data_7HPC
# 
_entry.id   7HPC 
# 
_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   7HPC         pdb_00007hpc 10.2210/pdb7hpc/pdb 
WWPDB D_1001407762 ?            ?                   
# 
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 2025-02-26 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_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               'Structure summary' 
# 
_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_deposit_group 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_pdbx_deposit_group.group_description' 
# 
_pdbx_database_status.entry_id                        7HPC 
_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   2024-11-07 
_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              frankfurt.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 
'Ni, X.'              1  
'Marples, P.G.'       2  
'Godoy, A.S.'         3  
'Koekemoer, L.'       4  
'Aschenbrenner, J.C.' 5  
'Balcomb, B.H.'       6  
'Fairhead, M.'        7  
'Lithgo, R.M.'        8  
'Lee, A.'             9  
'Kenton, N.'          10 
'Thompson, W.'        11 
'Tomlinson, C.W.E.'   12 
'Wild, C.'            13 
'Winokan, M.'         14 
'Williams, E.P.'      15 
'Chandran, A.V.'      16 
'Walsh, M.A.'         17 
'Fearon, D.'          18 
'von Delft, F.'       19 
# 
_citation.id                        primary 
_citation.title                     'PanDDA analysis group deposition' 
_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 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
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 'Serine protease subunit NS2B'                                                                      5067.486  1  
?                           ?    ? ? 
2 polymer     man 'Serine protease NS3'                                                                               18117.629 1  
3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                                78.133    4  
?                           ?    ? ? 
4 non-polymer syn '4-methyl-N-[(2-methyl-1H-imidazol-4-yl)methyl]-2-[(3S)-piperidin-3-yl]-1H-imidazole-5-carboxamide' 302.375   1  
?                           ?    ? ? 
5 non-polymer syn 'SULFATE ION'                                                                                       96.063    1  
?                           ?    ? ? 
6 water       nat water                                                                                               18.015    50 
?                           ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                                                                DMS   
4 '4-methyl-N-[(2-methyl-1H-imidazol-4-yl)methyl]-2-[(3S)-piperidin-3-yl]-1H-imidazole-5-carboxamide' A1BGW 
5 'SULFATE ION'                                                                                       SO4   
6 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   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1BGW non-polymer         . '4-methyl-N-[(2-methyl-1H-imidazol-4-yl)methyl]-2-[(3S)-piperidin-3-yl]-1H-imidazole-5-carboxamide' ? 
'C15 H22 N6 O'   302.375 
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 
SO4   non-polymer         . 'SULFATE ION'                                                                                       ? 
'O4 S -2'        96.063  
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 
# 
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   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  ?   ?   ?   B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BGW 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BGW 
_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 3 DMS   1  201 202 DMS   DMS B . 
D 4 A1BGW 1  202 301 A1BGW LIG B . 
E 3 DMS   1  203 302 DMS   DMS B . 
F 5 SO4   1  204 303 SO4   SO4 B . 
G 3 DMS   1  205 304 DMS   DMS B . 
H 3 DMS   1  206 305 DMS   DMS B . 
I 6 HOH   1  101 16  HOH   HOH A . 
I 6 HOH   2  102 118 HOH   HOH A . 
I 6 HOH   3  103 20  HOH   HOH A . 
I 6 HOH   4  104 34  HOH   HOH A . 
I 6 HOH   5  105 124 HOH   HOH A . 
I 6 HOH   6  106 105 HOH   HOH A . 
I 6 HOH   7  107 36  HOH   HOH A . 
I 6 HOH   8  108 50  HOH   HOH A . 
I 6 HOH   9  109 127 HOH   HOH A . 
I 6 HOH   10 110 131 HOH   HOH A . 
I 6 HOH   11 111 119 HOH   HOH A . 
J 6 HOH   1  301 5   HOH   HOH B . 
J 6 HOH   2  302 14  HOH   HOH B . 
J 6 HOH   3  303 68  HOH   HOH B . 
J 6 HOH   4  304 123 HOH   HOH B . 
J 6 HOH   5  305 134 HOH   HOH B . 
J 6 HOH   6  306 11  HOH   HOH B . 
J 6 HOH   7  307 128 HOH   HOH B . 
J 6 HOH   8  308 1   HOH   HOH B . 
J 6 HOH   9  309 24  HOH   HOH B . 
J 6 HOH   10 310 32  HOH   HOH B . 
J 6 HOH   11 311 129 HOH   HOH B . 
J 6 HOH   12 312 4   HOH   HOH B . 
J 6 HOH   13 313 31  HOH   HOH B . 
J 6 HOH   14 314 125 HOH   HOH B . 
J 6 HOH   15 315 56  HOH   HOH B . 
J 6 HOH   16 316 135 HOH   HOH B . 
J 6 HOH   17 317 132 HOH   HOH B . 
J 6 HOH   18 318 28  HOH   HOH B . 
J 6 HOH   19 319 10  HOH   HOH B . 
J 6 HOH   20 320 116 HOH   HOH B . 
J 6 HOH   21 321 18  HOH   HOH B . 
J 6 HOH   22 322 42  HOH   HOH B . 
J 6 HOH   23 323 3   HOH   HOH B . 
J 6 HOH   24 324 39  HOH   HOH B . 
J 6 HOH   25 325 130 HOH   HOH B . 
J 6 HOH   26 326 61  HOH   HOH B . 
J 6 HOH   27 327 21  HOH   HOH B . 
J 6 HOH   28 328 64  HOH   HOH B . 
J 6 HOH   29 329 58  HOH   HOH B . 
J 6 HOH   30 330 23  HOH   HOH B . 
J 6 HOH   31 331 27  HOH   HOH B . 
J 6 HOH   32 332 126 HOH   HOH B . 
J 6 HOH   33 333 136 HOH   HOH B . 
J 6 HOH   34 334 73  HOH   HOH B . 
J 6 HOH   35 335 87  HOH   HOH B . 
J 6 HOH   36 336 44  HOH   HOH B . 
J 6 HOH   37 337 57  HOH   HOH B . 
J 6 HOH   38 338 133 HOH   HOH B . 
J 6 HOH   39 339 75  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (20-OCT-2021)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
'data reduction' XDS     .                      ? 5 
'data reduction' XDS     .                      ? 6 
'data reduction' XDS     .                      ? 7 
'data reduction' XDS     .                      ? 8 
# 
_cell.entry_id           7HPC 
_cell.length_a           42.640 
_cell.length_b           42.640 
_cell.length_c           216.310 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HPC 
_symmetry.space_group_name_H-M             'P 43 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                95 
# 
_exptl.entry_id          7HPC 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.12 
_exptl_crystal.density_percent_sol   41.99 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_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   2023-11-20 
_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   0.92124 
_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        0.92124 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HPC 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             43.26 
_reflns.d_resolution_high            2.10 
_reflns.number_obs                   12602 
_reflns.percent_possible_obs         99.7 
_reflns.pdbx_Rmerge_I_obs            0.170 
_reflns.pdbx_netI_over_sigmaI        8.6 
_reflns.pdbx_redundancy              15.0 
_reflns.pdbx_Rrim_I_all              0.175 
_reflns.pdbx_Rpim_I_all              0.041 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     189018 
_reflns.pdbx_chi_squared             1.00 
_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                  2.10 
_reflns_shell.d_res_low                   2.15 
_reflns_shell.number_measured_all         11625 
_reflns_shell.number_unique_obs           905 
_reflns_shell.Rmerge_I_obs                3.822 
_reflns_shell.pdbx_chi_squared            0.91 
_reflns_shell.pdbx_redundancy             12.8 
_reflns_shell.percent_possible_obs        99.3 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             3.967 
_reflns_shell.pdbx_Rpim_I_all             0.997 
_reflns_shell.pdbx_CC_half                0.197 
_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                                 7HPC 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     12408 
_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                             41.84 
_refine.ls_d_res_high                            2.100 
_refine.ls_percent_reflns_obs                    98.6 
_refine.ls_R_factor_obs                          0.2382 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2356 
_refine.ls_R_factor_R_free                       0.2861 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.790 
_refine.ls_number_reflns_R_free                  594 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.944 
_refine.correlation_coeff_Fo_to_Fc_free          0.920 
_refine.B_iso_mean                               69.82 
_refine.aniso_B[1][1]                            -6.37200 
_refine.aniso_B[2][2]                            -6.37200 
_refine.aniso_B[3][3]                            12.74400 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_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             0.253 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.215 
_refine.pdbx_overall_SU_R_Blow_DPI               0.277 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.222 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HPC 
_refine_analyze.Luzzati_coordinate_error_obs    0.38 
_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        1472 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_refine_hist.number_atoms_solvent             50 
_refine_hist.number_atoms_total               1565 
_refine_hist.d_res_high                       2.100 
_refine_hist.d_res_low                        41.84 
# 
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                  0.008 ? 2.00  1567 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.02  ? 2.00  2128 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  534  '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  266  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1543 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.47  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           18.73 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  194  '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  1182 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   30 
_refine_ls_shell.d_res_high                       2.10 
_refine_ls_shell.d_res_low                        2.13 
_refine_ls_shell.number_reflns_R_work             407 
_refine_ls_shell.R_factor_R_work                  0.4151 
_refine_ls_shell.percent_reflns_obs               90.74 
_refine_ls_shell.R_factor_R_free                  0.4319 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.91 
_refine_ls_shell.number_reflns_R_free             21 
_refine_ls_shell.number_reflns_all                428 
_refine_ls_shell.R_factor_all                     0.4159 
# 
_struct.entry_id                  7HPC 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0015093-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HPC 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, 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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 3 ? 
F N N 5 ? 
G N N 3 ? 
H N N 3 ? 
I N N 6 ? 
J N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
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 7HPC A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HPC B 2 ? 168 ? Q32ZE1 1509 ? 1675 ? 11 177 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7HPC SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HPC MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HPC MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HPC LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5060 ? 
1 MORE         -32  ? 
1 'SSA (A^2)'  9730 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
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 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? 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 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA2 5 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
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 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 4 5 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N LEU B 89  ? N LEU B 98  O PRO B 129 ? O PRO B 138 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7HPC 
_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_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 64 ? ? 74.54   39.53   
2 1 LEU B 30 ? ? -100.89 -165.26 
3 1 CYS B 80 ? ? 75.65   -11.69  
4 1 LEU B 92 ? ? -124.46 -52.72  
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 324 ? J HOH . 
2 1 B HOH 336 ? J HOH . 
# 
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 -14.0575 -1.6117 -19.4979 -0.1392 -0.1586 -0.3570 0.2727 0.2071 0.1618 5.0694 6.2995 6.7686 
-2.6078 1.2634 1.7850 0.6405 0.5032 0.1678 -0.6531 -0.4480 -0.4392 -0.1819 0.4482 -0.1926 
'X-RAY DIFFRACTION' 2 ? refined -18.6678 0.8121  -15.8087 0.1064  0.0146  -0.1780 0.2814 0.0672 0.0628 1.6810 2.4390 2.6205 
-1.2593 0.8471 0.2396 0.4774 0.1746 0.1462 -0.2633 -0.4973 0.0646  0.0525  0.1790 0.0200  
# 
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 ? ? ? ? ? ? ? ? ? '{ B|* }' 
# 
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 SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLY 16  ? B GLY 7   
15 1 Y 1 B GLU 172 ? B GLU 163 
16 1 Y 1 B GLU 173 ? B GLU 164 
17 1 Y 1 B THR 174 ? B THR 165 
18 1 Y 1 B PRO 175 ? B PRO 166 
19 1 Y 1 B VAL 176 ? B VAL 167 
20 1 Y 1 B GLU 177 ? B GLU 168 
# 
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 
A1BGW N1   N Y N 1   
A1BGW N3   N Y N 2   
A1BGW C4   C N N 3   
A1BGW C5   C N N 4   
A1BGW C6   C Y N 5   
A1BGW C7   C Y N 6   
A1BGW C8   C N S 7   
A1BGW C10  C N N 8   
A1BGW C13  C Y N 9   
A1BGW C15  C Y N 10  
A1BGW C1   C N N 11  
A1BGW C2   C Y N 12  
A1BGW C3   C Y N 13  
A1BGW N2   N N N 14  
A1BGW O1   O N N 15  
A1BGW C9   C N N 16  
A1BGW C11  C N N 17  
A1BGW N4   N N N 18  
A1BGW C12  C N N 19  
A1BGW N5   N Y N 20  
A1BGW C14  C N N 21  
A1BGW N6   N Y N 22  
A1BGW H7   H N N 23  
A1BGW H4   H N N 24  
A1BGW H5   H N N 25  
A1BGW H8   H N N 26  
A1BGW H12  H N N 27  
A1BGW H11  H N N 28  
A1BGW H21  H N N 29  
A1BGW H1   H N N 30  
A1BGW H3   H N N 31  
A1BGW H2   H N N 32  
A1BGW H6   H N N 33  
A1BGW H10  H N N 34  
A1BGW H9   H N N 35  
A1BGW H14  H N N 36  
A1BGW H13  H N N 37  
A1BGW H24  H N N 38  
A1BGW H17  H N N 39  
A1BGW H16  H N N 40  
A1BGW H18  H N N 41  
A1BGW H20  H N N 42  
A1BGW H19  H N N 43  
A1BGW H22  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 
SO4   S    S N N 358 
SO4   O1   O N N 359 
SO4   O2   O N N 360 
SO4   O3   O N N 361 
SO4   O4   O N N 362 
THR   N    N N N 363 
THR   CA   C N S 364 
THR   C    C N N 365 
THR   O    O N N 366 
THR   CB   C N R 367 
THR   OG1  O N N 368 
THR   CG2  C N N 369 
THR   OXT  O N N 370 
THR   H    H N N 371 
THR   H2   H N N 372 
THR   HA   H N N 373 
THR   HB   H N N 374 
THR   HG1  H N N 375 
THR   HG21 H N N 376 
THR   HG22 H N N 377 
THR   HG23 H N N 378 
THR   HXT  H N N 379 
TRP   N    N N N 380 
TRP   CA   C N S 381 
TRP   C    C N N 382 
TRP   O    O N N 383 
TRP   CB   C N N 384 
TRP   CG   C Y N 385 
TRP   CD1  C Y N 386 
TRP   CD2  C Y N 387 
TRP   NE1  N Y N 388 
TRP   CE2  C Y N 389 
TRP   CE3  C Y N 390 
TRP   CZ2  C Y N 391 
TRP   CZ3  C Y N 392 
TRP   CH2  C Y N 393 
TRP   OXT  O N N 394 
TRP   H    H N N 395 
TRP   H2   H N N 396 
TRP   HA   H N N 397 
TRP   HB2  H N N 398 
TRP   HB3  H N N 399 
TRP   HD1  H N N 400 
TRP   HE1  H N N 401 
TRP   HE3  H N N 402 
TRP   HZ2  H N N 403 
TRP   HZ3  H N N 404 
TRP   HH2  H N N 405 
TRP   HXT  H N N 406 
TYR   N    N N N 407 
TYR   CA   C N S 408 
TYR   C    C N N 409 
TYR   O    O N N 410 
TYR   CB   C N N 411 
TYR   CG   C Y N 412 
TYR   CD1  C Y N 413 
TYR   CD2  C Y N 414 
TYR   CE1  C Y N 415 
TYR   CE2  C Y N 416 
TYR   CZ   C Y N 417 
TYR   OH   O N N 418 
TYR   OXT  O N N 419 
TYR   H    H N N 420 
TYR   H2   H N N 421 
TYR   HA   H N N 422 
TYR   HB2  H N N 423 
TYR   HB3  H N N 424 
TYR   HD1  H N N 425 
TYR   HD2  H N N 426 
TYR   HE1  H N N 427 
TYR   HE2  H N N 428 
TYR   HH   H N N 429 
TYR   HXT  H N N 430 
VAL   N    N N N 431 
VAL   CA   C N S 432 
VAL   C    C N N 433 
VAL   O    O N N 434 
VAL   CB   C N N 435 
VAL   CG1  C N N 436 
VAL   CG2  C N N 437 
VAL   OXT  O N N 438 
VAL   H    H N N 439 
VAL   H2   H N N 440 
VAL   HA   H N N 441 
VAL   HB   H N N 442 
VAL   HG11 H N N 443 
VAL   HG12 H N N 444 
VAL   HG13 H N N 445 
VAL   HG21 H N N 446 
VAL   HG22 H N N 447 
VAL   HG23 H N N 448 
VAL   HXT  H N N 449 
# 
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 
A1BGW C1  C2   sing N N 1   
A1BGW C2  N1   doub Y N 2   
A1BGW N1  C3   sing Y N 3   
A1BGW C3  C4   sing N N 4   
A1BGW C4  N2   sing N N 5   
A1BGW N2  C5   sing N N 6   
A1BGW C5  O1   doub N N 7   
A1BGW C5  C6   sing N N 8   
A1BGW C6  N3   sing Y N 9   
A1BGW N3  C7   sing Y N 10  
A1BGW C7  C8   sing N N 11  
A1BGW C8  C9   sing N N 12  
A1BGW C9  C10  sing N N 13  
A1BGW C10 C11  sing N N 14  
A1BGW C11 N4   sing N N 15  
A1BGW N4  C12  sing N N 16  
A1BGW C7  N5   doub Y N 17  
A1BGW N5  C13  sing Y N 18  
A1BGW C13 C14  sing N N 19  
A1BGW C3  C15  doub Y N 20  
A1BGW C15 N6   sing Y N 21  
A1BGW C2  N6   sing Y N 22  
A1BGW C6  C13  doub Y N 23  
A1BGW C8  C12  sing N N 24  
A1BGW N3  H7   sing N N 25  
A1BGW C4  H4   sing N N 26  
A1BGW C4  H5   sing N N 27  
A1BGW C8  H8   sing N N 28  
A1BGW C10 H12  sing N N 29  
A1BGW C10 H11  sing N N 30  
A1BGW C15 H21  sing N N 31  
A1BGW C1  H1   sing N N 32  
A1BGW C1  H3   sing N N 33  
A1BGW C1  H2   sing N N 34  
A1BGW N2  H6   sing N N 35  
A1BGW C9  H10  sing N N 36  
A1BGW C9  H9   sing N N 37  
A1BGW C11 H14  sing N N 38  
A1BGW C11 H13  sing N N 39  
A1BGW N4  H24  sing N N 40  
A1BGW C12 H17  sing N N 41  
A1BGW C12 H16  sing N N 42  
A1BGW C14 H18  sing N N 43  
A1BGW C14 H20  sing N N 44  
A1BGW C14 H19  sing N N 45  
A1BGW N6  H22  sing N N 46  
ALA   N   CA   sing N N 47  
ALA   N   H    sing N N 48  
ALA   N   H2   sing N N 49  
ALA   CA  C    sing N N 50  
ALA   CA  CB   sing N N 51  
ALA   CA  HA   sing N N 52  
ALA   C   O    doub N N 53  
ALA   C   OXT  sing N N 54  
ALA   CB  HB1  sing N N 55  
ALA   CB  HB2  sing N N 56  
ALA   CB  HB3  sing N N 57  
ALA   OXT HXT  sing N N 58  
ARG   N   CA   sing N N 59  
ARG   N   H    sing N N 60  
ARG   N   H2   sing N N 61  
ARG   CA  C    sing N N 62  
ARG   CA  CB   sing N N 63  
ARG   CA  HA   sing N N 64  
ARG   C   O    doub N N 65  
ARG   C   OXT  sing N N 66  
ARG   CB  CG   sing N N 67  
ARG   CB  HB2  sing N N 68  
ARG   CB  HB3  sing N N 69  
ARG   CG  CD   sing N N 70  
ARG   CG  HG2  sing N N 71  
ARG   CG  HG3  sing N N 72  
ARG   CD  NE   sing N N 73  
ARG   CD  HD2  sing N N 74  
ARG   CD  HD3  sing N N 75  
ARG   NE  CZ   sing N N 76  
ARG   NE  HE   sing N N 77  
ARG   CZ  NH1  sing N N 78  
ARG   CZ  NH2  doub N N 79  
ARG   NH1 HH11 sing N N 80  
ARG   NH1 HH12 sing N N 81  
ARG   NH2 HH21 sing N N 82  
ARG   NH2 HH22 sing N N 83  
ARG   OXT HXT  sing N N 84  
ASN   N   CA   sing N N 85  
ASN   N   H    sing N N 86  
ASN   N   H2   sing N N 87  
ASN   CA  C    sing N N 88  
ASN   CA  CB   sing N N 89  
ASN   CA  HA   sing N N 90  
ASN   C   O    doub N N 91  
ASN   C   OXT  sing N N 92  
ASN   CB  CG   sing N N 93  
ASN   CB  HB2  sing N N 94  
ASN   CB  HB3  sing N N 95  
ASN   CG  OD1  doub N N 96  
ASN   CG  ND2  sing N N 97  
ASN   ND2 HD21 sing N N 98  
ASN   ND2 HD22 sing N N 99  
ASN   OXT HXT  sing N N 100 
ASP   N   CA   sing N N 101 
ASP   N   H    sing N N 102 
ASP   N   H2   sing N N 103 
ASP   CA  C    sing N N 104 
ASP   CA  CB   sing N N 105 
ASP   CA  HA   sing N N 106 
ASP   C   O    doub N N 107 
ASP   C   OXT  sing N N 108 
ASP   CB  CG   sing N N 109 
ASP   CB  HB2  sing N N 110 
ASP   CB  HB3  sing N N 111 
ASP   CG  OD1  doub N N 112 
ASP   CG  OD2  sing N N 113 
ASP   OD2 HD2  sing N N 114 
ASP   OXT HXT  sing N N 115 
CYS   N   CA   sing N N 116 
CYS   N   H    sing N N 117 
CYS   N   H2   sing N N 118 
CYS   CA  C    sing N N 119 
CYS   CA  CB   sing N N 120 
CYS   CA  HA   sing N N 121 
CYS   C   O    doub N N 122 
CYS   C   OXT  sing N N 123 
CYS   CB  SG   sing N N 124 
CYS   CB  HB2  sing N N 125 
CYS   CB  HB3  sing N N 126 
CYS   SG  HG   sing N N 127 
CYS   OXT HXT  sing N N 128 
DMS   S   O    doub N N 129 
DMS   S   C1   sing N N 130 
DMS   S   C2   sing N N 131 
DMS   C1  H11  sing N N 132 
DMS   C1  H12  sing N N 133 
DMS   C1  H13  sing N N 134 
DMS   C2  H21  sing N N 135 
DMS   C2  H22  sing N N 136 
DMS   C2  H23  sing N N 137 
GLN   N   CA   sing N N 138 
GLN   N   H    sing N N 139 
GLN   N   H2   sing N N 140 
GLN   CA  C    sing N N 141 
GLN   CA  CB   sing N N 142 
GLN   CA  HA   sing N N 143 
GLN   C   O    doub N N 144 
GLN   C   OXT  sing N N 145 
GLN   CB  CG   sing N N 146 
GLN   CB  HB2  sing N N 147 
GLN   CB  HB3  sing N N 148 
GLN   CG  CD   sing N N 149 
GLN   CG  HG2  sing N N 150 
GLN   CG  HG3  sing N N 151 
GLN   CD  OE1  doub N N 152 
GLN   CD  NE2  sing N N 153 
GLN   NE2 HE21 sing N N 154 
GLN   NE2 HE22 sing N N 155 
GLN   OXT HXT  sing N N 156 
GLU   N   CA   sing N N 157 
GLU   N   H    sing N N 158 
GLU   N   H2   sing N N 159 
GLU   CA  C    sing N N 160 
GLU   CA  CB   sing N N 161 
GLU   CA  HA   sing N N 162 
GLU   C   O    doub N N 163 
GLU   C   OXT  sing N N 164 
GLU   CB  CG   sing N N 165 
GLU   CB  HB2  sing N N 166 
GLU   CB  HB3  sing N N 167 
GLU   CG  CD   sing N N 168 
GLU   CG  HG2  sing N N 169 
GLU   CG  HG3  sing N N 170 
GLU   CD  OE1  doub N N 171 
GLU   CD  OE2  sing N N 172 
GLU   OE2 HE2  sing N N 173 
GLU   OXT HXT  sing N N 174 
GLY   N   CA   sing N N 175 
GLY   N   H    sing N N 176 
GLY   N   H2   sing N N 177 
GLY   CA  C    sing N N 178 
GLY   CA  HA2  sing N N 179 
GLY   CA  HA3  sing N N 180 
GLY   C   O    doub N N 181 
GLY   C   OXT  sing N N 182 
GLY   OXT HXT  sing N N 183 
HIS   N   CA   sing N N 184 
HIS   N   H    sing N N 185 
HIS   N   H2   sing N N 186 
HIS   CA  C    sing N N 187 
HIS   CA  CB   sing N N 188 
HIS   CA  HA   sing N N 189 
HIS   C   O    doub N N 190 
HIS   C   OXT  sing N N 191 
HIS   CB  CG   sing N N 192 
HIS   CB  HB2  sing N N 193 
HIS   CB  HB3  sing N N 194 
HIS   CG  ND1  sing Y N 195 
HIS   CG  CD2  doub Y N 196 
HIS   ND1 CE1  doub Y N 197 
HIS   ND1 HD1  sing N N 198 
HIS   CD2 NE2  sing Y N 199 
HIS   CD2 HD2  sing N N 200 
HIS   CE1 NE2  sing Y N 201 
HIS   CE1 HE1  sing N N 202 
HIS   NE2 HE2  sing N N 203 
HIS   OXT HXT  sing N N 204 
HOH   O   H1   sing N N 205 
HOH   O   H2   sing N N 206 
ILE   N   CA   sing N N 207 
ILE   N   H    sing N N 208 
ILE   N   H2   sing N N 209 
ILE   CA  C    sing N N 210 
ILE   CA  CB   sing N N 211 
ILE   CA  HA   sing N N 212 
ILE   C   O    doub N N 213 
ILE   C   OXT  sing N N 214 
ILE   CB  CG1  sing N N 215 
ILE   CB  CG2  sing N N 216 
ILE   CB  HB   sing N N 217 
ILE   CG1 CD1  sing N N 218 
ILE   CG1 HG12 sing N N 219 
ILE   CG1 HG13 sing N N 220 
ILE   CG2 HG21 sing N N 221 
ILE   CG2 HG22 sing N N 222 
ILE   CG2 HG23 sing N N 223 
ILE   CD1 HD11 sing N N 224 
ILE   CD1 HD12 sing N N 225 
ILE   CD1 HD13 sing N N 226 
ILE   OXT HXT  sing N N 227 
LEU   N   CA   sing N N 228 
LEU   N   H    sing N N 229 
LEU   N   H2   sing N N 230 
LEU   CA  C    sing N N 231 
LEU   CA  CB   sing N N 232 
LEU   CA  HA   sing N N 233 
LEU   C   O    doub N N 234 
LEU   C   OXT  sing N N 235 
LEU   CB  CG   sing N N 236 
LEU   CB  HB2  sing N N 237 
LEU   CB  HB3  sing N N 238 
LEU   CG  CD1  sing N N 239 
LEU   CG  CD2  sing N N 240 
