A 1 126 ? 5.638  5.627   19.760 1.00 11.67 ? 132 VAL   A CB  1 
ATOM   973  C  CG1 . VAL   A 1 126 ? 5.105  4.399   19.054 1.00 13.65 ? 132 VAL   A CG1 1 
ATOM   974  C  CG2 . VAL   A 1 126 ? 7.174  5.777   19.615 1.00 12.20 ? 132 VAL   A CG2 1 
ATOM   975  N  N   . GLY   A 1 127 ? 6.103  8.230   17.574 1.00 10.97 ? 133 GLY   A N   1 
ATOM   976  C  CA  . GLY   A 1 127 ? 6.435  8.617   16.205 1.00 11.19 ? 133 GLY   A CA  1 
ATOM   977  C  C   . GLY   A 1 127 ? 7.881  8.299   15.919 1.00 10.88 ? 133 GLY   A C   1 
ATOM   978  O  O   . GLY   A 1 127 ? 8.750  8.435   16.801 1.00 12.26 ? 133 GLY   A O   1 
ATOM   979  N  N   . PHE   A 1 128 ? 8.137  7.882   14.687 1.00 10.32 ? 134 PHE   A N   1 
ATOM   980  C  CA  . PHE   A 1 128 ? 9.487  7.462   14.281 1.00 11.12 ? 134 PHE   A CA  1 
ATOM   981  C  C   . PHE   A 1 128 ? 9.953  8.262   13.065 1.00 10.54 ? 134 PHE   A C   1 
ATOM   982  O  O   . PHE   A 1 128 ? 9.206  8.433   12.098 1.00 11.15 ? 134 PHE   A O   1 
ATOM   983  C  CB  . PHE   A 1 128 ? 9.482  5.974   13.854 1.00 10.98 ? 134 PHE   A CB  1 
ATOM   984  C  CG  . PHE   A 1 128 ? 8.869  5.065   14.894 1.00 9.78  ? 134 PHE   A CG  1 
ATOM   985  C  CD1 . PHE   A 1 128 ? 9.613  4.614   15.978 1.00 8.95  ? 134 PHE   A CD1 1 
ATOM   986  C  CD2 . PHE   A 1 128 ? 7.549  4.651   14.771 1.00 11.27 ? 134 PHE   A CD2 1 
ATOM   987  C  CE1 . PHE   A 1 128 ? 9.051  3.738   16.909 1.00 9.82  ? 134 PHE   A CE1 1 
ATOM   988  C  CE2 . PHE   A 1 128 ? 6.994  3.784   15.715 1.00 11.71 ? 134 PHE   A CE2 1 
ATOM   989  C  CZ  . PHE   A 1 128 ? 7.765  3.323   16.771 1.00 10.83 ? 134 PHE   A CZ  1 
ATOM   990  N  N   . ALA   A 1 129 ? 11.176 8.737   13.134 1.00 9.94  ? 135 ALA   A N   1 
ATOM   991  C  CA  . ALA   A 1 129 ? 11.816 9.413   11.968 1.00 10.53 ? 135 ALA   A CA  1 
ATOM   992  C  C   . ALA   A 1 129 ? 12.333 8.325   11.031 1.00 10.99 ? 135 ALA   A C   1 
ATOM   993  O  O   . ALA   A 1 129 ? 13.222 7.566   11.430 1.00 10.84 ? 135 ALA   A O   1 
ATOM   994  C  CB  . ALA   A 1 129 ? 12.966 10.307  12.467 1.00 11.37 ? 135 ALA   A CB  1 
ATOM   995  N  N   . ASP   A 1 130 ? 11.813 8.243   9.793  1.00 10.93 ? 136 ASP   A N   1 
ATOM   996  C  CA  . ASP   A 1 130 ? 12.233 7.241   8.832  1.00 11.67 ? 136 ASP   A CA  1 
ATOM   997  C  C   . ASP   A 1 130 ? 13.638 7.578   8.338  1.00 11.11 ? 136 ASP   A C   1 
ATOM   998  O  O   . ASP   A 1 130 ? 13.979 8.755   8.137  1.00 12.47 ? 136 ASP   A O   1 
ATOM   999  C  CB  . ASP   A 1 130 ? 11.262 7.281   7.614  1.00 12.31 ? 136 ASP   A CB  1 
ATOM   1000 C  CG  . ASP   A 1 130 ? 11.378 6.159   6.591  1.00 17.64 ? 136 ASP   A CG  1 
ATOM   1001 O  OD1 . ASP   A 1 130 ? 11.707 5.055   6.965  1.00 15.23 ? 136 ASP   A OD1 1 
ATOM   1002 O  OD2 . ASP   A 1 130 ? 10.824 6.307   5.471  1.00 21.63 ? 136 ASP   A OD2 1 
ATOM   1003 N  N   . VAL   A 1 131 ? 14.425 6.531   8.097  1.00 10.58 ? 137 VAL   A N   1 
ATOM   1004 C  CA  . VAL   A 1 131 ? 15.747 6.689   7.454  1.00 11.00 ? 137 VAL   A CA  1 
ATOM   1005 C  C   . VAL   A 1 131 ? 15.887 5.874   6.160  1.00 11.72 ? 137 VAL   A C   1 
ATOM   1006 O  O   . VAL   A 1 131 ? 16.973 5.890   5.555  1.00 11.61 ? 137 VAL   A O   1 
ATOM   1007 C  CB  . VAL   A 1 131 ? 16.939 6.373   8.415  1.00 11.08 ? 137 VAL   A CB  1 
ATOM   1008 C  CG1 . VAL   A 1 131 ? 16.938 7.300   9.651  1.00 12.13 ? 137 VAL   A CG1 1 
ATOM   1009 C  CG2 . VAL   A 1 131 ? 16.929 4.889   8.840  1.00 11.46 ? 137 VAL   A CG2 1 
ATOM   1010 N  N   . ARG   A 1 132 ? 14.825 5.162   5.744  1.00 11.14 ? 138 ARG   A N   1 
ATOM   1011 C  CA  . ARG   A 1 132 ? 14.964 4.244   4.623  1.00 11.47 ? 138 ARG   A CA  1 
ATOM   1012 C  C   . ARG   A 1 132 ? 15.244 4.919   3.276  1.00 12.00 ? 138 ARG   A C   1 
ATOM   1013 O  O   . ARG   A 1 132 ? 15.707 4.247   2.322  1.00 13.51 ? 138 ARG   A O   1 
ATOM   1014 C  CB  . ARG   A 1 132 ? 13.729 3.338   4.517  1.00 12.09 ? 138 ARG   A CB  1 
ATOM   1015 C  CG  . ARG   A 1 132 ? 13.604 2.405   5.730  1.00 11.60 ? 138 ARG   A CG  1 
ATOM   1016 C  CD  . ARG   A 1 132 ? 12.343 1.562   5.552  1.00 11.60 ? 138 ARG   A CD  1 
ATOM   1017 N  NE  . ARG   A 1 132 ? 11.169 2.421   5.780  1.00 13.26 ? 138 ARG   A NE  1 
ATOM   1018 C  CZ  . ARG   A 1 132 ? 9.912  1.987   5.841  1.00 13.34 ? 138 ARG   A CZ  1 
ATOM   1019 N  NH1 . ARG   A 1 132 ? 9.628  0.702   5.594  1.00 13.83 ? 138 ARG   A NH1 1 
ATOM   1020 N  NH2 . ARG   A 1 132 ? 8.931  2.832   6.147  1.00 15.55 ? 138 ARG   A NH2 1 
ATOM   1021 N  N   . ASP   A 1 133 ? 14.924 6.228   3.142  1.00 11.98 ? 139 ASP   A N   1 
ATOM   1022 C  CA  . ASP   A 1 133 ? 15.207 6.912   1.868  1.00 12.78 ? 139 ASP   A CA  1 
ATOM   1023 C  C   . ASP   A 1 133 ? 16.645 7.455   1.808  1.00 12.78 ? 139 ASP   A C   1 
ATOM   1024 O  O   . ASP   A 1 133 ? 17.056 7.980   0.764  1.00 13.76 ? 139 ASP   A O   1 
ATOM   1025 C  CB  . ASP   A 1 133 ? 14.224 8.085   1.690  1.00 14.72 ? 139 ASP   A CB  1 
ATOM   1026 C  CG  . ASP   A 1 133 ? 14.377 9.114   2.804  1.00 17.07 ? 139 ASP   A CG  1 
ATOM   1027 O  OD1 . ASP   A 1 133 ? 14.358 8.723   3.994  1.00 17.54 ? 139 ASP   A OD1 1 
ATOM   1028 O  OD2 . ASP   A 1 133 ? 14.505 10.313  2.502  1.00 17.30 ? 139 ASP   A OD2 1 
ATOM   1029 N  N   . LEU   A 1 134 ? 17.409 7.411   2.916  1.00 12.13 ? 140 LEU   A N   1 
ATOM   1030 C  CA  . LEU   A 1 134 ? 18.777 7.983   2.993  1.00 12.50 ? 140 LEU   A CA  1 
ATOM   1031 C  C   . LEU   A 1 134 ? 19.768 6.946   2.484  1.00 11.87 ? 140 LEU   A C   1 
ATOM   1032 O  O   . LEU   A 1 134 ? 20.467 6.258   3.238  1.00 12.32 ? 140 LEU   A O   1 
ATOM   1033 C  CB  . LEU   A 1 134 ? 19.089 8.401   4.443  1.00 12.39 ? 140 LEU   A CB  1 
ATOM   1034 C  CG  . LEU   A 1 134 ? 18.079 9.403   5.066  1.00 13.34 ? 140 LEU   A CG  1 
ATOM   1035 C  CD1 . LEU   A 1 134 ? 18.479 9.722   6.513  1.00 13.95 ? 140 LEU   A CD1 1 
ATOM   1036 C  CD2 . LEU   A 1 134 ? 18.039 10.708  4.244  1.00 14.38 ? 140 LEU   A CD2 1 
ATOM   1037 N  N   . LEU   A 1 135 ? 19.809 6.810   1.147  1.00 11.44 ? 141 LEU   A N   1 
ATOM   1038 C  CA  . LEU   A 1 135 ? 20.573 5.728   0.525  1.00 11.82 ? 141 LEU   A CA  1 
ATOM   1039 C  C   . LEU   A 1 135 ? 22.069 5.873   0.744  1.00 12.75 ? 141 LEU   A C   1 
ATOM   1040 O  O   . LEU   A 1 135 ? 22.797 4.867   0.789  1.00 13.76 ? 141 LEU   A O   1 
ATOM   1041 C  CB  . LEU   A 1 135 ? 20.261 5.605   -1.003 1.00 12.76 ? 141 LEU   A CB  1 
ATOM   1042 C  CG  . LEU   A 1 135 ? 18.744 5.573   -1.359 1.00 14.68 ? 141 LEU   A CG  1 
ATOM   1043 C  CD1 . LEU   A 1 135 ? 18.575 5.270   -2.846 1.00 15.94 ? 141 LEU   A CD1 1 
ATOM   1044 C  CD2 . LEU   A 1 135 ? 17.924 4.583   -0.517 1.00 16.33 ? 141 LEU   A CD2 1 
ATOM   1045 N  N   . TRP   A 1 136 ? 22.529 7.126   0.884  1.00 12.33 ? 142 TRP   A N   1 
ATOM   1046 C  CA  . TRP   A 1 136 ? 23.939 7.379   1.089  1.00 13.44 ? 142 TRP   A CA  1 
ATOM   1047 C  C   . TRP   A 1 136 ? 24.466 6.811   2.398  1.00 14.43 ? 142 TRP   A C   1 
ATOM   1048 O  O   . TRP   A 1 136 ? 25.683 6.697   2.536  1.00 14.99 ? 142 TRP   A O   1 
ATOM   1049 C  CB  . TRP   A 1 136 ? 24.240 8.891   0.978  1.00 12.97 ? 142 TRP   A CB  1 
ATOM   1050 C  CG  . TRP   A 1 136 ? 23.399 9.730   1.900  1.00 13.47 ? 142 TRP   A CG  1 
ATOM   1051 C  CD1 . TRP   A 1 136 ? 22.238 10.370  1.581  1.00 15.60 ? 142 TRP   A CD1 1 
ATOM   1052 C  CD2 . TRP   A 1 136 ? 23.690 10.069  3.268  1.00 13.72 ? 142 TRP   A CD2 1 
ATOM   1053 N  NE1 . TRP   A 1 136 ? 21.759 11.051  2.687  1.00 15.59 ? 142 TRP   A NE1 1 
ATOM   1054 C  CE2 . TRP   A 1 136 ? 22.652 10.903  3.717  1.00 14.78 ? 142 TRP   A CE2 1 
ATOM   1055 C  CE3 . TRP   A 1 136 ? 24.752 9.779   4.137  1.00 14.45 ? 142 TRP   A CE3 1 
ATOM   1056 C  CZ2 . TRP   A 1 136 ? 22.635 11.414  5.011  1.00 14.82 ? 142 TRP   A CZ2 1 
ATOM   1057 C  CZ3 . TRP   A 1 136 ? 24.748 10.323  5.406  1.00 16.07 ? 142 TRP   A CZ3 1 
ATOM   1058 C  CH2 . TRP   A 1 136 ? 23.706 11.131  5.821  1.00 15.31 ? 142 TRP   A CH2 1 
ATOM   1059 N  N   . LEU   A 1 137 ? 23.608 6.445   3.373  1.00 12.45 ? 143 LEU   A N   1 
ATOM   1060 C  CA  . LEU   A 1 137 ? 24.113 5.822   4.603  1.00 14.16 ? 143 LEU   A CA  1 
ATOM   1061 C  C   . LEU   A 1 137 ? 24.814 4.488   4.299  1.00 16.47 ? 143 LEU   A C   1 
ATOM   1062 O  O   . LEU   A 1 137 ? 25.631 4.038   5.117  1.00 17.66 ? 143 LEU   A O   1 
ATOM   1063 C  CB  . LEU   A 1 137 ? 22.966 5.565   5.572  1.00 13.47 ? 143 LEU   A CB  1 
ATOM   1064 C  CG  . LEU   A 1 137 ? 22.397 6.808   6.221  1.00 13.90 ? 143 LEU   A CG  1 
ATOM   1065 C  CD1 . LEU   A 1 137 ? 21.119 6.451   6.991  1.00 15.54 ? 143 LEU   A CD1 1 
ATOM   1066 C  CD2 . LEU   A 1 137 ? 23.441 7.451   7.195  1.00 14.73 ? 143 LEU   A CD2 1 
ATOM   1067 N  N   . ASP   A 1 138 ? 24.519 3.855   3.141  1.00 17.76 ? 144 ASP   A N   1 
ATOM   1068 C  CA  . ASP   A 1 138 ? 25.102 2.546   2.771  1.00 20.31 ? 144 ASP   A CA  1 
ATOM   1069 C  C   . ASP   A 1 138 ? 26.440 2.651   2.055  1.00 24.85 ? 144 ASP   A C   1 
ATOM   1070 O  O   . ASP   A 1 138 ? 27.002 1.609   1.691  1.00 26.12 ? 144 ASP   A O   1 
ATOM   1071 C  CB  . ASP   A 1 138 ? 24.146 1.804   1.795  1.00 20.43 ? 144 ASP   A CB  1 
ATOM   1072 C  CG  . ASP   A 1 138 ? 22.797 1.452   2.359  1.00 23.95 ? 144 ASP   A CG  1 
ATOM   1073 O  OD1 . ASP   A 1 138 ? 22.634 1.540   3.592  1.00 26.76 ? 144 ASP   A OD1 1 
ATOM   1074 O  OD2 . ASP   A 1 138 ? 21.881 1.126   1.570  1.00 28.36 ? 144 ASP   A OD2 1 
ATOM   1075 N  N   . GLU   A 1 139 ? 26.948 3.864   1.804  1.00 26.87 ? 145 GLU   A N   1 
ATOM   1076 C  CA  . GLU   A 1 139 ? 28.209 4.009   1.072  1.00 30.79 ? 145 GLU   A CA  1 
ATOM   1077 C  C   . GLU   A 1 139 ? 29.217 4.924   1.776  1.00 33.73 ? 145 GLU   A C   1 
ATOM   1078 O  O   . GLU   A 1 139 ? 28.846 5.636   2.699  1.00 33.39 ? 145 GLU   A O   1 
ATOM   1079 C  CB  . GLU   A 1 139 ? 27.909 4.509   -0.356 1.00 35.44 ? 145 GLU   A CB  1 
ATOM   1080 C  CG  . GLU   A 1 139 ? 27.124 5.805   -0.389 1.00 42.84 ? 145 GLU   A CG  1 
ATOM   1081 C  CD  . GLU   A 1 139 ? 26.330 6.071   -1.656 1.00 49.79 ? 145 GLU   A CD  1 
ATOM   1082 O  OE1 . GLU   A 1 139 ? 26.107 7.263   -1.981 1.00 49.22 ? 145 GLU   A OE1 1 
ATOM   1083 O  OE2 . GLU   A 1 139 ? 25.923 5.086   -2.318 1.00 52.52 ? 145 GLU   A OE2 1 
ATOM   1084 N  N   . GLU   A 1 140 ? 30.476 4.947   1.285  1.00 36.82 ? 146 GLU   A N   1 
ATOM   1085 C  CA  . GLU   A 1 140 ? 31.580 5.807   1.722  1.00 40.43 ? 146 GLU   A CA  1 
ATOM   1086 C  C   . GLU   A 1 140 ? 32.135 5.395   3.074  1.00 43.19 ? 146 GLU   A C   1 
ATOM   1087 O  O   . GLU   A 1 140 ? 33.360 5.293   3.231  1.00 44.81 ? 146 GLU   A O   1 
ATOM   1088 C  CB  . GLU   A 1 140 ? 31.182 7.299   1.667  1.00 43.88 ? 146 GLU   A CB  1 
ATOM   1089 C  CG  . GLU   A 1 140 ? 32.122 8.268   2.363  1.00 51.04 ? 146 GLU   A CG  1 
ATOM   1090 C  CD  . GLU   A 1 140 ? 32.655 9.377   1.475  1.00 59.93 ? 146 GLU   A CD  1 
ATOM   1091 O  OE1 . GLU   A 1 140 ? 31.841 10.202  1.000  1.00 62.93 ? 146 GLU   A OE1 1 
ATOM   1092 O  OE2 . GLU   A 1 140 ? 33.887 9.420   1.251  1.00 60.89 ? 146 GLU   A OE2 1 
ATOM   1093 N  N   . SER   B 1 1   ? 21.723 -21.466 7.472  1.00 19.62 ? 7   SER   C N   1 
ATOM   1094 C  CA  . SER   B 1 1   ? 20.591 -21.249 8.398  1.00 18.67 ? 7   SER   C CA  1 
ATOM   1095 C  C   . SER   B 1 1   ? 20.534 -22.344 9.476  1.00 17.60 ? 7   SER   C C   1 
ATOM   1096 O  O   . SER   B 1 1   ? 21.188 -23.377 9.332  1.00 17.68 ? 7   SER   C O   1 
ATOM   1097 C  CB  . SER   B 1 1   ? 19.280 -21.248 7.610  1.00 21.37 ? 7   SER   C CB  1 
ATOM   1098 O  OG  . SER   B 1 1   ? 19.114 -22.533 7.027  1.00 25.63 ? 7   SER   C OG  1 
ATOM   1099 N  N   . GLY   B 1 2   ? 19.793 -22.093 10.566 1.00 16.30 ? 8   GLY   C N   1 
ATOM   1100 C  CA  . GLY   B 1 2   ? 19.620 -23.108 11.611 1.00 15.02 ? 8   GLY   C CA  1 
ATOM   1101 C  C   . GLY   B 1 2   ? 19.326 -22.492 12.960 1.00 14.10 ? 8   GLY   C C   1 
ATOM   1102 O  O   . GLY   B 1 2   ? 19.707 -21.354 13.203 1.00 14.57 ? 8   GLY   C O   1 
ATOM   1103 N  N   . ALA   B 1 3   ? 18.668 -23.231 13.859 1.00 12.90 ? 9   ALA   C N   1 
ATOM   1104 C  CA  . ALA   B 1 3   ? 18.354 -22.696 15.193 1.00 13.31 ? 9   ALA   C CA  1 
ATOM   1105 C  C   . ALA   B 1 3   ? 18.487 -23.804 16.237 1.00 12.72 ? 9   ALA   C C   1 
ATOM   1106 O  O   . ALA   B 1 3   ? 18.497 -25.001 15.877 1.00 13.19 ? 9   ALA   C O   1 
ATOM   1107 C  CB  . ALA   B 1 3   ? 16.912 -22.155 15.193 1.00 15.53 ? 9   ALA   C CB  1 
ATOM   1108 N  N   . ILE   B 1 4   ? 18.531 -23.400 17.524 1.00 12.18 ? 10  ILE   C N   1 
ATOM   1109 C  CA  . ILE   B 1 4   ? 18.443 -24.340 18.628 1.00 11.64 ? 10  ILE   C CA  1 
ATOM   1110 C  C   . ILE   B 1 4   ? 17.066 -24.146 19.237 1.00 11.97 ? 10  ILE   C C   1 
ATOM   1111 O  O   . ILE   B 1 4   ? 16.637 -23.007 19.454 1.00 12.78 ? 10  ILE   C O   1 
ATOM   1112 C  CB  . ILE   B 1 4   ? 19.502 -24.067 19.706 1.00 11.46 ? 10  ILE   C CB  1 
ATOM   1113 C  CG1 . ILE   B 1 4   ? 20.948 -23.945 19.134 1.00 12.65 ? 10  ILE   C CG1 1 
ATOM   1114 C  CG2 . ILE   B 1 4   ? 19.409 -25.119 20.803 1.00 12.30 ? 10  ILE   C CG2 1 
ATOM   1115 C  CD1 . ILE   B 1 4   ? 21.897 -23.253 20.152 1.00 13.62 ? 10  ILE   C CD1 1 
ATOM   1116 N  N   . TYR   B 1 5   ? 16.372 -25.245 19.556 1.00 11.68 ? 11  TYR   C N   1 
ATOM   1117 C  CA  . TYR   B 1 5   ? 15.044 -25.192 20.158 1.00 12.78 ? 11  TYR   C CA  1 
ATOM   1118 C  C   . TYR   B 1 5   ? 15.092 -25.873 21.529 1.00 13.30 ? 11  TYR   C C   1 
ATOM   1119 O  O   . TYR   B 1 5   ? 15.171 -27.091 21.596 1.00 15.39 ? 11  TYR   C O   1 
ATOM   1120 C  CB  . TYR   B 1 5   ? 13.988 -25.874 19.238 1.00 13.86 ? 11  TYR   C CB  1 
ATOM   1121 C  CG  . TYR   B 1 5   ? 13.783 -25.140 17.929 1.00 13.60 ? 11  TYR   C CG  1 
ATOM   1122 C  CD1 . TYR   B 1 5   ? 12.969 -24.017 17.860 1.00 13.63 ? 11  TYR   C CD1 1 
ATOM   1123 C  CD2 . TYR   B 1 5   ? 14.491 -25.500 16.788 1.00 15.36 ? 11  TYR   C CD2 1 
ATOM   1124 C  CE1 . TYR   B 1 5   ? 12.799 -23.330 16.669 1.00 15.24 ? 11  TYR   C CE1 1 
ATOM   1125 C  CE2 . TYR   B 1 5   ? 14.330 -24.816 15.588 1.00 17.27 ? 11  TYR   C CE2 1 
ATOM   1126 C  CZ  . TYR   B 1 5   ? 13.510 -23.711 15.546 1.00 17.22 ? 11  TYR   C CZ  1 
ATOM   1127 O  OH  . TYR   B 1 5   ? 13.374 -22.980 14.378 1.00 20.15 ? 11  TYR   C OH  1 
ATOM   1128 N  N   . VAL   B 1 6   ? 15.129 -25.109 22.609 1.00 12.70 ? 12  VAL   C N   1 
ATOM   1129 C  CA  . VAL   B 1 6   ? 15.185 -25.624 23.970 1.00 13.56 ? 12  VAL   C CA  1 
ATOM   1130 C  C   . VAL   B 1 6   ? 14.052 -25.016 24.793 1.00 14.23 ? 12  VAL   C C   1 
ATOM   1131 O  O   . VAL   B 1 6   ? 13.862 -23.814 24.795 1.00 13.39 ? 12  VAL   C O   1 
ATOM   1132 C  CB  . VAL   B 1 6   ? 16.579 -25.377 24.601 1.00 14.40 ? 12  VAL   C CB  1 
ATOM   1133 C  CG1 . VAL   B 1 6   ? 16.998 -23.897 24.484 1.00 14.87 ? 12  VAL   C CG1 1 
ATOM   1134 C  CG2 . VAL   B 1 6   ? 16.603 -25.859 26.046 1.00 16.47 ? 12  VAL   C CG2 1 
ATOM   1135 N  N   . GLY   B 1 7   ? 13.256 -25.842 25.483 1.00 15.06 ? 13  GLY   C N   1 
ATOM   1136 C  CA  . GLY   B 1 7   ? 12.118 -25.298 26.237 1.00 15.51 ? 13  GLY   C CA  1 
ATOM   1137 C  C   . GLY   B 1 7   ? 11.190 -24.471 25.354 1.00 15.49 ? 13  GLY   C C   1 
ATOM   1138 O  O   . GLY   B 1 7   ? 10.892 -24.878 24.219 1.00 16.12 ? 13  GLY   C O   1 
ATOM   1139 N  N   . ASN   B 1 8   ? 10.844 -23.257 25.786 1.00 15.18 ? 14  ASN   C N   1 
ATOM   1140 C  CA  . ASN   B 1 8   ? 10.057 -22.361 24.940 1.00 16.37 ? 14  ASN   C CA  1 
ATOM   1141 C  C   . ASN   B 1 8   ? 10.946 -21.252 24.379 1.00 15.43 ? 14  ASN   C C   1 
ATOM   1142 O  O   . ASN   B 1 8   ? 10.490 -20.122 24.214 1.00 16.23 ? 14  ASN   C O   1 
ATOM   1143 C  CB  . ASN   B 1 8   ? 8.817  -21.789 25.659 1.00 18.53 ? 14  ASN   C CB  1 
ATOM   1144 C  CG  . ASN   B 1 8   ? 7.732  -22.857 25.826 1.00 25.33 ? 14  ASN   C CG  1 
ATOM   1145 O  OD1 . ASN   B 1 8   ? 6.834  -22.990 24.991 1.00 29.65 ? 14  ASN   C OD1 1 
ATOM   1146 N  ND2 . ASN   B 1 8   ? 7.838  -23.678 26.870 1.00 26.50 ? 14  ASN   C ND2 1 
ATOM   1147 N  N   . TYR   B 1 9   ? 12.174 -21.637 23.995 1.00 13.88 ? 15  TYR   C N   1 
ATOM   1148 C  CA  . TYR   B 1 9   ? 13.111 -20.671 23.411 1.00 13.44 ? 15  TYR   C CA  1 
ATOM   1149 C  C   . TYR   B 1 9   ? 13.603 -21.159 22.032 1.00 12.75 ? 15  TYR   C C   1 
ATOM   1150 O  O   . TYR   B 1 9   ? 13.792 -22.370 21.811 1.00 13.37 ? 15  TYR   C O   1 
ATOM   1151 C  CB  . TYR   B 1 9   ? 14.347 -20.508 24.325 1.00 13.74 ? 15  TYR   C CB  1 
ATOM   1152 C  CG  . TYR   B 1 9   ? 14.021 -19.995 25.721 1.00 15.18 ? 15  TYR   C CG  1 
ATOM   1153 C  CD1 . TYR   B 1 9   ? 13.473 -18.742 25.903 1.00 17.22 ? 15  TYR   C CD1 1 
ATOM   1154 C  CD2 . TYR   B 1 9   ? 14.354 -20.734 26.855 1.00 16.67 ? 15  TYR   C CD2 1 
ATOM   1155 C  CE1 . TYR   B 1 9   ? 13.195 -18.255 27.179 1.00 19.31 ? 15  TYR   C CE1 1 
ATOM   1156 C  CE2 . TYR   B 1 9   ? 14.113 -20.239 28.141 1.00 19.58 ? 15  TYR   C CE2 1 
ATOM   1157 C  CZ  . TYR   B 1 9   ? 13.547 -18.993 28.287 1.00 21.86 ? 15  TYR   C CZ  1 
ATOM   1158 O  OH  . TYR   B 1 9   ? 13.278 -18.468 29.536 1.00 27.02 ? 15  TYR   C OH  1 
ATOM   1159 N  N   . ARG   B 1 10  ? 13.872 -20.211 21.133 1.00 11.56 ? 16  ARG   C N   1 
ATOM   1160 C  CA  . ARG   B 1 10  ? 14.476 -20.453 19.818 1.00 11.99 ? 16  ARG   C CA  1 
ATOM   1161 C  C   . ARG   B 1 10  ? 15.726 -19.571 19.803 1.00 11.76 ? 16  ARG   C C   1 
ATOM   1162 O  O   . ARG   B 1 10  ? 15.636 -18.365 20.040 1.00 12.99 ? 16  ARG   C O   1 
ATOM   1163 C  CB  . ARG   B 1 10  ? 13.473 -20.046 18.691 1.00 12.72 ? 16  ARG   C CB  1 
ATOM   1164 C  CG  . ARG   B 1 10  ? 14.109 -19.832 17.304 1.00 13.59 ? 16  ARG   C CG  1 
ATOM   1165 C  CD  . ARG   B 1 10  ? 13.065 -19.587 16.239 1.00 13.71 ? 16  ARG   C CD  1 
ATOM   1166 N  NE  . ARG   B 1 10  ? 13.526 -18.633 15.209 1.00 15.75 ? 16  ARG   C NE  1 
ATOM   1167 C  CZ  . ARG   B 1 10  ? 14.019 -18.956 14.012 1.00 17.77 ? 16  ARG   C CZ  1 
ATOM   1168 N  NH1 . ARG   B 1 10  ? 14.229 -20.236 13.688 1.00 18.32 ? 16  ARG   C NH1 1 
ATOM   1169 N  NH2 . ARG   B 1 10  ? 14.360 -18.004 13.149 1.00 17.83 ? 16  ARG   C NH2 1 
ATOM   1170 N  N   . VAL   B 1 11  ? 16.898 -20.199 19.599 1.00 11.63 ? 17  VAL   C N   1 
ATOM   1171 C  CA  . VAL   B 1 11  ? 18.180 -19.470 19.580 1.00 10.36 ? 17  VAL   C CA  1 
ATOM   1172 C  C   . VAL   B 1 11  ? 18.664 -19.422 18.136 1.00 11.45 ? 17  VAL   C C   1 
ATOM   1173 O  O   . VAL   B 1 11  ? 18.838 -20.498 17.512 1.00 11.98 ? 17  VAL   C O   1 
ATOM   1174 C  CB  . VAL   B 1 11  ? 19.251 -20.197 20.433 1.00 11.18 ? 17  VAL   C CB  1 
ATOM   1175 C  CG1 . VAL   B 1 11  ? 20.497 -19.326 20.520 1.00 13.28 ? 17  VAL   C CG1 1 
ATOM   1176 C  CG2 . VAL   B 1 11  ? 18.726 -20.534 21.843 1.00 12.52 ? 17  VAL   C CG2 1 
ATOM   1177 N  N   . VAL   B 1 12  ? 18.901 -18.205 17.587 1.00 10.19 ? 18  VAL   C N   1 
ATOM   1178 C  CA  A VAL   B 1 12  ? 19.363 -18.048 16.197 0.50 10.00 ? 18  VAL   C CA  1 
ATOM   1179 C  CA  B VAL   B 1 12  ? 19.321 -18.070 16.193 0.50 11.56 ? 18  VAL   C CA  1 
ATOM   1180 C  C   . VAL   B 1 12  ? 20.521 -17.078 16.136 1.00 11.16 ? 18  VAL   C C   1 
ATOM   1181 O  O   . VAL   B 1 12  ? 20.754 -16.293 17.074 1.00 11.01 ? 18  VAL   C O   1 
ATOM   1182 C  CB  A VAL   B 1 12  ? 18.229 -17.524 15.263 0.50 10.21 ? 18  VAL   C CB  1 
ATOM   1183 C  CB  B VAL   B 1 12  ? 18.050 -17.535 15.429 0.50 14.81 ? 18  VAL   C CB  1 
ATOM   1184 C  CG1 A VAL   B 1 12  ? 17.242 -18.629 14.969 0.50 12.68 ? 18  VAL   C CG1 1 
ATOM   1185 C  CG1 B VAL   B 1 12  ? 18.295 -17.300 13.949 0.50 15.32 ? 18  VAL   C CG1 1 
ATOM   1186 C  CG2 A VAL   B 1 12  ? 17.588 -16.226 15.797 0.50 7.80  ? 18  VAL   C CG2 1 
ATOM   1187 C  CG2 B VAL   B 1 12  ? 16.888 -18.499 15.592 0.50 17.96 ? 18  VAL   C CG2 1 
ATOM   1188 N  N   . ASN   B 1 13  ? 21.199 -17.004 14.965 1.00 11.32 ? 19  ASN   C N   1 
ATOM   1189 C  CA  . ASN   B 1 13  ? 22.198 -15.975 14.750 1.00 10.71 ? 19  ASN   C CA  1 
ATOM   1190 C  C   . ASN   B 1 13  ? 21.378 -14.646 14.682 1.00 10.97 ? 19  ASN   C C   1 
ATOM   1191 O  O   . ASN   B 1 13  ? 20.372 -14.549 13.980 1.00 11.32 ? 19  ASN   C O   1 
ATOM   1192 C  CB  . ASN   B 1 13  ? 22.864 -16.166 13.386 1.00 10.97 ? 19  ASN   C CB  1 
ATOM   1193 C  CG  . ASN   B 1 13  ? 23.725 -17.421 13.329 1.00 11.18 ? 19  ASN   C CG  1 
ATOM   1194 O  OD1 . ASN   B 1 13  ? 23.255 -18.480 12.888 1.00 12.15 ? 19  ASN   C OD1 1 
ATOM   1195 N  ND2 . ASN   B 1 13  ? 24.953 -17.310 13.806 1.00 11.47 ? 19  ASN   C ND2 1 
ATOM   1196 N  N   . ARG   B 1 14  ? 21.868 -13.614 15.398 1.00 11.19 ? 20  ARG   C N   1 
ATOM   1197 C  CA  . ARG   B 1 14  ? 21.158 -12.325 15.409 1.00 11.26 ? 20  ARG   C CA  1 
ATOM   1198 C  C   . ARG   B 1 14  ? 21.021 -11.785 13.979 1.00 12.73 ? 20  ARG   C C   1 
ATOM   1199 O  O   . ARG   B 1 14  ? 19.968 -11.251 13.629 1.00 12.73 ? 20  ARG   C O   1 
ATOM   1200 C  CB  . ARG   B 1 14  ? 21.928 -11.323 16.285 1.00 10.40 ? 20  ARG   C CB  1 
ATOM   1201 C  CG  . ARG   B 1 14  ? 21.120 -9.999  16.518 1.00 11.40 ? 20  ARG   C CG  1 
ATOM   1202 C  CD  . ARG   B 1 14  ? 22.005 -9.037  17.298 1.00 12.28 ? 20  ARG   C CD  1 
ATOM   1203 N  NE  . ARG   B 1 14  ? 21.338 -7.796  17.734 1.00 13.36 ? 20  ARG   C NE  1 
ATOM   1204 C  CZ  . ARG   B 1 14  ? 21.246 -6.693  17.000 1.00 14.42 ? 20  ARG   C CZ  1 
ATOM   1205 N  NH1 . ARG   B 1 14  ? 21.642 -6.697  15.733 1.00 15.38 ? 20  ARG   C NH1 1 
ATOM   1206 N  NH2 . ARG   B 1 14  ? 20.731 -5.584  17.522 1.00 14.10 ? 20  ARG   C NH2 1 
ATOM   1207 N  N   . HIS   B 1 15  ? 22.026 -11.993 13.125 1.00 12.88 ? 21  HIS   C N   1 
ATOM   1208 C  CA  . HIS   B 1 15  ? 21.956 -11.456 11.752 1.00 12.99 ? 21  HIS   C CA  1 
ATOM   1209 C  C   . HIS   B 1 15  ? 20.954 -12.181 10.848 1.00 13.47 ? 21  HIS   C C   1 
ATOM   1210 O  O   . HIS   B 1 15  ? 20.648 -11.696 9.768  1.00 15.15 ? 21  HIS   C O   1 
ATOM   1211 C  CB  . HIS   B 1 15  ? 23.368 -11.380 11.089 1.00 12.59 ? 21  HIS   C CB  1 
ATOM   1212 C  CG  . HIS   B 1 15  ? 23.933 -12.699 10.635 1.00 12.55 ? 21  HIS   C CG  1 
ATOM   1213 N  ND1 . HIS   B 1 15  ? 24.681 -13.498 11.490 1.00 13.24 ? 21  HIS   C ND1 1 
ATOM   1214 C  CD2 . HIS   B 1 15  ? 23.934 -13.244 9.394  1.00 12.82 ? 21  HIS   C CD2 1 
ATOM   1215 C  CE1 . HIS   B 1 15  ? 25.058 -14.559 10.773 1.00 13.91 ? 21  HIS   C CE1 1 
ATOM   1216 N  NE2 . HIS   B 1 15  ? 24.641 -14.446 9.496  1.00 13.16 ? 21  HIS   C NE2 1 
ATOM   1217 N  N   . LEU   B 1 16  ? 20.426 -13.325 11.281 1.00 12.39 ? 22  LEU   C N   1 
ATOM   1218 C  CA  . LEU   B 1 16  ? 19.395 -14.068 10.536 1.00 13.55 ? 22  LEU   C CA  1 
ATOM   1219 C  C   . LEU   B 1 16  ? 18.013 -14.018 11.207 1.00 14.72 ? 22  LEU   C C   1 
ATOM   1220 O  O   . LEU   B 1 16  ? 17.105 -14.721 10.757 1.00 15.35 ? 22  LEU   C O   1 
ATOM   1221 C  CB  . LEU   B 1 16  ? 19.851 -15.525 10.325 1.00 14.24 ? 22  LEU   C CB  1 
ATOM   1222 C  CG  . LEU   B 1 16  ? 21.156 -15.646 9.555  1.00 15.12 ? 22  LEU   C CG  1 
ATOM   1223 C  CD1 . LEU   B 1 16  ? 21.598 -17.122 9.470  1.00 15.49 ? 22  LEU   C CD1 1 
ATOM   1224 C  CD2 . LEU   B 1 16  ? 21.042 -15.053 8.151  1.00 14.76 ? 22  LEU   C CD2 1 
ATOM   1225 N  N   . ALA   B 1 17  ? 17.858 -13.237 12.284 1.00 14.66 ? 23  ALA   C N   1 
ATOM   1226 C  CA  . ALA   B 1 17  ? 16.578 -13.176 13.011 1.00 15.23 ? 23  ALA   C CA  1 
ATOM   1227 C  C   . ALA   B 1 17  ? 15.445 -12.661 12.123 1.00 16.40 ? 23  ALA   C C   1 
ATOM   1228 O  O   . ALA   B 1 17  ? 15.650 -11.747 11.316 1.00 16.71 ? 23  ALA   C O   1 
ATOM   1229 C  CB  . ALA   B 1 17  ? 16.704 -12.308 14.263 1.00 16.16 ? 23  ALA   C CB  1 
ATOM   1230 N  N   . THR   B 1 18  ? 14.274 -13.253 12.260 1.00 16.78 ? 24  THR   C N   1 
ATOM   1231 C  CA  . THR   B 1 18  ? 13.085 -12.857 11.489 1.00 17.05 ? 24  THR   C CA  1 
ATOM   1232 C  C   . THR   B 1 18  ? 12.286 -11.760 12.246 1.00 17.30 ? 24  THR   C C   1 
ATOM   1233 O  O   . THR   B 1 18  ? 12.547 -11.445 13.411 1.00 17.92 ? 24  THR   C O   1 
ATOM   1234 C  CB  . THR   B 1 18  ? 12.182 -14.080 11.261 1.00 17.82 ? 24  THR   C CB  1 
ATOM   1235 O  OG1 . THR   B 1 18  ? 11.658 -14.486 12.519 1.00 17.40 ? 24  THR   C OG1 1 
ATOM   1236 C  CG2 . THR   B 1 18  ? 12.882 -15.241 10.568 1.00 18.64 ? 24  THR   C CG2 1 
ATOM   1237 N  N   . HIS   B 1 19  ? 11.227 -11.187 11.577 1.00 18.54 ? 25  HIS   C N   1 
ATOM   1238 C  CA  . HIS   B 1 19  ? 10.346 -10.248 12.273 1.00 20.07 ? 25  HIS   C CA  1 
ATOM   1239 C  C   . HIS   B 1 19  ? 9.645  -10.963 13.429 1.00 17.94 ? 25  HIS   C C   1 
ATOM   1240 O  O   . HIS   B 1 19  ? 9.586  -10.372 14.517 1.00 18.37 ? 25  HIS   C O   1 
ATOM   1241 C  CB  . HIS   B 1 19  ? 9.289  -9.679  11.329 1.00 22.08 ? 25  HIS   C CB  1 
ATOM   1242 C  CG  . HIS   B 1 19  ? 8.184  -8.933  12.044 1.00 26.87 ? 25  HIS   C CG  1 
ATOM   1243 N  ND1 . HIS   B 1 19  ? 8.422  -7.732  12.693 1.00 29.23 ? 25  HIS   C ND1 1 
ATOM   1244 C  CD2 . HIS   B 1 19  ? 6.898  -9.292  12.259 1.00 29.73 ? 25  HIS   C CD2 1 
ATOM   1245 C  CE1 . HIS   B 1 19  ? 7.251  -7.338  13.176 1.00 30.41 ? 25  HIS   C CE1 1 
ATOM   1246 N  NE2 . HIS   B 1 19  ? 6.305  -8.258  12.973 1.00 30.91 ? 25  HIS   C NE2 1 
ATOM   1247 N  N   . ASN   B 1 20  ? 9.266  -12.255 13.261 1.00 18.63 ? 26  ASN   C N   1 
ATOM   1248 C  CA  . ASN   B 1 20  ? 8.615  -12.970 14.350 1.00 18.85 ? 26  ASN   C CA  1 
ATOM   1249 C  C   . ASN   B 1 20  ? 9.554  -13.112 15.537 1.00 17.41 ? 26  ASN   C C   1 
ATOM   1250 O  O   . ASN   B 1 20  ? 9.127  -12.984 16.673 1.00 16.61 ? 26  ASN   C O   1 
ATOM   1251 C  CB  . ASN   B 1 20  ? 8.112  -14.330 13.907 1.00 18.67 ? 26  ASN   C CB  1 
ATOM   1252 C  CG  . ASN   B 1 20  ? 7.283  -14.999 15.000 1.00 24.64 ? 26  ASN   C CG  1 
ATOM   1253 O  OD1 . ASN   B 1 20  ? 6.144  -14.580 15.251 1.00 27.70 ? 26  ASN   C OD1 1 
ATOM   1254 N  ND2 . ASN   B 1 20  ? 7.872  -15.985 15.721 1.00 26.73 ? 26  ASN   C ND2 1 
ATOM   1255 N  N   . ASP   B 1 21  ? 10.867 -13.335 15.284 1.00 16.59 ? 27  ASP   C N   1 
ATOM   1256 C  CA  . ASP   B 1 21  ? 11.834 -13.410 16.380 1.00 16.60 ? 27  ASP   C CA  1 
ATOM   1257 C  C   . ASP   B 1 21  ? 11.867 -12.091 17.174 1.00 15.96 ? 27  ASP   C C   1 
ATOM   1258 O  O   . ASP   B 1 21  ? 11.817 -12.096 18.397 1.00 15.76 ? 27  ASP   C O   1 
ATOM   1259 C  CB  . ASP   B 1 21  ? 13.260 -13.704 15.840 1.00 15.65 ? 27  ASP   C CB  1 
ATOM   1260 C  CG  . ASP   B 1 21  ? 13.456 -15.135 15.375 1.00 16.51 ? 27  ASP   C CG  1 
ATOM   1261 O  OD1 . ASP   B 1 21  ? 12.886 -16.046 16.006 1.00 16.26 ? 27  ASP   C OD1 1 
ATOM   1262 O  OD2 . ASP   B 1 21  ? 14.133 -15.343 14.343 1.00 14.68 ? 27  ASP   C OD2 1 
ATOM   1263 N  N   . TRP   B 1 22  ? 11.956 -10.953 16.448 1.00 16.52 ? 28  TRP   C N   1 
ATOM   1264 C  CA  . TRP   B 1 22  ? 11.993 -9.650  17.122 1.00 16.63 ? 28  TRP   C CA  1 
ATOM   1265 C  C   . TRP   B 1 22  ? 10.684 -9.295  17.853 1.00 16.65 ? 28  TRP   C C   1 
ATOM   1266 O  O   . TRP   B 1 22  ? 10.721 -8.664  18.926 1.00 17.18 ? 28  TRP   C O   1 
ATOM   1267 C  CB  . TRP   B 1 22  ? 12.367 -8.546  16.121 1.00 16.01 ? 28  TRP   C CB  1 
ATOM   1268 C  CG  . TRP   B 1 22  ? 13.849 -8.491  15.856 1.00 16.14 ? 28  TRP   C CG  1 
ATOM   1269 C  CD1 . TRP   B 1 22  ? 14.497 -8.963  14.759 1.00 18.04 ? 28  TRP   C CD1 1 
ATOM   1270 C  CD2 . TRP   B 1 22  ? 14.856 -7.912  16.704 1.00 15.24 ? 28  TRP   C CD2 1 
ATOM   1271 N  NE1 . TRP   B 1 22  ? 15.853 -8.703  14.861 1.00 17.27 ? 28  TRP   C NE1 1 
ATOM   1272 C  CE2 . TRP   B 1 22  ? 16.106 -8.107  16.068 1.00 16.28 ? 28  TRP   C CE2 1 
ATOM   1273 C  CE3 . TRP   B 1 22  ? 14.829 -7.255  17.932 1.00 17.44 ? 28  TRP   C CE3 1 
ATOM   1274 C  CZ2 . TRP   B 1 22  ? 17.282 -7.547  16.550 1.00 15.83 ? 28  TRP   C CZ2 1 
ATOM   1275 C  CZ3 . TRP   B 1 22  ? 16.030 -6.769  18.449 1.00 18.29 ? 28  TRP   C CZ3 1 
ATOM   1276 C  CH2 . TRP   B 1 22  ? 17.245 -6.961  17.765 1.00 16.99 ? 28  TRP   C CH2 1 
ATOM   1277 N  N   . ALA   B 1 23  ? 9.557  -9.759  17.305 1.00 16.65 ? 29  ALA   C N   1 
ATOM   1278 C  CA  . ALA   B 1 23  ? 8.227  -9.528  17.913 1.00 18.19 ? 29  ALA   C CA  1 
ATOM   1279 C  C   . ALA   B 1 23  ? 7.980  -10.407 19.141 1.00 19.41 ? 29  ALA   C C   1 
ATOM   1280 O  O   . ALA   B 1 23  ? 7.045  -10.161 19.906 1.00 20.75 ? 29  ALA   C O   1 
ATOM   1281 C  CB  . ALA   B 1 23  ? 7.126  -9.751  16.889 1.00 18.26 ? 29  ALA   C CB  1 
ATOM   1282 N  N   . ASN   B 1 24  ? 8.834  -11.435 19.351 1.00 18.64 ? 30  ASN   C N   1 
ATOM   1283 C  CA  . ASN   B 1 24  ? 8.716  -12.320 20.499 1.00 18.30 ? 30  ASN   C CA  1 
ATOM   1284 C  C   . ASN   B 1 24  ? 10.078 -12.388 21.197 1.00 17.22 ? 30  ASN   C C   1 
ATOM   1285 O  O   . ASN   B 1 24  ? 10.514 -13.452 21.617 1.00 15.67 ? 30  ASN   C O   1 
ATOM   1286 C  CB  . ASN   B 1 24  ? 8.258  -13.701 19.996 1.00 17.94 ? 30  ASN   C CB  1 
ATOM   1287 C  CG  . ASN   B 1 24  ? 6.830  -13.652 19.505 1.00 21.12 ? 30  ASN   C CG  1 
ATOM   1288 O  OD1 . ASN   B 1 24  ? 5.896  -13.678 20.320 1.00 21.37 ? 30  ASN   C OD1 1 
ATOM   1289 N  ND2 . ASN   B 1 24  ? 6.646  -13.529 18.195 1.00 21.08 ? 30  ASN   C ND2 1 
ATOM   1290 N  N   . LEU   B 1 25  ? 10.800 -11.267 21.279 1.00 16.86 ? 31  LEU   C N   1 
ATOM   1291 C  CA  . LEU   B 1 25  ? 12.168 -11.235 21.784 1.00 15.99 ? 31  LEU   C CA  1 
ATOM   1292 C  C   . LEU   B 1 25  ? 12.311 -11.528 23.249 1.00 17.33 ? 31  LEU   C C   1 
ATOM   1293 O  O   . LEU   B 1 25  ? 11.549 -10.999 24.083 1.00 18.86 ? 31  LEU   C O   1 
ATOM   1294 C  CB  . LEU   B 1 25  ? 12.774 -9.849  21.462 1.00 15.83 ? 31  LEU   C CB  1 
ATOM   1295 C  CG  . LEU   B 1 25  ? 14.229 -9.661  21.865 1.00 15.97 ? 31  LEU   C CG  1 
ATOM   1296 C  CD1 . LEU   B 1 25  ? 15.130 -10.517 20.987 1.00 14.66 ? 31  LEU   C CD1 1 
ATOM   1297 C  CD2 . LEU   B 1 25  ? 14.662 -8.203  21.694 1.00 17.26 ? 31  LEU   C CD2 1 
ATOM   1298 N  N   . VAL   B 1 26  ? 13.307 -12.379 23.584 1.00 16.48 ? 32  VAL   C N   1 
ATOM   1299 C  CA  . VAL   B 1 26  ? 13.658 -12.645 24.961 1.00 16.75 ? 32  VAL   C CA  1 
ATOM   1300 C  C   . VAL   B 1 26  ? 14.973 -11.929 25.286 1.00 17.70 ? 32  VAL   C C   1 
ATOM   1301 O  O   . VAL   B 1 26  ? 15.080 -11.252 26.309 1.00 19.18 ? 32  VAL   C O   1 
ATOM   1302 C  CB  . VAL   B 1 26  ? 13.775 -14.168 25.224 1.00 17.57 ? 32  VAL   C CB  1 
ATOM   1303 C  CG1 . VAL   B 1 26  ? 14.310 -14.447 26.623 1.00 18.75 ? 32  VAL   C CG1 1 
ATOM   1304 C  CG2 . VAL   B 1 26  ? 12.430 -14.869 25.004 1.00 17.78 ? 32  VAL   C CG2 1 
ATOM   1305 N  N   . TRP   B 1 27  ? 15.996 -12.086 24.419 1.00 15.24 ? 33  TRP   C N   1 
ATOM   1306 C  CA  . TRP   B 1 27  ? 17.319 -11.548 24.708 1.00 15.04 ? 33  TRP   C CA  1 
ATOM   1307 C  C   . TRP   B 1 27  ? 18.099 -11.495 23.413 1.00 14.25 ? 33  TRP   C C   1 
ATOM   1308 O  O   . TRP   B 1 27  ? 17.899 -12.366 22.559 1.00 14.67 ? 33  TRP   C O   1 
ATOM   1309 C  CB  . TRP   B 1 27  ? 18.027 -12.451 25.758 1.00 15.81 ? 33  TRP   C CB  1 
ATOM   1310 C  CG  . TRP   B 1 27  ? 19.507 -12.200 25.951 1.00 16.31 ? 33  TRP   C CG  1 
ATOM   1311 C  CD1 . TRP   B 1 27  ? 20.090 -11.260 26.752 1.00 18.42 ? 33  TRP   C CD1 1 
ATOM   1312 C  CD2 . TRP   B 1 27  ? 20.592 -12.902 25.300 1.00 15.46 ? 33  TRP   C CD2 1 
ATOM   1313 N  NE1 . TRP   B 1 27  ? 21.480 -11.354 26.670 1.00 19.06 ? 33  TRP   C NE1 1 
ATOM   1314 C  CE2 . TRP   B 1 27  ? 21.805 -12.352 25.779 1.00 16.68 ? 33  TRP   C CE2 1 
ATOM   1315 C  CE3 . TRP   B 1 27  ? 20.650 -13.934 24.352 1.00 15.67 ? 33  TRP   C CE3 1 
ATOM   1316 C  CZ2 . TRP   B 1 27  ? 23.061 -12.858 25.393 1.00 17.06 ? 33  TRP   C CZ2 1 
ATOM   1317 C  CZ3 . TRP   B 1 27  ? 21.889 -14.430 23.987 1.00 16.69 ? 33  TRP   C CZ3 1 
ATOM   1318 C  CH2 . TRP   B 1 27  ? 23.067 -13.854 24.460 1.00 16.37 ? 33  TRP   C CH2 1 
ATOM   1319 N  N   . GLU   B 1 28  ? 18.963 -10.500 23.250 1.00 13.72 ? 34  GLU   C N   1 
ATOM   1320 C  CA  . GLU   B 1 28  ? 19.825 -10.421 22.080 1.00 14.51 ? 34  GLU   C CA  1 
ATOM   1321 C  C   . GLU   B 1 28  ? 21.143 -9.740  22.404 1.00 14.57 ? 34  GLU   C C   1 
ATOM   1322 O  O   . GLU   B 1 28  ? 21.192 -8.884  23.297 1.00 14.35 ? 34  GLU   C O   1 
ATOM   1323 C  CB  . GLU   B 1 28  ? 19.152 -9.742  20.881 1.00 15.78 ? 34  GLU   C CB  1 
ATOM   1324 C  CG  . GLU   B 1 28  ? 18.573 -8.369  21.170 1.00 15.70 ? 34  GLU   C CG  1 
ATOM   1325 C  CD  . GLU   B 1 28  ? 19.559 -7.211  21.104 1.00 17.70 ? 34  GLU   C CD  1 
ATOM   1326 O  OE1 . GLU   B 1 28  ? 19.338 -6.188  21.798 1.00 19.82 ? 34  GLU   C OE1 1 
ATOM   1327 O  OE2 . GLU   B 1 28  ? 20.558 -7.320  20.349 1.00 15.95 ? 34  GLU   C OE2 1 
ATOM   1328 N  N   . ASP   B 1 29  ? 22.218 -10.113 21.688 1.00 13.11 ? 35  ASP   C N   1 
ATOM   1329 C  CA  . ASP   B 1 29  ? 23.511 -9.491  21.935 1.00 13.72 ? 35  ASP   C CA  1 
ATOM   1330 C  C   . ASP   B 1 29  ? 24.257 -9.451  20.611 1.00 13.69 ? 35  ASP   C C   1 
ATOM   1331 O  O   . ASP   B 1 29  ? 24.686 -10.493 20.119 1.00 13.08 ? 35  ASP   C O   1 
ATOM   1332 C  CB  . ASP   B 1 29  ? 24.266 -10.283 23.016 1.00 14.67 ? 35  ASP   C CB  1 
ATOM   1333 C  CG  . ASP   B 1 29  ? 25.593 -9.697  23.430 1.00 18.65 ? 35  ASP   C CG  1 
ATOM   1334 O  OD1 . ASP   B 1 29  ? 26.296 -9.148  22.571 1.00 20.33 ? 35  ASP   C OD1 1 
ATOM   1335 O  OD2 . ASP   B 1 29  ? 25.982 -9.881  24.591 1.00 18.78 ? 35  ASP   C OD2 1 
ATOM   1336 N  N   . SER   B 1 30  ? 24.430 -8.253  20.022 1.00 13.10 ? 36  SER   C N   1 
ATOM   1337 C  CA  A SER   B 1 30  ? 25.109 -8.129  18.739 0.50 13.78 ? 36  SER   C CA  1 
ATOM   1338 C  CA  B SER   B 1 30  ? 25.102 -8.162  18.729 0.50 13.42 ? 36  SER   C CA  1 
ATOM   1339 C  C   . SER   B 1 30  ? 26.573 -8.555  18.821 1.00 13.78 ? 36  SER   C C   1 
ATOM   1340 O  O   . SER   B 1 30  ? 27.089 -9.134  17.856 1.00 13.43 ? 36  SER   C O   1 
ATOM   1341 C  CB  A SER   B 1 30  ? 25.010 -6.688  18.242 0.50 16.35 ? 36  SER   C CB  1 
ATOM   1342 C  CB  B SER   B 1 30  ? 24.955 -6.761  18.149 0.50 15.29 ? 36  SER   C CB  1 
ATOM   1343 O  OG  A SER   B 1 30  ? 25.945 -6.397  17.216 0.50 18.03 ? 36  SER   C OG  1 
ATOM   1344 O  OG  B SER   B 1 30  ? 25.444 -5.798  19.067 0.50 15.81 ? 36  SER   C OG  1 
ATOM   1345 N  N   . SER   B 1 31  ? 27.242 -8.282  19.974 1.00 13.37 ? 37  SER   C N   1 
ATOM   1346 C  CA  . SER   B 1 31  ? 28.652 -8.667  20.080 1.00 14.59 ? 37  SER   C CA  1 
ATOM   1347 C  C   . SER   B 1 31  ? 28.837 -10.172 20.036 1.00 14.10 ? 37  SER   C C   1 
ATOM   1348 O  O   . SER   B 1 31  ? 29.927 -10.626 19.681 1.00 14.63 ? 37  SER   C O   1 
ATOM   1349 C  CB  . SER   B 1 31  ? 29.278 -8.096  21.338 1.00 17.32 ? 37  SER   C CB  1 
ATOM   1350 O  OG  . SER   B 1 31  ? 28.937 -8.822  22.499 1.00 23.11 ? 37  SER   C OG  1 
ATOM   1351 N  N   . ARG   B 1 32  ? 27.806 -10.966 20.344 1.00 12.22 ? 38  ARG   C N   1 
ATOM   1352 C  CA  . ARG   B 1 32  ? 27.911 -12.436 20.258 1.00 11.89 ? 38  ARG   C CA  1 
ATOM   1353 C  C   . ARG   B 1 32  ? 27.247 -13.013 19.006 1.00 11.80 ? 38  ARG   C C   1 
ATOM   1354 O  O   . ARG   B 1 32  ? 27.250 -14.227 18.820 1.00 11.40 ? 38  ARG   C O   1 
ATOM   1355 C  CB  . ARG   B 1 32  ? 27.176 -13.044 21.490 1.00 13.65 ? 38  ARG   C CB  1 
ATOM   1356 C  CG  . ARG   B 1 32  ? 27.841 -12.694 22.819 1.00 14.76 ? 38  ARG   C CG  1 
ATOM   1357 C  CD  . ARG   B 1 32  ? 27.074 -13.262 24.026 1.00 13.16 ? 38  ARG   C CD  1 
ATOM   1358 N  NE  . ARG   B 1 32  ? 27.123 -14.735 24.081 1.00 11.80 ? 38  ARG   C NE  1 
ATOM   1359 C  CZ  . ARG   B 1 32  ? 27.081 -15.453 25.206 1.00 12.78 ? 38  ARG   C CZ  1 
ATOM   1360 N  NH1 . ARG   B 1 32  ? 26.952 -14.853 26.383 1.00 12.94 ? 38  ARG   C NH1 1 
ATOM   1361 N  NH2 . ARG   B 1 32  ? 27.207 -16.783 25.162 1.00 12.41 ? 38  ARG   C NH2 1 
ATOM   1362 N  N   . ASP   B 1 33  ? 26.531 -12.172 18.212 1.00 10.68 ? 39  ASP   C N   1 
ATOM   1363 C  CA  . ASP   B 1 33  ? 25.742 -12.646 17.074 1.00 10.72 ? 39  ASP   C CA  1 
ATOM   1364 C  C   . ASP   B 1 33  ? 24.659 -13.599 17.509 1.00 10.82 ? 39  ASP   C C   1 
ATOM   1365 O  O   . ASP   B 1 33  ? 24.335 -14.513 16.765 1.00 10.96 ? 39  ASP   C O   1 
ATOM   1366 C  CB  . ASP   B 1 33  ? 26.593 -13.238 15.952 1.00 11.34 ? 39  ASP   C CB  1 
ATOM   1367 C  CG  . ASP   B 1 33  ? 25.804 -13.588 14.692 1.00 11.55 ? 39  ASP   C CG  1 
ATOM   1368 O  OD1 . ASP   B 1 33  ? 24.922 -12.760 14.285 1.00 12.03 ? 39  ASP   C OD1 1 
ATOM   1369 O  OD2 . ASP   B 1 33  ? 26.145 -14.605 14.047 1.00 12.09 ? 39  ASP   C OD2 1 
ATOM   1370 N  N   . LEU   B 1 34  ? 24.009 -13.341 18.675 1.00 10.09 ? 40  LEU   C N   1 
ATOM   1371 C  CA  . LEU   B 1 34  ? 22.938 -14.230 19.115 1.00 11.13 ? 40  LEU   C CA  1 
ATOM   1372 C  C   . LEU   B 1 34  ? 21.647 -13.498 19.381 1.00 11.43 ? 40  LEU   C C   1 
ATOM   1373 O  O   . LEU   B 1 34  ? 21.659 -12.336 19.831 1.00 12.37 ? 40  LEU   C O   1 
ATOM   1374 C  CB  . LEU   B 1 34  ? 23.310 -14.954 20.436 1.00 11.39 ? 40  LEU   C CB  1 
ATOM   1375 C  CG  . LEU   B 1 34  ? 24.382 -16.052 20.348 1.00 11.84 ? 40  LEU   C CG  1 
ATOM   1376 C  CD1 . LEU   B 1 34  ? 24.616 -16.632 21.767 1.00 12.60 ? 40  LEU   C CD1 1 
ATOM   1377 C  CD2 . LEU   B 1 34  ? 23.930 -17.141 19.406 1.00 12.53 ? 40  LEU   C CD2 1 
ATOM   1378 N  N   . LEU   B 1 35  ? 20.534 -14.187 19.146 1.00 10.68 ? 41  LEU   C N   1 
ATOM   1379 C  CA  . LEU   B 1 35  ? 19.214 -13.663 19.517 1.00 11.20 ? 41  LEU   C CA  1 
ATOM   1380 C  C   . LEU   B 1 35  ? 18.362 -14.853 19.960 1.00 12.00 ? 41  LEU   C C   1 
ATOM   1381 O  O   . LEU   B 1 35  ? 18.437 -15.921 19.369 1.00 12.33 ? 41  LEU   C O   1 
ATOM   1382 C  CB  . LEU   B 1 35  ? 18.562 -12.929 18.309 1.00 12.16 ? 41  LEU   C CB  1 
ATOM   1383 C  CG  . LEU   B 1 35  ? 17.150 -12.319 18.552 1.00 13.20 ? 41  LEU   C CG  1 
ATOM   1384 C  CD1 . LEU   B 1 35  ? 16.957 -10.993 17.795 1.00 14.98 ? 41  LEU   C CD1 1 
ATOM   1385 C  CD2 . LEU   B 1 35  ? 16.048 -13.336 18.230 1.00 12.53 ? 41  LEU   C CD2 1 
ATOM   1386 N  N   . VAL   B 1 36  ? 17.572 -14.659 21.020 1.00 12.21 ? 42  VAL   C N   1 
ATOM   1387 C  CA  . VAL   B 1 36  ? 16.675 -15.685 21.506 1.00 12.06 ? 42  VAL   C CA  1 
ATOM   1388 C  C   . VAL   B 1 36  ? 15.254 -15.131 21.502 1.00 12.38 ? 42  VAL   C C   1 
ATOM   1389 O  O   . VAL   B 1 36  ? 15.029 -14.013 22.002 1.00 13.64 ? 42  VAL   C O   1 
ATOM   1390 C  CB  . VAL   B 1 36  ? 17.072 -16.113 22.931 1.00 12.87 ? 42  VAL   C CB  1 
ATOM   1391 C  CG1 . VAL   B 1 36  ? 16.084 -17.132 23.510 1.00 13.91 ? 42  VAL   C CG1 1 
ATOM   1392 C  CG2 . VAL   B 1 36  ? 18.485 -16.703 22.974 1.00 12.88 ? 42  VAL   C CG2 1 
ATOM   1393 N  N   . SER   B 1 37  ? 14.311 -15.893 20.941 1.00 12.73 ? 43  SER   C N   1 
ATOM   1394 C  CA  . SER   B 1 37  ? 12.906 -15.540 20.912 1.00 13.10 ? 43  SER   C CA  1 
ATOM   1395 C  C   . SER   B 1 37  ? 12.091 -16.618 21.617 1.00 14.39 ? 43  SER   C C   1 
ATOM   1396 O  O   . SER   B 1 37  ? 12.576 -17.748 21.851 1.00 14.35 ? 43  SER   C O   1 
ATOM   1397 C  CB  . SER   B 1 37  ? 12.430 -15.346 19.467 1.00 14.52 ? 43  SER   C CB  1 
ATOM   1398 O  OG  . SER   B 1 37  ? 12.614 -16.521 18.673 1.00 15.13 ? 43  SER   C OG  1 
ATOM   1399 N  N   . SER   B 1 38  ? 10.824 -16.290 21.956 1.00 15.34 ? 44  SER   C N   1 
ATOM   1400 C  CA  . SER   B 1 38  ? 9.971  -17.258 22.633 1.00 16.13 ? 44  SER   C CA  1 
ATOM   1401 C  C   . SER   B 1 38  ? 9.148  -18.067 21.607 1.00 17.54 ? 44  SER   C C   1 
ATOM   1402 O  O   . SER   B 1 38  ? 8.856  -17.577 20.514 1.00 18.68 ? 44  SER   C O   1 
ATOM   1403 C  CB  . SER   B 1 38  ? 9.070  -16.552 23.643 1.00 17.65 ? 44  SER   C CB  1 
ATOM   1404 O  OG  . SER   B 1 38  ? 8.208  -15.652 22.974 1.00 21.92 ? 44  SER   C OG  1 
ATOM   1405 N  N   . THR   B 1 39  ? 8.805  -19.308 21.943 1.00 17.09 ? 45  THR   C N   1 
ATOM   1406 C  CA  . THR   B 1 39  ? 8.045  -20.188 21.057 1.00 17.78 ? 45  THR   C CA  1 
ATOM   1407 C  C   . THR   B 1 39  ? 6.750  -20.657 21.752 1.00 20.38 ? 45  THR   C C   1 
ATOM   1408 O  O   . THR   B 1 39  ? 6.693  -20.724 22.978 1.00 20.19 ? 45  THR   C O   1 
ATOM   1409 C  CB  . THR   B 1 39  ? 8.878  -21.427 20.687 1.00 17.89 ? 45  THR   C CB  1 
ATOM   1410 O  OG1 . THR   B 1 39  ? 9.111  -22.200 21.868 1.00 19.27 ? 45  THR   C OG1 1 
ATOM   1411 C  CG2 . THR   B 1 39  ? 10.245 -21.063 20.078 1.00 17.73 ? 45  THR   C CG2 1 
ATOM   1412 N  N   . THR   B 1 40  ? 5.759  -21.055 20.959 1.00 22.94 ? 46  THR   C N   1 
ATOM   1413 C  CA  . THR   B 1 40  ? 4.523  -21.617 21.520 1.00 24.60 ? 46  THR   C CA  1 
ATOM   1414 C  C   . THR   B 1 40  ? 4.752  -23.094 21.845 1.00 24.89 ? 46  THR   C C   1 
ATOM   1415 O  O   . THR   B 1 40  ? 4.371  -23.552 22.924 1.00 27.22 ? 46  THR   C O   1 
ATOM   1416 C  CB  . THR   B 1 40  ? 3.356  -21.395 20.550 1.00 28.94 ? 46  THR   C CB  1 
ATOM   1417 O  OG1 . THR   B 1 40  ? 3.687  -22.013 19.312 1.00 33.15 ? 46  THR   C OG1 1 
ATOM   1418 C  CG2 . THR   B 1 40  ? 3.107  -19.929 20.287 1.00 28.26 ? 46  THR   C CG2 1 
ATOM   1419 N  N   . ALA   B 1 41  ? 5.394  -23.840 20.931 1.00 23.18 ? 47  ALA   C N   1 
ATOM   1420 C  CA  . ALA   B 1 41  ? 5.641  -25.265 21.173 1.00 22.87 ? 47  ALA   C CA  1 
ATOM   1421 C  C   . ALA   B 1 41  ? 6.979  -25.491 21.910 1.00 21.19 ? 47  ALA   C C   1 
ATOM   1422 O  O   . ALA   B 1 41  ? 7.907  -24.703 21.763 1.00 20.49 ? 47  ALA   C O   1 
ATOM   1423 C  CB  . ALA   B 1 41  ? 5.651  -26.027 19.846 1.00 24.61 ? 47  ALA   C CB  1 
ATOM   1424 N  N   . GLN   B 1 42  ? 7.095  -26.555 22.674 1.00 20.63 ? 48  GLN   C N   1 
ATOM   1425 C  CA  . GLN   B 1 42  ? 8.324  -26.904 23.371 1.00 22.07 ? 48  GLN   C CA  1 
ATOM   1426 C  C   . GLN   B 1 42  ? 9.333  -27.505 22.392 1.00 21.08 ? 48  GLN   C C   1 
ATOM   1427 O  O   . GLN   B 1 42  ? 8.954  -28.223 21.454 1.00 22.75 ? 48  GLN   C O   1 
ATOM   1428 C  CB  . GLN   B 1 42  ? 8.010  -27.871 24.519 1.00 27.61 ? 48  GLN   C CB  1 
ATOM   1429 C  CG  . GLN   B 1 42  ? 7.359  -27.138 25.692 1.00 36.57 ? 48  GLN   C CG  1 
ATOM   1430 C  CD  . GLN   B 1 42  ? 7.076  -28.085 26.823 1.00 47.34 ? 48  GLN   C CD  1 
ATOM   1431 O  OE1 . GLN   B 1 42  ? 6.174  -28.932 26.748 1.00 50.92 ? 48  GLN   C OE1 1 
ATOM   1432 N  NE2 . GLN   B 1 42  ? 7.831  -27.957 27.905 1.00 50.13 ? 48  GLN   C NE2 1 
ATOM   1433 N  N   . GLY   B 1 43  ? 10.601 -27.157 22.595 1.00 17.85 ? 49  GLY   C N   1 
ATOM   1434 C  CA  . GLY   B 1 43  ? 11.722 -27.663 21.800 1.00 17.32 ? 49  GLY   C CA  1 
ATOM   1435 C  C   . GLY   B 1 43  ? 12.332 -28.900 22.436 1.00 17.26 ? 49  GLY   C C   1 
ATOM   1436 O  O   . GLY   B 1 43  ? 12.127 -29.151 23.631 1.00 20.33 ? 49  GLY   C O   1 
ATOM   1437 N  N   . CYS   B 1 44  ? 13.157 -29.595 21.693 1.00 15.35 ? 50  CYS   C N   1 
ATOM   1438 C  CA  . CYS   B 1 44  ? 13.704 -30.862 22.179 1.00 16.43 ? 50  CYS   C CA  1 
ATOM   1439 C  C   . CYS   B 1 44  ? 15.198 -30.917 22.320 1.00 17.32 ? 50  CYS   C C   1 
ATOM   1440 O  O   . CYS   B 1 44  ? 15.728 -31.971 22.688 1.00 19.63 ? 50  CYS   C O   1 
ATOM   1441 C  CB  . CYS   B 1 44  ? 13.207 -31.978 21.265 1.00 17.02 ? 50  CYS   C CB  1 
ATOM   1442 S  SG  . CYS   B 1 44  ? 11.418 -31.975 21.062 1.00 23.03 ? 50  CYS   C SG  1 
ATOM   1443 N  N   . ASP   B 1 45  ? 15.904 -29.824 22.029 1.00 14.44 ? 51  ASP   C N   1 
ATOM   1444 C  CA  . ASP   B 1 45  ? 17.358 -29.828 22.143 1.00 13.84 ? 51  ASP   C CA  1 
ATOM   1445 C  C   . ASP   B 1 45  ? 17.754 -29.609 23.599 1.00 13.72 ? 51  ASP   C C   1 
ATOM   1446 O  O   . ASP   B 1 45  ? 17.045 -28.936 24.379 1.00 15.67 ? 51  ASP   C O   1 
ATOM   1447 C  CB  . ASP   B 1 45  ? 17.964 -28.700 21.284 1.00 14.29 ? 51  ASP   C CB  1 
ATOM   1448 C  CG  . ASP   B 1 45  ? 17.780 -28.858 19.782 1.00 19.06 ? 51  ASP   C CG  1 
ATOM   1449 O  OD1 . ASP   B 1 45  ? 17.792 -30.019 19.286 1.00 18.99 ? 51  ASP   C OD1 1 
ATOM   1450 O  OD2 . ASP   B 1 45  ? 17.612 -27.822 19.090 1.00 16.39 ? 51  ASP   C OD2 1 
ATOM   1451 N  N   . THR   B 1 46  ? 18.880 -30.208 23.969 1.00 13.04 ? 52  THR   C N   1 
ATOM   1452 C  CA  . THR   B 1 46  ? 19.454 -30.023 25.301 1.00 13.00 ? 52  THR   C CA  1 
ATOM   1453 C  C   . THR   B 1 46  ? 20.722 -29.172 25.125 1.00 13.81 ? 52  THR   C C   1 
ATOM   1454 O  O   . THR   B 1 46  ? 21.536 -29.492 24.243 1.00 13.62 ? 52  THR   C O   1 
ATOM   1455 C  CB  . THR   B 1 46  ? 19.865 -31.386 25.889 1.00 15.75 ? 52  THR   C CB  1 
ATOM   1456 O  OG1 . THR   B 1 46  ? 18.661 -32.155 26.108 1.00 17.66 ? 52  THR   C OG1 1 
ATOM   1457 C  CG2 . THR   B 1 46  ? 20.676 -31.233 27.208 1.00 16.60 ? 52  THR   C CG2 1 
ATOM   1458 N  N   . ILE   B 1 47  ? 20.918 -28.153 25.952 1.00 13.00 ? 53  ILE   C N   1 
ATOM   1459 C  CA  . ILE   B 1 47  ? 22.126 -27.349 25.887 1.00 12.90 ? 53  ILE   C CA  1 
ATOM   1460 C  C   . ILE   B 1 47  ? 23.215 -28.035 26.726 1.00 11.95 ? 53  ILE   C C   1 
ATOM   1461 O  O   . ILE   B 1 47  ? 22.960 -28.451 27.866 1.00 12.66 ? 53  ILE   C O   1 
ATOM   1462 C  CB  . ILE   B 1 47  ? 21.880 -25.931 26.458 1.00 13.65 ? 53  ILE   C CB  1 
ATOM   1463 C  CG1 . ILE   B 1 47  ? 20.679 -25.243 25.811 1.00 13.99 ? 53  ILE   C CG1 1 
ATOM   1464 C  CG2 . ILE   B 1 47  ? 23.133 -25.076 26.350 1.00 13.92 ? 53  ILE   C CG2 1 
ATOM   1465 C  CD1 . ILE   B 1 47  ? 20.846 -25.103 24.253 1.00 16.87 ? 53  ILE   C CD1 1 
ATOM   1466 N  N   . ALA   B 1 48  ? 24.433 -28.123 26.195 1.00 10.69 ? 54  ALA   C N   1 
ATOM   1467 C  CA  . ALA   B 1 48  ? 25.553 -28.667 26.931 1.00 11.21 ? 54  ALA   C CA  1 
ATOM   1468 C  C   . ALA   B 1 48  ? 25.922 -27.753 28.088 1.00 12.00 ? 54  ALA   C C   1 
ATOM   1469 O  O   . ALA   B 1 48  ? 25.873 -26.526 27.962 1.00 11.11 ? 54  ALA   C O   1 
ATOM   1470 C  CB  . ALA   B 1 48  ? 26.767 -28.777 26.010 1.00 12.28 ? 54  ALA   C CB  1 
ATOM   1471 N  N   . ARG   B 1 49  ? 26.256 -28.338 29.255 1.00 11.43 ? 55  ARG   C N   1 
ATOM   1472 C  CA  . ARG   B 1 49  ? 26.717 -27.589 30.438 1.00 11.50 ? 55  ARG   C CA  1 
ATOM   1473 C  C   . ARG   B 1 49  ? 28.048 -28.275 30.782 1.00 12.42 ? 55  ARG   C C   1 
ATOM   1474 O  O   . ARG   B 1 49  ? 28.070 -29.310 31.471 1.00 13.43 ? 55  ARG   C O   1 
ATOM   1475 C  CB  . ARG   B 1 49  ? 25.691 -27.597 31.584 1.00 11.88 ? 55  ARG   C CB  1 
ATOM   1476 C  CG  . ARG   B 1 49  ? 24.327 -27.055 31.148 1.00 11.68 ? 55  ARG   C CG  1 
ATOM   1477 C  CD  . ARG   B 1 49  ? 24.341 -25.579 30.788 1.00 12.11 ? 55  ARG   C CD  1 
ATOM   1478 N  NE  . ARG   B 1 49  ? 23.006 -25.145 30.369 1.00 12.97 ? 55  ARG   C NE  1 
ATOM   1479 C  CZ  . ARG   B 1 49  ? 22.770 -24.045 29.647 1.00 13.62 ? 55  ARG   C CZ  1 
ATOM   1480 N  NH1 . ARG   B 1 49  ? 23.769 -23.235 29.309 1.00 12.23 ? 55  ARG   C NH1 1 
ATOM   1481 N  NH2 . ARG   B 1 49  ? 21.523 -23.736 29.275 1.00 13.37 ? 55  ARG   C NH2 1 
ATOM   1482 N  N   . CYS   B 1 50  ? 29.157 -27.690 30.279 1.00 10.96 ? 56  CYS   C N   1 
ATOM   1483 C  CA  . CYS   B 1 50  ? 30.464 -28.346 30.335 1.00 11.22 ? 56  CYS   C CA  1 
ATOM   1484 C  C   . CYS   B 1 50  ? 31.566 -27.418 29.807 1.00 10.56 ? 56  CYS   C C   1 
ATOM   1485 O  O   . CYS   B 1 50  ? 31.283 -26.331 29.324 1.00 11.51 ? 56  CYS   C O   1 
ATOM   1486 C  CB  . CYS   B 1 50  ? 30.407 -29.573 29.405 1.00 11.70 ? 56  CYS   C CB  1 
ATOM   1487 S  SG  . CYS   B 1 50  ? 30.292 -29.140 27.607 1.00 10.87 ? 56  CYS   C SG  1 
ATOM   1488 N  N   . ASP   B 1 51  ? 32.813 -27.920 29.826 1.00 11.96 ? 57  ASP   C N   1 
ATOM   1489 C  CA  . ASP   B 1 51  ? 33.945 -27.222 29.202 1.00 12.25 ? 57  ASP   C CA  1 
ATOM   1490 C  C   . ASP   B 1 51  ? 34.618 -28.081 28.122 1.00 12.76 ? 57  ASP   C C   1 
ATOM   1491 O  O   . ASP   B 1 51  ? 35.817 -27.923 27.872 1.00 13.66 ? 57  ASP   C O   1 
ATOM   1492 C  CB  . ASP   B 1 51  ? 34.984 -26.788 30.260 1.00 14.81 ? 57  ASP   C CB  1 
ATOM   1493 C  CG  . ASP   B 1 51  ? 35.639 -27.927 31.000 1.00 17.13 ? 57  ASP   C CG  1 
ATOM   1494 O  OD1 . ASP   B 1 51  ? 35.292 -29.081 30.749 1.00 17.23 ? 57  ASP   C OD1 1 
ATOM   1495 O  OD2 . ASP   B 1 51  ? 36.538 -27.647 31.853 1.00 24.49 ? 57  ASP   C OD2 1 
ATOM   1496 N  N   . CYS   B 1 52  ? 33.836 -28.886 27.427 1.00 11.84 ? 58  CYS   C N   1 
ATOM   1497 C  CA  . CYS   B 1 52  ? 34.382 -29.671 26.297 1.00 11.38 ? 58  CYS   C CA  1 
ATOM   1498 C  C   . CYS   B 1 52  ? 35.070 -28.788 25.266 1.00 11.75 ? 58  CYS   C C   1 
ATOM   1499 O  O   . CYS   B 1 52  ? 34.641 -27.652 25.019 1.00 12.00 ? 58  CYS   C O   1 
ATOM   1500 C  CB  . CYS   B 1 52  ? 33.301 -30.473 25.581 1.00 12.69 ? 58  CYS   C CB  1 
ATOM   1501 S  SG  . CYS   B 1 52  ? 32.689 -31.903 26.508 1.00 12.65 ? 58  CYS   C SG  1 
ATOM   1502 N  N   . GLN   B 1 53  ? 36.113 -29.331 24.658 1.00 11.13 ? 59  GLN   C N   1 
ATOM   1503 C  CA  . GLN   B 1 53  ? 36.794 -28.739 23.507 1.00 11.69 ? 59  GLN   C CA  1 
ATOM   1504 C  C   . GLN   B 1 53  ? 36.854 -29.666 22.326 1.00 11.83 ? 59  GLN   C C   1 
ATOM   1505 O  O   . GLN   B 1 53  ? 37.594 -29.420 21.367 1.00 12.15 ? 59  GLN   C O   1 
ATOM   1506 C  CB  . GLN   B 1 53  ? 38.202 -28.262 23.854 1.00 12.42 ? 59  GLN   C CB  1 
ATOM   1507 C  CG  . GLN   B 1 53  ? 38.188 -27.018 24.725 1.00 15.33 ? 59  GLN   C CG  1 
ATOM   1508 C  CD  . GLN   B 1 53  ? 39.564 -26.495 24.952 1.00 17.70 ? 59  GLN   C CD  1 
ATOM   1509 O  OE1 . GLN   B 1 53  ? 40.084 -26.538 26.082 1.00 19.27 ? 59  GLN   C OE1 1 
ATOM   1510 N  NE2 . GLN   B 1 53  ? 40.181 -25.952 23.910 1.00 15.77 ? 59  GLN   C NE2 1 
ATOM   1511 N  N   . THR   B 1 54  ? 36.072 -30.753 22.336 1.00 12.04 ? 60  THR   C N   1 
ATOM   1512 C  CA  . THR   B 1 54  ? 35.924 -31.597 21.152 1.00 12.52 ? 60  THR   C CA  1 
ATOM   1513 C  C   . THR   B 1 54  ? 34.444 -31.845 20.940 1.00 12.69 ? 60  THR   C C   1 
ATOM   1514 O  O   . THR   B 1 54  ? 33.648 -31.939 21.889 1.00 12.47 ? 60  THR   C O   1 
ATOM   1515 C  CB  . THR   B 1 54  ? 36.709 -32.886 21.193 1.00 15.16 ? 60  THR   C CB  1 
ATOM   1516 O  OG1 . THR   B 1 54  ? 36.176 -33.668 22.213 1.00 17.45 ? 60  THR   C OG1 1 
ATOM   1517 C  CG2 . THR   B 1 54  ? 38.212 -32.668 21.430 1.00 14.64 ? 60  THR   C CG2 1 
ATOM   1518 N  N   . GLY   B 1 55  ? 34.061 -31.958 19.674 1.00 10.38 ? 61  GLY   C N   1 
ATOM   1519 C  CA  . GLY   B 1 55  ? 32.663 -32.187 19.327 1.00 10.72 ? 61  GLY   C CA  1 
ATOM   1520 C  C   . GLY   B 1 55  ? 32.516 -32.384 17.835 1.00 10.55 ? 61  GLY   C C   1 
ATOM   1521 O  O   . GLY   B 1 55  ? 33.499 -32.712 17.147 1.00 11.92 ? 61  GLY   C O   1 
ATOM   1522 N  N   . VAL   B 1 56  ? 31.252 -32.291 17.359 1.00 9.98  ? 62  VAL   C N   1 
ATOM   1523 C  CA  . VAL   B 1 56  ? 30.947 -32.492 15.928 1.00 10.45 ? 62  VAL   C CA  1 
ATOM   1524 C  C   . VAL   B 1 56  ? 30.052 -31.354 15.496 1.00 10.17 ? 62  VAL   C C   1 
ATOM   1525 O  O   . VAL   B 1 56  ? 29.119 -31.014 16.224 1.00 11.15 ? 62  VAL   C O   1 
ATOM   1526 C  CB  . VAL   B 1 56  ? 30.211 -33.848 15.784 1.00 11.08 ? 62  VAL   C CB  1 
ATOM   1527 C  CG1 . VAL   B 1 56  ? 29.710 -34.046 14.348 1.00 11.98 ? 62  VAL   C CG1 1 
ATOM   1528 C  CG2 . VAL   B 1 56  ? 31.134 -35.014 16.186 1.00 11.24 ? 62  VAL   C CG2 1 
ATOM   1529 N  N   . TYR   B 1 57  ? 30.312 -30.759 14.317 1.00 9.60  ? 63  TYR   C N   1 
ATOM   1530 C  CA  . TYR   B 1 57  ? 29.421 -29.685 13.829 1.00 9.38  ? 63  TYR   C CA  1 
ATOM   1531 C  C   . TYR   B 1 57  ? 28.870 -30.024 12.452 1.00 10.03 ? 63  TYR   C C   1 
ATOM   1532 O  O   . TYR   B 1 57  ? 29.517 -30.739 11.675 1.00 11.23 ? 63  TYR   C O   1 
ATOM   1533 C  CB  . TYR   B 1 57  ? 30.120 -28.276 13.764 1.00 10.16 ? 63  TYR   C CB  1 
ATOM   1534 C  CG  . TYR   B 1 57  ? 30.995 -27.966 12.548 1.00 10.50 ? 63  TYR   C CG  1 
ATOM   1535 C  CD1 . TYR   B 1 57  ? 32.282 -28.466 12.451 1.00 11.34 ? 63  TYR   C CD1 1 
ATOM   1536 C  CD2 . TYR   B 1 57  ? 30.532 -27.133 11.522 1.00 10.85 ? 63  TYR   C CD2 1 
ATOM   1537 C  CE1 . TYR   B 1 57  ? 33.093 -28.161 11.360 1.00 12.29 ? 63  TYR   C CE1 1 
ATOM   1538 C  CE2 . TYR   B 1 57  ? 31.342 -26.809 10.445 1.00 12.42 ? 63  TYR   C CE2 1 
ATOM   1539 C  CZ  . TYR   B 1 57  ? 32.620 -27.316 10.380 1.00 13.12 ? 63  TYR   C CZ  1 
ATOM   1540 O  OH  . TYR   B 1 57  ? 33.472 -27.000 9.319  1.00 14.66 ? 63  TYR   C OH  1 
ATOM   1541 N  N   . TYR   B 1 58  ? 27.710 -29.447 12.159 1.00 10.27 ? 64  TYR   C N   1 
ATOM   1542 C  CA  . TYR   B 1 58  ? 27.091 -29.637 10.838 1.00 10.21 ? 64  TYR   C CA  1 
ATOM   1543 C  C   . TYR   B 1 58  ? 27.481 -28.513 9.903  1.00 10.65 ? 64  TYR   C C   1 
ATOM   1544 O  O   . TYR   B 1 58  ? 27.219 -27.342 10.186 1.00 10.68 ? 64  TYR   C O   1 
ATOM   1545 C  CB  . TYR   B 1 58  ? 25.556 -29.756 10.927 1.00 10.82 ? 64  TYR   C CB  1 
ATOM   1546 C  CG  . TYR   B 1 58  ? 24.942 -30.055 9.563  1.00 12.36 ? 64  TYR   C CG  1 
ATOM   1547 C  CD1 . TYR   B 1 58  ? 25.272 -31.215 8.867  1.00 13.62 ? 64  TYR   C CD1 1 
ATOM   1548 C  CD2 . TYR   B 1 58  ? 24.115 -29.140 8.934  1.00 12.88 ? 64  TYR   C CD2 1 
ATOM   1549 C  CE1 . TYR   B 1 58  ? 24.795 -31.452 7.577  1.00 13.44 ? 64  TYR   C CE1 1 
ATOM   1550 C  CE2 . TYR   B 1 58  ? 23.581 -29.407 7.664  1.00 13.89 ? 64  TYR   C CE2 1 
ATOM   1551 C  CZ  . TYR   B 1 58  ? 23.914 -30.572 7.006  1.00 14.24 ? 64  TYR   C CZ  1 
ATOM   1552 O  OH  . TYR   B 1 58  ? 23.409 -30.828 5.731  1.00 16.81 ? 64  TYR   C OH  1 
ATOM   1553 N  N   . CYS   B 1 59  ? 28.025 -28.887 8.753  1.00 10.61 ? 65  CYS   C N   1 
ATOM   1554 C  CA  . CYS   B 1 59  ? 28.400 -27.965 7.682  1.00 11.53 ? 65  CYS   C CA  1 
ATOM   1555 C  C   . CYS   B 1 59  ? 27.454 -28.181 6.478  1.00 12.45 ? 65  CYS   C C   1 
ATOM   1556 O  O   . CYS   B 1 59  ? 27.643 -29.115 5.687  1.00 12.90 ? 65  CYS   C O   1 
ATOM   1557 C  CB  . CYS   B 1 59  ? 29.850 -28.212 7.315  1.00 10.29 ? 65  CYS   C CB  1 
ATOM   1558 S  SG  . CYS   B 1 59  ? 30.412 -27.179 5.923  1.00 13.95 ? 65  CYS   C SG  1 
ATOM   1559 N  N   . SER   B 1 60  ? 26.466 -27.264 6.317  1.00 12.59 ? 66  SER   C N   1 
ATOM   1560 C  CA  . SER   B 1 60  ? 25.477 -27.408 5.256  1.00 13.46 ? 66  SER   C CA  1 
ATOM   1561 C  C   . SER   B 1 60  ? 26.102 -27.375 3.858  1.00 13.30 ? 66  SER   C C   1 
ATOM   1562 O  O   . SER   B 1 60  ? 25.634 -28.101 2.989  1.00 15.03 ? 66  SER   C O   1 
ATOM   1563 C  CB  . SER   B 1 60  ? 24.391 -26.347 5.391  1.00 15.34 ? 66  SER   C CB  1 
ATOM   1564 O  OG  . SER   B 1 60  ? 23.422 -26.643 4.396  1.00 19.51 ? 66  SER   C OG  1 
ATOM   1565 N  N   . SER   B 1 61  ? 27.110 -26.519 3.634  1.00 12.97 ? 67  SER   C N   1 
ATOM   1566 C  CA  . SER   B 1 61  ? 27.741 -26.404 2.313  1.00 13.58 ? 67  SER   C CA  1 
ATOM   1567 C  C   . SER   B 1 61  ? 28.540 -27.630 1.876  1.00 15.18 ? 67  SER   C C   1 
ATOM   1568 O  O   . SER   B 1 61  ? 28.910 -27.741 0.706  1.00 16.12 ? 67  SER   C O   1 
ATOM   1569 C  CB  . SER   B 1 61  ? 28.595 -25.146 2.276  1.00 13.58 ? 67  SER   C CB  1 
ATOM   1570 O  OG  . SER   B 1 61  ? 29.710 -25.216 3.134  1.00 14.74 ? 67  SER   C OG  1 
ATOM   1571 N  N   . ARG   B 1 62  ? 28.736 -28.597 2.790  1.00 14.08 ? 68  ARG   C N   1 
ATOM   1572 C  CA  . ARG   B 1 62  ? 29.358 -29.879 2.449  1.00 14.23 ? 68  ARG   C CA  1 
ATOM   1573 C  C   . ARG   B 1 62  ? 28.438 -31.058 2.714  1.00 13.95 ? 68  ARG   C C   1 
ATOM   1574 O  O   . ARG   B 1 62  ? 28.844 -32.212 2.496  1.00 14.72 ? 68  ARG   C O   1 
ATOM   1575 C  CB  . ARG   B 1 62  ? 30.649 -30.053 3.278  1.00 15.35 ? 68  ARG   C CB  1 
ATOM   1576 C  CG  . ARG   B 1 62  ? 31.678 -28.960 2.998  1.00 20.00 ? 68  ARG   C CG  1 
ATOM   1577 C  CD  . ARG   B 1 62  ? 32.388 -29.262 1.721  1.00 19.62 ? 68  ARG   C CD  1 
ATOM   1578 N  NE  . ARG   B 1 62  ? 33.395 -28.230 1.399  1.00 24.80 ? 68  ARG   C NE  1 
ATOM   1579 C  CZ  . ARG   B 1 62  ? 33.153 -27.133 0.688  1.00 30.46 ? 68  ARG   C CZ  1 
ATOM   1580 N  NH1 . ARG   B 1 62  ? 31.929 -26.887 0.226  1.00 30.19 ? 68  ARG   C NH1 1 
ATOM   1581 N  NH2 . ARG   B 1 62  ? 34.142 -26.280 0.408  1.00 31.46 ? 68  ARG   C NH2 1 
ATOM   1582 N  N   . ARG   B 1 63  ? 27.213 -30.810 3.239  1.00 14.51 ? 69  ARG   C N   1 
ATOM   1583 C  CA  . ARG   B 1 63  ? 26.268 -31.869 3.681  1.00 14.80 ? 69  ARG   C CA  1 
ATOM   1584 C  C   . ARG   B 1 63  ? 26.983 -32.875 4.590  1.00 16.33 ? 69  ARG   C C   1 
ATOM   1585 O  O   . ARG   B 1 63  ? 26.852 -34.098 4.407  1.00 17.64 ? 69  ARG   C O   1 
ATOM   1586 C  CB  . ARG   B 1 63  ? 25.618 -32.582 2.480  1.00 15.44 ? 69  ARG   C CB  1 
ATOM   1587 C  CG  . ARG   B 1 63  ? 24.783 -31.669 1.625  1.00 18.04 ? 69  ARG   C CG  1 
ATOM   1588 C  CD  . ARG   B 1 63  ? 23.586 -31.148 2.336  1.00 23.20 ? 69  ARG   C CD  1 
ATOM   1589 N  NE  . ARG   B 1 63  ? 22.579 -30.744 1.358  1.00 25.62 ? 69  ARG   C NE  1 
ATOM   1590 C  CZ  . ARG   B 1 63  ? 22.363 -29.489 0.993  1.00 26.34 ? 69  ARG   C CZ  1 
ATOM   1591 N  NH1 . ARG   B 1 63  ? 23.118 -28.505 1.480  1.00 23.72 ? 69  ARG   C NH1 1 
ATOM   1592 N  NH2 . ARG   B 1 63  ? 21.404 -29.204 0.131  1.00 26.78 ? 69  ARG   C NH2 1 
ATOM   1593 N  N   . LYS   B 1 64  ? 27.804 -32.363 5.516  1.00 14.83 ? 70  LYS   C N   1 
ATOM   1594 C  CA  . LYS   B 1 64  ? 28.642 -33.256 6.302  1.00 15.57 ? 70  LYS   C CA  1 
ATOM   1595 C  C   . LYS   B 1 64  ? 28.736 -32.796 7.742  1.00 14.58 ? 70  LYS   C C   1 
ATOM   1596 O  O   . LYS   B 1 64  ? 28.769 -31.588 8.026  1.00 13.87 ? 70  LYS   C O   1 
ATOM   1597 C  CB  . LYS   B 1 64  ? 30.067 -33.237 5.708  1.00 18.83 ? 70  LYS   C CB  1 
ATOM   1598 C  CG  . LYS   B 1 64  ? 30.408 -34.439 4.839  1.00 29.06 ? 70  LYS   C CG  1 
ATOM   1599 C  CD  . LYS   B 1 64  ? 31.927 -34.630 4.828  1.00 36.30 ? 70  LYS   C CD  1 
ATOM   1600 C  CE  . LYS   B 1 64  ? 32.347 -35.549 3.726  1.00 43.49 ? 70  LYS   C CE  1 
ATOM   1601 N  NZ  . LYS   B 1 64  ? 31.850 -35.076 2.407  1.00 48.56 ? 70  LYS   C NZ  1 
ATOM   1602 N  N   . HIS   B 1 65  ? 28.810 -33.756 8.665  1.00 13.16 ? 71  HIS   C N   1 
ATOM   1603 C  CA  . HIS   B 1 65  ? 29.094 -33.468 10.076 1.00 12.61 ? 71  HIS   C CA  1 
ATOM   1604 C  C   . HIS   B 1 65  ? 30.569 -33.744 10.272 1.00 14.23 ? 71  HIS   C C   1 
ATOM   1605 O  O   . HIS   B 1 65  ? 31.062 -34.832 9.932  1.00 17.50 ? 71  HIS   C O   1 
ATOM   1606 C  CB  . HIS   B 1 65  ? 28.259 -34.380 10.983 1.00 12.32 ? 71  HIS   C CB  1 
ATOM   1607 C  CG  . HIS   B 1 65  ? 26.800 -34.111 10.925 1.00 13.17 ? 71  HIS   C CG  1 
ATOM   1608 N  ND1 . HIS   B 1 65  ? 26.145 -33.336 11.891 1.00 15.60 ? 71  HIS   C ND1 1 
ATOM   1609 C  CD2 . HIS   B 1 65  ? 25.895 -34.541 10.021 1.00 13.12 ? 71  HIS   C CD2 1 
ATOM   1610 C  CE1 . HIS   B 1 65  ? 24.856 -33.358 11.562 1.00 13.81 ? 71  HIS   C CE1 1 
ATOM   1611 N  NE2 . HIS   B 1 65  ? 24.649 -34.074 10.456 1.00 15.91 ? 71  HIS   C NE2 1 
ATOM   1612 N  N   . TYR   B 1 66  ? 31.315 -32.756 10.791 1.00 12.42 ? 72  TYR   C N   1 
ATOM   1613 C  CA  . TYR   B 1 66  ? 32.757 -32.941 10.953 1.00 12.23 ? 72  TYR   C CA  1 
ATOM   1614 C  C   . TYR   B 1 66  ? 33.139 -33.007 12.419 1.00 11.96 ? 72  TYR   C C   1 
ATOM   1615 O  O   . TYR   B 1 66  ? 32.735 -32.122 13.194 1.00 12.03 ? 72  TYR   C O   1 
ATOM   1616 C  CB  . TYR   B 1 66  ? 33.490 -31.688 10.375 1.00 13.58 ? 72  TYR   C CB  1 
ATOM   1617 C  CG  . TYR   B 1 66  ? 33.489 -31.591 8.860  1.00 13.51 ? 72  TYR   C CG  1 
ATOM   1618 C  CD1 . TYR   B 1 66  ? 34.338 -32.370 8.094  1.00 16.11 ? 72  TYR   C CD1 1 
ATOM   1619 C  CD2 . TYR   B 1 66  ? 32.680 -30.676 8.204  1.00 13.77 ? 72  TYR   C CD2 1 
ATOM   1620 C  CE1 . TYR   B 1 66  ? 34.362 -32.264 6.709  1.00 16.89 ? 72  TYR   C CE1 1 
ATOM   1621 C  CE2 . TYR   B 1 66  ? 32.693 -30.558 6.822  1.00 15.27 ? 72  TYR   C CE2 1 
ATOM   1622 C  CZ  . TYR   B 1 66  ? 33.544 -31.353 6.076  1.00 16.42 ? 72  TYR   C CZ  1 
ATOM   1623 O  OH  . TYR   B 1 66  ? 33.556 -31.199 4.697  1.00 16.99 ? 72  TYR   C OH  1 
ATOM   1624 N  N   . PRO   B 1 67  ? 33.941 -33.993 12.825 1.00 12.19 ? 73  PRO   C N   1 
ATOM   1625 C  CA  . PRO   B 1 67  ? 34.470 -33.962 14.205 1.00 11.73 ? 73  PRO   C CA  1 
ATOM   1626 C  C   . PRO   B 1 67  ? 35.574 -32.904 14.303 1.00 12.87 ? 73  PRO   C C   1 
ATOM   1627 O  O   . PRO   B 1 67  ? 36.454 -32.859 13.420 1.00 14.09 ? 73  PRO   C O   1 
ATOM   1628 C  CB  . PRO   B 1 67  ? 35.044 -35.370 14.410 1.00 13.62 ? 73  PRO   C CB  1 
ATOM   1629 C  CG  . PRO   B 1 67  ? 35.214 -35.940 13.048 1.00 16.16 ? 73  PRO   C CG  1 
ATOM   1630 C  CD  . PRO   B 1 67  ? 34.444 -35.154 12.035 1.00 13.10 ? 73  PRO   C CD  1 
ATOM   1631 N  N   . VAL   B 1 68  ? 35.551 -32.080 15.340 1.00 11.15 ? 74  VAL   C N   1 
ATOM   1632 C  CA  . VAL   B 1 68  ? 36.549 -31.012 15.483 1.00 10.95 ? 74  VAL   C CA  1 
ATOM   1633 C  C   . VAL   B 1 68  ? 36.956 -30.799 16.904 1.00 10.67 ? 74  VAL   C C   1 
ATOM   1634 O  O   . VAL   B 1 68  ? 36.221 -31.089 17.855 1.00 11.18 ? 74  VAL   C O   1 
ATOM   1635 C  CB  . VAL   B 1 68  ? 35.959 -29.630 14.983 1.00 12.36 ? 74  VAL   C CB  1 
ATOM   1636 C  CG1 . VAL   B 1 68  ? 35.913 -29.536 13.435 1.00 13.63 ? 74  VAL   C CG1 1 
ATOM   1637 C  CG2 . VAL   B 1 68  ? 34.588 -29.307 15.639 1.00 13.95 ? 74  VAL   C CG2 1 
ATOM   1638 N  N   . SER   B 1 69  ? 38.193 -30.290 17.063 1.00 11.22 ? 75  SER   C N   1 
ATOM   1639 C  CA  . SER   B 1 69  ? 38.650 -29.648 18.297 1.00 11.16 ? 75  SER   C CA  1 
ATOM   1640 C  C   . SER   B 1 69  ? 38.339 -28.147 18.176 1.00 10.59 ? 75  SER   C C   1 
ATOM   1641 O  O   . SER   B 1 69  ? 38.466 -27.561 17.081 1.00 11.53 ? 75  SER   C O   1 
ATOM   1642 C  CB  . SER   B 1 69  ? 40.158 -29.813 18.474 1.00 12.75 ? 75  SER   C CB  1 
ATOM   1643 O  OG  . SER   B 1 69  ? 40.424 -31.194 18.653 1.00 18.05 ? 75  SER   C OG  1 
ATOM   1644 N  N   . PHE   B 1 70  ? 37.908 -27.503 19.268 1.00 9.96  ? 76  PHE   C N   1 
ATOM   1645 C  CA  . PHE   B 1 70  ? 37.534 -26.086 19.200 1.00 9.84  ? 76  PHE   C CA  1 
ATOM   1646 C  C   . PHE   B 1 70  ? 38.081 -25.358 20.452 1.00 10.68 ? 76  PHE   C C   1 
ATOM   1647 O  O   . PHE   B 1 70  ? 38.236 -25.956 21.533 1.00 11.00 ? 76  PHE   C O   1 
ATOM   1648 C  CB  . PHE   B 1 70  ? 35.998 -25.874 18.993 1.00 10.24 ? 76  PHE   C CB  1 
ATOM   1649 C  CG  . PHE   B 1 70  ? 35.134 -26.566 20.004 1.00 9.91  ? 76  PHE   C CG  1 
ATOM   1650 C  CD1 . PHE   B 1 70  ? 34.706 -27.875 19.804 1.00 10.32 ? 76  PHE   C CD1 1 
ATOM   1651 C  CD2 . PHE   B 1 70  ? 34.676 -25.878 21.108 1.00 10.99 ? 76  PHE   C CD2 1 
ATOM   1652 C  CE1 . PHE   B 1 70  ? 33.892 -28.497 20.725 1.00 10.22 ? 76  PHE   C CE1 1 
ATOM   1653 C  CE2 . PHE   B 1 70  ? 33.845 -26.506 22.030 1.00 11.58 ? 76  PHE   C CE2 1 
ATOM   1654 C  CZ  . PHE   B 1 70  ? 33.464 -27.812 21.838 1.00 11.37 ? 76  PHE   C CZ  1 
ATOM   1655 N  N   . SER   B 1 71  ? 38.296 -24.045 20.327 1.00 10.29 ? 77  SER   C N   1 
ATOM   1656 C  CA  . SER   B 1 71  ? 38.932 -23.261 21.382 1.00 11.12 ? 77  SER   C CA  1 
ATOM   1657 C  C   . SER   B 1 71  ? 37.952 -22.862 22.486 1.00 12.56 ? 77  SER   C C   1 
ATOM   1658 O  O   . SER   B 1 71  ? 36.768 -23.190 22.436 1.00 13.05 ? 77  SER   C O   1 
ATOM   1659 C  CB  . SER   B 1 71  ? 39.662 -22.077 20.755 1.00 10.92 ? 77  SER   C CB  1 
ATOM   1660 O  OG  . SER   B 1 71  ? 38.748 -21.186 20.128 1.00 13.38 ? 77  SER   C OG  1 
ATOM   1661 N  N   . LYS   B 1 72  ? 38.449 -22.185 23.507 1.00 12.24 ? 78  LYS   C N   1 
ATOM   1662 C  CA  . LYS   B 1 72  ? 37.598 -21.771 24.644 1.00 12.17 ? 78  LYS   C CA  1 
ATOM   1663 C  C   . LYS   B 1 72  ? 36.883 -20.477 24.246 1.00 13.03 ? 78  LYS   C C   1 
ATOM   1664 O  O   . LYS   B 1 72  ? 37.448 -19.667 23.494 1.00 12.90 ? 78  LYS   C O   1 
ATOM   1665 C  CB  . LYS   B 1 72  ? 38.490 -21.484 25.865 1.00 15.91 ? 78  LYS   C CB  1 
ATOM   1666 C  CG  . LYS   B 1 72  ? 39.233 -22.723 26.371 1.00 20.35 ? 78  LYS   C CG  1 
ATOM   1667 C  CD  . LYS   B 1 72  ? 40.259 -22.313 27.447 1.00 29.17 ? 78  LYS   C CD  1 
ATOM   1668 C  CE  . LYS   B 1 72  ? 41.020 -23.512 27.971 1.00 37.23 ? 78  LYS   C CE  1 
ATOM   1669 N  NZ  . LYS   B 1 72  ? 42.234 -23.091 28.722 1.00 41.05 ? 78  LYS   C NZ  1 
ATOM   1670 N  N   . PRO   B 1 73  ? 35.651 -20.224 24.709 1.00 12.34 ? 79  PRO   C N   1 
ATOM   1671 C  CA  . PRO   B 1 73  ? 34.911 -18.992 24.302 1.00 12.60 ? 79  PRO   C CA  1 
ATOM   1672 C  C   . PRO   B 1 73  ? 35.677 -17.736 24.669 1.00 12.81 ? 79  PRO   C C   1 
ATOM   1673 O  O   . PRO   B 1 73  ? 36.102 -17.592 25.842 1.00 14.62 ? 79  PRO   C O   1 
ATOM   1674 C  CB  . PRO   B 1 73  ? 33.599 -19.067 25.081 1.00 15.27 ? 79  PRO   C CB  1 
ATOM   1675 C  CG  . PRO   B 1 73  ? 33.495 -20.466 25.540 1.00 16.64 ? 79  PRO   C CG  1 
ATOM   1676 C  CD  . PRO   B 1 73  ? 34.870 -21.080 25.619 1.00 13.44 ? 79  PRO   C CD  1 
ATOM   1677 N  N   . SER   B 1 74  ? 35.912 -16.853 23.681 1.00 11.46 ? 80  SER   C N   1 
ATOM   1678 C  CA  . SER   B 1 74  ? 36.792 -15.715 23.893 1.00 13.15 ? 80  SER   C CA  1 
ATOM   1679 C  C   . SER   B 1 74  ? 36.392 -14.551 22.991 1.00 12.73 ? 80  SER   C C   1 
ATOM   1680 O  O   . SER   B 1 74  ? 35.527 -14.697 22.151 1.00 12.24 ? 80  SER   C O   1 
ATOM   1681 C  CB  . SER   B 1 74  ? 38.226 -16.102 23.515 1.00 17.67 ? 80  SER   C CB  1 
ATOM   1682 O  OG  . SER   B 1 74  ? 38.663 -17.266 24.201 1.00 23.51 ? 80  SER   C OG  1 
ATOM   1683 N  N   . LEU   B 1 75  ? 37.072 -13.402 23.166 1.00 13.36 ? 81  LEU   C N   1 
ATOM   1684 C  CA  . LEU   B 1 75  ? 36.920 -12.201 22.357 1.00 15.00 ? 81  LEU   C CA  1 
ATOM   1685 C  C   . LEU   B 1 75  ? 37.906 -12.344 21.187 1.00 15.59 ? 81  LEU   C C   1 
ATOM   1686 O  O   . LEU   B 1 75  ? 39.135 -12.348 21.410 1.00 16.19 ? 81  LEU   C O   1 
ATOM   1687 C  CB  . LEU   B 1 75  ? 37.242 -10.970 23.220 1.00 16.59 ? 81  LEU   C CB  1 
ATOM   1688 C  CG  . LEU   B 1 75  ? 36.888 -9.586  22.611 1.00 19.04 ? 81  LEU   C CG  1 
ATOM   1689 C  CD1 . LEU   B 1 75  ? 35.404 -9.425  22.413 1.00 17.80 ? 81  LEU   C CD1 1 
ATOM   1690 C  CD2 . LEU   B 1 75  ? 37.414 -8.462  23.537 1.00 21.48 ? 81  LEU   C CD2 1 
ATOM   1691 N  N   . ILE   B 1 76  ? 37.403 -12.560 19.974 1.00 15.58 ? 82  ILE   C N   1 
ATOM   1692 C  CA  . ILE   B 1 76  ? 38.202 -12.845 18.792 1.00 16.28 ? 82  ILE   C CA  1 
ATOM   1693 C  C   . ILE   B 1 76  ? 37.947 -11.806 17.705 1.00 16.44 ? 82  ILE   C C   1 
ATOM   1694 O  O   . ILE   B 1 76  ? 36.779 -11.473 17.438 1.00 15.62 ? 82  ILE   C O   1 
ATOM   1695 C  CB  . ILE   B 1 76  ? 37.807 -14.254 18.273 1.00 18.20 ? 82  ILE   C CB  1 
ATOM   1696 C  CG1 . ILE   B 1 76  ? 38.065 -15.378 19.323 1.00 19.79 ? 82  ILE   C CG1 1 
ATOM   1697 C  CG2 . ILE   B 1 76  ? 38.463 -14.558 16.924 1.00 19.91 ? 82  ILE   C CG2 1 
ATOM   1698 C  CD1 . ILE   B 1 76  ? 39.492 -15.946 19.386 1.00 21.65 ? 82  ILE   C CD1 1 
ATOM   1699 N  N   . PHE   B 1 77  ? 39.024 -11.345 17.045 1.00 16.72 ? 83  PHE   C N   1 
ATOM   1700 C  CA  . PHE   B 1 77  ? 38.864 -10.401 15.945 1.00 17.77 ? 83  PHE   C CA  1 
ATOM   1701 C  C   . PHE   B 1 77  ? 38.446 -11.199 14.709 1.00 18.00 ? 83  PHE   C C   1 
ATOM   1702 O  O   . PHE   B 1 77  ? 39.064 -12.223 14.349 1.00 20.07 ? 83  PHE   C O   1 
ATOM   1703 C  CB  . PHE   B 1 77  ? 40.167 -9.622  15.679 1.00 18.68 ? 83  PHE   C CB  1 
ATOM   1704 C  CG  . PHE   B 1 77  ? 39.907 -8.433  14.771 1.00 19.46 ? 83  PHE   C CG  1 
ATOM   1705 C  CD1 . PHE   B 1 77  ? 39.248 -7.310  15.243 1.00 20.05 ? 83  PHE   C CD1 1 
ATOM   1706 C  CD2 . PHE   B 1 77  ? 40.280 -8.464  13.436 1.00 20.78 ? 83  PHE   C CD2 1 
ATOM   1707 C  CE1 . PHE   B 1 77  ? 38.981 -6.235  14.396 1.00 21.57 ? 83  PHE   C CE1 1 
ATOM   1708 C  CE2 . PHE   B 1 77  ? 40.019 -7.387  12.603 1.00 21.11 ? 83  PHE   C CE2 1 
ATOM   1709 C  CZ  . PHE   B 1 77  ? 39.392 -6.279  13.088 1.00 21.67 ? 83  PHE   C CZ  1 
ATOM   1710 N  N   . VAL   B 1 78  ? 37.344 -10.763 14.082 1.00 16.09 ? 84  VAL   C N   1 
ATOM   1711 C  CA  . VAL   B 1 78  ? 36.783 -11.450 12.926 1.00 16.49 ? 84  VAL   C CA  1 
ATOM   1712 C  C   . VAL   B 1 78  ? 36.877 -10.498 11.729 1.00 16.03 ? 84  VAL   C C   1 
ATOM   1713 O  O   . VAL   B 1 78  ? 36.430 -9.366  11.849 1.00 15.77 ? 84  VAL   C O   1 
ATOM   1714 C  CB  . VAL   B 1 78  ? 35.296 -11.815 13.235 1.00 17.20 ? 84  VAL   C CB  1 
ATOM   1715 C  CG1 . VAL   B 1 78  ? 34.658 -12.569 12.081 1.00 18.80 ? 84  VAL   C CG1 1 
ATOM   1716 C  CG2 . VAL   B 1 78  ? 35.191 -12.647 14.517 1.00 17.86 ? 84  VAL   C CG2 1 
ATOM   1717 N  N   . GLU   B 1 79  ? 37.322 -10.972 10.548 1.00 15.11 ? 85  GLU   C N   1 
ATOM   1718 C  CA  . GLU   B 1 79  ? 37.326 -10.134 9.345  1.00 15.71 ? 85  GLU   C CA  1 
ATOM   1719 C  C   . GLU   B 1 79  ? 35.922 -9.856  8.872  1.00 15.52 ? 85  GLU   C C   1 
ATOM   1720 O  O   . GLU   B 1 79  ? 34.951 -10.517 9.264  1.00 14.85 ? 85  GLU   C O   1 
ATOM   1721 C  CB  . GLU   B 1 79  ? 38.175 -10.781 8.215  1.00 18.27 ? 85  GLU   C CB  1 
ATOM   1722 C  CG  . GLU   B 1 79  ? 39.661 -10.797 8.545  1.00 24.77 ? 85  GLU   C CG  1 
ATOM   1723 C  CD  . GLU   B 1 79  ? 40.269 -9.446  8.885  1.00 31.94 ? 85  GLU   C CD  1 
ATOM   1724 O  OE1 . GLU   B 1 79  ? 39.918 -8.431  8.236  1.00 34.42 ? 85  GLU   C OE1 1 
ATOM   1725 O  OE2 . GLU   B 1 79  ? 41.080 -9.396  9.834  1.00 31.61 ? 85  GLU   C OE2 1 
ATOM   1726 N  N   . ALA   B 1 80  ? 35.776 -8.830  8.052  1.00 16.44 ? 86  ALA   C N   1 
ATOM   1727 C  CA  . ALA   B 1 80  ? 34.501 -8.437  7.530  1.00 18.15 ? 86  ALA   C CA  1 
ATOM   1728 C  C   . ALA   B 1 80  ? 33.832 -9.568  6.775  1.00 20.19 ? 86  ALA   C C   1 
ATOM   1729 O  O   . ALA   B 1 80  ? 34.508 -10.357 6.114  1.00 21.39 ? 86  ALA   C O   1 
ATOM   1730 C  CB  . ALA   B 1 80  ? 34.688 -7.242  6.594  1.00 18.93 ? 86  ALA   C CB  1 
ATOM   1731 N  N   . SER   B 1 81  ? 32.545 -9.710  6.976  1.00 19.77 ? 87  SER   C N   1 
ATOM   1732 C  CA  . SER   B 1 81  ? 31.799 -10.730 6.277  1.00 20.53 ? 87  SER   C CA  1 
ATOM   1733 C  C   . SER   B 1 81  ? 30.684 -10.046 5.498  1.00 21.68 ? 87  SER   C C   1 
ATOM   1734 O  O   . SER   B 1 81  ? 30.566 -8.792  5.509  1.00 21.18 ? 87  SER   C O   1 
ATOM   1735 C  CB  . SER   B 1 81  ? 31.276 -11.749 7.288  1.00 21.40 ? 87  SER   C CB  1 
ATOM   1736 O  OG  . SER   B 1 81  ? 30.256 -11.098 8.026  1.00 22.61 ? 87  SER   C OG  1 
ATOM   1737 N  N   . GLU   B 1 82  ? 29.838 -10.852 4.827  1.00 24.26 ? 88  GLU   C N   1 
ATOM   1738 C  CA  . GLU   B 1 82  ? 28.738 -10.214 4.132  1.00 25.24 ? 88  GLU   C CA  1 
ATOM   1739 C  C   . GLU   B 1 82  ? 27.737 -9.574  5.112  1.00 24.63 ? 88  GLU   C C   1 
ATOM   1740 O  O   . GLU   B 1 82  ? 26.951 -8.726  4.707  1.00 25.76 ? 88  GLU   C O   1 
ATOM   1741 C  CB  . GLU   B 1 82  ? 28.065 -11.155 3.121  1.00 30.24 ? 88  GLU   C CB  1 
ATOM   1742 C  CG  . GLU   B 1 82  ? 27.410 -12.378 3.722  1.00 37.83 ? 88  GLU   C CG  1 
ATOM   1743 C  CD  . GLU   B 1 82  ? 26.821 -13.255 2.636  1.00 41.81 ? 88  GLU   C CD  1 
ATOM   1744 O  OE1 . GLU   B 1 82  ? 27.495 -13.432 1.595  1.00 42.77 ? 88  GLU   C OE1 1 
ATOM   1745 O  OE2 . GLU   B 1 82  ? 25.675 -13.727 2.809  1.00 43.73 ? 88  GLU   C OE2 1 
ATOM   1746 N  N   . TYR   B 1 83  ? 27.798 -9.925  6.424  1.00 21.91 ? 89  TYR   C N   1 
ATOM   1747 C  CA  . TYR   B 1 83  ? 26.780 -9.462  7.358  1.00 21.11 ? 89  TYR   C CA  1 
ATOM   1748 C  C   . TYR   B 1 83  ? 27.302 -8.566  8.532  1.00 20.82 ? 89  TYR   C C   1 
ATOM   1749 O  O   . TYR   B 1 83  ? 26.496 -7.947  9.212  1.00 21.56 ? 89  TYR   C O   1 
ATOM   1750 C  CB  . TYR   B 1 83  ? 25.967 -10.699 7.867  1.00 20.50 ? 89  TYR   C CB  1 
ATOM   1751 C  CG  . TYR   B 1 83  ? 26.815 -11.933 8.230  1.00 19.53 ? 89  TYR   C CG  1 
ATOM   1752 C  CD1 . TYR   B 1 83  ? 27.100 -12.930 7.282  1.00 19.41 ? 89  TYR   C CD1 1 
ATOM   1753 C  CD2 . TYR   B 1 83  ? 27.291 -12.119 9.520  1.00 18.53 ? 89  TYR   C CD2 1 
ATOM   1754 C  CE1 . TYR   B 1 83  ? 27.866 -14.061 7.617  1.00 17.28 ? 89  TYR   C CE1 1 
ATOM   1755 C  CE2 . TYR   B 1 83  ? 28.055 -13.217 9.858  1.00 18.88 ? 89  TYR   C CE2 1 
ATOM   1756 C  CZ  . TYR   B 1 83  ? 28.357 -14.186 8.906  1.00 18.74 ? 89  TYR   C CZ  1 
ATOM   1757 O  OH  . TYR   B 1 83  ? 29.143 -15.274 9.260  1.00 20.97 ? 89  TYR   C OH  1 
ATOM   1758 N  N   . TYR   B 1 84  ? 28.624 -8.455  8.767  1.00 17.76 ? 90  TYR   C N   1 
ATOM   1759 C  CA  . TYR   B 1 84  ? 29.168 -7.526  9.790  1.00 16.78 ? 90  TYR   C CA  1 
ATOM   1760 C  C   . TYR   B 1 84  ? 30.481 -6.919  9.250  1.00 15.92 ? 90  TYR   C C   1 
ATOM   1761 O  O   . TYR   B 1 84  ? 31.185 -7.588  8.495  1.00 15.72 ? 90  TYR   C O   1 
ATOM   1762 C  CB  . TYR   B 1 84  ? 29.530 -8.266  11.130 1.00 16.19 ? 90  TYR   C CB  1 
ATOM   1763 C  CG  . TYR   B 1 84  ? 28.361 -8.763  11.946 1.00 13.91 ? 90  TYR   C CG  1 
ATOM   1764 C  CD1 . TYR   B 1 84  ? 27.467 -7.883  12.531 1.00 14.15 ? 90  TYR   C CD1 1 
ATOM   1765 C  CD2 . TYR   B 1 84  ? 28.166 -10.102 12.142 1.00 12.55 ? 90  TYR   C CD2 1 
ATOM   1766 C  CE1 . TYR   B 1 84  ? 26.429 -8.334  13.344 1.00 13.89 ? 90  TYR   C CE1 1 
ATOM   1767 C  CE2 . TYR   B 1 84  ? 27.094 -10.574 12.906 1.00 13.18 ? 90  TYR   C CE2 1 
ATOM   1768 C  CZ  . TYR   B 1 84  ? 26.226 -9.684  13.516 1.00 14.24 ? 90  TYR   C CZ  1 
ATOM   1769 O  OH  . TYR   B 1 84  ? 25.164 -10.139 14.288 1.00 13.05 ? 90  TYR   C OH  1 
ATOM   1770 N  N   . PRO   B 1 85  ? 30.905 -5.764  9.748  1.00 15.89 ? 91  PRO   C N   1 
ATOM   1771 C  CA  . PRO   B 1 85  ? 32.258 -5.277  9.421  1.00 15.84 ? 91  PRO   C CA  1 
ATOM   1772 C  C   . PRO   B 1 85  ? 33.311 -6.093  10.207 1.00 16.01 ? 91  PRO   C C   1 
ATOM   1773 O  O   . PRO   B 1 85  ? 32.986 -6.903  11.112 1.00 15.94 ? 91  PRO   C O   1 
ATOM   1774 C  CB  . PRO   B 1 85  ? 32.219 -3.822  9.930  1.00 17.69 ? 91  PRO   C CB  1 
ATOM   1775 C  CG  . PRO   B 1 85  ? 31.295 -3.885  11.141 1.00 18.33 ? 91  PRO   C CG  1 
ATOM   1776 C  CD  . PRO   B 1 85  ? 30.213 -4.861  10.706 1.00 16.51 ? 91  PRO   C CD  1 
ATOM   1777 N  N   . ALA   B 1 86  ? 34.603 -5.819  9.953  1.00 15.20 ? 92  ALA   C N   1 
ATOM   1778 C  CA  . ALA   B 1 86  ? 35.674 -6.418  10.757 1.00 15.33 ? 92  ALA   C CA  1 
ATOM   1779 C  C   . ALA   B 1 86  ? 35.535 -5.888  12.199 1.00 16.32 ? 92  ALA   C C   1 
ATOM   1780 O  O   . ALA   B 1 86  ? 35.286 -4.684  12.383 1.00 18.37 ? 92  ALA   C O   1 
ATOM   1781 C  CB  . ALA   B 1 86  ? 37.038 -6.051  10.182 1.00 15.58 ? 92  ALA   C CB  1 
ATOM   1782 N  N   . ARG   B 1 87  ? 35.535 -6.780  13.187 1.00 15.12 ? 93  ARG   C N   1 
ATOM   1783 C  CA  . ARG   B 1 87  ? 35.277 -6.379  14.566 1.00 15.18 ? 93  ARG   C CA  1 
ATOM   1784 C  C   . ARG   B 1 87  ? 35.654 -7.480  15.535 1.00 15.02 ? 93  ARG   C C   1 
ATOM   1785 O  O   . ARG   B 1 87  ? 35.898 -8.609  15.104 1.00 14.67 ? 93  ARG   C O   1 
ATOM   1786 C  CB  . ARG   B 1 87  ? 33.760 -6.078  14.728 1.00 16.05 ? 93  ARG   C CB  1 
ATOM   1787 C  CG  . ARG   B 1 87  ? 32.887 -7.356  14.704 1.00 14.73 ? 93  ARG   C CG  1 
ATOM   1788 C  CD  . ARG   B 1 87  ? 31.400 -7.068  14.675 1.00 15.38 ? 93  ARG   C CD  1 
ATOM   1789 N  NE  . ARG   B 1 87  ? 30.676 -8.328  14.877 1.00 16.39 ? 93  ARG   C NE  1 
ATOM   1790 C  CZ  . ARG   B 1 87  ? 29.637 -8.511  15.663 1.00 18.13 ? 93  ARG   C CZ  1 
ATOM   1791 N  NH1 . ARG   B 1 87  ? 29.108 -7.477  16.329 1.00 17.24 ? 93  ARG   C NH1 1 
ATOM   1792 N  NH2 . ARG   B 1 87  ? 29.094 -9.728  15.783 1.00 17.90 ? 93  ARG   C NH2 1 
ATOM   1793 N  N   . TYR   B 1 88  ? 35.591 -7.193  16.860 1.00 16.45 ? 94  TYR   C N   1 
ATOM   1794 C  CA  . TYR   B 1 88  ? 35.726 -8.268  17.849 1.00 18.39 ? 94  TYR   C CA  1 
ATOM   1795 C  C   . TYR   B 1 88  ? 34.348 -8.873  18.107 1.00 16.97 ? 94  TYR   C C   1 
ATOM   1796 O  O   . TYR   B 1 88  ? 33.365 -8.152  18.295 1.00 18.19 ? 94  TYR   C O   1 
ATOM   1797 C  CB  . TYR   B 1 88  ? 36.248 -7.754  19.205 1.00 21.16 ? 94  TYR   C CB  1 
ATOM   1798 C  CG  . TYR   B 1 88  ? 37.693 -7.372  19.113 1.00 25.35 ? 94  TYR   C CG  1 
ATOM   1799 C  CD1 . TYR   B 1 88  ? 38.690 -8.327  19.247 1.00 27.95 ? 94  TYR   C CD1 1 
ATOM   1800 C  CD2 . TYR   B 1 88  ? 38.061 -6.077  18.765 1.00 28.49 ? 94  TYR   C CD2 1 
ATOM   1801 C  CE1 . TYR   B 1 88  ? 40.031 -7.986  19.100 1.00 30.01 ? 94  TYR   C CE1 1 
ATOM   1802 C  CE2 . TYR   B 1 88  ? 39.388 -5.727  18.604 1.00 30.88 ? 94  TYR   C CE2 1 
ATOM   1803 C  CZ  . TYR   B 1 88  ? 40.367 -6.686  18.750 1.00 32.17 ? 94  TYR   C CZ  1 
ATOM   1804 O  OH  . TYR   B 1 88  ? 41.662 -6.256  18.601 1.00 36.45 ? 94  TYR   C OH  1 
ATOM   1805 N  N   . GLN   B 1 89  ? 34.269 -10.197 18.113 1.00 14.95 ? 95  GLN   C N   1 
ATOM   1806 C  CA  . GLN   B 1 89  ? 33.027 -10.885 18.483 1.00 13.66 ? 95  GLN   C CA  1 
ATOM   1807 C  C   . GLN   B 1 89  ? 33.356 -11.614 19.816 1.00 12.40 ? 95  GLN   C C   1 
ATOM   1808 O  O   . GLN   B 1 89  ? 34.446 -12.185 19.957 1.00 13.37 ? 95  GLN   C O   1 
ATOM   1809 C  CB  . GLN   B 1 89  ? 32.640 -11.859 17.379 1.00 15.59 ? 95  GLN   C CB  1 
ATOM   1810 C  CG  . GLN   B 1 89  ? 31.365 -12.595 17.698 1.00 16.50 ? 95  GLN   C CG  1 
ATOM   1811 C  CD  . GLN   B 1 89  ? 30.689 -13.148 16.469 1.00 15.20 ? 95  GLN   C CD  1 
ATOM   1812 O  OE1 . GLN   B 1 89  ? 30.632 -12.542 15.398 1.00 15.94 ? 95  GLN   C OE1 1 
ATOM   1813 N  NE2 . GLN   B 1 89  ? 30.156 -14.292 16.648 1.00 13.13 ? 95  GLN   C NE2 1 
ATOM   1814 N  N   . SER   B 1 90  ? 32.453 -11.562 20.765 1.00 11.66 ? 96  SER   C N   1 
ATOM   1815 C  CA  . SER   B 1 90  ? 32.661 -12.177 22.067 1.00 12.13 ? 96  SER   C CA  1 
ATOM   1816 C  C   . SER   B 1 90  ? 32.044 -13.588 22.136 1.00 11.43 ? 96  SER   C C   1 
ATOM   1817 O  O   . SER   B 1 90  ? 31.211 -13.956 21.294 1.00 11.80 ? 96  SER   C O   1 
ATOM   1818 C  CB  . SER   B 1 90  ? 32.136 -11.291 23.211 1.00 13.79 ? 96  SER   C CB  1 
ATOM   1819 O  OG  . SER   B 1 90  ? 30.732 -11.227 23.065 1.00 15.58 ? 96  SER   C OG  1 
ATOM   1820 N  N   . HIS   B 1 91  ? 32.520 -14.386 23.124 1.00 11.37 ? 97  HIS   C N   1 
ATOM   1821 C  CA  . HIS   B 1 91  ? 32.028 -15.745 23.376 1.00 11.88 ? 97  HIS   C CA  1 
ATOM   1822 C  C   . HIS   B 1 91  ? 32.119 -16.622 22.117 1.00 12.22 ? 97  HIS   C C   1 
ATOM   1823 O  O   . HIS   B 1 91  ? 31.232 -17.442 21.857 1.00 12.17 ? 97  HIS   C O   1 
ATOM   1824 C  CB  . HIS   B 1 91  ? 30.588 -15.719 23.924 1.00 11.87 ? 97  HIS   C CB  1 
ATOM   1825 C  CG  . HIS   B 1 91  ? 30.456 -14.957 25.226 1.00 13.38 ? 97  HIS   C CG  1 
ATOM   1826 N  ND1 . HIS   B 1 91  ? 30.515 -15.616 26.453 1.00 14.41 ? 97  HIS   C ND1 1 
ATOM   1827 C  CD2 . HIS   B 1 91  ? 30.302 -13.609 25.463 1.00 14.49 ? 97  HIS   C CD2 1 
ATOM   1828 C  CE1 . HIS   B 1 91  ? 30.357 -14.679 27.396 1.00 14.90 ? 97  HIS   C CE1 1 
ATOM   1829 N  NE2 . HIS   B 1 91  ? 30.240 -13.443 26.854 1.00 16.01 ? 97  HIS   C NE2 1 
ATOM   1830 N  N   . LEU   B 1 92  ? 33.187 -16.427 21.355 1.00 10.98 ? 98  LEU   C N   1 
ATOM   1831 C  CA  . LEU   B 1 92  ? 33.408 -17.133 20.099 1.00 11.50 ? 98  LEU   C CA  1 
ATOM   1832 C  C   . LEU   B 1 92  ? 34.490 -18.206 20.283 1.00 10.39 ? 98  LEU   C C   1 
ATOM   1833 O  O   . LEU   B 1 92  ? 35.475 -18.023 20.996 1.00 10.97 ? 98  LEU   C O   1 
ATOM   1834 C  CB  . LEU   B 1 92  ? 33.849 -16.143 18.978 1.00 11.53 ? 98  LEU   C CB  1 
ATOM   1835 C  CG  . LEU   B 1 92  ? 33.922 -16.727 17.567 1.00 12.35 ? 98  LEU   C CG  1 
ATOM   1836 C  CD1 . LEU   B 1 92  ? 32.536 -17.031 17.027 1.00 13.24 ? 98  LEU   C CD1 1 
ATOM   1837 C  CD2 . LEU   B 1 92  ? 34.586 -15.694 16.591 1.00 13.69 ? 98  LEU   C CD2 1 
ATOM   1838 N  N   . MET   B 1 93  ? 34.275 -19.382 19.660 1.00 10.53 ? 99  MET   C N   1 
ATOM   1839 C  CA  . MET   B 1 93  ? 35.210 -20.515 19.700 1.00 9.81  ? 99  MET   C CA  1 
ATOM   1840 C  C   . MET   B 1 93  ? 35.609 -20.839 18.245 1.00 9.96  ? 99  MET   C C   1 
ATOM   1841 O  O   . MET   B 1 93  ? 34.726 -20.866 17.389 1.00 11.26 ? 99  MET   C O   1 
ATOM   1842 C  CB  . MET   B 1 93  ? 34.485 -21.722 20.312 1.00 11.28 ? 99  MET   C CB  1 
ATOM   1843 C  CG  . MET   B 1 93  ? 34.007 -21.398 21.710 1.00 11.89 ? 99  MET   C CG  1 
ATOM   1844 S  SD  . MET   B 1 93  ? 32.998 -22.748 22.376 1.00 13.03 ? 99  MET   C SD  1 
ATOM   1845 C  CE  . MET   B 1 93  ? 31.604 -22.701 21.298 1.00 13.21 ? 99  MET   C CE  1 
ATOM   1846 N  N   . LEU   B 1 94  ? 36.880 -21.100 17.973 1.00 9.97  ? 100 LEU   C N   1 
ATOM   1847 C  CA  . LEU   B 1 94  ? 37.291 -21.433 16.625 1.00 11.14 ? 100 LEU   C CA  1 
ATOM   1848 C  C   . LEU   B 1 94  ? 37.712 -22.886 16.498 1.00 11.27 ? 100 LEU   C C   1 
ATOM   1849 O  O   . LEU   B 1 94  ? 38.241 -23.473 17.434 1.00 11.71 ? 100 LEU   C O   1 
ATOM   1850 C  CB  . LEU   B 1 94  ? 38.517 -20.585 16.203 1.00 13.32 ? 100 LEU   C CB  1 
ATOM   1851 C  CG  . LEU   B 1 94  ? 38.361 -19.091 16.194 1.00 13.26 ? 100 LEU   C CG  1 
ATOM   1852 C  CD1 . LEU   B 1 94  ? 39.637 -18.454 15.705 1.00 16.77 ? 100 LEU   C CD1 1 
ATOM   1853 C  CD2 . LEU   B 1 94  ? 37.169 -18.637 15.344 1.00 14.97 ? 100 LEU   C CD2 1 
ATOM   1854 N  N   . ALA   B 1 95  ? 37.547 -23.430 15.278 1.00 11.40 ? 101 ALA   C N   1 
ATOM   1855 C  CA  . ALA   B 1 95  ? 38.069 -24.735 14.888 1.00 11.25 ? 101 ALA   C CA  1 
ATOM   1856 C  C   . ALA   B 1 95  ? 38.639 -24.638 13.469 1.00 11.42 ? 101 ALA   C C   1 
ATOM   1857 O  O   . ALA   B 1 95  ? 38.297 -23.697 12.736 1.00 11.50 ? 101 ALA   C O   1 
ATOM   1858 C  CB  . ALA   B 1 95  ? 36.971 -25.806 14.927 1.00 12.26 ? 101 ALA   C CB  1 
ATOM   1859 N  N   . VAL   B 1 96  ? 39.495 -25.579 13.059 1.00 11.24 ? 102 VAL   C N   1 
ATOM   1860 C  CA  . VAL   B 1 96  ? 39.947 -25.631 11.669 1.00 12.65 ? 102 VAL   C CA  1 
ATOM   1861 C  C   . VAL   B 1 96  ? 38.890 -26.385 10.885 1.00 13.59 ? 102 VAL   C C   1 
ATOM   1862 O  O   . VAL   B 1 96  ? 38.571 -27.556 11.179 1.00 14.56 ? 102 VAL   C O   1 
ATOM   1863 C  CB  . VAL   B 1 96  ? 41.309 -26.343 11.637 1.00 13.03 ? 102 VAL   C CB  1 
ATOM   1864 C  CG1 . VAL   B 1 96  ? 41.796 -26.440 10.198 1.00 14.51 ? 102 VAL   C CG1 1 
ATOM   1865 C  CG2 . VAL   B 1 96  ? 42.325 -25.595 12.486 1.00 13.98 ? 102 VAL   C CG2 1 
ATOM   1866 N  N   . GLY   B 1 97  ? 38.282 -25.671 9.934  1.00 13.93 ? 103 GLY   C N   1 
ATOM   1867 C  CA  . GLY   B 1 97  ? 37.210 -26.286 9.166  1.00 14.29 ? 103 GLY   C CA  1 
ATOM   1868 C  C   . GLY   B 1 97  ? 36.549 -25.302 8.240  1.00 15.54 ? 103 GLY   C C   1 
ATOM   1869 O  O   . GLY   B 1 97  ? 36.838 -24.095 8.254  1.00 16.24 ? 103 GLY   C O   1 
ATOM   1870 N  N   . HIS   B 1 98  ? 35.681 -25.833 7.395  1.00 15.31 ? 104 HIS   C N   1 
ATOM   1871 C  CA  . HIS   B 1 98  ? 34.975 -25.048 6.408  1.00 15.23 ? 104 HIS   C CA  1 
ATOM   1872 C  C   . HIS   B 1 98  ? 33.694 -24.376 6.907  1.00 15.06 ? 104 HIS   C C   1 
ATOM   1873 O  O   . HIS   B 1 98  ? 32.908 -25.015 7.638  1.00 14.82 ? 104 HIS   C O   1 
ATOM   1874 C  CB  . HIS   B 1 98  ? 34.603 -25.945 5.220  1.00 17.49 ? 104 HIS   C CB  1 
ATOM   1875 C  CG  . HIS   B 1 98  ? 34.013 -25.169 4.092  1.00 22.18 ? 104 HIS   C CG  1 
ATOM   1876 N  ND1 . HIS   B 1 98  ? 34.765 -24.240 3.385  1.00 24.87 ? 104 HIS   C ND1 1 
ATOM   1877 C  CD2 . HIS   B 1 98  ? 32.745 -25.173 3.613  1.00 24.24 ? 104 HIS   C CD2 1 
ATOM   1878 C  CE1 . HIS   B 1 98  ? 33.936 -23.719 2.483  1.00 26.89 ? 104 HIS   C CE1 1 
ATOM   1879 N  NE2 . HIS   B 1 98  ? 32.715 -24.269 2.566  1.00 26.87 ? 104 HIS   C NE2 1 
ATOM   1880 N  N   . SER   B 1 99  ? 33.460 -23.108 6.528  1.00 14.46 ? 105 SER   C N   1 
ATOM   1881 C  CA  . SER   B 1 99  ? 32.258 -22.335 6.930  1.00 14.64 ? 105 SER   C CA  1 
ATOM   1882 C  C   . SER   B 1 99  ? 31.994 -21.236 5.886  1.00 16.14 ? 105 SER   C C   1 
ATOM   1883 O  O   . SER   B 1 99  ? 32.780 -20.270 5.812  1.00 18.70 ? 105 SER   C O   1 
ATOM   1884 C  CB  . SER   B 1 99  ? 32.552 -21.662 8.271  1.00 16.53 ? 105 SER   C CB  1 
ATOM   1885 O  OG  . SER   B 1 99  ? 31.468 -20.857 8.726  1.00 18.22 ? 105 SER   C OG  1 
ATOM   1886 N  N   . GLU   B 1 100 ? 30.902 -21.378 5.119  1.00 14.77 ? 106 GLU   C N   1 
ATOM   1887 C  CA  . GLU   B 1 100 ? 30.401 -20.369 4.152  1.00 15.17 ? 106 GLU   C CA  1 
ATOM   1888 C  C   . GLU   B 1 100 ? 29.335 -19.543 4.953  1.00 13.46 ? 106 GLU   C C   1 
ATOM   1889 O  O   . GLU   B 1 100 ? 28.778 -20.003 5.976  1.00 12.77 ? 106 GLU   C O   1 
ATOM   1890 C  CB  . GLU   B 1 100 ? 29.638 -21.076 2.956  1.00 17.49 ? 106 GLU   C CB  1 
ATOM   1891 C  CG  . GLU   B 1 100 ? 30.440 -22.025 2.071  1.00 20.74 ? 106 GLU   C CG  1 
ATOM   1892 C  CD  . GLU   B 1 100 ? 31.443 -21.360 1.164  1.00 24.09 ? 106 GLU   C CD  1 
ATOM   1893 O  OE1 . GLU   B 1 100 ? 32.183 -22.094 0.477  1.00 27.76 ? 106 GLU   C OE1 1 
ATOM   1894 O  OE2 . GLU   B 1 100 ? 31.514 -20.110 1.161  1.00 24.03 ? 106 GLU   C OE2 1 
ATOM   1895 N  N   . PRO   B 1 101 ? 28.957 -18.354 4.454  1.00 13.99 ? 107 PRO   C N   1 
ATOM   1896 C  CA  . PRO   B 1 101 ? 27.895 -17.584 5.152  1.00 14.15 ? 107 PRO   C CA  1 
ATOM   1897 C  C   . PRO   B 1 101 ? 26.604 -18.408 5.363  1.00 14.72 ? 107 PRO   C C   1 
ATOM   1898 O  O   . PRO   B 1 101 ? 26.003 -18.369 6.450  1.00 13.73 ? 107 PRO   C O   1 
ATOM   1899 C  CB  . PRO   B 1 101 ? 27.650 -16.379 4.189  1.00 16.56 ? 107 PRO   C CB  1 
ATOM   1900 C  CG  . PRO   B 1 101 ? 28.967 -16.252 3.413  1.00 18.46 ? 107 PRO   C CG  1 
ATOM   1901 C  CD  . PRO   B 1 101 ? 29.551 -17.620 3.298  1.00 15.26 ? 107 PRO   C CD  1 
ATOM   1902 N  N   . GLY   B 1 102 ? 26.242 -19.236 4.394  1.00 12.80 ? 108 GLY   C N   1 
ATOM   1903 C  CA  . GLY   B 1 102 ? 25.041 -20.059 4.493  1.00 13.35 ? 108 GLY   C CA  1 
ATOM   1904 C  C   . GLY   B 1 102 ? 25.111 -21.164 5.536  1.00 13.52 ? 108 GLY   C C   1 
ATOM   1905 O  O   . GLY   B 1 102 ? 24.098 -21.806 5.863  1.00 14.01 ? 108 GLY   C O   1 
ATOM   1906 N  N   . ASP   B 1 103 ? 26.333 -21.424 6.029  1.00 12.58 ? 109 ASP   C N   1 
ATOM   1907 C  CA  . ASP   B 1 103 ? 26.510 -22.422 7.071  1.00 11.87 ? 109 ASP   C CA  1 
ATOM   1908 C  C   . ASP   B 1 103 ? 26.156 -21.919 8.484  1.00 11.18 ? 109 ASP   C C   1 
ATOM   1909 O  O   . ASP   B 1 103 ? 26.036 -22.744 9.395  1.00 11.77 ? 109 ASP   C O   1 
ATOM   1910 C  CB  . ASP   B 1 103 ? 27.968 -22.939 7.073  1.00 11.74 ? 109 ASP   C CB  1 
ATOM   1911 C  CG  . ASP   B 1 103 ? 28.239 -23.785 5.883  1.00 13.35 ? 109 ASP   C CG  1 
ATOM   1912 O  OD1 . ASP   B 1 103 ? 27.333 -24.524 5.469  1.00 14.88 ? 109 ASP   C OD1 1 
ATOM   1913 O  OD2 . ASP   B 1 103 ? 29.371 -23.700 5.339  1.00 13.84 ? 109 ASP   C OD2 1 
ATOM   1914 N  N   . CYS   B 1 104 ? 25.911 -20.611 8.669  1.00 11.20 ? 110 CYS   C N   1 
ATOM   1915 C  CA  . CYS   B 1 104 ? 25.548 -20.042 9.976  1.00 11.30 ? 110 CYS   C CA  1 
ATOM   1916 C  C   . CYS   B 1 104 ? 24.294 -20.724 10.483 1.00 11.58 ? 110 CYS   C C   1 
ATOM   1917 O  O   . CYS   B 1 104 ? 23.353 -20.948 9.720  1.00 12.39 ? 110 CYS   C O   1 
ATOM   1918 C  CB  . CYS   B 1 104 ? 25.342 -18.533 9.882  1.00 12.31 ? 110 CYS   C CB  1 