LEU   CG  HG   sing N N 241 
LEU   CD1 HD11 sing N N 242 
LEU   CD1 HD12 sing N N 243 
LEU   CD1 HD13 sing N N 244 
LEU   CD2 HD21 sing N N 245 
LEU   CD2 HD22 sing N N 246 
LEU   CD2 HD23 sing N N 247 
LEU   OXT HXT  sing N N 248 
LYS   N   CA   sing N N 249 
LYS   N   H    sing N N 250 
LYS   N   H2   sing N N 251 
LYS   CA  C    sing N N 252 
LYS   CA  CB   sing N N 253 
LYS   CA  HA   sing N N 254 
LYS   C   O    doub N N 255 
LYS   C   OXT  sing N N 256 
LYS   CB  CG   sing N N 257 
LYS   CB  HB2  sing N N 258 
LYS   CB  HB3  sing N N 259 
LYS   CG  CD   sing N N 260 
LYS   CG  HG2  sing N N 261 
LYS   CG  HG3  sing N N 262 
LYS   CD  CE   sing N N 263 
LYS   CD  HD2  sing N N 264 
LYS   CD  HD3  sing N N 265 
LYS   CE  NZ   sing N N 266 
LYS   CE  HE2  sing N N 267 
LYS   CE  HE3  sing N N 268 
LYS   NZ  HZ1  sing N N 269 
LYS   NZ  HZ2  sing N N 270 
LYS   NZ  HZ3  sing N N 271 
LYS   OXT HXT  sing N N 272 
MET   N   CA   sing N N 273 
MET   N   H    sing N N 274 
MET   N   H2   sing N N 275 
MET   CA  C    sing N N 276 
MET   CA  CB   sing N N 277 
MET   CA  HA   sing N N 278 
MET   C   O    doub N N 279 
MET   C   OXT  sing N N 280 
MET   CB  CG   sing N N 281 
MET   CB  HB2  sing N N 282 
MET   CB  HB3  sing N N 283 
MET   CG  SD   sing N N 284 
MET   CG  HG2  sing N N 285 
MET   CG  HG3  sing N N 286 
MET   SD  CE   sing N N 287 
MET   CE  HE1  sing N N 288 
MET   CE  HE2  sing N N 289 
MET   CE  HE3  sing N N 290 
MET   OXT HXT  sing N N 291 
PHE   N   CA   sing N N 292 
PHE   N   H    sing N N 293 
PHE   N   H2   sing N N 294 
PHE   CA  C    sing N N 295 
PHE   CA  CB   sing N N 296 
PHE   CA  HA   sing N N 297 
PHE   C   O    doub N N 298 
PHE   C   OXT  sing N N 299 
PHE   CB  CG   sing N N 300 
PHE   CB  HB2  sing N N 301 
PHE   CB  HB3  sing N N 302 
PHE   CG  CD1  doub Y N 303 
PHE   CG  CD2  sing Y N 304 
PHE   CD1 CE1  sing Y N 305 
PHE   CD1 HD1  sing N N 306 
PHE   CD2 CE2  doub Y N 307 
PHE   CD2 HD2  sing N N 308 
PHE   CE1 CZ   doub Y N 309 
PHE   CE1 HE1  sing N N 310 
PHE   CE2 CZ   sing Y N 311 
PHE   CE2 HE2  sing N N 312 
PHE   CZ  HZ   sing N N 313 
PHE   OXT HXT  sing N N 314 
PRO   N   CA   sing N N 315 
PRO   N   CD   sing N N 316 
PRO   N   H    sing N N 317 
PRO   CA  C    sing N N 318 
PRO   CA  CB   sing N N 319 
PRO   CA  HA   sing N N 320 
PRO   C   O    doub N N 321 
PRO   C   OXT  sing N N 322 
PRO   CB  CG   sing N N 323 
PRO   CB  HB2  sing N N 324 
PRO   CB  HB3  sing N N 325 
PRO   CG  CD   sing N N 326 
PRO   CG  HG2  sing N N 327 
PRO   CG  HG3  sing N N 328 
PRO   CD  HD2  sing N N 329 
PRO   CD  HD3  sing N N 330 
PRO   OXT HXT  sing N N 331 
SER   N   CA   sing N N 332 
SER   N   H    sing N N 333 
SER   N   H2   sing N N 334 
SER   CA  C    sing N N 335 
SER   CA  CB   sing N N 336 
SER   CA  HA   sing N N 337 
SER   C   O    doub N N 338 
SER   C   OXT  sing N N 339 
SER   CB  OG   sing N N 340 
SER   CB  HB2  sing N N 341 
SER   CB  HB3  sing N N 342 
SER   OG  HG   sing N N 343 
SER   OXT HXT  sing N N 344 
SO4   S   O1   doub N N 345 
SO4   S   O2   doub N N 346 
SO4   S   O3   sing N N 347 
SO4   S   O4   sing N N 348 
THR   N   CA   sing N N 349 
THR   N   H    sing N N 350 
THR   N   H2   sing N N 351 
THR   CA  C    sing N N 352 
THR   CA  CB   sing N N 353 
THR   CA  HA   sing N N 354 
THR   C   O    doub N N 355 
THR   C   OXT  sing N N 356 
THR   CB  OG1  sing N N 357 
THR   CB  CG2  sing N N 358 
THR   CB  HB   sing N N 359 
THR   OG1 HG1  sing N N 360 
THR   CG2 HG21 sing N N 361 
THR   CG2 HG22 sing N N 362 
THR   CG2 HG23 sing N N 363 
THR   OXT HXT  sing N N 364 
TRP   N   CA   sing N N 365 
TRP   N   H    sing N N 366 
TRP   N   H2   sing N N 367 
TRP   CA  C    sing N N 368 
TRP   CA  CB   sing N N 369 
TRP   CA  HA   sing N N 370 
TRP   C   O    doub N N 371 
TRP   C   OXT  sing N N 372 
TRP   CB  CG   sing N N 373 
TRP   CB  HB2  sing N N 374 
TRP   CB  HB3  sing N N 375 
TRP   CG  CD1  doub Y N 376 
TRP   CG  CD2  sing Y N 377 
TRP   CD1 NE1  sing Y N 378 
TRP   CD1 HD1  sing N N 379 
TRP   CD2 CE2  doub Y N 380 
TRP   CD2 CE3  sing Y N 381 
TRP   NE1 CE2  sing Y N 382 
TRP   NE1 HE1  sing N N 383 
TRP   CE2 CZ2  sing Y N 384 
TRP   CE3 CZ3  doub Y N 385 
TRP   CE3 HE3  sing N N 386 
TRP   CZ2 CH2  doub Y N 387 
TRP   CZ2 HZ2  sing N N 388 
TRP   CZ3 CH2  sing Y N 389 
TRP   CZ3 HZ3  sing N N 390 
TRP   CH2 HH2  sing N N 391 
TRP   OXT HXT  sing N N 392 
TYR   N   CA   sing N N 393 
TYR   N   H    sing N N 394 
TYR   N   H2   sing N N 395 
TYR   CA  C    sing N N 396 
TYR   CA  CB   sing N N 397 
TYR   CA  HA   sing N N 398 
TYR   C   O    doub N N 399 
TYR   C   OXT  sing N N 400 
TYR   CB  CG   sing N N 401 
TYR   CB  HB2  sing N N 402 
TYR   CB  HB3  sing N N 403 
TYR   CG  CD1  doub Y N 404 
TYR   CG  CD2  sing Y N 405 
TYR   CD1 CE1  sing Y N 406 
TYR   CD1 HD1  sing N N 407 
TYR   CD2 CE2  doub Y N 408 
TYR   CD2 HD2  sing N N 409 
TYR   CE1 CZ   doub Y N 410 
TYR   CE1 HE1  sing N N 411 
TYR   CE2 CZ   sing Y N 412 
TYR   CE2 HE2  sing N N 413 
TYR   CZ  OH   sing N N 414 
TYR   OH  HH   sing N N 415 
TYR   OXT HXT  sing N N 416 
VAL   N   CA   sing N N 417 
VAL   N   H    sing N N 418 
VAL   N   H2   sing N N 419 
VAL   CA  C    sing N N 420 
VAL   CA  CB   sing N N 421 
VAL   CA  HA   sing N N 422 
VAL   C   O    doub N N 423 
VAL   C   OXT  sing N N 424 
VAL   CB  CG1  sing N N 425 
VAL   CB  CG2  sing N N 426 
VAL   CB  HB   sing N N 427 
VAL   CG1 HG11 sing N N 428 
VAL   CG1 HG12 sing N N 429 
VAL   CG1 HG13 sing N N 430 
VAL   CG2 HG21 sing N N 431 
VAL   CG2 HG22 sing N N 432 
VAL   CG2 HG23 sing N N 433 
VAL   OXT HXT  sing N N 434 
# 
_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_1002322 
_pdbx_deposit_group.group_description   
'Crystallographic fragment screen of ZIKV NS2B-NS3 protease at the XChem facility of Diamond Light Source beamline I04-1' 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HPC 
_atom_sites.fract_transf_matrix[1][1]   0.023452 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.023452 
_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]   0.004623 
_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 
# 
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   . ASP   A 1 7   ? -21.680 19.713  -7.668  1.00 80.76  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.724 18.696  -7.597  1.00 80.77  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.850 17.940  -8.920  1.00 79.09  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.983 18.543  -9.986  1.00 79.31  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -24.074 19.291  -7.150  1.00 83.68  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -25.021 18.259  -6.553  1.00 90.89  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -25.181 18.244  -5.312  1.00 91.70  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.596 17.459  -7.327  1.00 94.42  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.797 16.610  -8.835  1.00 77.02  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.865 15.753  -10.003 1.00 75.26  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -24.267 15.524  -10.520 1.00 73.58  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -25.232 15.614  -9.762  1.00 73.62  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -22.162 14.435  -9.740  1.00 74.94  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.715 14.615  -9.501  1.00 75.86  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.926 13.029  -9.234  1.00 75.83  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -18.228 13.570  -9.128  1.00 73.74  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -24.372 15.245  -11.823 1.00 71.72  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.645 15.022  -12.487 1.00 70.73  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.493 14.072  -13.665 1.00 69.67  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -24.389 13.931  -14.206 1.00 69.58  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -26.296 16.347  -12.903 1.00 70.86  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.556 17.118  -13.972 1.00 71.96  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.652 18.117  -13.637 1.00 72.92  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.848 16.933  -15.321 1.00 72.61  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -24.008 18.865  -14.619 1.00 73.90  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -25.187 17.648  -16.307 1.00 73.27  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -24.273 18.621  -15.954 1.00 74.66  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -23.614 19.327  -16.933 1.00 76.89  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.588 13.388  -14.050 1.00 68.60  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.512 12.421  -15.154 1.00 68.26  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -27.283 12.868  -16.415 1.00 68.21  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -28.258 13.626  -16.316 1.00 69.11  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.926 11.000  -14.697 1.00 68.16  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.367 10.977  -14.161 1.00 68.93  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.948 10.448  -13.651 1.00 68.07  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.899 9.569   -14.056 1.00 70.20  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.817 12.428  -17.601 1.00 67.37  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.447 12.750  -18.894 1.00 67.89  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.501 11.490  -19.732 1.00 68.31  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.469 10.826  -19.860 1.00 68.96  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.617 13.779  -19.674 1.00 69.65  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.534 15.152  -19.044 1.00 75.53  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.765 16.170  -19.869 1.00 84.32  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.988 15.752  -20.758 1.00 85.28  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.924 17.388  -19.612 1.00 88.13  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.652 11.158  -20.342 1.00 67.95  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.717 9.951   -21.172 1.00 68.58  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.797 10.054  -22.369 1.00 69.42  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.727 11.106  -22.993 1.00 70.57  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -30.141 9.629   -21.597 1.00 69.85  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.312 8.180   -21.983 1.00 72.53  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.762 7.743   -21.976 1.00 75.59  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.894 6.306   -22.210 1.00 77.68  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.923 5.751   -23.420 1.00 79.86  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.826 6.507   -24.508 1.00 81.47  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -32.004 4.430   -23.551 1.00 77.01  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -27.032 8.992   -22.643 1.00 69.52  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -26.115 8.916   -23.783 1.00 69.74  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.480 7.826   -24.796 1.00 70.21  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.808 7.721   -25.827 1.00 70.93  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.679 8.734   -23.314 1.00 70.05  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.516 7.030   -24.524 1.00 69.64  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.952 6.028   -25.489 1.00 69.76  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.583 4.768   -24.948 1.00 69.86  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.747 4.611   -23.736 1.00 69.28  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.980 3.879   -25.877 1.00 69.75  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.542 2.568   -25.572 1.00 70.21  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.408 1.580   -25.426 1.00 71.48  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -27.371 1.737   -26.072 1.00 72.12  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.418 2.072   -26.733 1.00 70.51  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.813 2.636   -26.774 1.00 74.19  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -32.091 3.570   -26.013 1.00 74.22  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.614 2.183   -27.622 1.00 76.05  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.619 0.516   -24.643 1.00 71.64  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.621 -0.529  -24.507 1.00 71.84  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -28.014 -1.678  -25.404 1.00 73.36  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.930 -2.448  -25.099 1.00 73.31  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.386 -0.926  -23.057 1.00 71.34  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.914 0.303   -22.271 1.00 72.25  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.377 -2.042  -23.001 1.00 71.04  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.788 0.122   -20.833 1.00 73.33  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -27.347 -1.756  -26.560 0.50 73.87  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -27.338 -1.776  -26.550 0.50 74.03  ? 60  THR   A N   1 
ATOM   84   C CA  A THR   A 1 17  ? -27.584 -2.771  -27.583 0.50 74.49  ? 60  THR   A CA  1 
ATOM   85   C CA  B THR   A 1 17  ? -27.633 -2.774  -27.573 0.50 74.86  ? 60  THR   A CA  1 
ATOM   86   C C   A THR   A 1 17  ? -26.277 -3.259  -28.185 0.50 75.34  ? 60  THR   A C   1 
ATOM   87   C C   B THR   A 1 17  ? -26.358 -3.212  -28.302 0.50 75.55  ? 60  THR   A C   1 
ATOM   88   O O   A THR   A 1 17  ? -25.318 -2.493  -28.284 0.50 75.26  ? 60  THR   A O   1 
ATOM   89   O O   B THR   A 1 17  ? -25.456 -2.400  -28.498 0.50 75.51  ? 60  THR   A O   1 
ATOM   90   C CB  A THR   A 1 17  ? -28.409 -2.182  -28.752 0.50 75.10  ? 60  THR   A CB  1 
ATOM   91   C CB  B THR   A 1 17  ? -28.747 -2.210  -28.489 0.50 75.92  ? 60  THR   A CB  1 
ATOM   92   O OG1 A THR   A 1 17  ? -27.687 -1.109  -29.368 0.50 75.30  ? 60  THR   A OG1 1 
ATOM   93   O OG1 B THR   A 1 17  ? -30.001 -2.391  -27.832 0.50 76.93  ? 60  THR   A OG1 1 
ATOM   94   C CG2 A THR   A 1 17  ? -29.800 -1.730  -28.336 0.50 75.72  ? 60  THR   A CG2 1 
ATOM   95   C CG2 B THR   A 1 17  ? -28.796 -2.849  -29.855 0.50 76.15  ? 60  THR   A CG2 1 
ATOM   96   N N   . TRP   A 1 18  ? -26.268 -4.495  -28.672 1.00 76.19  ? 61  TRP   A N   1 
ATOM   97   C CA  . TRP   A 1 18  ? -25.118 -5.012  -29.404 1.00 79.11  ? 61  TRP   A CA  1 
ATOM   98   C C   . TRP   A 1 18  ? -25.295 -4.510  -30.858 1.00 83.41  ? 61  TRP   A C   1 
ATOM   99   O O   . TRP   A 1 18  ? -26.384 -4.635  -31.413 1.00 83.84  ? 61  TRP   A O   1 
ATOM   100  C CB  . TRP   A 1 18  ? -25.112 -6.555  -29.369 1.00 78.32  ? 61  TRP   A CB  1 
ATOM   101  C CG  . TRP   A 1 18  ? -24.051 -7.206  -30.204 1.00 78.26  ? 61  TRP   A CG  1 
ATOM   102  C CD1 . TRP   A 1 18  ? -24.133 -7.534  -31.529 1.00 79.28  ? 61  TRP   A CD1 1 
ATOM   103  C CD2 . TRP   A 1 18  ? -22.799 -7.729  -29.739 1.00 78.45  ? 61  TRP   A CD2 1 
ATOM   104  N NE1 . TRP   A 1 18  ? -22.985 -8.171  -31.930 1.00 79.62  ? 61  TRP   A NE1 1 
ATOM   105  C CE2 . TRP   A 1 18  ? -22.166 -8.343  -30.840 1.00 79.35  ? 61  TRP   A CE2 1 
ATOM   106  C CE3 . TRP   A 1 18  ? -22.143 -7.727  -28.499 1.00 78.65  ? 61  TRP   A CE3 1 
ATOM   107  C CZ2 . TRP   A 1 18  ? -20.901 -8.927  -30.740 1.00 79.78  ? 61  TRP   A CZ2 1 
ATOM   108  C CZ3 . TRP   A 1 18  ? -20.909 -8.333  -28.398 1.00 79.34  ? 61  TRP   A CZ3 1 
ATOM   109  C CH2 . TRP   A 1 18  ? -20.286 -8.896  -29.512 1.00 79.48  ? 61  TRP   A CH2 1 
ATOM   110  N N   . GLU   A 1 19  ? -24.247 -3.941  -31.468 1.00 86.57  ? 62  GLU   A N   1 
ATOM   111  C CA  . GLU   A 1 19  ? -24.332 -3.457  -32.842 1.00 90.36  ? 62  GLU   A CA  1 
ATOM   112  C C   . GLU   A 1 19  ? -23.518 -4.332  -33.791 1.00 93.91  ? 62  GLU   A C   1 
ATOM   113  O O   . GLU   A 1 19  ? -22.304 -4.471  -33.611 1.00 94.46  ? 62  GLU   A O   1 
ATOM   114  C CB  . GLU   A 1 19  ? -23.875 -1.999  -32.928 1.00 93.60  ? 62  GLU   A CB  1 
ATOM   115  C CG  . GLU   A 1 19  ? -24.674 -1.081  -32.017 1.00 100.01 ? 62  GLU   A CG  1 
ATOM   116  C CD  . GLU   A 1 19  ? -25.977 -0.549  -32.589 1.00 107.42 ? 62  GLU   A CD  1 
ATOM   117  O OE1 . GLU   A 1 19  ? -25.981 -0.100  -33.760 1.00 109.75 ? 62  GLU   A OE1 1 
ATOM   118  O OE2 . GLU   A 1 19  ? -26.992 -0.564  -31.856 1.00 109.15 ? 62  GLU   A OE2 1 
ATOM   119  N N   . LYS   A 1 20  ? -24.186 -4.956  -34.775 1.00 95.88  ? 63  LYS   A N   1 
ATOM   120  C CA  . LYS   A 1 20  ? -23.485 -5.802  -35.736 1.00 98.66  ? 63  LYS   A CA  1 
ATOM   121  C C   . LYS   A 1 20  ? -22.686 -4.904  -36.652 1.00 101.05 ? 63  LYS   A C   1 
ATOM   122  O O   . LYS   A 1 20  ? -23.186 -3.862  -37.086 1.00 101.34 ? 63  LYS   A O   1 
ATOM   123  C CB  . LYS   A 1 20  ? -24.464 -6.636  -36.585 1.00 101.12 ? 63  LYS   A CB  1 
ATOM   124  C CG  . LYS   A 1 20  ? -25.300 -7.640  -35.798 1.00 106.09 ? 63  LYS   A CG  1 
ATOM   125  C CD  . LYS   A 1 20  ? -26.326 -8.325  -36.706 1.00 110.39 ? 63  LYS   A CD  1 
ATOM   126  C CE  . LYS   A 1 20  ? -27.710 -8.412  -36.102 1.00 114.04 ? 63  LYS   A CE  1 
ATOM   127  N NZ  . LYS   A 1 20  ? -28.676 -9.044  -37.042 1.00 116.92 ? 63  LYS   A NZ  1 
ATOM   128  N N   . ASP   A 1 21  ? -21.458 -5.314  -36.965 1.00 102.61 ? 64  ASP   A N   1 
ATOM   129  C CA  . ASP   A 1 21  ? -20.569 -4.551  -37.844 1.00 104.68 ? 64  ASP   A CA  1 
ATOM   130  C C   . ASP   A 1 21  ? -19.996 -3.323  -37.131 1.00 104.44 ? 64  ASP   A C   1 
ATOM   131  O O   . ASP   A 1 21  ? -19.875 -2.246  -37.725 1.00 104.95 ? 64  ASP   A O   1 
ATOM   132  C CB  . ASP   A 1 21  ? -21.223 -4.169  -39.188 1.00 108.46 ? 64  ASP   A CB  1 
ATOM   133  C CG  . ASP   A 1 21  ? -21.741 -5.332  -40.013 1.00 118.06 ? 64  ASP   A CG  1 
ATOM   134  O OD1 . ASP   A 1 21  ? -21.009 -6.339  -40.148 1.00 120.38 ? 64  ASP   A OD1 1 
ATOM   135  O OD2 . ASP   A 1 21  ? -22.862 -5.216  -40.567 1.00 121.48 ? 64  ASP   A OD2 1 
ATOM   136  N N   . ALA   A 1 22  ? -19.650 -3.493  -35.854 1.00 103.26 ? 65  ALA   A N   1 
ATOM   137  C CA  . ALA   A 1 22  ? -18.972 -2.458  -35.094 1.00 102.61 ? 65  ALA   A CA  1 
ATOM   138  C C   . ALA   A 1 22  ? -17.442 -2.613  -35.373 1.00 102.26 ? 65  ALA   A C   1 
ATOM   139  O O   . ALA   A 1 22  ? -16.991 -3.637  -35.920 1.00 101.81 ? 65  ALA   A O   1 
ATOM   140  C CB  . ALA   A 1 22  ? -19.269 -2.631  -33.612 1.00 102.73 ? 65  ALA   A CB  1 
ATOM   141  N N   . GLU   A 1 23  ? -16.651 -1.589  -35.029 1.00 101.96 ? 66  GLU   A N   1 
ATOM   142  C CA  . GLU   A 1 23  ? -15.200 -1.624  -35.236 1.00 101.61 ? 66  GLU   A CA  1 
ATOM   143  C C   . GLU   A 1 23  ? -14.577 -2.717  -34.355 1.00 99.18  ? 66  GLU   A C   1 
ATOM   144  O O   . GLU   A 1 23  ? -14.665 -2.645  -33.135 1.00 98.08  ? 66  GLU   A O   1 
ATOM   145  C CB  . GLU   A 1 23  ? -14.611 -0.263  -34.848 1.00 105.77 ? 66  GLU   A CB  1 
ATOM   146  C CG  . GLU   A 1 23  ? -13.224 0.015   -35.395 1.00 112.25 ? 66  GLU   A CG  1 
ATOM   147  C CD  . GLU   A 1 23  ? -12.792 1.432   -35.071 1.00 121.52 ? 66  GLU   A CD  1 
ATOM   148  O OE1 . GLU   A 1 23  ? -12.759 1.782   -33.866 1.00 122.47 ? 66  GLU   A OE1 1 
ATOM   149  O OE2 . GLU   A 1 23  ? -12.521 2.203   -36.023 1.00 124.83 ? 66  GLU   A OE2 1 
ATOM   150  N N   . VAL   A 1 24  ? -13.969 -3.737  -34.975 1.00 97.71  ? 67  VAL   A N   1 
ATOM   151  C CA  . VAL   A 1 24  ? -13.347 -4.832  -34.221 1.00 96.50  ? 67  VAL   A CA  1 
ATOM   152  C C   . VAL   A 1 24  ? -11.878 -4.499  -33.960 1.00 94.88  ? 67  VAL   A C   1 
ATOM   153  O O   . VAL   A 1 24  ? -11.129 -4.358  -34.909 1.00 94.62  ? 67  VAL   A O   1 
ATOM   154  C CB  . VAL   A 1 24  ? -13.506 -6.202  -34.930 1.00 97.05  ? 67  VAL   A CB  1 
ATOM   155  C CG1 . VAL   A 1 24  ? -13.139 -7.324  -33.989 1.00 97.32  ? 67  VAL   A CG1 1 
ATOM   156  C CG2 . VAL   A 1 24  ? -14.930 -6.403  -35.441 1.00 97.65  ? 67  VAL   A CG2 1 
ATOM   157  N N   . THR   A 1 25  ? -11.470 -4.308  -32.691 1.00 93.70  ? 68  THR   A N   1 
ATOM   158  C CA  . THR   A 1 25  ? -10.078 -3.940  -32.378 1.00 93.31  ? 68  THR   A CA  1 
ATOM   159  C C   . THR   A 1 25  ? -9.653  -4.435  -30.974 1.00 92.81  ? 68  THR   A C   1 
ATOM   160  O O   . THR   A 1 25  ? -10.448 -5.069  -30.302 1.00 92.97  ? 68  THR   A O   1 
ATOM   161  C CB  . THR   A 1 25  ? -9.876  -2.418  -32.592 1.00 94.61  ? 68  THR   A CB  1 
ATOM   162  O OG1 . THR   A 1 25  ? -8.488  -2.159  -32.790 1.00 95.92  ? 68  THR   A OG1 1 
ATOM   163  C CG2 . THR   A 1 25  ? -10.406 -1.596  -31.444 1.00 94.29  ? 68  THR   A CG2 1 
ATOM   164  N N   . GLY   A 1 26  ? -8.405  -4.208  -30.566 1.00 92.34  ? 69  GLY   A N   1 
ATOM   165  C CA  . GLY   A 1 26  ? -7.933  -4.615  -29.251 1.00 92.56  ? 69  GLY   A CA  1 
ATOM   166  C C   . GLY   A 1 26  ? -7.454  -6.047  -29.153 1.00 92.75  ? 69  GLY   A C   1 
ATOM   167  O O   . GLY   A 1 26  ? -8.086  -6.968  -29.678 1.00 92.97  ? 69  GLY   A O   1 
ATOM   168  N N   . ASN   A 1 27  ? -6.344  -6.245  -28.442 1.00 92.43  ? 70  ASN   A N   1 
ATOM   169  C CA  . ASN   A 1 27  ? -5.767  -7.569  -28.259 1.00 92.74  ? 70  ASN   A CA  1 
ATOM   170  C C   . ASN   A 1 27  ? -6.327  -8.302  -26.979 1.00 91.08  ? 70  ASN   A C   1 
ATOM   171  O O   . ASN   A 1 27  ? -7.224  -7.774  -26.325 1.00 90.93  ? 70  ASN   A O   1 
ATOM   172  C CB  . ASN   A 1 27  ? -4.229  -7.468  -28.294 1.00 95.84  ? 70  ASN   A CB  1 
ATOM   173  C CG  . ASN   A 1 27  ? -3.659  -6.786  -27.080 1.00 101.29 ? 70  ASN   A CG  1 
ATOM   174  O OD1 . ASN   A 1 27  ? -4.077  -5.687  -26.704 1.00 102.97 ? 70  ASN   A OD1 1 
ATOM   175  N ND2 . ASN   A 1 27  ? -2.687  -7.421  -26.440 1.00 102.45 ? 70  ASN   A ND2 1 
ATOM   176  N N   . SER   A 1 28  ? -5.855  -9.544  -26.673 1.00 89.47  ? 71  SER   A N   1 
ATOM   177  C CA  . SER   A 1 28  ? -6.325  -10.357 -25.536 1.00 88.11  ? 71  SER   A CA  1 
ATOM   178  C C   . SER   A 1 28  ? -5.147  -10.826 -24.660 1.00 86.79  ? 71  SER   A C   1 
ATOM   179  O O   . SER   A 1 28  ? -4.789  -12.007 -24.673 1.00 87.32  ? 71  SER   A O   1 
ATOM   180  C CB  . SER   A 1 28  ? -7.100  -11.573 -26.042 1.00 89.16  ? 71  SER   A CB  1 
ATOM   181  O OG  . SER   A 1 28  ? -7.989  -11.261 -27.096 1.00 92.14  ? 71  SER   A OG  1 
ATOM   182  N N   . PRO   A 1 29  ? -4.526  -9.931  -23.880 1.00 85.18  ? 72  PRO   A N   1 
ATOM   183  C CA  . PRO   A 1 29  ? -3.342  -10.344 -23.115 1.00 84.28  ? 72  PRO   A CA  1 
ATOM   184  C C   . PRO   A 1 29  ? -3.637  -11.011 -21.778 1.00 83.40  ? 72  PRO   A C   1 
ATOM   185  O O   . PRO   A 1 29  ? -4.474  -10.539 -21.012 1.00 83.40  ? 72  PRO   A O   1 
ATOM   186  C CB  . PRO   A 1 29  ? -2.552  -9.048  -22.974 1.00 85.13  ? 72  PRO   A CB  1 
ATOM   187  C CG  . PRO   A 1 29  ? -3.611  -7.969  -22.971 1.00 85.80  ? 72  PRO   A CG  1 
ATOM   188  C CD  . PRO   A 1 29  ? -4.799  -8.487  -23.732 1.00 84.39  ? 72  PRO   A CD  1 
ATOM   189  N N   . ARG   A 1 30  ? -2.949  -12.122 -21.504 1.00 82.66  ? 73  ARG   A N   1 
ATOM   190  C CA  . ARG   A 1 30  ? -3.074  -12.843 -20.238 1.00 82.75  ? 73  ARG   A CA  1 
ATOM   191  C C   . ARG   A 1 30  ? -2.034  -12.280 -19.285 1.00 81.52  ? 73  ARG   A C   1 
ATOM   192  O O   . ARG   A 1 30  ? -0.838  -12.437 -19.512 1.00 81.57  ? 73  ARG   A O   1 
ATOM   193  C CB  . ARG   A 1 30  ? -2.909  -14.349 -20.443 1.00 85.14  ? 73  ARG   A CB  1 
ATOM   194  C CG  . ARG   A 1 30  ? -4.019  -14.911 -21.313 1.00 90.96  ? 73  ARG   A CG  1 