ATOM   1919 S  SG  . CYS   B 1 104 ? 26.871 -17.603 9.777  1.00 13.50 ? 110 CYS   C SG  1 
ATOM   1920 N  N   . GLY   B 1 105 ? 24.291 -21.058 11.766 1.00 9.97  ? 111 GLY   C N   1 
ATOM   1921 C  CA  . GLY   B 1 105 ? 23.167 -21.757 12.390 1.00 10.97 ? 111 GLY   C CA  1 
ATOM   1922 C  C   . GLY   B 1 105 ? 23.366 -23.250 12.539 1.00 11.13 ? 111 GLY   C C   1 
ATOM   1923 O  O   . GLY   B 1 105 ? 22.602 -23.897 13.262 1.00 11.66 ? 111 GLY   C O   1 
ATOM   1924 N  N   . GLY   B 1 106 ? 24.393 -23.817 11.884 1.00 11.22 ? 112 GLY   C N   1 
ATOM   1925 C  CA  . GLY   B 1 106 ? 24.695 -25.250 12.061 1.00 10.42 ? 112 GLY   C CA  1 
ATOM   1926 C  C   . GLY   B 1 106 ? 25.098 -25.550 13.498 1.00 10.42 ? 112 GLY   C C   1 
ATOM   1927 O  O   . GLY   B 1 106 ? 25.851 -24.772 14.110 1.00 10.58 ? 112 GLY   C O   1 
ATOM   1928 N  N   . ILE   B 1 107 ? 24.643 -26.667 14.036 1.00 10.27 ? 113 ILE   C N   1 
ATOM   1929 C  CA  . ILE   B 1 107 ? 24.941 -26.988 15.435 1.00 10.61 ? 113 ILE   C CA  1 
ATOM   1930 C  C   . ILE   B 1 107 ? 26.280 -27.637 15.643 1.00 10.24 ? 113 ILE   C C   1 
ATOM   1931 O  O   . ILE   B 1 107 ? 26.690 -28.517 14.879 1.00 10.48 ? 113 ILE   C O   1 
ATOM   1932 C  CB  . ILE   B 1 107 ? 23.779 -27.871 15.978 1.00 13.65 ? 113 ILE   C CB  1 
ATOM   1933 C  CG1 . ILE   B 1 107 ? 22.560 -26.925 16.386 1.00 16.52 ? 113 ILE   C CG1 1 
ATOM   1934 C  CG2 . ILE   B 1 107 ? 24.228 -28.707 17.228 1.00 13.66 ? 113 ILE   C CG2 1 
ATOM   1935 C  CD1 . ILE   B 1 107 ? 21.256 -27.696 16.771 1.00 19.82 ? 113 ILE   C CD1 1 
ATOM   1936 N  N   . LEU   B 1 108 ? 26.969 -27.169 16.713 1.00 9.75  ? 114 LEU   C N   1 
ATOM   1937 C  CA  . LEU   B 1 108 ? 28.127 -27.871 17.251 1.00 8.71  ? 114 LEU   C CA  1 
ATOM   1938 C  C   . LEU   B 1 108 ? 27.620 -28.619 18.514 1.00 9.49  ? 114 LEU   C C   1 
ATOM   1939 O  O   . LEU   B 1 108 ? 27.002 -27.988 19.398 1.00 9.38  ? 114 LEU   C O   1 
ATOM   1940 C  CB  . LEU   B 1 108 ? 29.208 -26.834 17.634 1.00 9.73  ? 114 LEU   C CB  1 
ATOM   1941 C  CG  . LEU   B 1 108 ? 30.395 -27.353 18.450 1.00 9.58  ? 114 LEU   C CG  1 
ATOM   1942 C  CD1 . LEU   B 1 108 ? 31.270 -28.322 17.564 1.00 10.53 ? 114 LEU   C CD1 1 
ATOM   1943 C  CD2 . LEU   B 1 108 ? 31.235 -26.194 18.952 1.00 9.98  ? 114 LEU   C CD2 1 
ATOM   1944 N  N   . ARG   B 1 109 ? 27.910 -29.915 18.605 1.00 9.46  ? 115 ARG   C N   1 
ATOM   1945 C  CA  . ARG   B 1 109 ? 27.459 -30.695 19.756 1.00 10.56 ? 115 ARG   C CA  1 
ATOM   1946 C  C   . ARG   B 1 109 ? 28.577 -31.531 20.322 1.00 11.12 ? 115 ARG   C C   1 
ATOM   1947 O  O   . ARG   B 1 109 ? 29.485 -31.990 19.603 1.00 11.09 ? 115 ARG   C O   1 
ATOM   1948 C  CB  . ARG   B 1 109 ? 26.298 -31.598 19.329 1.00 14.47 ? 115 ARG   C CB  1 
ATOM   1949 C  CG  . ARG   B 1 109 ? 26.641 -32.626 18.323 1.00 20.61 ? 115 ARG   C CG  1 
ATOM   1950 C  CD  . ARG   B 1 109 ? 25.389 -33.450 18.000 1.00 30.66 ? 115 ARG   C CD  1 
ATOM   1951 N  NE  . ARG   B 1 109 ? 24.452 -32.738 17.117 1.00 38.23 ? 115 ARG   C NE  1 
ATOM   1952 C  CZ  . ARG   B 1 109 ? 23.224 -32.343 17.473 1.00 45.13 ? 115 ARG   C CZ  1 
ATOM   1953 N  NH1 . ARG   B 1 109 ? 22.777 -32.560 18.712 1.00 43.81 ? 115 ARG   C NH1 1 
ATOM   1954 N  NH2 . ARG   B 1 109 ? 22.449 -31.699 16.604 1.00 46.87 ? 115 ARG   C NH2 1 
ATOM   1955 N  N   . CYS   B 1 110 ? 28.472 -31.797 21.617 1.00 10.93 ? 116 CYS   C N   1 
ATOM   1956 C  CA  . CYS   B 1 110 ? 29.428 -32.685 22.335 1.00 11.52 ? 116 CYS   C CA  1 
ATOM   1957 C  C   . CYS   B 1 110 ? 28.555 -33.769 23.031 1.00 12.61 ? 116 CYS   C C   1 
ATOM   1958 O  O   . CYS   B 1 110 ? 27.342 -33.834 22.830 1.00 12.70 ? 116 CYS   C O   1 
ATOM   1959 C  CB  . CYS   B 1 110 ? 30.237 -31.876 23.357 1.00 10.49 ? 116 CYS   C CB  1 
ATOM   1960 S  SG  . CYS   B 1 110 ? 29.215 -31.179 24.706 1.00 11.07 ? 116 CYS   C SG  1 
ATOM   1961 N  N   . GLN   B 1 111 ? 29.181 -34.633 23.894 1.00 12.96 ? 117 GLN   C N   1 
ATOM   1962 C  CA  . GLN   B 1 111 ? 28.377 -35.665 24.571 1.00 14.63 ? 117 GLN   C CA  1 
ATOM   1963 C  C   . GLN   B 1 111 ? 27.312 -35.084 25.509 1.00 15.31 ? 117 GLN   C C   1 
ATOM   1964 O  O   . GLN   B 1 111 ? 26.343 -35.773 25.848 1.00 16.73 ? 117 GLN   C O   1 
ATOM   1965 C  CB  . GLN   B 1 111 ? 29.289 -36.640 25.369 1.00 15.78 ? 117 GLN   C CB  1 
ATOM   1966 C  CG  . GLN   B 1 111 ? 29.965 -35.975 26.568 1.00 19.53 ? 117 GLN   C CG  1 
ATOM   1967 C  CD  . GLN   B 1 111 ? 30.925 -36.868 27.321 1.00 30.21 ? 117 GLN   C CD  1 
ATOM   1968 O  OE1 . GLN   B 1 111 ? 32.142 -36.804 27.103 1.00 34.30 ? 117 GLN   C OE1 1 
ATOM   1969 N  NE2 . GLN   B 1 111 ? 30.415 -37.667 28.264 1.00 31.62 ? 117 GLN   C NE2 1 
ATOM   1970 N  N   . HIS   B 1 112 ? 27.464 -33.811 25.914 1.00 13.28 ? 118 HIS   C N   1 
ATOM   1971 C  CA  . HIS   B 1 112 ? 26.516 -33.187 26.829 1.00 12.71 ? 118 HIS   C CA  1 
ATOM   1972 C  C   . HIS   B 1 112 ? 25.344 -32.497 26.154 1.00 13.14 ? 118 HIS   C C   1 
ATOM   1973 O  O   . HIS   B 1 112 ? 24.404 -32.090 26.868 1.00 13.62 ? 118 HIS   C O   1 
ATOM   1974 C  CB  . HIS   B 1 112 ? 27.238 -32.200 27.753 1.00 12.48 ? 118 HIS   C CB  1 
ATOM   1975 C  CG  . HIS   B 1 112 ? 28.393 -32.842 28.461 1.00 13.57 ? 118 HIS   C CG  1 
ATOM   1976 N  ND1 . HIS   B 1 112 ? 29.717 -32.616 28.104 1.00 9.77  ? 118 HIS   C ND1 1 
ATOM   1977 C  CD2 . HIS   B 1 112 ? 28.387 -33.645 29.543 1.00 15.03 ? 118 HIS   C CD2 1 
ATOM   1978 C  CE1 . HIS   B 1 112 ? 30.464 -33.311 28.953 1.00 13.73 ? 118 HIS   C CE1 1 
ATOM   1979 N  NE2 . HIS   B 1 112 ? 29.698 -33.953 29.826 1.00 15.56 ? 118 HIS   C NE2 1 
ATOM   1980 N  N   . GLY   B 1 113 ? 25.430 -32.237 24.853 1.00 11.57 ? 119 GLY   C N   1 
ATOM   1981 C  CA  . GLY   B 1 113 ? 24.347 -31.535 24.167 1.00 11.65 ? 119 GLY   C CA  1 
ATOM   1982 C  C   . GLY   B 1 113 ? 24.872 -30.483 23.202 1.00 10.87 ? 119 GLY   C C   1 
ATOM   1983 O  O   . GLY   B 1 113 ? 25.999 -30.597 22.709 1.00 11.21 ? 119 GLY   C O   1 
ATOM   1984 N  N   . VAL   B 1 114 ? 24.032 -29.470 22.938 1.00 10.33 ? 120 VAL   C N   1 
ATOM   1985 C  CA  . VAL   B 1 114 ? 24.383 -28.434 21.983 1.00 10.34 ? 120 VAL   C CA  1 
ATOM   1986 C  C   . VAL   B 1 114 ? 25.349 -27.428 22.630 1.00 10.29 ? 120 VAL   C C   1 
ATOM   1987 O  O   . VAL   B 1 114 ? 25.058 -26.864 23.705 1.00 11.12 ? 120 VAL   C O   1 
ATOM   1988 C  CB  . VAL   B 1 114 ? 23.115 -27.706 21.490 1.00 11.83 ? 120 VAL   C CB  1 
ATOM   1989 C  CG1 . VAL   B 1 114 ? 23.508 -26.533 20.592 1.00 13.16 ? 120 VAL   C CG1 1 
ATOM   1990 C  CG2 . VAL   B 1 114 ? 22.170 -28.667 20.763 1.00 12.74 ? 120 VAL   C CG2 1 
ATOM   1991 N  N   . VAL   B 1 115 ? 26.511 -27.198 22.004 1.00 9.17  ? 121 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 115 ? 27.547 -26.275 22.508 1.00 9.71  ? 121 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 115 ? 27.322 -24.872 21.977 1.00 10.62 ? 121 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 115 ? 27.570 -23.877 22.687 1.00 10.95 ? 121 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 115 ? 28.926 -26.809 22.094 1.00 9.83  ? 121 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 115 ? 30.026 -25.830 22.490 1.00 10.96 ? 121 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 115 ? 29.187 -28.192 22.708 1.00 11.87 ? 121 VAL   C CG2 1 
ATOM   1998 N  N   . GLY   B 1 116 ? 26.943 -24.775 20.718 1.00 10.10 ? 122 GLY   C N   1 
ATOM   1999 C  CA  . GLY   B 1 116 ? 26.758 -23.465 20.073 1.00 10.97 ? 122 GLY   C CA  1 
ATOM   2000 C  C   . GLY   B 1 116 ? 26.399 -23.625 18.611 1.00 10.08 ? 122 GLY   C C   1 
ATOM   2001 O  O   . GLY   B 1 116 ? 26.072 -24.750 18.191 1.00 9.91  ? 122 GLY   C O   1 
ATOM   2002 N  N   . ILE   B 1 117 ? 26.377 -22.505 17.862 1.00 9.84  ? 123 ILE   C N   1 
ATOM   2003 C  CA  . ILE   B 1 117 ? 26.028 -22.542 16.457 1.00 9.57  ? 123 ILE   C CA  1 
ATOM   2004 C  C   . ILE   B 1 117 ? 27.055 -21.821 15.636 1.00 8.94  ? 123 ILE   C C   1 
ATOM   2005 O  O   . ILE   B 1 117 ? 27.713 -20.855 16.095 1.00 10.21 ? 123 ILE   C O   1 
ATOM   2006 C  CB  . ILE   B 1 117 ? 24.633 -21.916 16.185 1.00 10.76 ? 123 ILE   C CB  1 
ATOM   2007 C  CG1 . ILE   B 1 117 ? 24.486 -20.489 16.807 1.00 12.04 ? 123 ILE   C CG1 1 
ATOM   2008 C  CG2 . ILE   B 1 117 ? 23.518 -22.859 16.636 1.00 12.06 ? 123 ILE   C CG2 1 
ATOM   2009 C  CD1 . ILE   B 1 117 ? 23.152 -19.701 16.397 1.00 13.04 ? 123 ILE   C CD1 1 
ATOM   2010 N  N   . VAL   B 1 118 ? 27.211 -22.251 14.372 1.00 9.49  ? 124 VAL   C N   1 
ATOM   2011 C  CA  . VAL   B 1 118 ? 28.147 -21.574 13.457 1.00 9.59  ? 124 VAL   C CA  1 
ATOM   2012 C  C   . VAL   B 1 118 ? 27.805 -20.092 13.325 1.00 9.65  ? 124 VAL   C C   1 
ATOM   2013 O  O   . VAL   B 1 118 ? 26.604 -19.769 13.136 1.00 9.65  ? 124 VAL   C O   1 
ATOM   2014 C  CB  . VAL   B 1 118 ? 28.117 -22.241 12.071 1.00 9.10  ? 124 VAL   C CB  1 
ATOM   2015 C  CG1 . VAL   B 1 118 ? 28.978 -21.450 11.071 1.00 10.56 ? 124 VAL   C CG1 1 
ATOM   2016 C  CG2 . VAL   B 1 118 ? 28.624 -23.683 12.141 1.00 10.36 ? 124 VAL   C CG2 1 
ATOM   2017 N  N   . SER   B 1 119 ? 28.814 -19.197 13.437 1.00 10.11 ? 125 SER   C N   1 
ATOM   2018 C  CA  . SER   B 1 119 ? 28.613 -17.752 13.306 1.00 9.27  ? 125 SER   C CA  1 
ATOM   2019 C  C   . SER   B 1 119 ? 29.621 -17.088 12.375 1.00 11.42 ? 125 SER   C C   1 
ATOM   2020 O  O   . SER   B 1 119 ? 29.271 -16.027 11.820 1.00 12.69 ? 125 SER   C O   1 
ATOM   2021 C  CB  . SER   B 1 119 ? 28.634 -17.161 14.720 1.00 10.31 ? 125 SER   C CB  1 
ATOM   2022 O  OG  . SER   B 1 119 ? 28.557 -15.724 14.664 1.00 11.46 ? 125 SER   C OG  1 
ATOM   2023 N  N   . THR   B 1 120 ? 30.849 -17.653 12.240 1.00 11.37 ? 126 THR   C N   1 
ATOM   2024 C  CA  . THR   B 1 120 ? 31.866 -16.979 11.420 1.00 10.70 ? 126 THR   C CA  1 
ATOM   2025 C  C   . THR   B 1 120 ? 32.590 -18.000 10.539 1.00 11.02 ? 126 THR   C C   1 
ATOM   2026 O  O   . THR   B 1 120 ? 32.543 -19.215 10.791 1.00 10.63 ? 126 THR   C O   1 
ATOM   2027 C  CB  . THR   B 1 120 ? 32.920 -16.192 12.296 1.00 10.88 ? 126 THR   C CB  1 
ATOM   2028 O  OG1 . THR   B 1 120 ? 33.784 -17.142 12.965 1.00 12.51 ? 126 THR   C OG1 1 
ATOM   2029 C  CG2 . THR   B 1 120 ? 32.278 -15.287 13.298 1.00 12.77 ? 126 THR   C CG2 1 
ATOM   2030 N  N   . GLY   B 1 121 ? 33.281 -17.497 9.509  1.00 11.68 ? 127 GLY   C N   1 
ATOM   2031 C  CA  . GLY   B 1 121 ? 34.123 -18.349 8.650  1.00 13.31 ? 127 GLY   C CA  1 
ATOM   2032 C  C   . GLY   B 1 121 ? 35.144 -17.491 7.937  1.00 16.92 ? 127 GLY   C C   1 
ATOM   2033 O  O   . GLY   B 1 121 ? 34.870 -16.346 7.613  1.00 18.45 ? 127 GLY   C O   1 
ATOM   2034 N  N   . GLY   B 1 122 ? 36.258 -18.044 7.587  1.00 20.10 ? 128 GLY   C N   1 
ATOM   2035 C  CA  . GLY   B 1 122 ? 37.329 -17.321 6.901  1.00 21.99 ? 128 GLY   C CA  1 
ATOM   2036 C  C   . GLY   B 1 122 ? 38.659 -17.922 7.244  1.00 22.48 ? 128 GLY   C C   1 
ATOM   2037 O  O   . GLY   B 1 122 ? 38.854 -18.437 8.336  1.00 22.68 ? 128 GLY   C O   1 
ATOM   2038 N  N   . ASN   B 1 123 ? 39.593 -17.862 6.290  1.00 22.10 ? 129 ASN   C N   1 
ATOM   2039 C  CA  . ASN   B 1 123 ? 40.945 -18.363 6.489  1.00 23.09 ? 129 ASN   C CA  1 
ATOM   2040 C  C   . ASN   B 1 123 ? 41.040 -19.850 6.842  1.00 21.35 ? 129 ASN   C C   1 
ATOM   2041 O  O   . ASN   B 1 123 ? 42.027 -20.244 7.457  1.00 22.63 ? 129 ASN   C O   1 
ATOM   2042 C  CB  . ASN   B 1 123 ? 41.651 -17.526 7.576  1.00 27.08 ? 129 ASN   C CB  1 
ATOM   2043 C  CG  . ASN   B 1 123 ? 42.170 -16.199 7.090  1.00 34.57 ? 129 ASN   C CG  1 
ATOM   2044 O  OD1 . ASN   B 1 123 ? 42.663 -16.075 5.953  1.00 34.65 ? 129 ASN   C OD1 1 
ATOM   2045 N  ND2 . ASN   B 1 123 ? 42.115 -15.192 7.958  1.00 38.20 ? 129 ASN   C ND2 1 
ATOM   2046 N  N   . GLY   B 1 124 ? 40.055 -20.666 6.459  1.00 19.18 ? 130 GLY   C N   1 
ATOM   2047 C  CA  . GLY   B 1 124 ? 40.079 -22.086 6.806  1.00 17.46 ? 130 GLY   C CA  1 
ATOM   2048 C  C   . GLY   B 1 124 ? 39.671 -22.343 8.246  1.00 16.04 ? 130 GLY   C C   1 
ATOM   2049 O  O   . GLY   B 1 124 ? 39.905 -23.437 8.759  1.00 15.30 ? 130 GLY   C O   1 
ATOM   2050 N  N   . LEU   B 1 125 ? 39.047 -21.347 8.903  1.00 14.43 ? 131 LEU   C N   1 
ATOM   2051 C  CA  . LEU   B 1 125 ? 38.606 -21.470 10.286 1.00 13.67 ? 131 LEU   C CA  1 
ATOM   2052 C  C   . LEU   B 1 125 ? 37.099 -21.329 10.304 1.00 13.79 ? 131 LEU   C C   1 
ATOM   2053 O  O   . LEU   B 1 125 ? 36.496 -20.683 9.419  1.00 17.37 ? 131 LEU   C O   1 
ATOM   2054 C  CB  . LEU   B 1 125 ? 39.238 -20.369 11.176 1.00 15.61 ? 131 LEU   C CB  1 
ATOM   2055 C  CG  . LEU   B 1 125 ? 40.769 -20.415 11.320 1.00 19.37 ? 131 LEU   C CG  1 
ATOM   2056 C  CD1 . LEU   B 1 125 ? 41.305 -19.108 11.841 1.00 22.16 ? 131 LEU   C CD1 1 
ATOM   2057 C  CD2 . LEU   B 1 125 ? 41.233 -21.552 12.156 1.00 20.52 ? 131 LEU   C CD2 1 
ATOM   2058 N  N   . VAL   B 1 126 ? 36.466 -21.988 11.253 1.00 11.00 ? 132 VAL   C N   1 
ATOM   2059 C  CA  . VAL   B 1 126 ? 35.022 -21.860 11.487 1.00 10.54 ? 132 VAL   C CA  1 
ATOM   2060 C  C   . VAL   B 1 126 ? 34.830 -21.396 12.945 1.00 10.18 ? 132 VAL   C C   1 
ATOM   2061 O  O   . VAL   B 1 126 ? 35.514 -21.895 13.847 1.00 10.42 ? 132 VAL   C O   1 
ATOM   2062 C  CB  . VAL   B 1 126 ? 34.240 -23.198 11.249 1.00 11.73 ? 132 VAL   C CB  1 
ATOM   2063 C  CG1 . VAL   B 1 126 ? 34.880 -24.418 11.940 1.00 13.59 ? 132 VAL   C CG1 1 
ATOM   2064 C  CG2 . VAL   B 1 126 ? 32.749 -23.057 11.617 1.00 11.60 ? 132 VAL   C CG2 1 
ATOM   2065 N  N   . GLY   B 1 127 ? 34.006 -20.377 13.137 1.00 10.41 ? 133 GLY   C N   1 
ATOM   2066 C  CA  . GLY   B 1 127 ? 33.745 -19.881 14.479 1.00 10.19 ? 133 GLY   C CA  1 
ATOM   2067 C  C   . GLY   B 1 127 ? 32.336 -20.202 14.926 1.00 9.87  ? 133 GLY   C C   1 
ATOM   2068 O  O   . GLY   B 1 127 ? 31.383 -20.056 14.155 1.00 10.31 ? 133 GLY   C O   1 
ATOM   2069 N  N   . PHE   B 1 128 ? 32.217 -20.569 16.202 1.00 9.46  ? 134 PHE   C N   1 
ATOM   2070 C  CA  . PHE   B 1 128 ? 30.936 -20.928 16.800 1.00 9.76  ? 134 PHE   C CA  1 
ATOM   2071 C  C   . PHE   B 1 128 ? 30.601 -20.009 17.965 1.00 8.84  ? 134 PHE   C C   1 
ATOM   2072 O  O   . PHE   B 1 128 ? 31.452 -19.740 18.818 1.00 9.49  ? 134 PHE   C O   1 
ATOM   2073 C  CB  . PHE   B 1 128 ? 31.007 -22.377 17.368 1.00 10.19 ? 134 PHE   C CB  1 
ATOM   2074 C  CG  . PHE   B 1 128 ? 31.509 -23.408 16.398 1.00 10.04 ? 134 PHE   C CG  1 
ATOM   2075 C  CD1 . PHE   B 1 128 ? 30.654 -23.999 15.491 1.00 9.79  ? 134 PHE   C CD1 1 
ATOM   2076 C  CD2 . PHE   B 1 128 ? 32.831 -23.800 16.419 1.00 11.14 ? 134 PHE   C CD2 1 
ATOM   2077 C  CE1 . PHE   B 1 128 ? 31.125 -24.964 14.609 1.00 10.47 ? 134 PHE   C CE1 1 
ATOM   2078 C  CE2 . PHE   B 1 128 ? 33.307 -24.753 15.523 1.00 10.89 ? 134 PHE   C CE2 1 
ATOM   2079 C  CZ  . PHE   B 1 128 ? 32.447 -25.338 14.642 1.00 10.80 ? 134 PHE   C CZ  1 
ATOM   2080 N  N   . ALA   B 1 129 ? 29.383 -19.510 17.962 1.00 9.20  ? 135 ALA   C N   1 
ATOM   2081 C  CA  . ALA   B 1 129 ? 28.883 -18.716 19.098 1.00 9.24  ? 135 ALA   C CA  1 
ATOM   2082 C  C   . ALA   B 1 129 ? 28.474 -19.676 20.243 1.00 10.95 ? 135 ALA   C C   1 
ATOM   2083 O  O   . ALA   B 1 129 ? 27.568 -20.483 20.069 1.00 10.24 ? 135 ALA   C O   1 
ATOM   2084 C  CB  . ALA   B 1 129 ? 27.659 -17.888 18.648 1.00 10.49 ? 135 ALA   C CB  1 
ATOM   2085 N  N   . ASP   B 1 130 ? 29.148 -19.588 21.376 1.00 10.11 ? 136 ASP   C N   1 
ATOM   2086 C  CA  . ASP   B 1 130 ? 28.882 -20.455 22.520 1.00 10.08 ? 136 ASP   C CA  1 
ATOM   2087 C  C   . ASP   B 1 130 ? 27.538 -20.114 23.132 1.00 10.23 ? 136 ASP   C C   1 
ATOM   2088 O  O   . ASP   B 1 130 ? 27.172 -18.926 23.216 1.00 10.97 ? 136 ASP   C O   1 
ATOM   2089 C  CB  . ASP   B 1 130 ? 29.998 -20.249 23.583 1.00 11.31 ? 136 ASP   C CB  1 
ATOM   2090 C  CG  . ASP   B 1 130 ? 29.906 -21.192 24.775 1.00 13.58 ? 136 ASP   C CG  1 
ATOM   2091 O  OD1 . ASP   B 1 130 ? 29.779 -22.378 24.570 1.00 12.46 ? 136 ASP   C OD1 1 
ATOM   2092 O  OD2 . ASP   B 1 130 ? 29.803 -20.683 25.937 1.00 15.75 ? 136 ASP   C OD2 1 
ATOM   2093 N  N   . VAL   B 1 131 ? 26.825 -21.148 23.618 1.00 9.61  ? 137 VAL   C N   1 
ATOM   2094 C  CA  . VAL   B 1 131 ? 25.602 -20.916 24.399 1.00 10.07 ? 137 VAL   C CA  1 
ATOM   2095 C  C   . VAL   B 1 131 ? 25.670 -21.587 25.787 1.00 10.74 ? 137 VAL   C C   1 
ATOM   2096 O  O   . VAL   B 1 131 ? 24.679 -21.525 26.550 1.00 10.99 ? 137 VAL   C O   1 
ATOM   2097 C  CB  . VAL   B 1 131 ? 24.329 -21.379 23.680 1.00 11.12 ? 137 VAL   C CB  1 
ATOM   2098 C  CG1 . VAL   B 1 131 ? 24.136 -20.584 22.358 1.00 11.23 ? 137 VAL   C CG1 1 
ATOM   2099 C  CG2 . VAL   B 1 131 ? 24.379 -22.888 23.382 1.00 11.14 ? 137 VAL   C CG2 1 
ATOM   2100 N  N   . ARG   B 1 132 ? 26.819 -22.193 26.154 1.00 10.59 ? 138 ARG   C N   1 
ATOM   2101 C  CA  . ARG   B 1 132 ? 26.874 -22.979 27.396 1.00 10.69 ? 138 ARG   C CA  1 
ATOM   2102 C  C   . ARG   B 1 132 ? 26.795 -22.157 28.682 1.00 11.11 ? 138 ARG   C C   1 
ATOM   2103 O  O   . ARG   B 1 132 ? 26.489 -22.717 29.767 1.00 12.14 ? 138 ARG   C O   1 
ATOM   2104 C  CB  . ARG   B 1 132 ? 28.112 -23.872 27.408 1.00 11.74 ? 138 ARG   C CB  1 
ATOM   2105 C  CG  . ARG   B 1 132 ? 28.104 -24.893 26.273 1.00 9.83  ? 138 ARG   C CG  1 
ATOM   2106 C  CD  . ARG   B 1 132 ? 29.387 -25.700 26.337 1.00 10.79 ? 138 ARG   C CD  1 
ATOM   2107 N  NE  . ARG   B 1 132 ? 30.481 -24.831 25.908 1.00 10.63 ? 138 ARG   C NE  1 
ATOM   2108 C  CZ  . ARG   B 1 132 ? 31.723 -25.233 25.710 1.00 11.57 ? 138 ARG   C CZ  1 
ATOM   2109 N  NH1 . ARG   B 1 132 ? 32.106 -26.462 26.069 1.00 10.28 ? 138 ARG   C NH1 1 
ATOM   2110 N  NH2 . ARG   B 1 132 ? 32.628 -24.396 25.219 1.00 11.88 ? 138 ARG   C NH2 1 
ATOM   2111 N  N   . ASP   B 1 133 ? 27.064 -20.855 28.598 1.00 10.81 ? 139 ASP   C N   1 
ATOM   2112 C  CA  . ASP   B 1 133 ? 26.978 -19.993 29.776 1.00 11.58 ? 139 ASP   C CA  1 
ATOM   2113 C  C   . ASP   B 1 133 ? 25.563 -19.457 29.976 1.00 12.92 ? 139 ASP   C C   1 
ATOM   2114 O  O   . ASP   B 1 133 ? 25.320 -18.837 31.012 1.00 13.70 ? 139 ASP   C O   1 
ATOM   2115 C  CB  . ASP   B 1 133 ? 27.946 -18.794 29.624 1.00 12.79 ? 139 ASP   C CB  1 
ATOM   2116 C  CG  . ASP   B 1 133 ? 27.601 -17.900 28.432 1.00 15.62 ? 139 ASP   C CG  1 
ATOM   2117 O  OD1 . ASP   B 1 133 ? 27.314 -18.444 27.350 1.00 14.22 ? 139 ASP   C OD1 1 
ATOM   2118 O  OD2 . ASP   B 1 133 ? 27.569 -16.641 28.607 1.00 17.23 ? 139 ASP   C OD2 1 
ATOM   2119 N  N   . LEU   B 1 134 ? 24.627 -19.680 29.018 1.00 12.32 ? 140 LEU   C N   1 
ATOM   2120 C  CA  . LEU   B 1 134 ? 23.266 -19.136 29.087 1.00 12.66 ? 140 LEU   C CA  1 
ATOM   2121 C  C   . LEU   B 1 134 ? 22.389 -20.100 29.863 1.00 12.32 ? 140 LEU   C C   1 
ATOM   2122 O  O   . LEU   B 1 134 ? 21.535 -20.818 29.324 1.00 12.25 ? 140 LEU   C O   1 
ATOM   2123 C  CB  . LEU   B 1 134 ? 22.730 -18.875 27.663 1.00 12.02 ? 140 LEU   C CB  1 
ATOM   2124 C  CG  . LEU   B 1 134 ? 23.618 -17.982 26.771 1.00 13.33 ? 140 LEU   C CG  1 
ATOM   2125 C  CD1 . LEU   B 1 134 ? 22.987 -17.816 25.346 1.00 13.92 ? 140 LEU   C CD1 1 
ATOM   2126 C  CD2 . LEU   B 1 134 ? 23.790 -16.593 27.378 1.00 15.17 ? 140 LEU   C CD2 1 
ATOM   2127 N  N   . LEU   B 1 135 ? 22.631 -20.142 31.201 1.00 12.94 ? 141 LEU   C N   1 
ATOM   2128 C  CA  . LEU   B 1 135 ? 21.985 -21.154 32.051 1.00 13.67 ? 141 LEU   C CA  1 
ATOM   2129 C  C   . LEU   B 1 135 ? 20.472 -20.992 32.115 1.00 13.81 ? 141 LEU   C C   1 
ATOM   2130 O  O   . LEU   B 1 135 ? 19.763 -21.994 32.271 1.00 14.60 ? 141 LEU   C O   1 
ATOM   2131 C  CB  . LEU   B 1 135 ? 22.573 -21.160 33.488 1.00 14.09 ? 141 LEU   C CB  1 
ATOM   2132 C  CG  . LEU   B 1 135 ? 23.767 -22.093 33.817 1.00 19.53 ? 141 LEU   C CG  1 
ATOM   2133 C  CD1 . LEU   B 1 135 ? 24.839 -22.141 32.735 1.00 18.34 ? 141 LEU   C CD1 1 
ATOM   2134 C  CD2 . LEU   B 1 135 ? 24.542 -21.583 35.048 1.00 20.65 ? 141 LEU   C CD2 1 
ATOM   2135 N  N   . TRP   B 1 136 ? 19.996 -19.751 31.922 1.00 14.27 ? 142 TRP   C N   1 
ATOM   2136 C  CA  . TRP   B 1 136 ? 18.573 -19.462 31.959 1.00 15.44 ? 142 TRP   C CA  1 
ATOM   2137 C  C   . TRP   B 1 136 ? 17.816 -20.160 30.828 1.00 15.68 ? 142 TRP   C C   1 
ATOM   2138 O  O   . TRP   B 1 136 ? 16.600 -20.270 30.927 1.00 16.86 ? 142 TRP   C O   1 
ATOM   2139 C  CB  . TRP   B 1 136 ? 18.318 -17.945 31.954 1.00 14.97 ? 142 TRP   C CB  1 
ATOM   2140 C  CG  . TRP   B 1 136 ? 19.006 -17.228 30.818 1.00 14.19 ? 142 TRP   C CG  1 
ATOM   2141 C  CD1 . TRP   B 1 136 ? 20.209 -16.586 30.869 1.00 15.68 ? 142 TRP   C CD1 1 
ATOM   2142 C  CD2 . TRP   B 1 136 ? 18.490 -17.021 29.482 1.00 14.72 ? 142 TRP   C CD2 1 
ATOM   2143 N  NE1 . TRP   B 1 136 ? 20.493 -16.014 29.638 1.00 15.74 ? 142 TRP   C NE1 1 
ATOM   2144 C  CE2 . TRP   B 1 136 ? 19.432 -16.238 28.785 1.00 15.08 ? 142 TRP   C CE2 1 
ATOM   2145 C  CE3 . TRP   B 1 136 ? 17.293 -17.368 28.839 1.00 15.57 ? 142 TRP   C CE3 1 
ATOM   2146 C  CZ2 . TRP   B 1 136 ? 19.253 -15.872 27.443 1.00 15.55 ? 142 TRP   C CZ2 1 
ATOM   2147 C  CZ3 . TRP   B 1 136 ? 17.097 -16.958 27.531 1.00 16.70 ? 142 TRP   C CZ3 1 
ATOM   2148 C  CH2 . TRP   B 1 136 ? 18.064 -16.212 26.854 1.00 16.51 ? 142 TRP   C CH2 1 
ATOM   2149 N  N   . LEU   B 1 137 ? 18.483 -20.648 29.763 1.00 14.44 ? 143 LEU   C N   1 
ATOM   2150 C  CA  . LEU   B 1 137 ? 17.768 -21.383 28.713 1.00 15.69 ? 143 LEU   C CA  1 
ATOM   2151 C  C   . LEU   B 1 137 ? 17.158 -22.687 29.277 1.00 17.43 ? 143 LEU   C C   1 
ATOM   2152 O  O   . LEU   B 1 137 ? 16.224 -23.219 28.667 1.00 19.68 ? 143 LEU   C O   1 
ATOM   2153 C  CB  . LEU   B 1 137 ? 18.710 -21.754 27.565 1.00 15.61 ? 143 LEU   C CB  1 
ATOM   2154 C  CG  . LEU   B 1 137 ? 19.163 -20.581 26.693 1.00 14.71 ? 143 LEU   C CG  1 
ATOM   2155 C  CD1 . LEU   B 1 137 ? 20.307 -21.048 25.735 1.00 15.67 ? 143 LEU   C CD1 1 
ATOM   2156 C  CD2 . LEU   B 1 137 ? 18.023 -20.031 25.840 1.00 16.12 ? 143 LEU   C CD2 1 
ATOM   2157 N  N   . ASP   B 1 138 ? 17.672 -23.199 30.424 1.00 17.02 ? 144 ASP   C N   1 
ATOM   2158 C  CA  . ASP   B 1 138 ? 17.201 -24.457 31.024 1.00 18.45 ? 144 ASP   C CA  1 
ATOM   2159 C  C   . ASP   B 1 138 ? 15.978 -24.257 31.917 1.00 22.16 ? 144 ASP   C C   1 
ATOM   2160 O  O   . ASP   B 1 138 ? 15.473 -25.264 32.432 1.00 22.78 ? 144 ASP   C O   1 
ATOM   2161 C  CB  . ASP   B 1 138 ? 18.296 -25.108 31.878 1.00 18.97 ? 144 ASP   C CB  1 
ATOM   2162 C  CG  . ASP   B 1 138 ? 19.541 -25.525 31.109 1.00 18.20 ? 144 ASP   C CG  1 
ATOM   2163 O  OD1 . ASP   B 1 138 ? 19.483 -25.557 29.863 1.00 18.02 ? 144 ASP   C OD1 1 
ATOM   2164 O  OD2 . ASP   B 1 138 ? 20.586 -25.811 31.770 1.00 20.32 ? 144 ASP   C OD2 1 
ATOM   2165 N  N   . GLU   B 1 139 ? 15.502 -23.015 32.110 1.00 23.92 ? 145 GLU   C N   1 
ATOM   2166 C  CA  . GLU   B 1 139 ? 14.374 -22.798 33.006 1.00 28.16 ? 145 GLU   C CA  1 
ATOM   2167 C  C   . GLU   B 1 139 ? 13.245 -22.018 32.341 1.00 32.20 ? 145 GLU   C C   1 
ATOM   2168 O  O   . GLU   B 1 139 ? 13.464 -21.300 31.369 1.00 33.36 ? 145 GLU   C O   1 
ATOM   2169 C  CB  . GLU   B 1 139 ? 14.881 -22.134 34.299 1.00 32.36 ? 145 GLU   C CB  1 
ATOM   2170 C  CG  . GLU   B 1 139 ? 15.653 -20.849 34.078 1.00 40.84 ? 145 GLU   C CG  1 
ATOM   2171 C  CD  . GLU   B 1 139 ? 16.642 -20.462 35.165 1.00 50.66 ? 145 GLU   C CD  1 
ATOM   2172 O  OE1 . GLU   B 1 139 ? 16.910 -19.247 35.320 1.00 50.84 ? 145 GLU   C OE1 1 
ATOM   2173 O  OE2 . GLU   B 1 139 ? 17.153 -21.373 35.857 1.00 54.30 ? 145 GLU   C OE2 1 
ATOM   2174 N  N   . GLU   B 1 140 ? 12.018 -22.199 32.839 1.00 34.41 ? 146 GLU   C N   1 
ATOM   2175 C  CA  . GLU   B 1 140 ? 10.833 -21.525 32.302 1.00 37.13 ? 146 GLU   C CA  1 
ATOM   2176 C  C   . GLU   B 1 140 ? 10.993 -20.005 32.316 1.00 38.49 ? 146 GLU   C C   1 
ATOM   2177 O  O   . GLU   B 1 140 ? 11.628 -19.458 33.225 1.00 39.60 ? 146 GLU   C O   1 
ATOM   2178 C  CB  . GLU   B 1 140 ? 9.593  -21.945 33.118 1.00 41.04 ? 146 GLU   C CB  1 
ATOM   2179 C  CG  . GLU   B 1 140 ? 8.295  -21.323 32.629 1.00 49.65 ? 146 GLU   C CG  1 
ATOM   2180 C  CD  . GLU   B 1 140 ? 7.768  -21.902 31.329 1.00 59.64 ? 146 GLU   C CD  1 
ATOM   2181 O  OE1 . GLU   B 1 140 ? 7.806  -21.188 30.298 1.00 61.98 ? 146 GLU   C OE1 1 
ATOM   2182 O  OE2 . GLU   B 1 140 ? 7.316  -23.071 31.341 1.00 62.37 ? 146 GLU   C OE2 1 
HETATM 2183 N  N1  . A1B5O C 2 .   ? 10.607 15.456  17.116 1.00 14.72 ? 201 A1B5O A N1  1 
HETATM 2184 C  C4  . A1B5O C 2 .   ? 4.387  14.928  25.155 1.00 25.40 ? 201 A1B5O A C4  1 
HETATM 2185 C  C5  . A1B5O C 2 .   ? 5.524  15.388  24.246 1.00 24.79 ? 201 A1B5O A C5  1 
HETATM 2186 C  C6  . A1B5O C 2 .   ? 6.383  14.236  23.758 1.00 22.81 ? 201 A1B5O A C6  1 
HETATM 2187 C  C7  . A1B5O C 2 .   ? 7.558  14.920  21.827 1.00 18.05 ? 201 A1B5O A C7  1 
HETATM 2188 C  C8  . A1B5O C 2 .   ? 9.572  16.285  22.281 1.00 17.56 ? 201 A1B5O A C8  1 
HETATM 2189 C  C10 . A1B5O C 2 .   ? 11.048 16.708  20.292 1.00 16.78 ? 201 A1B5O A C10 1 
HETATM 2190 C  C13 . A1B5O C 2 .   ? 8.677  16.109  20.023 1.00 17.04 ? 201 A1B5O A C13 1 
HETATM 2191 O  O2  . A1B5O C 2 .   ? 9.707  17.445  17.621 1.00 15.81 ? 201 A1B5O A O2  1 
HETATM 2192 C  C12 . A1B5O C 2 .   ? 10.117 16.337  17.970 1.00 15.75 ? 201 A1B5O A C12 1 
HETATM 2193 C  C11 . A1B5O C 2 .   ? 10.073 15.901  19.426 1.00 16.00 ? 201 A1B5O A C11 1 
HETATM 2194 C  C9  . A1B5O C 2 .   ? 10.994 16.230  21.743 1.00 17.80 ? 201 A1B5O A C9  1 
HETATM 2195 N  N   . A1B5O C 2 .   ? 8.639  15.583  21.389 1.00 17.24 ? 201 A1B5O A N   1 
HETATM 2196 O  O1  . A1B5O C 2 .   ? 6.737  14.419  21.105 1.00 17.73 ? 201 A1B5O A O1  1 
HETATM 2197 O  O   . A1B5O C 2 .   ? 7.541  14.858  23.147 1.00 20.25 ? 201 A1B5O A O   1 
HETATM 2198 C  C1  . A1B5O C 2 .   ? 6.887  13.377  24.910 1.00 24.30 ? 201 A1B5O A C1  1 
HETATM 2199 S  S   . A1B5O C 2 .   ? 7.833  11.901  24.395 1.00 24.52 ? 201 A1B5O A S   1 
HETATM 2200 C  C   . A1B5O C 2 .   ? 8.648  12.006  22.713 1.00 26.86 ? 201 A1B5O A C   1 
HETATM 2201 C  C3  . A1B5O C 2 .   ? 4.903  14.074  26.294 1.00 25.53 ? 201 A1B5O A C3  1 
HETATM 2202 C  C2  . A1B5O C 2 .   ? 5.725  12.901  25.774 1.00 25.49 ? 201 A1B5O A C2  1 
HETATM 2203 ZN ZN  . ZN    D 3 .   ? 11.334 -4.280  5.925  1.00 16.77 2 202 ZN    A ZN  1 
HETATM 2204 ZN ZN  . ZN    E 3 .   ? 30.446 -31.254 26.647 1.00 11.70 2 201 ZN    C ZN  1 
HETATM 2205 S  S   . DMS   F 4 .   ? 20.683 -32.220 9.771  1.00 88.30 ? 202 DMS   C S   1 
HETATM 2206 O  O   . DMS   F 4 .   ? 21.363 -32.378 8.449  1.00 88.35 ? 202 DMS   C O   1 
HETATM 2207 C  C1  . DMS   F 4 .   ? 21.732 -32.948 11.044 1.00 88.28 ? 202 DMS   C C1  1 
HETATM 2208 C  C2  . DMS   F 4 .   ? 20.918 -30.515 10.326 1.00 88.27 ? 202 DMS   C C2  1 
HETATM 2209 O  O   . HOH   G 5 .   ? 36.175 -2.547  11.098 1.00 24.62 ? 301 HOH   A O   1 
HETATM 2210 O  O   . HOH   G 5 .   ? 34.701 22.110  20.520 1.00 41.52 ? 302 HOH   A O   1 
HETATM 2211 O  O   . HOH   G 5 .   ? 8.291  25.627  23.147 1.00 29.93 ? 303 HOH   A O   1 
HETATM 2212 O  O   . HOH   G 5 .   ? 7.064  26.339  13.255 1.00 41.20 ? 304 HOH   A O   1 
HETATM 2213 O  O   . HOH   G 5 .   ? 35.196 -3.872  7.847  1.00 20.50 ? 305 HOH   A O   1 
HETATM 2214 O  O   . HOH   G 5 .   ? -0.420 16.068  8.418  1.00 42.08 ? 306 HOH   A O   1 
HETATM 2215 O  O   . HOH   G 5 .   ? 2.977  9.311   8.788  1.00 31.52 ? 307 HOH   A O   1 
HETATM 2216 O  O   . HOH   G 5 .   ? 11.189 8.514   4.179  1.00 18.45 ? 308 HOH   A O   1 
HETATM 2217 O  O   . HOH   G 5 .   ? 6.442  2.440   2.927  1.00 31.13 ? 309 HOH   A O   1 
HETATM 2218 O  O   . HOH   G 5 .   ? 30.331 10.758  15.722 1.00 26.20 ? 310 HOH   A O   1 
HETATM 2219 O  O   . HOH   G 5 .   ? 0.430  -0.991  19.232 1.00 25.58 ? 311 HOH   A O   1 
HETATM 2220 O  O   . HOH   G 5 .   ? 13.977 17.384  4.073  1.00 39.86 ? 312 HOH   A O   1 
HETATM 2221 O  O   . HOH   G 5 .   ? 2.732  -3.165  20.755 1.00 26.84 ? 313 HOH   A O   1 
HETATM 2222 O  O   . HOH   G 5 .   ? 23.279 21.716  7.148  1.00 23.77 ? 314 HOH   A O   1 
HETATM 2223 O  O   . HOH   G 5 .   ? 8.301  6.610   33.866 1.00 16.15 ? 315 HOH   A O   1 
HETATM 2224 O  O   . HOH   G 5 .   ? 4.791  -3.606  28.897 1.00 26.26 ? 316 HOH   A O   1 
HETATM 2225 O  O   . HOH   G 5 .   ? 27.838 8.089   1.788  1.00 35.75 ? 317 HOH   A O   1 
HETATM 2226 O  O   . HOH   G 5 .   ? 16.985 6.209   26.734 1.00 26.30 ? 318 HOH   A O   1 
HETATM 2227 O  O   . HOH   G 5 .   ? 8.776  19.533  19.195 1.00 17.54 ? 319 HOH   A O   1 
HETATM 2228 O  O   . HOH   G 5 .   ? 13.980 11.354  24.633 1.00 18.61 ? 320 HOH   A O   1 
HETATM 2229 O  O   . HOH   G 5 .   ? 8.508  -6.588  9.752  1.00 34.93 ? 321 HOH   A O   1 
HETATM 2230 O  O   . HOH   G 5 .   ? 11.558 17.961  4.857  1.00 27.78 ? 322 HOH   A O   1 
HETATM 2231 O  O   . HOH   G 5 .   ? 28.119 3.056   5.139  1.00 28.50 ? 323 HOH   A O   1 
HETATM 2232 O  O   . HOH   G 5 .   ? 14.901 11.316  0.050  1.00 25.81 ? 324 HOH   A O   1 
HETATM 2233 O  O   . HOH   G 5 .   ? 10.432 4.806   3.283  1.00 22.94 ? 325 HOH   A O   1 
HETATM 2234 O  O   . HOH   G 5 .   ? 31.337 20.083  11.878 1.00 25.25 ? 326 HOH   A O   1 
HETATM 2235 O  O   . HOH   G 5 .   ? 17.390 1.169   28.181 1.00 27.33 ? 327 HOH   A O   1 
HETATM 2236 O  O   . HOH   G 5 .   ? 22.522 0.982   17.416 1.00 15.50 ? 328 HOH   A O   1 
HETATM 2237 O  O   . HOH   G 5 .   ? 7.376  20.717  16.951 1.00 18.81 ? 329 HOH   A O   1 
HETATM 2238 O  O   . HOH   G 5 .   ? -0.168 1.160   15.702 1.00 11.91 ? 330 HOH   A O   1 
HETATM 2239 O  O   . HOH   G 5 .   ? 33.648 14.322  9.851  1.00 35.04 ? 331 HOH   A O   1 
HETATM 2240 O  O   . HOH   G 5 .   ? 18.263 21.904  9.434  1.00 17.60 ? 332 HOH   A O   1 
HETATM 2241 O  O   . HOH   G 5 .   ? 19.134 10.159  19.546 1.00 12.54 ? 333 HOH   A O   1 
HETATM 2242 O  O   . HOH   G 5 .   ? 20.787 -1.105  3.222  1.00 26.88 ? 334 HOH   A O   1 
HETATM 2243 O  O   . HOH   G 5 .   ? 6.730  -6.891  23.727 1.00 25.21 ? 335 HOH   A O   1 
HETATM 2244 O  O   . HOH   G 5 .   ? 0.765  8.318   5.154  1.00 52.90 ? 336 HOH   A O   1 
HETATM 2245 O  O   . HOH   G 5 .   ? 12.051 22.247  11.961 1.00 28.35 ? 337 HOH   A O   1 
HETATM 2246 O  O   . HOH   G 5 .   ? 28.299 10.927  2.867  1.00 47.87 ? 338 HOH   A O   1 
HETATM 2247 O  O   . HOH   G 5 .   ? 29.645 11.875  18.512 1.00 27.77 ? 339 HOH   A O   1 
HETATM 2248 O  O   . HOH   G 5 .   ? 4.409  15.766  20.750 1.00 32.39 ? 340 HOH   A O   1 
HETATM 2249 O  O   . HOH   G 5 .   ? 18.430 17.260  26.247 1.00 40.23 ? 341 HOH   A O   1 
HETATM 2250 O  O   . HOH   G 5 .   ? 21.997 2.403   -0.826 1.00 33.26 ? 342 HOH   A O   1 
HETATM 2251 O  O   . HOH   G 5 .   ? 35.097 11.130  12.526 1.00 44.87 ? 343 HOH   A O   1 
HETATM 2252 O  O   . HOH   G 5 .   ? 24.700 5.271   21.518 1.00 27.25 ? 344 HOH   A O   1 
HETATM 2253 O  O   . HOH   G 5 .   ? 19.791 18.146  23.797 1.00 33.16 ? 345 HOH   A O   1 
HETATM 2254 O  O   . HOH   G 5 .   ? 13.652 13.871  23.797 1.00 17.74 ? 346 HOH   A O   1 
HETATM 2255 O  O   . HOH   G 5 .   ? 21.100 19.915  18.182 1.00 31.69 ? 347 HOH   A O   1 
HETATM 2256 O  O   . HOH   G 5 .   ? 22.508 19.632  19.998 1.00 32.24 ? 348 HOH   A O   1 
HETATM 2257 O  O   . HOH   G 5 .   ? 5.929  17.920  21.110 1.00 25.38 ? 349 HOH   A O   1 
HETATM 2258 O  O   . HOH   G 5 .   ? 22.915 -5.975  12.297 1.00 42.29 ? 350 HOH   A O   1 
HETATM 2259 O  O   . HOH   G 5 .   ? 16.360 4.036   23.561 1.00 19.26 ? 351 HOH   A O   1 
HETATM 2260 O  O   . HOH   G 5 .   ? 13.455 4.143   23.408 1.00 12.53 ? 352 HOH   A O   1 
HETATM 2261 O  O   . HOH   G 5 .   ? 20.940 -4.091  14.201 1.00 15.86 ? 353 HOH   A O   1 
HETATM 2262 O  O   . HOH   G 5 .   ? 20.833 -2.551  16.888 1.00 14.80 ? 354 HOH   A O   1 
HETATM 2263 O  O   . HOH   G 5 .   ? 4.061  0.191   23.912 1.00 17.14 ? 355 HOH   A O   1 
HETATM 2264 O  O   . HOH   G 5 .   ? 9.586  19.202  25.819 1.00 37.57 ? 356 HOH   A O   1 
HETATM 2265 O  O   . HOH   G 5 .   ? 10.006 10.396  31.287 1.00 18.66 ? 357 HOH   A O   1 
HETATM 2266 O  O   . HOH   G 5 .   ? 5.391  19.157  23.633 1.00 30.18 ? 358 HOH   A O   1 
HETATM 2267 O  O   . HOH   G 5 .   ? 11.228 12.524  10.823 1.00 13.79 ? 359 HOH   A O   1 
HETATM 2268 O  O   . HOH   G 5 .   ? 22.863 11.826  22.031 1.00 35.20 ? 360 HOH   A O   1 
HETATM 2269 O  O   . HOH   G 5 .   ? 28.862 3.474   12.813 1.00 16.24 ? 361 HOH   A O   1 
HETATM 2270 O  O   . HOH   G 5 .   ? 26.904 -1.257  9.036  1.00 24.97 ? 362 HOH   A O   1 
HETATM 2271 O  O   . HOH   G 5 .   ? 7.970  -5.370  2.989  1.00 38.94 ? 363 HOH   A O   1 
HETATM 2272 O  O   . HOH   G 5 .   ? 35.125 8.072   9.461  1.00 53.95 ? 364 HOH   A O   1 
HETATM 2273 O  O   . HOH   G 5 .   ? 3.007  7.397   24.134 1.00 19.62 ? 365 HOH   A O   1 
HETATM 2274 O  O   . HOH   G 5 .   ? 15.663 24.022  14.361 1.00 36.02 ? 366 HOH   A O   1 
HETATM 2275 O  O   . HOH   G 5 .   ? 16.177 2.353   30.018 1.00 27.55 ? 367 HOH   A O   1 
HETATM 2276 O  O   . HOH   G 5 .   ? 15.041 -5.100  0.598  1.00 37.09 ? 368 HOH   A O   1 
HETATM 2277 O  O   . HOH   G 5 .   ? 3.972  9.573   27.407 1.00 30.13 ? 369 HOH   A O   1 
HETATM 2278 O  O   . HOH   G 5 .   ? 30.459 3.102   15.015 1.00 20.64 ? 370 HOH   A O   1 
HETATM 2279 O  O   . HOH   G 5 .   ? 29.185 12.105  21.330 1.00 30.12 ? 371 HOH   A O   1 
HETATM 2280 O  O   . HOH   G 5 .   ? 16.365 21.287  19.064 1.00 18.24 ? 372 HOH   A O   1 
HETATM 2281 O  O   . HOH   G 5 .   ? 9.675  4.100   33.433 1.00 11.78 ? 373 HOH   A O   1 
HETATM 2282 O  O   . HOH   G 5 .   ? 21.267 5.096   24.616 1.00 43.25 ? 374 HOH   A O   1 
HETATM 2283 O  O   . HOH   G 5 .   ? 13.165 11.311  9.024  1.00 11.91 ? 375 HOH   A O   1 
HETATM 2284 O  O   . HOH   G 5 .   ? 3.566  11.937  18.523 1.00 37.36 ? 376 HOH   A O   1 
HETATM 2285 O  O   . HOH   G 5 .   ? 14.578 24.361  17.497 1.00 29.80 ? 377 HOH   A O   1 
HETATM 2286 O  O   . HOH   G 5 .   ? 36.262 18.309  14.561 1.00 29.78 ? 378 HOH   A O   1 
HETATM 2287 O  O   . HOH   G 5 .   ? 22.907 -0.560  5.481  1.00 19.81 ? 379 HOH   A O   1 
HETATM 2288 O  O   . HOH   G 5 .   ? 9.109  -8.013  21.206 1.00 25.50 ? 380 HOH   A O   1 
HETATM 2289 O  O   . HOH   G 5 .   ? 33.640 11.243  15.762 1.00 42.80 ? 381 HOH   A O   1 
HETATM 2290 O  O   . HOH   G 5 .   ? 0.765  -0.748  9.064  1.00 28.95 ? 382 HOH   A O   1 
HETATM 2291 O  O   . HOH   G 5 .   ? 17.375 20.028  16.869 1.00 13.96 ? 383 HOH   A O   1 
HETATM 2292 O  O   . HOH   G 5 .   ? 28.921 15.914  4.442  1.00 34.77 ? 384 HOH   A O   1 
HETATM 2293 O  O   . HOH   G 5 .   ? 4.891  8.010   2.155  1.00 29.21 ? 385 HOH   A O   1 
HETATM 2294 O  O   . HOH   G 5 .   ? 29.899 -1.264  8.777  1.00 33.32 ? 386 HOH   A O   1 
HETATM 2295 O  O   . HOH   G 5 .   ? 19.278 3.080   19.372 1.00 21.85 ? 387 HOH   A O   1 
HETATM 2296 O  O   . HOH   G 5 .   ? 16.328 9.450   -1.573 1.00 17.55 ? 388 HOH   A O   1 
HETATM 2297 O  O   . HOH   G 5 .   ? 3.550  -8.278  9.836  1.00 49.84 ? 389 HOH   A O   1 
HETATM 2298 O  O   . HOH   G 5 .   ? 4.048  -4.242  6.069  1.00 26.12 ? 390 HOH   A O   1 
HETATM 2299 O  O   . HOH   G 5 .   ? 13.911 25.251  25.709 1.00 38.74 ? 391 HOH   A O   1 
HETATM 2300 O  O   . HOH   G 5 .   ? 31.953 8.855   7.830  1.00 23.44 ? 392 HOH   A O   1 
HETATM 2301 O  O   . HOH   G 5 .   ? 9.100  2.608   2.587  1.00 28.48 ? 393 HOH   A O   1 
HETATM 2302 O  O   . HOH   G 5 .   ? 27.173 -1.306  16.051 1.00 27.55 ? 394 HOH   A O   1 
HETATM 2303 O  O   . HOH   G 5 .   ? 9.658  22.003  9.861  1.00 35.52 ? 395 HOH   A O   1 
HETATM 2304 O  O   . HOH   G 5 .   ? 36.777 2.523   10.190 1.00 40.87 ? 396 HOH   A O   1 
HETATM 2305 O  O   . HOH   G 5 .   ? 32.698 16.671  9.321  1.00 30.28 ? 397 HOH   A O   1 
HETATM 2306 O  O   . HOH   G 5 .   ? 30.448 4.641   5.936  1.00 21.66 ? 398 HOH   A O   1 
HETATM 2307 O  O   . HOH   G 5 .   ? 14.406 -2.440  17.899 1.00 18.47 ? 399 HOH   A O   1 
HETATM 2308 O  O   . HOH   G 5 .   ? 19.491 20.513  5.701  1.00 48.49 ? 400 HOH   A O   1 
HETATM 2309 O  O   . HOH   G 5 .   ? 0.121  5.626   5.887  1.00 25.40 ? 401 HOH   A O   1 
HETATM 2310 O  O   . HOH   G 5 .   ? 18.051 17.748  4.092  1.00 30.54 ? 402 HOH   A O   1 
HETATM 2311 O  O   . HOH   G 5 .   ? 32.208 2.129   6.148  1.00 36.60 ? 403 HOH   A O   1 
HETATM 2312 O  O   . HOH   G 5 .   ? 3.278  0.416   28.783 1.00 42.73 ? 404 HOH   A O   1 
HETATM 2313 O  O   . HOH   G 5 .   ? 17.387 0.980   20.264 1.00 18.52 ? 405 HOH   A O   1 
HETATM 2314 O  O   . HOH   G 5 .   ? 19.784 13.122  2.100  1.00 34.10 ? 406 HOH   A O   1 
HETATM 2315 O  O   . HOH   G 5 .   ? 36.120 -0.401  12.867 1.00 29.63 ? 407 HOH   A O   1 
HETATM 2316 O  O   . HOH   G 5 .   ? 16.976 -3.533  27.735 1.00 33.86 ? 408 HOH   A O   1 
HETATM 2317 O  O   . HOH   G 5 .   ? 17.242 24.123  16.116 1.00 46.59 ? 409 HOH   A O   1 
HETATM 2318 O  O   . HOH   G 5 .   ? 14.808 14.777  26.203 1.00 33.75 ? 410 HOH   A O   1 
HETATM 2319 O  O   . HOH   G 5 .   ? 33.835 18.777  10.923 1.00 26.24 ? 411 HOH   A O   1 
HETATM 2320 O  O   . HOH   G 5 .   ? 5.603  5.511   32.595 1.00 19.04 ? 412 HOH   A O   1 
HETATM 2321 O  O   . HOH   G 5 .   ? 7.148  13.434  4.516  1.00 20.50 ? 413 HOH   A O   1 
HETATM 2322 O  O   . HOH   G 5 .   ? 27.473 17.749  24.265 1.00 23.55 ? 414 HOH   A O   1 
HETATM 2323 O  O   . HOH   G 5 .   ? 25.100 17.730  4.450  1.00 35.13 ? 415 HOH   A O   1 
HETATM 2324 O  O   . HOH   G 5 .   ? 16.809 -4.125  2.889  1.00 22.87 ? 416 HOH   A O   1 
HETATM 2325 O  O   . HOH   G 5 .   ? 30.302 15.929  23.031 1.00 25.29 ? 417 HOH   A O   1 
HETATM 2326 O  O   . HOH   G 5 .   ? 17.013 10.893  25.952 1.00 22.34 ? 418 HOH   A O   1 
HETATM 2327 O  O   . HOH   G 5 .   ? 2.560  16.517  18.935 1.00 28.23 ? 419 HOH   A O   1 
HETATM 2328 O  O   . HOH   G 5 .   ? 5.347  27.252  18.919 1.00 29.85 ? 420 HOH   A O   1 
HETATM 2329 O  O   . HOH   G 5 .   ? 33.852 5.388   16.802 1.00 29.58 ? 421 HOH   A O   1 
HETATM 2330 O  O   . HOH   G 5 .   ? 14.966 15.036  3.152  1.00 28.82 ? 422 HOH   A O   1 
HETATM 2331 O  O   . HOH   G 5 .   ? 20.800 -4.709  11.476 1.00 26.20 ? 423 HOH   A O   1 
HETATM 2332 O  O   . HOH   G 5 .   ? 24.535 10.789  22.907 1.00 37.48 ? 424 HOH   A O   1 
HETATM 2333 O  O   . HOH   G 5 .   ? 1.143  11.866  27.286 1.00 40.51 ? 425 HOH   A O   1 
HETATM 2334 O  O   . HOH   G 5 .   ? 0.405  -1.352  16.559 1.00 18.79 ? 426 HOH   A O   1 
HETATM 2335 O  O   . HOH   G 5 .   ? 2.010  8.508   26.152 1.00 37.30 ? 427 HOH   A O   1 
HETATM 2336 O  O   . HOH   G 5 .   ? 3.285  -0.470  21.288 1.00 26.43 ? 428 HOH   A O   1 
HETATM 2337 O  O   . HOH   G 5 .   ? 2.031  13.762  4.279  1.00 37.27 ? 429 HOH   A O   1 
HETATM 2338 O  O   . HOH   G 5 .   ? 36.199 16.195  17.161 1.00 42.70 ? 430 HOH   A O   1 
HETATM 2339 O  O   . HOH   G 5 .   ? 20.659 10.090  21.848 1.00 16.40 ? 431 HOH   A O   1 
HETATM 2340 O  O   . HOH   G 5 .   ? 24.293 -3.375  16.409 1.00 39.67 ? 432 HOH   A O   1 
HETATM 2341 O  O   . HOH   G 5 .   ? 2.304  14.613  16.812 1.00 35.96 ? 433 HOH   A O   1 
HETATM 2342 O  O   . HOH   G 5 .   ? 17.532 24.363  10.206 1.00 35.69 ? 434 HOH   A O   1 
HETATM 2343 O  O   . HOH   G 5 .   ? 6.279  23.792  9.762  1.00 33.53 ? 435 HOH   A O   1 
HETATM 2344 O  O   . HOH   G 5 .   ? 22.553 3.553   20.869 1.00 20.63 ? 436 HOH   A O   1 
HETATM 2345 O  O   . HOH   G 5 .   ? 23.227 19.092  6.207  1.00 20.63 ? 437 HOH   A O   1 
HETATM 2346 O  O   . HOH   G 5 .   ? 25.107 19.886  21.671 1.00 32.46 ? 438 HOH   A O   1 
HETATM 2347 O  O   . HOH   G 5 .   ? 19.590 -0.386  33.143 1.00 37.94 ? 439 HOH   A O   1 
HETATM 2348 O  O   . HOH   G 5 .   ? -0.724 15.785  11.363 1.00 27.90 ? 440 HOH   A O   1 
HETATM 2349 O  O   . HOH   G 5 .   ? 15.094 21.782  7.906  1.00 33.43 ? 441 HOH   A O   1 
HETATM 2350 O  O   . HOH   G 5 .   ? 33.986 7.958   16.795 1.00 32.82 ? 442 HOH   A O   1 
HETATM 2351 O  O   . HOH   G 5 .   ? 1.262  4.871   26.573 1.00 28.51 ? 443 HOH   A O   1 
HETATM 2352 O  O   . HOH   G 5 .   ? 30.622 19.687  8.632  1.00 40.53 ? 444 HOH   A O   1 
HETATM 2353 O  O   . HOH   G 5 .   ? 23.120 8.379   21.735 1.00 25.77 ? 445 HOH   A O   1 
HETATM 2354 O  O   . HOH   G 5 .   ? 16.784 -5.680  12.162 1.00 26.31 ? 446 HOH   A O   1 
HETATM 2355 O  O   . HOH   G 5 .   ? 17.215 -2.518  19.711 1.00 19.25 ? 447 HOH   A O   1 
HETATM 2356 O  O   . HOH   G 5 .   ? 19.856 9.204   -0.983 1.00 22.72 ? 448 HOH   A O   1 
HETATM 2357 O  O   . HOH   G 5 .   ? 31.883 7.064   5.574  1.00 32.58 ? 449 HOH   A O   1 
HETATM 2358 O  O   . HOH   G 5 .   ? 25.261 -1.004  16.625 1.00 39.61 ? 450 HOH   A O   1 
HETATM 2359 O  O   . HOH   G 5 .   ? 19.170 -3.197  33.653 1.00 38.31 ? 451 HOH   A O   1 
HETATM 2360 O  O   . HOH   G 5 .   ? 27.960 0.296   5.000  1.00 46.96 ? 452 HOH   A O   1 
HETATM 2361 O  O   . HOH   G 5 .   ? 29.019 19.023  6.100  1.00 50.30 ? 453 HOH   A O   1 
HETATM 2362 O  O   . HOH   G 5 .   ? 18.401 2.378   22.769 1.00 38.92 ? 454 HOH   A O   1 
HETATM 2363 O  O   . HOH   G 5 .   ? 4.978  4.964   -0.900 1.00 54.10 ? 455 HOH   A O   1 
HETATM 2364 O  O   . HOH   G 5 .   ? 29.729 0.905   16.706 1.00 31.80 ? 456 HOH   A O   1 
HETATM 2365 O  O   . HOH   G 5 .   ? 15.033 23.819  28.131 1.00 48.50 ? 457 HOH   A O   1 
HETATM 2366 O  O   . HOH   G 5 .   ? 2.162  -5.683  14.631 1.00 41.61 ? 458 HOH   A O   1 
HETATM 2367 O  O   . HOH   G 5 .   ? 16.971 -4.789  34.244 1.00 30.82 ? 459 HOH   A O   1 
HETATM 2368 O  O   . HOH   G 5 .   ? 11.608 24.348  13.581 1.00 35.78 ? 460 HOH   A O   1 
HETATM 2369 O  O   . HOH   G 5 .   ? 2.553  -0.293  26.272 1.00 39.90 ? 461 HOH   A O   1 
HETATM 2370 O  O   . HOH   G 5 .   ? 18.319 -2.394  23.457 1.00 50.84 ? 462 HOH   A O   1 
HETATM 2371 O  O   . HOH   G 5 .   ? 13.421 25.078  15.229 1.00 37.56 ? 463 HOH   A O   1 
HETATM 2372 O  O   . HOH   G 5 .   ? 30.127 7.149   18.006 1.00 29.69 ? 464 HOH   A O   1 
HETATM 2373 O  O   . HOH   G 5 .   ? 23.811 1.150   19.939 1.00 34.47 ? 465 HOH   A O   1 
HETATM 2374 O  O   . HOH   G 5 .   ? 6.351  -10.811 8.427  1.00 81.93 ? 466 HOH   A O   1 
HETATM 2375 O  O   . HOH   G 5 .   ? 22.014 8.848   -3.031 1.00 44.59 ? 467 HOH   A O   1 
HETATM 2376 O  O   . HOH   G 5 .   ? 39.021 -2.471  10.790 1.00 38.18 ? 468 HOH   A O   1 
HETATM 2377 O  O   . HOH   G 5 .   ? 21.166 -0.958  19.046 1.00 27.15 ? 469 HOH   A O   1 
HETATM 2378 O  O   . HOH   G 5 .   ? 31.149 4.722   17.186 1.00 24.57 ? 470 HOH   A O   1 
HETATM 2379 O  O   . HOH   G 5 .   ? 3.963  -6.798  23.806 1.00 53.68 ? 471 HOH   A O   1 
HETATM 2380 O  O   . HOH   G 5 .   ? 2.472  -5.102  22.596 1.00 41.95 ? 472 HOH   A O   1 
HETATM 2381 O  O   . HOH   G 5 .   ? 2.421  18.474  24.148 1.00 30.00 ? 473 HOH   A O   1 
HETATM 2382 O  O   . HOH   G 5 .   ? 15.971 -6.172  31.831 1.00 53.52 ? 474 HOH   A O   1 
HETATM 2383 O  O   . HOH   H 5 .   ? 31.147 -17.980 -0.028 1.00 33.64 ? 301 HOH   C O   1 
HETATM 2384 O  O   . HOH   H 5 .   ? 32.282 -6.856  20.100 1.00 46.10 ? 302 HOH   C O   1 
HETATM 2385 O  O   . HOH   H 5 .   ? 38.067 -7.400  6.928  1.00 19.74 ? 303 HOH   C O   1 
HETATM 2386 O  O   . HOH   H 5 .   ? 16.463 -15.801 8.562  1.00 54.94 ? 304 HOH   C O   1 
HETATM 2387 O  O   . HOH   H 5 .   ? 14.637 -18.615 31.693 1.00 38.52 ? 305 HOH   C O   1 
HETATM 2388 O  O   . HOH   H 5 .   ? 17.814 -6.016  23.843 1.00 25.14 ? 306 HOH   C O   1 
HETATM 2389 O  O   . HOH   H 5 .   ? 29.241 -26.105 -1.233 1.00 30.54 ? 307 HOH   C O   1 
HETATM 2390 O  O   . HOH   H 5 .   ? 17.530 -33.271 23.965 1.00 29.93 ? 308 HOH   C O   1 
HETATM 2391 O  O   . HOH   H 5 .   ? 18.914 -32.292 19.669 1.00 36.41 ? 309 HOH   C O   1 