ATOM   195  C CD  . ARG   A 1 30  ? -3.843  -16.391 -21.583 1.00 97.35  ? 73  ARG   A CD  1 
ATOM   196  N NE  . ARG   A 1 30  ? -4.665  -16.828 -22.717 1.00 102.10 ? 73  ARG   A NE  1 
ATOM   197  C CZ  . ARG   A 1 30  ? -5.929  -17.232 -22.616 1.00 104.65 ? 73  ARG   A CZ  1 
ATOM   198  N NH1 . ARG   A 1 30  ? -6.528  -17.271 -21.431 1.00 104.34 ? 73  ARG   A NH1 1 
ATOM   199  N NH2 . ARG   A 1 30  ? -6.602  -17.602 -23.697 1.00 104.54 ? 73  ARG   A NH2 1 
ATOM   200  N N   . LEU   A 1 31  ? -2.496  -11.569 -18.250 1.00 80.38  ? 74  LEU   A N   1 
ATOM   201  C CA  . LEU   A 1 31  ? -1.637  -10.865 -17.309 1.00 79.66  ? 74  LEU   A CA  1 
ATOM   202  C C   . LEU   A 1 31  ? -1.715  -11.432 -15.895 1.00 78.93  ? 74  LEU   A C   1 
ATOM   203  O O   . LEU   A 1 31  ? -2.791  -11.802 -15.447 1.00 78.96  ? 74  LEU   A O   1 
ATOM   204  C CB  . LEU   A 1 31  ? -2.075  -9.389  -17.276 1.00 79.71  ? 74  LEU   A CB  1 
ATOM   205  C CG  . LEU   A 1 31  ? -2.118  -8.685  -18.634 1.00 81.42  ? 74  LEU   A CG  1 
ATOM   206  C CD1 . LEU   A 1 31  ? -2.800  -7.353  -18.539 1.00 81.73  ? 74  LEU   A CD1 1 
ATOM   207  C CD2 . LEU   A 1 31  ? -0.720  -8.565  -19.228 1.00 82.36  ? 74  LEU   A CD2 1 
ATOM   208  N N   . ASP   A 1 32  ? -0.585  -11.446 -15.174 1.00 77.80  ? 75  ASP   A N   1 
ATOM   209  C CA  . ASP   A 1 32  ? -0.556  -11.870 -13.778 1.00 77.10  ? 75  ASP   A CA  1 
ATOM   210  C C   . ASP   A 1 32  ? -0.733  -10.611 -12.953 1.00 74.39  ? 75  ASP   A C   1 
ATOM   211  O O   . ASP   A 1 32  ? 0.187   -9.796  -12.917 1.00 75.17  ? 75  ASP   A O   1 
ATOM   212  C CB  . ASP   A 1 32  ? 0.803   -12.498 -13.435 1.00 80.58  ? 75  ASP   A CB  1 
ATOM   213  C CG  . ASP   A 1 32  ? 0.851   -14.012 -13.534 1.00 88.59  ? 75  ASP   A CG  1 
ATOM   214  O OD1 . ASP   A 1 32  ? -0.203  -14.626 -13.827 1.00 90.01  ? 75  ASP   A OD1 1 
ATOM   215  O OD2 . ASP   A 1 32  ? 1.944   -14.588 -13.307 1.00 91.98  ? 75  ASP   A OD2 1 
ATOM   216  N N   . VAL   A 1 33  ? -1.898  -10.421 -12.311 1.00 71.16  ? 76  VAL   A N   1 
ATOM   217  C CA  . VAL   A 1 33  ? -2.153  -9.189  -11.562 1.00 68.84  ? 76  VAL   A CA  1 
ATOM   218  C C   . VAL   A 1 33  ? -2.493  -9.440  -10.078 1.00 66.97  ? 76  VAL   A C   1 
ATOM   219  O O   . VAL   A 1 33  ? -2.829  -10.562 -9.678  1.00 66.78  ? 76  VAL   A O   1 
ATOM   220  C CB  . VAL   A 1 33  ? -3.242  -8.282  -12.251 1.00 68.62  ? 76  VAL   A CB  1 
ATOM   221  C CG1 . VAL   A 1 33  ? -2.978  -8.076  -13.739 1.00 68.60  ? 76  VAL   A CG1 1 
ATOM   222  C CG2 . VAL   A 1 33  ? -4.635  -8.838  -12.029 1.00 68.75  ? 76  VAL   A CG2 1 
ATOM   223  N N   . ALA   A 1 34  ? -2.391  -8.375  -9.263  1.00 65.22  ? 77  ALA   A N   1 
ATOM   224  C CA  . ALA   A 1 34  ? -2.763  -8.362  -7.855  1.00 64.33  ? 77  ALA   A CA  1 
ATOM   225  C C   . ALA   A 1 34  ? -3.787  -7.223  -7.630  1.00 63.01  ? 77  ALA   A C   1 
ATOM   226  O O   . ALA   A 1 34  ? -3.763  -6.225  -8.348  1.00 63.42  ? 77  ALA   A O   1 
ATOM   227  C CB  . ALA   A 1 34  ? -1.533  -8.160  -6.973  1.00 64.19  ? 77  ALA   A CB  1 
ATOM   228  N N   . LEU   A 1 35  ? -4.709  -7.390  -6.680  1.00 61.40  ? 78  LEU   A N   1 
ATOM   229  C CA  . LEU   A 1 35  ? -5.725  -6.371  -6.397  1.00 60.43  ? 78  LEU   A CA  1 
ATOM   230  C C   . LEU   A 1 35  ? -5.571  -5.950  -4.936  1.00 61.04  ? 78  LEU   A C   1 
ATOM   231  O O   . LEU   A 1 35  ? -5.611  -6.811  -4.031  1.00 61.47  ? 78  LEU   A O   1 
ATOM   232  C CB  . LEU   A 1 35  ? -7.133  -6.912  -6.679  1.00 59.43  ? 78  LEU   A CB  1 
ATOM   233  C CG  . LEU   A 1 35  ? -8.297  -5.978  -6.320  1.00 59.88  ? 78  LEU   A CG  1 
ATOM   234  C CD1 . LEU   A 1 35  ? -8.219  -4.655  -7.070  1.00 60.06  ? 78  LEU   A CD1 1 
ATOM   235  C CD2 . LEU   A 1 35  ? -9.621  -6.636  -6.569  1.00 59.90  ? 78  LEU   A CD2 1 
ATOM   236  N N   . ASP   A 1 36  ? -5.292  -4.656  -4.698  1.00 61.00  ? 79  ASP   A N   1 
ATOM   237  C CA  . ASP   A 1 36  ? -5.067  -4.206  -3.321  1.00 61.78  ? 79  ASP   A CA  1 
ATOM   238  C C   . ASP   A 1 36  ? -6.375  -3.691  -2.649  1.00 61.76  ? 79  ASP   A C   1 
ATOM   239  O O   . ASP   A 1 36  ? -7.413  -3.561  -3.299  1.00 61.46  ? 79  ASP   A O   1 
ATOM   240  C CB  . ASP   A 1 36  ? -3.888  -3.202  -3.236  1.00 63.49  ? 79  ASP   A CB  1 
ATOM   241  C CG  . ASP   A 1 36  ? -4.195  -1.776  -3.657  1.00 68.17  ? 79  ASP   A CG  1 
ATOM   242  O OD1 . ASP   A 1 36  ? -5.345  -1.505  -4.033  1.00 68.40  ? 79  ASP   A OD1 1 
ATOM   243  O OD2 . ASP   A 1 36  ? -3.282  -0.927  -3.588  1.00 71.15  ? 79  ASP   A OD2 1 
ATOM   244  N N   . GLU   A 1 37  ? -6.303  -3.413  -1.344  1.00 61.84  ? 80  GLU   A N   1 
ATOM   245  C CA  . GLU   A 1 37  ? -7.403  -2.940  -0.526  1.00 61.76  ? 80  GLU   A CA  1 
ATOM   246  C C   . GLU   A 1 37  ? -8.003  -1.626  -1.024  1.00 60.98  ? 80  GLU   A C   1 
ATOM   247  O O   . GLU   A 1 37  ? -9.161  -1.362  -0.752  1.00 61.18  ? 80  GLU   A O   1 
ATOM   248  C CB  . GLU   A 1 37  ? -6.935  -2.820  0.918   1.00 64.46  ? 80  GLU   A CB  1 
ATOM   249  C CG  . GLU   A 1 37  ? -8.053  -3.009  1.917   1.00 71.27  ? 80  GLU   A CG  1 
ATOM   250  C CD  . GLU   A 1 37  ? -7.715  -2.452  3.280   1.00 77.24  ? 80  GLU   A CD  1 
ATOM   251  O OE1 . GLU   A 1 37  ? -7.876  -1.226  3.482   1.00 79.72  ? 80  GLU   A OE1 1 
ATOM   252  O OE2 . GLU   A 1 37  ? -7.271  -3.241  4.141   1.00 78.70  ? 80  GLU   A OE2 1 
ATOM   253  N N   . SER   A 1 38  ? -7.249  -0.823  -1.791  1.00 59.81  ? 81  SER   A N   1 
ATOM   254  C CA  . SER   A 1 38  ? -7.772  0.411   -2.385  1.00 58.98  ? 81  SER   A CA  1 
ATOM   255  C C   . SER   A 1 38  ? -8.419  0.202   -3.764  1.00 58.26  ? 81  SER   A C   1 
ATOM   256  O O   . SER   A 1 38  ? -8.827  1.186   -4.388  1.00 58.47  ? 81  SER   A O   1 
ATOM   257  C CB  . SER   A 1 38  ? -6.668  1.449   -2.525  1.00 60.52  ? 81  SER   A CB  1 
ATOM   258  O OG  . SER   A 1 38  ? -6.200  1.829   -1.242  1.00 64.42  ? 81  SER   A OG  1 
ATOM   259  N N   . GLY   A 1 39  ? -8.520  -1.045  -4.234  1.00 57.34  ? 82  GLY   A N   1 
ATOM   260  C CA  . GLY   A 1 39  ? -9.105  -1.313  -5.540  1.00 57.68  ? 82  GLY   A CA  1 
ATOM   261  C C   . GLY   A 1 39  ? -8.133  -1.097  -6.693  1.00 58.41  ? 82  GLY   A C   1 
ATOM   262  O O   . GLY   A 1 39  ? -8.555  -1.064  -7.843  1.00 57.92  ? 82  GLY   A O   1 
ATOM   263  N N   . ASP   A 1 40  ? -6.821  -1.003  -6.414  1.00 59.38  ? 83  ASP   A N   1 
ATOM   264  C CA  . ASP   A 1 40  ? -5.820  -0.809  -7.456  1.00 61.29  ? 83  ASP   A CA  1 
ATOM   265  C C   . ASP   A 1 40  ? -5.187  -2.105  -7.975  1.00 62.65  ? 83  ASP   A C   1 
ATOM   266  O O   . ASP   A 1 40  ? -4.589  -2.866  -7.210  1.00 62.84  ? 83  ASP   A O   1 
ATOM   267  C CB  . ASP   A 1 40  ? -4.728  0.177   -6.998  1.00 63.40  ? 83  ASP   A CB  1 
ATOM   268  C CG  . ASP   A 1 40  ? -5.243  1.594   -6.840  1.00 69.71  ? 83  ASP   A CG  1 
ATOM   269  O OD1 . ASP   A 1 40  ? -6.126  1.998   -7.629  1.00 70.62  ? 83  ASP   A OD1 1 
ATOM   270  O OD2 . ASP   A 1 40  ? -4.771  2.295   -5.926  1.00 72.92  ? 83  ASP   A OD2 1 
ATOM   271  N N   . PHE   A 1 41  ? -5.299  -2.338  -9.286  1.00 63.27  ? 84  PHE   A N   1 
ATOM   272  C CA  . PHE   A 1 41  ? -4.665  -3.475  -9.926  1.00 64.32  ? 84  PHE   A CA  1 
ATOM   273  C C   . PHE   A 1 41  ? -3.206  -3.154  -10.176 1.00 68.10  ? 84  PHE   A C   1 
ATOM   274  O O   . PHE   A 1 41  ? -2.867  -2.032  -10.560 1.00 68.76  ? 84  PHE   A O   1 
ATOM   275  C CB  . PHE   A 1 41  ? -5.358  -3.825  -11.245 1.00 62.48  ? 84  PHE   A CB  1 
ATOM   276  C CG  . PHE   A 1 41  ? -6.673  -4.540  -11.064 1.00 61.61  ? 84  PHE   A CG  1 
ATOM   277  C CD1 . PHE   A 1 41  ? -6.712  -5.852  -10.635 1.00 61.84  ? 84  PHE   A CD1 1 
ATOM   278  C CD2 . PHE   A 1 41  ? -7.872  -3.898  -11.322 1.00 61.64  ? 84  PHE   A CD2 1 
ATOM   279  C CE1 . PHE   A 1 41  ? -7.926  -6.510  -10.487 1.00 62.35  ? 84  PHE   A CE1 1 
ATOM   280  C CE2 . PHE   A 1 41  ? -9.079  -4.560  -11.174 1.00 61.68  ? 84  PHE   A CE2 1 
ATOM   281  C CZ  . PHE   A 1 41  ? -9.103  -5.856  -10.753 1.00 61.51  ? 84  PHE   A CZ  1 
ATOM   282  N N   . SER   A 1 42  ? -2.332  -4.132  -9.967  1.00 70.75  ? 85  SER   A N   1 
ATOM   283  C CA  . SER   A 1 42  ? -0.902  -3.958  -10.213 1.00 73.79  ? 85  SER   A CA  1 
ATOM   284  C C   . SER   A 1 42  ? -0.334  -5.230  -10.824 1.00 77.57  ? 85  SER   A C   1 
ATOM   285  O O   . SER   A 1 42  ? -0.894  -6.307  -10.612 1.00 78.30  ? 85  SER   A O   1 
ATOM   286  C CB  . SER   A 1 42  ? -0.157  -3.611  -8.927  1.00 74.94  ? 85  SER   A CB  1 
ATOM   287  O OG  . SER   A 1 42  ? -0.207  -4.666  -7.980  1.00 77.17  ? 85  SER   A OG  1 
ATOM   288  N N   . LEU   A 1 43  ? 0.766   -5.120  -11.588 1.00 79.59  ? 86  LEU   A N   1 
ATOM   289  C CA  . LEU   A 1 43  ? 1.357   -6.302  -12.212 1.00 81.89  ? 86  LEU   A CA  1 
ATOM   290  C C   . LEU   A 1 43  ? 2.295   -7.038  -11.310 1.00 84.55  ? 86  LEU   A C   1 
ATOM   291  O O   . LEU   A 1 43  ? 3.148   -6.443  -10.652 1.00 84.70  ? 86  LEU   A O   1 
ATOM   292  C CB  . LEU   A 1 43  ? 2.072   -6.006  -13.551 1.00 81.66  ? 86  LEU   A CB  1 
ATOM   293  C CG  . LEU   A 1 43  ? 1.269   -5.333  -14.672 1.00 83.15  ? 86  LEU   A CG  1 
ATOM   294  C CD1 . LEU   A 1 43  ? 2.009   -5.434  -15.980 1.00 83.95  ? 86  LEU   A CD1 1 
ATOM   295  C CD2 . LEU   A 1 43  ? -0.103  -5.960  -14.852 1.00 83.86  ? 86  LEU   A CD2 1 
ATOM   296  N N   . VAL   A 1 44  ? 2.166   -8.357  -11.328 1.00 86.49  ? 87  VAL   A N   1 
ATOM   297  C CA  . VAL   A 1 44  ? 3.048   -9.273  -10.630 1.00 88.71  ? 87  VAL   A CA  1 
ATOM   298  C C   . VAL   A 1 44  ? 3.944   -9.852  -11.729 1.00 91.51  ? 87  VAL   A C   1 
ATOM   299  O O   . VAL   A 1 44  ? 3.427   -10.298 -12.762 1.00 91.58  ? 87  VAL   A O   1 
ATOM   300  C CB  . VAL   A 1 44  ? 2.242   -10.388 -9.925  1.00 88.95  ? 87  VAL   A CB  1 
ATOM   301  C CG1 . VAL   A 1 44  ? 3.174   -11.395 -9.260  1.00 89.39  ? 87  VAL   A CG1 1 
ATOM   302  C CG2 . VAL   A 1 44  ? 1.261   -9.800  -8.921  1.00 89.08  ? 87  VAL   A CG2 1 
ATOM   303  N N   . GLU   A 1 45  ? 5.272   -9.791  -11.557 1.00 93.68  ? 88  GLU   A N   1 
ATOM   304  C CA  . GLU   A 1 45  ? 6.180   -10.327 -12.579 1.00 96.23  ? 88  GLU   A CA  1 
ATOM   305  C C   . GLU   A 1 45  ? 7.234   -11.259 -12.001 1.00 97.98  ? 88  GLU   A C   1 
ATOM   306  O O   . GLU   A 1 45  ? 7.772   -12.107 -12.721 1.00 99.19  ? 88  GLU   A O   1 
ATOM   307  C CB  . GLU   A 1 45  ? 6.817   -9.206  -13.426 1.00 99.46  ? 88  GLU   A CB  1 
ATOM   308  C CG  . GLU   A 1 45  ? 5.826   -8.447  -14.302 1.00 105.36 ? 88  GLU   A CG  1 
ATOM   309  C CD  . GLU   A 1 45  ? 6.300   -8.194  -15.721 1.00 112.43 ? 88  GLU   A CD  1 
ATOM   310  O OE1 . GLU   A 1 45  ? 7.249   -8.883  -16.163 1.00 114.12 ? 88  GLU   A OE1 1 
ATOM   311  O OE2 . GLU   A 1 45  ? 5.722   -7.309  -16.392 1.00 114.02 ? 88  GLU   A OE2 1 
ATOM   312  N N   . GLU   B 2 8   ? -34.859 11.316  -14.856 1.00 77.76  ? 17  GLU   B N   1 
ATOM   313  C CA  . GLU   B 2 8   ? -34.732 10.303  -15.903 1.00 78.26  ? 17  GLU   B CA  1 
ATOM   314  C C   . GLU   B 2 8   ? -34.292 8.925   -15.388 1.00 78.37  ? 17  GLU   B C   1 
ATOM   315  O O   . GLU   B 2 8   ? -33.123 8.703   -15.086 1.00 79.06  ? 17  GLU   B O   1 
ATOM   316  C CB  . GLU   B 2 8   ? -33.819 10.768  -17.052 1.00 79.83  ? 17  GLU   B CB  1 
ATOM   317  C CG  . GLU   B 2 8   ? -34.066 9.998   -18.338 1.00 83.08  ? 17  GLU   B CG  1 
ATOM   318  C CD  . GLU   B 2 8   ? -33.358 10.543  -19.563 1.00 87.48  ? 17  GLU   B CD  1 
ATOM   319  O OE1 . GLU   B 2 8   ? -32.408 11.345  -19.395 1.00 87.46  ? 17  GLU   B OE1 1 
ATOM   320  O OE2 . GLU   B 2 8   ? -33.782 10.200  -20.692 1.00 89.47  ? 17  GLU   B OE2 1 
ATOM   321  N N   . THR   B 2 9   ? -35.236 7.999   -15.313 1.00 77.57  ? 18  THR   B N   1 
ATOM   322  C CA  . THR   B 2 9   ? -34.958 6.632   -14.899 1.00 77.24  ? 18  THR   B CA  1 
ATOM   323  C C   . THR   B 2 9   ? -35.126 5.641   -16.040 1.00 75.86  ? 18  THR   B C   1 
ATOM   324  O O   . THR   B 2 9   ? -35.310 4.459   -15.771 1.00 76.81  ? 18  THR   B O   1 
ATOM   325  C CB  . THR   B 2 9   ? -35.824 6.226   -13.708 1.00 79.32  ? 18  THR   B CB  1 
ATOM   326  O OG1 . THR   B 2 9   ? -37.184 6.635   -13.941 1.00 80.98  ? 18  THR   B OG1 1 
ATOM   327  C CG2 . THR   B 2 9   ? -35.296 6.779   -12.390 1.00 79.91  ? 18  THR   B CG2 1 
ATOM   328  N N   . THR   B 2 10  ? -35.079 6.094   -17.299 1.00 73.66  ? 19  THR   B N   1 
ATOM   329  C CA  . THR   B 2 10  ? -35.214 5.197   -18.439 1.00 72.05  ? 19  THR   B CA  1 
ATOM   330  C C   . THR   B 2 10  ? -33.957 4.346   -18.513 1.00 69.70  ? 19  THR   B C   1 
ATOM   331  O O   . THR   B 2 10  ? -32.852 4.874   -18.408 1.00 69.66  ? 19  THR   B O   1 
ATOM   332  C CB  . THR   B 2 10  ? -35.365 6.003   -19.761 1.00 73.48  ? 19  THR   B CB  1 
ATOM   333  O OG1 . THR   B 2 10  ? -36.281 7.087   -19.592 1.00 75.65  ? 19  THR   B OG1 1 
ATOM   334  C CG2 . THR   B 2 10  ? -35.812 5.141   -20.918 1.00 73.67  ? 19  THR   B CG2 1 
ATOM   335  N N   . ASP   B 2 11  ? -34.106 3.038   -18.745 1.00 67.88  ? 20  ASP   B N   1 
ATOM   336  C CA  . ASP   B 2 11  ? -32.996 2.105   -18.953 1.00 66.97  ? 20  ASP   B CA  1 
ATOM   337  C C   . ASP   B 2 11  ? -32.056 2.651   -20.068 1.00 66.07  ? 20  ASP   B C   1 
ATOM   338  O O   . ASP   B 2 11  ? -32.533 3.305   -20.999 1.00 66.57  ? 20  ASP   B O   1 
ATOM   339  C CB  . ASP   B 2 11  ? -33.570 0.752   -19.421 1.00 68.70  ? 20  ASP   B CB  1 
ATOM   340  C CG  . ASP   B 2 11  ? -33.633 -0.359  -18.390 1.00 73.45  ? 20  ASP   B CG  1 
ATOM   341  O OD1 . ASP   B 2 11  ? -34.120 -0.097  -17.257 1.00 73.24  ? 20  ASP   B OD1 1 
ATOM   342  O OD2 . ASP   B 2 11  ? -33.208 -1.503  -18.718 1.00 75.59  ? 20  ASP   B OD2 1 
ATOM   343  N N   . GLY   B 2 12  ? -30.755 2.429   -19.943 1.00 64.24  ? 21  GLY   B N   1 
ATOM   344  C CA  . GLY   B 2 12  ? -29.797 2.923   -20.923 1.00 62.46  ? 21  GLY   B CA  1 
ATOM   345  C C   . GLY   B 2 12  ? -28.472 3.338   -20.318 1.00 60.39  ? 21  GLY   B C   1 
ATOM   346  O O   . GLY   B 2 12  ? -28.231 3.113   -19.135 1.00 59.54  ? 21  GLY   B O   1 
ATOM   347  N N   . VAL   B 2 13  ? -27.584 3.920   -21.140 1.00 58.86  ? 22  VAL   B N   1 
ATOM   348  C CA  . VAL   B 2 13  ? -26.263 4.379   -20.701 1.00 57.31  ? 22  VAL   B CA  1 
ATOM   349  C C   . VAL   B 2 13  ? -26.278 5.905   -20.495 1.00 56.71  ? 22  VAL   B C   1 
ATOM   350  O O   . VAL   B 2 13  ? -26.977 6.623   -21.231 1.00 56.85  ? 22  VAL   B O   1 
ATOM   351  C CB  . VAL   B 2 13  ? -25.142 3.885   -21.648 1.00 56.89  ? 22  VAL   B CB  1 
ATOM   352  C CG1 . VAL   B 2 13  ? -25.318 4.433   -23.069 1.00 56.86  ? 22  VAL   B CG1 1 
ATOM   353  C CG2 . VAL   B 2 13  ? -23.767 4.223   -21.095 1.00 56.36  ? 22  VAL   B CG2 1 
ATOM   354  N N   . TYR   B 2 14  ? -25.616 6.388   -19.426 1.00 55.99  ? 23  TYR   B N   1 
ATOM   355  C CA  . TYR   B 2 14  ? -25.624 7.805   -19.056 1.00 56.40  ? 23  TYR   B CA  1 
ATOM   356  C C   . TYR   B 2 14  ? -24.236 8.407   -18.816 1.00 56.52  ? 23  TYR   B C   1 
ATOM   357  O O   . TYR   B 2 14  ? -23.338 7.728   -18.365 1.00 56.26  ? 23  TYR   B O   1 
ATOM   358  C CB  . TYR   B 2 14  ? -26.440 8.007   -17.754 1.00 56.31  ? 23  TYR   B CB  1 
ATOM   359  C CG  . TYR   B 2 14  ? -27.934 7.837   -17.909 1.00 56.26  ? 23  TYR   B CG  1 
ATOM   360  C CD1 . TYR   B 2 14  ? -28.492 6.587   -18.144 1.00 57.05  ? 23  TYR   B CD1 1 
ATOM   361  C CD2 . TYR   B 2 14  ? -28.796 8.909   -17.736 1.00 56.75  ? 23  TYR   B CD2 1 
ATOM   362  C CE1 . TYR   B 2 14  ? -29.863 6.425   -18.287 1.00 58.08  ? 23  TYR   B CE1 1 
ATOM   363  C CE2 . TYR   B 2 14  ? -30.169 8.766   -17.897 1.00 57.61  ? 23  TYR   B CE2 1 
ATOM   364  C CZ  . TYR   B 2 14  ? -30.700 7.518   -18.159 1.00 59.00  ? 23  TYR   B CZ  1 
ATOM   365  O OH  . TYR   B 2 14  ? -32.053 7.345   -18.274 1.00 60.71  ? 23  TYR   B OH  1 
ATOM   366  N N   . ARG   B 2 15  ? -24.097 9.714   -19.029 1.00 56.56  ? 24  ARG   B N   1 
ATOM   367  C CA  . ARG   B 2 15  ? -22.863 10.435  -18.722 1.00 56.18  ? 24  ARG   B CA  1 
ATOM   368  C C   . ARG   B 2 15  ? -22.974 10.948  -17.294 1.00 55.73  ? 24  ARG   B C   1 
ATOM   369  O O   . ARG   B 2 15  ? -24.034 11.417  -16.914 1.00 55.62  ? 24  ARG   B O   1 
ATOM   370  C CB  . ARG   B 2 15  ? -22.704 11.656  -19.652 1.00 56.29  ? 24  ARG   B CB  1 
ATOM   371  C CG  . ARG   B 2 15  ? -22.510 11.307  -21.124 1.00 58.04  ? 24  ARG   B CG  1 
ATOM   372  C CD  . ARG   B 2 15  ? -22.390 12.564  -21.964 1.00 60.64  ? 24  ARG   B CD  1 
ATOM   373  N NE  . ARG   B 2 15  ? -22.563 12.252  -23.382 1.00 63.56  ? 24  ARG   B NE  1 
ATOM   374  C CZ  . ARG   B 2 15  ? -21.571 11.961  -24.215 1.00 66.02  ? 24  ARG   B CZ  1 
ATOM   375  N NH1 . ARG   B 2 15  ? -20.311 11.987  -23.796 1.00 64.92  ? 24  ARG   B NH1 1 
ATOM   376  N NH2 . ARG   B 2 15  ? -21.830 11.636  -25.476 1.00 67.24  ? 24  ARG   B NH2 1 
ATOM   377  N N   . VAL   B 2 16  ? -21.883 10.939  -16.538 1.00 55.58  ? 25  VAL   B N   1 
ATOM   378  C CA  . VAL   B 2 16  ? -21.833 11.492  -15.188 1.00 56.84  ? 25  VAL   B CA  1 
ATOM   379  C C   . VAL   B 2 16  ? -20.969 12.745  -15.281 1.00 57.66  ? 25  VAL   B C   1 
ATOM   380  O O   . VAL   B 2 16  ? -19.809 12.677  -15.683 1.00 57.35  ? 25  VAL   B O   1 
ATOM   381  C CB  . VAL   B 2 16  ? -21.279 10.473  -14.166 1.00 58.30  ? 25  VAL   B CB  1 
ATOM   382  C CG1 . VAL   B 2 16  ? -21.268 11.060  -12.758 1.00 58.40  ? 25  VAL   B CG1 1 
ATOM   383  C CG2 . VAL   B 2 16  ? -22.070 9.159   -14.219 1.00 58.99  ? 25  VAL   B CG2 1 
ATOM   384  N N   . MET   B 2 17  ? -21.568 13.898  -14.997 1.00 59.04  ? 26  MET   B N   1 
ATOM   385  C CA  . MET   B 2 17  ? -20.958 15.212  -15.184 1.00 60.54  ? 26  MET   B CA  1 
ATOM   386  C C   . MET   B 2 17  ? -20.790 16.019  -13.887 1.00 63.12  ? 26  MET   B C   1 
ATOM   387  O O   . MET   B 2 17  ? -21.498 15.785  -12.912 1.00 62.61  ? 26  MET   B O   1 
ATOM   388  C CB  . MET   B 2 17  ? -21.882 16.053  -16.102 1.00 60.17  ? 26  MET   B CB  1 
ATOM   389  C CG  . MET   B 2 17  ? -22.391 15.353  -17.333 1.00 60.11  ? 26  MET   B CG  1 
ATOM   390  S SD  . MET   B 2 17  ? -21.090 15.126  -18.569 1.00 62.80  ? 26  MET   B SD  1 
ATOM   391  C CE  . MET   B 2 17  ? -20.581 16.818  -18.863 1.00 60.39  ? 26  MET   B CE  1 
ATOM   392  N N   . THR   B 2 18  ? -19.929 17.049  -13.923 1.00 65.52  ? 27  THR   B N   1 
ATOM   393  C CA  . THR   B 2 18  ? -19.788 17.960  -12.804 1.00 68.36  ? 27  THR   B CA  1 
ATOM   394  C C   . THR   B 2 18  ? -19.553 19.423  -13.256 1.00 70.84  ? 27  THR   B C   1 
ATOM   395  O O   . THR   B 2 18  ? -18.856 19.707  -14.237 1.00 70.61  ? 27  THR   B O   1 
ATOM   396  C CB  . THR   B 2 18  ? -18.742 17.479  -11.779 1.00 70.09  ? 27  THR   B CB  1 
ATOM   397  O OG1 . THR   B 2 18  ? -18.806 18.362  -10.648 1.00 71.94  ? 27  THR   B OG1 1 
ATOM   398  C CG2 . THR   B 2 18  ? -17.328 17.441  -12.348 1.00 69.88  ? 27  THR   B CG2 1 
ATOM   399  N N   . ARG   B 2 19  ? -20.172 20.350  -12.527 1.00 72.72  ? 28  ARG   B N   1 
ATOM   400  C CA  . ARG   B 2 19  ? -19.987 21.775  -12.756 1.00 75.10  ? 28  ARG   B CA  1 
ATOM   401  C C   . ARG   B 2 19  ? -18.965 22.403  -11.757 1.00 76.63  ? 28  ARG   B C   1 
ATOM   402  O O   . ARG   B 2 19  ? -18.752 23.614  -11.779 1.00 76.61  ? 28  ARG   B O   1 
ATOM   403  C CB  . ARG   B 2 19  ? -21.340 22.493  -12.701 1.00 77.90  ? 28  ARG   B CB  1 
ATOM   404  C CG  . ARG   B 2 19  ? -22.316 21.962  -13.742 1.00 83.31  ? 28  ARG   B CG  1 
ATOM   405  C CD  . ARG   B 2 19  ? -23.445 22.932  -14.042 1.00 88.50  ? 28  ARG   B CD  1 
ATOM   406  N NE  . ARG   B 2 19  ? -23.998 22.709  -15.381 1.00 93.17  ? 28  ARG   B NE  1 
ATOM   407  C CZ  . ARG   B 2 19  ? -25.187 22.162  -15.623 1.00 96.76  ? 28  ARG   B CZ  1 
ATOM   408  N NH1 . ARG   B 2 19  ? -25.973 21.789  -14.617 1.00 97.40  ? 28  ARG   B NH1 1 
ATOM   409  N NH2 . ARG   B 2 19  ? -25.603 21.991  -16.872 1.00 96.41  ? 28  ARG   B NH2 1 
ATOM   410  N N   . ARG   B 2 20  ? -18.326 21.569  -10.905 1.00 78.12  ? 29  ARG   B N   1 
ATOM   411  C CA  . ARG   B 2 20  ? -17.356 21.956  -9.875  1.00 80.05  ? 29  ARG   B CA  1 
ATOM   412  C C   . ARG   B 2 20  ? -16.052 22.499  -10.476 1.00 80.92  ? 29  ARG   B C   1 
ATOM   413  O O   . ARG   B 2 20  ? -15.394 23.353  -9.873  1.00 81.75  ? 29  ARG   B O   1 
ATOM   414  C CB  . ARG   B 2 20  ? -17.076 20.751  -8.959  1.00 82.52  ? 29  ARG   B CB  1 
ATOM   415  C CG  . ARG   B 2 20  ? -16.181 21.049  -7.772  1.00 87.90  ? 29  ARG   B CG  1 
ATOM   416  C CD  . ARG   B 2 20  ? -15.745 19.763  -7.097  1.00 92.79  ? 29  ARG   B CD  1 
ATOM   417  N NE  . ARG   B 2 20  ? -14.843 18.971  -7.940  1.00 96.77  ? 29  ARG   B NE  1 
ATOM   418  C CZ  . ARG   B 2 20  ? -13.623 18.585  -7.576  1.00 99.84  ? 29  ARG   B CZ  1 
ATOM   419  N NH1 . ARG   B 2 20  ? -13.148 18.904  -6.376  1.00 100.32 ? 29  ARG   B NH1 1 
ATOM   420  N NH2 . ARG   B 2 20  ? -12.876 17.860  -8.400  1.00 99.57  ? 29  ARG   B NH2 1 
ATOM   421  N N   . LEU   B 2 21  ? -15.695 22.024  -11.675 1.00 80.36  ? 30  LEU   B N   1 
ATOM   422  C CA  . LEU   B 2 21  ? -14.498 22.467  -12.374 1.00 80.18  ? 30  LEU   B CA  1 
ATOM   423  C C   . LEU   B 2 21  ? -14.871 23.502  -13.481 1.00 79.53  ? 30  LEU   B C   1 
ATOM   424  O O   . LEU   B 2 21  ? -15.963 24.089  -13.437 1.00 79.88  ? 30  LEU   B O   1 
ATOM   425  C CB  . LEU   B 2 21  ? -13.779 21.219  -12.937 1.00 80.72  ? 30  LEU   B CB  1 
ATOM   426  C CG  . LEU   B 2 21  ? -12.697 20.514  -12.082 1.00 82.79  ? 30  LEU   B CG  1 
ATOM   427  C CD1 . LEU   B 2 21  ? -12.947 20.615  -10.564 1.00 83.50  ? 30  LEU   B CD1 1 
ATOM   428  C CD2 . LEU   B 2 21  ? -12.559 19.051  -12.483 1.00 83.45  ? 30  LEU   B CD2 1 
ATOM   429  N N   . LEU   B 2 22  ? -13.948 23.787  -14.414 1.00 78.40  ? 31  LEU   B N   1 
ATOM   430  C CA  . LEU   B 2 22  ? -14.195 24.711  -15.521 1.00 77.93  ? 31  LEU   B CA  1 
ATOM   431  C C   . LEU   B 2 22  ? -15.234 24.067  -16.432 1.00 77.68  ? 31  LEU   B C   1 
ATOM   432  O O   . LEU   B 2 22  ? -15.122 22.877  -16.722 1.00 78.37  ? 31  LEU   B O   1 
ATOM   433  C CB  . LEU   B 2 22  ? -12.900 24.910  -16.300 1.00 77.57  ? 31  LEU   B CB  1 
ATOM   434  C CG  . LEU   B 2 22  ? -12.966 25.936  -17.383 1.00 78.40  ? 31  LEU   B CG  1 
ATOM   435  C CD1 . LEU   B 2 22  ? -12.612 27.315  -16.846 1.00 78.17  ? 31  LEU   B CD1 1 
ATOM   436  C CD2 . LEU   B 2 22  ? -12.084 25.526  -18.549 1.00 79.06  ? 31  LEU   B CD2 1 
ATOM   437  N N   . GLY   B 2 23  ? -16.276 24.806  -16.800 1.00 76.53  ? 32  GLY   B N   1 
ATOM   438  C CA  . GLY   B 2 23  ? -17.362 24.276  -17.619 1.00 75.83  ? 32  GLY   B CA  1 
ATOM   439  C C   . GLY   B 2 23  ? -17.996 23.006  -17.067 1.00 74.80  ? 32  GLY   B C   1 
ATOM   440  O O   . GLY   B 2 23  ? -17.906 22.722  -15.868 1.00 74.80  ? 32  GLY   B O   1 
ATOM   441  N N   . SER   B 2 24  ? -18.615 22.216  -17.943 1.00 73.84  ? 33  SER   B N   1 
ATOM   442  C CA  . SER   B 2 24  ? -19.205 20.943  -17.549 1.00 73.15  ? 33  SER   B CA  1 
ATOM   443  C C   . SER   B 2 24  ? -18.181 19.914  -17.913 1.00 71.14  ? 33  SER   B C   1 
ATOM   444  O O   . SER   B 2 24  ? -17.790 19.825  -19.073 1.00 70.45  ? 33  SER   B O   1 
ATOM   445  C CB  . SER   B 2 24  ? -20.496 20.681  -18.313 1.00 75.69  ? 33  SER   B CB  1 
ATOM   446  O OG  . SER   B 2 24  ? -21.473 21.663  -18.006 1.00 78.88  ? 33  SER   B OG  1 
ATOM   447  N N   . THR   B 2 25  ? -17.700 19.164  -16.918 1.00 69.81  ? 34  THR   B N   1 
ATOM   448  C CA  . THR   B 2 25  ? -16.655 18.179  -17.130 1.00 68.63  ? 34  THR   B CA  1 
ATOM   449  C C   . THR   B 2 25  ? -17.222 16.783  -16.958 1.00 67.16  ? 34  THR   B C   1 
ATOM   450  O O   . THR   B 2 25  ? -17.921 16.544  -15.970 1.00 67.56  ? 34  THR   B O   1 
ATOM   451  C CB  . THR   B 2 25  ? -15.491 18.461  -16.159 1.00 69.54  ? 34  THR   B CB  1 
ATOM   452  O OG1 . THR   B 2 25  ? -14.987 19.783  -16.398 1.00 71.14  ? 34  THR   B OG1 1 
ATOM   453  C CG2 . THR   B 2 25  ? -14.366 17.474  -16.304 1.00 69.43  ? 34  THR   B CG2 1 
ATOM   454  N N   . GLN   B 2 26  ? -16.965 15.866  -17.920 1.00 64.99  ? 35  GLN   B N   1 
ATOM   455  C CA  . GLN   B 2 26  ? -17.454 14.492  -17.768 1.00 63.48  ? 35  GLN   B CA  1 
ATOM   456  C C   . GLN   B 2 26  ? -16.450 13.656  -16.943 1.00 63.49  ? 35  GLN   B C   1 
ATOM   457  O O   . GLN   B 2 26  ? -15.313 13.435  -17.385 1.00 63.88  ? 35  GLN   B O   1 
ATOM   458  C CB  . GLN   B 2 26  ? -17.760 13.817  -19.123 1.00 61.66  ? 35  GLN   B CB  1 
ATOM   459  C CG  . GLN   B 2 26  ? -18.267 12.381  -18.962 1.00 60.34  ? 35  GLN   B CG  1 
ATOM   460  C CD  . GLN   B 2 26  ? -18.495 11.666  -20.274 1.00 64.25  ? 35  GLN   B CD  1 
ATOM   461  O OE1 . GLN   B 2 26  ? -19.152 12.169  -21.180 1.00 65.95  ? 35  GLN   B OE1 1 
ATOM   462  N NE2 . GLN   B 2 26  ? -17.965 10.465  -20.415 1.00 64.20  ? 35  GLN   B NE2 1 
ATOM   463  N N   . VAL   B 2 27  ? -16.870 13.202  -15.744 1.00 62.41  ? 36  VAL   B N   1 
ATOM   464  C CA  . VAL   B 2 27  ? -16.023 12.396  -14.852 1.00 61.65  ? 36  VAL   B CA  1 
ATOM   465  C C   . VAL   B 2 27  ? -16.189 10.871  -15.042 1.00 60.40  ? 36  VAL   B C   1 
ATOM   466  O O   . VAL   B 2 27  ? -15.335 10.086  -14.600 1.00 61.07  ? 36  VAL   B O   1 
ATOM   467  C CB  . VAL   B 2 27  ? -16.223 12.796  -13.363 1.00 62.46  ? 36  VAL   B CB  1 
ATOM   468  C CG1 . VAL   B 2 27  ? -15.761 14.226  -13.122 1.00 63.42  ? 36  VAL   B CG1 1 
ATOM   469  C CG2 . VAL   B 2 27  ? -17.670 12.629  -12.936 1.00 62.63  ? 36  VAL   B CG2 1 
ATOM   470  N N   . GLY   B 2 28  ? -17.278 10.461  -15.680 1.00 58.35  ? 37  GLY   B N   1 
ATOM   471  C CA  . GLY   B 2 28  ? -17.545 9.050   -15.890 1.00 56.71  ? 37  GLY   B CA  1 
ATOM   472  C C   . GLY   B 2 28  ? -18.848 8.768   -16.601 1.00 55.24  ? 37  GLY   B C   1 
ATOM   473  O O   . GLY   B 2 28  ? -19.463 9.663   -17.171 1.00 55.21  ? 37  GLY   B O   1 
ATOM   474  N N   . VAL   B 2 29  ? -19.253 7.500   -16.588 1.00 54.26  ? 38  VAL   B N   1 
ATOM   475  C CA  . VAL   B 2 29  ? -20.414 6.919   -17.265 1.00 53.22  ? 38  VAL   B CA  1 
ATOM   476  C C   . VAL   B 2 29  ? -21.076 5.887   -16.317 1.00 53.15  ? 38  VAL   B C   1 
ATOM   477  O O   . VAL   B 2 29  ? -20.438 5.375   -15.391 1.00 53.78  ? 38  VAL   B O   1 
ATOM   478  C CB  . VAL   B 2 29  ? -19.948 6.222   -18.596 1.00 52.59  ? 38  VAL   B CB  1 
ATOM   479  C CG1 . VAL   B 2 29  ? -21.104 5.578   -19.345 1.00 52.30  ? 38  VAL   B CG1 1 
ATOM   480  C CG2 . VAL   B 2 29  ? -19.186 7.175   -19.518 1.00 52.41  ? 38  VAL   B CG2 1 
ATOM   481  N N   . GLY   B 2 30  ? -22.338 5.580   -16.560 1.00 52.04  ? 39  GLY   B N   1 
ATOM   482  C CA  . GLY   B 2 30  ? -23.044 4.578   -15.782 1.00 51.50  ? 39  GLY   B CA  1 
ATOM   483  C C   . GLY   B 2 30  ? -24.182 3.940   -16.541 1.00 51.21  ? 39  GLY   B C   1 
ATOM   484  O O   . GLY   B 2 30  ? -24.533 4.385   -17.640 1.00 50.63  ? 39  GLY   B O   1 
ATOM   485  N N   . VAL   B 2 31  ? -24.779 2.904   -15.948 1.00 50.94  ? 40  VAL   B N   1 
ATOM   486  C CA  . VAL   B 2 31  ? -25.856 2.132   -16.559 1.00 51.45  ? 40  VAL   B CA  1 
ATOM   487  C C   . VAL   B 2 31  ? -27.090 2.252   -15.707 1.00 52.15  ? 40  VAL   B C   1 
ATOM   488  O O   . VAL   B 2 31  ? -27.023 1.994   -14.508 1.00 51.43  ? 40  VAL   B O   1 
ATOM   489  C CB  . VAL   B 2 31  ? -25.458 0.627   -16.670 1.00 51.81  ? 40  VAL   B CB  1 
ATOM   490  C CG1 . VAL   B 2 31  ? -26.648 -0.239  -17.085 1.00 52.38  ? 40  VAL   B CG1 1 
ATOM   491  C CG2 . VAL   B 2 31  ? -24.274 0.431   -17.619 1.00 51.82  ? 40  VAL   B CG2 1 
ATOM   492  N N   . MET   B 2 32  ? -28.231 2.559   -16.323 1.00 52.91  ? 41  MET   B N   1 
ATOM   493  C CA  . MET   B 2 32  ? -29.485 2.594   -15.594 1.00 54.21  ? 41  MET   B CA  1 
ATOM   494  C C   . MET   B 2 32  ? -30.231 1.307   -15.965 1.00 55.06  ? 41  MET   B C   1 
ATOM   495  O O   . MET   B 2 32  ? -30.484 1.067   -17.144 1.00 55.21  ? 41  MET   B O   1 
ATOM   496  C CB  . MET   B 2 32  ? -30.284 3.849   -15.975 1.00 55.18  ? 41  MET   B CB  1 
ATOM   497  C CG  . MET   B 2 32  ? -31.552 4.026   -15.195 1.00 57.34  ? 41  MET   B CG  1 
ATOM   498  S SD  . MET   B 2 32  ? -31.269 4.644   -13.520 1.00 63.53  ? 41  MET   B SD  1 
ATOM   499  C CE  . MET   B 2 32  ? -30.729 6.294   -13.891 1.00 62.86  ? 41  MET   B CE  1 
ATOM   500  N N   . GLN   B 2 33  ? -30.523 0.454   -14.985 1.00 55.36  ? 42  GLN   B N   1 
ATOM   501  C CA  . GLN   B 2 33  ? -31.260 -0.779  -15.232 1.00 56.53  ? 42  GLN   B CA  1 
ATOM   502  C C   . GLN   B 2 33  ? -32.135 -1.099  -14.045 1.00 57.34  ? 42  GLN   B C   1 
ATOM   503  O O   . GLN   B 2 33  ? -31.660 -1.041  -12.917 1.00 58.22  ? 42  GLN   B O   1 
ATOM   504  C CB  . GLN   B 2 33  ? -30.327 -1.951  -15.547 1.00 58.53  ? 42  GLN   B CB  1 
ATOM   505  C CG  . GLN   B 2 33  ? -31.113 -3.207  -15.926 1.00 62.84  ? 42  GLN   B CG  1 
ATOM   506  C CD  . GLN   B 2 33  ? -30.232 -4.302  -16.475 1.00 67.25  ? 42  GLN   B CD  1 
ATOM   507  O OE1 . GLN   B 2 33  ? -30.234 -5.436  -15.995 1.00 68.45  ? 42  GLN   B OE1 1 
ATOM   508  N NE2 . GLN   B 2 33  ? -29.444 -3.974  -17.484 1.00 68.26  ? 42  GLN   B NE2 1 
ATOM   509  N N   . GLU   B 2 34  ? -33.421 -1.375  -14.280 1.00 57.08  ? 43  GLU   B N   1 
ATOM   510  C CA  . GLU   B 2 34  ? -34.401 -1.692  -13.244 1.00 57.47  ? 43  GLU   B CA  1 
ATOM   511  C C   . GLU   B 2 34  ? -34.518 -0.608  -12.159 1.00 57.85  ? 43  GLU   B C   1 
ATOM   512  O O   . GLU   B 2 34  ? -34.779 -0.916  -11.000 1.00 58.62  ? 43  GLU   B O   1 
ATOM   513  C CB  . GLU   B 2 34  ? -34.148 -3.080  -12.628 1.00 60.24  ? 43  GLU   B CB  1 
ATOM   514  C CG  . GLU   B 2 34  ? -34.340 -4.224  -13.612 1.00 64.60  ? 43  GLU   B CG  1 
ATOM   515  C CD  . GLU   B 2 34  ? -33.547 -5.495  -13.351 1.00 73.42  ? 43  GLU   B CD  1 
ATOM   516  O OE1 . GLU   B 2 34  ? -33.905 -6.245  -12.415 1.00 75.29  ? 43  GLU   B OE1 1 
ATOM   517  O OE2 . GLU   B 2 34  ? -32.586 -5.763  -14.109 1.00 77.56  ? 43  GLU   B OE2 1 
ATOM   518  N N   . GLY   B 2 35  ? -34.378 0.652   -12.551 1.00 57.25  ? 44  GLY   B N   1 
ATOM   519  C CA  . GLY   B 2 35  ? -34.482 1.774   -11.621 1.00 56.82  ? 44  GLY   B CA  1 
ATOM   520  C C   . GLY   B 2 35  ? -33.239 2.011   -10.780 1.00 55.93  ? 44  GLY   B C   1 
ATOM   521  O O   . GLY   B 2 35  ? -33.258 2.866   -9.889  1.00 56.34  ? 44  GLY   B O   1 
ATOM   522  N N   . VAL   B 2 36  ? -32.142 1.258   -11.061 1.00 54.21  ? 45  VAL   B N   1 
ATOM   523  C CA  . VAL   B 2 36  ? -30.882 1.344   -10.327 1.00 52.85  ? 45  VAL   B CA  1 
ATOM   524  C C   . VAL   B 2 36  ? -29.777 1.869   -11.228 1.00 50.67  ? 45  VAL   B C   1 
ATOM   525  O O   . VAL   B 2 36  ? -29.640 1.427   -12.378 1.00 49.89  ? 45  VAL   B O   1 
ATOM   526  C CB  . VAL   B 2 36  ? -30.508 -0.006  -9.646  1.00 53.96  ? 45  VAL   B CB  1 
ATOM   527  C CG1 . VAL   B 2 36  ? -29.143 0.065   -8.955  1.00 54.95  ? 45  VAL   B CG1 1 
ATOM   528  C CG2 . VAL   B 2 36  ? -31.582 -0.424  -8.646  1.00 54.32  ? 45  VAL   B CG2 1 
ATOM   529  N N   . PHE   B 2 37  ? -29.051 2.881   -10.745 1.00 49.12  ? 46  PHE   B N   1 
ATOM   530  C CA  . PHE   B 2 37  ? -27.959 3.446   -11.505 1.00 48.41  ? 46  PHE   B CA  1 
ATOM   531  C C   . PHE   B 2 37  ? -26.666 2.768   -11.045 1.00 47.21  ? 46  PHE   B C   1 
ATOM   532  O O   . PHE   B 2 37  ? -26.389 2.745   -9.866  1.00 45.34  ? 46  PHE   B O   1 
ATOM   533  C CB  . PHE   B 2 37  ? -27.891 4.967   -11.338 1.00 47.85  ? 46  PHE   B CB  1 
ATOM   534  C CG  . PHE   B 2 37  ? -26.930 5.591   -12.322 1.00 47.50  ? 46  PHE   B CG  1 
ATOM   535  C CD1 . PHE   B 2 37  ? -27.156 5.505   -13.685 1.00 47.47  ? 46  PHE   B CD1 1 
ATOM   536  C CD2 . PHE   B 2 37  ? -25.771 6.215   -11.884 1.00 47.76  ? 46  PHE   B CD2 1 
ATOM   537  C CE1 . PHE   B 2 37  ? -26.246 6.035   -14.595 1.00 47.51  ? 46  PHE   B CE1 1 
ATOM   538  C CE2 . PHE   B 2 37  ? -24.870 6.754   -12.795 1.00 47.83  ? 46  PHE   B CE2 1 
ATOM   539  C CZ  . PHE   B 2 37  ? -25.120 6.666   -14.144 1.00 47.34  ? 46  PHE   B CZ  1 
ATOM   540  N N   . HIS   B 2 38  ? -25.877 2.202   -11.990 1.00 47.28  ? 47  HIS   B N   1 
ATOM   541  C CA  . HIS   B 2 38  ? -24.657 1.477   -11.650 1.00 47.71  ? 47  HIS   B CA  1 
ATOM   542  C C   . HIS   B 2 38  ? -23.467 2.211   -12.207 1.00 49.29  ? 47  HIS   B C   1 
ATOM   543  O O   . HIS   B 2 38  ? -23.453 2.506   -13.398 1.00 49.53  ? 47  HIS   B O   1 
ATOM   544  C CB  . HIS   B 2 38  ? -24.676 0.078   -12.271 1.00 47.16  ? 47  HIS   B CB  1 
ATOM   545  C CG  . HIS   B 2 38  ? -25.917 -0.698  -11.983 1.00 49.05  ? 47  HIS   B CG  1 
ATOM   546  N ND1 . HIS   B 2 38  ? -27.139 -0.346  -12.541 1.00 50.04  ? 47  HIS   B ND1 1 
ATOM   547  C CD2 . HIS   B 2 38  ? -26.089 -1.802  -11.213 1.00 49.82  ? 47  HIS   B CD2 1 
ATOM   548  C CE1 . HIS   B 2 38  ? -28.015 -1.226  -12.073 1.00 50.03  ? 47  HIS   B CE1 1 
ATOM   549  N NE2 . HIS   B 2 38  ? -27.429 -2.123  -11.276 1.00 50.61  ? 47  HIS   B NE2 1 
ATOM   550  N N   . THR   B 2 39  ? -22.456 2.494   -11.375 1.00 49.27  ? 48  THR   B N   1 
ATOM   551  C CA  . THR   B 2 39  ? -21.249 3.138   -11.898 1.00 49.91  ? 48  THR   B CA  1 
ATOM   552  C C   . THR   B 2 39  ? -20.010 2.624   -11.106 1.00 49.23  ? 48  THR   B C   1 
ATOM   553  O O   . THR   B 2 39  ? -20.117 1.685   -10.306 1.00 48.66  ? 48  THR   B O   1 
ATOM   554  C CB  . THR   B 2 39  ? -21.432 4.694   -11.999 1.00 51.23  ? 48  THR   B CB  1 
ATOM   555  O OG1 . THR   B 2 39  ? -20.335 5.254   -12.740 1.00 52.26  ? 48  THR   B OG1 1 
ATOM   556  C CG2 . THR   B 2 39  ? -21.557 5.356   -10.651 1.00 51.31  ? 48  THR   B CG2 1 
ATOM   557  N N   . MET   B 2 40  ? -18.832 3.185   -11.392 1.00 48.98  ? 49  MET   B N   1 
ATOM   558  C CA  . MET   B 2 40  ? -17.624 2.831   -10.663 1.00 48.96  ? 49  MET   B CA  1 
ATOM   559  C C   . MET   B 2 40  ? -17.512 3.769   -9.474  1.00 49.74  ? 49  MET   B C   1 
ATOM   560  O O   . MET   B 2 40  ? -17.902 4.939   -9.563  1.00 49.95  ? 49  MET   B O   1 
ATOM   561  C CB  . MET   B 2 40  ? -16.423 2.961   -11.582 1.00 48.97  ? 49  MET   B CB  1 
ATOM   562  C CG  . MET   B 2 40  ? -16.628 2.214   -12.887 1.00 49.94  ? 49  MET   B CG  1 
ATOM   563  S SD  . MET   B 2 40  ? -15.360 0.986   -13.093 1.00 64.32  ? 49  MET   B SD  1 
ATOM   564  C CE  . MET   B 2 40  ? -16.136 -0.392  -12.492 1.00 66.91  ? 49  MET   B CE  1 
ATOM   565  N N   . TRP   B 2 41  ? -16.986 3.271   -8.352  1.00 50.17  ? 50  TRP   B N   1 
ATOM   566  C CA  A TRP   B 2 41  ? -16.850 4.082   -7.154  0.50 51.21  ? 50  TRP   B CA  1 
ATOM   567  C CA  B TRP   B 2 41  ? -16.861 4.089   -7.151  0.50 50.82  ? 50  TRP   B CA  1 
ATOM   568  C C   . TRP   B 2 41  ? -15.979 5.315   -7.367  1.00 52.02  ? 50  TRP   B C   1 
ATOM   569  O O   . TRP   B 2 41  ? -16.284 6.370   -6.811  1.00 53.00  ? 50  TRP   B O   1 
ATOM   570  C CB  A TRP   B 2 41  ? -16.303 3.257   -5.989  0.50 51.46  ? 50  TRP   B CB  1 
ATOM   571  C CB  B TRP   B 2 41  ? -16.372 3.267   -5.946  0.50 50.48  ? 50  TRP   B CB  1 
ATOM   572  C CG  A TRP   B 2 41  ? -16.591 3.886   -4.666  0.50 52.09  ? 50  TRP   B CG  1 
ATOM   573  C CG  B TRP   B 2 41  ? -16.176 4.084   -4.701  0.50 50.40  ? 50  TRP   B CG  1 
ATOM   574  C CD1 A TRP   B 2 41  ? -17.698 3.695   -3.901  0.50 52.88  ? 50  TRP   B CD1 1 
ATOM   575  C CD1 B TRP   B 2 41  ? -15.076 4.812   -4.359  0.50 50.99  ? 50  TRP   B CD1 1 
ATOM   576  C CD2 A TRP   B 2 41  ? -15.792 4.862   -3.982  0.50 52.46  ? 50  TRP   B CD2 1 
ATOM   577  C CD2 B TRP   B 2 41  ? -17.118 4.257   -3.638  0.50 50.17  ? 50  TRP   B CD2 1 
ATOM   578  N NE1 A TRP   B 2 41  ? -17.630 4.472   -2.772  0.50 53.38  ? 50  TRP   B NE1 1 
ATOM   579  N NE1 B TRP   B 2 41  ? -15.294 5.465   -3.168  0.50 51.09  ? 50  TRP   B NE1 1 
ATOM   580  C CE2 A TRP   B 2 41  ? -16.473 5.205   -2.799  0.50 53.11  ? 50  TRP   B CE2 1 
ATOM   581  C CE2 B TRP   B 2 41  ? -16.534 5.128   -2.695  0.50 50.77  ? 50  TRP   B CE2 1 
ATOM   582  C CE3 A TRP   B 2 41  ? -14.548 5.452   -4.234  0.50 53.21  ? 50  TRP   B CE3 1 
ATOM   583  C CE3 B TRP   B 2 41  ? -18.406 3.775   -3.399  0.50 50.83  ? 50  TRP   B CE3 1 
ATOM   584  C CZ2 A TRP   B 2 41  ? -15.960 6.113   -1.878  0.50 54.00  ? 50  TRP   B CZ2 1 
ATOM   585  C CZ2 B TRP   B 2 41  ? -17.183 5.495   -1.513  0.50 51.46  ? 50  TRP   B CZ2 1 
ATOM   586  C CZ3 A TRP   B 2 41  ? -14.063 6.389   -3.341  0.50 54.04  ? 50  TRP   B CZ3 1 
ATOM   587  C CZ3 B TRP   B 2 41  ? -19.052 4.153   -2.236  0.50 51.59  ? 50  TRP   B CZ3 1 
ATOM   588  C CH2 A TRP   B 2 41  ? -14.758 6.698   -2.170  0.50 54.33  ? 50  TRP   B CH2 1 
ATOM   589  C CH2 B TRP   B 2 41  ? -18.439 4.992   -1.303  0.50 51.47  ? 50  TRP   B CH2 1 
ATOM   590  N N   . HIS   B 2 42  ? -14.876 5.185   -8.122  1.00 51.82  ? 51  HIS   B N   1 
ATOM   591  C CA  . HIS   B 2 42  ? -13.967 6.319   -8.286  1.00 52.70  ? 51  HIS   B CA  1 
ATOM   592  C C   . HIS   B 2 42  ? -14.543 7.488   -9.102  1.00 53.55  ? 51  HIS   B C   1 
ATOM   593  O O   . HIS   B 2 42  ? -13.981 8.579   -9.040  1.00 53.73  ? 51  HIS   B O   1 
ATOM   594  C CB  . HIS   B 2 42  ? -12.601 5.885   -8.818  1.00 53.08  ? 51  HIS   B CB  1 
ATOM   595  C CG  . HIS   B 2 42  ? -12.566 5.560   -10.277 1.00 53.97  ? 51  HIS   B CG  1 
ATOM   596  N ND1 . HIS   B 2 42  ? -12.675 4.256   -10.725 1.00 55.82  ? 51  HIS   B ND1 1 
ATOM   597  C CD2 . HIS   B 2 42  ? -12.391 6.376   -11.342 1.00 54.35  ? 51  HIS   B CD2 1 
ATOM   598  C CE1 . HIS   B 2 42  ? -12.540 4.317   -12.041 1.00 55.56  ? 51  HIS   B CE1 1 
ATOM   599  N NE2 . HIS   B 2 42  ? -12.399 5.577   -12.454 1.00 55.28  ? 51  HIS   B NE2 1 
ATOM   600  N N   . VAL   B 2 43  ? -15.678 7.285   -9.813  1.00 53.31  ? 52  VAL   B N   1 
ATOM   601  C CA  . VAL   B 2 43  ? -16.319 8.347   -10.579 1.00 53.28  ? 52  VAL   B CA  1 
ATOM   602  C C   . VAL   B 2 43  ? -17.038 9.335   -9.643  1.00 54.15  ? 52  VAL   B C   1 
ATOM   603  O O   . VAL   B 2 43  ? -16.840 10.543  -9.750  1.00 54.71  ? 52  VAL   B O   1 
ATOM   604  C CB  . VAL   B 2 43  ? -17.291 7.732   -11.620 1.00 53.81  ? 52  VAL   B CB  1 
ATOM   605  C CG1 . VAL   B 2 43  ? -18.231 8.789   -12.217 1.00 54.26  ? 52  VAL   B CG1 1 
ATOM   606  C CG2 . VAL   B 2 43  ? -16.525 6.988   -12.719 1.00 53.80  ? 52  VAL   B CG2 1 
ATOM   607  N N   . THR   B 2 44  ? -17.868 8.812   -8.714  1.00 53.49  ? 53  THR   B N   1 
ATOM   608  C CA  . THR   B 2 44  ? -18.669 9.635   -7.820  1.00 53.78  ? 53  THR   B CA  1 
ATOM   609  C C   . THR   B 2 44  ? -18.100 9.772   -6.411  1.00 54.96  ? 53  THR   B C   1 
ATOM   610  O O   . THR   B 2 44  ? -18.516 10.670  -5.688  1.00 55.35  ? 53  THR   B O   1 
ATOM   611  C CB  . THR   B 2 44  ? -20.110 9.081   -7.748  1.00 54.11  ? 53  THR   B CB  1 
ATOM   612  O OG1 . THR   B 2 44  ? -20.136 7.895   -6.952  1.00 54.80  ? 53  THR   B OG1 1 
ATOM   613  C CG2 . THR   B 2 44  ? -20.702 8.750   -9.131  1.00 54.88  ? 53  THR   B CG2 1 
ATOM   614  N N   . LYS   B 2 45  ? -17.186 8.886   -6.002  1.00 55.55  ? 54  LYS   B N   1 
ATOM   615  C CA  . LYS   B 2 45  ? -16.690 8.822   -4.614  1.00 57.40  ? 54  LYS   B CA  1 
ATOM   616  C C   . LYS   B 2 45  ? -17.859 8.575   -3.611  1.00 57.98  ? 54  LYS   B C   1 
ATOM   617  O O   . LYS   B 2 45  ? -17.742 8.912   -2.427  1.00 58.26  ? 54  LYS   B O   1 
ATOM   618  C CB  . LYS   B 2 45  ? -15.896 10.083  -4.204  1.00 60.41  ? 54  LYS   B CB  1 
ATOM   619  C CG  . LYS   B 2 45  ? -14.787 10.494  -5.156  1.00 66.56  ? 54  LYS   B CG  1 
ATOM   620  C CD  . LYS   B 2 45  ? -13.693 9.452   -5.261  1.00 73.74  ? 54  LYS   B CD  1 
ATOM   621  C CE  . LYS   B 2 45  ? -12.631 9.942   -6.227  1.00 80.81  ? 54  LYS   B CE  1 
ATOM   622  N NZ  . LYS   B 2 45  ? -11.955 8.817   -6.940  1.00 85.19  ? 54  LYS   B NZ  1 
ATOM   623  N N   . GLY   B 2 46  ? -18.975 8.019   -4.086  1.00 57.93  ? 55  GLY   B N   1 
ATOM   624  C CA  . GLY   B 2 46  ? -20.135 7.783   -3.236  1.00 58.44  ? 55  GLY   B CA  1 
ATOM   625  C C   . GLY   B 2 46  ? -21.059 8.978   -3.074  1.00 59.14  ? 55  GLY   B C   1 
ATOM   626  O O   . GLY   B 2 46  ? -22.016 8.910   -2.311  1.00 59.74  ? 55  GLY   B O   1 
ATOM   627  N N   . ALA   B 2 47  ? -20.801 10.085  -3.784  1.00 59.12  ? 56  ALA   B N   1 
ATOM   628  C CA  . ALA   B 2 47  ? -21.632 11.302  -3.703  1.00 59.13  ? 56  ALA   B CA  1 
ATOM   629  C C   . ALA   B 2 47  ? -23.012 11.126  -4.337  1.00 59.05  ? 56  ALA   B C   1 
ATOM   630  O O   . ALA   B 2 47  ? -23.162 10.336  -5.257  1.00 59.06  ? 56  ALA   B O   1 
ATOM   631  C CB  . ALA   B 2 47  ? -20.914 12.462  -4.395  1.00 58.92  ? 56  ALA   B CB  1 
ATOM   632  N N   . ALA   B 2 48  ? -23.991 11.931  -3.917  1.00 59.17  ? 57  ALA   B N   1 
ATOM   633  C CA  . ALA   B 2 48  ? -25.323 11.904  -4.511  1.00 59.70  ? 57  ALA   B CA  1 
ATOM   634  C C   . ALA   B 2 48  ? -25.301 12.468  -5.936  1.00 60.15  ? 57  ALA   B C   1 
ATOM   635  O O   . ALA   B 2 48  ? -24.430 13.261  -6.281  1.00 60.10  ? 57  ALA   B O   1 
ATOM   636  C CB  . ALA   B 2 48  ? -26.295 12.693  -3.655  1.00 59.90  ? 57  ALA   B CB  1 
ATOM   637  N N   . LEU   B 2 49  ? -26.258 12.057  -6.759  1.00 60.77  ? 58  LEU   B N   1 
ATOM   638  C CA  . LEU   B 2 49  ? -26.329 12.506  -8.148  1.00 62.78  ? 58  LEU   B CA  1 
ATOM   639  C C   . LEU   B 2 49  ? -27.659 13.175  -8.442  1.00 65.77  ? 58  LEU   B C   1 
ATOM   640  O O   . LEU   B 2 49  ? -28.666 12.873  -7.816  1.00 66.63  ? 58  LEU   B O   1 
ATOM   641  C CB  . LEU   B 2 49  ? -26.113 11.325  -9.113  1.00 62.37  ? 58  LEU   B CB  1 
ATOM   642  C CG  . LEU   B 2 49  ? -24.895 10.465  -8.837  1.00 63.54  ? 58  LEU   B CG  1 
ATOM   643  C CD1 . LEU   B 2 49  ? -24.891 9.217   -9.708  1.00 64.42  ? 58  LEU   B CD1 1 
ATOM   644  C CD2 . LEU   B 2 49  ? -23.629 11.246  -9.018  1.00 64.01  ? 58  LEU   B CD2 1 
ATOM   645  N N   . ARG   B 2 50  ? -27.665 14.086  -9.381  1.00 67.60  ? 59  ARG   B N   1 
ATOM   646  C CA  . ARG   B 2 50  ? -28.867 14.800  -9.783  1.00 70.02  ? 59  ARG   B CA  1 
ATOM   647  C C   . ARG   B 2 50  ? -29.353 14.235  -11.134 1.00 71.20  ? 59  ARG   B C   1 
ATOM   648  O O   . ARG   B 2 50  ? -28.540 13.817  -11.945 1.00 70.66  ? 59  ARG   B O   1 
ATOM   649  C CB  . ARG   B 2 50  ? -28.510 16.296  -9.890  1.00 72.98  ? 59  ARG   B CB  1 
ATOM   650  C CG  . ARG   B 2 50  ? -29.633 17.192  -10.356 1.00 79.47  ? 59  ARG   B CG  1 
ATOM   651  C CD  . ARG   B 2 50  ? -29.345 18.695  -10.198 1.00 84.26  ? 59  ARG   B CD  1 
ATOM   652  N NE  . ARG   B 2 50  ? -28.253 19.196  -11.049 1.00 88.02  ? 59  ARG   B NE  1 
ATOM   653  C CZ  . ARG   B 2 50  ? -28.363 19.439  -12.355 1.00 89.91  ? 59  ARG   B CZ  1 
ATOM   654  N NH1 . ARG   B 2 50  ? -29.498 19.173  -12.994 1.00 88.45  ? 59  ARG   B NH1 1 
ATOM   655  N NH2 . ARG   B 2 50  ? -27.329 19.916  -13.037 1.00 90.21  ? 59  ARG   B NH2 1 
ATOM   656  N N   . SER   B 2 51  ? -30.662 14.172  -11.357 1.00 72.70  ? 60  SER   B N   1 
ATOM   657  C CA  . SER   B 2 51  ? -31.222 13.743  -12.643 1.00 74.86  ? 60  SER   B CA  1 
ATOM   658  C C   . SER   B 2 51  ? -32.401 14.680  -12.954 1.00 77.90  ? 60  SER   B C   1 
ATOM   659  O O   . SER   B 2 51  ? -33.570 14.310  -12.798 1.00 78.75  ? 60  SER   B O   1 
ATOM   660  C CB  . SER   B 2 51  ? -31.683 12.295  -12.591 1.00 75.28  ? 60  SER   B CB  1 
ATOM   661  O OG  . SER   B 2 51  ? -32.186 11.918  -13.861 1.00 76.56  ? 60  SER   B OG  1 
ATOM   662  N N   . GLY   B 2 52  ? -32.074 15.909  -13.338 1.00 78.84  ? 61  GLY   B N   1 
ATOM   663  C CA  . GLY   B 2 52  ? -33.065 16.946  -13.544 1.00 79.88  ? 61  GLY   B CA  1 
ATOM   664  C C   . GLY   B 2 52  ? -33.370 17.487  -12.167 1.00 81.32  ? 61  GLY   B C   1 
ATOM   665  O O   . GLY   B 2 52  ? -32.443 17.843  -11.434 1.00 81.96  ? 61  GLY   B O   1 
ATOM   666  N N   . GLU   B 2 53  ? -34.648 17.493  -11.764 1.00 81.37  ? 62  GLU   B N   1 
ATOM   667  C CA  . GLU   B 2 53  ? -35.011 17.917  -10.408 1.00 81.35  ? 62  GLU   B CA  1 
ATOM   668  C C   . GLU   B 2 53  ? -34.730 16.801  -9.367  1.00 80.50  ? 62  GLU   B C   1 
ATOM   669  O O   . GLU   B 2 53  ? -34.469 17.104  -8.199  1.00 80.89  ? 62  GLU   B O   1 
ATOM   670  C CB  . GLU   B 2 53  ? -36.490 18.305  -10.340 1.00 84.38  ? 62  GLU   B CB  1 
ATOM   671  C CG  . GLU   B 2 53  ? -36.778 19.744  -10.717 1.00 90.94  ? 62  GLU   B CG  1 
ATOM   672  C CD  . GLU   B 2 53  ? -38.216 20.161  -10.455 1.00 98.87  ? 62  GLU   B CD  1 
ATOM   673  O OE1 . GLU   B 2 53  ? -39.007 20.211  -11.427 1.00 100.32 ? 62  GLU   B OE1 1 
ATOM   674  O OE2 . GLU   B 2 53  ? -38.554 20.432  -9.278  1.00 100.71 ? 62  GLU   B OE2 1 
ATOM   675  N N   . GLY   B 2 54  ? -34.797 15.538  -9.798  1.00 78.96  ? 63  GLY   B N   1 
ATOM   676  C CA  . GLY   B 2 54  ? -34.629 14.375  -8.934  1.00 77.81  ? 63  GLY   B CA  1 
ATOM   677  C C   . GLY   B 2 54  ? -33.247 14.117  -8.368  1.00 76.24  ? 63  GLY   B C   1 
ATOM   678  O O   . GLY   B 2 54  ? -32.236 14.470  -8.973  1.00 76.82  ? 63  GLY   B O   1 
ATOM   679  N N   . ARG   B 2 55  ? -33.196 13.470  -7.204  1.00 73.86  ? 64  ARG   B N   1 
ATOM   680  C CA  . ARG   B 2 55  ? -31.944 13.120  -6.547  1.00 72.17  ? 64  ARG   B CA  1 
ATOM   681  C C   . ARG   B 2 55  ? -31.778 11.597  -6.541  1.00 69.68  ? 64  ARG   B C   1 
ATOM   682  O O   . ARG   B 2 55  ? -32.752 10.864  -6.352  1.00 70.19  ? 64  ARG   B O   1 
ATOM   683  C CB  . ARG   B 2 55  ? -31.957 13.650  -5.105  1.00 73.89  ? 64  ARG   B CB  1 
ATOM   684  C CG  . ARG   B 2 55  ? -30.649 13.500  -4.343  1.00 77.57  ? 64  ARG   B CG  1 
ATOM   685  C CD  . ARG   B 2 55  ? -30.792 14.069  -2.939  1.00 80.85  ? 64  ARG   B CD  1 
ATOM   686  N NE  . ARG   B 2 55  ? -29.637 13.766  -2.095  1.00 84.77  ? 64  ARG   B NE  1 
ATOM   687  C CZ  . ARG   B 2 55  ? -28.873 14.684  -1.506  1.00 88.44  ? 64  ARG   B CZ  1 
ATOM   688  N NH1 . ARG   B 2 55  ? -29.138 15.977  -1.657  1.00 89.08  ? 64  ARG   B NH1 1 
ATOM   689  N NH2 . ARG   B 2 55  ? -27.850 14.314  -0.744  1.00 88.30  ? 64  ARG   B NH2 1 
ATOM   690  N N   . LEU   B 2 56  ? -30.560 11.120  -6.779  1.00 66.51  ? 65  LEU   B N   1 
ATOM   691  C CA  . LEU   B 2 56  ? -30.253 9.705   -6.717  1.00 64.41  ? 65  LEU   B CA  1 
ATOM   692  C C   . LEU   B 2 56  ? -29.329 9.559   -5.520  1.00 62.39  ? 65  LEU   B C   1 
ATOM   693  O O   . LEU   B 2 56  ? -28.263 10.182  -5.507  1.00 62.48  ? 65  LEU   B O   1 
ATOM   694  C CB  . LEU   B 2 56  ? -29.471 9.227   -7.959  1.00 64.45  ? 65  LEU   B CB  1 
ATOM   695  C CG  . LEU   B 2 56  ? -30.060 9.389   -9.349  1.00 65.60  ? 65  LEU   B CG  1 
ATOM   696  C CD1 . LEU   B 2 56  ? -29.206 8.654   -10.359 1.00 66.17  ? 65  LEU   B CD1 1 
ATOM   697  C CD2 . LEU   B 2 56  ? -31.472 8.866   -9.424  1.00 66.10  ? 65  LEU   B CD2 1 
ATOM   698  N N   . ASP   B 2 57  ? -29.708 8.756   -4.527  1.00 60.47  ? 66  ASP   B N   1 
ATOM   699  C CA  . ASP   B 2 57  ? -28.840 8.538   -3.373  1.00 60.05  ? 66  ASP   B CA  1 
ATOM   700  C C   . ASP   B 2 57  ? -28.111 7.191   -3.471  1.00 57.88  ? 66  ASP   B C   1 
ATOM   701  O O   . ASP   B 2 57  ? -28.667 6.229   -4.001  1.00 57.48  ? 66  ASP   B O   1 
ATOM   702  C CB  . ASP   B 2 57  ? -29.635 8.637   -2.067  1.00 64.06  ? 66  ASP   B CB  1 
ATOM   703  C CG  . ASP   B 2 57  ? -30.163 10.028  -1.820  1.00 72.72  ? 66  ASP   B CG  1 