HETATM 2392 O  O   . HOH   H 5 .   ? 24.404 -15.959 2.739  1.00 46.31 ? 310 HOH   C O   1 
HETATM 2393 O  O   . HOH   H 5 .   ? 26.458 -5.507  10.022 1.00 25.86 ? 311 HOH   C O   1 
HETATM 2394 O  O   . HOH   H 5 .   ? 7.007  -29.922 21.122 1.00 32.34 ? 312 HOH   C O   1 
HETATM 2395 O  O   . HOH   H 5 .   ? 38.701 -18.862 21.316 1.00 22.40 ? 313 HOH   C O   1 
HETATM 2396 O  O   . HOH   H 5 .   ? 30.611 -18.330 26.732 1.00 16.09 ? 314 HOH   C O   1 
HETATM 2397 O  O   . HOH   H 5 .   ? 3.336  -13.216 19.970 1.00 49.74 ? 315 HOH   C O   1 
HETATM 2398 O  O   . HOH   H 5 .   ? 19.729 -4.257  20.037 1.00 20.81 ? 316 HOH   C O   1 
HETATM 2399 O  O   . HOH   H 5 .   ? 30.796 -33.201 0.871  1.00 35.74 ? 317 HOH   C O   1 
HETATM 2400 O  O   . HOH   H 5 .   ? 35.262 -2.858  14.294 1.00 45.88 ? 318 HOH   C O   1 
HETATM 2401 O  O   . HOH   H 5 .   ? 10.084 -17.572 18.156 1.00 25.82 ? 319 HOH   C O   1 
HETATM 2402 O  O   . HOH   H 5 .   ? 17.738 -27.608 16.442 1.00 16.38 ? 320 HOH   C O   1 
HETATM 2403 O  O   . HOH   H 5 .   ? 24.477 -5.799  15.078 1.00 36.91 ? 321 HOH   C O   1 
HETATM 2404 O  O   . HOH   H 5 .   ? 43.972 -19.518 9.127  1.00 42.20 ? 322 HOH   C O   1 
HETATM 2405 O  O   . HOH   H 5 .   ? 14.585 -28.802 25.415 1.00 36.61 ? 323 HOH   C O   1 
HETATM 2406 O  O   . HOH   H 5 .   ? 14.720 -23.895 12.258 1.00 32.18 ? 324 HOH   C O   1 
HETATM 2407 O  O   . HOH   H 5 .   ? 23.843 -8.127  9.491  1.00 29.40 ? 325 HOH   C O   1 
HETATM 2408 O  O   . HOH   H 5 .   ? 35.972 -26.370 34.133 1.00 31.90 ? 326 HOH   C O   1 
HETATM 2409 O  O   . HOH   H 5 .   ? 21.804 -28.958 4.689  1.00 24.53 ? 327 HOH   C O   1 
HETATM 2410 O  O   . HOH   H 5 .   ? 28.079 -5.343  18.454 1.00 34.39 ? 328 HOH   C O   1 
HETATM 2411 O  O   . HOH   H 5 .   ? 20.607 -18.856 12.673 1.00 13.13 ? 329 HOH   C O   1 
HETATM 2412 O  O   . HOH   H 5 .   ? 22.849 -6.070  20.987 1.00 17.34 ? 330 HOH   C O   1 
HETATM 2413 O  O   . HOH   H 5 .   ? 31.094 -6.157  5.611  1.00 35.99 ? 331 HOH   C O   1 
HETATM 2414 O  O   . HOH   H 5 .   ? 35.955 -17.866 11.552 1.00 24.73 ? 332 HOH   C O   1 
HETATM 2415 O  O   . HOH   H 5 .   ? 35.194 -32.841 3.332  1.00 37.39 ? 333 HOH   C O   1 
HETATM 2416 O  O   . HOH   H 5 .   ? 24.049 -3.487  19.128 1.00 44.52 ? 334 HOH   C O   1 
HETATM 2417 O  O   . HOH   H 5 .   ? 25.897 -36.066 2.816  1.00 39.41 ? 335 HOH   C O   1 
HETATM 2418 O  O   . HOH   H 5 .   ? 24.837 -15.880 7.206  1.00 18.74 ? 336 HOH   C O   1 
HETATM 2419 O  O   . HOH   H 5 .   ? 16.391 -17.340 10.783 1.00 41.93 ? 337 HOH   C O   1 
HETATM 2420 O  O   . HOH   H 5 .   ? 22.566 -7.574  25.238 1.00 42.63 ? 338 HOH   C O   1 
HETATM 2421 O  O   . HOH   H 5 .   ? 9.970  -8.795  23.870 1.00 25.81 ? 339 HOH   C O   1 
HETATM 2422 O  O   . HOH   H 5 .   ? 13.259 -11.164 28.331 1.00 35.87 ? 340 HOH   C O   1 
HETATM 2423 O  O   . HOH   H 5 .   ? 40.318 -27.528 15.081 1.00 12.07 ? 341 HOH   C O   1 
HETATM 2424 O  O   . HOH   H 5 .   ? 10.484 -16.943 12.367 1.00 31.23 ? 342 HOH   C O   1 
HETATM 2425 O  O   . HOH   H 5 .   ? 37.151 -32.184 10.863 1.00 22.82 ? 343 HOH   C O   1 
HETATM 2426 O  O   . HOH   H 5 .   ? 30.967 -21.602 28.249 1.00 15.10 ? 344 HOH   C O   1 
HETATM 2427 O  O   . HOH   H 5 .   ? 25.860 -25.451 8.708  1.00 11.98 ? 345 HOH   C O   1 
HETATM 2428 O  O   . HOH   H 5 .   ? 11.834 -24.307 21.652 1.00 15.31 ? 346 HOH   C O   1 
HETATM 2429 O  O   . HOH   H 5 .   ? 37.127 -18.924 28.030 1.00 24.79 ? 347 HOH   C O   1 
HETATM 2430 O  O   . HOH   H 5 .   ? 38.788 -14.736 13.236 1.00 33.78 ? 348 HOH   C O   1 
HETATM 2431 O  O   . HOH   H 5 .   ? 29.824 -15.353 19.356 1.00 14.11 ? 349 HOH   C O   1 
HETATM 2432 O  O   . HOH   H 5 .   ? 18.582 -8.856  13.712 1.00 29.78 ? 350 HOH   C O   1 
HETATM 2433 O  O   . HOH   H 5 .   ? 25.562 -37.923 24.288 1.00 30.55 ? 351 HOH   C O   1 
HETATM 2434 O  O   . HOH   H 5 .   ? 31.773 -10.538 13.616 1.00 19.30 ? 352 HOH   C O   1 
HETATM 2435 O  O   . HOH   H 5 .   ? 23.390 -33.545 29.007 1.00 25.77 ? 353 HOH   C O   1 
HETATM 2436 O  O   . HOH   H 5 .   ? 39.954 -29.887 11.791 1.00 22.23 ? 354 HOH   C O   1 
HETATM 2437 O  O   . HOH   H 5 .   ? 10.890 -6.584  13.265 1.00 25.71 ? 355 HOH   C O   1 
HETATM 2438 O  O   . HOH   H 5 .   ? 40.053 -25.587 6.999  1.00 31.46 ? 356 HOH   C O   1 
HETATM 2439 O  O   . HOH   H 5 .   ? 13.666 -24.122 29.303 1.00 27.39 ? 357 HOH   C O   1 
HETATM 2440 O  O   . HOH   H 5 .   ? 30.097 -18.483 8.216  1.00 24.40 ? 358 HOH   C O   1 
HETATM 2441 O  O   . HOH   H 5 .   ? 36.862 -10.613 4.640  1.00 39.62 ? 359 HOH   C O   1 
HETATM 2442 O  O   . HOH   H 5 .   ? 10.381 -16.968 14.993 1.00 28.20 ? 360 HOH   C O   1 
HETATM 2443 O  O   . HOH   H 5 .   ? 32.424 -23.794 29.037 1.00 15.40 ? 361 HOH   C O   1 
HETATM 2444 O  O   . HOH   H 5 .   ? 33.743 -33.920 23.864 1.00 39.53 ? 362 HOH   C O   1 
HETATM 2445 O  O   . HOH   H 5 .   ? 20.598 -25.788 13.756 1.00 21.82 ? 363 HOH   C O   1 
HETATM 2446 O  O   . HOH   H 5 .   ? 36.122 -21.447 6.748  1.00 24.75 ? 364 HOH   C O   1 
HETATM 2447 O  O   . HOH   H 5 .   ? 32.493 -17.504 5.435  1.00 41.70 ? 365 HOH   C O   1 
HETATM 2448 O  O   . HOH   H 5 .   ? 29.631 -31.392 32.532 1.00 21.95 ? 366 HOH   C O   1 
HETATM 2449 O  O   . HOH   H 5 .   ? 16.867 -9.566  27.674 1.00 35.30 ? 367 HOH   C O   1 
HETATM 2450 O  O   . HOH   H 5 .   ? 19.042 -27.700 28.084 1.00 15.87 ? 368 HOH   C O   1 
HETATM 2451 O  O   . HOH   H 5 .   ? 5.682  -16.776 22.402 1.00 48.55 ? 369 HOH   C O   1 
HETATM 2452 O  O   . HOH   H 5 .   ? 10.597 -12.046 8.959  1.00 26.58 ? 370 HOH   C O   1 
HETATM 2453 O  O   . HOH   H 5 .   ? 14.649 -18.632 10.408 1.00 38.25 ? 371 HOH   C O   1 
HETATM 2454 O  O   . HOH   H 5 .   ? 34.893 -13.248 8.516  1.00 19.86 ? 372 HOH   C O   1 
HETATM 2455 O  O   . HOH   H 5 .   ? 10.021 -20.142 28.871 1.00 32.18 ? 373 HOH   C O   1 
HETATM 2456 O  O   . HOH   H 5 .   ? 22.777 -8.651  13.915 1.00 13.80 ? 374 HOH   C O   1 
HETATM 2457 O  O   . HOH   H 5 .   ? 35.977 -32.778 24.900 1.00 46.66 ? 375 HOH   C O   1 
HETATM 2458 O  O   . HOH   H 5 .   ? 21.091 -25.064 4.030  1.00 42.46 ? 376 HOH   C O   1 
HETATM 2459 O  O   . HOH   H 5 .   ? 4.249  -10.448 19.498 1.00 31.94 ? 377 HOH   C O   1 
HETATM 2460 O  O   . HOH   H 5 .   ? 28.008 -16.543 21.908 1.00 12.74 ? 378 HOH   C O   1 
HETATM 2461 O  O   . HOH   H 5 .   ? 18.794 -11.693 7.596  1.00 38.50 ? 379 HOH   C O   1 
HETATM 2462 O  O   . HOH   H 5 .   ? 38.127 -26.280 28.241 1.00 30.73 ? 380 HOH   C O   1 
HETATM 2463 O  O   . HOH   H 5 .   ? 32.796 -9.862  11.034 1.00 16.73 ? 381 HOH   C O   1 
HETATM 2464 O  O   . HOH   H 5 .   ? 31.363 -35.428 31.640 1.00 44.74 ? 382 HOH   C O   1 
HETATM 2465 O  O   . HOH   H 5 .   ? 26.809 -35.804 20.811 1.00 25.19 ? 383 HOH   C O   1 
HETATM 2466 O  O   . HOH   H 5 .   ? 43.029 -25.668 23.677 1.00 18.18 ? 384 HOH   C O   1 
HETATM 2467 O  O   . HOH   H 5 .   ? 35.765 -28.538 3.009  1.00 50.94 ? 385 HOH   C O   1 
HETATM 2468 O  O   . HOH   H 5 .   ? 37.590 -20.394 4.985  1.00 32.78 ? 386 HOH   C O   1 
HETATM 2469 O  O   . HOH   H 5 .   ? 29.857 -10.704 27.677 1.00 37.17 ? 387 HOH   C O   1 
HETATM 2470 O  O   . HOH   H 5 .   ? 31.936 -34.559 24.750 1.00 26.59 ? 388 HOH   C O   1 
HETATM 2471 O  O   . HOH   H 5 .   ? 22.574 -14.012 29.746 1.00 32.31 ? 389 HOH   C O   1 
HETATM 2472 O  O   . HOH   H 5 .   ? 37.522 -23.662 4.051  1.00 38.57 ? 390 HOH   C O   1 
HETATM 2473 O  O   . HOH   H 5 .   ? 29.514 -13.269 12.827 1.00 18.11 ? 391 HOH   C O   1 
HETATM 2474 O  O   . HOH   H 5 .   ? 12.813 -29.268 18.823 1.00 32.00 ? 392 HOH   C O   1 
HETATM 2475 O  O   . HOH   H 5 .   ? 37.593 -31.631 25.649 1.00 24.13 ? 393 HOH   C O   1 
HETATM 2476 O  O   . HOH   H 5 .   ? 30.998 -24.071 -1.298 1.00 21.68 ? 394 HOH   C O   1 
HETATM 2477 O  O   . HOH   H 5 .   ? 34.232 -13.620 25.348 1.00 16.90 ? 395 HOH   C O   1 
HETATM 2478 O  O   . HOH   H 5 .   ? 26.577 -12.103 27.266 1.00 24.96 ? 396 HOH   C O   1 
HETATM 2479 O  O   . HOH   H 5 .   ? 6.869  -9.293  22.683 1.00 36.96 ? 397 HOH   C O   1 
HETATM 2480 O  O   . HOH   H 5 .   ? 22.729 -28.311 12.573 1.00 18.63 ? 398 HOH   C O   1 
HETATM 2481 O  O   . HOH   H 5 .   ? 23.033 -25.575 8.811  1.00 18.95 ? 399 HOH   C O   1 
HETATM 2482 O  O   . HOH   H 5 .   ? 9.959  -24.930 19.702 1.00 19.34 ? 400 HOH   C O   1 
HETATM 2483 O  O   . HOH   H 5 .   ? 26.448 -6.255  22.215 1.00 30.62 ? 401 HOH   C O   1 
HETATM 2484 O  O   . HOH   H 5 .   ? 24.062 -17.707 33.393 1.00 30.18 ? 402 HOH   C O   1 
HETATM 2485 O  O   . HOH   H 5 .   ? 22.146 -23.990 6.063  1.00 29.92 ? 403 HOH   C O   1 
HETATM 2486 O  O   . HOH   H 5 .   ? 34.533 -35.271 18.106 1.00 32.39 ? 404 HOH   C O   1 
HETATM 2487 O  O   . HOH   H 5 .   ? 35.447 -24.834 24.582 1.00 15.85 ? 405 HOH   C O   1 
HETATM 2488 O  O   . HOH   H 5 .   ? 28.633 -36.568 7.856  1.00 19.57 ? 406 HOH   C O   1 
HETATM 2489 O  O   . HOH   H 5 .   ? 36.644 -29.455 10.038 1.00 20.00 ? 407 HOH   C O   1 
HETATM 2490 O  O   . HOH   H 5 .   ? 32.838 -30.443 31.619 1.00 17.61 ? 408 HOH   C O   1 
HETATM 2491 O  O   . HOH   H 5 .   ? 11.332 -22.568 28.606 1.00 24.63 ? 409 HOH   C O   1 
HETATM 2492 O  O   . HOH   H 5 .   ? 35.118 -13.851 6.066  1.00 42.28 ? 410 HOH   C O   1 
HETATM 2493 O  O   . HOH   H 5 .   ? 26.207 -31.425 14.850 1.00 19.38 ? 411 HOH   C O   1 
HETATM 2494 O  O   . HOH   H 5 .   ? 41.642 -12.521 17.722 1.00 23.67 ? 412 HOH   C O   1 
HETATM 2495 O  O   . HOH   H 5 .   ? 21.570 -19.033 5.808  1.00 27.73 ? 413 HOH   C O   1 
HETATM 2496 O  O   . HOH   H 5 .   ? 17.528 -24.402 8.680  1.00 47.36 ? 414 HOH   C O   1 
HETATM 2497 O  O   . HOH   H 5 .   ? 31.084 -12.309 10.597 1.00 16.02 ? 415 HOH   C O   1 
HETATM 2498 O  O   . HOH   H 5 .   ? 38.840 -13.229 25.535 1.00 26.09 ? 416 HOH   C O   1 
HETATM 2499 O  O   . HOH   H 5 .   ? 33.384 -20.594 -1.777 1.00 33.85 ? 417 HOH   C O   1 
HETATM 2500 O  O   . HOH   H 5 .   ? 3.938  -12.843 17.200 1.00 38.24 ? 418 HOH   C O   1 
HETATM 2501 O  O   . HOH   H 5 .   ? 9.650  -18.548 26.584 1.00 28.00 ? 419 HOH   C O   1 
HETATM 2502 O  O   . HOH   H 5 .   ? 8.651  -13.529 10.647 1.00 23.92 ? 420 HOH   C O   1 
HETATM 2503 O  O   . HOH   H 5 .   ? 35.196 -4.341  17.601 1.00 29.78 ? 421 HOH   C O   1 
HETATM 2504 O  O   . HOH   H 5 .   ? 25.782 -31.095 30.811 1.00 14.55 ? 422 HOH   C O   1 
HETATM 2505 O  O   . HOH   H 5 .   ? 15.068 -30.252 18.065 1.00 35.54 ? 423 HOH   C O   1 
HETATM 2506 O  O   . HOH   H 5 .   ? 4.919  -28.616 22.704 1.00 37.30 ? 424 HOH   C O   1 
HETATM 2507 O  O   . HOH   H 5 .   ? 39.789 -30.163 14.527 1.00 16.20 ? 425 HOH   C O   1 
HETATM 2508 O  O   . HOH   H 5 .   ? 9.526  -24.788 29.094 1.00 41.64 ? 426 HOH   C O   1 
HETATM 2509 O  O   . HOH   H 5 .   ? 30.115 -16.068 30.097 1.00 35.81 ? 427 HOH   C O   1 
HETATM 2510 O  O   . HOH   H 5 .   ? 38.734 -16.568 3.716  1.00 45.70 ? 428 HOH   C O   1 
HETATM 2511 O  O   . HOH   H 5 .   ? 36.568 -16.196 12.330 1.00 36.03 ? 429 HOH   C O   1 
HETATM 2512 O  O   . HOH   H 5 .   ? 35.534 -28.830 7.656  1.00 18.32 ? 430 HOH   C O   1 
HETATM 2513 O  O   . HOH   H 5 .   ? 6.436  -22.960 18.238 1.00 28.72 ? 431 HOH   C O   1 
HETATM 2514 O  O   . HOH   H 5 .   ? 20.317 -32.239 22.247 1.00 26.92 ? 432 HOH   C O   1 
HETATM 2515 O  O   . HOH   H 5 .   ? 10.689 -21.815 13.571 1.00 53.44 ? 433 HOH   C O   1 
HETATM 2516 O  O   . HOH   H 5 .   ? 39.186 -34.194 13.396 1.00 44.80 ? 434 HOH   C O   1 
HETATM 2517 O  O   . HOH   H 5 .   ? 44.090 -21.063 27.400 1.00 36.08 ? 435 HOH   C O   1 
HETATM 2518 O  O   . HOH   H 5 .   ? 18.587 -8.404  25.439 1.00 20.85 ? 436 HOH   C O   1 
HETATM 2519 O  O   . HOH   H 5 .   ? 16.995 -25.505 12.674 1.00 23.60 ? 437 HOH   C O   1 
HETATM 2520 O  O   . HOH   H 5 .   ? 10.189 -31.152 24.915 1.00 34.78 ? 438 HOH   C O   1 
HETATM 2521 O  O   . HOH   H 5 .   ? 3.772  -8.349  14.727 1.00 27.10 ? 439 HOH   C O   1 
HETATM 2522 O  O   . HOH   H 5 .   ? 32.617 -14.499 9.187  1.00 16.43 ? 440 HOH   C O   1 
HETATM 2523 O  O   . HOH   H 5 .   ? 6.667  -17.147 18.372 1.00 44.43 ? 441 HOH   C O   1 
HETATM 2524 O  O   . HOH   H 5 .   ? 6.352  -20.151 18.061 1.00 33.26 ? 442 HOH   C O   1 
HETATM 2525 O  O   . HOH   H 5 .   ? 18.661 -19.216 10.691 1.00 18.69 ? 443 HOH   C O   1 
HETATM 2526 O  O   . HOH   H 5 .   ? 33.902 -15.728 26.966 1.00 32.29 ? 444 HOH   C O   1 
HETATM 2527 O  O   . HOH   H 5 .   ? 9.978  -16.835 33.134 1.00 52.81 ? 445 HOH   C O   1 
HETATM 2528 O  O   . HOH   H 5 .   ? 16.366 -20.587 11.458 1.00 27.35 ? 446 HOH   C O   1 
HETATM 2529 O  O   . HOH   H 5 .   ? 6.468  -18.742 25.368 1.00 50.54 ? 447 HOH   C O   1 
HETATM 2530 O  O   . HOH   H 5 .   ? 37.378 -14.029 9.877  1.00 31.50 ? 448 HOH   C O   1 
HETATM 2531 O  O   . HOH   H 5 .   ? 31.349 -13.524 4.190  1.00 35.49 ? 449 HOH   C O   1 
HETATM 2532 O  O   . HOH   H 5 .   ? 20.180 -23.666 34.894 1.00 41.92 ? 450 HOH   C O   1 
HETATM 2533 O  O   . HOH   H 5 .   ? 34.615 -23.283 -1.126 1.00 37.61 ? 451 HOH   C O   1 
HETATM 2534 O  O   . HOH   H 5 .   ? 31.348 -15.852 7.072  1.00 31.47 ? 452 HOH   C O   1 
HETATM 2535 O  O   . HOH   H 5 .   ? 22.832 -33.924 5.412  1.00 33.95 ? 453 HOH   C O   1 
HETATM 2536 O  O   . HOH   H 5 .   ? 39.158 -33.931 17.441 1.00 58.71 ? 454 HOH   C O   1 
HETATM 2537 O  O   . HOH   H 5 .   ? 41.611 -31.700 15.666 1.00 30.06 ? 455 HOH   C O   1 
HETATM 2538 O  O   . HOH   H 5 .   ? 21.895 -17.712 33.694 1.00 27.13 ? 456 HOH   C O   1 
HETATM 2539 O  O   . HOH   H 5 .   ? 36.370 -24.717 27.142 1.00 31.78 ? 457 HOH   C O   1 
HETATM 2540 O  O   . HOH   H 5 .   ? 23.163 -31.099 13.363 1.00 35.93 ? 458 HOH   C O   1 
HETATM 2541 O  O   . HOH   H 5 .   ? 20.259 -19.013 35.644 1.00 38.72 ? 459 HOH   C O   1 
HETATM 2542 O  O   . HOH   H 5 .   ? 10.072 -27.313 18.384 1.00 34.32 ? 460 HOH   C O   1 
HETATM 2543 O  O   . HOH   H 5 .   ? 34.053 -31.995 29.418 1.00 25.76 ? 461 HOH   C O   1 
HETATM 2544 O  O   . HOH   H 5 .   ? 8.924  -12.887 25.334 1.00 55.58 ? 462 HOH   C O   1 
HETATM 2545 O  O   . HOH   H 5 .   ? 8.814  -19.199 17.032 1.00 33.61 ? 463 HOH   C O   1 
HETATM 2546 O  O   . HOH   H 5 .   ? 10.018 -17.250 30.483 1.00 64.77 ? 464 HOH   C O   1 
HETATM 2547 O  O   . HOH   H 5 .   ? 21.412 -27.005 10.279 1.00 34.64 ? 465 HOH   C O   1 
HETATM 2548 O  O   . HOH   H 5 .   ? 22.718 -16.874 5.181  1.00 49.13 ? 466 HOH   C O   1 
HETATM 2549 O  O   . HOH   H 5 .   ? 16.320 -27.664 14.147 1.00 35.01 ? 467 HOH   C O   1 
HETATM 2550 O  O   . HOH   H 5 .   ? 41.264 -15.502 13.287 1.00 38.12 ? 468 HOH   C O   1 
HETATM 2551 O  O   . HOH   H 5 .   ? 43.230 -28.595 23.188 1.00 29.42 ? 469 HOH   C O   1 
HETATM 2552 O  O   . HOH   H 5 .   ? 18.509 -26.367 10.292 1.00 43.21 ? 470 HOH   C O   1 
HETATM 2553 O  O   . HOH   H 5 .   ? 37.131 -29.207 5.489  1.00 43.55 ? 471 HOH   C O   1 
HETATM 2554 O  O   . HOH   H 5 .   ? 32.452 -19.480 28.928 1.00 23.54 ? 472 HOH   C O   1 
HETATM 2555 O  O   . HOH   H 5 .   ? 17.942 -18.066 8.390  1.00 34.58 ? 473 HOH   C O   1 
HETATM 2556 O  O   . HOH   H 5 .   ? 27.369 -4.026  8.038  1.00 55.14 ? 474 HOH   C O   1 
HETATM 2557 O  O   . HOH   H 5 .   ? 9.888  -21.490 16.233 1.00 34.87 ? 475 HOH   C O   1 
HETATM 2558 O  O   . HOH   H 5 .   ? 31.899 -32.336 33.053 1.00 29.80 ? 476 HOH   C O   1 
HETATM 2559 O  O   . HOH   H 5 .   ? 17.510 -15.156 34.420 1.00 50.39 ? 477 HOH   C O   1 
HETATM 2560 O  O   . HOH   H 5 .   ? 29.343 -16.277 32.492 1.00 36.24 ? 478 HOH   C O   1 
HETATM 2561 O  O   . HOH   H 5 .   ? 12.356 -12.579 7.674  1.00 40.82 ? 479 HOH   C O   1 
HETATM 2562 O  O   . HOH   H 5 .   ? 16.846 -28.892 28.716 1.00 40.45 ? 480 HOH   C O   1 
HETATM 2563 O  O   . HOH   H 5 .   ? 22.172 -2.932  20.697 1.00 38.49 ? 481 HOH   C O   1 
HETATM 2564 O  O   . HOH   H 5 .   ? 25.503 -33.666 31.366 1.00 25.61 ? 482 HOH   C O   1 
HETATM 2565 O  O   . HOH   H 5 .   ? 22.333 -7.825  11.302 1.00 28.24 ? 483 HOH   C O   1 
HETATM 2566 O  O   . HOH   H 5 .   ? 37.162 -23.546 -1.566 1.00 31.23 ? 484 HOH   C O   1 
HETATM 2567 O  O   . HOH   H 5 .   ? 35.352 -20.435 29.300 1.00 39.33 ? 485 HOH   C O   1 
HETATM 2568 O  O   . HOH   H 5 .   ? 8.928  -23.471 17.504 1.00 30.06 ? 486 HOH   C O   1 
HETATM 2569 O  O   . HOH   H 5 .   ? 37.470 -4.710  6.547  1.00 30.62 ? 487 HOH   C O   1 
HETATM 2570 O  O   . HOH   H 5 .   ? 3.270  -8.725  22.147 1.00 51.02 ? 488 HOH   C O   1 
HETATM 2571 O  O   . HOH   H 5 .   ? 35.066 -23.163 28.990 1.00 28.46 ? 489 HOH   C O   1 
HETATM 2572 O  O   . HOH   H 5 .   ? 20.337 -15.213 34.309 1.00 42.64 ? 490 HOH   C O   1 
HETATM 2573 O  O   . HOH   H 5 .   ? 3.191  -9.505  17.005 1.00 38.09 ? 491 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   ? 0.2191 0.2207 0.2011 0.0045  -0.0232 -0.0133 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2153 0.2175 0.2019 0.0054  -0.0252 -0.0116 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2092 0.2111 0.1991 0.0083  -0.0259 -0.0073 7   SER   A C   
4    O O   . SER   A 1   ? 0.2159 0.2175 0.2038 0.0091  -0.0255 -0.0054 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2614 0.2682 0.2459 0.0021  -0.0282 -0.0112 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3145 0.3249 0.2960 0.0016  -0.0305 -0.0072 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1830 0.1848 0.1779 0.0097  -0.0264 -0.0061 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1649 0.1661 0.1633 0.0120  -0.0262 -0.0029 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1516 0.1512 0.1545 0.0131  -0.0250 -0.0034 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1706 0.1687 0.1738 0.0125  -0.0241 -0.0057 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1365 0.1362 0.1431 0.0145  -0.0246 -0.0012 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1437 0.1425 0.1541 0.0149  -0.0232 -0.0017 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1429 0.1399 0.1552 0.0162  -0.0208 -0.0005 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1640 0.1605 0.1763 0.0171  -0.0206 0.0012  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1567 0.1588 0.1712 0.0144  -0.0248 -0.0012 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1273 0.1230 0.1408 0.0157  -0.0188 -0.0016 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1280 0.1220 0.1434 0.0160  -0.0158 -0.0015 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1352 0.1313 0.1566 0.0166  -0.0153 -0.0010 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1403 0.1381 0.1627 0.0155  -0.0161 -0.0017 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1353 0.1276 0.1475 0.0142  -0.0137 -0.0031 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1483 0.1401 0.1557 0.0135  -0.0145 -0.0033 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1425 0.1328 0.1558 0.0135  -0.0099 -0.0039 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1576 0.1499 0.1627 0.0114  -0.0138 -0.0037 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1331 0.1289 0.1595 0.0182  -0.0134 0.0002  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1432 0.1418 0.1770 0.0190  -0.0123 0.0008  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1405 0.1358 0.1761 0.0186  -0.0069 -0.0012 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1456 0.1382 0.1841 0.0202  -0.0042 -0.0006 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1530 0.1551 0.1931 0.0214  -0.0144 0.0045  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1525 0.1587 0.1900 0.0205  -0.0195 0.0058  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1578 0.1682 0.1973 0.0190  -0.0215 0.0052  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1636 0.1691 0.1959 0.0203  -0.0218 0.0069  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1554 0.1690 0.1917 0.0173  -0.0255 0.0055  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1754 0.1845 0.2043 0.0186  -0.0257 0.0072  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1680 0.1810 0.1988 0.0170  -0.0275 0.0062  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.1875 0.2036 0.2144 0.0144  -0.0308 0.0055  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1502 0.1456 0.1839 0.0162  -0.0051 -0.0035 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1537 0.1466 0.1874 0.0145  0.0003  -0.0062 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1642 0.1602 0.2032 0.0139  0.0021  -0.0069 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1541 0.1528 0.1918 0.0126  -0.0005 -0.0064 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1815 0.1723 0.2062 0.0109  0.0010  -0.0082 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1960 0.1893 0.2168 0.0094  -0.0028 -0.0073 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.1964 0.1855 0.2200 0.0079  0.0066  -0.0115 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1756 0.1710 0.2214 0.0150  0.0070  -0.0080 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1664 0.1654 0.2182 0.0144  0.0093  -0.0088 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1558 0.1604 0.2128 0.0161  0.0042  -0.0056 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1604 0.1666 0.2209 0.0190  0.0008  -0.0025 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1565 0.1641 0.2124 0.0135  0.0034  -0.0062 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1568 0.1693 0.2161 0.0139  -0.0014 -0.0039 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1462 0.1571 0.1970 0.0118  -0.0055 -0.0039 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1536 0.1671 0.2050 0.0102  -0.0077 -0.0036 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1676 0.1849 0.2341 0.0128  0.0008  -0.0044 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2156 0.2363 0.2939 0.0161  0.0039  -0.0033 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2470 0.2732 0.3332 0.0184  0.0008  -0.0001 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.1937 0.2111 0.2736 0.0162  0.0102  -0.0059 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1355 0.1423 0.1796 0.0122  -0.0064 -0.0041 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1341 0.1392 0.1715 0.0108  -0.0098 -0.0039 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1340 0.1384 0.1694 0.0128  -0.0129 -0.0028 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1439 0.1471 0.1800 0.0146  -0.0120 -0.0022 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1451 0.1468 0.1757 0.0087  -0.0078 -0.0049 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1557 0.1582 0.1860 0.0057  -0.0048 -0.0058 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1727 0.1770 0.2047 0.0041  -0.0060 -0.0051 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1748 0.1763 0.2028 0.0039  -0.0006 -0.0076 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1888 0.1941 0.2200 0.0010  -0.0032 -0.0055 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.1860 0.1886 0.2122 0.0003  0.0022  -0.0084 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.1922 0.1969 0.2202 -0.0010 0.0008  -0.0071 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2374 0.2436 0.2636 -0.0050 0.0037  -0.0076 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1311 0.1356 0.1637 0.0120  -0.0162 -0.0027 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1318 0.1356 0.1610 0.0129  -0.0187 -0.0023 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1350 0.1352 0.1587 0.0118  -0.0188 -0.0034 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1369 0.1366 0.1608 0.0103  -0.0192 -0.0039 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1397 0.1474 0.1712 0.0123  -0.0220 -0.0018 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1484 0.1554 0.1749 0.0117  -0.0244 -0.0024 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1563 0.1685 0.1845 0.0101  -0.0276 -0.0020 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1675 0.1782 0.1907 0.0077  -0.0288 -0.0045 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2050 0.2158 0.2234 0.0071  -0.0301 -0.0049 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2088 0.2211 0.2266 0.0090  -0.0308 -0.0023 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.1961 0.2052 0.2104 0.0046  -0.0301 -0.0082 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1265 0.1246 0.1465 0.0125  -0.0183 -0.0034 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1167 0.1126 0.1330 0.0119  -0.0184 -0.0036 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1334 0.1288 0.1475 0.0126  -0.0200 -0.0043 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1437 0.1394 0.1562 0.0135  -0.0203 -0.0040 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1316 0.1265 0.1450 0.0116  -0.0165 -0.0033 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1472 0.1414 0.1584 0.0109  -0.0171 -0.0025 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1354 0.1308 0.1498 0.0102  -0.0141 -0.0034 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1184 0.1125 0.1324 0.0120  -0.0206 -0.0052 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1243 0.1177 0.1361 0.0121  -0.0213 -0.0068 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1368 0.1277 0.1489 0.0125  -0.0201 -0.0072 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1453 0.1351 0.1596 0.0125  -0.0195 -0.0057 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1414 0.1361 0.1539 0.0105  -0.0227 -0.0084 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.1735 0.1721 0.1867 0.0105  -0.0243 -0.0071 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1596 0.1531 0.1753 0.0090  -0.0222 -0.0091 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1395 0.1295 0.1498 0.0127  -0.0197 -0.0090 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1437 0.1312 0.1562 0.0134  -0.0180 -0.0096 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1535 0.1383 0.1687 0.0122  -0.0175 -0.0110 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1515 0.1366 0.1651 0.0102  -0.0181 -0.0135 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1452 0.1323 0.1554 0.0135  -0.0169 -0.0121 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1429 0.1324 0.1503 0.0144  -0.0172 -0.0108 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1685 0.1598 0.1723 0.0136  -0.0184 -0.0109 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1515 0.1415 0.1612 0.0158  -0.0162 -0.0092 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1329 0.1153 0.1523 0.0130  -0.0164 -0.0091 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1398 0.1186 0.1623 0.0116  -0.0154 -0.0103 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1618 0.1376 0.1835 0.0104  -0.0136 -0.0152 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1648 0.1393 0.1860 0.0077  -0.0136 -0.0178 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1386 0.1149 0.1662 0.0131  -0.0144 -0.0066 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1538 0.1257 0.1850 0.0115  -0.0132 -0.0070 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1555 0.1248 0.1925 0.0134  -0.0121 -0.0023 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1822 0.1470 0.2229 0.0119  -0.0110 -0.0015 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2185 0.1768 0.2633 0.0115  -0.0081 -0.0042 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2366 0.1926 0.2813 0.0122  -0.0058 -0.0088 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2356 0.1893 0.2841 0.0101  -0.0069 -0.0027 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1662 0.1414 0.1874 0.0117  -0.0119 -0.0167 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1781 0.1503 0.1984 0.0100  -0.0092 -0.0220 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.1872 0.1626 0.2007 0.0064  -0.0110 -0.0253 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.1923 0.1656 0.2034 0.0035  -0.0089 -0.0303 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.1690 0.1397 0.1917 0.0124  -0.0062 -0.0227 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.1637 0.1391 0.1817 0.0129  -0.0072 -0.0226 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.1728 0.1517 0.1915 0.0152  -0.0091 -0.0181 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.1693 0.1458 0.1820 0.0109  -0.0061 -0.0266 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.1770 0.1588 0.1911 0.0148  -0.0092 -0.0192 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.1671 0.1478 0.1775 0.0123  -0.0075 -0.0241 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1758 0.1563 0.1861 0.0065  -0.0144 -0.0225 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.1738 0.1586 0.1789 0.0035  -0.0169 -0.0238 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.1820 0.1698 0.1886 0.0020  -0.0196 -0.0221 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.1921 0.1848 0.1959 -0.0001 -0.0223 -0.0218 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.1736 0.1623 0.1751 0.0048  -0.0184 -0.0217 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.1999 0.1869 0.1999 0.0058  -0.0157 -0.0233 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2086 0.1992 0.2050 0.0068  -0.0173 -0.0208 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2143 0.1998 0.2107 0.0023  -0.0133 -0.0289 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1732 0.1585 0.1846 0.0029  -0.0190 -0.0206 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1699 0.1583 0.1833 0.0015  -0.0210 -0.0191 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.1891 0.1793 0.2009 -0.0031 -0.0219 -0.0226 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.1994 0.1854 0.2100 -0.0055 -0.0195 -0.0268 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1676 0.1527 0.1857 0.0025  -0.0197 -0.0171 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.1690 0.1656 0.1813 -0.0046 -0.0249 -0.0208 24  THR   A N   
135  C CA  . THR   A 18  ? 0.1809 0.1814 0.1918 -0.0096 -0.0266 -0.0234 24  THR   A CA  
136  C C   . THR   A 18  ? 0.1881 0.1870 0.2034 -0.0117 -0.0258 -0.0241 24  THR   A C   
137  O O   . THR   A 18  ? 0.1774 0.1733 0.1968 -0.0090 -0.0244 -0.0218 24  THR   A O   
138  C CB  . THR   A 18  ? 0.1993 0.2090 0.2101 -0.0100 -0.0308 -0.0199 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2069 0.2191 0.2240 -0.0073 -0.0315 -0.0160 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2210 0.2323 0.2277 -0.0080 -0.0318 -0.0182 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.1913 0.1931 0.2054 -0.0172 -0.0269 -0.0272 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.1814 0.1827 0.1998 -0.0198 -0.0263 -0.0277 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.1820 0.1893 0.2061 -0.0174 -0.0283 -0.0228 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.1808 0.1850 0.2090 -0.0167 -0.0266 -0.0217 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.2060 0.2102 0.2218 -0.0269 -0.0272 -0.0321 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.3256 0.3280 0.3460 -0.0297 -0.0259 -0.0331 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.3867 0.3787 0.4092 -0.0287 -0.0217 -0.0344 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.3557 0.3655 0.3797 -0.0328 -0.0284 -0.0317 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.3959 0.3887 0.4223 -0.0318 -0.0215 -0.0344 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.3797 0.3833 0.4072 -0.0345 -0.0254 -0.0330 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.1691 0.1843 0.1937 -0.0158 -0.0315 -0.0195 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.1781 0.1986 0.2091 -0.0132 -0.0325 -0.0152 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1668 0.1813 0.1991 -0.0086 -0.0296 -0.0134 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1631 0.1785 0.2001 -0.0079 -0.0284 -0.0118 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2072 0.2364 0.2398 -0.0117 -0.0360 -0.0115 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3077 0.3425 0.3486 -0.0093 -0.0363 -0.0077 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3536 0.3939 0.3995 -0.0121 -0.0372 -0.0075 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3323 0.3653 0.3751 -0.0043 -0.0347 -0.0050 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1577 0.1667 0.1858 -0.0059 -0.0283 -0.0138 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1582 0.1624 0.1869 -0.0024 -0.0258 -0.0121 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1453 0.1444 0.1758 -0.0040 -0.0236 -0.0128 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1481 0.1471 0.1811 -0.0031 -0.0223 -0.0106 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1525 0.1523 0.1767 -0.0001 -0.0249 -0.0126 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.1737 0.1772 0.1961 0.0019  -0.0265 -0.0110 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.1648 0.1723 0.1904 0.0034  -0.0272 -0.0084 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.1721 0.1743 0.1902 0.0019  -0.0268 -0.0124 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1516 0.1464 0.1808 -0.0066 -0.0227 -0.0158 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1556 0.1449 0.1872 -0.0081 -0.0204 -0.0160 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1636 0.1567 0.1991 -0.0110 -0.0208 -0.0153 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.1683 0.1583 0.2060 -0.0112 -0.0190 -0.0134 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1571 0.1399 0.1872 -0.0104 -0.0186 -0.0200 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1676 0.1449 0.1963 -0.0072 -0.0167 -0.0201 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.1782 0.1552 0.2033 -0.0066 -0.0166 -0.0227 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1721 0.1442 0.2035 -0.0043 -0.0147 -0.0169 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.1810 0.1530 0.2071 -0.0032 -0.0144 -0.0216 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.1757 0.1450 0.2059 -0.0016 -0.0136 -0.0176 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1956 0.1660 0.2302 -0.0039 -0.0141 -0.0129 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.1933 0.1584 0.2267 0.0015  -0.0118 -0.0144 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2023 0.1686 0.2390 -0.0011 -0.0128 -0.0094 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2087 0.1727 0.2453 0.0018  -0.0118 -0.0099 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1556 0.1559 0.1921 -0.0133 -0.0231 -0.0163 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.1605 0.1662 0.2018 -0.0161 -0.0236 -0.0156 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.1775 0.1877 0.2224 -0.0131 -0.0232 -0.0120 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.1895 0.2033 0.2390 -0.0150 -0.0226 -0.0112 29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.1761 0.1891 0.2178 -0.0199 -0.0266 -0.0175 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1594 0.1690 0.2024 -0.0089 -0.0231 -0.0103 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1539 0.1669 0.2000 -0.0064 -0.0218 -0.0078 30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1536 0.1606 0.1956 -0.0040 -0.0198 -0.0067 30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1523 0.1604 0.1938 -0.0013 -0.0191 -0.0056 30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1742 0.1936 0.2227 -0.0040 -0.0237 -0.0066 30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2087 0.2361 0.2626 -0.0066 -0.0260 -0.0065 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2237 0.2558 0.2838 -0.0073 -0.0249 -0.0055 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2072 0.2368 0.2586 -0.0088 -0.0291 -0.0077 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1525 0.1534 0.1922 -0.0052 -0.0188 -0.0068 31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1458 0.1420 0.1821 -0.0033 -0.0177 -0.0051 31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1530 0.1504 0.1890 -0.0033 -0.0158 -0.0028 31  LEU   A C   
197  O O   . LEU   A 25  ? 0.1756 0.1742 0.2138 -0.0058 -0.0145 -0.0021 31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1478 0.1374 0.1836 -0.0044 -0.0171 -0.0051 31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.1660 0.1515 0.1997 -0.0024 -0.0164 -0.0025 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.1645 0.1502 0.1955 0.0005  -0.0173 -0.0035 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1846 0.1636 0.2202 -0.0032 -0.0152 -0.0017 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1513 0.1485 0.1841 -0.0013 -0.0154 -0.0018 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.1608 0.1589 0.1917 -0.0023 -0.0134 0.0000  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.1730 0.1675 0.2006 -0.0026 -0.0138 0.0029  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.1814 0.1758 0.2081 -0.0050 -0.0128 0.0055  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.1554 0.1560 0.1851 -0.0007 -0.0123 -0.0011 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.1716 0.1727 0.1976 -0.0028 -0.0099 0.0000  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.1642 0.1688 0.1992 0.0000  -0.0117 -0.0027 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.1598 0.1521 0.1860 -0.0002 -0.0152 0.0030  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1608 0.1511 0.1854 0.0002  -0.0157 0.0063  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1599 0.1476 0.1854 0.0030  -0.0167 0.0053  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1660 0.1545 0.1905 0.0044  -0.0172 0.0023  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.1737 0.1674 0.1940 -0.0007 -0.0152 0.0078  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.1823 0.1761 0.2010 -0.0004 -0.0164 0.0116  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2116 0.2059 0.2304 -0.0021 -0.0169 0.0165  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.1825 0.1769 0.2000 0.0018  -0.0173 0.0113  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2360 0.2319 0.2542 -0.0011 -0.0184 0.0196  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2122 0.2082 0.2297 0.0013  -0.0185 0.0162  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.1842 0.1785 0.2008 0.0039  -0.0173 0.0079  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2130 0.2111 0.2297 0.0027  -0.0196 0.0173  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.1920 0.1875 0.2071 0.0051  -0.0181 0.0088  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.1991 0.1966 0.2147 0.0046  -0.0192 0.0132  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1731 0.1575 0.2007 0.0038  -0.0169 0.0079  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1797 0.1616 0.2086 0.0065  -0.0170 0.0068  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1917 0.1729 0.2231 0.0078  -0.0172 0.0116  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1903 0.1709 0.2237 0.0065  -0.0172 0.0159  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1895 0.1673 0.2209 0.0064  -0.0162 0.0030  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.1820 0.1555 0.2172 0.0047  -0.0150 0.0042  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2169 0.1854 0.2570 0.0063  -0.0138 0.0076  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2269 0.1926 0.2701 0.0049  -0.0131 0.0109  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2087 0.1760 0.2503 0.0090  -0.0133 0.0072  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1619 0.1436 0.1940 0.0103  -0.0174 0.0115  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1626 0.1450 0.1987 0.0119  -0.0178 0.0166  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1690 0.1492 0.2083 0.0150  -0.0165 0.0143  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1660 0.1490 0.2021 0.0157  -0.0169 0.0119  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1919 0.1809 0.2240 0.0105  -0.0196 0.0203  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2343 0.2262 0.2705 0.0115  -0.0209 0.0269  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2701 0.2596 0.3127 0.0148  -0.0200 0.0277  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2691 0.2663 0.3022 0.0089  -0.0226 0.0312  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1648 0.1396 0.2106 0.0167  -0.0146 0.0146  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1741 0.1462 0.2237 0.0194  -0.0123 0.0117  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1777 0.1500 0.2271 0.0194  -0.0124 0.0116  36  SER   A CA  
243  C C   . SER   A 30  ? 0.1746 0.1519 0.2269 0.0218  -0.0132 0.0157  36  SER   A C   
244  O O   . SER   A 30  ? 0.1703 0.1486 0.2222 0.0233  -0.0121 0.0124  36  SER   A O   
245  C CB  A SER   A 30  ? 0.1990 0.1635 0.2561 0.0204  -0.0092 0.0114  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2143 0.1787 0.2708 0.0203  -0.0091 0.0106  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2265 0.1884 0.2892 0.0234  -0.0062 0.0095  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2591 0.2229 0.3224 0.0216  -0.0094 0.0179  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1674 0.1489 0.2223 0.0218  -0.0153 0.0230  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1708 0.1588 0.2286 0.0235  -0.0167 0.0273  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1705 0.1639 0.2204 0.0219  -0.0182 0.0243  37  SER   A C   
252  O O   . SER   A 31  ? 0.1768 0.1748 0.2289 0.0232  -0.0185 0.0259  37  SER   A O   
253  C CB  . SER   A 31  ? 0.1865 0.1793 0.2479 0.0229  -0.0193 0.0363  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2473 0.2448 0.3002 0.0187  -0.0220 0.0377  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1478 0.1407 0.1895 0.0191  -0.0187 0.0204  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1423 0.1389 0.1771 0.0176  -0.0195 0.0174  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1397 0.1326 0.1715 0.0183  -0.0179 0.0108  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1371 0.1322 0.1637 0.0173  -0.0182 0.0085  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1506 0.1495 0.1790 0.0140  -0.0208 0.0180  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1554 0.1599 0.1841 0.0120  -0.0228 0.0245  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1518 0.1584 0.1735 0.0076  -0.0233 0.0241  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1533 0.1617 0.1689 0.0060  -0.0227 0.0201  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.1724 0.1842 0.1820 0.0018  -0.0227 0.0200  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.1915 0.2064 0.1995 -0.0015 -0.0235 0.0239  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1525 0.1647 0.1576 0.0006  -0.0215 0.0161  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1344 0.1217 0.1687 0.0191  -0.0161 0.0078  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1298 0.1146 0.1603 0.0186  -0.0151 0.0020  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1408 0.1271 0.1654 0.0164  -0.0166 0.0005  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1375 0.1244 0.1582 0.0160  -0.0167 -0.0025 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1457 0.1316 0.1755 0.0199  -0.0139 -0.0005 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1533 0.1369 0.1789 0.0187  -0.0129 -0.0060 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1569 0.1367 0.1833 0.0177  -0.0119 -0.0087 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1478 0.1338 0.1691 0.0185  -0.0131 -0.0076 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1305 0.1173 0.1550 0.0149  -0.0175 0.0028  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1297 0.1180 0.1502 0.0132  -0.0182 0.0014  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1420 0.1283 0.1638 0.0117  -0.0181 0.0006  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1449 0.1291 0.1701 0.0114  -0.0177 0.0026  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1342 0.1260 0.1521 0.0118  -0.0188 0.0042  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1385 0.1331 0.1536 0.0121  -0.0190 0.0044  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1578 0.1557 0.1697 0.0095  -0.0191 0.0063  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1465 0.1403 0.1590 0.0127  -0.0186 0.0009  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1321 0.1195 0.1520 0.0109  -0.0185 -0.0019 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1358 0.1230 0.1574 0.0091  -0.0186 -0.0026 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1406 0.1313 0.1609 0.0087  -0.0189 -0.0030 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1453 0.1374 0.1638 0.0097  -0.0194 -0.0040 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1320 0.1170 0.1549 0.0084  -0.0185 -0.0057 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1480 0.1333 0.1728 0.0059  -0.0188 -0.0067 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1644 0.1454 0.1910 0.0043  -0.0177 -0.0091 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1343 0.1245 0.1585 0.0052  -0.0203 -0.0079 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1367 0.1287 0.1586 0.0071  -0.0182 -0.0021 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1266 0.1217 0.1491 0.0069  -0.0177 -0.0027 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1332 0.1301 0.1595 0.0055  -0.0179 -0.0035 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1468 0.1425 0.1744 0.0037  -0.0174 -0.0028 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1292 0.1253 0.1500 0.0059  -0.0158 -0.0014 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1504 0.1489 0.1732 0.0058  -0.0140 -0.0025 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1442 0.1395 0.1611 0.0065  -0.0158 -0.0006 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1291 0.1292 0.1576 0.0062  -0.0188 -0.0043 43  SER   A N   