ATOM   704  O OD1 . ASP   B 2 57  ? -29.383 10.993  -1.968  1.00 73.91  ? 66  ASP   B OD1 1 
ATOM   705  O OD2 . ASP   B 2 57  ? -31.357 10.156  -1.495  1.00 77.42  ? 66  ASP   B OD2 1 
ATOM   706  N N   . PRO   B 2 58  ? -26.847 7.109   -3.010  1.00 56.47  ? 67  PRO   B N   1 
ATOM   707  C CA  . PRO   B 2 58  ? -26.135 5.817   -3.060  1.00 55.70  ? 67  PRO   B CA  1 
ATOM   708  C C   . PRO   B 2 58  ? -26.826 4.752   -2.191  1.00 54.48  ? 67  PRO   B C   1 
ATOM   709  O O   . PRO   B 2 58  ? -27.478 5.087   -1.222  1.00 54.67  ? 67  PRO   B O   1 
ATOM   710  C CB  . PRO   B 2 58  ? -24.736 6.171   -2.536  1.00 56.51  ? 67  PRO   B CB  1 
ATOM   711  C CG  . PRO   B 2 58  ? -24.954 7.357   -1.659  1.00 57.04  ? 67  PRO   B CG  1 
ATOM   712  C CD  . PRO   B 2 58  ? -26.038 8.149   -2.341  1.00 55.69  ? 67  PRO   B CD  1 
ATOM   713  N N   . TYR   B 2 59  ? -26.728 3.474   -2.564  1.00 53.16  ? 68  TYR   B N   1 
ATOM   714  C CA  . TYR   B 2 59  ? -27.389 2.393   -1.838  1.00 52.24  ? 68  TYR   B CA  1 
ATOM   715  C C   . TYR   B 2 59  ? -26.359 1.349   -1.405  1.00 51.60  ? 68  TYR   B C   1 
ATOM   716  O O   . TYR   B 2 59  ? -26.403 0.888   -0.285  1.00 51.85  ? 68  TYR   B O   1 
ATOM   717  C CB  . TYR   B 2 59  ? -28.477 1.767   -2.734  1.00 51.57  ? 68  TYR   B CB  1 
ATOM   718  C CG  . TYR   B 2 59  ? -29.260 0.637   -2.102  1.00 50.82  ? 68  TYR   B CG  1 
ATOM   719  C CD1 . TYR   B 2 59  ? -28.723 -0.640  -2.009  1.00 50.77  ? 68  TYR   B CD1 1 
ATOM   720  C CD2 . TYR   B 2 59  ? -30.570 0.823   -1.681  1.00 51.06  ? 68  TYR   B CD2 1 
ATOM   721  C CE1 . TYR   B 2 59  ? -29.436 -1.683  -1.438  1.00 51.41  ? 68  TYR   B CE1 1 
ATOM   722  C CE2 . TYR   B 2 59  ? -31.309 -0.225  -1.149  1.00 51.65  ? 68  TYR   B CE2 1 
ATOM   723  C CZ  . TYR   B 2 59  ? -30.746 -1.486  -1.058  1.00 52.60  ? 68  TYR   B CZ  1 
ATOM   724  O OH  . TYR   B 2 59  ? -31.462 -2.532  -0.532  1.00 54.60  ? 68  TYR   B OH  1 
ATOM   725  N N   . TRP   B 2 60  ? -25.455 0.971   -2.290  1.00 50.74  ? 69  TRP   B N   1 
ATOM   726  C CA  . TRP   B 2 60  ? -24.397 0.013   -1.987  1.00 50.27  ? 69  TRP   B CA  1 
ATOM   727  C C   . TRP   B 2 60  ? -23.114 0.496   -2.698  1.00 51.23  ? 69  TRP   B C   1 
ATOM   728  O O   . TRP   B 2 60  ? -23.175 1.044   -3.801  1.00 50.83  ? 69  TRP   B O   1 
ATOM   729  C CB  . TRP   B 2 60  ? -24.773 -1.421  -2.467  1.00 49.23  ? 69  TRP   B CB  1 
ATOM   730  C CG  . TRP   B 2 60  ? -23.613 -2.388  -2.450  1.00 49.34  ? 69  TRP   B CG  1 
ATOM   731  C CD1 . TRP   B 2 60  ? -23.141 -3.087  -1.368  1.00 50.30  ? 69  TRP   B CD1 1 
ATOM   732  C CD2 . TRP   B 2 60  ? -22.706 -2.670  -3.539  1.00 48.76  ? 69  TRP   B CD2 1 
ATOM   733  N NE1 . TRP   B 2 60  ? -22.032 -3.829  -1.734  1.00 50.15  ? 69  TRP   B NE1 1 
ATOM   734  C CE2 . TRP   B 2 60  ? -21.720 -3.550  -3.048  1.00 49.33  ? 69  TRP   B CE2 1 
ATOM   735  C CE3 . TRP   B 2 60  ? -22.622 -2.236  -4.874  1.00 49.33  ? 69  TRP   B CE3 1 
ATOM   736  C CZ2 . TRP   B 2 60  ? -20.659 -3.991  -3.836  1.00 49.88  ? 69  TRP   B CZ2 1 
ATOM   737  C CZ3 . TRP   B 2 60  ? -21.580 -2.686  -5.663  1.00 49.97  ? 69  TRP   B CZ3 1 
ATOM   738  C CH2 . TRP   B 2 60  ? -20.618 -3.561  -5.153  1.00 50.15  ? 69  TRP   B CH2 1 
ATOM   739  N N   . GLY   B 2 61  ? -21.971 0.198   -2.107  1.00 51.61  ? 70  GLY   B N   1 
ATOM   740  C CA  . GLY   B 2 61  ? -20.683 0.525   -2.705  1.00 51.84  ? 70  GLY   B CA  1 
ATOM   741  C C   . GLY   B 2 61  ? -19.546 -0.217  -2.040  1.00 51.19  ? 70  GLY   B C   1 
ATOM   742  O O   . GLY   B 2 61  ? -19.668 -0.632  -0.890  1.00 51.94  ? 70  GLY   B O   1 
ATOM   743  N N   . ASP   B 2 62  ? -18.431 -0.346  -2.723  1.00 50.26  ? 71  ASP   B N   1 
ATOM   744  C CA  . ASP   B 2 62  ? -17.265 -1.055  -2.221  1.00 50.54  ? 71  ASP   B CA  1 
ATOM   745  C C   . ASP   B 2 62  ? -16.028 -0.483  -2.940  1.00 50.35  ? 71  ASP   B C   1 
ATOM   746  O O   . ASP   B 2 62  ? -15.976 -0.516  -4.157  1.00 48.83  ? 71  ASP   B O   1 
ATOM   747  C CB  . ASP   B 2 62  ? -17.413 -2.562  -2.526  1.00 52.68  ? 71  ASP   B CB  1 
ATOM   748  C CG  . ASP   B 2 62  ? -16.414 -3.465  -1.818  1.00 59.25  ? 71  ASP   B CG  1 
ATOM   749  O OD1 . ASP   B 2 62  ? -15.231 -3.432  -2.179  1.00 62.32  ? 71  ASP   B OD1 1 
ATOM   750  O OD2 . ASP   B 2 62  ? -16.833 -4.246  -0.942  1.00 61.23  ? 71  ASP   B OD2 1 
ATOM   751  N N   . VAL   B 2 63  ? -15.042 0.038   -2.190  1.00 51.05  ? 72  VAL   B N   1 
ATOM   752  C CA  . VAL   B 2 63  ? -13.845 0.611   -2.799  1.00 51.56  ? 72  VAL   B CA  1 
ATOM   753  C C   . VAL   B 2 63  ? -12.974 -0.475  -3.455  1.00 52.83  ? 72  VAL   B C   1 
ATOM   754  O O   . VAL   B 2 63  ? -12.375 -0.203  -4.492  1.00 54.11  ? 72  VAL   B O   1 
ATOM   755  C CB  . VAL   B 2 63  ? -13.067 1.506   -1.794  1.00 51.72  ? 72  VAL   B CB  1 
ATOM   756  C CG1 . VAL   B 2 63  ? -11.585 1.627   -2.145  1.00 52.17  ? 72  VAL   B CG1 1 
ATOM   757  C CG2 . VAL   B 2 63  ? -13.706 2.879   -1.685  1.00 51.85  ? 72  VAL   B CG2 1 
ATOM   758  N N   . LYS   B 2 64  ? -12.952 -1.705  -2.915  1.00 52.66  ? 73  LYS   B N   1 
ATOM   759  C CA  . LYS   B 2 64  ? -12.105 -2.749  -3.496  1.00 52.58  ? 73  LYS   B CA  1 
ATOM   760  C C   . LYS   B 2 64  ? -12.637 -3.212  -4.829  1.00 51.98  ? 73  LYS   B C   1 
ATOM   761  O O   . LYS   B 2 64  ? -11.879 -3.353  -5.783  1.00 51.49  ? 73  LYS   B O   1 
ATOM   762  C CB  . LYS   B 2 64  ? -11.865 -3.917  -2.521  1.00 53.93  ? 73  LYS   B CB  1 
ATOM   763  C CG  . LYS   B 2 64  ? -10.787 -4.861  -3.054  1.00 58.14  ? 73  LYS   B CG  1 
ATOM   764  C CD  . LYS   B 2 64  ? -10.350 -5.864  -2.000  1.00 64.02  ? 73  LYS   B CD  1 
ATOM   765  C CE  . LYS   B 2 64  ? -9.604  -6.970  -2.686  1.00 68.96  ? 73  LYS   B CE  1 
ATOM   766  N NZ  . LYS   B 2 64  ? -9.353  -8.108  -1.772  1.00 71.40  ? 73  LYS   B NZ  1 
ATOM   767  N N   . GLN   B 2 65  ? -13.949 -3.416  -4.910  1.00 52.04  ? 74  GLN   B N   1 
ATOM   768  C CA  . GLN   B 2 65  ? -14.585 -3.787  -6.180  1.00 52.17  ? 74  GLN   B CA  1 
ATOM   769  C C   . GLN   B 2 65  ? -14.637 -2.601  -7.143  1.00 52.26  ? 74  GLN   B C   1 
ATOM   770  O O   . GLN   B 2 65  ? -14.787 -2.804  -8.346  1.00 53.14  ? 74  GLN   B O   1 
ATOM   771  C CB  . GLN   B 2 65  ? -16.014 -4.283  -5.939  1.00 53.90  ? 74  GLN   B CB  1 
ATOM   772  C CG  . GLN   B 2 65  ? -16.089 -5.546  -5.095  1.00 59.07  ? 74  GLN   B CG  1 
ATOM   773  C CD  . GLN   B 2 65  ? -17.520 -6.042  -5.006  1.00 67.14  ? 74  GLN   B CD  1 
ATOM   774  O OE1 . GLN   B 2 65  ? -18.239 -6.151  -6.027  1.00 68.67  ? 74  GLN   B OE1 1 
ATOM   775  N NE2 . GLN   B 2 65  ? -17.964 -6.362  -3.780  1.00 69.01  ? 74  GLN   B NE2 1 
ATOM   776  N N   . ASP   B 2 66  ? -14.590 -1.365  -6.605  1.00 51.55  ? 75  ASP   B N   1 
ATOM   777  C CA  . ASP   B 2 66  ? -14.664 -0.115  -7.339  1.00 50.66  ? 75  ASP   B CA  1 
ATOM   778  C C   . ASP   B 2 66  ? -16.011 -0.011  -8.015  1.00 48.62  ? 75  ASP   B C   1 
ATOM   779  O O   . ASP   B 2 66  ? -16.082 0.405   -9.156  1.00 47.87  ? 75  ASP   B O   1 
ATOM   780  C CB  . ASP   B 2 66  ? -13.493 0.038   -8.354  1.00 51.54  ? 75  ASP   B CB  1 
ATOM   781  C CG  . ASP   B 2 66  ? -13.379 1.447   -8.900  1.00 54.77  ? 75  ASP   B CG  1 
ATOM   782  O OD1 . ASP   B 2 66  ? -13.665 2.394   -8.144  1.00 56.61  ? 75  ASP   B OD1 1 
ATOM   783  O OD2 . ASP   B 2 66  ? -13.014 1.602   -10.099 1.00 54.78  ? 75  ASP   B OD2 1 
ATOM   784  N N   . LEU   B 2 67  ? -17.092 -0.346  -7.298  1.00 47.75  ? 76  LEU   B N   1 
ATOM   785  C CA  . LEU   B 2 67  ? -18.461 -0.240  -7.821  1.00 47.08  ? 76  LEU   B CA  1 
ATOM   786  C C   . LEU   B 2 67  ? -19.375 0.502   -6.835  1.00 47.48  ? 76  LEU   B C   1 
ATOM   787  O O   . LEU   B 2 67  ? -19.141 0.490   -5.620  1.00 46.97  ? 76  LEU   B O   1 
ATOM   788  C CB  . LEU   B 2 67  ? -19.055 -1.631  -8.053  1.00 46.72  ? 76  LEU   B CB  1 
ATOM   789  C CG  . LEU   B 2 67  ? -18.425 -2.456  -9.149  1.00 47.79  ? 76  LEU   B CG  1 
ATOM   790  C CD1 . LEU   B 2 67  ? -19.015 -3.844  -9.163  1.00 48.13  ? 76  LEU   B CD1 1 
ATOM   791  C CD2 . LEU   B 2 67  ? -18.583 -1.770  -10.524 1.00 48.04  ? 76  LEU   B CD2 1 
ATOM   792  N N   . VAL   B 2 68  ? -20.459 1.083   -7.353  1.00 47.27  ? 77  VAL   B N   1 
ATOM   793  C CA  . VAL   B 2 68  ? -21.466 1.736   -6.516  1.00 46.88  ? 77  VAL   B CA  1 
ATOM   794  C C   . VAL   B 2 68  ? -22.836 1.669   -7.255  1.00 46.40  ? 77  VAL   B C   1 
ATOM   795  O O   . VAL   B 2 68  ? -22.874 1.722   -8.470  1.00 45.16  ? 77  VAL   B O   1 
ATOM   796  C CB  . VAL   B 2 68  ? -21.048 3.193   -6.154  1.00 46.61  ? 77  VAL   B CB  1 
ATOM   797  C CG1 . VAL   B 2 68  ? -20.901 4.050   -7.413  1.00 46.80  ? 77  VAL   B CG1 1 
ATOM   798  C CG2 . VAL   B 2 68  ? -22.015 3.831   -5.181  1.00 45.83  ? 77  VAL   B CG2 1 
ATOM   799  N N   . SER   B 2 69  ? -23.938 1.527   -6.516  1.00 46.87  ? 78  SER   B N   1 
ATOM   800  C CA  . SER   B 2 69  ? -25.292 1.488   -7.075  1.00 47.78  ? 78  SER   B CA  1 
ATOM   801  C C   . SER   B 2 69  ? -26.157 2.579   -6.400  1.00 49.16  ? 78  SER   B C   1 
ATOM   802  O O   . SER   B 2 69  ? -25.930 2.934   -5.244  1.00 49.20  ? 78  SER   B O   1 
ATOM   803  C CB  . SER   B 2 69  ? -25.915 0.099   -6.917  1.00 48.14  ? 78  SER   B CB  1 
ATOM   804  O OG  . SER   B 2 69  ? -26.286 -0.165  -5.569  1.00 49.40  ? 78  SER   B OG  1 
ATOM   805  N N   . TYR   B 2 70  ? -27.120 3.136   -7.138  1.00 49.71  ? 79  TYR   B N   1 
ATOM   806  C CA  . TYR   B 2 70  ? -27.971 4.227   -6.655  1.00 50.52  ? 79  TYR   B CA  1 
ATOM   807  C C   . TYR   B 2 70  ? -29.422 3.795   -6.756  1.00 51.71  ? 79  TYR   B C   1 
ATOM   808  O O   . TYR   B 2 70  ? -29.814 3.193   -7.769  1.00 51.81  ? 79  TYR   B O   1 
ATOM   809  C CB  . TYR   B 2 70  ? -27.760 5.511   -7.518  1.00 50.41  ? 79  TYR   B CB  1 
ATOM   810  C CG  . TYR   B 2 70  ? -26.447 6.197   -7.226  1.00 50.96  ? 79  TYR   B CG  1 
ATOM   811  C CD1 . TYR   B 2 70  ? -25.249 5.698   -7.733  1.00 51.86  ? 79  TYR   B CD1 1 
ATOM   812  C CD2 . TYR   B 2 70  ? -26.391 7.313   -6.403  1.00 51.69  ? 79  TYR   B CD2 1 
ATOM   813  C CE1 . TYR   B 2 70  ? -24.030 6.293   -7.427  1.00 52.86  ? 79  TYR   B CE1 1 
ATOM   814  C CE2 . TYR   B 2 70  ? -25.178 7.903   -6.067  1.00 52.67  ? 79  TYR   B CE2 1 
ATOM   815  C CZ  . TYR   B 2 70  ? -23.997 7.384   -6.576  1.00 54.11  ? 79  TYR   B CZ  1 
ATOM   816  O OH  . TYR   B 2 70  ? -22.793 7.960   -6.252  1.00 55.60  ? 79  TYR   B OH  1 
ATOM   817  N N   . CYS   B 2 71  ? -30.213 4.121   -5.715  1.00 52.01  ? 80  CYS   B N   1 
ATOM   818  C CA  . CYS   B 2 71  ? -31.659 3.842   -5.606  1.00 53.79  ? 80  CYS   B CA  1 
ATOM   819  C C   . CYS   B 2 71  ? -32.001 2.386   -5.291  1.00 53.40  ? 80  CYS   B C   1 
ATOM   820  O O   . CYS   B 2 71  ? -33.159 2.101   -4.964  1.00 53.92  ? 80  CYS   B O   1 
ATOM   821  C CB  . CYS   B 2 71  ? -32.436 4.329   -6.826  1.00 56.17  ? 80  CYS   B CB  1 
ATOM   822  S SG  . CYS   B 2 71  ? -31.929 5.961   -7.420  1.00 63.50  ? 80  CYS   B SG  1 
ATOM   823  N N   . GLY   B 2 72  ? -31.026 1.488   -5.382  1.00 52.14  ? 81  GLY   B N   1 
ATOM   824  C CA  . GLY   B 2 72  ? -31.289 0.093   -5.083  1.00 51.63  ? 81  GLY   B CA  1 
ATOM   825  C C   . GLY   B 2 72  ? -30.076 -0.786  -5.197  1.00 50.50  ? 81  GLY   B C   1 
ATOM   826  O O   . GLY   B 2 72  ? -28.970 -0.329  -5.506  1.00 50.04  ? 81  GLY   B O   1 
ATOM   827  N N   . PRO   B 2 73  ? -30.276 -2.068  -4.888  1.00 49.71  ? 82  PRO   B N   1 
ATOM   828  C CA  . PRO   B 2 73  ? -29.156 -3.009  -4.974  1.00 49.99  ? 82  PRO   B CA  1 
ATOM   829  C C   . PRO   B 2 73  ? -28.688 -3.239  -6.403  1.00 50.94  ? 82  PRO   B C   1 
ATOM   830  O O   . PRO   B 2 73  ? -29.471 -3.071  -7.359  1.00 51.57  ? 82  PRO   B O   1 
ATOM   831  C CB  . PRO   B 2 73  ? -29.728 -4.301  -4.379  1.00 50.57  ? 82  PRO   B CB  1 
ATOM   832  C CG  . PRO   B 2 73  ? -31.210 -4.190  -4.575  1.00 50.74  ? 82  PRO   B CG  1 
ATOM   833  C CD  . PRO   B 2 73  ? -31.532 -2.724  -4.467  1.00 48.71  ? 82  PRO   B CD  1 
ATOM   834  N N   . TRP   B 2 74  ? -27.420 -3.691  -6.546  1.00 50.96  ? 83  TRP   B N   1 
ATOM   835  C CA  . TRP   B 2 74  ? -26.790 -4.023  -7.818  1.00 51.49  ? 83  TRP   B CA  1 
ATOM   836  C C   . TRP   B 2 74  ? -27.660 -5.041  -8.581  1.00 52.57  ? 83  TRP   B C   1 
ATOM   837  O O   . TRP   B 2 74  ? -28.066 -6.040  -8.005  1.00 52.60  ? 83  TRP   B O   1 
ATOM   838  C CB  . TRP   B 2 74  ? -25.363 -4.552  -7.580  1.00 50.99  ? 83  TRP   B CB  1 
ATOM   839  C CG  . TRP   B 2 74  ? -24.564 -4.719  -8.834  1.00 50.44  ? 83  TRP   B CG  1 
ATOM   840  C CD1 . TRP   B 2 74  ? -24.489 -5.837  -9.607  1.00 50.75  ? 83  TRP   B CD1 1 
ATOM   841  C CD2 . TRP   B 2 74  ? -23.732 -3.735  -9.470  1.00 50.06  ? 83  TRP   B CD2 1 
ATOM   842  N NE1 . TRP   B 2 74  ? -23.666 -5.613  -10.680 1.00 50.94  ? 83  TRP   B NE1 1 
ATOM   843  C CE2 . TRP   B 2 74  ? -23.206 -4.323  -10.636 1.00 50.38  ? 83  TRP   B CE2 1 
ATOM   844  C CE3 . TRP   B 2 74  ? -23.358 -2.421  -9.153  1.00 49.92  ? 83  TRP   B CE3 1 
ATOM   845  C CZ2 . TRP   B 2 74  ? -22.359 -3.632  -11.507 1.00 50.58  ? 83  TRP   B CZ2 1 
ATOM   846  C CZ3 . TRP   B 2 74  ? -22.514 -1.744  -10.007 1.00 49.97  ? 83  TRP   B CZ3 1 
ATOM   847  C CH2 . TRP   B 2 74  ? -22.044 -2.339  -11.184 1.00 50.41  ? 83  TRP   B CH2 1 
ATOM   848  N N   . LYS   B 2 75  ? -28.029 -4.724  -9.837  1.00 53.23  ? 84  LYS   B N   1 
ATOM   849  C CA  . LYS   B 2 75  ? -28.931 -5.550  -10.647 1.00 54.00  ? 84  LYS   B CA  1 
ATOM   850  C C   . LYS   B 2 75  ? -28.226 -6.355  -11.729 1.00 55.88  ? 84  LYS   B C   1 
ATOM   851  O O   . LYS   B 2 75  ? -28.793 -7.325  -12.224 1.00 56.52  ? 84  LYS   B O   1 
ATOM   852  C CB  . LYS   B 2 75  ? -29.964 -4.650  -11.348 1.00 54.20  ? 84  LYS   B CB  1 
ATOM   853  C CG  . LYS   B 2 75  ? -30.802 -3.811  -10.404 1.00 55.35  ? 84  LYS   B CG  1 
ATOM   854  C CD  . LYS   B 2 75  ? -31.837 -4.666  -9.699  1.00 58.69  ? 84  LYS   B CD  1 
ATOM   855  C CE  . LYS   B 2 75  ? -32.824 -3.844  -8.902  1.00 61.43  ? 84  LYS   B CE  1 
ATOM   856  N NZ  . LYS   B 2 75  ? -33.653 -4.703  -8.028  1.00 63.10  ? 84  LYS   B NZ  1 
ATOM   857  N N   . LEU   B 2 76  ? -27.051 -5.914  -12.169 1.00 56.54  ? 85  LEU   B N   1 
ATOM   858  C CA  . LEU   B 2 76  ? -26.356 -6.539  -13.288 1.00 57.83  ? 85  LEU   B CA  1 
ATOM   859  C C   . LEU   B 2 76  ? -25.695 -7.858  -12.873 1.00 60.13  ? 85  LEU   B C   1 
ATOM   860  O O   . LEU   B 2 76  ? -24.823 -7.873  -12.002 1.00 59.98  ? 85  LEU   B O   1 
ATOM   861  C CB  . LEU   B 2 76  ? -25.357 -5.543  -13.924 1.00 57.78  ? 85  LEU   B CB  1 
ATOM   862  C CG  . LEU   B 2 76  ? -25.868 -4.071  -14.093 1.00 58.40  ? 85  LEU   B CG  1 
ATOM   863  C CD1 . LEU   B 2 76  ? -24.794 -3.166  -14.630 1.00 58.48  ? 85  LEU   B CD1 1 
ATOM   864  C CD2 . LEU   B 2 76  ? -27.047 -4.001  -15.017 1.00 58.60  ? 85  LEU   B CD2 1 
ATOM   865  N N   . ASP   B 2 77  ? -26.126 -8.977  -13.489 1.00 61.57  ? 86  ASP   B N   1 
ATOM   866  C CA  . ASP   B 2 77  ? -25.604 -10.286 -13.111 1.00 63.27  ? 86  ASP   B CA  1 
ATOM   867  C C   . ASP   B 2 77  ? -25.028 -11.141 -14.269 1.00 63.52  ? 86  ASP   B C   1 
ATOM   868  O O   . ASP   B 2 77  ? -24.455 -12.205 -13.981 1.00 64.60  ? 86  ASP   B O   1 
ATOM   869  C CB  . ASP   B 2 77  ? -26.660 -11.090 -12.319 1.00 66.45  ? 86  ASP   B CB  1 
ATOM   870  C CG  . ASP   B 2 77  ? -28.005 -11.252 -13.014 1.00 74.60  ? 86  ASP   B CG  1 
ATOM   871  O OD1 . ASP   B 2 77  ? -28.162 -10.732 -14.150 1.00 75.58  ? 86  ASP   B OD1 1 
ATOM   872  O OD2 . ASP   B 2 77  ? -28.906 -11.905 -12.424 1.00 78.33  ? 86  ASP   B OD2 1 
ATOM   873  N N   . ALA   B 2 78  ? -25.135 -10.702 -15.534 1.00 62.48  ? 87  ALA   B N   1 
ATOM   874  C CA  . ALA   B 2 78  ? -24.560 -11.498 -16.632 1.00 62.09  ? 87  ALA   B CA  1 
ATOM   875  C C   . ALA   B 2 78  ? -23.033 -11.517 -16.529 1.00 61.98  ? 87  ALA   B C   1 
ATOM   876  O O   . ALA   B 2 78  ? -22.430 -10.579 -15.998 1.00 60.96  ? 87  ALA   B O   1 
ATOM   877  C CB  . ALA   B 2 78  ? -25.010 -10.993 -18.000 1.00 61.39  ? 87  ALA   B CB  1 
ATOM   878  N N   . ALA   B 2 79  ? -22.415 -12.605 -17.025 1.00 62.44  ? 88  ALA   B N   1 
ATOM   879  C CA  . ALA   B 2 79  ? -20.973 -12.772 -16.986 1.00 63.43  ? 88  ALA   B CA  1 
ATOM   880  C C   . ALA   B 2 79  ? -20.411 -13.144 -18.350 1.00 65.04  ? 88  ALA   B C   1 
ATOM   881  O O   . ALA   B 2 79  ? -21.095 -13.800 -19.127 1.00 65.02  ? 88  ALA   B O   1 
ATOM   882  C CB  . ALA   B 2 79  ? -20.624 -13.866 -15.987 1.00 63.36  ? 88  ALA   B CB  1 
ATOM   883  N N   . TRP   B 2 80  ? -19.142 -12.778 -18.620 1.00 66.40  ? 89  TRP   B N   1 
ATOM   884  C CA  . TRP   B 2 80  ? -18.415 -13.157 -19.843 1.00 68.11  ? 89  TRP   B CA  1 
ATOM   885  C C   . TRP   B 2 80  ? -18.304 -14.670 -19.871 1.00 68.88  ? 89  TRP   B C   1 
ATOM   886  O O   . TRP   B 2 80  ? -18.018 -15.250 -18.829 1.00 68.07  ? 89  TRP   B O   1 
ATOM   887  C CB  . TRP   B 2 80  ? -16.985 -12.591 -19.811 1.00 68.65  ? 89  TRP   B CB  1 
ATOM   888  C CG  . TRP   B 2 80  ? -16.186 -12.919 -21.038 1.00 69.72  ? 89  TRP   B CG  1 
ATOM   889  C CD1 . TRP   B 2 80  ? -16.614 -12.867 -22.332 1.00 70.88  ? 89  TRP   B CD1 1 
ATOM   890  C CD2 . TRP   B 2 80  ? -14.791 -13.240 -21.090 1.00 70.31  ? 89  TRP   B CD2 1 
ATOM   891  N NE1 . TRP   B 2 80  ? -15.587 -13.201 -23.183 1.00 71.33  ? 89  TRP   B NE1 1 
ATOM   892  C CE2 . TRP   B 2 80  ? -14.455 -13.436 -22.446 1.00 71.03  ? 89  TRP   B CE2 1 
ATOM   893  C CE3 . TRP   B 2 80  ? -13.805 -13.445 -20.119 1.00 71.02  ? 89  TRP   B CE3 1 
ATOM   894  C CZ2 . TRP   B 2 80  ? -13.175 -13.828 -22.852 1.00 71.33  ? 89  TRP   B CZ2 1 
ATOM   895  C CZ3 . TRP   B 2 80  ? -12.536 -13.827 -20.530 1.00 71.63  ? 89  TRP   B CZ3 1 
ATOM   896  C CH2 . TRP   B 2 80  ? -12.226 -13.976 -21.887 1.00 71.24  ? 89  TRP   B CH2 1 
ATOM   897  N N   . ASP   B 2 81  ? -18.553 -15.315 -21.026 1.00 70.42  ? 90  ASP   B N   1 
ATOM   898  C CA  . ASP   B 2 81  ? -18.484 -16.778 -21.071 1.00 72.64  ? 90  ASP   B CA  1 
ATOM   899  C C   . ASP   B 2 81  ? -17.036 -17.345 -21.142 1.00 74.93  ? 90  ASP   B C   1 
ATOM   900  O O   . ASP   B 2 81  ? -16.867 -18.567 -21.109 1.00 75.75  ? 90  ASP   B O   1 
ATOM   901  C CB  . ASP   B 2 81  ? -19.371 -17.381 -22.169 1.00 73.72  ? 90  ASP   B CB  1 
ATOM   902  C CG  . ASP   B 2 81  ? -19.022 -17.005 -23.586 1.00 79.19  ? 90  ASP   B CG  1 
ATOM   903  O OD1 . ASP   B 2 81  ? -18.018 -16.287 -23.783 1.00 80.35  ? 90  ASP   B OD1 1 
ATOM   904  O OD2 . ASP   B 2 81  ? -19.767 -17.410 -24.508 1.00 82.10  ? 90  ASP   B OD2 1 
ATOM   905  N N   . GLY   B 2 82  ? -16.035 -16.463 -21.219 1.00 75.29  ? 91  GLY   B N   1 
ATOM   906  C CA  . GLY   B 2 82  ? -14.630 -16.838 -21.307 1.00 76.19  ? 91  GLY   B CA  1 
ATOM   907  C C   . GLY   B 2 82  ? -14.188 -17.284 -22.695 1.00 76.94  ? 91  GLY   B C   1 
ATOM   908  O O   . GLY   B 2 82  ? -13.047 -17.735 -22.866 1.00 77.59  ? 91  GLY   B O   1 
ATOM   909  N N   . LEU   B 2 83  ? -15.092 -17.196 -23.684 1.00 76.50  ? 92  LEU   B N   1 
ATOM   910  C CA  . LEU   B 2 83  ? -14.845 -17.620 -25.051 1.00 77.05  ? 92  LEU   B CA  1 
ATOM   911  C C   . LEU   B 2 83  ? -15.084 -16.542 -26.087 1.00 77.77  ? 92  LEU   B C   1 
ATOM   912  O O   . LEU   B 2 83  ? -14.250 -16.340 -26.955 1.00 78.73  ? 92  LEU   B O   1 
ATOM   913  C CB  . LEU   B 2 83  ? -15.771 -18.798 -25.413 1.00 77.54  ? 92  LEU   B CB  1 
ATOM   914  C CG  . LEU   B 2 83  ? -15.485 -20.190 -24.857 1.00 80.40  ? 92  LEU   B CG  1 
ATOM   915  C CD1 . LEU   B 2 83  ? -16.281 -21.226 -25.647 1.00 81.21  ? 92  LEU   B CD1 1 
ATOM   916  C CD2 . LEU   B 2 83  ? -13.983 -20.537 -24.903 1.00 81.01  ? 92  LEU   B CD2 1 
ATOM   917  N N   . SER   B 2 84  ? -16.270 -15.909 -26.073 1.00 77.14  ? 93  SER   B N   1 
ATOM   918  C CA  . SER   B 2 84  ? -16.687 -15.021 -27.137 1.00 76.25  ? 93  SER   B CA  1 
ATOM   919  C C   . SER   B 2 84  ? -16.230 -13.574 -27.029 1.00 74.89  ? 93  SER   B C   1 
ATOM   920  O O   . SER   B 2 84  ? -15.824 -13.110 -25.962 1.00 74.92  ? 93  SER   B O   1 
ATOM   921  C CB  . SER   B 2 84  ? -18.208 -15.071 -27.318 1.00 78.20  ? 93  SER   B CB  1 
ATOM   922  O OG  . SER   B 2 84  ? -18.888 -15.769 -26.286 1.00 80.96  ? 93  SER   B OG  1 
ATOM   923  N N   . GLU   B 2 85  ? -16.293 -12.870 -28.172 1.00 73.86  ? 94  GLU   B N   1 
ATOM   924  C CA  . GLU   B 2 85  ? -16.029 -11.441 -28.266 1.00 73.75  ? 94  GLU   B CA  1 
ATOM   925  C C   . GLU   B 2 85  ? -17.157 -10.660 -27.542 1.00 72.34  ? 94  GLU   B C   1 
ATOM   926  O O   . GLU   B 2 85  ? -18.260 -11.168 -27.302 1.00 72.35  ? 94  GLU   B O   1 
ATOM   927  C CB  . GLU   B 2 85  ? -15.883 -10.971 -29.744 1.00 75.54  ? 94  GLU   B CB  1 
ATOM   928  C CG  . GLU   B 2 85  ? -14.502 -11.276 -30.317 1.00 79.32  ? 94  GLU   B CG  1 
ATOM   929  C CD  . GLU   B 2 85  ? -14.175 -10.728 -31.697 1.00 85.24  ? 94  GLU   B CD  1 
ATOM   930  O OE1 . GLU   B 2 85  ? -15.096 -10.233 -32.386 1.00 82.88  ? 94  GLU   B OE1 1 
ATOM   931  O OE2 . GLU   B 2 85  ? -12.984 -10.791 -32.083 1.00 88.44  ? 94  GLU   B OE2 1 
ATOM   932  N N   . VAL   B 2 86  ? -16.830 -9.452  -27.127 1.00 70.75  ? 95  VAL   B N   1 
ATOM   933  C CA  . VAL   B 2 86  ? -17.721 -8.587  -26.358 1.00 69.15  ? 95  VAL   B CA  1 
ATOM   934  C C   . VAL   B 2 86  ? -17.679 -7.185  -26.960 1.00 68.55  ? 95  VAL   B C   1 
ATOM   935  O O   . VAL   B 2 86  ? -16.798 -6.889  -27.770 1.00 70.07  ? 95  VAL   B O   1 
ATOM   936  C CB  . VAL   B 2 86  ? -17.300 -8.552  -24.846 1.00 67.87  ? 95  VAL   B CB  1 
ATOM   937  C CG1 . VAL   B 2 86  ? -17.147 -9.951  -24.268 1.00 68.10  ? 95  VAL   B CG1 1 
ATOM   938  C CG2 . VAL   B 2 86  ? -16.024 -7.742  -24.653 1.00 67.46  ? 95  VAL   B CG2 1 
ATOM   939  N N   . GLN   B 2 87  ? -18.601 -6.309  -26.547 1.00 66.60  ? 96  GLN   B N   1 
ATOM   940  C CA  . GLN   B 2 87  ? -18.604 -4.941  -27.021 1.00 64.82  ? 96  GLN   B CA  1 
ATOM   941  C C   . GLN   B 2 87  ? -18.507 -3.975  -25.854 1.00 63.40  ? 96  GLN   B C   1 
ATOM   942  O O   . GLN   B 2 87  ? -19.273 -4.063  -24.906 1.00 62.69  ? 96  GLN   B O   1 
ATOM   943  C CB  . GLN   B 2 87  ? -19.836 -4.638  -27.908 1.00 64.70  ? 96  GLN   B CB  1 
ATOM   944  C CG  . GLN   B 2 87  ? -19.598 -5.067  -29.346 1.00 68.26  ? 96  GLN   B CG  1 
ATOM   945  C CD  . GLN   B 2 87  ? -20.706 -4.770  -30.328 1.00 70.00  ? 96  GLN   B CD  1 
ATOM   946  O OE1 . GLN   B 2 87  ? -21.581 -3.930  -30.104 1.00 70.27  ? 96  GLN   B OE1 1 
ATOM   947  N NE2 . GLN   B 2 87  ? -20.664 -5.450  -31.466 1.00 70.19  ? 96  GLN   B NE2 1 
ATOM   948  N N   . LEU   B 2 88  ? -17.559 -3.055  -25.940 1.00 62.33  ? 97  LEU   B N   1 
ATOM   949  C CA  . LEU   B 2 88  ? -17.463 -1.968  -25.007 1.00 61.66  ? 97  LEU   B CA  1 
ATOM   950  C C   . LEU   B 2 88  ? -18.316 -0.856  -25.641 1.00 61.44  ? 97  LEU   B C   1 
ATOM   951  O O   . LEU   B 2 88  ? -18.024 -0.436  -26.769 1.00 61.95  ? 97  LEU   B O   1 
ATOM   952  C CB  . LEU   B 2 88  ? -16.006 -1.487  -24.883 1.00 61.35  ? 97  LEU   B CB  1 
ATOM   953  C CG  . LEU   B 2 88  ? -15.827 -0.150  -24.139 1.00 61.66  ? 97  LEU   B CG  1 
ATOM   954  C CD1 . LEU   B 2 88  ? -16.295 -0.251  -22.702 1.00 60.53  ? 97  LEU   B CD1 1 
ATOM   955  C CD2 . LEU   B 2 88  ? -14.402 0.374   -24.255 1.00 62.13  ? 97  LEU   B CD2 1 
ATOM   956  N N   . LEU   B 2 89  ? -19.389 -0.425  -24.966 1.00 60.48  ? 98  LEU   B N   1 
ATOM   957  C CA  . LEU   B 2 89  ? -20.181 0.695   -25.441 1.00 60.58  ? 98  LEU   B CA  1 
ATOM   958  C C   . LEU   B 2 89  ? -19.491 1.882   -24.783 1.00 61.46  ? 98  LEU   B C   1 
ATOM   959  O O   . LEU   B 2 89  ? -19.781 2.216   -23.639 1.00 61.10  ? 98  LEU   B O   1 
ATOM   960  C CB  . LEU   B 2 89  ? -21.666 0.555   -25.026 1.00 60.50  ? 98  LEU   B CB  1 
ATOM   961  C CG  . LEU   B 2 89  ? -22.668 1.705   -25.318 1.00 61.91  ? 98  LEU   B CG  1 
ATOM   962  C CD1 . LEU   B 2 89  ? -22.554 2.208   -26.713 1.00 63.39  ? 98  LEU   B CD1 1 
ATOM   963  C CD2 . LEU   B 2 89  ? -24.097 1.235   -25.130 1.00 62.37  ? 98  LEU   B CD2 1 
ATOM   964  N N   . ALA   B 2 90  ? -18.483 2.443   -25.473 1.00 62.18  ? 99  ALA   B N   1 
ATOM   965  C CA  . ALA   B 2 90  ? -17.674 3.545   -24.956 1.00 62.58  ? 99  ALA   B CA  1 
ATOM   966  C C   . ALA   B 2 90  ? -18.395 4.856   -25.075 1.00 62.54  ? 99  ALA   B C   1 
ATOM   967  O O   . ALA   B 2 90  ? -18.809 5.213   -26.170 1.00 63.15  ? 99  ALA   B O   1 
ATOM   968  C CB  . ALA   B 2 90  ? -16.359 3.635   -25.715 1.00 62.35  ? 99  ALA   B CB  1 
ATOM   969  N N   . VAL   B 2 91  ? -18.502 5.617   -23.971 1.00 61.50  ? 100 VAL   B N   1 
ATOM   970  C CA  . VAL   B 2 91  ? -19.122 6.935   -24.018 1.00 61.20  ? 100 VAL   B CA  1 
ATOM   971  C C   . VAL   B 2 91  ? -18.024 7.959   -23.641 1.00 62.04  ? 100 VAL   B C   1 
ATOM   972  O O   . VAL   B 2 91  ? -17.847 8.296   -22.473 1.00 62.05  ? 100 VAL   B O   1 
ATOM   973  C CB  . VAL   B 2 91  ? -20.351 6.985   -23.086 1.00 60.99  ? 100 VAL   B CB  1 
ATOM   974  C CG1 . VAL   B 2 91  ? -21.050 8.345   -23.178 1.00 61.69  ? 100 VAL   B CG1 1 
ATOM   975  C CG2 . VAL   B 2 91  ? -21.319 5.846   -23.404 1.00 60.31  ? 100 VAL   B CG2 1 
ATOM   976  N N   . PRO   B 2 92  ? -17.240 8.421   -24.628 1.00 62.90  ? 101 PRO   B N   1 
ATOM   977  C CA  . PRO   B 2 92  ? -16.117 9.322   -24.322 1.00 63.83  ? 101 PRO   B CA  1 
ATOM   978  C C   . PRO   B 2 92  ? -16.555 10.759  -24.082 1.00 65.27  ? 101 PRO   B C   1 
ATOM   979  O O   . PRO   B 2 92  ? -17.600 11.183  -24.576 1.00 65.74  ? 101 PRO   B O   1 
ATOM   980  C CB  . PRO   B 2 92  ? -15.217 9.215   -25.579 1.00 65.15  ? 101 PRO   B CB  1 
ATOM   981  C CG  . PRO   B 2 92  ? -15.883 8.205   -26.503 1.00 65.37  ? 101 PRO   B CG  1 
ATOM   982  C CD  . PRO   B 2 92  ? -17.317 8.125   -26.069 1.00 63.10  ? 101 PRO   B CD  1 
ATOM   983  N N   . PRO   B 2 93  ? -15.769 11.532  -23.311 1.00 65.50  ? 102 PRO   B N   1 
ATOM   984  C CA  . PRO   B 2 93  ? -16.168 12.926  -23.037 1.00 65.82  ? 102 PRO   B CA  1 
ATOM   985  C C   . PRO   B 2 93  ? -16.262 13.767  -24.305 1.00 67.22  ? 102 PRO   B C   1 
ATOM   986  O O   . PRO   B 2 93  ? -15.354 13.768  -25.139 1.00 67.56  ? 102 PRO   B O   1 
ATOM   987  C CB  . PRO   B 2 93  ? -15.082 13.441  -22.089 1.00 66.16  ? 102 PRO   B CB  1 
ATOM   988  C CG  . PRO   B 2 93  ? -14.389 12.192  -21.564 1.00 66.65  ? 102 PRO   B CG  1 
ATOM   989  C CD  . PRO   B 2 93  ? -14.505 11.166  -22.638 1.00 64.93  ? 102 PRO   B CD  1 
ATOM   990  N N   . GLY   B 2 94  ? -17.396 14.436  -24.465 1.00 67.75  ? 103 GLY   B N   1 
ATOM   991  C CA  . GLY   B 2 94  ? -17.669 15.278  -25.620 1.00 68.26  ? 103 GLY   B CA  1 
ATOM   992  C C   . GLY   B 2 94  ? -17.939 14.524  -26.910 1.00 68.92  ? 103 GLY   B C   1 
ATOM   993  O O   . GLY   B 2 94  ? -18.186 15.145  -27.933 1.00 68.65  ? 103 GLY   B O   1 
ATOM   994  N N   . GLU   B 2 95  ? -17.883 13.190  -26.891 1.00 69.65  ? 104 GLU   B N   1 
ATOM   995  C CA  . GLU   B 2 95  ? -18.092 12.402  -28.102 1.00 70.62  ? 104 GLU   B CA  1 
ATOM   996  C C   . GLU   B 2 95  ? -19.299 11.486  -27.966 1.00 70.85  ? 104 GLU   B C   1 
ATOM   997  O O   . GLU   B 2 95  ? -19.689 11.128  -26.855 1.00 70.36  ? 104 GLU   B O   1 
ATOM   998  C CB  . GLU   B 2 95  ? -16.827 11.587  -28.433 1.00 73.44  ? 104 GLU   B CB  1 
ATOM   999  C CG  . GLU   B 2 95  ? -15.568 12.437  -28.538 1.00 78.94  ? 104 GLU   B CG  1 
ATOM   1000 C CD  . GLU   B 2 95  ? -14.284 11.670  -28.801 1.00 85.68  ? 104 GLU   B CD  1 
ATOM   1001 O OE1 . GLU   B 2 95  ? -14.349 10.425  -28.921 1.00 86.53  ? 104 GLU   B OE1 1 
ATOM   1002 O OE2 . GLU   B 2 95  ? -13.214 12.315  -28.904 1.00 88.50  ? 104 GLU   B OE2 1 
ATOM   1003 N N   . ARG   B 2 96  ? -19.898 11.116  -29.103 1.00 70.88  ? 105 ARG   B N   1 
ATOM   1004 C CA  . ARG   B 2 96  ? -21.060 10.234  -29.134 1.00 71.95  ? 105 ARG   B CA  1 
ATOM   1005 C C   . ARG   B 2 96  ? -20.703 8.782   -28.694 1.00 71.86  ? 105 ARG   B C   1 
ATOM   1006 O O   . ARG   B 2 96  ? -19.543 8.382   -28.822 1.00 72.29  ? 105 ARG   B O   1 
ATOM   1007 C CB  . ARG   B 2 96  ? -21.652 10.274  -30.555 1.00 74.76  ? 105 ARG   B CB  1 
ATOM   1008 C CG  . ARG   B 2 96  ? -22.769 9.286   -30.816 1.00 80.24  ? 105 ARG   B CG  1 
ATOM   1009 C CD  . ARG   B 2 96  ? -23.841 9.836   -31.732 1.00 85.83  ? 105 ARG   B CD  1 
ATOM   1010 N NE  . ARG   B 2 96  ? -23.336 10.300  -33.024 1.00 89.99  ? 105 ARG   B NE  1 
ATOM   1011 C CZ  . ARG   B 2 96  ? -23.055 9.506   -34.054 1.00 94.94  ? 105 ARG   B CZ  1 
ATOM   1012 N NH1 . ARG   B 2 96  ? -23.155 8.185   -33.931 1.00 95.47  ? 105 ARG   B NH1 1 
ATOM   1013 N NH2 . ARG   B 2 96  ? -22.636 10.023  -35.205 1.00 95.04  ? 105 ARG   B NH2 1 
ATOM   1014 N N   . ALA   B 2 97  ? -21.687 8.022   -28.132 1.00 70.92  ? 106 ALA   B N   1 
ATOM   1015 C CA  . ALA   B 2 97  ? -21.543 6.624   -27.707 1.00 70.71  ? 106 ALA   B CA  1 
ATOM   1016 C C   . ALA   B 2 97  ? -21.097 5.767   -28.892 1.00 71.90  ? 106 ALA   B C   1 
ATOM   1017 O O   . ALA   B 2 97  ? -21.634 5.918   -29.984 1.00 72.21  ? 106 ALA   B O   1 
ATOM   1018 C CB  . ALA   B 2 97  ? -22.864 6.104   -27.177 1.00 69.95  ? 106 ALA   B CB  1 
ATOM   1019 N N   . LYS   B 2 98  ? -20.121 4.876   -28.693 1.00 72.72  ? 107 LYS   B N   1 
ATOM   1020 C CA  . LYS   B 2 98  ? -19.584 4.057   -29.794 1.00 73.73  ? 107 LYS   B CA  1 
ATOM   1021 C C   . LYS   B 2 98  ? -19.349 2.622   -29.329 1.00 73.37  ? 107 LYS   B C   1 
ATOM   1022 O O   . LYS   B 2 98  ? -18.800 2.436   -28.257 1.00 73.95  ? 107 LYS   B O   1 
ATOM   1023 C CB  . LYS   B 2 98  ? -18.252 4.678   -30.234 1.00 76.87  ? 107 LYS   B CB  1 
ATOM   1024 C CG  . LYS   B 2 98  ? -17.712 4.224   -31.583 1.00 83.58  ? 107 LYS   B CG  1 
ATOM   1025 C CD  . LYS   B 2 98  ? -16.344 4.886   -31.909 1.00 89.37  ? 107 LYS   B CD  1 
ATOM   1026 C CE  . LYS   B 2 98  ? -15.289 4.717   -30.809 1.00 92.15  ? 107 LYS   B CE  1 
ATOM   1027 N NZ  . LYS   B 2 98  ? -15.204 5.886   -29.885 1.00 92.66  ? 107 LYS   B NZ  1 
ATOM   1028 N N   . ASN   B 2 99  ? -19.760 1.613   -30.107 1.00 72.62  ? 108 ASN   B N   1 
ATOM   1029 C CA  . ASN   B 2 99  ? -19.546 0.210   -29.725 1.00 72.85  ? 108 ASN   B CA  1 
ATOM   1030 C C   . ASN   B 2 99  ? -18.238 -0.273  -30.310 1.00 73.21  ? 108 ASN   B C   1 
ATOM   1031 O O   . ASN   B 2 99  ? -18.016 -0.092  -31.501 1.00 74.63  ? 108 ASN   B O   1 
ATOM   1032 C CB  . ASN   B 2 99  ? -20.671 -0.693  -30.248 1.00 73.41  ? 108 ASN   B CB  1 
ATOM   1033 C CG  . ASN   B 2 99  ? -22.035 -0.467  -29.631 1.00 77.09  ? 108 ASN   B CG  1 
ATOM   1034 O OD1 . ASN   B 2 99  ? -22.670 0.596   -29.791 1.00 78.18  ? 108 ASN   B OD1 1 
ATOM   1035 N ND2 . ASN   B 2 99  ? -22.552 -1.490  -28.963 1.00 76.95  ? 108 ASN   B ND2 1 
ATOM   1036 N N   . ILE   B 2 100 ? -17.386 -0.902  -29.513 1.00 72.26  ? 109 ILE   B N   1 
ATOM   1037 C CA  . ILE   B 2 100 ? -16.118 -1.451  -29.985 1.00 72.07  ? 109 ILE   B CA  1 
ATOM   1038 C C   . ILE   B 2 100 ? -16.079 -2.931  -29.652 1.00 71.61  ? 109 ILE   B C   1 
ATOM   1039 O O   . ILE   B 2 100 ? -16.158 -3.297  -28.480 1.00 71.30  ? 109 ILE   B O   1 
ATOM   1040 C CB  . ILE   B 2 100 ? -14.910 -0.746  -29.340 1.00 72.92  ? 109 ILE   B CB  1 
ATOM   1041 C CG1 . ILE   B 2 100 ? -14.943 0.759   -29.576 1.00 74.44  ? 109 ILE   B CG1 1 
ATOM   1042 C CG2 . ILE   B 2 100 ? -13.600 -1.372  -29.816 1.00 73.42  ? 109 ILE   B CG2 1 
ATOM   1043 C CD1 . ILE   B 2 100 ? -14.799 1.165   -31.045 1.00 75.93  ? 109 ILE   B CD1 1 
ATOM   1044 N N   . GLN   B 2 101 ? -15.919 -3.777  -30.659 1.00 71.17  ? 110 GLN   B N   1 
ATOM   1045 C CA  . GLN   B 2 101 ? -15.869 -5.216  -30.458 1.00 71.94  ? 110 GLN   B CA  1 
ATOM   1046 C C   . GLN   B 2 101 ? -14.444 -5.692  -30.229 1.00 72.40  ? 110 GLN   B C   1 
ATOM   1047 O O   . GLN   B 2 101 ? -13.558 -5.393  -31.022 1.00 73.05  ? 110 GLN   B O   1 
ATOM   1048 C CB  . GLN   B 2 101 ? -16.461 -5.940  -31.678 1.00 73.75  ? 110 GLN   B CB  1 
ATOM   1049 C CG  . GLN   B 2 101 ? -16.594 -7.441  -31.477 1.00 76.38  ? 110 GLN   B CG  1 
ATOM   1050 C CD  . GLN   B 2 101 ? -17.633 -8.014  -32.399 1.00 80.78  ? 110 GLN   B CD  1 
ATOM   1051 O OE1 . GLN   B 2 101 ? -18.661 -7.391  -32.670 1.00 79.59  ? 110 GLN   B OE1 1 
ATOM   1052 N NE2 . GLN   B 2 101 ? -17.376 -9.222  -32.909 1.00 83.56  ? 110 GLN   B NE2 1 
ATOM   1053 N N   . THR   B 2 102 ? -14.230 -6.477  -29.181 1.00 71.83  ? 111 THR   B N   1 
ATOM   1054 C CA  . THR   B 2 102 ? -12.912 -7.010  -28.885 1.00 72.22  ? 111 THR   B CA  1 
ATOM   1055 C C   . THR   B 2 102 ? -13.032 -8.389  -28.263 1.00 72.62  ? 111 THR   B C   1 
ATOM   1056 O O   . THR   B 2 102 ? -14.114 -8.753  -27.785 1.00 73.35  ? 111 THR   B O   1 
ATOM   1057 C CB  . THR   B 2 102 ? -12.175 -6.037  -27.943 1.00 74.22  ? 111 THR   B CB  1 
ATOM   1058 O OG1 . THR   B 2 102 ? -10.796 -6.396  -27.868 1.00 75.25  ? 111 THR   B OG1 1 
ATOM   1059 C CG2 . THR   B 2 102 ? -12.812 -5.948  -26.520 1.00 74.36  ? 111 THR   B CG2 1 
ATOM   1060 N N   . LEU   B 2 103 ? -11.938 -9.170  -28.269 1.00 72.02  ? 112 LEU   B N   1 
ATOM   1061 C CA  . LEU   B 2 103 ? -11.943 -10.446 -27.576 1.00 72.13  ? 112 LEU   B CA  1 
ATOM   1062 C C   . LEU   B 2 103 ? -11.157 -10.161 -26.312 1.00 71.93  ? 112 LEU   B C   1 
ATOM   1063 O O   . LEU   B 2 103 ? -9.993  -9.747  -26.379 1.00 71.67  ? 112 LEU   B O   1 
ATOM   1064 C CB  . LEU   B 2 103 ? -11.281 -11.625 -28.324 1.00 72.73  ? 112 LEU   B CB  1 
ATOM   1065 C CG  . LEU   B 2 103 ? -11.315 -12.918 -27.464 1.00 74.68  ? 112 LEU   B CG  1 
ATOM   1066 C CD1 . LEU   B 2 103 ? -12.552 -13.698 -27.730 1.00 75.41  ? 112 LEU   B CD1 1 
ATOM   1067 C CD2 . LEU   B 2 103 ? -10.061 -13.775 -27.617 1.00 75.76  ? 112 LEU   B CD2 1 
ATOM   1068 N N   . PRO   B 2 104 ? -11.769 -10.389 -25.145 1.00 71.72  ? 113 PRO   B N   1 
ATOM   1069 C CA  . PRO   B 2 104 ? -11.063 -10.085 -23.899 1.00 72.04  ? 113 PRO   B CA  1 
ATOM   1070 C C   . PRO   B 2 104 ? -9.871  -10.979 -23.571 1.00 73.55  ? 113 PRO   B C   1 
ATOM   1071 O O   . PRO   B 2 104 ? -9.837  -12.174 -23.880 1.00 74.20  ? 113 PRO   B O   1 
ATOM   1072 C CB  . PRO   B 2 104 ? -12.152 -10.211 -22.821 1.00 72.10  ? 113 PRO   B CB  1 
ATOM   1073 C CG  . PRO   B 2 104 ? -13.451 -10.213 -23.565 1.00 72.77  ? 113 PRO   B CG  1 
ATOM   1074 C CD  . PRO   B 2 104 ? -13.156 -10.823 -24.902 1.00 70.84  ? 113 PRO   B CD  1 
ATOM   1075 N N   . GLY   B 2 105 ? -8.920  -10.375 -22.873 1.00 73.51  ? 114 GLY   B N   1 
ATOM   1076 C CA  . GLY   B 2 105 ? -7.786  -11.052 -22.276 1.00 73.63  ? 114 GLY   B CA  1 
ATOM   1077 C C   . GLY   B 2 105 ? -8.188  -11.533 -20.888 1.00 73.97  ? 114 GLY   B C   1 
ATOM   1078 O O   . GLY   B 2 105 ? -9.379  -11.641 -20.576 1.00 73.84  ? 114 GLY   B O   1 
ATOM   1079 N N   . ILE   B 2 106 ? -7.207  -11.861 -20.045 1.00 74.07  ? 115 ILE   B N   1 
ATOM   1080 C CA  . ILE   B 2 106 ? -7.462  -12.395 -18.715 1.00 74.18  ? 115 ILE   B CA  1 
ATOM   1081 C C   . ILE   B 2 106 ? -6.558  -11.753 -17.682 1.00 73.63  ? 115 ILE   B C   1 
ATOM   1082 O O   . ILE   B 2 106 ? -5.355  -11.651 -17.887 1.00 73.96  ? 115 ILE   B O   1 
ATOM   1083 C CB  . ILE   B 2 106 ? -7.199  -13.936 -18.700 1.00 75.66  ? 115 ILE   B CB  1 
ATOM   1084 C CG1 . ILE   B 2 106 ? -8.172  -14.716 -19.595 1.00 78.10  ? 115 ILE   B CG1 1 
ATOM   1085 C CG2 . ILE   B 2 106 ? -7.169  -14.515 -17.282 1.00 76.34  ? 115 ILE   B CG2 1 
ATOM   1086 C CD1 . ILE   B 2 106 ? -9.523  -14.810 -19.085 1.00 80.21  ? 115 ILE   B CD1 1 
ATOM   1087 N N   . PHE   B 2 107 ? -7.118  -11.430 -16.529 1.00 72.77  ? 116 PHE   B N   1 
ATOM   1088 C CA  . PHE   B 2 107 ? -6.349  -11.019 -15.375 1.00 72.33  ? 116 PHE   B CA  1 
ATOM   1089 C C   . PHE   B 2 107 ? -6.318  -12.272 -14.520 1.00 72.79  ? 116 PHE   B C   1 
ATOM   1090 O O   . PHE   B 2 107 ? -7.381  -12.752 -14.125 1.00 73.03  ? 116 PHE   B O   1 
ATOM   1091 C CB  . PHE   B 2 107 ? -7.083  -9.926  -14.581 1.00 71.54  ? 116 PHE   B CB  1 
ATOM   1092 C CG  . PHE   B 2 107 ? -6.860  -8.497  -15.015 1.00 71.33  ? 116 PHE   B CG  1 
ATOM   1093 C CD1 . PHE   B 2 107 ? -6.164  -8.206  -16.181 1.00 71.42  ? 116 PHE   B CD1 1 
ATOM   1094 C CD2 . PHE   B 2 107 ? -7.361  -7.445  -14.268 1.00 71.22  ? 116 PHE   B CD2 1 
ATOM   1095 C CE1 . PHE   B 2 107 ? -5.977  -6.891  -16.585 1.00 71.85  ? 116 PHE   B CE1 1 
ATOM   1096 C CE2 . PHE   B 2 107 ? -7.172  -6.132  -14.677 1.00 71.58  ? 116 PHE   B CE2 1 
ATOM   1097 C CZ  . PHE   B 2 107 ? -6.485  -5.863  -15.833 1.00 71.54  ? 116 PHE   B CZ  1 
ATOM   1098 N N   . LYS   B 2 108 ? -5.131  -12.825 -14.245 1.00 72.69  ? 117 LYS   B N   1 
ATOM   1099 C CA  . LYS   B 2 108 ? -5.016  -13.981 -13.368 1.00 72.85  ? 117 LYS   B CA  1 
ATOM   1100 C C   . LYS   B 2 108 ? -4.678  -13.430 -11.996 1.00 72.18  ? 117 LYS   B C   1 
ATOM   1101 O O   . LYS   B 2 108 ? -3.679  -12.718 -11.863 1.00 71.89  ? 117 LYS   B O   1 
ATOM   1102 C CB  . LYS   B 2 108 ? -3.900  -14.930 -13.832 1.00 75.99  ? 117 LYS   B CB  1 
ATOM   1103 C CG  . LYS   B 2 108 ? -4.017  -15.354 -15.298 1.00 82.42  ? 117 LYS   B CG  1 
ATOM   1104 C CD  . LYS   B 2 108 ? -2.772  -16.108 -15.772 1.00 89.13  ? 117 LYS   B CD  1 
ATOM   1105 C CE  . LYS   B 2 108 ? -1.867  -15.263 -16.651 1.00 94.80  ? 117 LYS   B CE  1 
ATOM   1106 N NZ  . LYS   B 2 108 ? -0.853  -16.086 -17.381 1.00 98.11  ? 117 LYS   B NZ  1 
ATOM   1107 N N   . THR   B 2 109 ? -5.527  -13.701 -10.990 1.00 71.50  ? 118 THR   B N   1 
ATOM   1108 C CA  . THR   B 2 109 ? -5.288  -13.247 -9.616  1.00 71.77  ? 118 THR   B CA  1 
ATOM   1109 C C   . THR   B 2 109 ? -5.211  -14.460 -8.647  1.00 72.50  ? 118 THR   B C   1 
ATOM   1110 O O   . THR   B 2 109 ? -5.605  -15.570 -9.014  1.00 72.84  ? 118 THR   B O   1 
ATOM   1111 C CB  . THR   B 2 109 ? -6.350  -12.185 -9.144  1.00 72.12  ? 118 THR   B CB  1 
ATOM   1112 O OG1 . THR   B 2 109 ? -7.520  -12.808 -8.606  1.00 72.53  ? 118 THR   B OG1 1 
ATOM   1113 C CG2 . THR   B 2 109 ? -6.727  -11.176 -10.216 1.00 71.85  ? 118 THR   B CG2 1 
ATOM   1114 N N   . LYS   B 2 110 ? -4.745  -14.239 -7.407  1.00 72.36  ? 119 LYS   B N   1 
ATOM   1115 C CA  . LYS   B 2 110 ? -4.718  -15.299 -6.401  1.00 73.12  ? 119 LYS   B CA  1 
ATOM   1116 C C   . LYS   B 2 110 ? -6.159  -15.749 -6.029  1.00 74.17  ? 119 LYS   B C   1 
ATOM   1117 O O   . LYS   B 2 110 ? -6.331  -16.837 -5.484  1.00 74.21  ? 119 LYS   B O   1 
ATOM   1118 C CB  . LYS   B 2 110 ? -3.955  -14.835 -5.148  1.00 74.16  ? 119 LYS   B CB  1 
ATOM   1119 C CG  . LYS   B 2 110 ? -4.661  -13.723 -4.384  1.00 77.36  ? 119 LYS   B CG  1 
ATOM   1120 C CD  . LYS   B 2 110 ? -4.125  -13.562 -2.977  1.00 81.43  ? 119 LYS   B CD  1 
ATOM   1121 C CE  . LYS   B 2 110 ? -4.971  -12.651 -2.122  1.00 84.40  ? 119 LYS   B CE  1 
ATOM   1122 N NZ  . LYS   B 2 110 ? -4.363  -11.303 -1.998  1.00 87.00  ? 119 LYS   B NZ  1 
ATOM   1123 N N   . ASP   B 2 111 ? -7.187  -14.923 -6.350  1.00 74.40  ? 120 ASP   B N   1 
ATOM   1124 C CA  . ASP   B 2 111 ? -8.586  -15.207 -6.072  1.00 74.90  ? 120 ASP   B CA  1 
ATOM   1125 C C   . ASP   B 2 111 ? -9.403  -15.602 -7.300  1.00 75.28  ? 120 ASP   B C   1 
ATOM   1126 O O   . ASP   B 2 111 ? -10.626 -15.628 -7.209  1.00 75.94  ? 120 ASP   B O   1 
ATOM   1127 C CB  . ASP   B 2 111 ? -9.234  -13.985 -5.428  1.00 76.91  ? 120 ASP   B CB  1 
ATOM   1128 C CG  . ASP   B 2 111 ? -8.664  -13.652 -4.073  1.00 81.47  ? 120 ASP   B CG  1 
ATOM   1129 O OD1 . ASP   B 2 111 ? -8.733  -14.509 -3.181  1.00 81.47  ? 120 ASP   B OD1 1 
ATOM   1130 O OD2 . ASP   B 2 111 ? -8.159  -12.527 -3.907  1.00 84.76  ? 120 ASP   B OD2 1 
ATOM   1131 N N   . GLY   B 2 112 ? -8.758  -15.887 -8.428  1.00 74.63  ? 121 GLY   B N   1 
ATOM   1132 C CA  . GLY   B 2 112 ? -9.475  -16.277 -9.632  1.00 74.45  ? 121 GLY   B CA  1 
ATOM   1133 C C   . GLY   B 2 112 ? -9.185  -15.419 -10.841 1.00 74.37  ? 121 GLY   B C   1 
ATOM   1134 O O   . GLY   B 2 112 ? -8.514  -14.394 -10.738 1.00 74.38  ? 121 GLY   B O   1 
ATOM   1135 N N   . ASP   B 2 113 ? -9.677  -15.849 -12.004 1.00 74.32  ? 122 ASP   B N   1 
ATOM   1136 C CA  . ASP   B 2 113 ? -9.475  -15.143 -13.262 1.00 74.56  ? 122 ASP   B CA  1 
ATOM   1137 C C   . ASP   B 2 113 ? -10.633 -14.209 -13.568 1.00 74.01  ? 122 ASP   B C   1 
ATOM   1138 O O   . ASP   B 2 113 ? -11.782 -14.536 -13.279 1.00 74.48  ? 122 ASP   B O   1 
ATOM   1139 C CB  . ASP   B 2 113 ? -9.315  -16.139 -14.401 1.00 77.22  ? 122 ASP   B CB  1 
ATOM   1140 C CG  . ASP   B 2 113 ? -8.077  -17.005 -14.334 1.00 85.03  ? 122 ASP   B CG  1 
ATOM   1141 O OD1 . ASP   B 2 113 ? -7.283  -16.840 -13.375 1.00 87.51  ? 122 ASP   B OD1 1 
ATOM   1142 O OD2 . ASP   B 2 113 ? -7.896  -17.853 -15.244 1.00 88.14  ? 122 ASP   B OD2 1 
ATOM   1143 N N   . ILE   B 2 114 ? -10.330 -13.046 -14.162 1.00 72.58  ? 123 ILE   B N   1 
ATOM   1144 C CA  . ILE   B 2 114 ? -11.312 -12.021 -14.500 1.00 71.96  ? 123 ILE   B CA  1 
ATOM   1145 C C   . ILE   B 2 114 ? -11.099 -11.633 -15.968 1.00 70.86  ? 123 ILE   B C   1 
ATOM   1146 O O   . ILE   B 2 114 ? -9.953  -11.537 -16.410 1.00 70.84  ? 123 ILE   B O   1 
ATOM   1147 C CB  . ILE   B 2 114 ? -11.101 -10.769 -13.584 1.00 72.33  ? 123 ILE   B CB  1 
ATOM   1148 C CG1 . ILE   B 2 114 ? -11.095 -11.128 -12.111 1.00 74.00  ? 123 ILE   B CG1 1 
ATOM   1149 C CG2 . ILE   B 2 114 ? -12.117 -9.683  -13.854 1.00 72.71  ? 123 ILE   B CG2 1 
ATOM   1150 C CD1 . ILE   B 2 114 ? -10.462 -10.064 -11.223 1.00 75.66  ? 123 ILE   B CD1 1 
ATOM   1151 N N   . GLY   B 2 115 ? -12.183 -11.383 -16.705 1.00 69.54  ? 124 GLY   B N   1 
ATOM   1152 C CA  . GLY   B 2 115 ? -12.060 -10.923 -18.087 1.00 69.18  ? 124 GLY   B CA  1 
ATOM   1153 C C   . GLY   B 2 115 ? -11.431 -9.541  -18.128 1.00 68.46  ? 124 GLY   B C   1 
ATOM   1154 O O   . GLY   B 2 115 ? -11.467 -8.821  -17.123 1.00 69.15  ? 124 GLY   B O   1 
ATOM   1155 N N   . ALA   B 2 116 ? -10.788 -9.181  -19.227 1.00 67.39  ? 125 ALA   B N   1 
ATOM   1156 C CA  . ALA   B 2 116 ? -10.152 -7.871  -19.323 1.00 67.21  ? 125 ALA   B CA  1 
ATOM   1157 C C   . ALA   B 2 116 ? -10.198 -7.343  -20.733 1.00 68.27  ? 125 ALA   B C   1 
ATOM   1158 O O   . ALA   B 2 116 ? -10.033 -8.104  -21.663 1.00 69.11  ? 125 ALA   B O   1 
ATOM   1159 C CB  . ALA   B 2 116 ? -8.730  -7.926  -18.795 1.00 66.64  ? 125 ALA   B CB  1 
ATOM   1160 N N   . VAL   B 2 117 ? -10.434 -6.052  -20.905 1.00 68.71  ? 126 VAL   B N   1 
ATOM   1161 C CA  A VAL   B 2 117 ? -10.508 -5.446  -22.237 0.50 69.61  ? 126 VAL   B CA  1 
ATOM   1162 C CA  B VAL   B 2 117 ? -10.541 -5.428  -22.212 0.50 69.69  ? 126 VAL   B CA  1 
ATOM   1163 C C   . VAL   B 2 117 ? -9.336  -4.495  -22.472 1.00 70.84  ? 126 VAL   B C   1 
ATOM   1164 O O   . VAL   B 2 117 ? -9.053  -3.607  -21.667 1.00 71.05  ? 126 VAL   B O   1 
ATOM   1165 C CB  A VAL   B 2 117 ? -11.879 -4.812  -22.578 0.50 69.78  ? 126 VAL   B CB  1 
ATOM   1166 C CB  B VAL   B 2 117 ? -11.933 -4.751  -22.310 0.50 70.00  ? 126 VAL   B CB  1 
ATOM   1167 C CG1 A VAL   B 2 117 ? -12.935 -5.892  -22.784 0.50 70.09  ? 126 VAL   B CG1 1 
ATOM   1168 C CG1 B VAL   B 2 117 ? -11.935 -3.562  -23.247 0.50 70.48  ? 126 VAL   B CG1 1 
ATOM   1169 C CG2 A VAL   B 2 117 ? -12.319 -3.819  -21.511 0.50 70.05  ? 126 VAL   B CG2 1 
ATOM   1170 C CG2 B VAL   B 2 117 ? -12.999 -5.766  -22.709 0.50 70.24  ? 126 VAL   B CG2 1 
ATOM   1171 N N   . ALA   B 2 118 ? -8.600  -4.736  -23.561 1.00 72.13  ? 127 ALA   B N   1 
ATOM   1172 C CA  . ALA   B 2 118 ? -7.417  -3.959  -23.879 1.00 73.60  ? 127 ALA   B CA  1 
ATOM   1173 C C   . ALA   B 2 118 ? -7.731  -2.794  -24.791 1.00 74.74  ? 127 ALA   B C   1 
ATOM   1174 O O   . ALA   B 2 118 ? -7.330  -2.764  -25.953 1.00 75.27  ? 127 ALA   B O   1 
ATOM   1175 C CB  . ALA   B 2 118 ? -6.346  -4.859  -24.479 1.00 73.88  ? 127 ALA   B CB  1 
ATOM   1176 N N   . LEU   B 2 119 ? -8.476  -1.826  -24.259 1.00 74.78  ? 128 LEU   B N   1 
ATOM   1177 C CA  . LEU   B 2 119 ? -8.851  -0.638  -25.009 1.00 75.05  ? 128 LEU   B CA  1 
ATOM   1178 C C   . LEU   B 2 119 ? -8.496  0.592   -24.184 1.00 74.79  ? 128 LEU   B C   1 
ATOM   1179 O O   . LEU   B 2 119 ? -8.795  0.629   -22.988 1.00 75.05  ? 128 LEU   B O   1 
ATOM   1180 C CB  . LEU   B 2 119 ? -10.362 -0.662  -25.285 1.00 75.77  ? 128 LEU   B CB  1 
ATOM   1181 C CG  . LEU   B 2 119 ? -10.838 -1.764  -26.227 1.00 77.62  ? 128 LEU   B CG  1 
ATOM   1182 C CD1 . LEU   B 2 119 ? -12.358 -1.824  -26.283 1.00 78.15  ? 128 LEU   B CD1 1 
ATOM   1183 C CD2 . LEU   B 2 119 ? -10.241 -1.602  -27.618 1.00 78.48  ? 128 LEU   B CD2 1 
ATOM   1184 N N   . ASP   B 2 120 ? -7.851  1.592   -24.802 1.00 74.17  ? 129 ASP   B N   1 
ATOM   1185 C CA  . ASP   B 2 120 ? -7.499  2.811   -24.083 1.00 74.12  ? 129 ASP   B CA  1 
ATOM   1186 C C   . ASP   B 2 120 ? -8.449  3.927   -24.411 1.00 72.47  ? 129 ASP   B C   1 
ATOM   1187 O O   . ASP   B 2 120 ? -8.679  4.225   -25.579 1.00 72.84  ? 129 ASP   B O   1 
ATOM   1188 C CB  . ASP   B 2 120 ? -6.048  3.241   -24.331 1.00 77.54  ? 129 ASP   B CB  1 
ATOM   1189 C CG  . ASP   B 2 120 ? -5.420  3.949   -23.131 1.00 85.16  ? 129 ASP   B CG  1 
ATOM   1190 O OD1 . ASP   B 2 120 ? -6.182  4.544   -22.316 1.00 86.12  ? 129 ASP   B OD1 1 
ATOM   1191 O OD2 . ASP   B 2 120 ? -4.172  3.895   -22.994 1.00 88.52  ? 129 ASP   B OD2 1 
ATOM   1192 N N   . TYR   B 2 121 ? -8.991  4.556   -23.379 1.00 70.68  ? 130 TYR   B N   1 
ATOM   1193 C CA  . TYR   B 2 121 ? -9.939  5.652   -23.518 1.00 69.85  ? 130 TYR   B CA  1 
ATOM   1194 C C   . TYR   B 2 121 ? -9.691  6.694   -22.410 1.00 68.86  ? 130 TYR   B C   1 
ATOM   1195 O O   . TYR   B 2 121 ? -9.099  6.362   -21.379 1.00 69.07  ? 130 TYR   B O   1 
ATOM   1196 C CB  . TYR   B 2 121 ? -11.382 5.110   -23.431 1.00 70.20  ? 130 TYR   B CB  1 
ATOM   1197 C CG  . TYR   B 2 121 ? -11.895 4.580   -24.744 1.00 71.16  ? 130 TYR   B CG  1 
ATOM   1198 C CD1 . TYR   B 2 121 ? -12.358 5.441   -25.729 1.00 72.18  ? 130 TYR   B CD1 1 
ATOM   1199 C CD2 . TYR   B 2 121 ? -11.869 3.222   -25.026 1.00 72.28  ? 130 TYR   B CD2 1 
ATOM   1200 C CE1 . TYR   B 2 121 ? -12.764 4.965   -26.969 1.00 73.60  ? 130 TYR   B CE1 1 
ATOM   1201 C CE2 . TYR   B 2 121 ? -12.291 2.731   -26.256 1.00 73.29  ? 130 TYR   B CE2 1 
ATOM   1202 C CZ  . TYR   B 2 121 ? -12.718 3.609   -27.232 1.00 74.78  ? 130 TYR   B CZ  1 
ATOM   1203 O OH  . TYR   B 2 121 ? -13.132 3.139   -28.453 1.00 76.89  ? 130 TYR   B OH  1 
ATOM   1204 N N   . PRO   B 2 122 ? -10.170 7.950   -22.571 1.00 67.31  ? 131 PRO   B N   1 
ATOM   1205 C CA  . PRO   B 2 122 ? -9.952  8.952   -21.511 1.00 65.40  ? 131 PRO   B CA  1 
ATOM   1206 C C   . PRO   B 2 122 ? -10.549 8.524   -20.173 1.00 63.10  ? 131 PRO   B C   1 
ATOM   1207 O O   . PRO   B 2 122 ? -11.504 7.746   -20.157 1.00 62.65  ? 131 PRO   B O   1 
ATOM   1208 C CB  . PRO   B 2 122 ? -10.659 10.194  -22.052 1.00 66.93  ? 131 PRO   B CB  1 
ATOM   1209 C CG  . PRO   B 2 122 ? -10.657 10.013  -23.578 1.00 68.13  ? 131 PRO   B CG  1 
ATOM   1210 C CD  . PRO   B 2 122 ? -10.857 8.528   -23.749 1.00 67.12  ? 131 PRO   B CD  1 
ATOM   1211 N N   . ALA   B 2 123 ? -9.970  9.012   -19.053 1.00 61.31  ? 132 ALA   B N   1 
ATOM   1212 C CA  . ALA   B 2 123 ? -10.408 8.729   -17.683 1.00 60.49  ? 132 ALA   B CA  1 
ATOM   1213 C C   . ALA   B 2 123 ? -11.936 8.867   -17.507 1.00 59.83  ? 132 ALA   B C   1 