298  C CA  . SER   A 37  ? 0.1271 0.1308 0.1602 0.0047  -0.0193 -0.0047 43  SER   A CA  
299  C C   . SER   A 37  ? 0.1434 0.1512 0.1808 0.0057  -0.0179 -0.0040 43  SER   A C   
300  O O   . SER   A 37  ? 0.1394 0.1465 0.1757 0.0077  -0.0166 -0.0036 43  SER   A O   
301  C CB  . SER   A 37  ? 0.1410 0.1463 0.1742 0.0040  -0.0220 -0.0059 43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1587 0.1658 0.1906 0.0060  -0.0234 -0.0054 43  SER   A OG  
303  N N   . SER   A 38  ? 0.1517 0.1635 0.1944 0.0044  -0.0177 -0.0039 44  SER   A N   
304  C CA  . SER   A 38  ? 0.1575 0.1734 0.2061 0.0057  -0.0157 -0.0032 44  SER   A CA  
305  C C   . SER   A 38  ? 0.1657 0.1869 0.2194 0.0076  -0.0182 -0.0017 44  SER   A C   
306  O O   . SER   A 38  ? 0.1857 0.2092 0.2387 0.0063  -0.0217 -0.0016 44  SER   A O   
307  C CB  . SER   A 38  ? 0.1888 0.2074 0.2417 0.0032  -0.0137 -0.0035 44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2147 0.2365 0.2702 0.0012  -0.0164 -0.0036 44  SER   A OG  
309  N N   . THR   A 39  ? 0.1651 0.1880 0.2237 0.0104  -0.0161 -0.0005 45  THR   A N   
310  C CA  . THR   A 39  ? 0.1806 0.2088 0.2453 0.0127  -0.0185 0.0023  45  THR   A CA  
311  C C   . THR   A 39  ? 0.1945 0.2284 0.2703 0.0141  -0.0162 0.0038  45  THR   A C   
312  O O   . THR   A 39  ? 0.1961 0.2282 0.2740 0.0140  -0.0114 0.0020  45  THR   A O   
313  C CB  . THR   A 39  ? 0.1902 0.2147 0.2522 0.0155  -0.0181 0.0034  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2068 0.2276 0.2707 0.0170  -0.0130 0.0024  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.1972 0.2163 0.2490 0.0144  -0.0197 0.0018  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2040 0.2454 0.2873 0.0153  -0.0194 0.0072  46  THR   A N   
317  C CA  . THR   A 40  ? 0.2218 0.2697 0.3180 0.0174  -0.0172 0.0094  46  THR   A CA  
318  C C   . THR   A 40  ? 0.2292 0.2740 0.3302 0.0219  -0.0136 0.0111  46  THR   A C   
319  O O   . THR   A 40  ? 0.2475 0.2917 0.3557 0.0235  -0.0080 0.0100  46  THR   A O   
320  C CB  . THR   A 40  ? 0.2585 0.3172 0.3618 0.0166  -0.0225 0.0133  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3191 0.3790 0.4195 0.0176  -0.0270 0.0165  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.2701 0.3311 0.3687 0.0114  -0.0252 0.0109  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.2256 0.2677 0.3225 0.0236  -0.0161 0.0133  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.2370 0.2752 0.3386 0.0277  -0.0125 0.0149  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.2284 0.2563 0.3206 0.0269  -0.0080 0.0104  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.2269 0.2512 0.3078 0.0240  -0.0099 0.0078  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.2691 0.3098 0.3713 0.0297  -0.0174 0.0202  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.2196 0.2429 0.3165 0.0293  -0.0022 0.0096  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.2284 0.2428 0.3167 0.0279  0.0022  0.0053  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.2183 0.2284 0.3003 0.0288  -0.0004 0.0070  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.2282 0.2402 0.3161 0.0319  -0.0025 0.0118  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.2671 0.2779 0.3629 0.0294  0.0102  0.0030  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.3431 0.3569 0.4421 0.0271  0.0141  -0.0003 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.4074 0.4173 0.5133 0.0280  0.0230  -0.0036 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.3941 0.4055 0.5133 0.0322  0.0259  -0.0011 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.4435 0.4485 0.5406 0.0238  0.0278  -0.0092 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.1827 0.1877 0.2529 0.0259  -0.0004 0.0038  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.1842 0.1853 0.2476 0.0261  -0.0024 0.0047  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.1718 0.1658 0.2350 0.0267  0.0031  0.0030  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.1807 0.1720 0.2463 0.0258  0.0089  -0.0004 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.1617 0.1524 0.2207 0.0272  0.0016  0.0047  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.1815 0.1648 0.2403 0.0274  0.0068  0.0032  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.1880 0.1670 0.2356 0.0238  0.0075  -0.0003 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.2054 0.1783 0.2520 0.0231  0.0120  -0.0022 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.1885 0.1710 0.2539 0.0312  0.0058  0.0086  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.2479 0.2355 0.3301 0.0360  0.0065  0.0136  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.1625 0.1445 0.2022 0.0215  0.0034  -0.0012 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.1562 0.1355 0.1863 0.0181  0.0037  -0.0039 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.1725 0.1503 0.1996 0.0145  0.0081  -0.0084 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.1916 0.1720 0.2214 0.0140  0.0091  -0.0094 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.1587 0.1419 0.1830 0.0174  -0.0019 -0.0029 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.1817 0.1666 0.2066 0.0196  -0.0060 0.0007  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.1875 0.1694 0.2130 0.0206  -0.0050 0.0024  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.1701 0.1591 0.1940 0.0197  -0.0101 0.0018  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.1790 0.1534 0.2001 0.0114  0.0106  -0.0109 52  THR   A N   
356  C CA  . THR   A 46  ? 0.1990 0.1731 0.2149 0.0065  0.0143  -0.0152 52  THR   A CA  
357  C C   . THR   A 46  ? 0.1951 0.1720 0.2024 0.0034  0.0105  -0.0149 52  THR   A C   
358  O O   . THR   A 46  ? 0.2097 0.1862 0.2148 0.0041  0.0080  -0.0133 52  THR   A O   
359  C CB  . THR   A 46  ? 0.2456 0.2136 0.2616 0.0043  0.0211  -0.0189 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3280 0.2930 0.3406 0.0039  0.0202  -0.0182 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.2453 0.2099 0.2719 0.0081  0.0256  -0.0188 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.1838 0.1643 0.1870 -0.0001 0.0101  -0.0159 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.1718 0.1558 0.1685 -0.0028 0.0064  -0.0147 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.1837 0.1669 0.1738 -0.0082 0.0094  -0.0176 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.1860 0.1678 0.1741 -0.0122 0.0142  -0.0212 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.1698 0.1585 0.1657 -0.0039 0.0039  -0.0131 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.1755 0.1648 0.1778 0.0005  0.0017  -0.0112 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.1727 0.1655 0.1639 -0.0057 -0.0002 -0.0107 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.1872 0.1765 0.1915 0.0045  -0.0025 -0.0087 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.1661 0.1509 0.1527 -0.0092 0.0068  -0.0163 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.1675 0.1532 0.1475 -0.0150 0.0085  -0.0185 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.1834 0.1754 0.1585 -0.0200 0.0072  -0.0180 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.1735 0.1700 0.1498 -0.0184 0.0029  -0.0142 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.1807 0.1683 0.1593 -0.0144 0.0052  -0.0164 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.1900 0.1819 0.1592 -0.0267 0.0112  -0.0219 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.1996 0.1984 0.1627 -0.0328 0.0099  -0.0210 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.2267 0.2282 0.1829 -0.0394 0.0105  -0.0228 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.2371 0.2367 0.1877 -0.0458 0.0156  -0.0280 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.2219 0.2190 0.1835 -0.0358 0.0148  -0.0246 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.2194 0.2139 0.1889 -0.0294 0.0148  -0.0233 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.1897 0.1893 0.1614 -0.0264 0.0086  -0.0174 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.1749 0.1722 0.1536 -0.0213 0.0088  -0.0167 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.2008 0.1999 0.1837 -0.0171 0.0043  -0.0126 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.1907 0.1935 0.1720 -0.0170 -0.0005 -0.0085 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.2179 0.2150 0.2069 -0.0132 0.0047  -0.0125 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.2055 0.2120 0.1620 -0.0384 0.0055  -0.0188 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.2150 0.2241 0.1667 -0.0436 0.0056  -0.0201 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.2208 0.2391 0.1736 -0.0430 -0.0009 -0.0141 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.2288 0.2503 0.1864 -0.0382 -0.0051 -0.0091 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.2143 0.2150 0.1690 -0.0404 0.0089  -0.0231 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2035 0.2033 0.1664 -0.0308 0.0043  -0.0182 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.2465 0.2688 0.1959 -0.0478 -0.0013 -0.0147 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.2625 0.2939 0.2143 -0.0472 -0.0069 -0.0092 57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.2636 0.2925 0.2188 -0.0440 -0.0068 -0.0096 57  ASP   A C   
395  O O   . ASP   A 51  ? 0.2639 0.3006 0.2198 -0.0459 -0.0099 -0.0067 57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.3352 0.3772 0.2802 -0.0567 -0.0087 -0.0080 57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.4728 0.5130 0.4103 -0.0649 -0.0044 -0.0143 57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.5001 0.5297 0.4380 -0.0631 0.0006  -0.0195 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5391 0.5885 0.4701 -0.0737 -0.0059 -0.0138 57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.2427 0.2617 0.2006 -0.0391 -0.0036 -0.0125 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2208 0.2372 0.1813 -0.0363 -0.0035 -0.0125 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2147 0.2376 0.1811 -0.0314 -0.0083 -0.0073 58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2237 0.2474 0.1943 -0.0266 -0.0107 -0.0043 58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2336 0.2389 0.1965 -0.0315 0.0002  -0.0152 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.2358 0.2317 0.1942 -0.0365 0.0074  -0.0218 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.1835 0.2103 0.1507 -0.0325 -0.0092 -0.0064 59  GLN   A N   
407  C CA  A GLN   A 53  ? 0.1740 0.2058 0.1477 -0.0275 -0.0125 -0.0023 59  GLN   A CA  
408  C CA  B GLN   A 53  ? 0.1787 0.2111 0.1522 -0.0279 -0.0126 -0.0023 59  GLN   A CA  
409  C C   . GLN   A 53  ? 0.1712 0.1982 0.1460 -0.0251 -0.0106 -0.0040 59  GLN   A C   
410  O O   . GLN   A 53  ? 0.1848 0.2162 0.1638 -0.0225 -0.0121 -0.0018 59  GLN   A O   
411  C CB  A GLN   A 53  ? 0.1800 0.2243 0.1558 -0.0305 -0.0164 0.0021  59  GLN   A CB  
412  C CB  B GLN   A 53  ? 0.1941 0.2390 0.1690 -0.0319 -0.0159 0.0014  59  GLN   A CB  
413  C CG  A GLN   A 53  ? 0.1694 0.2177 0.1442 -0.0322 -0.0185 0.0047  59  GLN   A CG  
414  C CG  B GLN   A 53  ? 0.2084 0.2613 0.1870 -0.0311 -0.0199 0.0068  59  GLN   A CG  
415  C CD  A GLN   A 53  ? 0.1707 0.2150 0.1507 -0.0252 -0.0195 0.0069  59  GLN   A CD  
416  C CD  B GLN   A 53  ? 0.2161 0.2823 0.1997 -0.0328 -0.0238 0.0122  59  GLN   A CD  
417  O OE1 A GLN   A 53  ? 0.1545 0.1967 0.1326 -0.0256 -0.0195 0.0070  59  GLN   A OE1 
418  O OE1 B GLN   A 53  ? 0.2334 0.3086 0.2138 -0.0394 -0.0259 0.0142  59  GLN   A OE1 
419  N NE2 A GLN   A 53  ? 0.1579 0.2011 0.1444 -0.0190 -0.0202 0.0083  59  GLN   A NE2 
420  N NE2 B GLN   A 53  ? 0.1868 0.2553 0.1786 -0.0271 -0.0247 0.0147  59  GLN   A NE2 
421  N N   . THR   A 54  ? 0.1639 0.1814 0.1350 -0.0258 -0.0068 -0.0078 60  THR   A N   
422  C CA  . THR   A 54  ? 0.1617 0.1732 0.1335 -0.0231 -0.0049 -0.0087 60  THR   A CA  
423  C C   . THR   A 54  ? 0.1685 0.1703 0.1406 -0.0193 -0.0028 -0.0100 60  THR   A C   
424  O O   . THR   A 54  ? 0.1831 0.1816 0.1536 -0.0209 -0.0010 -0.0119 60  THR   A O   
425  C CB  . THR   A 54  ? 0.1974 0.2076 0.1656 -0.0284 -0.0022 -0.0109 60  THR   A CB  
426  O OG1 . THR   A 54  ? 0.2766 0.2808 0.2405 -0.0328 0.0014  -0.0146 60  THR   A OG1 
427  C CG2 . THR   A 54  ? 0.1958 0.2167 0.1643 -0.0326 -0.0044 -0.0095 60  THR   A CG2 
428  N N   . GLY   A 55  ? 0.1409 0.1394 0.1154 -0.0147 -0.0032 -0.0088 61  GLY   A N   
429  C CA  . GLY   A 55  ? 0.1484 0.1396 0.1243 -0.0109 -0.0020 -0.0090 61  GLY   A CA  
430  C C   . GLY   A 55  ? 0.1524 0.1418 0.1297 -0.0071 -0.0029 -0.0072 61  GLY   A C   
431  O O   . GLY   A 55  ? 0.1607 0.1522 0.1369 -0.0083 -0.0029 -0.0067 61  GLY   A O   
432  N N   . VAL   A 56  ? 0.1391 0.1246 0.1186 -0.0032 -0.0033 -0.0062 62  VAL   A N   
433  C CA  . VAL   A 56  ? 0.1376 0.1217 0.1175 -0.0003 -0.0044 -0.0042 62  VAL   A CA  
434  C C   . VAL   A 56  ? 0.1376 0.1234 0.1199 0.0033  -0.0070 -0.0032 62  VAL   A C   
435  O O   . VAL   A 56  ? 0.1534 0.1383 0.1378 0.0044  -0.0071 -0.0036 62  VAL   A O   
436  C CB  . VAL   A 56  ? 0.1705 0.1473 0.1506 -0.0001 -0.0019 -0.0033 62  VAL   A CB  
437  C CG1 . VAL   A 56  ? 0.1996 0.1756 0.1799 0.0026  -0.0035 -0.0002 62  VAL   A CG1 
438  C CG2 . VAL   A 56  ? 0.1834 0.1573 0.1608 -0.0043 0.0013  -0.0046 62  VAL   A CG2 
439  N N   . TYR   A 57  ? 0.1289 0.1178 0.1109 0.0048  -0.0088 -0.0025 63  TYR   A N   
440  C CA  . TYR   A 57  ? 0.1230 0.1131 0.1068 0.0075  -0.0109 -0.0021 63  TYR   A CA  
441  C C   . TYR   A 57  ? 0.1362 0.1254 0.1184 0.0085  -0.0119 -0.0006 63  TYR   A C   
442  O O   . TYR   A 57  ? 0.1466 0.1358 0.1259 0.0072  -0.0112 0.0002  63  TYR   A O   
443  C CB  . TYR   A 57  ? 0.1360 0.1308 0.1214 0.0080  -0.0119 -0.0032 63  TYR   A CB  
444  C CG  . TYR   A 57  ? 0.1283 0.1258 0.1126 0.0079  -0.0117 -0.0038 63  TYR   A CG  
445  C CD1 . TYR   A 57  ? 0.1412 0.1409 0.1245 0.0060  -0.0103 -0.0039 63  TYR   A CD1 
446  C CD2 . TYR   A 57  ? 0.1445 0.1425 0.1287 0.0092  -0.0124 -0.0046 63  TYR   A CD2 
447  C CE1 . TYR   A 57  ? 0.1540 0.1566 0.1369 0.0058  -0.0094 -0.0046 63  TYR   A CE1 
448  C CE2 . TYR   A 57  ? 0.1572 0.1576 0.1404 0.0087  -0.0113 -0.0058 63  TYR   A CE2 
449  C CZ  . TYR   A 57  ? 0.1664 0.1691 0.1491 0.0073  -0.0097 -0.0057 63  TYR   A CZ  
450  O OH  . TYR   A 57  ? 0.1797 0.1851 0.1618 0.0067  -0.0080 -0.0072 63  TYR   A OH  
451  N N   . TYR   A 58  ? 0.1337 0.1232 0.1174 0.0102  -0.0137 0.0000  64  TYR   A N   
452  C CA  . TYR   A 58  ? 0.1343 0.1246 0.1159 0.0104  -0.0154 0.0017  64  TYR   A CA  
453  C C   . TYR   A 58  ? 0.1278 0.1216 0.1074 0.0098  -0.0160 -0.0006 64  TYR   A C   
454  O O   . TYR   A 58  ? 0.1366 0.1315 0.1184 0.0106  -0.0164 -0.0025 64  TYR   A O   
455  C CB  . TYR   A 58  ? 0.1449 0.1348 0.1297 0.0120  -0.0171 0.0038  64  TYR   A CB  
456  C CG  . TYR   A 58  ? 0.1599 0.1518 0.1423 0.0115  -0.0194 0.0065  64  TYR   A CG  
457  C CD1 . TYR   A 58  ? 0.1656 0.1564 0.1457 0.0107  -0.0192 0.0097  64  TYR   A CD1 
458  C CD2 . TYR   A 58  ? 0.1587 0.1542 0.1405 0.0111  -0.0218 0.0058  64  TYR   A CD2 
459  C CE1 . TYR   A 58  ? 0.1759 0.1697 0.1528 0.0095  -0.0217 0.0128  64  TYR   A CE1 
460  C CE2 . TYR   A 58  ? 0.1633 0.1620 0.1417 0.0096  -0.0242 0.0082  64  TYR   A CE2 
461  C CZ  . TYR   A 58  ? 0.1707 0.1689 0.1468 0.0088  -0.0243 0.0121  64  TYR   A CZ  
462  O OH  . TYR   A 58  ? 0.2025 0.2049 0.1746 0.0067  -0.0272 0.0153  64  TYR   A OH  
463  N N   . CYS   A 59  ? 0.1348 0.1297 0.1101 0.0082  -0.0157 -0.0002 65  CYS   A N   
464  C CA  . CYS   A 59  ? 0.1505 0.1483 0.1231 0.0070  -0.0153 -0.0029 65  CYS   A CA  
465  C C   . CYS   A 59  ? 0.1553 0.1547 0.1239 0.0054  -0.0173 -0.0015 65  CYS   A C   
466  O O   . CYS   A 59  ? 0.1625 0.1624 0.1269 0.0037  -0.0176 0.0011  65  CYS   A O   
467  C CB  . CYS   A 59  ? 0.1364 0.1353 0.1071 0.0056  -0.0128 -0.0039 65  CYS   A CB  
468  S SG  . CYS   A 59  ? 0.1654 0.1676 0.1332 0.0039  -0.0109 -0.0079 65  CYS   A SG  
469  N N   . SER   A 60  ? 0.1599 0.1605 0.1293 0.0055  -0.0189 -0.0030 66  SER   A N   
470  C CA  . SER   A 60  ? 0.1678 0.1713 0.1332 0.0032  -0.0214 -0.0015 66  SER   A CA  
471  C C   . SER   A 60  ? 0.1672 0.1733 0.1254 -0.0005 -0.0204 -0.0033 66  SER   A C   
472  O O   . SER   A 60  ? 0.1813 0.1902 0.1347 -0.0030 -0.0226 0.0000  66  SER   A O   
473  C CB  . SER   A 60  ? 0.1997 0.2043 0.1674 0.0033  -0.0230 -0.0033 66  SER   A CB  
474  O OG  . SER   A 60  ? 0.2722 0.2764 0.2395 0.0023  -0.0208 -0.0087 66  SER   A OG  
475  N N   . SER   A 61  ? 0.1535 0.1591 0.1113 -0.0009 -0.0168 -0.0080 67  SER   A N   
476  C CA  . SER   A 61  ? 0.1569 0.1649 0.1082 -0.0046 -0.0145 -0.0107 67  SER   A CA  
477  C C   . SER   A 61  ? 0.1601 0.1687 0.1076 -0.0059 -0.0139 -0.0076 67  SER   A C   
478  O O   . SER   A 61  ? 0.1615 0.1724 0.1028 -0.0094 -0.0122 -0.0091 67  SER   A O   
479  C CB  . SER   A 61  ? 0.1608 0.1680 0.1148 -0.0042 -0.0102 -0.0168 67  SER   A CB  
480  O OG  . SER   A 61  ? 0.1539 0.1598 0.1136 -0.0011 -0.0082 -0.0164 67  SER   A OG  
481  N N   . ARG   A 62  ? 0.1596 0.1658 0.1104 -0.0035 -0.0151 -0.0031 68  ARG   A N   
482  C CA  . ARG   A 62  ? 0.1582 0.1639 0.1059 -0.0048 -0.0147 0.0007  68  ARG   A CA  
483  C C   . ARG   A 62  ? 0.1801 0.1842 0.1288 -0.0038 -0.0179 0.0072  68  ARG   A C   
484  O O   . ARG   A 62  ? 0.1885 0.1912 0.1352 -0.0048 -0.0176 0.0112  68  ARG   A O   
485  C CB  . ARG   A 62  ? 0.1592 0.1629 0.1108 -0.0033 -0.0116 -0.0007 68  ARG   A CB  
486  C CG  . ARG   A 62  ? 0.1633 0.1694 0.1154 -0.0040 -0.0081 -0.0061 68  ARG   A CG  
487  C CD  . ARG   A 62  ? 0.1696 0.1784 0.1151 -0.0078 -0.0060 -0.0067 68  ARG   A CD  
488  N NE  . ARG   A 62  ? 0.2001 0.2114 0.1476 -0.0081 -0.0018 -0.0120 68  ARG   A NE  
489  C CZ  . ARG   A 62  ? 0.1934 0.2061 0.1393 -0.0094 0.0001  -0.0167 68  ARG   A CZ  
490  N NH1 . ARG   A 62  ? 0.1882 0.2008 0.1303 -0.0108 -0.0023 -0.0169 68  ARG   A NH1 
491  N NH2 . ARG   A 62  ? 0.2101 0.2247 0.1593 -0.0093 0.0048  -0.0214 68  ARG   A NH2 
492  N N   . ARG   A 63  ? 0.1887 0.1926 0.1415 -0.0017 -0.0206 0.0085  69  ARG   A N   
493  C CA  . ARG   A 63  ? 0.1899 0.1920 0.1466 0.0003  -0.0229 0.0146  69  ARG   A CA  
494  C C   . ARG   A 63  ? 0.2212 0.2179 0.1813 0.0020  -0.0204 0.0161  69  ARG   A C   
495  O O   . ARG   A 63  ? 0.2372 0.2316 0.1974 0.0020  -0.0206 0.0214  69  ARG   A O   
496  C CB  . ARG   A 63  ? 0.2178 0.2233 0.1702 -0.0020 -0.0261 0.0205  69  ARG   A CB  
497  C CG  . ARG   A 63  ? 0.2184 0.2296 0.1687 -0.0039 -0.0292 0.0198  69  ARG   A CG  
498  C CD  . ARG   A 63  ? 0.2365 0.2518 0.1857 -0.0053 -0.0336 0.0280  69  ARG   A CD  
499  N NE  . ARG   A 63  ? 0.2335 0.2557 0.1789 -0.0086 -0.0368 0.0270  69  ARG   A NE  
500  C CZ  . ARG   A 63  ? 0.2141 0.2413 0.1498 -0.0142 -0.0376 0.0258  69  ARG   A CZ  
501  N NH1 . ARG   A 63  ? 0.2426 0.2691 0.1718 -0.0168 -0.0354 0.0261  69  ARG   A NH1 
502  N NH2 . ARG   A 63  ? 0.2365 0.2698 0.1687 -0.0178 -0.0403 0.0241  69  ARG   A NH2 
503  N N   . LYS   A 64  ? 0.1964 0.1911 0.1589 0.0031  -0.0178 0.0117  70  LYS   A N   
504  C CA  . LYS   A 64  ? 0.1917 0.1821 0.1560 0.0033  -0.0151 0.0120  70  LYS   A CA  
505  C C   . LYS   A 64  ? 0.1805 0.1691 0.1497 0.0051  -0.0137 0.0089  70  LYS   A C   
506  O O   . LYS   A 64  ? 0.1700 0.1612 0.1403 0.0057  -0.0141 0.0054  70  LYS   A O   
507  C CB  . LYS   A 64  ? 0.2448 0.2369 0.2045 0.0005  -0.0128 0.0100  70  LYS   A CB  
508  C CG  . LYS   A 64  ? 0.3962 0.3870 0.3515 -0.0019 -0.0124 0.0143  70  LYS   A CG  
509  C CD  . LYS   A 64  ? 0.5139 0.5047 0.4674 -0.0042 -0.0090 0.0119  70  LYS   A CD  
510  C CE  . LYS   A 64  ? 0.5913 0.5774 0.5439 -0.0058 -0.0074 0.0157  70  LYS   A CE  
511  N NZ  . LYS   A 64  ? 0.6157 0.5959 0.5737 -0.0041 -0.0063 0.0161  70  LYS   A NZ  
512  N N   . HIS   A 65  ? 0.1713 0.1552 0.1432 0.0055  -0.0118 0.0099  71  HIS   A N   
513  C CA  . HIS   A 65  ? 0.1654 0.1479 0.1405 0.0058  -0.0101 0.0068  71  HIS   A CA  
514  C C   . HIS   A 65  ? 0.1937 0.1767 0.1663 0.0030  -0.0078 0.0048  71  HIS   A C   
515  O O   . HIS   A 65  ? 0.2365 0.2169 0.2069 0.0012  -0.0062 0.0065  71  HIS   A O   
516  C CB  . HIS   A 65  ? 0.1558 0.1329 0.1349 0.0070  -0.0087 0.0083  71  HIS   A CB  
517  C CG  . HIS   A 65  ? 0.1659 0.1435 0.1490 0.0098  -0.0108 0.0104  71  HIS   A CG  
518  N ND1 . HIS   A 65  ? 0.2064 0.1846 0.1930 0.0112  -0.0109 0.0081  71  HIS   A ND1 
519  C CD2 . HIS   A 65  ? 0.1608 0.1389 0.1451 0.0112  -0.0129 0.0148  71  HIS   A CD2 
520  C CE1 . HIS   A 65  ? 0.1928 0.1718 0.1832 0.0134  -0.0128 0.0110  71  HIS   A CE1 
521  N NE2 . HIS   A 65  ? 0.2089 0.1882 0.1982 0.0135  -0.0143 0.0152  71  HIS   A NE2 
522  N N   . TYR   A 66  ? 0.1567 0.1436 0.1302 0.0026  -0.0076 0.0017  72  TYR   A N   
523  C CA  . TYR   A 66  ? 0.1640 0.1534 0.1364 -0.0001 -0.0059 0.0001  72  TYR   A CA  
524  C C   . TYR   A 66  ? 0.1560 0.1457 0.1304 -0.0014 -0.0050 -0.0015 72  TYR   A C   
525  O O   . TYR   A 66  ? 0.1488 0.1399 0.1257 0.0001  -0.0062 -0.0024 72  TYR   A O   
526  C CB  . TYR   A 66  ? 0.1741 0.1698 0.1471 0.0005  -0.0065 -0.0015 72  TYR   A CB  
527  C CG  . TYR   A 66  ? 0.1684 0.1652 0.1381 0.0003  -0.0066 -0.0010 72  TYR   A CG  
528  C CD1 . TYR   A 66  ? 0.1841 0.1810 0.1502 -0.0022 -0.0050 -0.0001 72  TYR   A CD1 
529  C CD2 . TYR   A 66  ? 0.1661 0.1638 0.1356 0.0020  -0.0081 -0.0016 72  TYR   A CD2 
530  C CE1 . TYR   A 66  ? 0.2036 0.2023 0.1658 -0.0032 -0.0048 0.0001  72  TYR   A CE1 
531  C CE2 . TYR   A 66  ? 0.1875 0.1869 0.1528 0.0009  -0.0080 -0.0017 72  TYR   A CE2 
532  C CZ  . TYR   A 66  ? 0.1977 0.1976 0.1591 -0.0018 -0.0064 -0.0007 72  TYR   A CZ  
533  O OH  . TYR   A 66  ? 0.2259 0.2279 0.1821 -0.0037 -0.0060 -0.0008 72  TYR   A OH  
534  N N   . PRO   A 67  ? 0.1637 0.1524 0.1366 -0.0049 -0.0028 -0.0021 73  PRO   A N   
535  C CA  . PRO   A 67  ? 0.1624 0.1530 0.1360 -0.0075 -0.0021 -0.0040 73  PRO   A CA  
536  C C   . PRO   A 67  ? 0.1712 0.1704 0.1469 -0.0077 -0.0037 -0.0045 73  PRO   A C   
537  O O   . PRO   A 67  ? 0.2100 0.2131 0.1860 -0.0079 -0.0036 -0.0041 73  PRO   A O   
538  C CB  . PRO   A 67  ? 0.1855 0.1728 0.1565 -0.0119 0.0008  -0.0047 73  PRO   A CB  
539  C CG  . PRO   A 67  ? 0.2184 0.2047 0.1876 -0.0116 0.0013  -0.0028 73  PRO   A CG  
540  C CD  . PRO   A 67  ? 0.1734 0.1594 0.1433 -0.0072 -0.0009 -0.0010 73  PRO   A CD  
541  N N   . VAL   A 68  ? 0.1537 0.1561 0.1314 -0.0079 -0.0050 -0.0049 74  VAL   A N   
542  C CA  . VAL   A 68  ? 0.1678 0.1788 0.1492 -0.0077 -0.0067 -0.0041 74  VAL   A CA  
543  C C   . VAL   A 68  ? 0.1517 0.1669 0.1332 -0.0111 -0.0075 -0.0041 74  VAL   A C   
544  O O   . VAL   A 68  ? 0.1614 0.1728 0.1404 -0.0127 -0.0069 -0.0052 74  VAL   A O   
545  C CB  . VAL   A 68  ? 0.1948 0.2066 0.1799 -0.0030 -0.0085 -0.0034 74  VAL   A CB  
546  C CG1 . VAL   A 68  ? 0.2077 0.2183 0.1926 -0.0006 -0.0079 -0.0037 74  VAL   A CG1 
547  C CG2 . VAL   A 68  ? 0.2028 0.2098 0.1874 -0.0014 -0.0092 -0.0036 74  VAL   A CG2 
548  N N   . SER   A 69  ? 0.1496 0.1738 0.1343 -0.0125 -0.0088 -0.0026 75  SER   A N   
549  C CA  . SER   A 69  ? 0.1505 0.1817 0.1365 -0.0154 -0.0108 -0.0011 75  SER   A CA  
550  C C   . SER   A 69  ? 0.1429 0.1775 0.1349 -0.0107 -0.0131 0.0015  75  SER   A C   
551  O O   . SER   A 69  ? 0.1522 0.1885 0.1491 -0.0068 -0.0130 0.0023  75  SER   A O   
552  C CB  . SER   A 69  ? 0.1943 0.2348 0.1819 -0.0195 -0.0113 0.0000  75  SER   A CB  
553  O OG  . SER   A 69  ? 0.3172 0.3541 0.2991 -0.0245 -0.0088 -0.0027 75  SER   A OG  
554  N N   . PHE   A 70  ? 0.1348 0.1705 0.1268 -0.0112 -0.0148 0.0028  76  PHE   A N   
555  C CA  . PHE   A 70  ? 0.1399 0.1773 0.1377 -0.0067 -0.0167 0.0055  76  PHE   A CA  
556  C C   . PHE   A 70  ? 0.1444 0.1902 0.1444 -0.0093 -0.0195 0.0094  76  PHE   A C   
557  O O   . PHE   A 70  ? 0.1523 0.2005 0.1470 -0.0149 -0.0198 0.0090  76  PHE   A O   
558  C CB  . PHE   A 70  ? 0.1509 0.1793 0.1467 -0.0036 -0.0159 0.0036  76  PHE   A CB  
559  C CG  . PHE   A 70  ? 0.1439 0.1675 0.1339 -0.0067 -0.0149 0.0015  76  PHE   A CG  
560  C CD1 . PHE   A 70  ? 0.1522 0.1693 0.1376 -0.0080 -0.0123 -0.0016 76  PHE   A CD1 
561  C CD2 . PHE   A 70  ? 0.1417 0.1667 0.1313 -0.0079 -0.0161 0.0028  76  PHE   A CD2 
562  C CE1 . PHE   A 70  ? 0.1626 0.1747 0.1441 -0.0104 -0.0105 -0.0037 76  PHE   A CE1 
563  C CE2 . PHE   A 70  ? 0.1493 0.1698 0.1338 -0.0109 -0.0143 0.0003  76  PHE   A CE2 
564  C CZ  . PHE   A 70  ? 0.1597 0.1737 0.1407 -0.0119 -0.0113 -0.0031 76  PHE   A CZ  
565  N N   . SER   A 71  ? 0.1391 0.1893 0.1468 -0.0055 -0.0213 0.0134  77  SER   A N   
566  C CA  . SER   A 71  ? 0.1410 0.2000 0.1522 -0.0074 -0.0245 0.0186  77  SER   A CA  
567  C C   . SER   A 71  ? 0.1412 0.1966 0.1480 -0.0089 -0.0253 0.0190  77  SER   A C   
568  O O   . SER   A 71  ? 0.1496 0.1958 0.1530 -0.0069 -0.0234 0.0154  77  SER   A O   
569  C CB  . SER   A 71  ? 0.1718 0.2358 0.1944 -0.0022 -0.0256 0.0232  77  SER   A CB  
570  O OG  . SER   A 71  ? 0.1694 0.2254 0.1951 0.0032  -0.0242 0.0221  77  SER   A OG  
571  N N   . LYS   A 72  ? 0.1455 0.2088 0.1520 -0.0126 -0.0281 0.0233  78  LYS   A N   
572  C CA  . LYS   A 72  ? 0.1490 0.2102 0.1512 -0.0147 -0.0289 0.0241  78  LYS   A CA  
573  C C   . LYS   A 72  ? 0.1625 0.2198 0.1717 -0.0085 -0.0294 0.0268  78  LYS   A C   
574  O O   . LYS   A 72  ? 0.1663 0.2259 0.1846 -0.0038 -0.0301 0.0300  78  LYS   A O   
575  C CB  . LYS   A 72  ? 0.1722 0.2447 0.1723 -0.0211 -0.0322 0.0289  78  LYS   A CB  
576  C CG  . LYS   A 72  ? 0.2322 0.3066 0.2231 -0.0287 -0.0309 0.0246  78  LYS   A CG  
577  C CD  . LYS   A 72  ? 0.3130 0.3988 0.2997 -0.0366 -0.0341 0.0287  78  LYS   A CD  
578  C CE  . LYS   A 72  ? 0.4045 0.4900 0.3804 -0.0452 -0.0317 0.0228  78  LYS   A CE  
579  N NZ  . LYS   A 72  ? 0.4556 0.5507 0.4249 -0.0539 -0.0342 0.0256  78  LYS   A NZ  
580  N N   . PRO   A 73  ? 0.1664 0.2174 0.1718 -0.0086 -0.0286 0.0252  79  PRO   A N   
581  C CA  . PRO   A 73  ? 0.1643 0.2109 0.1759 -0.0034 -0.0287 0.0273  79  PRO   A CA  
582  C C   . PRO   A 73  ? 0.1679 0.2221 0.1878 -0.0019 -0.0318 0.0352  79  PRO   A C   
583  O O   . PRO   A 73  ? 0.1754 0.2378 0.1934 -0.0065 -0.0346 0.0399  79  PRO   A O   
584  C CB  . PRO   A 73  ? 0.2097 0.2510 0.2149 -0.0057 -0.0276 0.0249  79  PRO   A CB  
585  C CG  . PRO   A 73  ? 0.2541 0.2945 0.2506 -0.0107 -0.0257 0.0199  79  PRO   A CG  
586  C CD  . PRO   A 73  ? 0.1874 0.2352 0.1833 -0.0137 -0.0269 0.0212  79  PRO   A CD  
587  N N   . SER   A 74  ? 0.1517 0.2035 0.1811 0.0041  -0.0311 0.0367  80  SER   A N   
588  C CA  . SER   A 74  ? 0.1606 0.2191 0.2005 0.0065  -0.0333 0.0445  80  SER   A CA  
589  C C   . SER   A 74  ? 0.1423 0.1934 0.1907 0.0127  -0.0313 0.0449  80  SER   A C   
590  O O   . SER   A 74  ? 0.1519 0.1938 0.1977 0.0147  -0.0284 0.0387  80  SER   A O   
591  C CB  . SER   A 74  ? 0.2398 0.3063 0.2854 0.0073  -0.0338 0.0461  80  SER   A CB  
592  O OG  . SER   A 74  ? 0.3753 0.4477 0.4126 0.0012  -0.0349 0.0444  80  SER   A OG  
593  N N   . LEU   A 75  ? 0.1620 0.2178 0.2215 0.0156  -0.0328 0.0525  81  LEU   A N   
594  C CA  . LEU   A 75  ? 0.1769 0.2260 0.2466 0.0215  -0.0304 0.0536  81  LEU   A CA  
595  C C   . LEU   A 75  ? 0.1955 0.2455 0.2738 0.0258  -0.0277 0.0517  81  LEU   A C   
596  O O   . LEU   A 75  ? 0.2033 0.2633 0.2890 0.0263  -0.0294 0.0570  81  LEU   A O   
597  C CB  . LEU   A 75  ? 0.1913 0.2455 0.2690 0.0220  -0.0335 0.0638  81  LEU   A CB  
598  C CG  . LEU   A 75  ? 0.2208 0.2670 0.3086 0.0271  -0.0311 0.0661  81  LEU   A CG  
599  C CD1 . LEU   A 75  ? 0.2269 0.2621 0.3068 0.0259  -0.0290 0.0600  81  LEU   A CD1 
600  C CD2 . LEU   A 75  ? 0.2471 0.2998 0.3435 0.0275  -0.0345 0.0778  81  LEU   A CD2 
601  N N   . ILE   A 76  ? 0.1846 0.2257 0.2614 0.0281  -0.0235 0.0439  82  ILE   A N   
602  C CA  . ILE   A 76  ? 0.2096 0.2507 0.2922 0.0312  -0.0200 0.0402  82  ILE   A CA  
603  C C   . ILE   A 76  ? 0.2257 0.2577 0.3163 0.0360  -0.0153 0.0374  82  ILE   A C   
604  O O   . ILE   A 76  ? 0.2182 0.2413 0.3041 0.0356  -0.0141 0.0336  82  ILE   A O   
605  C CB  . ILE   A 76  ? 0.2432 0.2819 0.3141 0.0282  -0.0189 0.0325  82  ILE   A CB  
606  C CG1 . ILE   A 76  ? 0.2699 0.3164 0.3326 0.0230  -0.0227 0.0345  82  ILE   A CG1 
607  C CG2 . ILE   A 76  ? 0.2676 0.3051 0.3427 0.0310  -0.0147 0.0277  82  ILE   A CG2 
608  C CD1 . ILE   A 76  ? 0.2823 0.3296 0.3384 0.0207  -0.0220 0.0301  82  ILE   A CD1 
609  N N   . PHE   A 77  ? 0.2276 0.2619 0.3305 0.0402  -0.0123 0.0387  83  PHE   A N   
610  C CA  . PHE   A 77  ? 0.2443 0.2695 0.3553 0.0443  -0.0068 0.0351  83  PHE   A CA  
611  C C   . PHE   A 77  ? 0.2552 0.2737 0.3572 0.0429  -0.0029 0.0248  83  PHE   A C   
612  O O   . PHE   A 77  ? 0.2751 0.2978 0.3721 0.0413  -0.0027 0.0216  83  PHE   A O   
613  C CB  . PHE   A 77  ? 0.2583 0.2882 0.3868 0.0495  -0.0040 0.0399  83  PHE   A CB  
614  C CG  . PHE   A 77  ? 0.2913 0.3108 0.4298 0.0537  0.0019  0.0376  83  PHE   A CG  
615  C CD1 . PHE   A 77  ? 0.3235 0.3377 0.4666 0.0550  0.0011  0.0424  83  PHE   A CD1 
616  C CD2 . PHE   A 77  ? 0.3193 0.3338 0.4615 0.0557  0.0087  0.0300  83  PHE   A CD2 
617  C CE1 . PHE   A 77  ? 0.3556 0.3593 0.5080 0.0584  0.0071  0.0398  83  PHE   A CE1 
618  C CE2 . PHE   A 77  ? 0.3271 0.3313 0.4780 0.0589  0.0149  0.0268  83  PHE   A CE2 
619  C CZ  . PHE   A 77  ? 0.3479 0.3465 0.5044 0.0604  0.0141  0.0319  83  PHE   A CZ  
620  N N   . VAL   A 78  ? 0.2280 0.2362 0.3264 0.0426  -0.0005 0.0198  84  VAL   A N   
621  C CA  . VAL   A 78  ? 0.2202 0.2224 0.3097 0.0406  0.0027  0.0105  84  VAL   A CA  
622  C C   . VAL   A 78  ? 0.2338 0.2278 0.3314 0.0433  0.0093  0.0059  84  VAL   A C   
623  O O   . VAL   A 78  ? 0.2239 0.2120 0.3273 0.0447  0.0104  0.0077  84  VAL   A O   
624  C CB  . VAL   A 78  ? 0.2145 0.2127 0.2911 0.0367  -0.0004 0.0079  84  VAL   A CB  
625  C CG1 . VAL   A 78  ? 0.2227 0.2160 0.2903 0.0343  0.0023  -0.0007 84  VAL   A CG1 
626  C CG2 . VAL   A 78  ? 0.2107 0.2162 0.2803 0.0340  -0.0058 0.0120  84  VAL   A CG2 
627  N N   . GLU   A 79  ? 0.2493 0.2431 0.3471 0.0434  0.0138  0.0000  85  GLU   A N   
628  C CA  . GLU   A 79  ? 0.2687 0.2551 0.3737 0.0453  0.0212  -0.0056 85  GLU   A CA  
629  C C   . GLU   A 79  ? 0.2758 0.2522 0.3740 0.0425  0.0228  -0.0114 85  GLU   A C   
630  O O   . GLU   A 79  ? 0.2645 0.2407 0.3498 0.0385  0.0189  -0.0135 85  GLU   A O   
631  C CB  . GLU   A 79  ? 0.2966 0.2852 0.3982 0.0440  0.0253  -0.0122 85  GLU   A CB  
632  C CG  . GLU   A 79  ? 0.3823 0.3647 0.4931 0.0461  0.0341  -0.0181 85  GLU   A CG  
633  C CD  . GLU   A 79  ? 0.4697 0.4527 0.6000 0.0522  0.0372  -0.0122 85  GLU   A CD  
634  O OE1 . GLU   A 79  ? 0.4525 0.4279 0.5899 0.0541  0.0391  -0.0109 85  GLU   A OE1 
635  O OE2 . GLU   A 79  ? 0.5111 0.5027 0.6502 0.0551  0.0376  -0.0083 85  GLU   A OE2 
636  N N   . ALA   A 80  ? 0.2850 0.2531 0.3924 0.0444  0.0290  -0.0145 86  ALA   A N   
637  C CA  . ALA   A 80  ? 0.2953 0.2536 0.3967 0.0410  0.0315  -0.0210 86  ALA   A CA  
638  C C   . ALA   A 80  ? 0.2852 0.2434 0.3721 0.0357  0.0319  -0.0294 86  ALA   A C   
639  O O   . ALA   A 80  ? 0.2923 0.2541 0.3775 0.0353  0.0346  -0.0329 86  ALA   A O   
640  C CB  . ALA   A 80  ? 0.3093 0.2586 0.4231 0.0435  0.0397  -0.0246 86  ALA   A CB  
641  N N   . SER   A 81  ? 0.2691 0.2244 0.3456 0.0315  0.0289  -0.0318 87  SER   A N   
642  C CA  . SER   A 81  ? 0.2699 0.2259 0.3323 0.0260  0.0284  -0.0387 87  SER   A CA  
643  C C   . SER   A 81  ? 0.2700 0.2180 0.3288 0.0219  0.0306  -0.0444 87  SER   A C   
644  O O   . SER   A 81  ? 0.2815 0.2229 0.3492 0.0238  0.0332  -0.0435 87  SER   A O   
645  C CB  . SER   A 81  ? 0.2707 0.2337 0.3234 0.0244  0.0207  -0.0344 87  SER   A CB  
646  O OG  . SER   A 81  ? 0.2528 0.2142 0.3053 0.0241  0.0166  -0.0304 87  SER   A OG  
647  N N   . GLU   A 82  ? 0.2712 0.2203 0.3173 0.0163  0.0291  -0.0497 88  GLU   A N   
648  C CA  . GLU   A 82  ? 0.2833 0.2267 0.3249 0.0114  0.0301  -0.0549 88  GLU   A CA  
649  C C   . GLU   A 82  ? 0.2640 0.2081 0.3049 0.0116  0.0239  -0.0491 88  GLU   A C   
650  O O   . GLU   A 82  ? 0.2742 0.2135 0.3138 0.0082  0.0246  -0.0520 88  GLU   A O   
651  C CB  . GLU   A 82  ? 0.3555 0.3013 0.3838 0.0047  0.0303  -0.0620 88  GLU   A CB  
652  C CG  . GLU   A 82  ? 0.4506 0.4044 0.4686 0.0024  0.0226  -0.0584 88  GLU   A CG  
653  C CD  . GLU   A 82  ? 0.6032 0.5619 0.6098 -0.0025 0.0224  -0.0627 88  GLU   A CD  
654  O OE1 . GLU   A 82  ? 0.6560 0.6145 0.6543 -0.0088 0.0223  -0.0677 88  GLU   A OE1 
655  O OE2 . GLU   A 82  ? 0.6223 0.5854 0.6279 -0.0005 0.0223  -0.0608 88  GLU   A OE2 
656  N N   . TYR   A 83  ? 0.2498 0.1999 0.2924 0.0152  0.0185  -0.0410 89  TYR   A N   
657  C CA  . TYR   A 83  ? 0.2231 0.1745 0.2650 0.0152  0.0132  -0.0356 89  TYR   A CA  
658  C C   . TYR   A 83  ? 0.2208 0.1700 0.2730 0.0195  0.0131  -0.0291 89  TYR   A C   
659  O O   . TYR   A 83  ? 0.2194 0.1669 0.2722 0.0186  0.0108  -0.0265 89  TYR   A O   
660  C CB  . TYR   A 83  ? 0.2187 0.1781 0.2530 0.0148  0.0073  -0.0321 89  TYR   A CB  
661  C CG  . TYR   A 83  ? 0.2252 0.1873 0.2491 0.0102  0.0063  -0.0372 89  TYR   A CG  
662  C CD1 . TYR   A 83  ? 0.2431 0.2047 0.2618 0.0059  0.0045  -0.0397 89  TYR   A CD1 
663  C CD2 . TYR   A 83  ? 0.2841 0.2499 0.3037 0.0099  0.0071  -0.0389 89  TYR   A CD2 
664  C CE1 . TYR   A 83  ? 0.2716 0.2373 0.2811 0.0015  0.0027  -0.0430 89  TYR   A CE1 
665  C CE2 . TYR   A 83  ? 0.3089 0.2777 0.3186 0.0054  0.0059  -0.0426 89  TYR   A CE2 
666  C CZ  . TYR   A 83  ? 0.3180 0.2869 0.3228 0.0011  0.0036  -0.0445 89  TYR   A CZ  
667  O OH  . TYR   A 83  ? 0.3678 0.3411 0.3633 -0.0037 0.0016  -0.0470 89  TYR   A OH  
668  N N   . TYR   A 84  ? 0.2206 0.1707 0.2816 0.0241  0.0154  -0.0258 90  TYR   A N   
669  C CA  . TYR   A 84  ? 0.2186 0.1679 0.2901 0.0281  0.0147  -0.0181 90  TYR   A CA  
670  C C   . TYR   A 84  ? 0.2415 0.1880 0.3252 0.0324  0.0204  -0.0178 90  TYR   A C   
671  O O   . TYR   A 84  ? 0.2468 0.1962 0.3300 0.0330  0.0227  -0.0212 90  TYR   A O   
672  C CB  . TYR   A 84  ? 0.2042 0.1625 0.2741 0.0297  0.0087  -0.0105 90  TYR   A CB  
673  C CG  . TYR   A 84  ? 0.1825 0.1442 0.2423 0.0264  0.0035  -0.0097 90  TYR   A CG  
674  C CD1 . TYR   A 84  ? 0.1818 0.1414 0.2419 0.0253  0.0015  -0.0066 90  TYR   A CD1 
675  C CD2 . TYR   A 84  ? 0.1812 0.1483 0.2318 0.0246  0.0009  -0.0116 90  TYR   A CD2 
676  C CE1 . TYR   A 84  ? 0.1657 0.1289 0.2178 0.0225  -0.0027 -0.0059 90  TYR   A CE1 
677  C CE2 . TYR   A 84  ? 0.1841 0.1542 0.2274 0.0222  -0.0033 -0.0106 90  TYR   A CE2 
678  C CZ  . TYR   A 84  ? 0.1640 0.1322 0.2082 0.0212  -0.0048 -0.0081 90  TYR   A CZ  
679  O OH  . TYR   A 84  ? 0.1561 0.1273 0.1941 0.0190  -0.0083 -0.0073 90  TYR   A OH  
680  N N   . PRO   A 85  ? 0.2615 0.2040 0.3572 0.0358  0.0220  -0.0124 91  PRO   A N   
681  C CA  . PRO   A 85  ? 0.2744 0.2163 0.3842 0.0410  0.0267  -0.0100 91  PRO   A CA  
682  C C   . PRO   A 85  ? 0.2836 0.2367 0.3957 0.0439  0.0223  -0.0027 91  PRO   A C   
683  O O   . PRO   A 85  ? 0.2702 0.2302 0.3737 0.0419  0.0159  0.0009  91  PRO   A O   
684  C CB  . PRO   A 85  ? 0.2872 0.2222 0.4085 0.0435  0.0284  -0.0045 91  PRO   A CB  
685  C CG  . PRO   A 85  ? 0.2934 0.2312 0.4072 0.0409  0.0217  0.0006  91  PRO   A CG  
686  C CD  . PRO   A 85  ? 0.2641 0.2037 0.3619 0.0354  0.0192  -0.0069 91  PRO   A CD  
687  N N   . ALA   A 86  ? 0.2941 0.2494 0.4188 0.0485  0.0258  -0.0001 92  ALA   A N   
688  C CA  . ALA   A 86  ? 0.2888 0.2556 0.4175 0.0510  0.0218  0.0073  92  ALA   A CA  
689  C C   . ALA   A 86  ? 0.2804 0.2516 0.4108 0.0515  0.0154  0.0175  92  ALA   A C   
690  O O   . ALA   A 86  ? 0.2881 0.2535 0.4263 0.0531  0.0165  0.0216  92  ALA   A O   
691  C CB  . ALA   A 86  ? 0.2971 0.2649 0.4424 0.0564  0.0274  0.0091  92  ALA   A CB  
692  N N   . ARG   A 87  ? 0.2608 0.2412 0.3819 0.0489  0.0090  0.0208  93  ARG   A N   
693  C CA  . ARG   A 87  ? 0.2518 0.2365 0.3723 0.0480  0.0032  0.0295  93  ARG   A CA  
694  C C   . ARG   A 87  ? 0.2257 0.2216 0.3385 0.0456  -0.0025 0.0329  93  ARG   A C   
695  O O   . ARG   A 87  ? 0.2593 0.2583 0.3659 0.0443  -0.0020 0.0278  93  ARG   A O   
696  C CB  . ARG   A 87  ? 0.2626 0.2398 0.3734 0.0443  0.0022  0.0261  93  ARG   A CB  
697  C CG  . ARG   A 87  ? 0.2623 0.2418 0.3571 0.0397  -0.0005 0.0201  93  ARG   A CG  
698  C CD  . ARG   A 87  ? 0.2290 0.2011 0.3156 0.0364  0.0001  0.0142  93  ARG   A CD  
699  N NE  . ARG   A 87  ? 0.2202 0.1958 0.2943 0.0324  -0.0040 0.0127  93  ARG   A NE  
700  C CZ  . ARG   A 87  ? 0.2144 0.1933 0.2799 0.0306  -0.0050 0.0083  93  ARG   A CZ  
701  N NH1 . ARG   A 87  ? 0.2230 0.2030 0.2895 0.0319  -0.0025 0.0048  93  ARG   A NH1 
702  N NH2 . ARG   A 87  ? 0.1767 0.1577 0.2329 0.0275  -0.0082 0.0076  93  ARG   A NH2 
703  N N   . TYR   A 88  ? 0.2149 0.2163 0.3270 0.0442  -0.0076 0.0410  94  TYR   A N   
704  C CA  . TYR   A 88  ? 0.2185 0.2294 0.3216 0.0405  -0.0127 0.0433  94  TYR   A CA  
705  C C   . TYR   A 88  ? 0.2025 0.2094 0.2912 0.0360  -0.0142 0.0381  94  TYR   A C   
706  O O   . TYR   A 88  ? 0.1996 0.2011 0.2869 0.0350  -0.0145 0.0390  94  TYR   A O   
707  C CB  . TYR   A 88  ? 0.2233 0.2430 0.3318 0.0403  -0.0174 0.0545  94  TYR   A CB  
708  C CG  . TYR   A 88  ? 0.2406 0.2677 0.3634 0.0444  -0.0169 0.0606  94  TYR   A CG  
709  C CD1 . TYR   A 88  ? 0.2390 0.2761 0.3606 0.0433  -0.0186 0.0609  94  TYR   A CD1 
710  C CD2 . TYR   A 88  ? 0.2518 0.2752 0.3903 0.0497  -0.0139 0.0654  94  TYR   A CD2 
711  C CE1 . TYR   A 88  ? 0.2580 0.3029 0.3938 0.0472  -0.0180 0.0664  94  TYR   A CE1 
712  C CE2 . TYR   A 88  ? 0.2566 0.2871 0.4101 0.0541  -0.0129 0.0709  94  TYR   A CE2 
713  C CZ  . TYR   A 88  ? 0.2698 0.3113 0.4220 0.0529  -0.0149 0.0710  94  TYR   A CZ  
714  O OH  . TYR   A 88  ? 0.3123 0.3623 0.4797 0.0571  -0.0140 0.0766  94  TYR   A OH  
715  N N   . GLN   A 89  ? 0.1761 0.1859 0.2547 0.0332  -0.0152 0.0332  95  GLN   A N   
716  C CA  . GLN   A 89  ? 0.1568 0.1642 0.2229 0.0292  -0.0167 0.0290  95  GLN   A CA  
717  C C   . GLN   A 89  ? 0.1504 0.1661 0.2110 0.0257  -0.0208 0.0334  95  GLN   A C   
718  O O   . GLN   A 89  ? 0.1571 0.1802 0.2191 0.0254  -0.0220 0.0355  95  GLN   A O   
719  C CB  . GLN   A 89  ? 0.1555 0.1594 0.2150 0.0286  -0.0145 0.0207  95  GLN   A CB  
720  C CG  . GLN   A 89  ? 0.1545 0.1566 0.2028 0.0250  -0.0160 0.0172  95  GLN   A CG  
721  C CD  . GLN   A 89  ? 0.1622 0.1600 0.2051 0.0246  -0.0140 0.0100  95  GLN   A CD  
722  O OE1 . GLN   A 89  ? 0.1557 0.1487 0.2015 0.0261  -0.0111 0.0064  95  GLN   A OE1 
723  N NE2 . GLN   A 89  ? 0.1528 0.1520 0.1874 0.0222  -0.0154 0.0078  95  GLN   A NE2 
724  N N   . SER   A 90  ? 0.1495 0.1647 0.2042 0.0225  -0.0228 0.0348  96  SER   A N   
725  C CA  . SER   A 90  ? 0.1571 0.1798 0.2056 0.0182  -0.0260 0.0382  96  SER   A CA  
726  C C   . SER   A 90  ? 0.1522 0.1739 0.1898 0.0149  -0.0255 0.0317  96  SER   A C   
727  O O   . SER   A 90  ? 0.1570 0.1722 0.1918 0.0159  -0.0234 0.0257  96  SER   A O   
728  C CB  . SER   A 90  ? 0.1831 0.2063 0.2314 0.0161  -0.0279 0.0436  96  SER   A CB  
729  O OG  . SER   A 90  ? 0.2277 0.2432 0.2713 0.0153  -0.0261 0.0388  96  SER   A OG  
730  N N   . HIS   A 91  ? 0.1516 0.1802 0.1837 0.0108  -0.0275 0.0334  97  HIS   A N   
731  C CA  . HIS   A 91  ? 0.1441 0.1717 0.1665 0.0073  -0.0267 0.0280  97  HIS   A CA  
732  C C   . HIS   A 91  ? 0.1359 0.1600 0.1578 0.0096  -0.0245 0.0226  97  HIS   A C   
733  O O   . HIS   A 91  ? 0.1495 0.1692 0.1656 0.0086  -0.0231 0.0176  97  HIS   A O   
734  C CB  . HIS   A 91  ? 0.1672 0.1895 0.1845 0.0055  -0.0257 0.0253  97  HIS   A CB  
735  C CG  . HIS   A 91  ? 0.1749 0.2010 0.1911 0.0022  -0.0274 0.0304  97  HIS   A CG  
736  N ND1 . HIS   A 91  ? 0.2122 0.2428 0.2207 -0.0035 -0.0279 0.0304  97  HIS   A ND1 
737  C CD2 . HIS   A 91  ? 0.1889 0.2144 0.2102 0.0035  -0.0285 0.0354  97  HIS   A CD2 
738  C CE1 . HIS   A 91  ? 0.2226 0.2562 0.2313 -0.0058 -0.0296 0.0357  97  HIS   A CE1 
739  N NE2 . HIS   A 91  ? 0.2165 0.2471 0.2331 -0.0016 -0.0301 0.0392  97  HIS   A NE2 
740  N N   . LEU   A 92  ? 0.1322 0.1590 0.1605 0.0124  -0.0244 0.0240  98  LEU   A N   
741  C CA  . LEU   A 92  ? 0.1327 0.1569 0.1607 0.0143  -0.0222 0.0193  98  LEU   A CA  
742  C C   . LEU   A 92  ? 0.1235 0.1542 0.1491 0.0117  -0.0228 0.0196  98  LEU   A C   
743  O O   . LEU   A 92  ? 0.1328 0.1712 0.1617 0.0103  -0.0248 0.0244  98  LEU   A O   
744  C CB  . LEU   A 92  ? 0.1404 0.1627 0.1775 0.0189  -0.0205 0.0197  98  LEU   A CB  
745  C CG  . LEU   A 92  ? 0.1768 0.1962 0.2131 0.0205  -0.0177 0.0144  98  LEU   A CG  
746  C CD1 . LEU   A 92  ? 0.1797 0.1923 0.2091 0.0198  -0.0167 0.0093  98  LEU   A CD1 
747  C CD2 . LEU   A 92  ? 0.2065 0.2246 0.2525 0.0246  -0.0150 0.0144  98  LEU   A CD2 
748  N N   . MET   A 93  ? 0.1284 0.1561 0.1482 0.0106  -0.0212 0.0148  99  MET   A N   
749  C CA  . MET   A 93  ? 0.1329 0.1654 0.1497 0.0077  -0.0212 0.0143  99  MET   A CA  
750  C C   . MET   A 93  ? 0.1369 0.1676 0.1554 0.0101  -0.0190 0.0114  99  MET   A C   
751  O O   . MET   A 93  ? 0.1516 0.1757 0.1681 0.0120  -0.0174 0.0078  99  MET   A O   
752  C CB  . MET   A 93  ? 0.1422 0.1712 0.1500 0.0038  -0.0206 0.0111  99  MET   A CB  
753  C CG  . MET   A 93  ? 0.1456 0.1761 0.1508 0.0007  -0.0220 0.0131  99  MET   A CG  
754  S SD  . MET   A 93  ? 0.1842 0.2099 0.1801 -0.0038 -0.0199 0.0086  99  MET   A SD  
755  C CE  . MET   A 93  ? 0.2219 0.2382 0.2186 0.0010  -0.0181 0.0051  99  MET   A CE  
756  N N   . LEU   A 94  ? 0.1321 0.1693 0.1546 0.0099  -0.0190 0.0130  100 LEU   A N   
757  C CA  . LEU   A 94  ? 0.1469 0.1830 0.1708 0.0117  -0.0164 0.0101  100 LEU   A CA  
758  C C   . LEU   A 94  ? 0.1300 0.1674 0.1478 0.0081  -0.0158 0.0081  100 LEU   A C   
759  O O   . LEU   A 94  ? 0.1385 0.1812 0.1544 0.0042  -0.0173 0.0099  100 LEU   A O   
760  C CB  . LEU   A 94  ? 0.1657 0.2081 0.2002 0.0147  -0.0158 0.0130  100 LEU   A CB  
761  C CG  . LEU   A 94  ? 0.2016 0.2422 0.2442 0.0188  -0.0156 0.0152  100 LEU   A CG  
762  C CD1 . LEU   A 94  ? 0.2292 0.2756 0.2838 0.0222  -0.0138 0.0177  100 LEU   A CD1 
763  C CD2 . LEU   A 94  ? 0.2268 0.2577 0.2665 0.0208  -0.0132 0.0104  100 LEU   A CD2 
764  N N   . ALA   A 95  ? 0.1324 0.1658 0.1477 0.0089  -0.0134 0.0045  101 ALA   A N   
765  C CA  . ALA   A 95  ? 0.1387 0.1727 0.1489 0.0057  -0.0122 0.0029  101 ALA   A CA  
766  C C   . ALA   A 95  ? 0.1287 0.1628 0.1410 0.0075  -0.0096 0.0009  101 ALA   A C   
767  O O   . ALA   A 95  ? 0.1379 0.1696 0.1535 0.0108  -0.0083 -0.0004 101 ALA   A O   
768  C CB  . ALA   A 95  ? 0.1617 0.1880 0.1635 0.0039  -0.0120 0.0006  101 ALA   A CB  
769  N N   . VAL   A 96  ? 0.1269 0.1634 0.1366 0.0048  -0.0082 0.0000  102 VAL   A N   
770  C CA  . VAL   A 96  ? 0.1409 0.1771 0.1505 0.0055  -0.0054 -0.0022 102 VAL   A CA  
771  C C   . VAL   A 96  ? 0.1668 0.1947 0.1675 0.0046  -0.0048 -0.0045 102 VAL   A C   
772  O O   . VAL   A 96  ? 0.1888 0.2137 0.1839 0.0019  -0.0054 -0.0042 102 VAL   A O   
773  C CB  . VAL   A 96  ? 0.1363 0.1793 0.1474 0.0026  -0.0043 -0.0016 102 VAL   A CB  
774  C CG1 . VAL   A 96  ? 0.1497 0.1920 0.1592 0.0026  -0.0009 -0.0042 102 VAL   A CG1 
775  C CG2 . VAL   A 96  ? 0.1189 0.1715 0.1403 0.0039  -0.0053 0.0017  102 VAL   A CG2 
776  N N   . GLY   A 97  ? 0.1537 0.1783 0.1538 0.0067  -0.0036 -0.0066 103 GLY   A N   
777  C CA  . GLY   A 97  ? 0.1728 0.1913 0.1652 0.0058  -0.0037 -0.0078 103 GLY   A CA  
778  C C   . GLY   A 97  ? 0.1761 0.1926 0.1684 0.0075  -0.0025 -0.0104 103 GLY   A C   
779  O O   . GLY   A 97  ? 0.1782 0.1965 0.1768 0.0098  -0.0013 -0.0115 103 GLY   A O   
780  N N   . HIS   A 98  ? 0.1827 0.1959 0.1680 0.0059  -0.0024 -0.0112 104 HIS   A N   
781  C CA  . HIS   A 98  ? 0.1837 0.1955 0.1672 0.0062  -0.0013 -0.0141 104 HIS   A CA  
782  C C   . HIS   A 98  ? 0.1815 0.1900 0.1660 0.0079  -0.0034 -0.0143 104 HIS   A C   
783  O O   . HIS   A 98  ? 0.1634 0.1695 0.1459 0.0079  -0.0062 -0.0119 104 HIS   A O   
784  C CB  . HIS   A 98  ? 0.1938 0.2047 0.1687 0.0030  -0.0009 -0.0144 104 HIS   A CB  
785  C CG  . HIS   A 98  ? 0.1871 0.1975 0.1587 0.0019  0.0005  -0.0178 104 HIS   A CG  
786  N ND1 . HIS   A 98  ? 0.2001 0.2128 0.1743 0.0017  0.0047  -0.0219 104 HIS   A ND1 
787  C CD2 . HIS   A 98  ? 0.1863 0.1947 0.1530 0.0007  -0.0016 -0.0180 104 HIS   A CD2 
788  C CE1 . HIS   A 98  ? 0.2042 0.2154 0.1740 -0.0001 0.0054  -0.0251 104 HIS   A CE1 
789  N NE2 . HIS   A 98  ? 0.1889 0.1980 0.1540 -0.0009 0.0013  -0.0227 104 HIS   A NE2 
790  N N   . SER   A 99  ? 0.1833 0.1913 0.1711 0.0091  -0.0018 -0.0172 105 SER   A N   
791  C CA  . SER   A 99  ? 0.1873 0.1921 0.1760 0.0101  -0.0034 -0.0178 105 SER   A CA  
792  C C   . SER   A 99  ? 0.2159 0.2197 0.2051 0.0096  -0.0002 -0.0225 105 SER   A C   
793  O O   . SER   A 99  ? 0.2530 0.2578 0.2487 0.0113  0.0031  -0.0242 105 SER   A O   
794  C CB  . SER   A 99  ? 0.2039 0.2086 0.1996 0.0128  -0.0048 -0.0155 105 SER   A CB  
795  O OG  . SER   A 99  ? 0.2253 0.2269 0.2226 0.0138  -0.0061 -0.0159 105 SER   A OG  
796  N N   . GLU   A 100 ? 0.1910 0.1931 0.1743 0.0072  -0.0010 -0.0245 106 GLU   A N   
797  C CA  . GLU   A 100 ? 0.2125 0.2132 0.1951 0.0056  0.0025  -0.0299 106 GLU   A CA  
798  C C   . GLU   A 100 ? 0.2277 0.2256 0.2094 0.0049  0.0002  -0.0305 106 GLU   A C   
799  O O   . GLU   A 100 ? 0.2334 0.2311 0.2149 0.0058  -0.0040 -0.0268 106 GLU   A O   
800  C CB  . GLU   A 100 ? 0.2038 0.2066 0.1780 0.0013  0.0047  -0.0327 106 GLU   A CB  
801  C CG  . GLU   A 100 ? 0.2126 0.2166 0.1777 -0.0019 0.0005  -0.0302 106 GLU   A CG  
802  C CD  . GLU   A 100 ? 0.1950 0.2018 0.1511 -0.0066 0.0019  -0.0318 106 GLU   A CD  
803  O OE1 . GLU   A 100 ? 0.2452 0.2524 0.1955 -0.0106 0.0027  -0.0356 106 GLU   A OE1 
804  O OE2 . GLU   A 100 ? 0.1981 0.2069 0.1524 -0.0069 0.0024  -0.0294 106 GLU   A OE2 
805  N N   . PRO   A 101 ? 0.2645 0.2600 0.2461 0.0032  0.0032  -0.0358 107 PRO   A N   
806  C CA  . PRO   A 101 ? 0.2683 0.2616 0.2488 0.0018  0.0011  -0.0367 107 PRO   A CA  
807  C C   . PRO   A 101 ? 0.2692 0.2654 0.2421 -0.0011 -0.0039 -0.0338 107 PRO   A C   
808  O O   . PRO   A 101 ? 0.2696 0.2689 0.2350 -0.0044 -0.0043 -0.0340 107 PRO   A O   
809  C CB  . PRO   A 101 ? 0.2868 0.2772 0.2661 -0.0013 0.0061  -0.0439 107 PRO   A CB  
810  C CG  . PRO   A 101 ? 0.2986 0.2884 0.2841 0.0013  0.0114  -0.0458 107 PRO   A CG  
811  C CD  . PRO   A 101 ? 0.2708 0.2653 0.2539 0.0022  0.0094  -0.0415 107 PRO   A CD  
812  N N   . GLY   A 102 ? 0.2334 0.2292 0.2092 0.0006  -0.0077 -0.0303 108 GLY   A N   
813  C CA  . GLY   A 102 ? 0.2343 0.2331 0.2061 -0.0008 -0.0125 -0.0264 108 GLY   A CA  
814  C C   . GLY   A 102 ? 0.2016 0.2008 0.1767 0.0028  -0.0148 -0.0208 108 GLY   A C   
815  O O   . GLY   A 102 ? 0.2136 0.2144 0.1881 0.0028  -0.0183 -0.0173 108 GLY   A O   
816  N N   . ASP   A 103 ? 0.1939 0.1922 0.1721 0.0053  -0.0128 -0.0201 109 ASP   A N   
817  C CA  . ASP   A 103 ? 0.1770 0.1754 0.1572 0.0076  -0.0144 -0.0157 109 ASP   A CA  
818  C C   . ASP   A 103 ? 0.1660 0.1627 0.1520 0.0101  -0.0153 -0.0141 109 ASP   A C   
819  O O   . ASP   A 103 ? 0.1591 0.1558 0.1461 0.0112  -0.0166 -0.0110 109 ASP   A O   
820  C CB  . ASP   A 103 ? 0.1580 0.1572 0.1384 0.0082  -0.0121 -0.0155 109 ASP   A CB  
821  C CG  . ASP   A 103 ? 0.1708 0.1718 0.1446 0.0055  -0.0117 -0.0154 109 ASP   A CG  
822  O OD1 . ASP   A 103 ? 0.1673 0.1690 0.1371 0.0041  -0.0143 -0.0131 109 ASP   A OD1 
823  O OD2 . ASP   A 103 ? 0.1628 0.1649 0.1359 0.0049  -0.0088 -0.0174 109 ASP   A OD2 
824  N N   . CYS   A 104 ? 0.1500 0.1451 0.1396 0.0105  -0.0144 -0.0163 110 CYS   A N   
825  C CA  . CYS   A 104 ? 0.1533 0.1471 0.1480 0.0124  -0.0154 -0.0144 110 CYS   A CA  
826  C C   . CYS   A 104 ? 0.1514 0.1460 0.1450 0.0119  -0.0181 -0.0122 110 CYS   A C   
827  O O   . CYS   A 104 ? 0.1623 0.1581 0.1531 0.0102  -0.0196 -0.0126 110 CYS   A O   
828  C CB  . CYS   A 104 ? 0.1648 0.1561 0.1635 0.0126  -0.0138 -0.0168 110 CYS   A CB  
829  S SG  . CYS   A 104 ? 0.1936 0.1841 0.1978 0.0147  -0.0101 -0.0177 110 CYS   A SG  
830  N N   . GLY   A 105 ? 0.1436 0.1379 0.1398 0.0133  -0.0187 -0.0097 111 GLY   A N   
831  C CA  . GLY   A 105 ? 0.1513 0.1461 0.1481 0.0133  -0.0204 -0.0077 111 GLY   A CA  
832  C C   . GLY   A 105 ? 0.1418 0.1368 0.1370 0.0137  -0.0204 -0.0054 111 GLY   A C   
833  O O   . GLY   A 105 ? 0.1498 0.1446 0.1471 0.0143  -0.0208 -0.0036 111 GLY   A O   
834  N N   . GLY   A 106 ? 0.1449 0.1401 0.1371 0.0133  -0.0195 -0.0055 112 GLY   A N   
835  C CA  . GLY   A 106 ? 0.1328 0.1272 0.1236 0.0133  -0.0191 -0.0034 112 GLY   A CA  
836  C C   . GLY   A 106 ? 0.1245 0.1175 0.1175 0.0137  -0.0177 -0.0030 112 GLY   A C   
837  O O   . GLY   A 106 ? 0.1278 0.1214 0.1217 0.0135  -0.0170 -0.0039 112 GLY   A O   
838  N N   . ILE   A 107 ? 0.1319 0.1230 0.1256 0.0139  -0.0170 -0.0015 113 ILE   A N   
839  C CA  . ILE   A 107 ? 0.1223 0.1120 0.1171 0.0132  -0.0150 -0.0020 113 ILE   A CA  
840  C C   . ILE   A 107 ? 0.1236 0.1129 0.1156 0.0115  -0.0135 -0.0025 113 ILE   A C   
841  O O   . ILE   A 107 ? 0.1319 0.1201 0.1219 0.0111  -0.0130 -0.0017 113 ILE   A O   
842  C CB  . ILE   A 107 ? 0.1383 0.1255 0.1359 0.0140  -0.0140 -0.0009 113 ILE   A CB  
843  C CG1 . ILE   A 107 ? 0.1693 0.1581 0.1706 0.0150  -0.0151 -0.0009 113 ILE   A CG1 
844  C CG2 . ILE   A 107 ? 0.1530 0.1375 0.1504 0.0124  -0.0107 -0.0021 113 ILE   A CG2 
845  C CD1 . ILE   A 107 ? 0.1919 0.1795 0.1980 0.0164  -0.0141 0.0006  113 ILE   A CD1 
846  N N   . LEU   A 108 ? 0.1156 0.1063 0.1075 0.0100  -0.0128 -0.0034 114 LEU   A N   
847  C CA  . LEU   A 108 ? 0.1164 0.1076 0.1059 0.0074  -0.0112 -0.0039 114 LEU   A CA  
848  C C   . LEU   A 108 ? 0.1188 0.1072 0.1082 0.0056  -0.0088 -0.0049 114 LEU   A C   
849  O O   . LEU   A 108 ? 0.1323 0.1212 0.1232 0.0056  -0.0088 -0.0053 114 LEU   A O   
850  C CB  . LEU   A 108 ? 0.1295 0.1255 0.1196 0.0064  -0.0123 -0.0036 114 LEU   A CB  
851  C CG  . LEU   A 108 ? 0.1338 0.1325 0.1217 0.0028  -0.0113 -0.0038 114 LEU   A CG  
852  C CD1 . LEU   A 108 ? 0.1529 0.1515 0.1389 0.0019  -0.0104 -0.0040 114 LEU   A CD1 
853  C CD2 . LEU   A 108 ? 0.1391 0.1439 0.1290 0.0020  -0.0132 -0.0021 114 LEU   A CD2 
854  N N   . ARG   A 109 ? 0.1300 0.1152 0.1175 0.0037  -0.0063 -0.0057 115 ARG   A N   
855  C CA  . ARG   A 109 ? 0.1404 0.1218 0.1278 0.0017  -0.0029 -0.0076 115 ARG   A CA  
856  C C   . ARG   A 109 ? 0.1435 0.1240 0.1270 -0.0027 -0.0004 -0.0094 115 ARG   A C   
857  O O   . ARG   A 109 ? 0.1532 0.1349 0.1348 -0.0037 -0.0010 -0.0088 115 ARG   A O   
858  C CB  . ARG   A 109 ? 0.1585 0.1347 0.1497 0.0046  -0.0013 -0.0067 115 ARG   A CB  
859  C CG  . ARG   A 109 ? 0.1620 0.1351 0.1525 0.0052  -0.0008 -0.0050 115 ARG   A CG  
860  C CD  . ARG   A 109 ? 0.1826 0.1513 0.1783 0.0083  0.0005  -0.0029 115 ARG   A CD  
861  N NE  . ARG   A 109 ? 0.1975 0.1697 0.1959 0.0116  -0.0033 -0.0002 115 ARG   A NE  
862  C CZ  . ARG   A 109 ? 0.1870 0.1596 0.1906 0.0139  -0.0034 0.0006  115 ARG   A CZ  
863  N NH1 . ARG   A 109 ? 0.1873 0.1571 0.1941 0.0134  0.0003  -0.0015 115 ARG   A NH1 
864  N NH2 . ARG   A 109 ? 0.1939 0.1704 0.1995 0.0161  -0.0071 0.0031  115 ARG   A NH2 
865  N N   . CYS   A 110 ? 0.1591 0.1374 0.1412 -0.0061 0.0030  -0.0122 116 CYS   A N   
866  C CA  . CYS   A 110 ? 0.2054 0.1817 0.1835 -0.0114 0.0064  -0.0149 116 CYS   A CA  
867  C C   . CYS   A 110 ? 0.2329 0.2008 0.2130 -0.0117 0.0120  -0.0176 116 CYS   A C   
868  O O   . CYS   A 110 ? 0.2392 0.2043 0.2245 -0.0073 0.0124  -0.0164 116 CYS   A O   
869  C CB  . CYS   A 110 ? 0.2063 0.1890 0.1801 -0.0165 0.0055  -0.0162 116 CYS   A CB  
870  S SG  . CYS   A 110 ? 0.1985 0.1817 0.1722 -0.0180 0.0071  -0.0181 116 CYS   A SG  
871  N N   . GLN   A 111 ? 0.2908 0.2548 0.2674 -0.0171 0.0167  -0.0215 117 GLN   A N   
872  C CA  . GLN   A 111 ? 0.3175 0.2729 0.2970 -0.0174 0.0231  -0.0245 117 GLN   A CA  
873  C C   . GLN   A 111 ? 0.3134 0.2693 0.2948 -0.0172 0.0250  -0.0265 117 GLN   A C   
874  O O   . GLN   A 111 ? 0.3469 0.2964 0.3337 -0.0149 0.0295  -0.0278 117 GLN   A O   
875  C CB  . GLN   A 111 ? 0.3293 0.2802 0.3039 -0.0243 0.0284  -0.0293 117 GLN   A CB  
876  C CG  . GLN   A 111 ? 0.4041 0.3613 0.3712 -0.0318 0.0283  -0.0328 117 GLN   A CG  
877  C CD  . GLN   A 111 ? 0.4843 0.4485 0.4467 -0.0352 0.0242  -0.0312 117 GLN   A CD  
878  O OE1 . GLN   A 111 ? 0.5016 0.4696 0.4663 -0.0307 0.0193  -0.0267 117 GLN   A OE1 
879  N NE2 . GLN   A 111 ? 0.4860 0.4523 0.4418 -0.0435 0.0265  -0.0352 117 GLN   A NE2 
880  N N   . HIS   A 112 ? 0.2557 0.2195 0.2336 -0.0190 0.0213  -0.0261 118 HIS   A N   
881  C CA  . HIS   A 112 ? 0.2434 0.2084 0.2222 -0.0195 0.0230  -0.0278 118 HIS   A CA  
882  C C   . HIS   A 112 ? 0.2401 0.2065 0.2256 -0.0129 0.0199  -0.0242 118 HIS   A C   
883  O O   . HIS   A 112 ? 0.2599 0.2264 0.2479 -0.0126 0.0221  -0.0256 118 HIS   A O   
884  C CB  . HIS   A 112 ? 0.2249 0.1977 0.1965 -0.0255 0.0208  -0.0287 118 HIS   A CB  
885  C CG  . HIS   A 112 ? 0.2612 0.2342 0.2256 -0.0331 0.0234  -0.0322 118 HIS   A CG  
886  N ND1 . HIS   A 112 ? 0.2523 0.2317 0.2129 -0.0356 0.0190  -0.0300 118 HIS   A ND1 
887  C CD2 . HIS   A 112 ? 0.2913 0.2592 0.2521 -0.0391 0.0301  -0.0382 118 HIS   A CD2 
888  C CE1 . HIS   A 112 ? 0.3036 0.2821 0.2581 -0.0432 0.0227  -0.0342 118 HIS   A CE1 
889  N NE2 . HIS   A 112 ? 0.3049 0.2762 0.2589 -0.0457 0.0296  -0.0396 118 HIS   A NE2 
890  N N   . GLY   A 113 ? 0.2114 0.1797 0.1995 -0.0082 0.0150  -0.0199 119 GLY   A N   
891  C CA  . GLY   A 113 ? 0.1926 0.1627 0.1863 -0.0028 0.0119  -0.0167 119 GLY   A CA  
892  C C   . GLY   A 113 ? 0.1686 0.1444 0.1608 -0.0011 0.0058  -0.0134 119 GLY   A C   
893  O O   . GLY   A 113 ? 0.1786 0.1561 0.1671 -0.0026 0.0041  -0.0128 119 GLY   A O   
894  N N   . VAL   A 114 ? 0.1487 0.1273 0.1444 0.0020  0.0030  -0.0115 120 VAL   A N   
895  C CA  . VAL   A 114 ? 0.1368 0.1196 0.1320 0.0039  -0.0020 -0.0089 120 VAL   A CA  
896  C C   . VAL   A 114 ? 0.1341 0.1216 0.1255 0.0008  -0.0037 -0.0088 120 VAL   A C   
897  O O   . VAL   A 114 ? 0.1419 0.1308 0.1324 -0.0015 -0.0026 -0.0097 120 VAL   A O   
898  C CB  . VAL   A 114 ? 0.1489 0.1328 0.1490 0.0075  -0.0041 -0.0072 120 VAL   A CB  
899  C CG1 . VAL   A 114 ? 0.1672 0.1546 0.1666 0.0088  -0.0083 -0.0055 120 VAL   A CG1 
900  C CG2 . VAL   A 114 ? 0.1632 0.1443 0.1678 0.0106  -0.0034 -0.0059 120 VAL   A CG2 
901  N N   . VAL   A 115 ? 0.1313 0.1216 0.1210 0.0008  -0.0062 -0.0074 121 VAL   A N   
902  C CA  . VAL   A 115 ? 0.1442 0.1398 0.1319 -0.0015 -0.0082 -0.0061 121 VAL   A CA  
903  C C   . VAL   A 115 ? 0.1363 0.1343 0.1275 0.0015  -0.0114 -0.0037 121 VAL   A C   
904  O O   . VAL   A 115 ? 0.1475 0.1489 0.1389 0.0003  -0.0127 -0.0020 121 VAL   A O   
905  C CB  . VAL   A 115 ? 0.1459 0.1436 0.1312 -0.0033 -0.0086 -0.0059 121 VAL   A CB  
906  C CG1 . VAL   A 115 ? 0.1526 0.1574 0.1379 -0.0050 -0.0113 -0.0033 121 VAL   A CG1 
907  C CG2 . VAL   A 115 ? 0.1675 0.1625 0.1490 -0.0074 -0.0050 -0.0087 121 VAL   A CG2 
908  N N   . GLY   A 116 ? 0.1347 0.1309 0.1283 0.0051  -0.0124 -0.0034 122 GLY   A N   
909  C CA  . GLY   A 116 ? 0.1388 0.1363 0.1355 0.0076  -0.0146 -0.0021 122 GLY   A CA  
910  C C   . GLY   A 116 ? 0.1295 0.1252 0.1271 0.0102  -0.0153 -0.0027 122 GLY   A C   
911  O O   . GLY   A 116 ? 0.1263 0.1197 0.1228 0.0105  -0.0144 -0.0034 122 GLY   A O   
912  N N   . ILE   A 117 ? 0.1230 0.1194 0.1229 0.0119  -0.0165 -0.0024 123 ILE   A N   
913  C CA  . ILE   A 117 ? 0.1224 0.1175 0.1221 0.0134  -0.0170 -0.0035 123 ILE   A CA  
914  C C   . ILE   A 117 ? 0.1223 0.1189 0.1230 0.0141  -0.0169 -0.0039 123 ILE   A C   
915  O O   . ILE   A 117 ? 0.1332 0.1313 0.1369 0.0144  -0.0169 -0.0027 123 ILE   A O   
916  C CB  . ILE   A 117 ? 0.1402 0.1342 0.1417 0.0141  -0.0179 -0.0041 123 ILE   A CB  
917  C CG1 . ILE   A 117 ? 0.1497 0.1438 0.1543 0.0142  -0.0182 -0.0037 123 ILE   A CG1 
918  C CG2 . ILE   A 117 ? 0.1576 0.1508 0.1593 0.0140  -0.0178 -0.0037 123 ILE   A CG2 
919  C CD1 . ILE   A 117 ? 0.1586 0.1515 0.1650 0.0143  -0.0189 -0.0048 123 ILE   A CD1 
920  N N   . VAL   A 118 ? 0.1275 0.1237 0.1262 0.0143  -0.0165 -0.0052 124 VAL   A N   
921  C CA  . VAL   A 118 ? 0.1253 0.1226 0.1252 0.0150  -0.0155 -0.0063 124 VAL   A CA  
922  C C   . VAL   A 118 ? 0.1276 0.1237 0.1315 0.0160  -0.0152 -0.0072 124 VAL   A C   
923  O O   . VAL   A 118 ? 0.1314 0.1255 0.1346 0.0156  -0.0160 -0.0084 124 VAL   A O   
924  C CB  . VAL   A 118 ? 0.1345 0.1316 0.1305 0.0142  -0.0150 -0.0080 124 VAL   A CB  
925  C CG1 . VAL   A 118 ? 0.1507 0.1487 0.1482 0.0146  -0.0129 -0.0101 124 VAL   A CG1 
926  C CG2 . VAL   A 118 ? 0.1414 0.1390 0.1340 0.0132  -0.0148 -0.0067 124 VAL   A CG2 
927  N N   . SER   A 119 ? 0.1349 0.1322 0.1435 0.0172  -0.0141 -0.0065 125 SER   A N   
928  C CA  . SER   A 119 ? 0.1351 0.1302 0.1487 0.0185  -0.0132 -0.0070 125 SER   A CA  
929  C C   . SER   A 119 ? 0.1620 0.1572 0.1799 0.0199  -0.0104 -0.0086 125 SER   A C   
930  O O   . SER   A 119 ? 0.1787 0.1705 0.1999 0.0206  -0.0086 -0.0107 125 SER   A O   
931  C CB  . SER   A 119 ? 0.1522 0.1482 0.1695 0.0189  -0.0145 -0.0033 125 SER   A CB  
932  O OG  . SER   A 119 ? 0.1497 0.1433 0.1730 0.0203  -0.0135 -0.0026 125 SER   A OG  
933  N N   . THR   A 120 ? 0.1587 0.1575 0.1772 0.0203  -0.0096 -0.0079 126 THR   A N   
934  C CA  . THR   A 120 ? 0.1805 0.1799 0.2043 0.0219  -0.0062 -0.0096 126 THR   A CA  
935  C C   . THR   A 120 ? 0.2065 0.2086 0.2260 0.0206  -0.0049 -0.0115 126 THR   A C   
936  O O   . THR   A 120 ? 0.1882 0.1920 0.2020 0.0188  -0.0069 -0.0104 126 THR   A O   
937  C CB  . THR   A 120 ? 0.1893 0.1921 0.2227 0.0244  -0.0061 -0.0051 126 THR   A CB  
938  O OG1 . THR   A 120 ? 0.2194 0.2283 0.2521 0.0236  -0.0079 -0.0019 126 THR   A OG1 
939  C CG2 . THR   A 120 ? 0.1997 0.2005 0.2368 0.0253  -0.0077 -0.0019 126 THR   A CG2 
940  N N   . GLY   A 121 ? 0.2357 0.2378 0.2581 0.0212  -0.0011 -0.0146 127 GLY   A N   
941  C CA  . GLY   A 121 ? 0.2518 0.2566 0.2700 0.0196  0.0005  -0.0165 127 GLY   A CA  
942  C C   . GLY   A 121 ? 0.2539 0.2605 0.2791 0.0212  0.0053  -0.0187 127 GLY   A C   
943  O O   . GLY   A 121 ? 0.2386 0.2452 0.2737 0.0242  0.0070  -0.0174 127 GLY   A O   
944  N N   . GLY   A 122 ? 0.2552 0.2638 0.2757 0.0191  0.0074  -0.0213 128 GLY   A N   
945  C CA  . GLY   A 122 ? 0.2533 0.2639 0.2793 0.0199  0.0128  -0.0244 128 GLY   A CA  
946  C C   . GLY   A 122 ? 0.2519 0.2696 0.2838 0.0210  0.0131  -0.0211 128 GLY   A C   
947  O O   . GLY   A 122 ? 0.2486 0.2698 0.2833 0.0219  0.0093  -0.0160 128 GLY   A O   
948  N N   . ASN   A 123 ? 0.2545 0.2749 0.2886 0.0206  0.0179  -0.0243 129 ASN   A N   
949  C CA  . ASN   A 123 ? 0.2684 0.2964 0.3100 0.0217  0.0189  -0.0215 129 ASN   A CA  
950  C C   . ASN   A 123 ? 0.2298 0.2620 0.2647 0.0188  0.0148  -0.0181 129 ASN   A C   
951  O O   . ASN   A 123 ? 0.2120 0.2513 0.2536 0.0194  0.0142  -0.0146 129 ASN   A O   
952  C CB  . ASN   A 123 ? 0.3024 0.3334 0.3587 0.0264  0.0187  -0.0171 129 ASN   A CB  
953  C CG  . ASN   A 123 ? 0.3523 0.3792 0.4180 0.0297  0.0244  -0.0206 129 ASN   A CG  
954  O OD1 . ASN   A 123 ? 0.3627 0.3864 0.4256 0.0283  0.0298  -0.0269 129 ASN   A OD1 
955  N ND2 . ASN   A 123 ? 0.3626 0.3890 0.4394 0.0337  0.0237  -0.0166 129 ASN   A ND2 
956  N N   . GLY   A 124 ? 0.2137 0.2418 0.2364 0.0155  0.0123  -0.0189 130 GLY   A N   
957  C CA  . GLY   A 124 ? 0.1917 0.2221 0.2087 0.0129  0.0089  -0.0158 130 GLY   A CA  
958  C C   . GLY   A 124 ? 0.1568 0.1876 0.1757 0.0137  0.0044  -0.0114 130 GLY   A C   
959  O O   . GLY   A 124 ? 0.1680 0.2011 0.1839 0.0114  0.0022  -0.0091 130 GLY   A O   
960  N N   . LEU   A 125 ? 0.1394 0.1673 0.1623 0.0164  0.0032  -0.0107 131 LEU   A N   
961  C CA  . LEU   A 125 ? 0.1403 0.1684 0.1642 0.0167  -0.0009 -0.0068 131 LEU   A CA  
962  C C   . LEU   A 125 ? 0.1403 0.1612 0.1578 0.0165  -0.0026 -0.0081 131 LEU   A C   
963  O O   . LEU   A 125 ? 0.1611 0.1777 0.1763 0.0168  -0.0009 -0.0116 131 LEU   A O   
964  C CB  . LEU   A 125 ? 0.1343 0.1659 0.1697 0.0201  -0.0009 -0.0038 131 LEU   A CB  
965  C CG  . LEU   A 125 ? 0.1444 0.1849 0.1885 0.0208  0.0001  -0.0011 131 LEU   A CG  
966  C CD1 . LEU   A 125 ? 0.1777 0.2208 0.2351 0.0251  0.0012  0.0017  131 LEU   A CD1 
967  C CD2 . LEU   A 125 ? 0.1440 0.1905 0.1853 0.0174  -0.0037 0.0027  131 LEU   A CD2 
968  N N   . VAL   A 126 ? 0.1227 0.1430 0.1373 0.0154  -0.0059 -0.0056 132 VAL   A N   
969  C CA  . VAL   A 126 ? 0.1290 0.1437 0.1393 0.0154  -0.0077 -0.0062 132 VAL   A CA  
970  C C   . VAL   A 126 ? 0.1357 0.1517 0.1495 0.0159  -0.0101 -0.0028 132 VAL   A C   
971  O O   . VAL   A 126 ? 0.1448 0.1653 0.1592 0.0143  -0.0114 -0.0002 132 VAL   A O   
972  C CB  . VAL   A 126 ? 0.1435 0.1550 0.1451 0.0129  -0.0086 -0.0070 132 VAL   A CB  
973  C CG1 . VAL   A 126 ? 0.1685 0.1824 0.1680 0.0106  -0.0093 -0.0051 132 VAL   A CG1 
974  C CG2 . VAL   A 126 ? 0.1526 0.1594 0.1516 0.0133  -0.0103 -0.0072 132 VAL   A CG2 
975  N N   . GLY   A 127 ? 0.1295 0.1421 0.1452 0.0174  -0.0107 -0.0028 133 GLY   A N   
976  C CA  . GLY   A 127 ? 0.1310 0.1449 0.1494 0.0175  -0.0129 0.0007  133 GLY   A CA  
977  C C   . GLY   A 127 ? 0.1302 0.1396 0.1434 0.0164  -0.0142 -0.0002 133 GLY   A C   
978  O O   . GLY   A 127 ? 0.1501 0.1551 0.1606 0.0168  -0.0136 -0.0030 133 GLY   A O   
979  N N   . PHE   A 128 ? 0.1231 0.1341 0.1348 0.0146  -0.0159 0.0021  134 PHE   A N   
980  C CA  . PHE   A 128 ? 0.1359 0.1433 0.1434 0.0134  -0.0166 0.0013  134 PHE   A CA  
981  C C   . PHE   A 128 ? 0.1274 0.1356 0.1374 0.0132  -0.0179 0.0039  134 PHE   A C   
982  O O   . PHE   A 128 ? 0.1329 0.1459 0.1449 0.0120  -0.0189 0.0072  134 PHE   A O   
983  C CB  . PHE   A 128 ? 0.1358 0.1435 0.1380 0.0105  -0.0164 0.0008  134 PHE   A CB  
984  C CG  . PHE   A 128 ? 0.1216 0.1289 0.1212 0.0102  -0.0152 -0.0008 134 PHE   A CG  
985  C CD1 . PHE   A 128 ? 0.1133 0.1165 0.1101 0.0109  -0.0147 -0.0027 134 PHE   A CD1 
986  C CD2 . PHE   A 128 ? 0.1388 0.1506 0.1389 0.0087  -0.0149 0.0000  134 PHE   A CD2 
987  C CE1 . PHE   A 128 ? 0.1255 0.1283 0.1194 0.0102  -0.0136 -0.0035 134 PHE   A CE1 
988  C CE2 . PHE   A 128 ? 0.1454 0.1567 0.1428 0.0080  -0.0136 -0.0014 134 PHE   A CE2 
989  C CZ  . PHE   A 128 ? 0.1370 0.1435 0.1311 0.0087  -0.0129 -0.0030 134 PHE   A CZ  
990  N N   . ALA   A 129 ? 0.1211 0.1254 0.1310 0.0138  -0.0179 0.0029  135 ALA   A N   
991  C CA  . ALA   A 129 ? 0.1280 0.1326 0.1393 0.0130  -0.0189 0.0052  135 ALA   A CA  
992  C C   . ALA   A 129 ? 0.1353 0.1407 0.1415 0.0098  -0.0188 0.0050  135 ALA   A C   
993  O O   . ALA   A 129 ? 0.1354 0.1377 0.1389 0.0096  -0.0179 0.0023  135 ALA   A O   
994  C CB  . ALA   A 129 ? 0.1396 0.1397 0.1526 0.0144  -0.0186 0.0037  135 ALA   A CB  
995  N N   . ASP   A 130 ? 0.1335 0.1432 0.1388 0.0071  -0.0197 0.0077  136 ASP   A N   
996  C CA  . ASP   A 130 ? 0.1443 0.1548 0.1443 0.0033  -0.0188 0.0067  136 ASP   A CA  
997  C C   . ASP   A 130 ? 0.1384 0.1460 0.1380 0.0028  -0.0181 0.0060  136 ASP   A C   
998  O O   . ASP   A 130 ? 0.1544 0.1619 0.1573 0.0040  -0.0192 0.0082  136 ASP   A O   
999  C CB  . ASP   A 130 ? 0.1506 0.1678 0.1493 -0.0004 -0.0203 0.0102  136 ASP   A CB  
1000 C CG  . ASP   A 130 ? 0.2198 0.2386 0.2119 -0.0058 -0.0190 0.0084  136 ASP   A CG  
1001 O OD1 . ASP   A 130 ? 0.1915 0.2065 0.1805 -0.0065 -0.0166 0.0044  136 ASP   A OD1 
1002 O OD2 . ASP   A 130 ? 0.2690 0.2940 0.2590 -0.0099 -0.0204 0.0114  136 ASP   A OD2 
1003 N N   . VAL   A 131 ? 0.1335 0.1388 0.1297 0.0011  -0.0160 0.0030  137 VAL   A N   
1004 C CA  . VAL   A 131 ? 0.1395 0.1431 0.1355 0.0000  -0.0147 0.0021  137 VAL   A CA  
1005 C C   . VAL   A 131 ? 0.1497 0.1549 0.1407 -0.0050 -0.0125 0.0008  137 VAL   A C   
1006 O O   . VAL   A 131 ? 0.1488 0.1529 0.1395 -0.0063 -0.0106 -0.0005 137 VAL   A O   
1007 C CB  . VAL   A 131 ? 0.1411 0.1403 0.1396 0.0029  -0.0135 -0.0005 137 VAL   A CB  
1008 C CG1 . VAL   A 131 ? 0.1536 0.1516 0.1558 0.0065  -0.0155 0.0002  137 VAL   A CG1 
1009 C CG2 . VAL   A 131 ? 0.1473 0.1442 0.1441 0.0028  -0.0113 -0.0031 137 VAL   A CG2 
1010 N N   . ARG   A 132 ? 0.1428 0.1508 0.1299 -0.0081 -0.0123 0.0007  138 ARG   A N   
1011 C CA  . ARG   A 132 ? 0.1486 0.1574 0.1301 -0.0137 -0.0094 -0.0019 138 ARG   A CA  
1012 C C   . ARG   A 132 ? 0.1548 0.1678 0.1333 -0.0180 -0.0098 0.0001  138 ARG   A C   
1013 O O   . ARG   A 132 ? 0.1756 0.1886 0.1493 -0.0229 -0.0064 -0.0029 138 ARG   A O   
1014 C CB  . ARG   A 132 ? 0.1569 0.1680 0.1344 -0.0170 -0.0092 -0.0027 138 ARG   A CB  
1015 C CG  . ARG   A 132 ? 0.1518 0.1579 0.1311 -0.0138 -0.0077 -0.0053 138 ARG   A CG  
1016 C CD  . ARG   A 132 ? 0.1522 0.1609 0.1275 -0.0177 -0.0074 -0.0060 138 ARG   A CD  
1017 N NE  . ARG   A 132 ? 0.1704 0.1855 0.1479 -0.0167 -0.0116 -0.0017 138 ARG   A NE  
1018 C CZ  . ARG   A 132 ? 0.1705 0.1899 0.1466 -0.0191 -0.0126 -0.0010 138 ARG   A CZ  
1019 N NH1 . ARG   A 132 ? 0.1788 0.1964 0.1500 -0.0235 -0.0096 -0.0047 138 ARG   A NH1 
1020 N NH2 . ARG   A 132 ? 0.1951 0.2203 0.1753 -0.0170 -0.0160 0.0032  138 ARG   A NH2 
1021 N N   . ASP   A 133 ? 0.1524 0.1691 0.1337 -0.0167 -0.0135 0.0053  139 ASP   A N   
1022 C CA  . ASP   A 133 ? 0.1621 0.1830 0.1406 -0.0210 -0.0142 0.0083  139 ASP   A CA  
1023 C C   . ASP   A 133 ? 0.1626 0.1796 0.1434 -0.0194 -0.0124 0.0072  139 ASP   A C   
1024 O O   . ASP   A 133 ? 0.1750 0.1948 0.1531 -0.0232 -0.0123 0.0092  139 ASP   A O   
1025 C CB  . ASP   A 133 ? 0.1838 0.2103 0.1653 -0.0201 -0.0188 0.0153  139 ASP   A CB  
1026 C CG  . ASP   A 133 ? 0.2121 0.2347 0.2018 -0.0133 -0.0204 0.0172  139 ASP   A CG  
1027 O OD1 . ASP   A 133 ? 0.2186 0.2369 0.2110 -0.0093 -0.0195 0.0139  139 ASP   A OD1 
1028 O OD2 . ASP   A 133 ? 0.2135 0.2370 0.2067 -0.0124 -0.0222 0.0218  139 ASP   A OD2 
1029 N N   . LEU   A 134 ? 0.1544 0.1660 0.1403 -0.0143 -0.0114 0.0047  140 LEU   A N   
1030 C CA  . LEU   A 134 ? 0.1590 0.1678 0.1483 -0.0127 -0.0101 0.0039  140 LEU   A CA  
1031 C C   . LEU   A 134 ? 0.1522 0.1593 0.1394 -0.0152 -0.0054 -0.0009 140 LEU   A C   
1032 O O   . LEU   A 134 ? 0.1580 0.1614 0.1488 -0.0122 -0.0032 -0.0042 140 LEU   A O   
1033 C CB  . LEU   A 134 ? 0.1567 0.1617 0.1524 -0.0068 -0.0115 0.0036  140 LEU   A CB  
1034 C CG  . LEU   A 134 ? 0.1675 0.1731 0.1661 -0.0040 -0.0151 0.0073  140 LEU   A CG  
1035 C CD1 . LEU   A 134 ? 0.1750 0.1767 0.1784 0.0007  -0.0157 0.0057  140 LEU   A CD1 
1036 C CD2 . LEU   A 134 ? 0.1796 0.1874 0.1794 -0.0054 -0.0168 0.0121  140 LEU   A CD2 
1037 N N   . LEU   A 135 ? 0.1477 0.1579 0.1291 -0.0212 -0.0035 -0.0012 141 LEU   A N   
1038 C CA  . LEU   A 135 ? 0.1539 0.1625 0.1326 -0.0246 0.0022  -0.0065 141 LEU   A CA  
1039 C C   . LEU   A 135 ? 0.1646 0.1706 0.1492 -0.0220 0.0050  -0.0085 141 LEU   A C   
1040 O O   . LEU   A 135 ? 0.1777 0.1808 0.1643 -0.0217 0.0098  -0.0131 141 LEU   A O   
1041 C CB  . LEU   A 135 ? 0.1672 0.1805 0.1372 -0.0328 0.0039  -0.0068 141 LEU   A CB  
1042 C CG  . LEU   A 135 ? 0.1918 0.2100 0.1560 -0.0363 0.0004  -0.0037 141 LEU   A CG  
1043 C CD1 . LEU   A 135 ? 0.2092 0.2325 0.1638 -0.0455 0.0026  -0.0048 141 LEU   A CD1 
1044 C CD2 . LEU   A 135 ? 0.2132 0.2289 0.1782 -0.0341 0.0005  -0.0062 141 LEU   A CD2 
1045 N N   . TRP   A 136 ? 0.1578 0.1649 0.1457 -0.0203 0.0021  -0.0049 142 TRP   A N   
1046 C CA  . TRP   A 136 ? 0.1703 0.1762 0.1641 -0.0183 0.0042  -0.0064 142 TRP   A CA  
1047 C C   . TRP   A 136 ? 0.1816 0.1842 0.1825 -0.0126 0.0045  -0.0083 142 TRP   A C   
1048 O O   . TRP   A 136 ? 0.1868 0.1893 0.1934 -0.0112 0.0069  -0.0100 142 TRP   A O   
1049 C CB  . TRP   A 136 ? 0.1632 0.1706 0.1588 -0.0183 0.0011  -0.0020 142 TRP   A CB  
1050 C CG  . TRP   A 136 ? 0.1691 0.1755 0.1670 -0.0145 -0.0040 0.0017  142 TRP   A CG  
1051 C CD1 . TRP   A 136 ? 0.1966 0.2047 0.1915 -0.0157 -0.0073 0.0061  142 TRP   A CD1 
1052 C CD2 . TRP   A 136 ? 0.1712 0.1749 0.1753 -0.0094 -0.0060 0.0015  142 TRP   A CD2 
1053 N NE1 . TRP   A 136 ? 0.1956 0.2016 0.1951 -0.0111 -0.0105 0.0080  142 TRP   A NE1 
1054 C CE2 . TRP   A 136 ? 0.1847 0.1878 0.1890 -0.0077 -0.0097 0.0049  142 TRP   A CE2 
1055 C CE3 . TRP   A 136 ? 0.1790 0.1813 0.1888 -0.0064 -0.0050 -0.0011 142 TRP   A CE3 
1056 C CZ2 . TRP   A 136 ? 0.1846 0.1851 0.1934 -0.0036 -0.0118 0.0048  142 TRP   A CZ2 
1057 C CZ3 . TRP   A 136 ? 0.1987 0.1994 0.2124 -0.0028 -0.0079 -0.0005 142 TRP   A CZ3 
1058 C CH2 . TRP   A 136 ? 0.1898 0.1893 0.2026 -0.0016 -0.0109 0.0020  142 TRP   A CH2 
1059 N N   . LEU   A 137 ? 0.1569 0.1578 0.1582 -0.0094 0.0019  -0.0078 143 LEU   A N   
1060 C CA  . LEU   A 137 ? 0.1773 0.1758 0.1848 -0.0046 0.0021  -0.0090 143 LEU   A CA  
1061 C C   . LEU   A 137 ? 0.2065 0.2031 0.2164 -0.0049 0.0076  -0.0127 143 LEU   A C   
1062 O O   . LEU   A 137 ? 0.2195 0.2152 0.2365 -0.0010 0.0083  -0.0130 143 LEU   A O   
1063 C CB  . LEU   A 137 ? 0.1696 0.1666 0.1756 -0.0022 -0.0010 -0.0079 143 LEU   A CB  
1064 C CG  . LEU   A 137 ? 0.1746 0.1725 0.1810 -0.0005 -0.0057 -0.0047 143 LEU   A CG  
1065 C CD1 . LEU   A 137 ? 0.1964 0.1935 0.2006 0.0011  -0.0077 -0.0041 143 LEU   A CD1 
1066 C CD2 . LEU   A 137 ? 0.1832 0.1810 0.1956 0.0026  -0.0073 -0.0043 143 LEU   A CD2 
1067 N N   . ASP   A 138 ? 0.2246 0.2210 0.2290 -0.0096 0.0117  -0.0155 144 ASP   A N   
1068 C CA  . ASP   A 138 ? 0.2572 0.2506 0.2639 -0.0103 0.0183  -0.0200 144 ASP   A CA  
1069 C C   . ASP   A 138 ? 0.3128 0.3077 0.3239 -0.0116 0.0229  -0.0221 144 ASP   A C   
1070 O O   . ASP   A 138 ? 0.3287 0.3209 0.3429 -0.0120 0.0293  -0.0261 144 ASP   A O   
1071 C CB  . ASP   A 138 ? 0.2621 0.2544 0.2599 -0.0162 0.0215  -0.0231 144 ASP   A CB  
1072 C CG  . ASP   A 138 ? 0.3083 0.2995 0.3021 -0.0158 0.0183  -0.0218 144 ASP   A CG  
1073 O OD1 . ASP   A 138 ? 0.3429 0.3329 0.3411 -0.0105 0.0146  -0.0192 144 ASP   A OD1 
1074 O OD2 . ASP   A 138 ? 0.3664 0.3586 0.3523 -0.0212 0.0192  -0.0234 144 ASP   A OD2 
1075 N N   . GLU   A 139 ? 0.3369 0.3355 0.3484 -0.0124 0.0204  -0.0197 145 GLU   A N   
1076 C CA  . GLU   A 139 ? 0.3846 0.3852 0.4000 -0.0141 0.0249  -0.0217 145 GLU   A CA  
1077 C C   . GLU   A 139 ? 0.4183 0.4216 0.4418 -0.0105 0.0218  -0.0188 145 GLU   A C   
1078 O O   . GLU   A 139 ? 0.4137 0.4173 0.4378 -0.0077 0.0159  -0.0153 145 GLU   A O   
1079 C CB  . GLU   A 139 ? 0.4459 0.4489 0.4517 -0.0214 0.0266  -0.0224 145 GLU   A CB  
1080 C CG  . GLU   A 139 ? 0.5406 0.5461 0.5410 -0.0227 0.0200  -0.0172 145 GLU   A CG  
1081 C CD  . GLU   A 139 ? 0.6313 0.6395 0.6209 -0.0298 0.0201  -0.0165 145 GLU   A CD  
1082 O OE1 . GLU   A 139 ? 0.6240 0.6352 0.6110 -0.0315 0.0161  -0.0118 145 GLU   A OE1 
1083 O OE2 . GLU   A 139 ? 0.6680 0.6757 0.6519 -0.0340 0.0241  -0.0204 145 GLU   A OE2 
1084 N N   . GLU   A 140 ? 0.4547 0.4604 0.4841 -0.0112 0.0262  -0.0205 146 GLU   A N   
1085 C CA  . GLU   A 140 ? 0.4966 0.5060 0.5337 -0.0092 0.0241  -0.0184 146 GLU   A CA  
1086 C C   . GLU   A 140 ? 0.5279 0.5380 0.5750 -0.0031 0.0216  -0.0167 146 GLU   A C   
1087 O O   . GLU   A 140 ? 0.5439 0.5575 0.6010 -0.0011 0.0236  -0.0168 146 GLU   A O   
1088 C CB  . GLU   A 140 ? 0.5417 0.5525 0.5732 -0.0116 0.0188  -0.0148 146 GLU   A CB  
1089 C CG  . GLU   A 140 ? 0.6290 0.6427 0.6676 -0.0096 0.0155  -0.0124 146 GLU   A CG  
1090 C CD  . GLU   A 140 ? 0.7413 0.7575 0.7782 -0.0140 0.0163  -0.0115 146 GLU   A CD  
1091 O OE1 . GLU   A 140 ? 0.7824 0.7972 0.8115 -0.0170 0.0139  -0.0091 146 GLU   A OE1 
1092 O OE2 . GLU   A 140 ? 0.7500 0.7698 0.7938 -0.0145 0.0195  -0.0127 146 GLU   A OE2 
1093 N N   . SER   B 1   ? 0.2434 0.2492 0.2530 -0.0031 -0.0336 0.0350  7   SER   C N   
1094 C CA  . SER   B 1   ? 0.2271 0.2351 0.2473 -0.0035 -0.0344 0.0355  7   SER   C CA  
1095 C C   . SER   B 1   ? 0.2144 0.2210 0.2332 -0.0028 -0.0330 0.0317  7   SER   C C   
1096 O O   . SER   B 1   ? 0.2194 0.2231 0.2291 -0.0024 -0.0325 0.0292  7   SER   C O   
1097 C CB  . SER   B 1   ? 0.2605 0.2684 0.2829 -0.0057 -0.0395 0.0392  7   SER   C CB  
1098 O OG  . SER   B 1   ? 0.3191 0.3234 0.3315 -0.0070 -0.0423 0.0379  7   SER   C OG  
1099 N N   . GLY   B 2   ? 0.1943 0.2027 0.2222 -0.0027 -0.0318 0.0314  8   GLY   C N   
1100 C CA  . GLY   B 2   ? 0.1792 0.1859 0.2057 -0.0023 -0.0304 0.0284  8   GLY   C CA  
1101 C C   . GLY   B 2   ? 0.1640 0.1725 0.1991 -0.0014 -0.0270 0.0273  8   GLY   C C   
1102 O O   . GLY   B 2   ? 0.1676 0.1782 0.2078 -0.0006 -0.0250 0.0276  8   GLY   C O   
1103 N N   . ALA   B 3   ? 0.1488 0.1561 0.1852 -0.0016 -0.0260 0.0260  9   ALA   C N   
1104 C CA  . ALA   B 3   ? 0.1516 0.1596 0.1946 -0.0009 -0.0222 0.0247  9   ALA   C CA  
1105 C C   . ALA   B 3   ? 0.1469 0.1522 0.1844 -0.0004 -0.0203 0.0220  9   ALA   C C   
1106 O O   . ALA   B 3   ? 0.1558 0.1587 0.1868 -0.0009 -0.0223 0.0217  9   ALA   C O   
1107 C CB  . ALA   B 3   ? 0.1752 0.1851 0.2297 -0.0022 -0.0226 0.0275  9   ALA   C CB  
1108 N N   . ILE   B 4   ? 0.1394 0.1444 0.1791 0.0004  -0.0165 0.0201  10  ILE   C N   
1109 C CA  . ILE   B 4   ? 0.1350 0.1370 0.1701 0.0007  -0.0145 0.0181  10  ILE   C CA  
1110 C C   . ILE   B 4   ? 0.1363 0.1385 0.1798 -0.0003 -0.0120 0.0192  10  ILE   C C   
1111 O O   . ILE   B 4   ? 0.1432 0.1474 0.1950 -0.0003 -0.0100 0.0198  10  ILE   C O   
1112 C CB  . ILE   B 4   ? 0.1347 0.1358 0.1649 0.0022  -0.0119 0.0152  10  ILE   C CB  
1113 C CG1 . ILE   B 4   ? 0.1513 0.1533 0.1763 0.0033  -0.0138 0.0142  10  ILE   C CG1 
1114 C CG2 . ILE   B 4   ? 0.1485 0.1461 0.1727 0.0024  -0.0102 0.0138  10  ILE   C CG2 
1115 C CD1 . ILE   B 4   ? 0.1639 0.1660 0.1875 0.0044  -0.0118 0.0116  10  ILE   C CD1 
1116 N N   . TYR   B 5   ? 0.1339 0.1339 0.1760 -0.0011 -0.0118 0.0196  11  TYR   C N   
1117 C CA  . TYR   B 5   ? 0.1449 0.1449 0.1956 -0.0021 -0.0090 0.0207  11  TYR   C CA  
1118 C C   . TYR   B 5   ? 0.1548 0.1511 0.1996 -0.0017 -0.0049 0.0187  11  TYR   C C   
1119 O O   . TYR   B 5   ? 0.1841 0.1778 0.2227 -0.0019 -0.0060 0.0186  11  TYR   C O   
1120 C CB  . TYR   B 5   ? 0.1566 0.1574 0.2126 -0.0040 -0.0125 0.0235  11  TYR   C CB  
1121 C CG  . TYR   B 5   ? 0.1502 0.1544 0.2121 -0.0047 -0.0168 0.0261  11  TYR   C CG  
1122 C CD1 . TYR   B 5   ? 0.1454 0.1528 0.2197 -0.0050 -0.0158 0.0282  11  TYR   C CD1 
1123 C CD2 . TYR   B 5   ? 0.1751 0.1791 0.2296 -0.0049 -0.0214 0.0263  11  TYR   C CD2 
1124 C CE1 . TYR   B 5   ? 0.1631 0.1735 0.2425 -0.0056 -0.0200 0.0310  11  TYR   C CE1 
1125 C CE2 . TYR   B 5   ? 0.1972 0.2036 0.2554 -0.0057 -0.0252 0.0289  11  TYR   C CE2 
1126 C CZ  . TYR   B 5   ? 0.1913 0.2011 0.2619 -0.0060 -0.0248 0.0314  11  TYR   C CZ  
1127 O OH  . TYR   B 5   ? 0.2264 0.2386 0.3005 -0.0067 -0.0288 0.0345  11  TYR   C OH  
1128 N N   . VAL   B 6   ? 0.1471 0.1427 0.1927 -0.0010 -0.0003 0.0170  12  VAL   C N   
1129 C CA  . VAL   B 6   ? 0.1616 0.1532 0.2004 -0.0006 0.0038  0.0152  12  VAL   C CA  
1130 C C   . VAL   B 6   ? 0.1676 0.1587 0.2145 -0.0012 0.0096  0.0153  12  VAL   C C   
1131 O O   . VAL   B 6   ? 0.1539 0.1470 0.2080 -0.0010 0.0115  0.0149  12  VAL   C O   
1132 C CB  . VAL   B 6   ? 0.1763 0.1662 0.2047 0.0008  0.0037  0.0123  12  VAL   C CB  
1133 C CG1 . VAL   B 6   ? 0.1798 0.1724 0.2129 0.0012  0.0043  0.0110  12  VAL   C CG1 
1134 C CG2 . VAL   B 6   ? 0.2067 0.1920 0.2270 0.0009  0.0077  0.0107  12  VAL   C CG2 
1135 N N   . GLY   B 7   ? 0.1791 0.1675 0.2257 -0.0020 0.0128  0.0160  13  GLY   C N   
1136 C CA  . GLY   B 7   ? 0.1820 0.1699 0.2373 -0.0025 0.0192  0.0163  13  GLY   C CA  
1137 C C   . GLY   B 7   ? 0.1748 0.1675 0.2462 -0.0031 0.0184  0.0186  13  GLY   C C   
1138 O O   . GLY   B 7   ? 0.1801 0.1756 0.2566 -0.0040 0.0131  0.0212  13  GLY   C O   
1139 N N   . ASN   B 8   ? 0.1683 0.1616 0.2471 -0.0027 0.0228  0.0177  14  ASN   C N   
1140 C CA  . ASN   B 8   ? 0.1764 0.1744 0.2711 -0.0029 0.0217  0.0203  14  ASN   C CA  
1141 C C   . ASN   B 8   ? 0.1640 0.1640 0.2583 -0.0019 0.0189  0.0193  14  ASN   C C   
1142 O O   . ASN   B 8   ? 0.1696 0.1719 0.2753 -0.0016 0.0208  0.0201  14  ASN   C O   
1143 C CB  . ASN   B 8   ? 0.1995 0.1974 0.3071 -0.0031 0.0290  0.0207  14  ASN   C CB  
1144 C CG  . ASN   B 8   ? 0.2841 0.2816 0.3969 -0.0044 0.0306  0.0231  14  ASN   C CG  
1145 O OD1 . ASN   B 8   ? 0.3331 0.3345 0.4590 -0.0054 0.0276  0.0266  14  ASN   C OD1 
1146 N ND2 . ASN   B 8   ? 0.3040 0.2967 0.4064 -0.0046 0.0349  0.0214  14  ASN   C ND2 
1147 N N   . TYR   B 9   ? 0.1485 0.1480 0.2308 -0.0015 0.0143  0.0182  15  TYR   C N   
1148 C CA  . TYR   B 9   ? 0.1425 0.1440 0.2241 -0.0007 0.0115  0.0175  15  TYR   C CA  
1149 C C   . TYR   B 9   ? 0.1338 0.1378 0.2128 -0.0010 0.0044  0.0197  15  TYR   C C   
1150 O O   . TYR   B 9   ? 0.1446 0.1473 0.2160 -0.0014 0.0017  0.0200  15  TYR   C O   
1151 C CB  . TYR   B 9   ? 0.1516 0.1499 0.2208 0.0002  0.0132  0.0133  15  TYR   C CB  
1152 C CG  . TYR   B 9   ? 0.1712 0.1659 0.2398 0.0003  0.0202  0.0104  15  TYR   C CG  
1153 C CD1 . TYR   B 9   ? 0.1932 0.1886 0.2724 0.0005  0.0242  0.0099  15  TYR   C CD1 
1154 C CD2 . TYR   B 9   ? 0.1955 0.1857 0.2520 0.0003  0.0227  0.0079  15  TYR   C CD2 
1155 C CE1 . TYR   B 9   ? 0.2216 0.2129 0.2993 0.0006  0.0311  0.0067  15  TYR   C CE1 
1156 C CE2 . TYR   B 9   ? 0.2347 0.2207 0.2884 0.0003  0.0291  0.0050  15  TYR   C CE2 
1157 C CZ  . TYR   B 9   ? 0.2599 0.2465 0.3241 0.0004  0.0335  0.0041  15  TYR   C CZ  
1158 O OH  . TYR   B 9   ? 0.3278 0.3097 0.3891 0.0003  0.0404  0.0008  15  TYR   C OH  
1159 N N   . ARG   B 10  ? 0.1160 0.1230 0.2002 -0.0008 0.0018  0.0212  16  ARG   C N   
1160 C CA  . ARG   B 10  ? 0.1220 0.1309 0.2025 -0.0010 -0.0043 0.0231  16  ARG   C CA  
1161 C C   . ARG   B 10  ? 0.1204 0.1295 0.1968 0.0001  -0.0041 0.0211  16  ARG   C C   
1162 O O   . ARG   B 10  ? 0.1333 0.1433 0.2171 0.0005  -0.0016 0.0209  16  ARG   C O   
1163 C CB  . ARG   B 10  ? 0.1262 0.1385 0.2184 -0.0020 -0.0076 0.0275  16  ARG   C CB  
1164 C CG  . ARG   B 10  ? 0.1378 0.1519 0.2268 -0.0022 -0.0131 0.0297  16  ARG   C CG  
1165 C CD  . ARG   B 10  ? 0.1351 0.1520 0.2340 -0.0035 -0.0173 0.0343  16  ARG   C CD  
1166 N NE  . ARG   B 10  ? 0.1596 0.1785 0.2601 -0.0033 -0.0202 0.0368  16  ARG   C NE  
1167 C CZ  . ARG   B 10  ? 0.1878 0.2067 0.2807 -0.0040 -0.0252 0.0385  16  ARG   C CZ  
1168 N NH1 . ARG   B 10  ? 0.1989 0.2156 0.2815 -0.0048 -0.0278 0.0373  16  ARG   C NH1 
1169 N NH2 . ARG   B 10  ? 0.1874 0.2078 0.2823 -0.0038 -0.0272 0.0411  16  ARG   C NH2 
1170 N N   . VAL   B 11  ? 0.1229 0.1309 0.1880 0.0006  -0.0064 0.0196  17  VAL   C N   
1171 C CA  . VAL   B 11  ? 0.1078 0.1164 0.1694 0.0015  -0.0065 0.0178  17  VAL   C CA  
1172 C C   . VAL   B 11  ? 0.1212 0.1319 0.1818 0.0014  -0.0107 0.0203  17  VAL   C C   
1173 O O   . VAL   B 11  ? 0.1305 0.1404 0.1843 0.0011  -0.0136 0.0210  17  VAL   C O   
1174 C CB  . VAL   B 11  ? 0.1229 0.1289 0.1732 0.0023  -0.0059 0.0143  17  VAL   C CB  
1175 C CG1 . VAL   B 11  ? 0.1496 0.1564 0.1985 0.0031  -0.0058 0.0124  17  VAL   C CG1 
1176 C CG2 . VAL   B 11  ? 0.1415 0.1444 0.1897 0.0023  -0.0020 0.0122  17  VAL   C CG2 
1177 N N   . VAL   B 12  ? 0.1026 0.1154 0.1694 0.0015  -0.0108 0.0217  18  VAL   C N   
1178 C CA  A VAL   B 12  ? 0.1001 0.1146 0.1654 0.0013  -0.0144 0.0245  18  VAL   C CA  
1179 C CA  B VAL   B 12  ? 0.1199 0.1343 0.1852 0.0013  -0.0144 0.0246  18  VAL   C CA  
1180 C C   . VAL   B 12  ? 0.1143 0.1297 0.1799 0.0021  -0.0132 0.0235  18  VAL   C C   
1181 O O   . VAL   B 12  ? 0.1113 0.1264 0.1807 0.0025  -0.0101 0.0211  18  VAL   C O   
1182 C CB  A VAL   B 12  ? 0.0991 0.1154 0.1734 0.0003  -0.0167 0.0291  18  VAL   C CB  
1183 C CB  B VAL   B 12  ? 0.1570 0.1733 0.2325 0.0003  -0.0162 0.0289  18  VAL   C CB  
1184 C CG1 A VAL   B 12  ? 0.1310 0.1467 0.2041 -0.0008 -0.0193 0.0305  18  VAL   C CG1 
1185 C CG1 B VAL   B 12  ? 0.1636 0.1811 0.2375 -0.0003 -0.0202 0.0325  18  VAL   C CG1 
1186 C CG2 A VAL   B 12  ? 0.0639 0.0816 0.1508 0.0005  -0.0136 0.0297  18  VAL   C CG2 
1187 C CG2 B VAL   B 12  ? 0.1966 0.2122 0.2734 -0.0007 -0.0173 0.0297  18  VAL   C CG2 
1188 N N   . ASN   B 13  ? 0.1172 0.1335 0.1795 0.0020  -0.0155 0.0255  19  ASN   C N   
1189 C CA  . ASN   B 13  ? 0.1082 0.1258 0.1728 0.0025  -0.0144 0.0254  19  ASN   C CA  
1190 C C   . ASN   B 13  ? 0.1071 0.1260 0.1837 0.0021  -0.0133 0.0279  19  ASN   C C   
1191 O O   . ASN   B 13  ? 0.1098 0.1295 0.1909 0.0014  -0.0154 0.0317  19  ASN   C O   
1192 C CB  . ASN   B 13  ? 0.1133 0.1313 0.1724 0.0024  -0.0166 0.0279  19  ASN   C CB  
1193 C CG  . ASN   B 13  ? 0.1200 0.1365 0.1684 0.0030  -0.0172 0.0256  19  ASN   C CG  
1194 O OD1 . ASN   B 13  ? 0.1348 0.1497 0.1772 0.0025  -0.0193 0.0262  19  ASN   C OD1 
1195 N ND2 . ASN   B 13  ? 0.1241 0.1410 0.1708 0.0040  -0.0154 0.0229  19  ASN   C ND2 
1196 N N   . ARG   B 14  ? 0.1080 0.1271 0.1900 0.0026  -0.0104 0.0258  20  ARG   C N   
1197 C CA  . ARG   B 14  ? 0.1047 0.1246 0.1987 0.0024  -0.0088 0.0278  20  ARG   C CA  
1198 C C   . ARG   B 14  ? 0.1215 0.1430 0.2190 0.0020  -0.0114 0.0333  20  ARG   C C   
1199 O O   . ARG   B 14  ? 0.1184 0.1407 0.2247 0.0017  -0.0122 0.0368  20  ARG   C O   
1200 C CB  . ARG   B 14  ? 0.0927 0.1120 0.1906 0.0027  -0.0054 0.0243  20  ARG   C CB  
1201 C CG  . ARG   B 14  ? 0.1010 0.1201 0.2120 0.0026  -0.0029 0.0255  20  ARG   C CG  
1202 C CD  . ARG   B 14  ? 0.1117 0.1296 0.2254 0.0027  0.0001  0.0217  20  ARG   C CD  
1203 N NE  . ARG   B 14  ? 0.1217 0.1386 0.2474 0.0027  0.0035  0.0215  20  ARG   C NE  
1204 C CZ  . ARG   B 14  ? 0.1315 0.1494 0.2671 0.0027  0.0036  0.0251  20  ARG   C CZ  
1205 N NH1 . ARG   B 14  ? 0.1434 0.1633 0.2777 0.0026  0.0004  0.0297  20  ARG   C NH1 
1206 N NH2 . ARG   B 14  ? 0.1243 0.1406 0.2708 0.0028  0.0071  0.0243  20  ARG   C NH2 
1207 N N   . HIS   B 15  ? 0.1257 0.1475 0.2161 0.0020  -0.0129 0.0343  21  HIS   C N   
1208 C CA  . HIS   B 15  ? 0.1263 0.1490 0.2183 0.0014  -0.0152 0.0396  21  HIS   C CA  
1209 C C   . HIS   B 15  ? 0.1334 0.1561 0.2222 0.0006  -0.0194 0.0434  21  HIS   C C   
1210 O O   . HIS   B 15  ? 0.1539 0.1771 0.2445 -0.0001 -0.0218 0.0483  21  HIS   C O   
1211 C CB  . HIS   B 15  ? 0.1233 0.1461 0.2089 0.0016  -0.0146 0.0396  21  HIS   C CB  
1212 C CG  . HIS   B 15  ? 0.1275 0.1493 0.2003 0.0017  -0.0161 0.0384  21  HIS   C CG  
1213 N ND1 . HIS   B 15  ? 0.1381 0.1594 0.2055 0.0024  -0.0147 0.0336  21  HIS   C ND1 
1214 C CD2 . HIS   B 15  ? 0.1338 0.1547 0.1986 0.0011  -0.0186 0.0415  21  HIS   C CD2 
1215 C CE1 . HIS   B 15  ? 0.1504 0.1705 0.2076 0.0024  -0.0162 0.0338  21  HIS   C CE1 
1216 N NE2 . HIS   B 15  ? 0.1419 0.1615 0.1966 0.0015  -0.0183 0.0382  21  HIS   C NE2 
1217 N N   . LEU   B 16  ? 0.1216 0.1434 0.2057 0.0004  -0.0204 0.0413  22  LEU   C N   
1218 C CA  . LEU   B 16  ? 0.1371 0.1588 0.2191 -0.0008 -0.0247 0.0444  22  LEU   C CA  
1219 C C   . LEU   B 16  ? 0.1481 0.1707 0.2404 -0.0011 -0.0248 0.0450  22  LEU   C C   
1220 O O   . LEU   B 16  ? 0.1563 0.1789 0.2480 -0.0021 -0.0284 0.0470  22  LEU   C O   
1221 C CB  . LEU   B 16  ? 0.1510 0.1707 0.2196 -0.0011 -0.0262 0.0419  22  LEU   C CB  
1222 C CG  . LEU   B 16  ? 0.1657 0.1843 0.2245 -0.0008 -0.0259 0.0416  22  LEU   C CG  
1223 C CD1 . LEU   B 16  ? 0.1752 0.1915 0.2218 -0.0008 -0.0266 0.0387  22  LEU   C CD1 
1224 C CD2 . LEU   B 16  ? 0.1615 0.1802 0.2192 -0.0017 -0.0286 0.0468  22  LEU   C CD2 
1225 N N   . ALA   B 17  ? 0.1441 0.1671 0.2457 -0.0002 -0.0206 0.0429  23  ALA   C N   
1226 C CA  . ALA   B 17  ? 0.1477 0.1713 0.2596 -0.0003 -0.0193 0.0431  23  ALA   C CA  
1227 C C   . ALA   B 17  ? 0.1584 0.1841 0.2807 -0.0010 -0.0229 0.0490  23  ALA   C C   
1228 O O   . ALA   B 17  ? 0.1608 0.1874 0.2867 -0.0010 -0.0244 0.0528  23  ALA   C O   
1229 C CB  . ALA   B 17  ? 0.1573 0.1803 0.2765 0.0008  -0.0136 0.0396  23  ALA   C CB  
1230 N N   . THR   B 18  ? 0.1612 0.1877 0.2887 -0.0017 -0.0245 0.0502  24  THR   C N   
1231 C CA  . THR   B 18  ? 0.1601 0.1889 0.2990 -0.0025 -0.0286 0.0561  24  THR   C CA  
1232 C C   . THR   B 18  ? 0.1568 0.1871 0.3133 -0.0014 -0.0243 0.0569  24  THR   C C   
1233 O O   . THR   B 18  ? 0.1644 0.1933 0.3230 -0.0004 -0.0182 0.0524  24  THR   C O   
1234 C CB  . THR   B 18  ? 0.1702 0.1994 0.3074 -0.0040 -0.0326 0.0570  24  THR   C CB  