ATOM   1214 O O   . ALA   B 2 123 ? -12.563 8.029   -16.842 1.00 59.00  ? 132 ALA   B O   1 
ATOM   1215 C CB  . ALA   B 2 123 ? -9.694  9.668   -16.718 1.00 60.39  ? 132 ALA   B CB  1 
ATOM   1216 N N   . GLY   B 2 124 ? -12.513 9.898   -18.151 1.00 58.96  ? 133 GLY   B N   1 
ATOM   1217 C CA  . GLY   B 2 124 ? -13.943 10.205  -18.115 1.00 58.13  ? 133 GLY   B CA  1 
ATOM   1218 C C   . GLY   B 2 124 ? -14.843 9.166   -18.759 1.00 57.03  ? 133 GLY   B C   1 
ATOM   1219 O O   . GLY   B 2 124 ? -16.070 9.271   -18.671 1.00 55.88  ? 133 GLY   B O   1 
ATOM   1220 N N   . THR   B 2 125 ? -14.245 8.148   -19.421 1.00 56.79  ? 134 THR   B N   1 
ATOM   1221 C CA  . THR   B 2 125 ? -14.997 7.033   -20.013 1.00 57.43  ? 134 THR   B CA  1 
ATOM   1222 C C   . THR   B 2 125 ? -15.311 5.934   -18.958 1.00 56.26  ? 134 THR   B C   1 
ATOM   1223 O O   . THR   B 2 125 ? -16.098 5.040   -19.253 1.00 56.15  ? 134 THR   B O   1 
ATOM   1224 C CB  . THR   B 2 125 ? -14.266 6.474   -21.259 1.00 60.19  ? 134 THR   B CB  1 
ATOM   1225 O OG1 . THR   B 2 125 ? -13.910 7.552   -22.129 1.00 61.45  ? 134 THR   B OG1 1 
ATOM   1226 C CG2 . THR   B 2 125 ? -15.102 5.468   -22.047 1.00 61.09  ? 134 THR   B CG2 1 
ATOM   1227 N N   . SER   B 2 126 ? -14.701 6.002   -17.734 1.00 55.64  ? 135 SER   B N   1 
ATOM   1228 C CA  . SER   B 2 126 ? -14.911 5.040   -16.637 1.00 55.26  ? 135 SER   B CA  1 
ATOM   1229 C C   . SER   B 2 126 ? -16.377 4.838   -16.308 1.00 54.34  ? 135 SER   B C   1 
ATOM   1230 O O   . SER   B 2 126 ? -17.086 5.803   -16.088 1.00 54.50  ? 135 SER   B O   1 
ATOM   1231 C CB  . SER   B 2 126 ? -14.214 5.512   -15.371 1.00 56.76  ? 135 SER   B CB  1 
ATOM   1232 O OG  . SER   B 2 126 ? -12.812 5.411   -15.518 1.00 59.39  ? 135 SER   B OG  1 
ATOM   1233 N N   . GLY   B 2 127 ? -16.809 3.590   -16.265 1.00 53.31  ? 136 GLY   B N   1 
ATOM   1234 C CA  . GLY   B 2 127 ? -18.190 3.218   -16.004 1.00 52.84  ? 136 GLY   B CA  1 
ATOM   1235 C C   . GLY   B 2 127 ? -18.915 2.736   -17.250 1.00 52.59  ? 136 GLY   B C   1 
ATOM   1236 O O   . GLY   B 2 127 ? -20.025 2.215   -17.148 1.00 52.32  ? 136 GLY   B O   1 
ATOM   1237 N N   . SER   B 2 128 ? -18.323 2.928   -18.458 1.00 52.60  ? 137 SER   B N   1 
ATOM   1238 C CA  . SER   B 2 128 ? -18.940 2.469   -19.702 1.00 53.48  ? 137 SER   B CA  1 
ATOM   1239 C C   . SER   B 2 128 ? -19.196 0.940   -19.652 1.00 54.53  ? 137 SER   B C   1 
ATOM   1240 O O   . SER   B 2 128 ? -18.332 0.176   -19.241 1.00 54.75  ? 137 SER   B O   1 
ATOM   1241 C CB  . SER   B 2 128 ? -18.060 2.823   -20.903 1.00 55.27  ? 137 SER   B CB  1 
ATOM   1242 O OG  . SER   B 2 128 ? -18.048 4.209   -21.204 1.00 56.95  ? 137 SER   B OG  1 
ATOM   1243 N N   . PRO   B 2 129 ? -20.387 0.489   -20.076 1.00 55.28  ? 138 PRO   B N   1 
ATOM   1244 C CA  . PRO   B 2 129 ? -20.689 -0.950  -20.021 1.00 55.57  ? 138 PRO   B CA  1 
ATOM   1245 C C   . PRO   B 2 129 ? -20.089 -1.809  -21.123 1.00 57.42  ? 138 PRO   B C   1 
ATOM   1246 O O   . PRO   B 2 129 ? -19.925 -1.401  -22.293 1.00 56.86  ? 138 PRO   B O   1 
ATOM   1247 C CB  . PRO   B 2 129 ? -22.207 -0.983  -20.123 1.00 55.82  ? 138 PRO   B CB  1 
ATOM   1248 C CG  . PRO   B 2 129 ? -22.534 0.220   -20.994 1.00 55.91  ? 138 PRO   B CG  1 
ATOM   1249 C CD  . PRO   B 2 129 ? -21.532 1.276   -20.588 1.00 54.29  ? 138 PRO   B CD  1 
ATOM   1250 N N   . ILE   B 2 130 ? -19.794 -3.048  -20.732 1.00 58.68  ? 139 ILE   B N   1 
ATOM   1251 C CA  . ILE   B 2 130 ? -19.284 -4.087  -21.603 1.00 59.56  ? 139 ILE   B CA  1 
ATOM   1252 C C   . ILE   B 2 130 ? -20.430 -5.081  -21.753 1.00 60.50  ? 139 ILE   B C   1 
ATOM   1253 O O   . ILE   B 2 130 ? -21.106 -5.411  -20.772 1.00 59.56  ? 139 ILE   B O   1 
ATOM   1254 C CB  . ILE   B 2 130 ? -18.029 -4.708  -21.013 1.00 60.37  ? 139 ILE   B CB  1 
ATOM   1255 C CG1 . ILE   B 2 130 ? -16.947 -3.643  -20.828 1.00 61.12  ? 139 ILE   B CG1 1 
ATOM   1256 C CG2 . ILE   B 2 130 ? -17.537 -5.884  -21.876 1.00 61.06  ? 139 ILE   B CG2 1 
ATOM   1257 C CD1 . ILE   B 2 130 ? -15.859 -4.130  -19.908 1.00 62.43  ? 139 ILE   B CD1 1 
ATOM   1258 N N   . LEU   B 2 131 ? -20.736 -5.458  -23.006 1.00 61.66  ? 140 LEU   B N   1 
ATOM   1259 C CA  . LEU   B 2 131 ? -21.910 -6.282  -23.275 1.00 63.61  ? 140 LEU   B CA  1 
ATOM   1260 C C   . LEU   B 2 131 ? -21.662 -7.582  -24.025 1.00 64.43  ? 140 LEU   B C   1 
ATOM   1261 O O   . LEU   B 2 131 ? -20.711 -7.693  -24.787 1.00 64.77  ? 140 LEU   B O   1 
ATOM   1262 C CB  . LEU   B 2 131 ? -22.996 -5.479  -24.027 1.00 64.65  ? 140 LEU   B CB  1 
ATOM   1263 C CG  . LEU   B 2 131 ? -22.771 -3.997  -24.289 1.00 66.76  ? 140 LEU   B CG  1 
ATOM   1264 C CD1 . LEU   B 2 131 ? -23.524 -3.554  -25.499 1.00 66.84  ? 140 LEU   B CD1 1 
ATOM   1265 C CD2 . LEU   B 2 131 ? -23.113 -3.172  -23.046 1.00 67.71  ? 140 LEU   B CD2 1 
ATOM   1266 N N   . ASP   B 2 132 ? -22.552 -8.565  -23.818 1.00 64.87  ? 141 ASP   B N   1 
ATOM   1267 C CA  . ASP   B 2 132 ? -22.508 -9.840  -24.538 1.00 65.98  ? 141 ASP   B CA  1 
ATOM   1268 C C   . ASP   B 2 132 ? -23.370 -9.746  -25.841 1.00 67.62  ? 141 ASP   B C   1 
ATOM   1269 O O   . ASP   B 2 132 ? -24.011 -8.717  -26.064 1.00 68.27  ? 141 ASP   B O   1 
ATOM   1270 C CB  . ASP   B 2 132 ? -22.928 -11.005 -23.614 1.00 66.02  ? 141 ASP   B CB  1 
ATOM   1271 C CG  . ASP   B 2 132 ? -24.395 -11.057 -23.239 1.00 68.00  ? 141 ASP   B CG  1 
ATOM   1272 O OD1 . ASP   B 2 132 ? -25.146 -10.203 -23.693 1.00 67.44  ? 141 ASP   B OD1 1 
ATOM   1273 O OD2 . ASP   B 2 132 ? -24.779 -11.962 -22.491 1.00 70.58  ? 141 ASP   B OD2 1 
ATOM   1274 N N   . LYS   B 2 133 ? -23.419 -10.793 -26.675 1.00 68.69  ? 142 LYS   B N   1 
ATOM   1275 C CA  . LYS   B 2 133 ? -24.164 -10.745 -27.951 1.00 70.30  ? 142 LYS   B CA  1 
ATOM   1276 C C   . LYS   B 2 133 ? -25.671 -10.572 -27.801 1.00 70.82  ? 142 LYS   B C   1 
ATOM   1277 O O   . LYS   B 2 133 ? -26.331 -10.214 -28.779 1.00 70.92  ? 142 LYS   B O   1 
ATOM   1278 C CB  . LYS   B 2 133 ? -23.852 -11.941 -28.852 1.00 74.08  ? 142 LYS   B CB  1 
ATOM   1279 C CG  . LYS   B 2 133 ? -22.432 -11.885 -29.408 1.00 81.59  ? 142 LYS   B CG  1 
ATOM   1280 C CD  . LYS   B 2 133 ? -22.005 -13.147 -30.169 1.00 88.32  ? 142 LYS   B CD  1 
ATOM   1281 C CE  . LYS   B 2 133 ? -20.593 -13.533 -29.800 1.00 93.29  ? 142 LYS   B CE  1 
ATOM   1282 N NZ  . LYS   B 2 133 ? -20.322 -14.964 -30.107 1.00 96.84  ? 142 LYS   B NZ  1 
ATOM   1283 N N   . CYS   B 2 134 ? -26.216 -10.763 -26.582 1.00 70.46  ? 143 CYS   B N   1 
ATOM   1284 C CA  . CYS   B 2 134 ? -27.638 -10.478 -26.350 1.00 70.38  ? 143 CYS   B CA  1 
ATOM   1285 C C   . CYS   B 2 134 ? -27.879 -9.064  -25.845 1.00 68.36  ? 143 CYS   B C   1 
ATOM   1286 O O   . CYS   B 2 134 ? -29.026 -8.736  -25.590 1.00 68.57  ? 143 CYS   B O   1 
ATOM   1287 C CB  . CYS   B 2 134 ? -28.274 -11.486 -25.405 1.00 72.87  ? 143 CYS   B CB  1 
ATOM   1288 S SG  . CYS   B 2 134 ? -27.945 -13.200 -25.837 1.00 81.55  ? 143 CYS   B SG  1 
ATOM   1289 N N   . GLY   B 2 135 ? -26.837 -8.256  -25.674 1.00 66.74  ? 144 GLY   B N   1 
ATOM   1290 C CA  . GLY   B 2 135 ? -26.983 -6.903  -25.151 1.00 66.04  ? 144 GLY   B CA  1 
ATOM   1291 C C   . GLY   B 2 135 ? -26.997 -6.834  -23.633 1.00 64.83  ? 144 GLY   B C   1 
ATOM   1292 O O   . GLY   B 2 135 ? -27.279 -5.776  -23.070 1.00 64.82  ? 144 GLY   B O   1 
ATOM   1293 N N   . ARG   B 2 136 ? -26.681 -7.947  -22.954 1.00 63.80  ? 145 ARG   B N   1 
ATOM   1294 C CA  . ARG   B 2 136 ? -26.621 -8.002  -21.488 1.00 63.48  ? 145 ARG   B CA  1 
ATOM   1295 C C   . ARG   B 2 136 ? -25.302 -7.442  -20.984 1.00 62.02  ? 145 ARG   B C   1 
ATOM   1296 O O   . ARG   B 2 136 ? -24.242 -7.782  -21.501 1.00 61.97  ? 145 ARG   B O   1 
ATOM   1297 C CB  . ARG   B 2 136 ? -26.819 -9.442  -20.973 1.00 65.30  ? 145 ARG   B CB  1 
ATOM   1298 C CG  . ARG   B 2 136 ? -28.208 -9.999  -21.263 1.00 70.15  ? 145 ARG   B CG  1 
ATOM   1299 C CD  . ARG   B 2 136 ? -28.380 -11.393 -20.718 1.00 75.98  ? 145 ARG   B CD  1 
ATOM   1300 N NE  . ARG   B 2 136 ? -27.477 -12.331 -21.381 1.00 81.90  ? 145 ARG   B NE  1 
ATOM   1301 C CZ  . ARG   B 2 136 ? -27.031 -13.461 -20.839 1.00 86.67  ? 145 ARG   B CZ  1 
ATOM   1302 N NH1 . ARG   B 2 136 ? -27.395 -13.806 -19.607 1.00 86.78  ? 145 ARG   B NH1 1 
ATOM   1303 N NH2 . ARG   B 2 136 ? -26.204 -14.247 -21.517 1.00 88.07  ? 145 ARG   B NH2 1 
ATOM   1304 N N   . VAL   B 2 137 ? -25.369 -6.558  -20.002 1.00 60.92  ? 146 VAL   B N   1 
ATOM   1305 C CA  . VAL   B 2 137 ? -24.194 -5.944  -19.395 1.00 59.91  ? 146 VAL   B CA  1 
ATOM   1306 C C   . VAL   B 2 137 ? -23.497 -6.985  -18.531 1.00 59.12  ? 146 VAL   B C   1 
ATOM   1307 O O   . VAL   B 2 137 ? -24.067 -7.484  -17.561 1.00 60.15  ? 146 VAL   B O   1 
ATOM   1308 C CB  . VAL   B 2 137 ? -24.596 -4.681  -18.592 1.00 60.43  ? 146 VAL   B CB  1 
ATOM   1309 C CG1 . VAL   B 2 137 ? -23.379 -4.004  -17.973 1.00 61.23  ? 146 VAL   B CG1 1 
ATOM   1310 C CG2 . VAL   B 2 137 ? -25.359 -3.699  -19.474 1.00 60.41  ? 146 VAL   B CG2 1 
ATOM   1311 N N   . ILE   B 2 138 ? -22.291 -7.360  -18.925 1.00 57.38  ? 147 ILE   B N   1 
ATOM   1312 C CA  . ILE   B 2 138 ? -21.464 -8.326  -18.208 1.00 56.45  ? 147 ILE   B CA  1 
ATOM   1313 C C   . ILE   B 2 138 ? -20.408 -7.648  -17.309 1.00 55.63  ? 147 ILE   B C   1 
ATOM   1314 O O   . ILE   B 2 138 ? -19.671 -8.344  -16.620 1.00 56.09  ? 147 ILE   B O   1 
ATOM   1315 C CB  . ILE   B 2 138 ? -20.811 -9.333  -19.200 1.00 56.43  ? 147 ILE   B CB  1 
ATOM   1316 C CG1 . ILE   B 2 138 ? -19.974 -8.585  -20.247 1.00 57.66  ? 147 ILE   B CG1 1 
ATOM   1317 C CG2 . ILE   B 2 138 ? -21.882 -10.196 -19.843 1.00 56.52  ? 147 ILE   B CG2 1 
ATOM   1318 C CD1 . ILE   B 2 138 ? -19.316 -9.450  -21.339 1.00 59.71  ? 147 ILE   B CD1 1 
ATOM   1319 N N   . GLY   B 2 139 ? -20.349 -6.317  -17.299 1.00 54.56  ? 148 GLY   B N   1 
ATOM   1320 C CA  . GLY   B 2 139 ? -19.405 -5.599  -16.458 1.00 54.40  ? 148 GLY   B CA  1 
ATOM   1321 C C   . GLY   B 2 139 ? -19.185 -4.168  -16.888 1.00 54.15  ? 148 GLY   B C   1 
ATOM   1322 O O   . GLY   B 2 139 ? -19.723 -3.734  -17.913 1.00 54.19  ? 148 GLY   B O   1 
ATOM   1323 N N   . LEU   B 2 140 ? -18.382 -3.425  -16.102 1.00 53.46  ? 149 LEU   B N   1 
ATOM   1324 C CA  . LEU   B 2 140 ? -18.066 -2.021  -16.361 1.00 53.23  ? 149 LEU   B CA  1 
ATOM   1325 C C   . LEU   B 2 140 ? -16.565 -1.786  -16.569 1.00 54.38  ? 149 LEU   B C   1 
ATOM   1326 O O   . LEU   B 2 140 ? -15.727 -2.433  -15.940 1.00 54.73  ? 149 LEU   B O   1 
ATOM   1327 C CB  . LEU   B 2 140 ? -18.571 -1.116  -15.237 1.00 52.29  ? 149 LEU   B CB  1 
ATOM   1328 C CG  . LEU   B 2 140 ? -20.052 -1.216  -14.834 1.00 52.55  ? 149 LEU   B CG  1 
ATOM   1329 C CD1 . LEU   B 2 140 ? -20.371 -0.222  -13.687 1.00 52.95  ? 149 LEU   B CD1 1 
ATOM   1330 C CD2 . LEU   B 2 140 ? -20.981 -1.021  -16.035 1.00 52.16  ? 149 LEU   B CD2 1 
ATOM   1331 N N   . TYR   B 2 141 ? -16.247 -0.843  -17.459 1.00 54.75  ? 150 TYR   B N   1 
ATOM   1332 C CA  . TYR   B 2 141 ? -14.898 -0.447  -17.846 1.00 55.43  ? 150 TYR   B CA  1 
ATOM   1333 C C   . TYR   B 2 141 ? -14.357 0.619   -16.932 1.00 55.05  ? 150 TYR   B C   1 
ATOM   1334 O O   . TYR   B 2 141 ? -15.123 1.479   -16.517 1.00 55.95  ? 150 TYR   B O   1 
ATOM   1335 C CB  . TYR   B 2 141 ? -14.974 0.125   -19.283 1.00 56.38  ? 150 TYR   B CB  1 
ATOM   1336 C CG  . TYR   B 2 141 ? -13.683 0.703   -19.838 1.00 58.15  ? 150 TYR   B CG  1 
ATOM   1337 C CD1 . TYR   B 2 141 ? -13.459 2.077   -19.849 1.00 59.49  ? 150 TYR   B CD1 1 
ATOM   1338 C CD2 . TYR   B 2 141 ? -12.709 -0.120  -20.394 1.00 59.27  ? 150 TYR   B CD2 1 
ATOM   1339 C CE1 . TYR   B 2 141 ? -12.292 2.616   -20.389 1.00 60.94  ? 150 TYR   B CE1 1 
ATOM   1340 C CE2 . TYR   B 2 141 ? -11.546 0.407   -20.958 1.00 60.46  ? 150 TYR   B CE2 1 
ATOM   1341 C CZ  . TYR   B 2 141 ? -11.335 1.779   -20.947 1.00 61.76  ? 150 TYR   B CZ  1 
ATOM   1342 O OH  . TYR   B 2 141 ? -10.183 2.318   -21.502 1.00 62.38  ? 150 TYR   B OH  1 
ATOM   1343 N N   . GLY   B 2 142 ? -13.056 0.610   -16.655 1.00 54.27  ? 151 GLY   B N   1 
ATOM   1344 C CA  . GLY   B 2 142 ? -12.475 1.673   -15.847 1.00 55.14  ? 151 GLY   B CA  1 
ATOM   1345 C C   . GLY   B 2 142 ? -11.602 1.295   -14.675 1.00 56.41  ? 151 GLY   B C   1 
ATOM   1346 O O   . GLY   B 2 142 ? -10.966 2.189   -14.114 1.00 57.20  ? 151 GLY   B O   1 
ATOM   1347 N N   . ASN   B 2 143 ? -11.551 0.008   -14.280 1.00 56.17  ? 152 ASN   B N   1 
ATOM   1348 C CA  . ASN   B 2 143 ? -10.614 -0.399  -13.229 1.00 57.90  ? 152 ASN   B CA  1 
ATOM   1349 C C   . ASN   B 2 143 ? -9.640  -1.390  -13.818 1.00 60.49  ? 152 ASN   B C   1 
ATOM   1350 O O   . ASN   B 2 143 ? -10.008 -2.527  -14.099 1.00 60.80  ? 152 ASN   B O   1 
ATOM   1351 C CB  . ASN   B 2 143 ? -11.282 -0.984  -11.983 1.00 57.25  ? 152 ASN   B CB  1 
ATOM   1352 C CG  . ASN   B 2 143 ? -10.350 -0.998  -10.779 1.00 57.75  ? 152 ASN   B CG  1 
ATOM   1353 O OD1 . ASN   B 2 143 ? -9.316  -0.302  -10.755 1.00 58.33  ? 152 ASN   B OD1 1 
ATOM   1354 N ND2 . ASN   B 2 143 ? -10.684 -1.796  -9.752  1.00 54.72  ? 152 ASN   B ND2 1 
ATOM   1355 N N   . GLY   B 2 144 ? -8.422  -0.943  -14.043 1.00 62.17  ? 153 GLY   B N   1 
ATOM   1356 C CA  . GLY   B 2 144 ? -7.419  -1.800  -14.645 1.00 64.83  ? 153 GLY   B CA  1 
ATOM   1357 C C   . GLY   B 2 144 ? -5.992  -1.422  -14.354 1.00 67.47  ? 153 GLY   B C   1 
ATOM   1358 O O   . GLY   B 2 144 ? -5.676  -0.901  -13.279 1.00 67.23  ? 153 GLY   B O   1 
ATOM   1359 N N   . VAL   B 2 145 ? -5.124  -1.678  -15.331 1.00 69.50  ? 154 VAL   B N   1 
ATOM   1360 C CA  . VAL   B 2 145 ? -3.695  -1.493  -15.151 1.00 72.31  ? 154 VAL   B CA  1 
ATOM   1361 C C   . VAL   B 2 145 ? -2.977  -1.003  -16.435 1.00 75.26  ? 154 VAL   B C   1 
ATOM   1362 O O   . VAL   B 2 145 ? -3.531  -1.059  -17.531 1.00 75.13  ? 154 VAL   B O   1 
ATOM   1363 C CB  . VAL   B 2 145 ? -3.136  -2.861  -14.646 1.00 73.01  ? 154 VAL   B CB  1 
ATOM   1364 C CG1 . VAL   B 2 145 ? -3.049  -3.877  -15.779 1.00 73.10  ? 154 VAL   B CG1 1 
ATOM   1365 C CG2 . VAL   B 2 145 ? -1.799  -2.703  -13.937 1.00 74.03  ? 154 VAL   B CG2 1 
ATOM   1366 N N   . VAL   B 2 146 ? -1.738  -0.515  -16.281 1.00 77.67  ? 155 VAL   B N   1 
ATOM   1367 C CA  . VAL   B 2 146 ? -0.904  -0.064  -17.383 1.00 80.33  ? 155 VAL   B CA  1 
ATOM   1368 C C   . VAL   B 2 146 ? 0.178   -1.117  -17.578 1.00 83.38  ? 155 VAL   B C   1 
ATOM   1369 O O   . VAL   B 2 146 ? 0.918   -1.411  -16.640 1.00 83.60  ? 155 VAL   B O   1 
ATOM   1370 C CB  . VAL   B 2 146 ? -0.311  1.321   -17.096 1.00 81.16  ? 155 VAL   B CB  1 
ATOM   1371 C CG1 . VAL   B 2 146 ? 0.705   1.697   -18.157 1.00 82.19  ? 155 VAL   B CG1 1 
ATOM   1372 C CG2 . VAL   B 2 146 ? -1.413  2.367   -17.021 1.00 81.70  ? 155 VAL   B CG2 1 
ATOM   1373 N N   . ILE   B 2 147 ? 0.244   -1.727  -18.772 1.00 85.49  ? 156 ILE   B N   1 
ATOM   1374 C CA  . ILE   B 2 147 ? 1.208   -2.799  -19.016 1.00 88.05  ? 156 ILE   B CA  1 
ATOM   1375 C C   . ILE   B 2 147 ? 2.579   -2.280  -19.498 1.00 90.27  ? 156 ILE   B C   1 
ATOM   1376 O O   . ILE   B 2 147 ? 2.710   -1.080  -19.740 1.00 90.39  ? 156 ILE   B O   1 
ATOM   1377 C CB  . ILE   B 2 147 ? 0.578   -3.846  -19.972 1.00 88.95  ? 156 ILE   B CB  1 
ATOM   1378 C CG1 . ILE   B 2 147 ? 0.187   -3.228  -21.317 1.00 89.56  ? 156 ILE   B CG1 1 
ATOM   1379 C CG2 . ILE   B 2 147 ? -0.622  -4.500  -19.302 1.00 89.99  ? 156 ILE   B CG2 1 
ATOM   1380 C CD1 . ILE   B 2 147 ? -0.294  -4.242  -22.348 1.00 90.44  ? 156 ILE   B CD1 1 
ATOM   1381 N N   . LYS   B 2 148 ? 3.609   -3.177  -19.614 1.00 91.70  ? 157 LYS   B N   1 
ATOM   1382 C CA  . LYS   B 2 148 ? 4.957   -2.842  -20.101 1.00 93.44  ? 157 LYS   B CA  1 
ATOM   1383 C C   . LYS   B 2 148 ? 4.956   -2.115  -21.464 1.00 94.91  ? 157 LYS   B C   1 
ATOM   1384 O O   . LYS   B 2 148 ? 5.941   -1.468  -21.822 1.00 95.73  ? 157 LYS   B O   1 
ATOM   1385 C CB  . LYS   B 2 148 ? 5.834   -4.098  -20.183 1.00 95.93  ? 157 LYS   B CB  1 
ATOM   1386 C CG  . LYS   B 2 148 ? 6.966   -4.121  -19.160 1.00 100.79 ? 157 LYS   B CG  1 
ATOM   1387 C CD  . LYS   B 2 148 ? 7.830   -5.375  -19.272 1.00 105.40 ? 157 LYS   B CD  1 
ATOM   1388 C CE  . LYS   B 2 148 ? 8.541   -5.485  -20.603 1.00 109.09 ? 157 LYS   B CE  1 
ATOM   1389 N NZ  . LYS   B 2 148 ? 9.461   -4.340  -20.848 1.00 111.09 ? 157 LYS   B NZ  1 
ATOM   1390 N N   . ASN   B 2 149 ? 3.862   -2.240  -22.228 1.00 94.90  ? 158 ASN   B N   1 
ATOM   1391 C CA  . ASN   B 2 149 ? 3.654   -1.564  -23.513 1.00 95.01  ? 158 ASN   B CA  1 
ATOM   1392 C C   . ASN   B 2 149 ? 3.429   -0.045  -23.331 1.00 94.30  ? 158 ASN   B C   1 
ATOM   1393 O O   . ASN   B 2 149 ? 3.598   0.726   -24.282 1.00 94.70  ? 158 ASN   B O   1 
ATOM   1394 C CB  . ASN   B 2 149 ? 2.347   -2.082  -24.137 1.00 97.18  ? 158 ASN   B CB  1 
ATOM   1395 C CG  . ASN   B 2 149 ? 2.445   -3.227  -25.104 1.00 102.07 ? 158 ASN   B CG  1 
ATOM   1396 O OD1 . ASN   B 2 149 ? 3.527   -3.594  -25.585 1.00 104.45 ? 158 ASN   B OD1 1 
ATOM   1397 N ND2 . ASN   B 2 149 ? 1.290   -3.798  -25.434 1.00 102.39 ? 158 ASN   B ND2 1 
ATOM   1398 N N   . GLY   B 2 150 ? 2.922   0.341   -22.160 1.00 92.83  ? 159 GLY   B N   1 
ATOM   1399 C CA  . GLY   B 2 150 ? 2.489   1.696   -21.858 1.00 91.82  ? 159 GLY   B CA  1 
ATOM   1400 C C   . GLY   B 2 150 ? 0.979   1.841   -22.003 1.00 90.26  ? 159 GLY   B C   1 
ATOM   1401 O O   . GLY   B 2 150 ? 0.392   2.818   -21.516 1.00 90.86  ? 159 GLY   B O   1 
ATOM   1402 N N   . SER   B 2 151 ? 0.326   0.860   -22.672 1.00 87.89  ? 160 SER   B N   1 
ATOM   1403 C CA  . SER   B 2 151 ? -1.114  0.862   -22.892 1.00 85.97  ? 160 SER   B CA  1 
ATOM   1404 C C   . SER   B 2 151 ? -1.909  0.433   -21.645 1.00 82.14  ? 160 SER   B C   1 
ATOM   1405 O O   . SER   B 2 151 ? -1.363  -0.144  -20.700 1.00 81.84  ? 160 SER   B O   1 
ATOM   1406 C CB  . SER   B 2 151 ? -1.471  0.002   -24.102 1.00 88.30  ? 160 SER   B CB  1 
ATOM   1407 O OG  . SER   B 2 151 ? -0.971  -1.312  -23.926 1.00 91.74  ? 160 SER   B OG  1 
ATOM   1408 N N   . TYR   B 2 152 ? -3.209  0.750   -21.660 1.00 78.90  ? 161 TYR   B N   1 
ATOM   1409 C CA  . TYR   B 2 152 ? -4.149  0.496   -20.585 1.00 75.81  ? 161 TYR   B CA  1 
ATOM   1410 C C   . TYR   B 2 152 ? -5.018  -0.739  -20.842 1.00 72.70  ? 161 TYR   B C   1 
ATOM   1411 O O   . TYR   B 2 152 ? -5.528  -0.918  -21.937 1.00 72.49  ? 161 TYR   B O   1 
ATOM   1412 C CB  . TYR   B 2 152 ? -5.026  1.744   -20.403 1.00 75.44  ? 161 TYR   B CB  1 
ATOM   1413 C CG  . TYR   B 2 152 ? -5.981  1.643   -19.241 1.00 75.33  ? 161 TYR   B CG  1 
ATOM   1414 C CD1 . TYR   B 2 152 ? -5.517  1.650   -17.936 1.00 75.78  ? 161 TYR   B CD1 1 
ATOM   1415 C CD2 . TYR   B 2 152 ? -7.347  1.531   -19.448 1.00 75.80  ? 161 TYR   B CD2 1 
ATOM   1416 C CE1 . TYR   B 2 152 ? -6.384  1.524   -16.863 1.00 76.48  ? 161 TYR   B CE1 1 
ATOM   1417 C CE2 . TYR   B 2 152 ? -8.224  1.396   -18.386 1.00 76.73  ? 161 TYR   B CE2 1 
ATOM   1418 C CZ  . TYR   B 2 152 ? -7.737  1.397   -17.093 1.00 77.47  ? 161 TYR   B CZ  1 
ATOM   1419 O OH  . TYR   B 2 152 ? -8.592  1.288   -16.039 1.00 79.08  ? 161 TYR   B OH  1 
ATOM   1420 N N   . VAL   B 2 153 ? -5.182  -1.594  -19.829 1.00 70.24  ? 162 VAL   B N   1 
ATOM   1421 C CA  . VAL   B 2 153 ? -6.003  -2.798  -19.932 1.00 68.49  ? 162 VAL   B CA  1 
ATOM   1422 C C   . VAL   B 2 153 ? -6.965  -2.784  -18.735 1.00 66.09  ? 162 VAL   B C   1 
ATOM   1423 O O   . VAL   B 2 153 ? -6.522  -2.758  -17.598 1.00 65.74  ? 162 VAL   B O   1 
ATOM   1424 C CB  . VAL   B 2 153 ? -5.119  -4.088  -19.993 1.00 69.35  ? 162 VAL   B CB  1 
ATOM   1425 C CG1 . VAL   B 2 153 ? -5.959  -5.360  -19.908 1.00 69.73  ? 162 VAL   B CG1 1 
ATOM   1426 C CG2 . VAL   B 2 153 ? -4.255  -4.106  -21.256 1.00 70.04  ? 162 VAL   B CG2 1 
ATOM   1427 N N   . SER   B 2 154 ? -8.273  -2.725  -18.990 1.00 64.49  ? 163 SER   B N   1 
ATOM   1428 C CA  . SER   B 2 154 ? -9.262  -2.664  -17.912 1.00 63.18  ? 163 SER   B CA  1 
ATOM   1429 C C   . SER   B 2 154 ? -9.857  -4.019  -17.612 1.00 61.54  ? 163 SER   B C   1 
ATOM   1430 O O   . SER   B 2 154 ? -10.157 -4.749  -18.537 1.00 61.49  ? 163 SER   B O   1 
ATOM   1431 C CB  . SER   B 2 154 ? -10.383 -1.693  -18.286 1.00 63.25  ? 163 SER   B CB  1 
ATOM   1432 O OG  . SER   B 2 154 ? -11.594 -1.869  -17.563 1.00 62.82  ? 163 SER   B OG  1 
ATOM   1433 N N   . ALA   B 2 155 ? -10.169 -4.288  -16.341 1.00 59.58  ? 164 ALA   B N   1 
ATOM   1434 C CA  . ALA   B 2 155 ? -10.892 -5.493  -15.985 1.00 58.39  ? 164 ALA   B CA  1 
ATOM   1435 C C   . ALA   B 2 155 ? -12.355 -5.370  -16.472 1.00 57.25  ? 164 ALA   B C   1 
ATOM   1436 O O   . ALA   B 2 155 ? -12.866 -4.272  -16.725 1.00 56.56  ? 164 ALA   B O   1 
ATOM   1437 C CB  . ALA   B 2 155 ? -10.879 -5.672  -14.468 1.00 58.64  ? 164 ALA   B CB  1 
ATOM   1438 N N   . ILE   B 2 156 ? -13.016 -6.505  -16.637 1.00 56.95  ? 165 ILE   B N   1 
ATOM   1439 C CA  . ILE   B 2 156 ? -14.441 -6.530  -16.886 1.00 56.80  ? 165 ILE   B CA  1 
ATOM   1440 C C   . ILE   B 2 156 ? -14.974 -6.656  -15.440 1.00 55.80  ? 165 ILE   B C   1 
ATOM   1441 O O   . ILE   B 2 156 ? -14.914 -7.747  -14.866 1.00 55.25  ? 165 ILE   B O   1 
ATOM   1442 C CB  . ILE   B 2 156 ? -14.864 -7.698  -17.799 1.00 57.12  ? 165 ILE   B CB  1 
ATOM   1443 C CG1 . ILE   B 2 156 ? -14.256 -7.480  -19.209 1.00 57.65  ? 165 ILE   B CG1 1 
ATOM   1444 C CG2 . ILE   B 2 156 ? -16.412 -7.773  -17.876 1.00 57.72  ? 165 ILE   B CG2 1 
ATOM   1445 C CD1 . ILE   B 2 156 ? -14.648 -8.479  -20.232 1.00 58.27  ? 165 ILE   B CD1 1 
ATOM   1446 N N   . THR   B 2 157 ? -15.381 -5.509  -14.819 1.00 55.40  ? 166 THR   B N   1 
ATOM   1447 C CA  . THR   B 2 157 ? -15.823 -5.513  -13.412 1.00 54.84  ? 166 THR   B CA  1 
ATOM   1448 C C   . THR   B 2 157 ? -17.311 -5.703  -13.285 1.00 54.68  ? 166 THR   B C   1 
ATOM   1449 O O   . THR   B 2 157 ? -18.071 -4.842  -13.702 1.00 55.41  ? 166 THR   B O   1 
ATOM   1450 C CB  . THR   B 2 157 ? -15.410 -4.240  -12.686 1.00 54.79  ? 166 THR   B CB  1 
ATOM   1451 O OG1 . THR   B 2 157 ? -14.011 -4.033  -12.817 1.00 55.01  ? 166 THR   B OG1 1 
ATOM   1452 C CG2 . THR   B 2 157 ? -15.784 -4.276  -11.227 1.00 55.17  ? 166 THR   B CG2 1 
ATOM   1453 N N   . GLN   B 2 158 ? -17.728 -6.794  -12.675 1.00 53.88  ? 167 GLN   B N   1 
ATOM   1454 C CA  . GLN   B 2 158 ? -19.132 -7.090  -12.473 1.00 54.53  ? 167 GLN   B CA  1 
ATOM   1455 C C   . GLN   B 2 158 ? -19.436 -7.163  -10.960 1.00 55.88  ? 167 GLN   B C   1 
ATOM   1456 O O   . GLN   B 2 158 ? -18.606 -7.616  -10.183 1.00 54.71  ? 167 GLN   B O   1 
ATOM   1457 C CB  . GLN   B 2 158 ? -19.489 -8.426  -13.162 1.00 55.12  ? 167 GLN   B CB  1 
ATOM   1458 C CG  . GLN   B 2 158 ? -20.975 -8.803  -13.137 1.00 56.82  ? 167 GLN   B CG  1 
ATOM   1459 C CD  . GLN   B 2 158 ? -21.914 -7.724  -13.671 1.00 57.70  ? 167 GLN   B CD  1 
ATOM   1460 O OE1 . GLN   B 2 158 ? -22.052 -6.640  -13.093 1.00 57.43  ? 167 GLN   B OE1 1 
ATOM   1461 N NE2 . GLN   B 2 158 ? -22.625 -8.011  -14.745 1.00 55.70  ? 167 GLN   B NE2 1 
ATOM   1462 N N   . GLY   B 2 159 ? -20.610 -6.692  -10.570 1.00 57.61  ? 168 GLY   B N   1 
ATOM   1463 C CA  . GLY   B 2 159 ? -21.050 -6.777  -9.197  1.00 60.69  ? 168 GLY   B CA  1 
ATOM   1464 C C   . GLY   B 2 159 ? -21.758 -8.091  -8.935  1.00 64.71  ? 168 GLY   B C   1 
ATOM   1465 O O   . GLY   B 2 159 ? -21.862 -8.964  -9.809  1.00 65.10  ? 168 GLY   B O   1 
ATOM   1466 N N   . LYS   B 2 160 ? -22.271 -8.229  -7.724  1.00 67.28  ? 169 LYS   B N   1 
ATOM   1467 C CA  . LYS   B 2 160 ? -23.012 -9.412  -7.337  1.00 70.29  ? 169 LYS   B CA  1 
ATOM   1468 C C   . LYS   B 2 160 ? -24.462 -8.979  -7.097  1.00 72.51  ? 169 LYS   B C   1 