1235 O OG1 . THR   B 18  ? 0.1634 0.1922 0.3054 -0.0036 -0.0279 0.0534  24  THR   C OG1 
1236 C CG2 . THR   B 18  ? 0.1870 0.2141 0.3071 -0.0051 -0.0363 0.0557  24  THR   C CG2 
1237 N N   . HIS   B 19  ? 0.1671 0.2000 0.3371 -0.0018 -0.0278 0.0627  25  HIS   C N   
1238 C CA  . HIS   B 19  ? 0.1800 0.2142 0.3682 -0.0007 -0.0236 0.0637  25  HIS   C CA  
1239 C C   . HIS   B 19  ? 0.1521 0.1859 0.3438 -0.0006 -0.0192 0.0599  25  HIS   C C   
1240 O O   . HIS   B 19  ? 0.1558 0.1882 0.3540 0.0006  -0.0122 0.0565  25  HIS   C O   
1241 C CB  . HIS   B 19  ? 0.1997 0.2371 0.4021 -0.0011 -0.0288 0.0710  25  HIS   C CB  
1242 C CG  . HIS   B 19  ? 0.2529 0.2920 0.4759 0.0000  -0.0245 0.0722  25  HIS   C CG  
1243 N ND1 . HIS   B 19  ? 0.2803 0.3181 0.5121 0.0017  -0.0182 0.0706  25  HIS   C ND1 
1244 C CD2 . HIS   B 19  ? 0.2841 0.3255 0.5199 -0.0004 -0.0251 0.0742  25  HIS   C CD2 
1245 C CE1 . HIS   B 19  ? 0.2886 0.3282 0.5387 0.0025  -0.0153 0.0722  25  HIS   C CE1 
1246 N NE2 . HIS   B 19  ? 0.2930 0.3349 0.5465 0.0013  -0.0190 0.0744  25  HIS   C NE2 
1247 N N   . ASN   B 20  ? 0.1629 0.1969 0.3481 -0.0021 -0.0226 0.0597  26  ASN   C N   
1248 C CA  . ASN   B 20  ? 0.1649 0.1982 0.3531 -0.0021 -0.0182 0.0565  26  ASN   C CA  
1249 C C   . ASN   B 20  ? 0.1514 0.1810 0.3289 -0.0011 -0.0116 0.0498  26  ASN   C C   
1250 O O   . ASN   B 20  ? 0.1399 0.1682 0.3230 -0.0004 -0.0052 0.0470  26  ASN   C O   
1251 C CB  . ASN   B 20  ? 0.1643 0.1981 0.3472 -0.0040 -0.0233 0.0576  26  ASN   C CB  
1252 C CG  . ASN   B 20  ? 0.2380 0.2714 0.4267 -0.0041 -0.0185 0.0552  26  ASN   C CG  
1253 O OD1 . ASN   B 20  ? 0.2703 0.3060 0.4762 -0.0039 -0.0166 0.0577  26  ASN   C OD1 
1254 N ND2 . ASN   B 20  ? 0.2702 0.3003 0.4452 -0.0042 -0.0157 0.0503  26  ASN   C ND2 
1255 N N   . ASP   B 21  ? 0.1469 0.1747 0.3089 -0.0010 -0.0130 0.0474  27  ASP   C N   
1256 C CA  . ASP   B 21  ? 0.1513 0.1759 0.3035 -0.0002 -0.0077 0.0414  27  ASP   C CA  
1257 C C   . ASP   B 21  ? 0.1404 0.1641 0.3019 0.0011  -0.0016 0.0396  27  ASP   C C   
1258 O O   . ASP   B 21  ? 0.1390 0.1601 0.2997 0.0016  0.0043  0.0353  27  ASP   C O   
1259 C CB  . ASP   B 21  ? 0.1447 0.1682 0.2816 -0.0002 -0.0106 0.0400  27  ASP   C CB  
1260 C CG  . ASP   B 21  ? 0.1599 0.1827 0.2847 -0.0012 -0.0147 0.0398  27  ASP   C CG  
1261 O OD1 . ASP   B 21  ? 0.1574 0.1792 0.2811 -0.0016 -0.0134 0.0382  27  ASP   C OD1 
1262 O OD2 . ASP   B 21  ? 0.1393 0.1623 0.2561 -0.0016 -0.0190 0.0413  27  ASP   C OD2 
1263 N N   . TRP   B 22  ? 0.1443 0.1695 0.3139 0.0015  -0.0031 0.0429  28  TRP   C N   
1264 C CA  . TRP   B 22  ? 0.1428 0.1669 0.3221 0.0027  0.0025  0.0412  28  TRP   C CA  
1265 C C   . TRP   B 22  ? 0.1380 0.1621 0.3325 0.0032  0.0074  0.0415  28  TRP   C C   
1266 O O   . TRP   B 22  ? 0.1446 0.1659 0.3423 0.0040  0.0143  0.0373  28  TRP   C O   
1267 C CB  . TRP   B 22  ? 0.1326 0.1581 0.3177 0.0030  -0.0004 0.0452  28  TRP   C CB  
1268 C CG  . TRP   B 22  ? 0.1389 0.1632 0.3110 0.0029  -0.0016 0.0431  28  TRP   C CG  
1269 C CD1 . TRP   B 22  ? 0.1659 0.1913 0.3284 0.0022  -0.0071 0.0457  28  TRP   C CD1 
1270 C CD2 . TRP   B 22  ? 0.1298 0.1514 0.2977 0.0033  0.0029  0.0378  28  TRP   C CD2 
1271 N NE1 . TRP   B 22  ? 0.1594 0.1834 0.3132 0.0024  -0.0059 0.0426  28  TRP   C NE1 
1272 C CE2 . TRP   B 22  ? 0.1466 0.1684 0.3034 0.0030  -0.0003 0.0377  28  TRP   C CE2 
1273 C CE3 . TRP   B 22  ? 0.1572 0.1760 0.3295 0.0039  0.0092  0.0331  28  TRP   C CE3 
1274 C CZ2 . TRP   B 22  ? 0.1430 0.1630 0.2955 0.0032  0.0022  0.0338  28  TRP   C CZ2 
1275 C CZ3 . TRP   B 22  ? 0.1709 0.1873 0.3368 0.0039  0.0113  0.0286  28  TRP   C CZ3 
1276 C CH2 . TRP   B 22  ? 0.1573 0.1747 0.3137 0.0035  0.0075  0.0291  28  TRP   C CH2 
1277 N N   . ALA   B 23  ? 0.1340 0.1612 0.3374 0.0027  0.0042  0.0460  29  ALA   C N   
1278 C CA  . ALA   B 23  ? 0.1478 0.1757 0.3675 0.0032  0.0088  0.0470  29  ALA   C CA  
1279 C C   . ALA   B 23  ? 0.1661 0.1914 0.3799 0.0029  0.0144  0.0421  29  ALA   C C   
1280 O O   . ALA   B 23  ? 0.1794 0.2041 0.4049 0.0035  0.0204  0.0414  29  ALA   C O   
1281 C CB  . ALA   B 23  ? 0.1431 0.1756 0.3752 0.0024  0.0026  0.0538  29  ALA   C CB  
1282 N N   . ASN   B 24  ? 0.1632 0.1864 0.3587 0.0022  0.0128  0.0388  30  ASN   C N   
1283 C CA  . ASN   B 24  ? 0.1626 0.1827 0.3503 0.0019  0.0176  0.0345  30  ASN   C CA  
1284 C C   . ASN   B 24  ? 0.1559 0.1720 0.3264 0.0022  0.0196  0.0288  30  ASN   C C   
1285 O O   . ASN   B 24  ? 0.1414 0.1555 0.2985 0.0016  0.0192  0.0264  30  ASN   C O   
1286 C CB  . ASN   B 24  ? 0.1586 0.1805 0.3424 0.0005  0.0127  0.0369  30  ASN   C CB  
1287 C CG  . ASN   B 24  ? 0.1916 0.2173 0.3935 0.0001  0.0112  0.0420  30  ASN   C CG  
1288 O OD1 . ASN   B 24  ? 0.1916 0.2169 0.4034 0.0003  0.0171  0.0414  30  ASN   C OD1 
1289 N ND2 . ASN   B 24  ? 0.1882 0.2176 0.3952 -0.0006 0.0035  0.0472  30  ASN   C ND2 
1290 N N   . LEU   B 25  ? 0.1515 0.1664 0.3226 0.0029  0.0212  0.0271  31  LEU   C N   
1291 C CA  . LEU   B 25  ? 0.1464 0.1583 0.3027 0.0030  0.0216  0.0223  31  LEU   C CA  
1292 C C   . LEU   B 25  ? 0.1679 0.1750 0.3156 0.0030  0.0278  0.0166  31  LEU   C C   
1293 O O   . LEU   B 25  ? 0.1854 0.1903 0.3409 0.0033  0.0344  0.0149  31  LEU   C O   
1294 C CB  . LEU   B 25  ? 0.1425 0.1545 0.3045 0.0036  0.0219  0.0222  31  LEU   C CB  
1295 C CG  . LEU   B 25  ? 0.1493 0.1589 0.2986 0.0035  0.0217  0.0177  31  LEU   C CG  
1296 C CD1 . LEU   B 25  ? 0.1357 0.1474 0.2739 0.0030  0.0152  0.0194  31  LEU   C CD1 
1297 C CD2 . LEU   B 25  ? 0.1631 0.1723 0.3205 0.0039  0.0232  0.0174  31  LEU   C CD2 
1298 N N   . VAL   B 26  ? 0.1632 0.1684 0.2945 0.0026  0.0257  0.0137  32  VAL   C N   
1299 C CA  . VAL   B 26  ? 0.1720 0.1722 0.2923 0.0024  0.0304  0.0084  32  VAL   C CA  
1300 C C   . VAL   B 26  ? 0.1872 0.1854 0.2999 0.0025  0.0299  0.0045  32  VAL   C C   
1301 O O   . VAL   B 26  ? 0.2078 0.2019 0.3189 0.0024  0.0350  0.0001  32  VAL   C O   
1302 C CB  . VAL   B 26  ? 0.1868 0.1861 0.2948 0.0020  0.0284  0.0082  32  VAL   C CB  
1303 C CG1 . VAL   B 26  ? 0.2080 0.2019 0.3025 0.0018  0.0323  0.0031  32  VAL   C CG1 
1304 C CG2 . VAL   B 26  ? 0.1862 0.1871 0.3024 0.0016  0.0293  0.0118  32  VAL   C CG2 
1305 N N   . TRP   B 27  ? 0.1567 0.1576 0.2647 0.0025  0.0239  0.0059  33  TRP   C N   
1306 C CA  . TRP   B 27  ? 0.1570 0.1566 0.2580 0.0024  0.0228  0.0023  33  TRP   C CA  
1307 C C   . TRP   B 27  ? 0.1453 0.1489 0.2472 0.0025  0.0170  0.0056  33  TRP   C C   
1308 O O   . TRP   B 27  ? 0.1502 0.1565 0.2507 0.0026  0.0132  0.0092  33  TRP   C O   
1309 C CB  . TRP   B 27  ? 0.1731 0.1692 0.2583 0.0020  0.0229  -0.0017 33  TRP   C CB  
1310 C CG  . TRP   B 27  ? 0.1824 0.1779 0.2595 0.0018  0.0200  -0.0047 33  TRP   C CG  
1311 C CD1 . TRP   B 27  ? 0.2106 0.2031 0.2863 0.0012  0.0222  -0.0092 33  TRP   C CD1 
1312 C CD2 . TRP   B 27  ? 0.1730 0.1712 0.2434 0.0020  0.0143  -0.0035 33  TRP   C CD2 
1313 N NE1 . TRP   B 27  ? 0.2207 0.2141 0.2895 0.0010  0.0178  -0.0107 33  TRP   C NE1 
1314 C CE2 . TRP   B 27  ? 0.1903 0.1873 0.2562 0.0016  0.0133  -0.0071 33  TRP   C CE2 
1315 C CE3 . TRP   B 27  ? 0.1754 0.1765 0.2434 0.0024  0.0103  0.0002  33  TRP   C CE3 
1316 C CZ2 . TRP   B 27  ? 0.1964 0.1955 0.2562 0.0018  0.0085  -0.0069 33  TRP   C CZ2 
1317 C CZ3 . TRP   B 27  ? 0.1901 0.1927 0.2511 0.0027  0.0061  0.0000  33  TRP   C CZ3 
1318 C CH2 . TRP   B 27  ? 0.1873 0.1893 0.2454 0.0025  0.0053  -0.0032 33  TRP   C CH2 
1319 N N   . GLU   B 28  ? 0.1377 0.1416 0.2419 0.0025  0.0166  0.0044  34  GLU   C N   
1320 C CA  . GLU   B 28  ? 0.1466 0.1539 0.2508 0.0026  0.0118  0.0073  34  GLU   C CA  
1321 C C   . GLU   B 28  ? 0.1487 0.1552 0.2499 0.0023  0.0115  0.0039  34  GLU   C C   
1322 O O   . GLU   B 28  ? 0.1460 0.1495 0.2496 0.0019  0.0150  0.0000  34  GLU   C O   
1323 C CB  . GLU   B 28  ? 0.1576 0.1679 0.2740 0.0028  0.0106  0.0126  34  GLU   C CB  
1324 C CG  . GLU   B 28  ? 0.1526 0.1618 0.2820 0.0030  0.0148  0.0124  34  GLU   C CG  
1325 C CD  . GLU   B 28  ? 0.1771 0.1858 0.3095 0.0027  0.0152  0.0108  34  GLU   C CD  
1326 O OE1 . GLU   B 28  ? 0.2026 0.2085 0.3420 0.0027  0.0196  0.0081  34  GLU   C OE1 
1327 O OE2 . GLU   B 28  ? 0.1556 0.1664 0.2839 0.0026  0.0115  0.0123  34  GLU   C OE2 
1328 N N   . ASP   B 29  ? 0.1310 0.1399 0.2272 0.0023  0.0075  0.0051  35  ASP   C N   
1329 C CA  . ASP   B 29  ? 0.1393 0.1479 0.2340 0.0019  0.0069  0.0022  35  ASP   C CA  
1330 C C   . ASP   B 29  ? 0.1371 0.1494 0.2337 0.0022  0.0036  0.0060  35  ASP   C C   
1331 O O   . ASP   B 29  ? 0.1313 0.1451 0.2205 0.0026  0.0008  0.0074  35  ASP   C O   
1332 C CB  . ASP   B 29  ? 0.1560 0.1625 0.2389 0.0017  0.0060  -0.0023 35  ASP   C CB  
1333 C CG  . ASP   B 29  ? 0.2069 0.2132 0.2886 0.0011  0.0048  -0.0057 35  ASP   C CG  
1334 O OD1 . ASP   B 29  ? 0.2254 0.2344 0.3126 0.0010  0.0034  -0.0037 35  ASP   C OD1 
1335 O OD2 . ASP   B 29  ? 0.2119 0.2153 0.2864 0.0005  0.0050  -0.0101 35  ASP   C OD2 
1336 N N   . SER   B 30  ? 0.1261 0.1394 0.2321 0.0019  0.0044  0.0079  36  SER   C N   
1337 C CA  A SER   B 30  ? 0.1332 0.1496 0.2409 0.0021  0.0021  0.0119  36  SER   C CA  
1338 C CA  B SER   B 30  ? 0.1287 0.1451 0.2361 0.0021  0.0020  0.0119  36  SER   C CA  
1339 C C   . SER   B 30  ? 0.1350 0.1524 0.2360 0.0020  0.0003  0.0096  36  SER   C C   
1340 O O   . SER   B 30  ? 0.1311 0.1507 0.2285 0.0024  -0.0018 0.0125  36  SER   C O   
1341 C CB  A SER   B 30  ? 0.1617 0.1783 0.2812 0.0017  0.0037  0.0141  36  SER   C CB  
1342 C CB  B SER   B 30  ? 0.1483 0.1651 0.2675 0.0018  0.0035  0.0146  36  SER   C CB  
1343 O OG  A SER   B 30  ? 0.1819 0.2008 0.3025 0.0016  0.0022  0.0171  36  SER   C OG  
1344 O OG  B SER   B 30  ? 0.1541 0.1689 0.2778 0.0011  0.0059  0.0102  36  SER   C OG  
1345 N N   . SER   B 31  ? 0.1309 0.1467 0.2304 0.0014  0.0010  0.0045  37  SER   C N   
1346 C CA  . SER   B 31  ? 0.1474 0.1646 0.2422 0.0013  -0.0012 0.0026  37  SER   C CA  
1347 C C   . SER   B 31  ? 0.1444 0.1622 0.2290 0.0022  -0.0035 0.0029  37  SER   C C   
1348 O O   . SER   B 31  ? 0.1513 0.1713 0.2334 0.0026  -0.0054 0.0031  37  SER   C O   
1349 C CB  . SER   B 31  ? 0.1826 0.1977 0.2776 0.0003  -0.0008 -0.0028 37  SER   C CB  
1350 O OG  . SER   B 31  ? 0.2598 0.2721 0.3461 0.0003  -0.0010 -0.0064 37  SER   C OG  
1351 N N   . ARG   B 32  ? 0.1230 0.1391 0.2024 0.0026  -0.0033 0.0031  38  ARG   C N   
1352 C CA  . ARG   B 32  ? 0.1218 0.1381 0.1919 0.0035  -0.0054 0.0036  38  ARG   C CA  
1353 C C   . ARG   B 32  ? 0.1205 0.1380 0.1900 0.0040  -0.0062 0.0081  38  ARG   C C   
1354 O O   . ARG   B 32  ? 0.1179 0.1352 0.1801 0.0046  -0.0077 0.0087  38  ARG   C O   
1355 C CB  . ARG   B 32  ? 0.1472 0.1602 0.2111 0.0034  -0.0045 0.0008  38  ARG   C CB  
1356 C CG  . ARG   B 32  ? 0.1629 0.1738 0.2240 0.0027  -0.0044 -0.0041 38  ARG   C CG  
1357 C CD  . ARG   B 32  ? 0.1464 0.1533 0.2002 0.0025  -0.0030 -0.0066 38  ARG   C CD  
1358 N NE  . ARG   B 32  ? 0.1323 0.1389 0.1772 0.0034  -0.0050 -0.0056 38  ARG   C NE  
1359 C CZ  . ARG   B 32  ? 0.1487 0.1521 0.1847 0.0033  -0.0051 -0.0079 38  ARG   C CZ  
1360 N NH1 . ARG   B 32  ? 0.1528 0.1527 0.1863 0.0024  -0.0033 -0.0116 38  ARG   C NH1 
1361 N NH2 . ARG   B 32  ? 0.1464 0.1496 0.1753 0.0042  -0.0071 -0.0066 38  ARG   C NH2 
1362 N N   . ASP   B 33  ? 0.1035 0.1218 0.1806 0.0036  -0.0052 0.0114  39  ASP   C N   
1363 C CA  . ASP   B 33  ? 0.1040 0.1231 0.1804 0.0037  -0.0066 0.0158  39  ASP   C CA  
1364 C C   . ASP   B 33  ? 0.1071 0.1246 0.1795 0.0037  -0.0069 0.0155  39  ASP   C C   
1365 O O   . ASP   B 33  ? 0.1104 0.1280 0.1781 0.0038  -0.0090 0.0178  39  ASP   C O   
1366 C CB  . ASP   B 33  ? 0.1130 0.1336 0.1842 0.0041  -0.0084 0.0179  39  ASP   C CB  
1367 C CG  . ASP   B 33  ? 0.1162 0.1369 0.1858 0.0038  -0.0101 0.0225  39  ASP   C CG  
1368 O OD1 . ASP   B 33  ? 0.1197 0.1409 0.1965 0.0032  -0.0101 0.0255  39  ASP   C OD1 
1369 O OD2 . ASP   B 33  ? 0.1257 0.1461 0.1874 0.0041  -0.0117 0.0231  39  ASP   C OD2 
1370 N N   . LEU   B 34  ? 0.0977 0.1133 0.1725 0.0035  -0.0046 0.0129  40  LEU   C N   
1371 C CA  . LEU   B 34  ? 0.1124 0.1264 0.1843 0.0034  -0.0043 0.0129  40  LEU   C CA  
1372 C C   . LEU   B 34  ? 0.1132 0.1267 0.1944 0.0030  -0.0018 0.0139  40  LEU   C C   
1373 O O   . LEU   B 34  ? 0.1230 0.1359 0.2110 0.0029  0.0008  0.0126  40  LEU   C O   
1374 C CB  . LEU   B 34  ? 0.1193 0.1307 0.1829 0.0036  -0.0034 0.0086  40  LEU   C CB  
1375 C CG  . LEU   B 34  ? 0.1280 0.1396 0.1822 0.0043  -0.0060 0.0077  40  LEU   C CG  
1376 C CD1 . LEU   B 34  ? 0.1411 0.1497 0.1878 0.0044  -0.0052 0.0040  40  LEU   C CD1 
1377 C CD2 . LEU   B 34  ? 0.1379 0.1498 0.1885 0.0044  -0.0082 0.0107  40  LEU   C CD2 
1378 N N   . LEU   B 35  ? 0.1034 0.1169 0.1855 0.0028  -0.0024 0.0162  41  LEU   C N   
1379 C CA  . LEU   B 35  ? 0.1068 0.1199 0.1986 0.0026  0.0004  0.0172  41  LEU   C CA  
1380 C C   . LEU   B 35  ? 0.1186 0.1305 0.2067 0.0023  0.0007  0.0170  41  LEU   C C   
1381 O O   . LEU   B 35  ? 0.1248 0.1371 0.2066 0.0021  -0.0026 0.0185  41  LEU   C O   
1382 C CB  . LEU   B 35  ? 0.1146 0.1305 0.2170 0.0024  -0.0015 0.0223  41  LEU   C CB  
1383 C CG  . LEU   B 35  ? 0.1234 0.1396 0.2387 0.0023  0.0011  0.0241  41  LEU   C CG  
1384 C CD1 . LEU   B 35  ? 0.1413 0.1594 0.2684 0.0025  0.0008  0.0276  41  LEU   C CD1 
1385 C CD2 . LEU   B 35  ? 0.1143 0.1314 0.2305 0.0017  -0.0010 0.0268  41  LEU   C CD2 
1386 N N   . VAL   B 36  ? 0.1208 0.1306 0.2127 0.0023  0.0051  0.0151  42  VAL   C N   
1387 C CA  . VAL   B 36  ? 0.1199 0.1284 0.2099 0.0019  0.0063  0.0153  42  VAL   C CA  
1388 C C   . VAL   B 36  ? 0.1191 0.1285 0.2228 0.0017  0.0091  0.0176  42  VAL   C C   
1389 O O   . VAL   B 36  ? 0.1328 0.1414 0.2442 0.0020  0.0132  0.0163  42  VAL   C O   
1390 C CB  . VAL   B 36  ? 0.1348 0.1392 0.2151 0.0020  0.0098  0.0106  42  VAL   C CB  
1391 C CG1 . VAL   B 36  ? 0.1491 0.1517 0.2278 0.0016  0.0120  0.0110  42  VAL   C CG1 
1392 C CG2 . VAL   B 36  ? 0.1392 0.1429 0.2070 0.0024  0.0066  0.0086  42  VAL   C CG2 
1393 N N   . SER   B 37  ? 0.1217 0.1328 0.2293 0.0011  0.0069  0.0210  43  SER   C N   
1394 C CA  . SER   B 37  ? 0.1212 0.1337 0.2430 0.0008  0.0090  0.0237  43  SER   C CA  
1395 C C   . SER   B 37  ? 0.1386 0.1494 0.2589 0.0002  0.0114  0.0232  43  SER   C C   
1396 O O   . SER   B 37  ? 0.1427 0.1516 0.2508 -0.0001 0.0100  0.0217  43  SER   C O   
1397 C CB  . SER   B 37  ? 0.1349 0.1515 0.2652 0.0003  0.0033  0.0291  43  SER   C CB  
1398 O OG  . SER   B 37  ? 0.1454 0.1625 0.2672 -0.0006 -0.0023 0.0307  43  SER   C OG  
1399 N N   . SER   B 38  ? 0.1458 0.1574 0.2795 0.0001  0.0154  0.0247  44  SER   C N   
1400 C CA  . SER   B 38  ? 0.1563 0.1663 0.2902 -0.0006 0.0184  0.0245  44  SER   C CA  
1401 C C   . SER   B 38  ? 0.1709 0.1843 0.3113 -0.0019 0.0129  0.0291  44  SER   C C   
1402 O O   . SER   B 38  ? 0.1812 0.1983 0.3304 -0.0021 0.0081  0.0328  44  SER   C O   
1403 C CB  . SER   B 38  ? 0.1725 0.1811 0.3170 -0.0001 0.0266  0.0233  44  SER   C CB  
1404 O OG  . SER   B 38  ? 0.2194 0.2317 0.3818 0.0001  0.0261  0.0270  44  SER   C OG  
1405 N N   . THR   B 39  ? 0.1673 0.1792 0.3027 -0.0028 0.0131  0.0289  45  THR   C N   
1406 C CA  . THR   B 39  ? 0.1736 0.1880 0.3141 -0.0043 0.0077  0.0326  45  THR   C CA  
1407 C C   . THR   B 39  ? 0.2031 0.2173 0.3540 -0.0051 0.0125  0.0336  45  THR   C C   
1408 O O   . THR   B 39  ? 0.2028 0.2136 0.3506 -0.0046 0.0197  0.0308  45  THR   C O   
1409 C CB  . THR   B 39  ? 0.1809 0.1931 0.3056 -0.0050 0.0030  0.0315  45  THR   C CB  
1410 O OG1 . THR   B 39  ? 0.2030 0.2110 0.3183 -0.0047 0.0078  0.0284  45  THR   C OG1 
1411 C CG2 . THR   B 39  ? 0.1826 0.1947 0.2964 -0.0041 -0.0008 0.0302  45  THR   C CG2 
1412 N N   . THR   B 40  ? 0.2306 0.2481 0.3929 -0.0066 0.0081  0.0377  46  THR   C N   
1413 C CA  . THR   B 40  ? 0.2478 0.2656 0.4211 -0.0077 0.0121  0.0391  46  THR   C CA  
1414 C C   . THR   B 40  ? 0.2568 0.2711 0.4177 -0.0088 0.0116  0.0376  46  THR   C C   
1415 O O   . THR   B 40  ? 0.2874 0.2989 0.4478 -0.0088 0.0183  0.0362  46  THR   C O   
1416 C CB  . THR   B 40  ? 0.2948 0.3180 0.4869 -0.0089 0.0072  0.0442  46  THR   C CB  
1417 O OG1 . THR   B 40  ? 0.3498 0.3743 0.5355 -0.0104 -0.0024 0.0460  46  THR   C OG1 
1418 C CG2 . THR   B 40  ? 0.2806 0.3070 0.4860 -0.0076 0.0081  0.0460  46  THR   C CG2 
1419 N N   . ALA   B 41  ? 0.2387 0.2528 0.3892 -0.0097 0.0040  0.0378  47  ALA   C N   
1420 C CA  . ALA   B 41  ? 0.2398 0.2502 0.3790 -0.0107 0.0032  0.0365  47  ALA   C CA  
1421 C C   . ALA   B 41  ? 0.2262 0.2320 0.3470 -0.0091 0.0059  0.0324  47  ALA   C C   
1422 O O   . ALA   B 41  ? 0.2192 0.2252 0.3340 -0.0077 0.0051  0.0309  47  ALA   C O   
1423 C CB  . ALA   B 41  ? 0.2622 0.2738 0.3991 -0.0125 -0.0058 0.0385  47  ALA   C CB  
1424 N N   . GLN   B 42  ? 0.2233 0.2250 0.3355 -0.0094 0.0087  0.0310  48  GLN   C N   
1425 C CA  . GLN   B 42  ? 0.2487 0.2460 0.3438 -0.0080 0.0104  0.0277  48  GLN   C CA  
1426 C C   . GLN   B 42  ? 0.2398 0.2368 0.3243 -0.0080 0.0032  0.0272  48  GLN   C C   
1427 O O   . GLN   B 42  ? 0.2598 0.2577 0.3467 -0.0095 -0.0019 0.0290  48  GLN   C O   
1428 C CB  . GLN   B 42  ? 0.3219 0.3147 0.4123 -0.0084 0.0158  0.0271  48  GLN   C CB  
1429 C CG  . GLN   B 42  ? 0.4338 0.4255 0.5300 -0.0079 0.0244  0.0264  48  GLN   C CG  
1430 C CD  . GLN   B 42  ? 0.5739 0.5607 0.6639 -0.0083 0.0300  0.0260  48  GLN   C CD  
1431 O OE1 . GLN   B 42  ? 0.6171 0.6038 0.7139 -0.0099 0.0305  0.0283  48  GLN   C OE1 
1432 N NE2 . GLN   B 42  ? 0.6151 0.5975 0.6921 -0.0071 0.0343  0.0232  48  GLN   C NE2 
1433 N N   . GLY   B 43  ? 0.2031 0.1987 0.2764 -0.0063 0.0031  0.0247  49  GLY   C N   
1434 C CA  . GLY   B 43  ? 0.2002 0.1951 0.2628 -0.0058 -0.0023 0.0238  49  GLY   C CA  
1435 C C   . GLY   B 43  ? 0.2050 0.1952 0.2556 -0.0054 -0.0016 0.0223  49  GLY   C C   
1436 O O   . GLY   B 43  ? 0.2456 0.2329 0.2938 -0.0051 0.0034  0.0215  49  GLY   C O   
1437 N N   . CYS   B 44  ? 0.1839 0.1730 0.2265 -0.0051 -0.0061 0.0217  50  CYS   C N   
1438 C CA  . CYS   B 44  ? 0.2024 0.1871 0.2349 -0.0047 -0.0059 0.0207  50  CYS   C CA  
1439 C C   . CYS   B 44  ? 0.2178 0.2011 0.2392 -0.0027 -0.0070 0.0186  50  CYS   C C   
1440 O O   . CYS   B 44  ? 0.2510 0.2305 0.2643 -0.0020 -0.0072 0.0180  50  CYS   C O   
1441 C CB  . CYS   B 44  ? 0.2099 0.1933 0.2435 -0.0064 -0.0099 0.0220  50  CYS   C CB  
1442 S SG  . CYS   B 44  ? 0.2803 0.2659 0.3288 -0.0091 -0.0094 0.0248  50  CYS   C SG  
1443 N N   . ASP   B 45  ? 0.1803 0.1664 0.2018 -0.0016 -0.0078 0.0176  51  ASP   C N   
1444 C CA  . ASP   B 45  ? 0.1760 0.1614 0.1886 0.0002  -0.0089 0.0157  51  ASP   C CA  
1445 C C   . ASP   B 45  ? 0.1767 0.1601 0.1844 0.0013  -0.0052 0.0142  51  ASP   C C   
1446 O O   . ASP   B 45  ? 0.2000 0.1835 0.2118 0.0008  -0.0014 0.0141  51  ASP   C O   
1447 C CB  . ASP   B 45  ? 0.1794 0.1688 0.1947 0.0008  -0.0109 0.0154  51  ASP   C CB  
1448 C CG  . ASP   B 45  ? 0.2385 0.2294 0.2561 -0.0002 -0.0149 0.0168  51  ASP   C CG  
1449 O OD1 . ASP   B 45  ? 0.2400 0.2284 0.2532 -0.0007 -0.0171 0.0169  51  ASP   C OD1 
1450 O OD2 . ASP   B 45  ? 0.2017 0.1960 0.2251 -0.0006 -0.0160 0.0178  51  ASP   C OD2 
1451 N N   . THR   B 46  ? 0.1718 0.1530 0.1706 0.0027  -0.0064 0.0130  52  THR   C N   
1452 C CA  . THR   B 46  ? 0.1743 0.1532 0.1665 0.0037  -0.0042 0.0116  52  THR   C CA  
1453 C C   . THR   B 46  ? 0.1841 0.1657 0.1748 0.0050  -0.0062 0.0099  52  THR   C C   
1454 O O   . THR   B 46  ? 0.1817 0.1646 0.1713 0.0058  -0.0095 0.0099  52  THR   C O   
1455 C CB  . THR   B 46  ? 0.2133 0.1878 0.1971 0.0044  -0.0048 0.0121  52  THR   C CB  
1456 O OG1 . THR   B 46  ? 0.2378 0.2097 0.2237 0.0030  -0.0024 0.0139  52  THR   C OG1 
1457 C CG2 . THR   B 46  ? 0.2278 0.1999 0.2031 0.0055  -0.0038 0.0109  52  THR   C CG2 
1458 N N   . ILE   B 47  ? 0.1739 0.1559 0.1641 0.0050  -0.0042 0.0082  53  ILE   C N   
1459 C CA  . ILE   B 47  ? 0.1722 0.1565 0.1614 0.0060  -0.0062 0.0065  53  ILE   C CA  
1460 C C   . ILE   B 47  ? 0.1642 0.1459 0.1441 0.0072  -0.0080 0.0056  53  ILE   C C   
1461 O O   . ILE   B 47  ? 0.1765 0.1543 0.1501 0.0070  -0.0062 0.0055  53  ILE   C O   
1462 C CB  . ILE   B 47  ? 0.1802 0.1654 0.1730 0.0053  -0.0034 0.0047  53  ILE   C CB  
1463 C CG1 . ILE   B 47  ? 0.1804 0.1679 0.1834 0.0042  -0.0012 0.0059  53  ILE   C CG1 
1464 C CG2 . ILE   B 47  ? 0.1828 0.1705 0.1756 0.0060  -0.0057 0.0029  53  ILE   C CG2 
1465 C CD1 . ILE   B 47  ? 0.2135 0.2049 0.2225 0.0043  -0.0045 0.0076  53  ILE   C CD1 
1466 N N   . ALA   B 48  ? 0.1476 0.1314 0.1270 0.0085  -0.0114 0.0053  54  ALA   C N   
1467 C CA  . ALA   B 48  ? 0.1571 0.1393 0.1296 0.0098  -0.0138 0.0048  54  ALA   C CA  
1468 C C   . ALA   B 48  ? 0.1685 0.1500 0.1376 0.0093  -0.0133 0.0026  54  ALA   C C   
1469 O O   . ALA   B 48  ? 0.1548 0.1387 0.1287 0.0086  -0.0123 0.0010  54  ALA   C O   
1470 C CB  . ALA   B 48  ? 0.1686 0.1541 0.1438 0.0112  -0.0170 0.0048  54  ALA   C CB  
1471 N N   . ARG   B 49  ? 0.1654 0.1432 0.1258 0.0096  -0.0142 0.0026  55  ARG   C N   
1472 C CA  . ARG   B 49  ? 0.1687 0.1449 0.1235 0.0090  -0.0146 0.0003  55  ARG   C CA  
1473 C C   . ARG   B 49  ? 0.1819 0.1581 0.1320 0.0105  -0.0196 0.0009  55  ARG   C C   
1474 O O   . ARG   B 49  ? 0.1985 0.1708 0.1410 0.0110  -0.0204 0.0026  55  ARG   C O   
1475 C CB  . ARG   B 49  ? 0.1775 0.1485 0.1252 0.0077  -0.0104 -0.0001 55  ARG   C CB  
1476 C CG  . ARG   B 49  ? 0.1724 0.1440 0.1272 0.0065  -0.0054 -0.0001 55  ARG   C CG  
1477 C CD  . ARG   B 49  ? 0.1743 0.1492 0.1365 0.0058  -0.0043 -0.0024 55  ARG   C CD  
1478 N NE  . ARG   B 49  ? 0.1825 0.1580 0.1525 0.0049  0.0002  -0.0018 55  ARG   C NE  
1479 C CZ  . ARG   B 49  ? 0.1862 0.1653 0.1659 0.0045  0.0012  -0.0025 55  ARG   C CZ  
1480 N NH1 . ARG   B 49  ? 0.1668 0.1489 0.1491 0.0048  -0.0016 -0.0040 55  ARG   C NH1 
1481 N NH2 . ARG   B 49  ? 0.1802 0.1599 0.1677 0.0038  0.0049  -0.0014 55  ARG   C NH2 
1482 N N   . CYS   B 50  ? 0.1602 0.1407 0.1157 0.0112  -0.0227 -0.0001 56  CYS   C N   
1483 C CA  . CYS   B 50  ? 0.1634 0.1451 0.1180 0.0129  -0.0275 0.0009  56  CYS   C CA  
1484 C C   . CYS   B 50  ? 0.1506 0.1376 0.1130 0.0131  -0.0300 -0.0007 56  CYS   C C   
1485 O O   . CYS   B 50  ? 0.1599 0.1493 0.1280 0.0120  -0.0280 -0.0022 56  CYS   C O   
1486 C CB  . CYS   B 50  ? 0.1684 0.1503 0.1256 0.0145  -0.0275 0.0034  56  CYS   C CB  
1487 S SG  . CYS   B 50  ? 0.1527 0.1395 0.1208 0.0147  -0.0256 0.0034  56  CYS   C SG  
1488 N N   . ASP   B 51  ? 0.1672 0.1561 0.1309 0.0147  -0.0343 0.0002  57  ASP   C N   
1489 C CA  . ASP   B 51  ? 0.1661 0.1605 0.1389 0.0152  -0.0365 -0.0007 57  ASP   C CA  
1490 C C   . ASP   B 51  ? 0.1697 0.1666 0.1486 0.0175  -0.0370 0.0014  57  ASP   C C   
1491 O O   . ASP   B 51  ? 0.1777 0.1785 0.1630 0.0185  -0.0397 0.0014  57  ASP   C O   
1492 C CB  . ASP   B 51  ? 0.1990 0.1939 0.1699 0.0148  -0.0414 -0.0020 57  ASP   C CB  
1493 C CG  . ASP   B 51  ? 0.2308 0.2237 0.1963 0.0162  -0.0457 0.0001  57  ASP   C CG  
1494 O OD1 . ASP   B 51  ? 0.2337 0.2243 0.1967 0.0177  -0.0446 0.0025  57  ASP   C OD1 
1495 O OD2 . ASP   B 51  ? 0.3243 0.3178 0.2882 0.0158  -0.0506 -0.0006 57  ASP   C OD2 
1496 N N   . CYS   B 52  ? 0.1590 0.1540 0.1367 0.0181  -0.0342 0.0028  58  CYS   C N   
1497 C CA  . CYS   B 52  ? 0.1509 0.1476 0.1338 0.0201  -0.0338 0.0042  58  CYS   C CA  
1498 C C   . CYS   B 52  ? 0.1509 0.1527 0.1428 0.0202  -0.0330 0.0034  58  CYS   C C   
1499 O O   . CYS   B 52  ? 0.1528 0.1562 0.1472 0.0185  -0.0313 0.0021  58  CYS   C O   
1500 C CB  . CYS   B 52  ? 0.1695 0.1631 0.1497 0.0200  -0.0307 0.0053  58  CYS   C CB  
1501 S SG  . CYS   B 52  ? 0.1740 0.1613 0.1453 0.0205  -0.0313 0.0071  58  CYS   C SG  
1502 N N   . GLN   B 53  ? 0.1407 0.1446 0.1377 0.0222  -0.0338 0.0042  59  GLN   C N   
1503 C CA  . GLN   B 53  ? 0.1436 0.1518 0.1490 0.0227  -0.0321 0.0039  59  GLN   C CA  
1504 C C   . GLN   B 53  ? 0.1454 0.1525 0.1517 0.0243  -0.0294 0.0049  59  GLN   C C   
1505 O O   . GLN   B 53  ? 0.1464 0.1564 0.1588 0.0251  -0.0277 0.0049  59  GLN   C O   
1506 C CB  . GLN   B 53  ? 0.1488 0.1614 0.1617 0.0234  -0.0349 0.0036  59  GLN   C CB  
1507 C CG  . GLN   B 53  ? 0.1850 0.1991 0.1984 0.0213  -0.0370 0.0019  59  GLN   C CG  
1508 C CD  . GLN   B 53  ? 0.2105 0.2293 0.2325 0.0217  -0.0401 0.0015  59  GLN   C CD  
1509 O OE1 . GLN   B 53  ? 0.2310 0.2497 0.2515 0.0215  -0.0447 0.0012  59  GLN   C OE1 
1510 N NE2 . GLN   B 53  ? 0.1818 0.2046 0.2129 0.0221  -0.0377 0.0016  59  GLN   C NE2 
1511 N N   . THR   B 54  ? 0.1517 0.1542 0.1515 0.0246  -0.0288 0.0056  60  THR   C N   
1512 C CA  . THR   B 54  ? 0.1588 0.1591 0.1578 0.0255  -0.0260 0.0060  60  THR   C CA  
1513 C C   . THR   B 54  ? 0.1643 0.1608 0.1570 0.0237  -0.0246 0.0061  60  THR   C C   
1514 O O   . THR   B 54  ? 0.1638 0.1580 0.1519 0.0227  -0.0257 0.0064  60  THR   C O   
1515 C CB  . THR   B 54  ? 0.1925 0.1910 0.1924 0.0282  -0.0266 0.0069  60  THR   C CB  
1516 O OG1 . THR   B 54  ? 0.2248 0.2193 0.2188 0.0282  -0.0286 0.0078  60  THR   C OG1 
1517 C CG2 . THR   B 54  ? 0.1818 0.1846 0.1898 0.0301  -0.0283 0.0072  60  THR   C CG2 
1518 N N   . GLY   B 55  ? 0.1356 0.1312 0.1277 0.0233  -0.0221 0.0059  61  GLY   C N   
1519 C CA  . GLY   B 55  ? 0.1426 0.1349 0.1299 0.0214  -0.0212 0.0061  61  GLY   C CA  
1520 C C   . GLY   B 55  ? 0.1410 0.1323 0.1274 0.0210  -0.0192 0.0059  61  GLY   C C   
1521 O O   . GLY   B 55  ? 0.1577 0.1493 0.1457 0.0227  -0.0178 0.0054  61  GLY   C O   
1522 N N   . VAL   B 56  ? 0.1355 0.1250 0.1188 0.0188  -0.0189 0.0061  62  VAL   C N   
1523 C CA  . VAL   B 56  ? 0.1430 0.1306 0.1235 0.0180  -0.0177 0.0060  62  VAL   C CA  
1524 C C   . VAL   B 56  ? 0.1381 0.1280 0.1201 0.0157  -0.0180 0.0068  62  VAL   C C   
1525 O O   . VAL   B 56  ? 0.1501 0.1404 0.1331 0.0143  -0.0190 0.0074  62  VAL   C O   
1526 C CB  . VAL   B 56  ? 0.1545 0.1366 0.1298 0.0175  -0.0181 0.0057  62  VAL   C CB  
1527 C CG1 . VAL   B 56  ? 0.1682 0.1477 0.1393 0.0160  -0.0176 0.0052  62  VAL   C CG1 
1528 C CG2 . VAL   B 56  ? 0.1577 0.1370 0.1322 0.0201  -0.0177 0.0051  62  VAL   C CG2 
1529 N N   . TYR   B 57  ? 0.1306 0.1217 0.1126 0.0152  -0.0169 0.0071  63  TYR   C N   
1530 C CA  . TYR   B 57  ? 0.1265 0.1196 0.1101 0.0130  -0.0175 0.0085  63  TYR   C CA  
1531 C C   . TYR   B 57  ? 0.1377 0.1278 0.1158 0.0115  -0.0178 0.0090  63  TYR   C C   
1532 O O   . TYR   B 57  ? 0.1553 0.1427 0.1287 0.0124  -0.0164 0.0079  63  TYR   C O   
1533 C CB  . TYR   B 57  ? 0.1328 0.1308 0.1223 0.0133  -0.0164 0.0091  63  TYR   C CB  
1534 C CG  . TYR   B 57  ? 0.1373 0.1359 0.1260 0.0138  -0.0144 0.0095  63  TYR   C CG  
1535 C CD1 . TYR   B 57  ? 0.1477 0.1463 0.1367 0.0159  -0.0124 0.0083  63  TYR   C CD1 
1536 C CD2 . TYR   B 57  ? 0.1417 0.1409 0.1298 0.0121  -0.0142 0.0112  63  TYR   C CD2 
1537 C CE1 . TYR   B 57  ? 0.1597 0.1588 0.1484 0.0164  -0.0096 0.0087  63  TYR   C CE1 
1538 C CE2 . TYR   B 57  ? 0.1619 0.1614 0.1486 0.0125  -0.0118 0.0118  63  TYR   C CE2 
1539 C CZ  . TYR   B 57  ? 0.1707 0.1702 0.1577 0.0146  -0.0092 0.0104  63  TYR   C CZ  
1540 O OH  . TYR   B 57  ? 0.1904 0.1900 0.1764 0.0151  -0.0059 0.0109  63  TYR   C OH  
1541 N N   . TYR   B 58  ? 0.1402 0.1309 0.1192 0.0093  -0.0195 0.0105  64  TYR   C N   
1542 C CA  . TYR   B 58  ? 0.1421 0.1302 0.1157 0.0074  -0.0208 0.0114  64  TYR   C CA  
1543 C C   . TYR   B 58  ? 0.1467 0.1372 0.1208 0.0070  -0.0200 0.0130  64  TYR   C C   
1544 O O   . TYR   B 58  ? 0.1436 0.1379 0.1241 0.0065  -0.0203 0.0147  64  TYR   C O   
1545 C CB  . TYR   B 58  ? 0.1498 0.1369 0.1243 0.0050  -0.0239 0.0126  64  TYR   C CB  
1546 C CG  . TYR   B 58  ? 0.1725 0.1565 0.1407 0.0029  -0.0261 0.0134  64  TYR   C CG  
1547 C CD1 . TYR   B 58  ? 0.1930 0.1719 0.1527 0.0028  -0.0259 0.0114  64  TYR   C CD1 
1548 C CD2 . TYR   B 58  ? 0.1776 0.1636 0.1481 0.0008  -0.0285 0.0160  64  TYR   C CD2 
1549 C CE1 . TYR   B 58  ? 0.1943 0.1696 0.1465 0.0006  -0.0281 0.0117  64  TYR   C CE1 
1550 C CE2 . TYR   B 58  ? 0.1937 0.1766 0.1574 -0.0014 -0.0314 0.0169  64  TYR   C CE2 
1551 C CZ  . TYR   B 58  ? 0.2032 0.1806 0.1572 -0.0016 -0.0312 0.0145  64  TYR   C CZ  
1552 O OH  . TYR   B 58  ? 0.2399 0.2134 0.1856 -0.0041 -0.0342 0.0150  64  TYR   C OH  
1553 N N   . CYS   B 59  ? 0.1495 0.1370 0.1165 0.0071  -0.0188 0.0125  65  CYS   C N   
1554 C CA  . CYS   B 59  ? 0.1614 0.1500 0.1267 0.0065  -0.0176 0.0143  65  CYS   C CA  
1555 C C   . CYS   B 59  ? 0.1770 0.1619 0.1343 0.0039  -0.0204 0.0155  65  CYS   C C   
1556 O O   . CYS   B 59  ? 0.1874 0.1672 0.1354 0.0036  -0.0199 0.0138  65  CYS   C O   
1557 C CB  . CYS   B 59  ? 0.1466 0.1345 0.1097 0.0086  -0.0134 0.0127  65  CYS   C CB  
1558 S SG  . CYS   B 59  ? 0.1939 0.1823 0.1538 0.0079  -0.0108 0.0150  65  CYS   C SG  
1559 N N   . SER   B 60  ? 0.1766 0.1639 0.1377 0.0020  -0.0235 0.0185  66  SER   C N   
1560 C CA  . SER   B 60  ? 0.1909 0.1751 0.1454 -0.0007 -0.0273 0.0202  66  SER   C CA  
1561 C C   . SER   B 60  ? 0.1936 0.1743 0.1374 -0.0013 -0.0259 0.0206  66  SER   C C   
1562 O O   . SER   B 60  ? 0.2205 0.1962 0.1545 -0.0031 -0.0282 0.0200  66  SER   C O   
1563 C CB  . SER   B 60  ? 0.2108 0.1988 0.1733 -0.0023 -0.0307 0.0238  66  SER   C CB  
1564 O OG  . SER   B 60  ? 0.2667 0.2516 0.2229 -0.0050 -0.0353 0.0255  66  SER   C OG  
1565 N N   . SER   B 61  ? 0.1881 0.1710 0.1336 0.0001  -0.0220 0.0216  67  SER   C N   
1566 C CA  . SER   B 61  ? 0.2003 0.1799 0.1357 -0.0004 -0.0197 0.0223  67  SER   C CA  
1567 C C   . SER   B 61  ? 0.2257 0.1998 0.1513 0.0006  -0.0163 0.0185  67  SER   C C   
1568 O O   . SER   B 61  ? 0.2427 0.2123 0.1573 -0.0001 -0.0144 0.0185  67  SER   C O   
1569 C CB  . SER   B 61  ? 0.1969 0.1806 0.1384 0.0009  -0.0162 0.0247  67  SER   C CB  
1570 O OG  . SER   B 61  ? 0.2083 0.1948 0.1570 0.0036  -0.0119 0.0224  67  SER   C OG  
1571 N N   . ARG   B 62  ? 0.2109 0.1845 0.1397 0.0022  -0.0155 0.0153  68  ARG   C N   
1572 C CA  . ARG   B 62  ? 0.2174 0.1853 0.1379 0.0032  -0.0126 0.0115  68  ARG   C CA  
1573 C C   . ARG   B 62  ? 0.2164 0.1803 0.1335 0.0019  -0.0163 0.0094  68  ARG   C C   
1574 O O   . ARG   B 62  ? 0.2300 0.1886 0.1408 0.0026  -0.0142 0.0060  68  ARG   C O   
1575 C CB  . ARG   B 62  ? 0.2280 0.1987 0.1563 0.0067  -0.0077 0.0097  68  ARG   C CB  
1576 C CG  . ARG   B 62  ? 0.2843 0.2588 0.2169 0.0079  -0.0035 0.0115  68  ARG   C CG  
1577 C CD  . ARG   B 62  ? 0.2846 0.2541 0.2066 0.0080  0.0011  0.0106  68  ARG   C CD  
1578 N NE  . ARG   B 62  ? 0.3476 0.3206 0.2741 0.0090  0.0057  0.0126  68  ARG   C NE  
1579 C CZ  . ARG   B 62  ? 0.4197 0.3937 0.3440 0.0073  0.0053  0.0160  68  ARG   C CZ  
1580 N NH1 . ARG   B 62  ? 0.4189 0.3911 0.3370 0.0045  0.0000  0.0181  68  ARG   C NH1 
1581 N NH2 . ARG   B 62  ? 0.4299 0.4067 0.3587 0.0084  0.0101  0.0177  68  ARG   C NH2 
1582 N N   . ARG   B 63  ? 0.2209 0.1873 0.1433 0.0001  -0.0215 0.0112  69  ARG   C N   
1583 C CA  . ARG   B 63  ? 0.2256 0.1891 0.1475 -0.0011 -0.0250 0.0096  69  ARG   C CA  
1584 C C   . ARG   B 63  ? 0.2445 0.2068 0.1692 0.0015  -0.0218 0.0065  69  ARG   C C   
1585 O O   . ARG   B 63  ? 0.2650 0.2215 0.1836 0.0011  -0.0221 0.0038  69  ARG   C O   
1586 C CB  . ARG   B 63  ? 0.2401 0.1968 0.1496 -0.0041 -0.0281 0.0085  69  ARG   C CB  
1587 C CG  . ARG   B 63  ? 0.2737 0.2314 0.1804 -0.0070 -0.0325 0.0121  69  ARG   C CG  
1588 C CD  . ARG   B 63  ? 0.3338 0.2965 0.2514 -0.0083 -0.0373 0.0149  69  ARG   C CD  
1589 N NE  . ARG   B 63  ? 0.3663 0.3278 0.2793 -0.0117 -0.0430 0.0178  69  ARG   C NE  
1590 C CZ  . ARG   B 63  ? 0.3730 0.3384 0.2894 -0.0123 -0.0445 0.0219  69  ARG   C CZ  
1591 N NH1 . ARG   B 63  ? 0.3357 0.3060 0.2594 -0.0098 -0.0404 0.0234  69  ARG   C NH1 
1592 N NH2 . ARG   B 63  ? 0.3801 0.3444 0.2928 -0.0154 -0.0505 0.0248  69  ARG   C NH2 
1593 N N   . LYS   B 64  ? 0.2210 0.1882 0.1543 0.0042  -0.0189 0.0069  70  LYS   C N   
1594 C CA  . LYS   B 64  ? 0.2299 0.1960 0.1657 0.0069  -0.0160 0.0045  70  LYS   C CA  
1595 C C   . LYS   B 64  ? 0.2118 0.1836 0.1584 0.0085  -0.0164 0.0055  70  LYS   C C   
1596 O O   . LYS   B 64  ? 0.1991 0.1762 0.1518 0.0085  -0.0165 0.0076  70  LYS   C O   
1597 C CB  . LYS   B 64  ? 0.2722 0.2376 0.2056 0.0092  -0.0108 0.0032  70  LYS   C CB  
1598 C CG  . LYS   B 64  ? 0.4076 0.3655 0.3310 0.0093  -0.0085 0.0001  70  LYS   C CG  
1599 C CD  . LYS   B 64  ? 0.4983 0.4564 0.4244 0.0127  -0.0028 -0.0014 70  LYS   C CD  
1600 C CE  . LYS   B 64  ? 0.5955 0.5459 0.5111 0.0128  0.0008  -0.0044 70  LYS   C CE  
1601 N NZ  . LYS   B 64  ? 0.6635 0.6119 0.5698 0.0108  0.0022  -0.0037 70  LYS   C NZ  
1602 N N   . HIS   B 65  ? 0.1938 0.1640 0.1424 0.0098  -0.0163 0.0041  71  HIS   C N   
1603 C CA  . HIS   B 65  ? 0.1826 0.1571 0.1395 0.0115  -0.0163 0.0047  71  HIS   C CA  
1604 C C   . HIS   B 65  ? 0.2022 0.1774 0.1612 0.0146  -0.0129 0.0035  71  HIS   C C   
1605 O O   . HIS   B 65  ? 0.2464 0.2170 0.2015 0.0159  -0.0112 0.0017  71  HIS   C O   
1606 C CB  . HIS   B 65  ? 0.1795 0.1516 0.1370 0.0110  -0.0183 0.0044  71  HIS   C CB  
1607 C CG  . HIS   B 65  ? 0.1901 0.1623 0.1479 0.0081  -0.0215 0.0058  71  HIS   C CG  
1608 N ND1 . HIS   B 65  ? 0.2173 0.1936 0.1818 0.0075  -0.0226 0.0075  71  HIS   C ND1 
1609 C CD2 . HIS   B 65  ? 0.1924 0.1609 0.1452 0.0055  -0.0237 0.0057  71  HIS   C CD2 
1610 C CE1 . HIS   B 65  ? 0.1950 0.1703 0.1594 0.0048  -0.0252 0.0086  71  HIS   C CE1 
1611 N NE2 . HIS   B 65  ? 0.2253 0.1962 0.1829 0.0035  -0.0264 0.0076  71  HIS   C NE2 
1612 N N   . TYR   B 66  ? 0.1752 0.1558 0.1410 0.0159  -0.0120 0.0045  72  TYR   C N   
1613 C CA  . TYR   B 66  ? 0.1710 0.1530 0.1406 0.0188  -0.0091 0.0036  72  TYR   C CA  
1614 C C   . TYR   B 66  ? 0.1646 0.1494 0.1406 0.0204  -0.0106 0.0039  72  TYR   C C   
1615 O O   . TYR   B 66  ? 0.1629 0.1514 0.1429 0.0195  -0.0125 0.0050  72  TYR   C O   
1616 C CB  . TYR   B 66  ? 0.1854 0.1717 0.1587 0.0189  -0.0070 0.0047  72  TYR   C CB  
1617 C CG  . TYR   B 66  ? 0.1878 0.1713 0.1542 0.0178  -0.0046 0.0046  72  TYR   C CG  
1618 C CD1 . TYR   B 66  ? 0.2233 0.2031 0.1858 0.0194  -0.0007 0.0029  72  TYR   C CD1 
1619 C CD2 . TYR   B 66  ? 0.1918 0.1760 0.1555 0.0153  -0.0059 0.0064  72  TYR   C CD2 
1620 C CE1 . TYR   B 66  ? 0.2369 0.2133 0.1915 0.0182  0.0019  0.0027  72  TYR   C CE1 
1621 C CE2 . TYR   B 66  ? 0.2143 0.1955 0.1704 0.0142  -0.0041 0.0066  72  TYR   C CE2 
1622 C CZ  . TYR   B 66  ? 0.2320 0.2091 0.1829 0.0155  0.0000  0.0047  72  TYR   C CZ  
1623 O OH  . TYR   B 66  ? 0.2435 0.2169 0.1852 0.0142  0.0022  0.0049  72  TYR   C OH  
1624 N N   . PRO   B 67  ? 0.1676 0.1507 0.1449 0.0229  -0.0097 0.0030  73  PRO   C N   
1625 C CA  . PRO   B 67  ? 0.1587 0.1449 0.1420 0.0245  -0.0115 0.0036  73  PRO   C CA  
1626 C C   . PRO   B 67  ? 0.1687 0.1607 0.1597 0.0255  -0.0107 0.0041  73  PRO   C C   
1627 O O   . PRO   B 67  ? 0.1833 0.1759 0.1762 0.0267  -0.0075 0.0036  73  PRO   C O   
1628 C CB  . PRO   B 67  ? 0.1842 0.1664 0.1670 0.0268  -0.0108 0.0029  73  PRO   C CB  
1629 C CG  . PRO   B 67  ? 0.2192 0.1973 0.1975 0.0270  -0.0074 0.0014  73  PRO   C CG  
1630 C CD  . PRO   B 67  ? 0.1820 0.1601 0.1555 0.0243  -0.0070 0.0014  73  PRO   C CD  
1631 N N   . VAL   B 68  ? 0.1442 0.1401 0.1393 0.0250  -0.0131 0.0048  74  VAL   C N   
1632 C CA  . VAL   B 68  ? 0.1372 0.1387 0.1402 0.0255  -0.0128 0.0051  74  VAL   C CA  
1633 C C   . VAL   B 68  ? 0.1313 0.1355 0.1386 0.0262  -0.0160 0.0053  74  VAL   C C   
1634 O O   . VAL   B 68  ? 0.1397 0.1419 0.1432 0.0255  -0.0185 0.0054  74  VAL   C O   
1635 C CB  . VAL   B 68  ? 0.1540 0.1580 0.1576 0.0232  -0.0122 0.0056  74  VAL   C CB  
1636 C CG1 . VAL   B 68  ? 0.1717 0.1741 0.1720 0.0226  -0.0089 0.0059  74  VAL   C CG1 
1637 C CG2 . VAL   B 68  ? 0.1757 0.1786 0.1758 0.0210  -0.0146 0.0059  74  VAL   C CG2 
1638 N N   . SER   B 69  ? 0.1341 0.1427 0.1496 0.0274  -0.0160 0.0053  75  SER   C N   
1639 C CA  . SER   B 69  ? 0.1305 0.1426 0.1508 0.0272  -0.0196 0.0053  75  SER   C CA  
1640 C C   . SER   B 69  ? 0.1213 0.1366 0.1443 0.0250  -0.0192 0.0051  75  SER   C C   
1641 O O   . SER   B 69  ? 0.1320 0.1487 0.1573 0.0245  -0.0161 0.0054  75  SER   C O   
1642 C CB  . SER   B 69  ? 0.1465 0.1622 0.1758 0.0295  -0.0201 0.0056  75  SER   C CB  
1643 O OG  . SER   B 69  ? 0.2152 0.2279 0.2429 0.0317  -0.0206 0.0061  75  SER   C OG  
1644 N N   . PHE   B 70  ? 0.1135 0.1294 0.1356 0.0235  -0.0221 0.0045  76  PHE   C N   
1645 C CA  . PHE   B 70  ? 0.1102 0.1284 0.1351 0.0214  -0.0215 0.0041  76  PHE   C CA  
1646 C C   . PHE   B 70  ? 0.1188 0.1395 0.1477 0.0207  -0.0249 0.0030  76  PHE   C C   
1647 O O   . PHE   B 70  ? 0.1242 0.1436 0.1501 0.0213  -0.0281 0.0026  76  PHE   C O   
1648 C CB  . PHE   B 70  ? 0.1185 0.1336 0.1372 0.0195  -0.0205 0.0043  76  PHE   C CB  
1649 C CG  . PHE   B 70  ? 0.1177 0.1292 0.1296 0.0192  -0.0223 0.0040  76  PHE   C CG  
1650 C CD1 . PHE   B 70  ? 0.1261 0.1338 0.1323 0.0201  -0.0220 0.0046  76  PHE   C CD1 
1651 C CD2 . PHE   B 70  ? 0.1318 0.1431 0.1428 0.0178  -0.0238 0.0030  76  PHE   C CD2 
1652 C CE1 . PHE   B 70  ? 0.1278 0.1321 0.1282 0.0196  -0.0233 0.0046  76  PHE   C CE1 
1653 C CE2 . PHE   B 70  ? 0.1427 0.1503 0.1470 0.0174  -0.0247 0.0029  76  PHE   C CE2 
1654 C CZ  . PHE   B 70  ? 0.1428 0.1471 0.1421 0.0183  -0.0245 0.0039  76  PHE   C CZ  
1655 N N   . SER   B 71  ? 0.1108 0.1346 0.1457 0.0193  -0.0243 0.0024  77  SER   C N   
1656 C CA  . SER   B 71  ? 0.1190 0.1452 0.1584 0.0184  -0.0275 0.0010  77  SER   C CA  
1657 C C   . SER   B 71  ? 0.1403 0.1635 0.1733 0.0166  -0.0291 -0.0006 77  SER   C C   
1658 O O   . SER   B 71  ? 0.1500 0.1697 0.1762 0.0161  -0.0276 -0.0002 77  SER   C O   
1659 C CB  . SER   B 71  ? 0.1118 0.1422 0.1611 0.0176  -0.0260 0.0010  77  SER   C CB  
1660 O OG  . SER   B 71  ? 0.1433 0.1730 0.1921 0.0160  -0.0231 0.0013  77  SER   C OG  
1661 N N   . LYS   B 72  ? 0.1353 0.1596 0.1703 0.0155  -0.0322 -0.0023 78  LYS   C N   
1662 C CA  . LYS   B 72  ? 0.1379 0.1587 0.1660 0.0137  -0.0333 -0.0043 78  LYS   C CA  
1663 C C   . LYS   B 72  ? 0.1475 0.1685 0.1789 0.0119  -0.0302 -0.0051 78  LYS   C C   
1664 O O   . LYS   B 72  ? 0.1418 0.1663 0.1819 0.0116  -0.0290 -0.0048 78  LYS   C O   
1665 C CB  . LYS   B 72  ? 0.1850 0.2064 0.2133 0.0130  -0.0382 -0.0062 78  LYS   C CB  
1666 C CG  . LYS   B 72  ? 0.2422 0.2634 0.2678 0.0149  -0.0420 -0.0049 78  LYS   C CG  
1667 C CD  . LYS   B 72  ? 0.3529 0.3754 0.3800 0.0139  -0.0477 -0.0065 78  LYS   C CD  
1668 C CE  . LYS   B 72  ? 0.4554 0.4781 0.4811 0.0159  -0.0521 -0.0046 78  LYS   C CE  
1669 N NZ  . LYS   B 72  ? 0.5023 0.5269 0.5307 0.0149  -0.0584 -0.0058 78  LYS   C NZ  
1670 N N   . PRO   B 73  ? 0.1419 0.1593 0.1676 0.0106  -0.0285 -0.0060 79  PRO   C N   
1671 C CA  . PRO   B 73  ? 0.1437 0.1612 0.1738 0.0091  -0.0254 -0.0065 79  PRO   C CA  
1672 C C   . PRO   B 73  ? 0.1434 0.1629 0.1803 0.0077  -0.0265 -0.0087 79  PRO   C C   
1673 O O   . PRO   B 73  ? 0.1679 0.1860 0.2016 0.0068  -0.0295 -0.0113 79  PRO   C O   
1674 C CB  . PRO   B 73  ? 0.1815 0.1945 0.2043 0.0082  -0.0238 -0.0075 79  PRO   C CB  
1675 C CG  . PRO   B 73  ? 0.2025 0.2130 0.2168 0.0094  -0.0253 -0.0067 79  PRO   C CG  
1676 C CD  . PRO   B 73  ? 0.1607 0.1736 0.1762 0.0107  -0.0291 -0.0063 79  PRO   C CD  
1677 N N   . SER   B 74  ? 0.1223 0.1448 0.1682 0.0073  -0.0244 -0.0077 80  SER   C N   
1678 C CA  . SER   B 74  ? 0.1403 0.1651 0.1943 0.0060  -0.0255 -0.0094 80  SER   C CA  
1679 C C   . SER   B 74  ? 0.1320 0.1579 0.1938 0.0051  -0.0219 -0.0083 80  SER   C C   
1680 O O   . SER   B 74  ? 0.1263 0.1516 0.1870 0.0056  -0.0192 -0.0058 80  SER   C O   
1681 C CB  . SER   B 74  ? 0.1942 0.2233 0.2541 0.0071  -0.0278 -0.0084 80  SER   C CB  
1682 O OG  . SER   B 74  ? 0.2703 0.2988 0.3242 0.0083  -0.0313 -0.0087 80  SER   C OG  
1683 N N   . LEU   B 75  ? 0.1367 0.1642 0.2066 0.0036  -0.0224 -0.0099 81  LEU   C N   
1684 C CA  . LEU   B 75  ? 0.1542 0.1829 0.2330 0.0027  -0.0193 -0.0087 81  LEU   C CA  
1685 C C   . LEU   B 75  ? 0.1578 0.1909 0.2435 0.0037  -0.0185 -0.0056 81  LEU   C C   
1686 O O   . LEU   B 75  ? 0.1627 0.1988 0.2536 0.0036  -0.0208 -0.0065 81  LEU   C O   
1687 C CB  . LEU   B 75  ? 0.1729 0.2006 0.2569 0.0004  -0.0202 -0.0124 81  LEU   C CB  
1688 C CG  . LEU   B 75  ? 0.2008 0.2285 0.2940 -0.0008 -0.0168 -0.0116 81  LEU   C CG  
1689 C CD1 . LEU   B 75  ? 0.1872 0.2117 0.2772 -0.0005 -0.0136 -0.0104 81  LEU   C CD1 
1690 C CD2 . LEU   B 75  ? 0.2305 0.2569 0.3289 -0.0031 -0.0183 -0.0158 81  LEU   C CD2 
1691 N N   . ILE   B 76  ? 0.1578 0.1913 0.2430 0.0047  -0.0155 -0.0020 82  ILE   C N   
1692 C CA  . ILE   B 76  ? 0.1643 0.2009 0.2534 0.0058  -0.0139 0.0011  82  ILE   C CA  
1693 C C   . ILE   B 76  ? 0.1640 0.2012 0.2593 0.0050  -0.0104 0.0040  82  ILE   C C   
1694 O O   . ILE   B 76  ? 0.1553 0.1901 0.2481 0.0046  -0.0090 0.0053  82  ILE   C O   
1695 C CB  . ILE   B 76  ? 0.1920 0.2275 0.2721 0.0077  -0.0136 0.0028  82  ILE   C CB  
1696 C CG1 . ILE   B 76  ? 0.2145 0.2491 0.2883 0.0086  -0.0170 0.0005  82  ILE   C CG1 
1697 C CG2 . ILE   B 76  ? 0.2122 0.2498 0.2945 0.0088  -0.0109 0.0059  82  ILE   C CG2 
1698 C CD1 . ILE   B 76  ? 0.2356 0.2734 0.3136 0.0098  -0.0186 0.0003  82  ILE   C CD1 
1699 N N   . PHE   B 77  ? 0.1637 0.2042 0.2674 0.0049  -0.0088 0.0055  83  PHE   C N   
1700 C CA  . PHE   B 77  ? 0.1751 0.2159 0.2842 0.0042  -0.0053 0.0089  83  PHE   C CA  
1701 C C   . PHE   B 77  ? 0.1808 0.2207 0.2825 0.0056  -0.0031 0.0126  83  PHE   C C   
1702 O O   . PHE   B 77  ? 0.2079 0.2488 0.3060 0.0071  -0.0028 0.0129  83  PHE   C O   
1703 C CB  . PHE   B 77  ? 0.1816 0.2259 0.3023 0.0035  -0.0039 0.0093  83  PHE   C CB  
1704 C CG  . PHE   B 77  ? 0.1896 0.2335 0.3164 0.0024  -0.0005 0.0127  83  PHE   C CG  
1705 C CD1 . PHE   B 77  ? 0.1961 0.2381 0.3274 0.0008  -0.0007 0.0118  83  PHE   C CD1 
1706 C CD2 . PHE   B 77  ? 0.2057 0.2507 0.3333 0.0030  0.0032  0.0170  83  PHE   C CD2 
1707 C CE1 . PHE   B 77  ? 0.2136 0.2551 0.3509 0.0000  0.0024  0.0154  83  PHE   C CE1 
1708 C CE2 . PHE   B 77  ? 0.2084 0.2527 0.3408 0.0020  0.0062  0.0206  83  PHE   C CE2 
1709 C CZ  . PHE   B 77  ? 0.2143 0.2570 0.3521 0.0005  0.0056  0.0200  83  PHE   C CZ  
1710 N N   . VAL   B 78  ? 0.1582 0.1958 0.2573 0.0051  -0.0018 0.0152  84  VAL   C N   
1711 C CA  . VAL   B 78  ? 0.1664 0.2026 0.2575 0.0059  -0.0005 0.0186  84  VAL   C CA  
1712 C C   . VAL   B 78  ? 0.1591 0.1955 0.2544 0.0052  0.0026  0.0230  84  VAL   C C   
1713 O O   . VAL   B 78  ? 0.1539 0.1899 0.2555 0.0040  0.0029  0.0239  84  VAL   C O   
1714 C CB  . VAL   B 78  ? 0.1787 0.2119 0.2629 0.0058  -0.0025 0.0185  84  VAL   C CB  
1715 C CG1 . VAL   B 78  ? 0.2026 0.2339 0.2779 0.0063  -0.0021 0.0217  84  VAL   C CG1 
1716 C CG2 . VAL   B 78  ? 0.1887 0.2212 0.2688 0.0063  -0.0052 0.0144  84  VAL   C CG2 
1717 N N   . GLU   B 79  ? 0.1489 0.1853 0.2398 0.0059  0.0051  0.0258  85  GLU   C N   
1718 C CA  . GLU   B 79  ? 0.1561 0.1919 0.2488 0.0051  0.0081  0.0305  85  GLU   C CA  
1719 C C   . GLU   B 79  ? 0.1562 0.1893 0.2441 0.0044  0.0067  0.0335  85  GLU   C C   
1720 O O   . GLU   B 79  ? 0.1503 0.1818 0.2321 0.0047  0.0038  0.0322  85  GLU   C O   
1721 C CB  . GLU   B 79  ? 0.1903 0.2261 0.2779 0.0060  0.0117  0.0325  85  GLU   C CB  
1722 C CG  . GLU   B 79  ? 0.2687 0.3078 0.3647 0.0065  0.0139  0.0305  85  GLU   C CG  
1723 C CD  . GLU   B 79  ? 0.3540 0.3958 0.4638 0.0052  0.0150  0.0309  85  GLU   C CD  
1724 O OE1 . GLU   B 79  ? 0.3849 0.4256 0.4974 0.0041  0.0168  0.0345  85  GLU   C OE1 
1725 O OE2 . GLU   B 79  ? 0.3461 0.3908 0.4641 0.0053  0.0137  0.0275  85  GLU   C OE2 
1726 N N   . ALA   B 80  ? 0.1668 0.1993 0.2584 0.0035  0.0085  0.0378  86  ALA   C N   
1727 C CA  . ALA   B 80  ? 0.1901 0.2204 0.2790 0.0028  0.0068  0.0415  86  ALA   C CA  
1728 C C   . ALA   B 80  ? 0.2212 0.2491 0.2968 0.0032  0.0052  0.0429  86  ALA   C C   
1729 O O   . ALA   B 80  ? 0.2392 0.2663 0.3072 0.0037  0.0070  0.0429  86  ALA   C O   
1730 C CB  . ALA   B 80  ? 0.1983 0.2284 0.2925 0.0018  0.0094  0.0467  86  ALA   C CB  
1731 N N   . SER   B 81  ? 0.2171 0.2437 0.2904 0.0028  0.0018  0.0434  87  SER   C N   
1732 C CA  . SER   B 81  ? 0.2315 0.2556 0.2929 0.0028  -0.0004 0.0447  87  SER   C CA  
1733 C C   . SER   B 81  ? 0.2465 0.2692 0.3080 0.0017  -0.0026 0.0500  87  SER   C C   
1734 O O   . SER   B 81  ? 0.2367 0.2602 0.3078 0.0012  -0.0018 0.0527  87  SER   C O   
1735 C CB  . SER   B 81  ? 0.2436 0.2675 0.3021 0.0034  -0.0030 0.0403  87  SER   C CB  
1736 O OG  . SER   B 81  ? 0.2562 0.2807 0.3222 0.0030  -0.0049 0.0403  87  SER   C OG  
1737 N N   . GLU   B 82  ? 0.2833 0.3036 0.3347 0.0012  -0.0056 0.0517  88  GLU   C N   
1738 C CA  . GLU   B 82  ? 0.2958 0.3150 0.3481 0.0001  -0.0086 0.0570  88  GLU   C CA  
1739 C C   . GLU   B 82  ? 0.2836 0.3045 0.3477 0.0002  -0.0105 0.0566  88  GLU   C C   
1740 O O   . GLU   B 82  ? 0.2961 0.3170 0.3658 -0.0005 -0.0122 0.0611  88  GLU   C O   
1741 C CB  . GLU   B 82  ? 0.3647 0.3808 0.4036 -0.0008 -0.0120 0.0591  88  GLU   C CB  
1742 C CG  . GLU   B 82  ? 0.4623 0.4780 0.4969 -0.0006 -0.0149 0.0553  88  GLU   C CG  
1743 C CD  . GLU   B 82  ? 0.5184 0.5306 0.5395 -0.0018 -0.0183 0.0573  88  GLU   C CD  
1744 O OE1 . GLU   B 82  ? 0.5348 0.5444 0.5459 -0.0022 -0.0166 0.0588  88  GLU   C OE1 
1745 O OE2 . GLU   B 82  ? 0.5430 0.5549 0.5639 -0.0026 -0.0227 0.0574  88  GLU   C OE2 
1746 N N   . TYR   B 83  ? 0.2473 0.2696 0.3157 0.0009  -0.0099 0.0511  89  TYR   C N   
1747 C CA  . TYR   B 83  ? 0.2337 0.2569 0.3116 0.0010  -0.0112 0.0503  89  TYR   C CA  
1748 C C   . TYR   B 83  ? 0.2258 0.2504 0.3148 0.0014  -0.0082 0.0468  89  TYR   C C   
1749 O O   . TYR   B 83  ? 0.2322 0.2570 0.3299 0.0014  -0.0083 0.0465  89  TYR   C O   
1750 C CB  . TYR   B 83  ? 0.2281 0.2506 0.3003 0.0011  -0.0138 0.0475  89  TYR   C CB  
1751 C CG  . TYR   B 83  ? 0.2191 0.2410 0.2821 0.0018  -0.0129 0.0429  89  TYR   C CG  
1752 C CD1 . TYR   B 83  ? 0.2220 0.2422 0.2732 0.0016  -0.0139 0.0436  89  TYR   C CD1 
1753 C CD2 . TYR   B 83  ? 0.2051 0.2279 0.2711 0.0026  -0.0113 0.0379  89  TYR   C CD2 
1754 C CE1 . TYR   B 83  ? 0.1978 0.2172 0.2417 0.0025  -0.0129 0.0395  89  TYR   C CE1 
1755 C CE2 . TYR   B 83  ? 0.2122 0.2345 0.2708 0.0034  -0.0108 0.0342  89  TYR   C CE2 
1756 C CZ  . TYR   B 83  ? 0.2143 0.2351 0.2626 0.0034  -0.0114 0.0351  89  TYR   C CZ  
1757 O OH  . TYR   B 83  ? 0.2447 0.2650 0.2869 0.0044  -0.0107 0.0315  89  TYR   C OH  
1758 N N   . TYR   B 84  ? 0.1867 0.2122 0.2759 0.0018  -0.0054 0.0442  90  TYR   C N   
1759 C CA  . TYR   B 84  ? 0.1705 0.1970 0.2700 0.0018  -0.0031 0.0410  90  TYR   C CA  
1760 C C   . TYR   B 84  ? 0.1584 0.1859 0.2606 0.0015  -0.0004 0.0422  90  TYR   C C   
1761 O O   . TYR   B 84  ? 0.1583 0.1860 0.2529 0.0018  0.0003  0.0432  90  TYR   C O   
1762 C CB  . TYR   B 84  ? 0.1637 0.1906 0.2610 0.0023  -0.0032 0.0346  90  TYR   C CB  
1763 C CG  . TYR   B 84  ? 0.1355 0.1613 0.2316 0.0025  -0.0048 0.0325  90  TYR   C CG  
1764 C CD1 . TYR   B 84  ? 0.1359 0.1610 0.2408 0.0022  -0.0041 0.0325  90  TYR   C CD1 
1765 C CD2 . TYR   B 84  ? 0.1217 0.1468 0.2084 0.0030  -0.0064 0.0307  90  TYR   C CD2 
1766 C CE1 . TYR   B 84  ? 0.1332 0.1572 0.2375 0.0023  -0.0048 0.0304  90  TYR   C CE1 
1767 C CE2 . TYR   B 84  ? 0.1302 0.1543 0.2162 0.0030  -0.0075 0.0290  90  TYR   C CE2 
1768 C CZ  . TYR   B 84  ? 0.1409 0.1644 0.2357 0.0027  -0.0065 0.0289  90  TYR   C CZ  
1769 O OH  . TYR   B 84  ? 0.1263 0.1487 0.2210 0.0028  -0.0067 0.0272  90  TYR   C OH  
1770 N N   . PRO   B 85  ? 0.1541 0.1823 0.2672 0.0011  0.0016  0.0413  91  PRO   C N   
1771 C CA  . PRO   B 85  ? 0.1518 0.1813 0.2686 0.0008  0.0043  0.0416  91  PRO   C CA  
1772 C C   . PRO   B 85  ? 0.1544 0.1855 0.2684 0.0013  0.0044  0.0362  91  PRO   C C   
1773 O O   . PRO   B 85  ? 0.1550 0.1859 0.2646 0.0018  0.0024  0.0321  91  PRO   C O   
1774 C CB  . PRO   B 85  ? 0.1709 0.2002 0.3011 -0.0001 0.0058  0.0415  91  PRO   C CB  
1775 C CG  . PRO   B 85  ? 0.1788 0.2070 0.3108 0.0001  0.0042  0.0373  91  PRO   C CG  
1776 C CD  . PRO   B 85  ? 0.1590 0.1864 0.2819 0.0007  0.0018  0.0394  91  PRO   C CD  
1777 N N   . ALA   B 86  ? 0.1423 0.1751 0.2601 0.0010  0.0068  0.0361  92  ALA   C N   
1778 C CA  . ALA   B 86  ? 0.1432 0.1780 0.2613 0.0014  0.0066  0.0313  92  ALA   C CA  
1779 C C   . ALA   B 86  ? 0.1535 0.1883 0.2783 0.0008  0.0050  0.0264  92  ALA   C C   
1780 O O   . ALA   B 86  ? 0.1769 0.2108 0.3105 -0.0003 0.0059  0.0270  92  ALA   C O   
1781 C CB  . ALA   B 86  ? 0.1437 0.1808 0.2675 0.0012  0.0096  0.0327  92  ALA   C CB  
1782 N N   . ARG   B 87  ? 0.1401 0.1748 0.2596 0.0013  0.0026  0.0220  93  ARG   C N   
1783 C CA  . ARG   B 87  ? 0.1401 0.1738 0.2629 0.0006  0.0011  0.0173  93  ARG   C CA  
1784 C C   . ARG   B 87  ? 0.1402 0.1742 0.2564 0.0012  -0.0015 0.0129  93  ARG   C C   
1785 O O   . ARG   B 87  ? 0.1378 0.1727 0.2468 0.0025  -0.0021 0.0138  93  ARG   C O   
1786 C CB  . ARG   B 87  ? 0.1524 0.1832 0.2742 0.0005  0.0010  0.0181  93  ARG   C CB  
1787 C CG  . ARG   B 87  ? 0.1396 0.1694 0.2505 0.0016  -0.0007 0.0184  93  ARG   C CG  
1788 C CD  . ARG   B 87  ? 0.1484 0.1760 0.2599 0.0015  -0.0007 0.0201  93  ARG   C CD  
1789 N NE  . ARG   B 87  ? 0.1647 0.1914 0.2667 0.0023  -0.0024 0.0195  93  ARG   C NE  
1790 C CZ  . ARG   B 87  ? 0.1878 0.2126 0.2886 0.0023  -0.0027 0.0177  93  ARG   C CZ  
1791 N NH1 . ARG   B 87  ? 0.1744 0.1978 0.2829 0.0017  -0.0012 0.0162  93  ARG   C NH1 
1792 N NH2 . ARG   B 87  ? 0.1879 0.2120 0.2803 0.0030  -0.0042 0.0173  93  ARG   C NH2 
1793 N N   . TYR   B 88  ? 0.1583 0.1910 0.2758 0.0004  -0.0031 0.0082  94  TYR   C N   
1794 C CA  . TYR   B 88  ? 0.1857 0.2179 0.2952 0.0010  -0.0058 0.0045  94  TYR   C CA  
1795 C C   . TYR   B 88  ? 0.1713 0.2006 0.2728 0.0016  -0.0060 0.0046  94  TYR   C C   
1796 O O   . TYR   B 88  ? 0.1867 0.2138 0.2908 0.0010  -0.0046 0.0047  94  TYR   C O   
1797 C CB  . TYR   B 88  ? 0.2200 0.2514 0.3324 -0.0004 -0.0078 -0.0007 94  TYR   C CB  
1798 C CG  . TYR   B 88  ? 0.2693 0.3041 0.3897 -0.0011 -0.0086 -0.0012 94  TYR   C CG  
1799 C CD1 . TYR   B 88  ? 0.3022 0.3396 0.4203 -0.0002 -0.0109 -0.0018 94  TYR   C CD1 
1800 C CD2 . TYR   B 88  ? 0.3053 0.3407 0.4366 -0.0025 -0.0067 -0.0005 94  TYR   C CD2 
1801 C CE1 . TYR   B 88  ? 0.3241 0.3651 0.4513 -0.0008 -0.0115 -0.0019 94  TYR   C CE1 
1802 C CE2 . TYR   B 88  ? 0.3315 0.3703 0.4715 -0.0033 -0.0072 -0.0006 94  TYR   C CE2 
1803 C CZ  . TYR   B 88  ? 0.3474 0.3892 0.4856 -0.0024 -0.0095 -0.0013 94  TYR   C CZ  
1804 O OH  . TYR   B 88  ? 0.3969 0.4424 0.5456 -0.0032 -0.0098 -0.0012 94  TYR   C OH  
1805 N N   . GLN   B 89  ? 0.1487 0.1779 0.2412 0.0029  -0.0075 0.0047  95  GLN   C N   
1806 C CA  . GLN   B 89  ? 0.1358 0.1623 0.2209 0.0033  -0.0078 0.0044  95  GLN   C CA  
1807 C C   . GLN   B 89  ? 0.1224 0.1476 0.2012 0.0034  -0.0101 0.0002  95  GLN   C C   
1808 O O   . GLN   B 89  ? 0.1345 0.1615 0.2120 0.0040  -0.0120 -0.0007 95  GLN   C O   
1809 C CB  . GLN   B 89  ? 0.1620 0.1889 0.2414 0.0045  -0.0078 0.0081  95  GLN   C CB  
1810 C CG  . GLN   B 89  ? 0.1766 0.2009 0.2496 0.0047  -0.0082 0.0081  95  GLN   C CG  
1811 C CD  . GLN   B 89  ? 0.1612 0.1855 0.2308 0.0052  -0.0082 0.0122  95  GLN   C CD  
1812 O OE1 . GLN   B 89  ? 0.1691 0.1943 0.2424 0.0049  -0.0073 0.0156  95  GLN   C OE1 
1813 N NE2 . GLN   B 89  ? 0.1379 0.1607 0.2001 0.0057  -0.0093 0.0118  95  GLN   C NE2 
1814 N N   . SER   B 90  ? 0.1152 0.1373 0.1906 0.0029  -0.0098 -0.0021 96  SER   C N   
1815 C CA  . SER   B 90  ? 0.1242 0.1442 0.1925 0.0028  -0.0118 -0.0058 96  SER   C CA  
1816 C C   . SER   B 90  ? 0.1190 0.1375 0.1778 0.0040  -0.0125 -0.0048 96  SER   C C   
1817 O O   . SER   B 90  ? 0.1238 0.1424 0.1821 0.0046  -0.0112 -0.0017 96  SER   C O   
1818 C CB  . SER   B 90  ? 0.1463 0.1628 0.2150 0.0013  -0.0106 -0.0096 96  SER   C CB  
1819 O OG  . SER   B 90  ? 0.1697 0.1840 0.2381 0.0015  -0.0078 -0.0082 96  SER   C OG  
1820 N N   . HIS   B 91  ? 0.1210 0.1383 0.1727 0.0043  -0.0150 -0.0072 97  HIS   C N   
1821 C CA  . HIS   B 91  ? 0.1312 0.1465 0.1739 0.0053  -0.0157 -0.0064 97  HIS   C CA  
1822 C C   . HIS   B 91  ? 0.1349 0.1523 0.1773 0.0067  -0.0158 -0.0029 97  HIS   C C   
1823 O O   . HIS   B 91  ? 0.1363 0.1521 0.1741 0.0072  -0.0152 -0.0013 97  HIS   C O   
1824 C CB  . HIS   B 91  ? 0.1334 0.1451 0.1726 0.0047  -0.0132 -0.0070 97  HIS   C CB  
1825 C CG  . HIS   B 91  ? 0.1541 0.1625 0.1916 0.0034  -0.0125 -0.0109 97  HIS   C CG  
1826 N ND1 . HIS   B 91  ? 0.1715 0.1766 0.1994 0.0032  -0.0138 -0.0133 97  HIS   C ND1 
1827 C CD2 . HIS   B 91  ? 0.1663 0.1740 0.2100 0.0020  -0.0105 -0.0129 97  HIS   C CD2 
1828 C CE1 . HIS   B 91  ? 0.1789 0.1810 0.2063 0.0017  -0.0125 -0.0169 97  HIS   C CE1 
1829 N NE2 . HIS   B 91  ? 0.1893 0.1928 0.2264 0.0010  -0.0104 -0.0170 97  HIS   C NE2 
1830 N N   . LEU   B 92  ? 0.1163 0.1371 0.1638 0.0072  -0.0164 -0.0018 98  LEU   C N   
1831 C CA  . LEU   B 92  ? 0.1225 0.1448 0.1696 0.0085  -0.0159 0.0011  98  LEU   C CA  
1832 C C   . LEU   B 92  ? 0.1092 0.1324 0.1533 0.0099  -0.0180 0.0007  98  LEU   C C   
1833 O O   . LEU   B 92  ? 0.1151 0.1398 0.1619 0.0099  -0.0200 -0.0012 98  LEU   C O   
1834 C CB  . LEU   B 92  ? 0.1192 0.1444 0.1743 0.0081  -0.0140 0.0032  98  LEU   C CB  
1835 C CG  . LEU   B 92  ? 0.1299 0.1558 0.1833 0.0090  -0.0128 0.0063  98  LEU   C CG  
1836 C CD1 . LEU   B 92  ? 0.1435 0.1670 0.1925 0.0086  -0.0122 0.0084  98  LEU   C CD1 
1837 C CD2 . LEU   B 92  ? 0.1435 0.1720 0.2046 0.0086  -0.0108 0.0083  98  LEU   C CD2 
1838 N N   . MET   B 93  ? 0.1131 0.1352 0.1519 0.0112  -0.0177 0.0023  99  MET   C N   
1839 C CA  . MET   B 93  ? 0.1046 0.1271 0.1411 0.0129  -0.0191 0.0023  99  MET   C CA  
1840 C C   . MET   B 93  ? 0.1055 0.1293 0.1435 0.0139  -0.0169 0.0044  99  MET   C C   
1841 O O   . MET   B 93  ? 0.1236 0.1458 0.1586 0.0134  -0.0153 0.0061  99  MET   C O   
1842 C CB  . MET   B 93  ? 0.1273 0.1461 0.1552 0.0135  -0.0203 0.0020  99  MET   C CB  
1843 C CG  . MET   B 93  ? 0.1366 0.1535 0.1617 0.0124  -0.0217 0.0000  99  MET   C CG  
1844 S SD  . MET   B 93  ? 0.1559 0.1681 0.1710 0.0128  -0.0222 0.0002  99  MET   C SD  
1845 C CE  . MET   B 93  ? 0.1586 0.1696 0.1736 0.0120  -0.0194 0.0022  99  MET   C CE  
1846 N N   . LEU   B 94  ? 0.1036 0.1298 0.1456 0.0152  -0.0168 0.0045  100 LEU   C N   
1847 C CA  . LEU   B 94  ? 0.1180 0.1446 0.1605 0.0162  -0.0139 0.0063  100 LEU   C CA  
1848 C C   . LEU   B 94  ? 0.1217 0.1467 0.1599 0.0182  -0.0140 0.0062  100 LEU   C C   
1849 O O   . LEU   B 94  ? 0.1269 0.1522 0.1658 0.0193  -0.0165 0.0051  100 LEU   C O   
1850 C CB  . LEU   B 94  ? 0.1411 0.1719 0.1933 0.0163  -0.0123 0.0067  100 LEU   C CB  
1851 C CG  . LEU   B 94  ? 0.1376 0.1702 0.1959 0.0144  -0.0117 0.0070  100 LEU   C CG  
1852 C CD1 . LEU   B 94  ? 0.1775 0.2141 0.2456 0.0146  -0.0098 0.0077  100 LEU   C CD1 
1853 C CD2 . LEU   B 94  ? 0.1612 0.1917 0.2156 0.0132  -0.0098 0.0090  100 LEU   C CD2 
1854 N N   . ALA   B 95  ? 0.1253 0.1484 0.1595 0.0187  -0.0112 0.0074  101 ALA   C N   
1855 C CA  . ALA   B 95  ? 0.1251 0.1462 0.1561 0.0207  -0.0101 0.0072  101 ALA   C CA  
1856 C C   . ALA   B 95  ? 0.1269 0.1482 0.1587 0.0212  -0.0057 0.0084  101 ALA   C C   
1857 O O   . ALA   B 95  ? 0.1276 0.1495 0.1597 0.0197  -0.0040 0.0097  101 ALA   C O   
1858 C CB  . ALA   B 95  ? 0.1428 0.1590 0.1642 0.0206  -0.0111 0.0070  101 ALA   C CB  
1859 N N   . VAL   B 96  ? 0.1248 0.1454 0.1570 0.0233  -0.0035 0.0080  102 VAL   C N   
1860 C CA  . VAL   B 96  ? 0.1435 0.1629 0.1742 0.0237  0.0015  0.0088  102 VAL   C CA  
1861 C C   . VAL   B 96  ? 0.1613 0.1750 0.1799 0.0230  0.0020  0.0087  102 VAL   C C   
1862 O O   . VAL   B 96  ? 0.1765 0.1867 0.1901 0.0239  0.0008  0.0075  102 VAL   C O   
1863 C CB  . VAL   B 96  ? 0.1457 0.1665 0.1828 0.0264  0.0039  0.0082  102 VAL   C CB  
1864 C CG1 . VAL   B 96  ? 0.1659 0.1848 0.2007 0.0269  0.0100  0.0088  102 VAL   C CG1 
1865 C CG2 . VAL   B 96  ? 0.1515 0.1784 0.2014 0.0269  0.0023  0.0083  102 VAL   C CG2 
1866 N N   . GLY   B 97  ? 0.1675 0.1801 0.1817 0.0211  0.0034  0.0102  103 GLY   C N   
1867 C CA  . GLY   B 97  ? 0.1777 0.1849 0.1805 0.0199  0.0031  0.0103  103 GLY   C CA  
1868 C C   . GLY   B 97  ? 0.1948 0.2016 0.1941 0.0177  0.0036  0.0125  103 GLY   C C   
1869 O O   . GLY   B 97  ? 0.2001 0.2108 0.2062 0.0170  0.0042  0.0141  103 GLY   C O   
1870 N N   . HIS   B 98  ? 0.1970 0.1990 0.1858 0.0164  0.0031  0.0127  104 HIS   C N   
1871 C CA  . HIS   B 98  ? 0.1980 0.1989 0.1818 0.0142  0.0029  0.0153  104 HIS   C CA  
1872 C C   . HIS   B 98  ? 0.1946 0.1970 0.1805 0.0123  -0.0017 0.0168  104 HIS   C C   
1873 O O   . HIS   B 98  ? 0.1924 0.1936 0.1772 0.0120  -0.0050 0.0156  104 HIS   C O   
1874 C CB  . HIS   B 98  ? 0.2331 0.2276 0.2039 0.0134  0.0038  0.0147  104 HIS   C CB  
1875 C CG  . HIS   B 98  ? 0.2951 0.2881 0.2596 0.0111  0.0035  0.0177  104 HIS   C CG  
1876 N ND1 . HIS   B 98  ? 0.3280 0.3225 0.2943 0.0111  0.0074  0.0199  104 HIS   C ND1 
1877 C CD2 . HIS   B 98  ? 0.3245 0.3147 0.2819 0.0087  -0.0005 0.0191  104 HIS   C CD2 
1878 C CE1 . HIS   B 98  ? 0.3568 0.3491 0.3160 0.0088  0.0056  0.0227  104 HIS   C CE1 
1879 N NE2 . HIS   B 98  ? 0.3592 0.3489 0.3129 0.0073  0.0006  0.0223  104 HIS   C NE2 
1880 N N   . SER   B 99  ? 0.1852 0.1898 0.1744 0.0109  -0.0018 0.0197  105 SER   C N   
1881 C CA  . SER   B 99  ? 0.1859 0.1920 0.1786 0.0092  -0.0056 0.0215  105 SER   C CA  
1882 C C   . SER   B 99  ? 0.2050 0.2113 0.1970 0.0077  -0.0051 0.0253  105 SER   C C   
1883 O O   . SER   B 99  ? 0.2343 0.2435 0.2328 0.0081  -0.0024 0.0266  105 SER   C O   
1884 C CB  . SER   B 99  ? 0.2045 0.2151 0.2083 0.0100  -0.0060 0.0204  105 SER   C CB  
1885 O OG  . SER   B 99  ? 0.2241 0.2360 0.2324 0.0086  -0.0087 0.0219  105 SER   C OG  
1886 N N   . GLU   B 100 ? 0.1910 0.1943 0.1757 0.0059  -0.0080 0.0273  106 GLU   C N   
1887 C CA  . GLU   B 100 ? 0.1967 0.1997 0.1801 0.0041  -0.0089 0.0316  106 GLU   C CA  
1888 C C   . GLU   B 100 ? 0.1706 0.1768 0.1638 0.0033  -0.0125 0.0332  106 GLU   C C   
1889 O O   . GLU   B 100 ? 0.1605 0.1675 0.1572 0.0036  -0.0145 0.0310  106 GLU   C O   
1890 C CB  . GLU   B 100 ? 0.2323 0.2301 0.2023 0.0023  -0.0115 0.0328  106 GLU   C CB  
1891 C CG  . GLU   B 100 ? 0.2789 0.2720 0.2370 0.0028  -0.0082 0.0309  106 GLU   C CG  
1892 C CD  . GLU   B 100 ? 0.3224 0.3151 0.2779 0.0031  -0.0033 0.0329  106 GLU   C CD  
1893 O OE1 . GLU   B 100 ? 0.3732 0.3620 0.3197 0.0036  0.0005  0.0311  106 GLU   C OE1 
1894 O OE2 . GLU   B 100 ? 0.3180 0.3140 0.2811 0.0028  -0.0028 0.0362  106 GLU   C OE2 
1895 N N   . PRO   B 101 ? 0.1757 0.1832 0.1729 0.0022  -0.0132 0.0373  107 PRO   C N   
1896 C CA  . PRO   B 101 ? 0.1735 0.1835 0.1804 0.0016  -0.0161 0.0388  107 PRO   C CA  
1897 C C   . PRO   B 101 ? 0.1822 0.1907 0.1864 0.0005  -0.0205 0.0383  107 PRO   C C   
1898 O O   . PRO   B 101 ? 0.1665 0.1769 0.1783 0.0008  -0.0214 0.0369  107 PRO   C O   
1899 C CB  . PRO   B 101 ? 0.2033 0.2137 0.2122 0.0004  -0.0166 0.0441  107 PRO   C CB  
1900 C CG  . PRO   B 101 ? 0.2294 0.2387 0.2331 0.0010  -0.0122 0.0445  107 PRO   C CG  
1901 C CD  . PRO   B 101 ? 0.1931 0.1997 0.1870 0.0017  -0.0107 0.0407  107 PRO   C CD  
1902 N N   . GLY   B 102 ? 0.1628 0.1676 0.1560 -0.0006 -0.0227 0.0390  108 GLY   C N   
1903 C CA  . GLY   B 102 ? 0.1711 0.1742 0.1619 -0.0019 -0.0271 0.0386  108 GLY   C CA  
1904 C C   . GLY   B 102 ? 0.1735 0.1761 0.1642 -0.0009 -0.0264 0.0341  108 GLY   C C   
1905 O O   . GLY   B 102 ? 0.1798 0.1816 0.1709 -0.0018 -0.0295 0.0335  108 GLY   C O   
1906 N N   . ASP   B 103 ? 0.1615 0.1645 0.1518 0.0010  -0.0224 0.0310  109 ASP   C N   
1907 C CA  . ASP   B 103 ? 0.1527 0.1552 0.1431 0.0022  -0.0217 0.0271  109 ASP   C CA  
1908 C C   . ASP   B 103 ? 0.1393 0.1452 0.1403 0.0029  -0.0215 0.0262  109 ASP   C C   
1909 O O   . ASP   B 103 ? 0.1471 0.1521 0.1478 0.0035  -0.0216 0.0236  109 ASP   C O   
1910 C CB  . ASP   B 103 ? 0.1526 0.1543 0.1392 0.0042  -0.0178 0.0244  109 ASP   C CB  
1911 C CG  . ASP   B 103 ? 0.1784 0.1755 0.1534 0.0037  -0.0173 0.0240  109 ASP   C CG  
1912 O OD1 . ASP   B 103 ? 0.2010 0.1948 0.1697 0.0022  -0.0205 0.0240  109 ASP   C OD1 
1913 O OD2 . ASP   B 103 ? 0.1856 0.1823 0.1578 0.0048  -0.0136 0.0237  109 ASP   C OD2 
1914 N N   . CYS   B 104 ? 0.1357 0.1446 0.1452 0.0026  -0.0212 0.0284  110 CYS   C N   
1915 C CA  . CYS   B 104 ? 0.1330 0.1443 0.1519 0.0030  -0.0206 0.0273  110 CYS   C CA  
1916 C C   . CYS   B 104 ? 0.1368 0.1470 0.1563 0.0021  -0.0228 0.0269  110 CYS   C C   
1917 O O   . CYS   B 104 ? 0.1480 0.1571 0.1658 0.0007  -0.0258 0.0293  110 CYS   C O   
1918 C CB  . CYS   B 104 ? 0.1419 0.1559 0.1699 0.0026  -0.0200 0.0300  110 CYS   C CB  
1919 S SG  . CYS   B 104 ? 0.1553 0.1713 0.1862 0.0037  -0.0166 0.0296  110 CYS   C SG  
1920 N N   . GLY   B 105 ? 0.1156 0.1259 0.1373 0.0030  -0.0215 0.0241  111 GLY   C N   
1921 C CA  . GLY   B 105 ? 0.1284 0.1375 0.1510 0.0022  -0.0228 0.0237  111 GLY   C CA  
1922 C C   . GLY   B 105 ? 0.1342 0.1402 0.1486 0.0026  -0.0233 0.0215  111 GLY   C C   
1923 O O   . GLY   B 105 ? 0.1410 0.1458 0.1561 0.0022  -0.0236 0.0207  111 GLY   C O   
1924 N N   . GLY   B 106 ? 0.1383 0.1428 0.1454 0.0034  -0.0230 0.0205  112 GLY   C N   
1925 C CA  . GLY   B 106 ? 0.1316 0.1327 0.1315 0.0040  -0.0230 0.0182  112 GLY   C CA  
1926 C C   . GLY   B 106 ? 0.1310 0.1323 0.1326 0.0055  -0.0214 0.0159  112 GLY   C C   
1927 O O   . GLY   B 106 ? 0.1309 0.1347 0.1363 0.0065  -0.0197 0.0151  112 GLY   C O   
1928 N N   . ILE   B 107 ? 0.1310 0.1296 0.1295 0.0054  -0.0219 0.0148  113 ILE   C N   
1929 C CA  . ILE   B 107 ? 0.1353 0.1335 0.1343 0.0066  -0.0206 0.0130  113 ILE   C CA  
1930 C C   . ILE   B 107 ? 0.1324 0.1296 0.1272 0.0086  -0.0199 0.0113  113 ILE   C C   
1931 O O   . ILE   B 107 ? 0.1378 0.1328 0.1277 0.0091  -0.0202 0.0109  113 ILE   C O   
1932 C CB  . ILE   B 107 ? 0.1750 0.1705 0.1732 0.0055  -0.0212 0.0132  113 ILE   C CB  
1933 C CG1 . ILE   B 107 ? 0.2080 0.2056 0.2138 0.0041  -0.0208 0.0147  113 ILE   C CG1 
1934 C CG2 . ILE   B 107 ? 0.1769 0.1703 0.1719 0.0069  -0.0201 0.0115  113 ILE   C CG2 
1935 C CD1 . ILE   B 107 ? 0.2502 0.2456 0.2572 0.0027  -0.0211 0.0154  113 ILE   C CD1 
1936 N N   . LEU   B 108 ? 0.1247 0.1238 0.1220 0.0097  -0.0189 0.0101  114 LEU   C N   
1937 C CA  . LEU   B 108 ? 0.1127 0.1110 0.1073 0.0117  -0.0188 0.0087  114 LEU   C CA  
1938 C C   . LEU   B 108 ? 0.1243 0.1199 0.1162 0.0118  -0.0191 0.0082  114 LEU   C C   
1939 O O   . LEU   B 108 ? 0.1220 0.1182 0.1161 0.0109  -0.0186 0.0081  114 LEU   C O   
1940 C CB  . LEU   B 108 ? 0.1229 0.1248 0.1219 0.0126  -0.0183 0.0079  114 LEU   C CB  
1941 C CG  . LEU   B 108 ? 0.1213 0.1233 0.1194 0.0144  -0.0189 0.0066  114 LEU   C CG  
1942 C CD1 . LEU   B 108 ? 0.1344 0.1354 0.1304 0.0161  -0.0185 0.0067  114 LEU   C CD1 
1943 C CD2 . LEU   B 108 ? 0.1233 0.1290 0.1268 0.0146  -0.0191 0.0058  114 LEU   C CD2 
1944 N N   . ARG   B 109 ? 0.1265 0.1190 0.1139 0.0128  -0.0196 0.0079  115 ARG   C N   
1945 C CA  . ARG   B 109 ? 0.1425 0.1319 0.1268 0.0129  -0.0198 0.0079  115 ARG   C CA  
1946 C C   . ARG   B 109 ? 0.1510 0.1390 0.1325 0.0151  -0.0206 0.0074  115 ARG   C C   
1947 O O   . ARG   B 109 ? 0.1505 0.1386 0.1321 0.0165  -0.0207 0.0071  115 ARG   C O   
1948 C CB  . ARG   B 109 ? 0.1939 0.1799 0.1761 0.0115  -0.0198 0.0087  115 ARG   C CB  
1949 C CG  . ARG   B 109 ? 0.2736 0.2570 0.2526 0.0121  -0.0204 0.0084  115 ARG   C CG  
1950 C CD  . ARG   B 109 ? 0.4027 0.3825 0.3800 0.0103  -0.0209 0.0091  115 ARG   C CD  
1951 N NE  . ARG   B 109 ? 0.4969 0.4785 0.4772 0.0080  -0.0216 0.0099  115 ARG   C NE  
1952 C CZ  . ARG   B 109 ? 0.5828 0.5651 0.5669 0.0062  -0.0215 0.0111  115 ARG   C CZ  
1953 N NH1 . ARG   B 109 ? 0.5662 0.5474 0.5509 0.0063  -0.0202 0.0113  115 ARG   C NH1 
1954 N NH2 . ARG   B 109 ? 0.6029 0.5872 0.5906 0.0044  -0.0227 0.0122  115 ARG   C NH2 
1955 N N   . CYS   B 110 ? 0.1500 0.1363 0.1290 0.0153  -0.0209 0.0075  116 CYS   C N   
1956 C CA  . CYS   B 110 ? 0.1590 0.1436 0.1352 0.0173  -0.0223 0.0076  116 CYS   C CA  
1957 C C   . CYS   B 110 ? 0.1760 0.1556 0.1473 0.0168  -0.0219 0.0088  116 CYS   C C   
1958 O O   . CYS   B 110 ? 0.1778 0.1558 0.1489 0.0150  -0.0206 0.0092  116 CYS   C O   
1959 C CB  . CYS   B 110 ? 0.1449 0.1319 0.1218 0.0178  -0.0237 0.0070  116 CYS   C CB  
1960 S SG  . CYS   B 110 ? 0.1538 0.1394 0.1274 0.0159  -0.0227 0.0067  116 CYS   C SG  
1961 N N   . GLN   B 111 ? 0.1826 0.1596 0.1504 0.0184  -0.0233 0.0096  117 GLN   C N   
1962 C CA  . GLN   B 111 ? 0.2070 0.1789 0.1700 0.0180  -0.0226 0.0110  117 GLN   C CA  
1963 C C   . GLN   B 111 ? 0.2167 0.1877 0.1774 0.0160  -0.0210 0.0113  117 GLN   C C   
1964 O O   . GLN   B 111 ? 0.2367 0.2040 0.1950 0.0150  -0.0194 0.0125  117 GLN   C O   
1965 C CB  . GLN   B 111 ? 0.2236 0.1928 0.1833 0.0202  -0.0246 0.0124  117 GLN   C CB  
1966 C CG  . GLN   B 111 ? 0.2713 0.2421 0.2286 0.0206  -0.0266 0.0124  117 GLN   C CG  
1967 C CD  . GLN   B 111 ? 0.4082 0.3768 0.3628 0.0228  -0.0295 0.0142  117 GLN   C CD  
1968 O OE1 . GLN   B 111 ? 0.4577 0.4292 0.4163 0.0247  -0.0318 0.0141  117 GLN   C OE1 
1969 N NE2 . GLN   B 111 ? 0.4299 0.3935 0.3781 0.0226  -0.0294 0.0162  117 GLN   C NE2 
1970 N N   . HIS   B 112 ? 0.1894 0.1637 0.1514 0.0154  -0.0209 0.0100  118 HIS   C N   
1971 C CA  . HIS   B 112 ? 0.1833 0.1564 0.1431 0.0136  -0.0186 0.0098  118 HIS   C CA  
1972 C C   . HIS   B 112 ? 0.1864 0.1612 0.1516 0.0117  -0.0161 0.0095  118 HIS   C C   
1973 O O   . HIS   B 112 ? 0.1932 0.1667 0.1577 0.0103  -0.0134 0.0094  118 HIS   C O   
1974 C CB  . HIS   B 112 ? 0.1806 0.1553 0.1382 0.0137  -0.0197 0.0084  118 HIS   C CB  
1975 C CG  . HIS   B 112 ? 0.1965 0.1698 0.1493 0.0155  -0.0230 0.0091  118 HIS   C CG  
1976 N ND1 . HIS   B 112 ? 0.1460 0.1229 0.1023 0.0170  -0.0262 0.0085  118 HIS   C ND1 
1977 C CD2 . HIS   B 112 ? 0.2191 0.1879 0.1642 0.0158  -0.0236 0.0106  118 HIS   C CD2 
1978 C CE1 . HIS   B 112 ? 0.1985 0.1732 0.1500 0.0183  -0.0290 0.0097  118 HIS   C CE1 
1979 N NE2 . HIS   B 112 ? 0.2257 0.1954 0.1699 0.0177  -0.0277 0.0111  118 HIS   C NE2 
1980 N N   . GLY   B 113 ? 0.1637 0.1416 0.1343 0.0117  -0.0168 0.0092  119 GLY   C N   
1981 C CA  . GLY   B 113 ? 0.1622 0.1421 0.1385 0.0099  -0.0152 0.0093  119 GLY   C CA  
1982 C C   . GLY   B 113 ? 0.1491 0.1335 0.1304 0.0100  -0.0162 0.0085  119 GLY   C C   
1983 O O   . GLY   B 113 ? 0.1532 0.1389 0.1340 0.0114  -0.0179 0.0080  119 GLY   C O   
1984 N N   . VAL   B 114 ? 0.1398 0.1263 0.1265 0.0086  -0.0148 0.0086  120 VAL   C N   
1985 C CA  . VAL   B 114 ? 0.1368 0.1273 0.1287 0.0085  -0.0155 0.0084  120 VAL   C CA  
1986 C C   . VAL   B 114 ? 0.1353 0.1279 0.1278 0.0092  -0.0154 0.0067  120 VAL   C C   
1987 O O   . VAL   B 114 ? 0.1462 0.1381 0.1383 0.0087  -0.0138 0.0057  120 VAL   C O   
1988 C CB  . VAL   B 114 ? 0.1530 0.1451 0.1514 0.0067  -0.0143 0.0096  120 VAL   C CB  
1989 C CG1 . VAL   B 114 ? 0.1668 0.1627 0.1704 0.0067  -0.0150 0.0097  120 VAL   C CG1 
1990 C CG2 . VAL   B 114 ? 0.1651 0.1554 0.1637 0.0056  -0.0152 0.0112  120 VAL   C CG2 
1991 N N   . VAL   B 115 ? 0.1200 0.1150 0.1135 0.0103  -0.0170 0.0063  121 VAL   C N   
1992 C CA  . VAL   B 115 ? 0.1254 0.1228 0.1206 0.0109  -0.0175 0.0048  121 VAL   C CA  
1993 C C   . VAL   B 115 ? 0.1336 0.1341 0.1356 0.0099  -0.0164 0.0047  121 VAL   C C   
1994 O O   . VAL   B 115 ? 0.1367 0.1382 0.1410 0.0094  -0.0158 0.0032  121 VAL   C O   
1995 C CB  . VAL   B 115 ? 0.1268 0.1255 0.1212 0.0126  -0.0194 0.0047  121 VAL   C CB  
1996 C CG1 . VAL   B 115 ? 0.1391 0.1407 0.1368 0.0130  -0.0203 0.0032  121 VAL   C CG1 
1997 C CG2 . VAL   B 115 ? 0.1558 0.1511 0.1441 0.0138  -0.0206 0.0049  121 VAL   C CG2 
1998 N N   . GLY   B 116 ? 0.1255 0.1274 0.1307 0.0094  -0.0163 0.0064  122 GLY   C N   
1999 C CA  . GLY   B 116 ? 0.1333 0.1381 0.1453 0.0086  -0.0155 0.0071  122 GLY   C CA  
2000 C C   . GLY   B 116 ? 0.1214 0.1269 0.1345 0.0082  -0.0162 0.0094  122 GLY   C C   
2001 O O   . GLY   B 116 ? 0.1215 0.1249 0.1301 0.0082  -0.0171 0.0100  122 GLY   C O   
2002 N N   . ILE   B 117 ? 0.1157 0.1238 0.1344 0.0076  -0.0158 0.0106  123 ILE   C N   
2003 C CA  . ILE   B 117 ? 0.1122 0.1206 0.1309 0.0070  -0.0167 0.0131  123 ILE   C CA  
2004 C C   . ILE   B 117 ? 0.1028 0.1135 0.1234 0.0074  -0.0163 0.0137  123 ILE   C C   
2005 O O   . ILE   B 117 ? 0.1165 0.1294 0.1420 0.0077  -0.0152 0.0128  123 ILE   C O   
2006 C CB  . ILE   B 117 ? 0.1253 0.1342 0.1494 0.0054  -0.0169 0.0153  123 ILE   C CB  
2007 C CG1 . ILE   B 117 ? 0.1381 0.1490 0.1703 0.0052  -0.0150 0.0150  123 ILE   C CG1 
2008 C CG2 . ILE   B 117 ? 0.1431 0.1497 0.1654 0.0047  -0.0173 0.0153  123 ILE   C CG2 
2009 C CD1 . ILE   B 117 ? 0.1478 0.1597 0.1878 0.0039  -0.0150 0.0178  123 ILE   C CD1 
2010 N N   . VAL   B 118 ? 0.1113 0.1213 0.1280 0.0073  -0.0170 0.0153  124 VAL   C N   
2011 C CA  . VAL   B 118 ? 0.1115 0.1233 0.1296 0.0076  -0.0160 0.0164  124 VAL   C CA  
2012 C C   . VAL   B 118 ? 0.1089 0.1231 0.1347 0.0067  -0.0154 0.0182  124 VAL   C C   
2013 O O   . VAL   B 118 ? 0.1081 0.1221 0.1364 0.0055  -0.0165 0.0202  124 VAL   C O   
2014 C CB  . VAL   B 118 ? 0.1083 0.1180 0.1195 0.0073  -0.0165 0.0180  124 VAL   C CB  
2015 C CG1 . VAL   B 118 ? 0.1259 0.1372 0.1382 0.0074  -0.0148 0.0196  124 VAL   C CG1 
2016 C CG2 . VAL   B 118 ? 0.1274 0.1344 0.1317 0.0084  -0.0165 0.0159  124 VAL   C CG2 
2017 N N   . SER   B 119 ? 0.1123 0.1289 0.1430 0.0072  -0.0138 0.0178  125 SER   C N   
2018 C CA  . SER   B 119 ? 0.0984 0.1169 0.1370 0.0064  -0.0129 0.0195  125 SER   C CA  
2019 C C   . SER   B 119 ? 0.1244 0.1445 0.1650 0.0066  -0.0114 0.0212  125 SER   C C   
2020 O O   . SER   B 119 ? 0.1386 0.1596 0.1842 0.0057  -0.0110 0.0240  125 SER   C O   
2021 C CB  . SER   B 119 ? 0.1095 0.1288 0.1536 0.0065  -0.0123 0.0167  125 SER   C CB  
2022 O OG  . SER   B 119 ? 0.1206 0.1414 0.1733 0.0058  -0.0111 0.0179  125 SER   C OG  
2023 N N   . THR   B 120 ? 0.1245 0.1451 0.1623 0.0077  -0.0103 0.0198  126 THR   C N   
2024 C CA  . THR   B 120 ? 0.1146 0.1368 0.1553 0.0078  -0.0080 0.0213  126 THR   C CA  
2025 C C   . THR   B 120 ? 0.1216 0.1424 0.1549 0.0088  -0.0067 0.0215  126 THR   C C   
2026 O O   . THR   B 120 ? 0.1193 0.1382 0.1465 0.0096  -0.0077 0.0196  126 THR   C O   
2027 C CB  . THR   B 120 ? 0.1130 0.1381 0.1624 0.0082  -0.0069 0.0192  126 THR   C CB  
2028 O OG1 . THR   B 120 ? 0.1341 0.1597 0.1814 0.0095  -0.0073 0.0163  126 THR   C OG1 
2029 C CG2 . THR   B 120 ? 0.1346 0.1603 0.1903 0.0073  -0.0078 0.0181  126 THR   C CG2 
2030 N N   . GLY   B 121 ? 0.1295 0.1509 0.1634 0.0087  -0.0042 0.0237  127 GLY   C N   
2031 C CA  . GLY   B 121 ? 0.1528 0.1727 0.1803 0.0097  -0.0017 0.0235  127 GLY   C CA  
2032 C C   . GLY   B 121 ? 0.1963 0.2181 0.2285 0.0097  0.0020  0.0255  127 GLY   C C   
2033 O O   . GLY   B 121 ? 0.2139 0.2366 0.2505 0.0085  0.0024  0.0282  127 GLY   C O   
2034 N N   . GLY   B 122 ? 0.2369 0.2588 0.2682 0.0110  0.0052  0.0245  128 GLY   C N   
2035 C CA  . GLY   B 122 ? 0.2586 0.2822 0.2949 0.0111  0.0095  0.0263  128 GLY   C CA  
2036 C C   . GLY   B 122 ? 0.2624 0.2882 0.3035 0.0130  0.0120  0.0239  128 GLY   C C   
2037 O O   . GLY   B 122 ? 0.2633 0.2905 0.3079 0.0140  0.0095  0.0211  128 GLY   C O   
2038 N N   . ASN   B 123 ? 0.2576 0.2832 0.2989 0.0135  0.0171  0.0254  129 ASN   C N   
2039 C CA  . ASN   B 123 ? 0.2671 0.2951 0.3150 0.0154  0.0203  0.0236  129 ASN   C CA  
2040 C C   . ASN   B 123 ? 0.2475 0.2736 0.2901 0.0173  0.0193  0.0206  129 ASN   C C   
2041 O O   . ASN   B 123 ? 0.2600 0.2890 0.3107 0.0189  0.0198  0.0189  129 ASN   C O   
2042 C CB  . ASN   B 123 ? 0.3108 0.3444 0.3736 0.0153  0.0186  0.0227  129 ASN   C CB  
2043 C CG  . ASN   B 123 ? 0.4021 0.4381 0.4734 0.0141  0.0219  0.0254  129 ASN   C CG  
2044 O OD1 . ASN   B 123 ? 0.4040 0.4389 0.4734 0.0142  0.0272  0.0277  129 ASN   C OD1 
2045 N ND2 . ASN   B 123 ? 0.4438 0.4830 0.5247 0.0129  0.0190  0.0250  129 ASN   C ND2 
2046 N N   . GLY   B 124 ? 0.2259 0.2471 0.2560 0.0170  0.0177  0.0202  130 GLY   C N   
2047 C CA  . GLY   B 124 ? 0.2065 0.2252 0.2317 0.0186  0.0167  0.0175  130 GLY   C CA  
2048 C C   . GLY   B 124 ? 0.1866 0.2071 0.2157 0.0189  0.0113  0.0155  130 GLY   C C   
2049 O O   . GLY   B 124 ? 0.1780 0.1974 0.2059 0.0205  0.0103  0.0135  130 GLY   C O   
2050 N N   . LEU   B 125 ? 0.1641 0.1870 0.1974 0.0173  0.0080  0.0162  131 LEU   C N   
2051 C CA  . LEU   B 125 ? 0.1531 0.1772 0.1890 0.0173  0.0033  0.0144  131 LEU   C CA  
2052 C C   . LEU   B 125 ? 0.1577 0.1791 0.1870 0.0155  0.0004  0.0151  131 LEU   C C   
2053 O O   . LEU   B 125 ? 0.2044 0.2247 0.2308 0.0141  0.0013  0.0175  131 LEU   C O   
2054 C CB  . LEU   B 125 ? 0.1721 0.2011 0.2199 0.0168  0.0021  0.0141  131 LEU   C CB  
2055 C CG  . LEU   B 125 ? 0.2154 0.2480 0.2727 0.0184  0.0041  0.0135  131 LEU   C CG  
2056 C CD1 . LEU   B 125 ? 0.2454 0.2824 0.3141 0.0172  0.0034  0.0136  131 LEU   C CD1 
2057 C CD2 . LEU   B 125 ? 0.2298 0.2626 0.2874 0.0203  0.0018  0.0114  131 LEU   C CD2 
2058 N N   . VAL   B 126 ? 0.1237 0.1439 0.1504 0.0157  -0.0029 0.0134  132 VAL   C N   
2059 C CA  . VAL   B 126 ? 0.1200 0.1382 0.1424 0.0141  -0.0056 0.0140  132 VAL   C CA  
2060 C C   . VAL   B 126 ? 0.1129 0.1331 0.1409 0.0138  -0.0082 0.0124  132 VAL   C C   
2061 O O   . VAL   B 126 ? 0.1149 0.1361 0.1449 0.0151  -0.0092 0.0105  132 VAL   C O   
2062 C CB  . VAL   B 126 ? 0.1398 0.1535 0.1525 0.0143  -0.0068 0.0133  132 VAL   C CB  
2063 C CG1 . VAL   B 126 ? 0.1640 0.1767 0.1756 0.0162  -0.0072 0.0111  132 VAL   C CG1 
2064 C CG2 . VAL   B 126 ? 0.1392 0.1516 0.1498 0.0126  -0.0097 0.0139  132 VAL   C CG2 
2065 N N   . GLY   B 127 ? 0.1146 0.1355 0.1455 0.0123  -0.0090 0.0133  133 GLY   C N   
2066 C CA  . GLY   B 127 ? 0.1100 0.1320 0.1451 0.0118  -0.0108 0.0116  133 GLY   C CA  
2067 C C   . GLY   B 127 ? 0.1082 0.1276 0.1391 0.0109  -0.0124 0.0115  133 GLY   C C   
2068 O O   . GLY   B 127 ? 0.1148 0.1329 0.1438 0.0099  -0.0123 0.0136  133 GLY   C O   
2069 N N   . PHE   B 128 ? 0.1037 0.1223 0.1335 0.0112  -0.0139 0.0093  134 PHE   C N   
2070 C CA  . PHE   B 128 ? 0.1094 0.1255 0.1358 0.0105  -0.0148 0.0090  134 PHE   C CA  
2071 C C   . PHE   B 128 ? 0.0963 0.1128 0.1267 0.0096  -0.0147 0.0074  134 PHE   C C   
2072 O O   . PHE   B 128 ? 0.1037 0.1211 0.1358 0.0099  -0.0154 0.0053  134 PHE   C O   
2073 C CB  . PHE   B 128 ? 0.1180 0.1315 0.1377 0.0115  -0.0160 0.0078  134 PHE   C CB  
2074 C CG  . PHE   B 128 ? 0.1179 0.1304 0.1333 0.0127  -0.0157 0.0086  134 PHE   C CG  
2075 C CD1 . PHE   B 128 ? 0.1170 0.1270 0.1278 0.0120  -0.0157 0.0100  134 PHE   C CD1 
2076 C CD2 . PHE   B 128 ? 0.1311 0.1447 0.1475 0.0143  -0.0155 0.0077  134 PHE   C CD2 
2077 C CE1 . PHE   B 128 ? 0.1278 0.1360 0.1339 0.0129  -0.0151 0.0101  134 PHE   C CE1 
2078 C CE2 . PHE   B 128 ? 0.1296 0.1418 0.1424 0.0155  -0.0145 0.0081  134 PHE   C CE2 
2079 C CZ  . PHE   B 128 ? 0.1313 0.1405 0.1384 0.0147  -0.0142 0.0091  134 PHE   C CZ  
2080 N N   . ALA   B 129 ? 0.1006 0.1162 0.1328 0.0084  -0.0141 0.0084  135 ALA   C N   
2081 C CA  . ALA   B 129 ? 0.1003 0.1153 0.1356 0.0076  -0.0133 0.0065  135 ALA   C CA  
2082 C C   . ALA   B 129 ? 0.1251 0.1370 0.1538 0.0078  -0.0137 0.0047  135 ALA   C C   
2083 O O   . ALA   B 129 ? 0.1178 0.1280 0.1432 0.0077  -0.0137 0.0059  135 ALA   C O   
2084 C CB  . ALA   B 129 ? 0.1143 0.1293 0.1550 0.0065  -0.0119 0.0085  135 ALA   C CB  
2085 N N   . ASP   B 130 ? 0.1154 0.1267 0.1422 0.0080  -0.0143 0.0020  136 ASP   C N   
2086 C CA  . ASP   B 130 ? 0.1184 0.1266 0.1380 0.0082  -0.0148 0.0006  136 ASP   C CA  
2087 C C   . ASP   B 130 ? 0.1210 0.1267 0.1408 0.0071  -0.0123 0.0002  136 ASP   C C   
2088 O O   . ASP   B 130 ? 0.1283 0.1346 0.1540 0.0062  -0.0105 -0.0005 136 ASP   C O   
2089 C CB  . ASP   B 130 ? 0.1346 0.1428 0.1522 0.0084  -0.0166 -0.0021 136 ASP   C CB  
2090 C CG  . ASP   B 130 ? 0.1676 0.1722 0.1764 0.0086  -0.0177 -0.0033 136 ASP   C CG  
2091 O OD1 . ASP   B 130 ? 0.1552 0.1585 0.1596 0.0096  -0.0183 -0.0018 136 ASP   C OD1 
2092 O OD2 . ASP   B 130 ? 0.1968 0.1991 0.2026 0.0077  -0.0173 -0.0057 136 ASP   C OD2 
2093 N N   . VAL   B 131 ? 0.1162 0.1190 0.1301 0.0072  -0.0119 0.0005  137 VAL   C N   
2094 C CA  . VAL   B 131 ? 0.1229 0.1230 0.1367 0.0062  -0.0089 -0.0001 137 VAL   C CA  
2095 C C   . VAL   B 131 ? 0.1358 0.1319 0.1405 0.0062  -0.0086 -0.0019 137 VAL   C C   
2096 O O   . VAL   B 131 ? 0.1404 0.1335 0.1436 0.0054  -0.0055 -0.0025 137 VAL   C O   
2097 C CB  . VAL   B 131 ? 0.1353 0.1353 0.1521 0.0058  -0.0078 0.0026  137 VAL   C CB  
2098 C CG1 . VAL   B 131 ? 0.1326 0.1361 0.1579 0.0055  -0.0083 0.0048  137 VAL   C CG1 
2099 C CG2 . VAL   B 131 ? 0.1380 0.1366 0.1486 0.0065  -0.0097 0.0041  137 VAL   C CG2 
2100 N N   . ARG   B 132 ? 0.1360 0.1318 0.1348 0.0071  -0.0117 -0.0027 138 ARG   C N   
2101 C CA  . ARG   B 132 ? 0.1417 0.1334 0.1310 0.0072  -0.0120 -0.0036 138 ARG   C CA  
2102 C C   . ARG   B 132 ? 0.1494 0.1381 0.1347 0.0060  -0.0104 -0.0067 138 ARG   C C   
2103 O O   . ARG   B 132 ? 0.1668 0.1512 0.1433 0.0057  -0.0094 -0.0073 138 ARG   C O   
2104 C CB  . ARG   B 132 ? 0.1562 0.1486 0.1413 0.0086  -0.0162 -0.0031 138 ARG   C CB  
2105 C CG  . ARG   B 132 ? 0.1310 0.1246 0.1178 0.0098  -0.0171 -0.0005 138 ARG   C CG  
2106 C CD  . ARG   B 132 ? 0.1439 0.1382 0.1280 0.0114  -0.0207 -0.0001 138 ARG   C CD  
2107 N NE  . ARG   B 132 ? 0.1385 0.1369 0.1286 0.0116  -0.0223 -0.0011 138 ARG   C NE  
2108 C CZ  . ARG   B 132 ? 0.1492 0.1497 0.1406 0.0131  -0.0251 -0.0008 138 ARG   C CZ  
2109 N NH1 . ARG   B 132 ? 0.1352 0.1337 0.1217 0.0145  -0.0271 0.0003  138 ARG   C NH1 
2110 N NH2 . ARG   B 132 ? 0.1495 0.1540 0.1478 0.0131  -0.0260 -0.0015 138 ARG   C NH2 
2111 N N   . ASP   B 133 ? 0.1431 0.1336 0.1342 0.0053  -0.0098 -0.0087 139 ASP   C N   
2112 C CA  . ASP   B 133 ? 0.1552 0.1423 0.1425 0.0039  -0.0080 -0.0121 139 ASP   C CA  
2113 C C   . ASP   B 133 ? 0.1719 0.1567 0.1622 0.0031  -0.0023 -0.0126 139 ASP   C C   
2114 O O   . ASP   B 133 ? 0.1845 0.1654 0.1706 0.0019  0.0004  -0.0156 139 ASP   C O   
2115 C CB  . ASP   B 133 ? 0.1677 0.1575 0.1606 0.0034  -0.0099 -0.0144 139 ASP   C CB  
2116 C CG  . ASP   B 133 ? 0.1982 0.1918 0.2034 0.0034  -0.0081 -0.0131 139 ASP   C CG  
2117 O OD1 . ASP   B 133 ? 0.1783 0.1746 0.1875 0.0043  -0.0083 -0.0098 139 ASP   C OD1 
2118 O OD2 . ASP   B 133 ? 0.2170 0.2103 0.2273 0.0023  -0.0063 -0.0154 139 ASP   C OD2 
2119 N N   . LEU   B 134 ? 0.1612 0.1481 0.1588 0.0035  -0.0004 -0.0096 140 LEU   C N   
2120 C CA  . LEU   B 134 ? 0.1640 0.1496 0.1674 0.0028  0.0048  -0.0094 140 LEU   C CA  
2121 C C   . LEU   B 134 ? 0.1634 0.1449 0.1598 0.0026  0.0077  -0.0088 140 LEU   C C   
2122 O O   . LEU   B 134 ? 0.1611 0.1434 0.1609 0.0028  0.0086  -0.0058 140 LEU   C O   
2123 C CB  . LEU   B 134 ? 0.1504 0.1406 0.1655 0.0031  0.0045  -0.0062 140 LEU   C CB  
2124 C CG  . LEU   B 134 ? 0.1635 0.1577 0.1853 0.0033  0.0019  -0.0061 140 LEU   C CG  
2125 C CD1 . LEU   B 134 ? 0.1663 0.1643 0.1981 0.0036  0.0014  -0.0023 140 LEU   C CD1 
2126 C CD2 . LEU   B 134 ? 0.1860 0.1790 0.2113 0.0025  0.0042  -0.0093 140 LEU   C CD2 
2127 N N   . LEU   B 135 ? 0.1765 0.1531 0.1623 0.0020  0.0090  -0.0116 141 LEU   C N   
2128 C CA  . LEU   B 135 ? 0.1902 0.1621 0.1670 0.0018  0.0116  -0.0109 141 LEU   C CA  
2129 C C   . LEU   B 135 ? 0.1903 0.1609 0.1734 0.0012  0.0180  -0.0100 141 LEU   C C   
2130 O O   . LEU   B 135 ? 0.2018 0.1706 0.1825 0.0013  0.0198  -0.0077 141 LEU   C O   
2131 C CB  . LEU   B 135 ? 0.2021 0.1685 0.1649 0.0011  0.0116  -0.0140 141 LEU   C CB  
2132 C CG  . LEU   B 135 ? 0.2746 0.2403 0.2271 0.0017  0.0056  -0.0133 141 LEU   C CG  
2133 C CD1 . LEU   B 135 ? 0.2553 0.2269 0.2145 0.0028  -0.0003 -0.0121 141 LEU   C CD1 
2134 C CD2 . LEU   B 135 ? 0.2940 0.2554 0.2353 0.0006  0.0042  -0.0171 141 LEU   C CD2 
2135 N N   . TRP   B 136 ? 0.1927 0.1644 0.1853 0.0008  0.0213  -0.0114 142 TRP   C N   
2136 C CA  . TRP   B 136 ? 0.2049 0.1758 0.2059 0.0005  0.0276  -0.0106 142 TRP   C CA  
2137 C C   . TRP   B 136 ? 0.2033 0.1784 0.2139 0.0009  0.0262  -0.0060 142 TRP   C C   
2138 O O   . TRP   B 136 ? 0.2163 0.1908 0.2333 0.0005  0.0308  -0.0046 142 TRP   C O   
2139 C CB  . TRP   B 136 ? 0.1958 0.1670 0.2058 0.0001  0.0311  -0.0130 142 TRP   C CB  
2140 C CG  . TRP   B 136 ? 0.1812 0.1578 0.2000 0.0006  0.0264  -0.0122 142 TRP   C CG  
2141 C CD1 . TRP   B 136 ? 0.2010 0.1780 0.2167 0.0005  0.0230  -0.0147 142 TRP   C CD1 
2142 C CD2 . TRP   B 136 ? 0.1816 0.1636 0.2141 0.0011  0.0248  -0.0084 142 TRP   C CD2 
2143 N NE1 . TRP   B 136 ? 0.1964 0.1787 0.2229 0.0010  0.0199  -0.0127 142 TRP   C NE1 
2144 C CE2 . TRP   B 136 ? 0.1838 0.1690 0.2201 0.0013  0.0210  -0.0088 142 TRP   C CE2 
2145 C CE3 . TRP   B 136 ? 0.1884 0.1727 0.2306 0.0012  0.0263  -0.0047 142 TRP   C CE3 
2146 C CZ2 . TRP   B 136 ? 0.1843 0.1745 0.2320 0.0018  0.0186  -0.0053 142 TRP   C CZ2 
2147 C CZ3 . TRP   B 136 ? 0.1971 0.1865 0.2509 0.0015  0.0234  -0.0014 142 TRP   C CZ3 
2148 C CH2 . TRP   B 136 ? 0.1931 0.1851 0.2490 0.0018  0.0198  -0.0017 142 TRP   C CH2 
2149 N N   . LEU   B 137 ? 0.1858 0.1651 0.1978 0.0015  0.0201  -0.0038 143 LEU   C N   
2150 C CA  . LEU   B 137 ? 0.1980 0.1805 0.2174 0.0016  0.0183  0.0002  143 LEU   C CA  
2151 C C   . LEU   B 137 ? 0.2233 0.2024 0.2366 0.0013  0.0201  0.0016  143 LEU   C C   
2152 O O   . LEU   B 137 ? 0.2487 0.2295 0.2694 0.0009  0.0203  0.0045  143 LEU   C O   
2153 C CB  . LEU   B 137 ? 0.1959 0.1821 0.2149 0.0023  0.0119  0.0017  143 LEU   C CB  
2154 C CG  . LEU   B 137 ? 0.1805 0.1708 0.2076 0.0025  0.0099  0.0017  143 LEU   C CG  
2155 C CD1 . LEU   B 137 ? 0.1928 0.1858 0.2167 0.0032  0.0042  0.0027  143 LEU   C CD1 
2156 C CD2 . LEU   B 137 ? 0.1929 0.1862 0.2332 0.0021  0.0111  0.0044  143 LEU   C CD2 
2157 N N   . ASP   B 138 ? 0.2239 0.1983 0.2243 0.0013  0.0211  -0.0002 144 ASP   C N   
2158 C CA  . ASP   B 138 ? 0.2456 0.2162 0.2391 0.0010  0.0228  0.0013  144 ASP   C CA  
2159 C C   . ASP   B 138 ? 0.2931 0.2602 0.2886 0.0001  0.0305  0.0010  144 ASP   C C   
2160 O O   . ASP   B 138 ? 0.3037 0.2675 0.2945 -0.0003 0.0328  0.0026  144 ASP   C O   
2161 C CB  . ASP   B 138 ? 0.2585 0.2253 0.2369 0.0015  0.0204  0.0001  144 ASP   C CB  
2162 C CG  . ASP   B 138 ? 0.2484 0.2182 0.2247 0.0026  0.0133  0.0007  144 ASP   C CG  
2163 O OD1 . ASP   B 138 ? 0.2418 0.2161 0.2268 0.0029  0.0105  0.0023  144 ASP   C OD1 
2164 O OD2 . ASP   B 138 ? 0.2796 0.2472 0.2454 0.0031  0.0106  -0.0005 144 ASP   C OD2 
2165 N N   . GLU   B 139 ? 0.3130 0.2804 0.3155 -0.0002 0.0348  -0.0009 145 GLU   C N   
2166 C CA  . GLU   B 139 ? 0.3673 0.3309 0.3717 -0.0009 0.0430  -0.0016 145 GLU   C CA  
2167 C C   . GLU   B 139 ? 0.4111 0.3787 0.4336 -0.0010 0.0463  -0.0002 145 GLU   C C   
2168 O O   . GLU   B 139 ? 0.4211 0.3935 0.4528 -0.0006 0.0426  0.0003  145 GLU   C O   
2169 C CB  . GLU   B 139 ? 0.4265 0.3844 0.4188 -0.0012 0.0467  -0.0060 145 GLU   C CB  
2170 C CG  . GLU   B 139 ? 0.5324 0.4921 0.5270 -0.0009 0.0445  -0.0091 145 GLU   C CG  
2171 C CD  . GLU   B 139 ? 0.6636 0.6181 0.6430 -0.0014 0.0442  -0.0134 145 GLU   C CD  
2172 O OE1 . GLU   B 139 ? 0.6653 0.6193 0.6471 -0.0017 0.0455  -0.0169 145 GLU   C OE1 
2173 O OE2 . GLU   B 139 ? 0.7157 0.6665 0.6809 -0.0015 0.0422  -0.0133 145 GLU   C OE2 
2174 N N   . GLU   B 140 ? 0.4379 0.4035 0.4660 -0.0016 0.0532  0.0009  146 GLU   C N   
2175 C CA  . GLU   B 140 ? 0.4650 0.4342 0.5116 -0.0017 0.0567  0.0026  146 GLU   C CA  
2176 C C   . GLU   B 140 ? 0.4799 0.4498 0.5326 -0.0012 0.0588  -0.0003 146 GLU   C C   
2177 O O   . GLU   B 140 ? 0.4992 0.4644 0.5410 -0.0012 0.0614  -0.0044 146 GLU   C O   
2178 C CB  . GLU   B 140 ? 0.5144 0.4803 0.5646 -0.0024 0.0651  0.0036  146 GLU   C CB  
2179 C CG  . GLU   B 140 ? 0.6151 0.5850 0.6863 -0.0025 0.0691  0.0057  146 GLU   C CG  
2180 C CD  . GLU   B 140 ? 0.7351 0.7114 0.8195 -0.0028 0.0629  0.0104  146 GLU   C CD  
2181 O OE1 . GLU   B 140 ? 0.7595 0.7410 0.8546 -0.0024 0.0583  0.0117  146 GLU   C OE1 
2182 O OE2 . GLU   B 140 ? 0.7701 0.7460 0.8537 -0.0037 0.0626  0.0129  146 GLU   C OE2 
2183 N N1  . A1B5O C .   ? 0.1788 0.1657 0.2148 0.0240  -0.0071 -0.0063 201 A1B5O A N1  
2184 C C4  . A1B5O C .   ? 0.3124 0.3047 0.3480 0.0217  0.0226  -0.0364 201 A1B5O A C4  
2185 C C5  . A1B5O C .   ? 0.3060 0.2945 0.3414 0.0222  0.0184  -0.0336 201 A1B5O A C5  
2186 C C6  . A1B5O C .   ? 0.2832 0.2742 0.3094 0.0202  0.0119  -0.0300 201 A1B5O A C6  
2187 C C7  . A1B5O C .   ? 0.2219 0.2103 0.2537 0.0228  0.0060  -0.0228 201 A1B5O A C7  
2188 C C8  . A1B5O C .   ? 0.2200 0.1988 0.2484 0.0197  0.0067  -0.0282 201 A1B5O A C8  
2189 C C10 . A1B5O C .   ? 0.2097 0.1868 0.2412 0.0208  0.0008  -0.0209 201 A1B5O A C10 
2190 C C13 . A1B5O C .   ? 0.2079 0.1919 0.2477 0.0252  0.0029  -0.0170 201 A1B5O A C13 
2191 O O2  . A1B5O C .   ? 0.1900 0.1710 0.2395 0.0276  -0.0011 -0.0075 201 A1B5O A O2  
2192 C C12 . A1B5O C .   ? 0.1914 0.1749 0.2321 0.0252  -0.0032 -0.0094 201 A1B5O A C12 
2193 C C11 . A1B5O C .   ? 0.1968 0.1795 0.2316 0.0234  -0.0010 -0.0155 201 A1B5O A C11 
2194 C C9  . A1B5O C .   ? 0.2248 0.2026 0.2490 0.0180  0.0025  -0.0265 201 A1B5O A C9  
2195 N N   . A1B5O C .   ? 0.2129 0.1970 0.2451 0.0225  0.0047  -0.0226 201 A1B5O A N   
2196 O O1  . A1B5O C .   ? 0.2150 0.2080 0.2507 0.0247  0.0046  -0.0184 201 A1B5O A O1  
2197 O O   . A1B5O C .   ? 0.2520 0.2392 0.2783 0.0202  0.0091  -0.0286 201 A1B5O A O   
2198 C C1  . A1B5O C .   ? 0.3057 0.2975 0.3199 0.0157  0.0115  -0.0337 201 A1B5O A C1  
2199 S S   . A1B5O C .   ? 0.3104 0.3048 0.3165 0.0142  0.0045  -0.0287 201 A1B5O A S   
2200 C C   . A1B5O C .   ? 0.3381 0.3380 0.3445 0.0149  0.0044  -0.0257 201 A1B5O A C   
2201 C C3  . A1B5O C .   ? 0.3183 0.3114 0.3403 0.0165  0.0222  -0.0404 201 A1B5O A C3  
2202 C C2  . A1B5O C .   ? 0.3199 0.3152 0.3334 0.0149  0.0152  -0.0360 201 A1B5O A C2  
# 