ATOM   1469 O O   . LYS   B 2 160 ? -24.711 -8.008  -6.387  1.00 72.94  ? 169 LYS   B O   1 
ATOM   1470 C CB  . LYS   B 2 160 ? -22.384 -10.052 -6.085  1.00 73.24  ? 169 LYS   B CB  1 
ATOM   1471 C CG  . LYS   B 2 160 ? -23.105 -11.294 -5.596  1.00 79.54  ? 169 LYS   B CG  1 
ATOM   1472 C CD  . LYS   B 2 160 ? -22.305 -12.017 -4.513  1.00 85.63  ? 169 LYS   B CD  1 
ATOM   1473 C CE  . LYS   B 2 160 ? -22.863 -13.389 -4.188  1.00 90.47  ? 169 LYS   B CE  1 
ATOM   1474 N NZ  . LYS   B 2 160 ? -24.028 -13.317 -3.264  1.00 93.47  ? 169 LYS   B NZ  1 
ATOM   1475 N N   . ARG   B 2 161 ? -25.409 -9.655  -7.746  1.00 73.69  ? 170 ARG   B N   1 
ATOM   1476 C CA  . ARG   B 2 161 ? -26.823 -9.373  -7.565  1.00 75.31  ? 170 ARG   B CA  1 
ATOM   1477 C C   . ARG   B 2 161 ? -27.318 -10.302 -6.440  1.00 77.46  ? 170 ARG   B C   1 
ATOM   1478 O O   . ARG   B 2 161 ? -27.165 -11.518 -6.548  1.00 77.42  ? 170 ARG   B O   1 
ATOM   1479 C CB  . ARG   B 2 161 ? -27.587 -9.624  -8.890  1.00 76.00  ? 170 ARG   B CB  1 
ATOM   1480 C CG  . ARG   B 2 161 ? -29.100 -9.734  -8.746  1.00 77.82  ? 170 ARG   B CG  1 
ATOM   1481 C CD  . ARG   B 2 161 ? -29.822 -9.490  -10.054 1.00 80.33  ? 170 ARG   B CD  1 
ATOM   1482 N NE  . ARG   B 2 161 ? -31.254 -9.261  -9.853  1.00 82.68  ? 170 ARG   B NE  1 
ATOM   1483 C CZ  . ARG   B 2 161 ? -32.037 -8.600  -10.701 1.00 84.66  ? 170 ARG   B CZ  1 
ATOM   1484 N NH1 . ARG   B 2 161 ? -31.533 -8.075  -11.814 1.00 83.22  ? 170 ARG   B NH1 1 
ATOM   1485 N NH2 . ARG   B 2 161 ? -33.328 -8.442  -10.434 1.00 84.79  ? 170 ARG   B NH2 1 
ATOM   1486 N N   . GLU   B 2 162 ? -27.859 -9.740  -5.353  1.00 78.98  ? 171 GLU   B N   1 
ATOM   1487 C CA  . GLU   B 2 162 ? -28.382 -10.562 -4.259  1.00 81.29  ? 171 GLU   B CA  1 
ATOM   1488 C C   . GLU   B 2 162 ? -29.762 -11.143 -4.610  1.00 82.21  ? 171 GLU   B C   1 
ATOM   1489 O O   . GLU   B 2 162 ? -30.202 -12.117 -3.998  1.00 82.81  ? 171 GLU   B O   1 
ATOM   1490 C CB  . GLU   B 2 162 ? -28.438 -9.768  -2.947  1.00 85.10  ? 171 GLU   B CB  1 
ATOM   1491 C CG  . GLU   B 2 162 ? -27.104 -9.710  -2.221  1.00 92.60  ? 171 GLU   B CG  1 
ATOM   1492 C CD  . GLU   B 2 162 ? -26.727 -10.997 -1.512  1.00 102.20 ? 171 GLU   B CD  1 
ATOM   1493 O OE1 . GLU   B 2 162 ? -27.102 -11.147 -0.325  1.00 105.12 ? 171 GLU   B OE1 1 
ATOM   1494 O OE2 . GLU   B 2 162 ? -26.058 -11.853 -2.137  1.00 104.38 ? 171 GLU   B OE2 1 
HETATM 1495 S S   . DMS   C 3 .   ? -18.790 12.042  -0.320  1.00 85.93  ? 201 DMS   B S   1 
HETATM 1496 O O   . DMS   C 3 .   ? -19.447 10.724  -0.478  1.00 85.81  ? 201 DMS   B O   1 
HETATM 1497 C C1  . DMS   C 3 .   ? -19.873 13.250  -1.005  1.00 86.01  ? 201 DMS   B C1  1 
HETATM 1498 C C2  . DMS   C 3 .   ? -17.627 12.170  -1.651  1.00 85.62  ? 201 DMS   B C2  1 
HETATM 1499 N N1  . A1BGW D 4 .   ? -7.686  4.792   -17.205 0.95 60.15  ? 202 A1BGW B N1  1 
HETATM 1500 N N3  . A1BGW D 4 .   ? -8.800  4.500   -12.401 0.95 58.93  ? 202 A1BGW B N3  1 
HETATM 1501 C C4  . A1BGW D 4 .   ? -10.043 4.306   -16.498 0.95 59.20  ? 202 A1BGW B C4  1 
HETATM 1502 C C5  . A1BGW D 4 .   ? -9.176  5.590   -14.617 0.95 58.95  ? 202 A1BGW B C5  1 
HETATM 1503 C C6  . A1BGW D 4 .   ? -8.897  5.631   -13.177 0.95 59.08  ? 202 A1BGW B C6  1 
HETATM 1504 C C7  . A1BGW D 4 .   ? -8.606  4.914   -11.108 0.95 59.16  ? 202 A1BGW B C7  1 
HETATM 1505 C C8  . A1BGW D 4 .   ? -8.274  4.099   -9.897  0.95 59.19  ? 202 A1BGW B C8  1 
HETATM 1506 C C10 . A1BGW D 4 .   ? -9.976  3.338   -8.055  0.95 58.93  ? 202 A1BGW B C10 1 
HETATM 1507 C C13 . A1BGW D 4 .   ? -8.757  6.705   -12.315 0.95 59.40  ? 202 A1BGW B C13 1 
HETATM 1508 C C15 . A1BGW D 4 .   ? -9.160  4.825   -18.874 0.95 59.64  ? 202 A1BGW B C15 1 
HETATM 1509 C C1  . A1BGW D 4 .   ? -5.587  5.301   -18.435 0.95 61.16  ? 202 A1BGW B C1  1 
HETATM 1510 C C2  . A1BGW D 4 .   ? -7.045  5.053   -18.329 0.95 60.27  ? 202 A1BGW B C2  1 
HETATM 1511 C C3  . A1BGW D 4 .   ? -9.022  4.652   -17.532 0.95 59.67  ? 202 A1BGW B C3  1 
HETATM 1512 N N2  . A1BGW D 4 .   ? -9.560  4.421   -15.131 0.95 58.97  ? 202 A1BGW B N2  1 
HETATM 1513 O O1  . A1BGW D 4 .   ? -9.059  6.598   -15.311 0.95 58.94  ? 202 A1BGW B O1  1 
HETATM 1514 C C9  . A1BGW D 4 .   ? -9.164  4.469   -8.688  0.95 59.25  ? 202 A1BGW B C9  1 
HETATM 1515 C C11 . A1BGW D 4 .   ? -9.273  2.006   -8.181  0.95 58.70  ? 202 A1BGW B C11 1 
HETATM 1516 N N4  . A1BGW D 4 .   ? -9.104  1.719   -9.608  0.95 58.66  ? 202 A1BGW B N4  1 
HETATM 1517 C C12 . A1BGW D 4 .   ? -8.123  2.617   -10.237 0.95 58.87  ? 202 A1BGW B C12 1 
HETATM 1518 N N5  . A1BGW D 4 .   ? -8.533  6.255   -11.082 0.95 59.45  ? 202 A1BGW B N5  1 
HETATM 1519 C C14 . A1BGW D 4 .   ? -8.823  8.175   -12.559 0.95 59.67  ? 202 A1BGW B C14 1 
HETATM 1520 N N6  . A1BGW D 4 .   ? -7.907  5.096   -19.359 0.95 59.94  ? 202 A1BGW B N6  1 
HETATM 1521 S S   . DMS   E 3 .   ? -22.917 -14.082 -25.720 1.00 108.00 ? 203 DMS   B S   1 
HETATM 1522 O O   . DMS   E 3 .   ? -21.586 -13.453 -25.575 1.00 107.86 ? 203 DMS   B O   1 
HETATM 1523 C C1  . DMS   E 3 .   ? -22.946 -15.384 -24.519 1.00 108.10 ? 203 DMS   B C1  1 
HETATM 1524 C C2  . DMS   E 3 .   ? -22.817 -15.087 -27.176 1.00 108.12 ? 203 DMS   B C2  1 
HETATM 1525 S S   . SO4   F 5 .   ? -21.272 14.152  -33.676 1.00 149.36 ? 204 SO4   B S   1 
HETATM 1526 O O1  . SO4   F 5 .   ? -19.843 13.992  -33.393 1.00 149.38 ? 204 SO4   B O1  1 
HETATM 1527 O O2  . SO4   F 5 .   ? -21.837 15.141  -32.763 1.00 149.47 ? 204 SO4   B O2  1 
HETATM 1528 O O3  . SO4   F 5 .   ? -21.456 14.611  -35.051 1.00 149.20 ? 204 SO4   B O3  1 
HETATM 1529 O O4  . SO4   F 5 .   ? -21.957 12.870  -33.486 1.00 149.39 ? 204 SO4   B O4  1 
HETATM 1530 S S   . DMS   G 3 .   ? -16.857 -14.325 -30.764 1.00 128.63 ? 205 DMS   B S   1 
HETATM 1531 O O   . DMS   G 3 .   ? -17.812 -15.439 -30.799 1.00 128.64 ? 205 DMS   B O   1 
HETATM 1532 C C1  . DMS   G 3 .   ? -17.038 -13.506 -32.328 1.00 128.52 ? 205 DMS   B C1  1 
HETATM 1533 C C2  . DMS   G 3 .   ? -15.268 -15.074 -31.005 1.00 128.61 ? 205 DMS   B C2  1 
HETATM 1534 S S   . DMS   H 3 .   ? -29.275 -6.674  -18.650 1.00 118.21 ? 206 DMS   B S   1 
HETATM 1535 O O   . DMS   H 3 .   ? -27.859 -6.311  -18.742 1.00 117.93 ? 206 DMS   B O   1 
HETATM 1536 C C1  . DMS   H 3 .   ? -29.356 -8.401  -18.267 1.00 118.13 ? 206 DMS   B C1  1 
HETATM 1537 C C2  . DMS   H 3 .   ? -29.936 -6.658  -20.303 1.00 118.15 ? 206 DMS   B C2  1 
HETATM 1538 O O   . HOH   I 6 .   ? -29.481 15.645  -15.104 1.00 78.21  ? 101 HOH   A O   1 
HETATM 1539 O O   . HOH   I 6 .   ? -4.834  -14.617 -25.296 1.00 55.54  ? 102 HOH   A O   1 
HETATM 1540 O O   . HOH   I 6 .   ? -6.984  -8.955  -3.169  1.00 54.96  ? 103 HOH   A O   1 
HETATM 1541 O O   . HOH   I 6 .   ? -2.267  -4.010  -6.350  1.00 61.45  ? 104 HOH   A O   1 
HETATM 1542 O O   . HOH   I 6 .   ? -26.742 1.453   -29.777 1.00 91.89  ? 105 HOH   A O   1 
HETATM 1543 O O   . HOH   I 6 .   ? -28.588 -6.152  -28.137 1.00 66.65  ? 106 HOH   A O   1 
HETATM 1544 O O   . HOH   I 6 .   ? -31.067 12.949  -16.665 1.00 72.21  ? 107 HOH   A O   1 
HETATM 1545 O O   . HOH   I 6 .   ? -31.192 0.389   -23.284 1.00 64.28  ? 108 HOH   A O   1 
HETATM 1546 O O   . HOH   I 6 .   ? -22.136 15.433  -6.181  1.00 62.18  ? 109 HOH   A O   1 
HETATM 1547 O O   . HOH   I 6 .   ? -22.511 -0.938  -36.011 1.00 86.86  ? 110 HOH   A O   1 
HETATM 1548 O O   . HOH   I 6 .   ? -3.727  -0.413  -0.078  1.00 66.66  ? 111 HOH   A O   1 
HETATM 1549 O O   . HOH   J 6 .   ? -26.281 -8.024  -16.623 1.00 51.09  ? 301 HOH   B O   1 
HETATM 1550 O O   . HOH   J 6 .   ? -6.684  -0.490  -10.965 1.00 50.09  ? 302 HOH   B O   1 
HETATM 1551 O O   . HOH   J 6 .   ? -22.368 -13.757 -21.434 1.00 62.18  ? 303 HOH   B O   1 
HETATM 1552 O O   . HOH   J 6 .   ? -7.693  1.976   -13.643 1.00 50.45  ? 304 HOH   B O   1 
HETATM 1553 O O   . HOH   J 6 .   ? -6.975  -10.716 -5.466  1.00 67.24  ? 305 HOH   B O   1 
HETATM 1554 O O   . HOH   J 6 .   ? -34.107 1.874   -15.435 1.00 62.38  ? 306 HOH   B O   1 
HETATM 1555 O O   . HOH   J 6 .   ? -9.557  -6.613  -25.486 1.00 67.14  ? 307 HOH   B O   1 
HETATM 1556 O O   . HOH   J 6 .   ? -13.288 -2.283  -14.734 1.00 52.50  ? 308 HOH   B O   1 
HETATM 1557 O O   . HOH   J 6 .   ? -16.874 -7.372  -8.122  1.00 76.77  ? 309 HOH   B O   1 
HETATM 1558 O O   . HOH   J 6 .   ? -12.631 -3.655  -10.003 1.00 56.64  ? 310 HOH   B O   1 
HETATM 1559 O O   . HOH   J 6 .   ? -20.772 -7.011  -5.583  1.00 67.79  ? 311 HOH   B O   1 
HETATM 1560 O O   . HOH   J 6 .   ? -18.165 -10.642 -16.597 1.00 56.10  ? 312 HOH   B O   1 
HETATM 1561 O O   . HOH   J 6 .   ? -12.412 2.312   -5.674  1.00 50.85  ? 313 HOH   B O   1 
HETATM 1562 O O   . HOH   J 6 .   ? -15.933 8.932   -30.729 1.00 73.95  ? 314 HOH   B O   1 
HETATM 1563 O O   . HOH   J 6 .   ? -16.638 -14.624 -16.427 1.00 60.89  ? 315 HOH   B O   1 
HETATM 1564 O O   . HOH   J 6 .   ? -4.811  -0.641  -24.693 1.00 78.88  ? 316 HOH   B O   1 
HETATM 1565 O O   . HOH   J 6 .   ? -15.928 -8.876  -11.823 1.00 65.00  ? 317 HOH   B O   1 
HETATM 1566 O O   . HOH   J 6 .   ? -3.548  -11.653 -6.845  1.00 62.41  ? 318 HOH   B O   1 
HETATM 1567 O O   . HOH   J 6 .   ? -19.097 15.349  -22.294 1.00 59.75  ? 319 HOH   B O   1 
HETATM 1568 O O   . HOH   J 6 .   ? -14.897 -12.451 -16.513 1.00 62.71  ? 320 HOH   B O   1 
HETATM 1569 O O   . HOH   J 6 .   ? -20.287 -13.669 -22.934 1.00 58.18  ? 321 HOH   B O   1 
HETATM 1570 O O   . HOH   J 6 .   ? -20.395 -7.831  -2.950  1.00 61.50  ? 322 HOH   B O   1 
HETATM 1571 O O   . HOH   J 6 .   ? -26.096 -4.582  -4.035  1.00 47.90  ? 323 HOH   B O   1 
HETATM 1572 O O   . HOH   J 6 .   ? -21.320 7.166   0.000   0.50 57.16  ? 324 HOH   B O   1 
HETATM 1573 O O   . HOH   J 6 .   ? -14.328 -6.312  -1.661  1.00 68.04  ? 325 HOH   B O   1 
HETATM 1574 O O   . HOH   J 6 .   ? -30.044 -5.211  -0.977  1.00 59.20  ? 326 HOH   B O   1 
HETATM 1575 O O   . HOH   J 6 .   ? -17.090 15.292  -33.867 1.00 72.88  ? 327 HOH   B O   1 
HETATM 1576 O O   . HOH   J 6 .   ? -19.605 -5.648  -0.740  1.00 54.72  ? 328 HOH   B O   1 
HETATM 1577 O O   . HOH   J 6 .   ? -16.957 13.381  -5.392  1.00 72.86  ? 329 HOH   B O   1 
HETATM 1578 O O   . HOH   J 6 .   ? -32.337 7.031   -4.036  1.00 73.46  ? 330 HOH   B O   1 
HETATM 1579 O O   . HOH   J 6 .   ? -2.709  -8.599  -3.091  1.00 71.68  ? 331 HOH   B O   1 
HETATM 1580 O O   . HOH   J 6 .   ? -10.025 -15.724 -24.297 1.00 60.06  ? 332 HOH   B O   1 
HETATM 1581 O O   . HOH   J 6 .   ? -5.594  3.696   -14.000 1.00 77.17  ? 333 HOH   B O   1 
HETATM 1582 O O   . HOH   J 6 .   ? -7.181  11.471  -19.198 1.00 60.11  ? 334 HOH   B O   1 
HETATM 1583 O O   . HOH   J 6 .   ? -1.122  -14.696 -9.922  1.00 68.57  ? 335 HOH   B O   1 
HETATM 1584 O O   . HOH   J 6 .   ? -21.320 3.340   0.000   0.50 74.75  ? 336 HOH   B O   1 
HETATM 1585 O O   . HOH   J 6 .   ? -17.653 27.464  -14.202 1.00 82.21  ? 337 HOH   B O   1 
HETATM 1586 O O   . HOH   J 6 .   ? -14.386 -7.064  -9.203  1.00 91.34  ? 338 HOH   B O   1 
HETATM 1587 O O   . HOH   J 6 .   ? -11.857 14.017  -14.631 1.00 71.44  ? 339 HOH   B 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   . ASP   A 7   ? 1.4196 0.6810 0.9678 0.3997  0.0488  -0.1316 50  ASP   A N   
2    C CA  . ASP   A 7   ? 1.3814 0.7535 0.9342 0.4276  0.0639  -0.1332 50  ASP   A CA  
3    C C   . ASP   A 7   ? 1.3462 0.7462 0.9126 0.4191  0.0837  -0.0904 50  ASP   A C   
4    O O   . ASP   A 7   ? 1.3800 0.7094 0.9239 0.4331  0.0820  -0.0700 50  ASP   A O   
5    C CB  . ASP   A 7   ? 1.4257 0.8063 0.9474 0.4913  0.0525  -0.1709 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 1.4684 0.9790 1.0062 0.5103  0.0694  -0.1842 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 1.4690 1.0183 0.9969 0.5211  0.0675  -0.2169 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 1.4854 1.0577 1.0446 0.5133  0.0850  -0.1618 50  ASP   A OD2 
9    N N   . MET   A 8   ? 1.2774 0.7746 0.8745 0.3981  0.1008  -0.0772 51  MET   A N   
10   C CA  . MET   A 8   ? 1.2394 0.7697 0.8505 0.3894  0.1167  -0.0420 51  MET   A CA  
11   C C   . MET   A 8   ? 1.2050 0.7812 0.8096 0.4346  0.1166  -0.0483 51  MET   A C   
12   O O   . MET   A 8   ? 1.1895 0.8131 0.7945 0.4661  0.1122  -0.0798 51  MET   A O   
13   C CB  . MET   A 8   ? 1.1994 0.8024 0.8456 0.3486  0.1308  -0.0267 51  MET   A CB  
14   C CG  . MET   A 8   ? 1.2188 0.7831 0.8805 0.3054  0.1293  -0.0180 51  MET   A CG  
15   S SD  . MET   A 8   ? 1.1778 0.8267 0.8767 0.2678  0.1414  -0.0019 51  MET   A SD  
16   C CE  . MET   A 8   ? 1.1594 0.7574 0.8849 0.2232  0.1356  0.0036  51  MET   A CE  
17   N N   . TYR   A 9   ? 1.1869 0.7522 0.7861 0.4398  0.1210  -0.0203 52  TYR   A N   
18   C CA  . TYR   A 9   ? 1.1610 0.7686 0.7578 0.4834  0.1151  -0.0271 52  TYR   A CA  
19   C C   . TYR   A 9   ? 1.1363 0.7694 0.7413 0.4713  0.1232  0.0031  52  TYR   A C   
20   O O   . TYR   A 9   ? 1.1518 0.7428 0.7490 0.4387  0.1340  0.0333  52  TYR   A O   
21   C CB  . TYR   A 9   ? 1.2039 0.7320 0.7566 0.5352  0.0953  -0.0392 52  TYR   A CB  
22   C CG  . TYR   A 9   ? 1.2725 0.6825 0.7791 0.5313  0.0936  -0.0053 52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 1.3252 0.6350 0.8105 0.5097  0.0921  -0.0001 52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 1.2952 0.6886 0.7749 0.5535  0.0920  0.0196  52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 1.3893 0.5864 0.8322 0.5025  0.0956  0.0350  52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 1.3583 0.6401 0.7855 0.5512  0.0958  0.0554  52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 1.4145 0.5976 0.8247 0.5236  0.1002  0.0653  52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 1.4969 0.5676 0.8569 0.5157  0.1098  0.1054  52  TYR   A OH  
29   N N   . ILE   A 10  ? 1.0911 0.7991 0.7161 0.4971  0.1179  -0.0080 53  ILE   A N   
30   C CA  . ILE   A 10  ? 1.0760 0.8100 0.7075 0.4893  0.1204  0.0140  53  ILE   A CA  
31   C C   . ILE   A 10  ? 1.0978 0.8004 0.6936 0.5403  0.1012  0.0156  53  ILE   A C   
32   O O   . ILE   A 10  ? 1.1137 0.8127 0.6995 0.5864  0.0836  -0.0089 53  ILE   A O   
33   C CB  . ILE   A 10  ? 1.0200 0.8626 0.7074 0.4664  0.1280  0.0042  53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 0.9921 0.9134 0.7134 0.4967  0.1203  -0.0308 53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 1.0074 0.8650 0.7139 0.4172  0.1455  0.0118  53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 0.9570 0.9765 0.7339 0.4742  0.1271  -0.0355 53  ILE   A CD1 
37   N N   . GLU   A 11  ? 1.1039 0.7812 0.6746 0.5367  0.1033  0.0433  54  GLU   A N   
38   C CA  . GLU   A 11  ? 1.1375 0.7804 0.6616 0.5871  0.0833  0.0480  54  GLU   A CA  
39   C C   . GLU   A 11  ? 1.1193 0.8181 0.6583 0.5811  0.0807  0.0538  54  GLU   A C   
40   O O   . GLU   A 11  ? 1.1273 0.8231 0.6699 0.5408  0.1007  0.0770  54  GLU   A O   
41   C CB  . GLU   A 11  ? 1.2269 0.7445 0.6749 0.5943  0.0907  0.0837  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 1.3375 0.7729 0.7593 0.6038  0.0881  0.0797  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 1.5181 0.8208 0.8647 0.6070  0.0970  0.1189  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 1.5452 0.8276 0.8674 0.5872  0.1163  0.1541  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 1.6070 0.8234 0.9181 0.6287  0.0866  0.1150  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 1.0952 0.8434 0.6432 0.6226  0.0537  0.0307  55  ARG   A N   
47   C CA  . ARG   A 12  ? 1.0830 0.8785 0.6440 0.6182  0.0456  0.0312  55  ARG   A CA  
48   C C   . ARG   A 12  ? 1.1458 0.8610 0.6310 0.6252  0.0535  0.0675  55  ARG   A C   
49   O O   . ARG   A 12  ? 1.2126 0.8424 0.6262 0.6601  0.0498  0.0850  55  ARG   A O   
50   C CB  . ARG   A 12  ? 1.0654 0.9315 0.6572 0.6613  0.0103  -0.0057 55  ARG   A CB  
51   C CG  . ARG   A 12  ? 1.0599 0.9982 0.6976 0.6406  0.0016  -0.0168 55  ARG   A CG  
52   C CD  . ARG   A 12  ? 1.0436 1.0794 0.7493 0.6641  -0.0292 -0.0609 55  ARG   A CD  
53   N NE  . ARG   A 12  ? 1.0306 1.1310 0.7898 0.6340  -0.0370 -0.0728 55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 1.0718 1.1608 0.8015 0.6568  -0.0634 -0.0769 55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 1.1454 1.1631 0.7870 0.7109  -0.0813 -0.0665 55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 1.0018 1.1421 0.7822 0.6262  -0.0717 -0.0901 55  ARG   A NH2 
57   N N   . ALA   A 13  ? 1.1355 0.8732 0.6328 0.5916  0.0676  0.0809  56  ALA   A N   
58   C CA  . ALA   A 13  ? 1.1805 0.8587 0.6106 0.5971  0.0806  0.1138  56  ALA   A CA  
59   C C   . ALA   A 13  ? 1.1762 0.8937 0.5979 0.6196  0.0587  0.1007  56  ALA   A C   
60   O O   . ALA   A 13  ? 1.2215 0.8944 0.5791 0.6329  0.0684  0.1248  56  ALA   A O   
61   C CB  . ALA   A 13  ? 1.1859 0.8470 0.6288 0.5430  0.1183  0.1416  56  ALA   A CB  
62   N N   . GLY   A 14  ? 1.1203 0.9198 0.6057 0.6233  0.0306  0.0625  57  GLY   A N   
63   C CA  . GLY   A 14  ? 1.1117 0.9454 0.5934 0.6459  0.0021  0.0432  57  GLY   A CA  
64   C C   . GLY   A 14  ? 1.0516 0.9771 0.6254 0.6168  -0.0143 0.0094  57  GLY   A C   
65   O O   . GLY   A 14  ? 1.0062 0.9770 0.6492 0.5776  -0.0005 0.0021  57  GLY   A O   
66   N N   . ASP   A 15  ? 1.0434 0.9927 0.6140 0.6379  -0.0453 -0.0120 58  ASP   A N   
67   C CA  . ASP   A 15  ? 0.9964 1.0209 0.6505 0.6087  -0.0643 -0.0435 58  ASP   A CA  
68   C C   . ASP   A 15  ? 1.0174 1.0265 0.6719 0.5673  -0.0417 -0.0248 58  ASP   A C   
69   O O   . ASP   A 15  ? 1.0685 1.0200 0.6517 0.5791  -0.0246 0.0020  58  ASP   A O   
70   C CB  . ASP   A 15  ? 0.9952 1.0428 0.6412 0.6532  -0.1144 -0.0792 58  ASP   A CB  
71   C CG  . ASP   A 15  ? 1.0128 1.1105 0.6954 0.6900  -0.1491 -0.1141 58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 1.0061 1.1096 0.7042 0.6905  -0.1330 -0.1080 58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 1.0227 1.1523 0.7145 0.7240  -0.1956 -0.1503 58  ASP   A OD2 
74   N N   . ILE   A 16  ? 0.9761 1.0367 0.7092 0.5215  -0.0422 -0.0392 59  ILE   A N   
75   C CA  . ILE   A 16  ? 0.9836 1.0281 0.7181 0.4875  -0.0279 -0.0258 59  ILE   A CA  
76   C C   . ILE   A 16  ? 0.9959 1.0531 0.7382 0.5005  -0.0657 -0.0553 59  ILE   A C   
77   O O   . ILE   A 16  ? 0.9541 1.0618 0.7696 0.4793  -0.0888 -0.0843 59  ILE   A O   
78   C CB  . ILE   A 16  ? 0.9482 1.0187 0.7437 0.4310  -0.0018 -0.0152 59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 0.9729 1.0228 0.7495 0.4254  0.0306  0.0099  59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 0.9531 1.0017 0.7443 0.4046  0.0060  -0.0037 59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 0.9623 1.0374 0.7864 0.3802  0.0535  0.0176  59  ILE   A CD1 
82   N N   A THR   A 17  ? 1.0437 1.0545 0.7085 0.5373  -0.0722 -0.0495 60  THR   A N   
83   N N   B THR   A 17  ? 1.0454 1.0565 0.7110 0.5365  -0.0721 -0.0494 60  THR   A N   
84   C CA  A THR   A 17  ? 1.0564 1.0664 0.7075 0.5610  -0.1113 -0.0798 60  THR   A CA  
85   C CA  B THR   A 17  ? 1.0597 1.0715 0.7133 0.5608  -0.1124 -0.0810 60  THR   A CA  
86   C C   A THR   A 17  ? 1.1050 1.0673 0.6904 0.5711  -0.0947 -0.0616 60  THR   A C   
87   C C   B THR   A 17  ? 1.1094 1.0712 0.6899 0.5768  -0.0982 -0.0638 60  THR   A C   
88   O O   A THR   A 17  ? 1.1346 1.0618 0.6632 0.5799  -0.0577 -0.0261 60  THR   A O   
89   O O   B THR   A 17  ? 1.1419 1.0670 0.6601 0.5904  -0.0632 -0.0292 60  THR   A O   
90   C CB  A THR   A 17  ? 1.0820 1.0886 0.6829 0.6240  -0.1486 -0.1026 60  THR   A CB  
91   C CB  B THR   A 17  ? 1.0760 1.1016 0.7069 0.6148  -0.1532 -0.1098 60  THR   A CB  
92   O OG1 A THR   A 17  ? 1.1368 1.0863 0.6378 0.6623  -0.1233 -0.0685 60  THR   A OG1 
93   O OG1 B THR   A 17  ? 1.0333 1.1274 0.7624 0.5921  -0.1757 -0.1407 60  THR   A OG1 
94   C CG2 A THR   A 17  ? 1.0478 1.1123 0.7169 0.6258  -0.1732 -0.1297 60  THR   A CG2 
95   C CG2 B THR   A 17  ? 1.1050 1.1096 0.6788 0.6615  -0.1933 -0.1366 60  THR   A CG2 
96   N N   . TRP   A 18  ? 1.1138 1.0749 0.7060 0.5737  -0.1237 -0.0884 61  TRP   A N   
97   C CA  . TRP   A 18  ? 1.1864 1.1076 0.7117 0.5956  -0.1135 -0.0795 61  TRP   A CA  
98   C C   . TRP   A 18  ? 1.2811 1.1770 0.7113 0.6643  -0.1327 -0.0889 61  TRP   A C   
99   O O   . TRP   A 18  ? 1.2793 1.1912 0.7151 0.6915  -0.1798 -0.1254 61  TRP   A O   
100  C CB  . TRP   A 18  ? 1.1632 1.0847 0.7280 0.5769  -0.1430 -0.1094 61  TRP   A CB  
101  C CG  . TRP   A 18  ? 1.1972 1.0821 0.6942 0.6086  -0.1407 -0.1108 61  TRP   A CG  
102  C CD1 . TRP   A 18  ? 1.2401 1.1046 0.6675 0.6649  -0.1719 -0.1385 61  TRP   A CD1 
103  C CD2 . TRP   A 18  ? 1.2049 1.0742 0.7016 0.5887  -0.1099 -0.0897 61  TRP   A CD2 
104  N NE1 . TRP   A 18  ? 1.2687 1.1071 0.6495 0.6823  -0.1572 -0.1341 61  TRP   A NE1 
105  C CE2 . TRP   A 18  ? 1.2478 1.0911 0.6760 0.6356  -0.1212 -0.1060 61  TRP   A CE2 
106  C CE3 . TRP   A 18  ? 1.1888 1.0658 0.7338 0.5404  -0.0759 -0.0609 61  TRP   A CE3 
107  C CZ2 . TRP   A 18  ? 1.2627 1.0929 0.6758 0.6359  -0.0975 -0.0943 61  TRP   A CZ2 
108  C CZ3 . TRP   A 18  ? 1.2075 1.0691 0.7379 0.5403  -0.0574 -0.0503 61  TRP   A CZ3 
109  C CH2 . TRP   A 18  ? 1.2369 1.0782 0.7048 0.5878  -0.0665 -0.0664 61  TRP   A CH2 
110  N N   . GLU   A 19  ? 1.3623 1.2212 0.7059 0.6926  -0.0966 -0.0563 62  GLU   A N   
111  C CA  . GLU   A 19  ? 1.4563 1.2832 0.6936 0.7597  -0.1082 -0.0582 62  GLU   A CA  
112  C C   . GLU   A 19  ? 1.5301 1.3361 0.7018 0.7933  -0.1100 -0.0686 62  GLU   A C   
113  O O   . GLU   A 19  ? 1.5432 1.3421 0.7040 0.7778  -0.0660 -0.0414 62  GLU   A O   
114  C CB  . GLU   A 19  ? 1.5287 1.3228 0.7048 0.7712  -0.0627 -0.0098 62  GLU   A CB  
115  C CG  . GLU   A 19  ? 1.5860 1.3951 0.8189 0.7459  -0.0632 -0.0030 62  GLU   A CG  
116  C CD  . GLU   A 19  ? 1.6877 1.4976 0.8960 0.7927  -0.1087 -0.0283 62  GLU   A CD  
117  O OE1 . GLU   A 19  ? 1.7666 1.5342 0.8693 0.8526  -0.1174 -0.0223 62  GLU   A OE1 
118  O OE2 . GLU   A 19  ? 1.6663 1.5215 0.9596 0.7716  -0.1346 -0.0536 62  GLU   A OE2 
119  N N   . LYS   A 20  ? 1.5699 1.3707 0.7026 0.8406  -0.1633 -0.1125 63  LYS   A N   
120  C CA  . LYS   A 20  ? 1.6359 1.4150 0.6976 0.8813  -0.1699 -0.1293 63  LYS   A CA  
121  C C   . LYS   A 20  ? 1.7183 1.4633 0.6578 0.9292  -0.1253 -0.0897 63  LYS   A C   
122  O O   . LYS   A 20  ? 1.7480 1.4729 0.6297 0.9594  -0.1252 -0.0732 63  LYS   A O   
123  C CB  . LYS   A 20  ? 1.6724 1.4509 0.7188 0.9235  -0.2443 -0.1913 63  LYS   A CB  
124  C CG  . LYS   A 20  ? 1.6839 1.4935 0.8534 0.8740  -0.2906 -0.2335 63  LYS   A CG  
125  C CD  . LYS   A 20  ? 1.7415 1.5523 0.9003 0.9158  -0.3679 -0.2977 63  LYS   A CD  
126  C CE  . LYS   A 20  ? 1.7344 1.5916 1.0071 0.8790  -0.4122 -0.3302 63  LYS   A CE  
127  N NZ  . LYS   A 20  ? 1.7708 1.6338 1.0378 0.9207  -0.4911 -0.3967 63  LYS   A NZ  
128  N N   . ASP   A 21  ? 1.7540 1.4921 0.6527 0.9381  -0.0870 -0.0743 64  ASP   A N   
129  C CA  . ASP   A 21  ? 1.8268 1.5383 0.6123 0.9785  -0.0343 -0.0332 64  ASP   A CA  
130  C C   . ASP   A 21  ? 1.8171 1.5257 0.6255 0.9345  0.0292  0.0269  64  ASP   A C   
131  O O   . ASP   A 21  ? 1.8636 1.5372 0.5870 0.9608  0.0604  0.0646  64  ASP   A O   
132  C CB  . ASP   A 21  ? 1.9289 1.6037 0.5885 1.0558  -0.0642 -0.0456 64  ASP   A CB  
133  C CG  . ASP   A 21  ? 2.0622 1.7359 0.6875 1.1064  -0.1302 -0.1092 64  ASP   A CG  
134  O OD1 . ASP   A 21  ? 2.0875 1.7706 0.7158 1.1107  -0.1264 -0.1286 64  ASP   A OD1 
135  O OD2 . ASP   A 21  ? 2.1207 1.7826 0.7125 1.1464  -0.1882 -0.1420 64  ASP   A OD2 
136  N N   . ALA   A 22  ? 1.7549 1.4942 0.6743 0.8683  0.0457  0.0351  65  ALA   A N   
137  C CA  . ALA   A 22  ? 1.7356 1.4756 0.6874 0.8226  0.1027  0.0853  65  ALA   A CA  
138  C C   . ALA   A 22  ? 1.7341 1.4880 0.6634 0.8214  0.1614  0.1123  65  ALA   A C   
139  O O   . ALA   A 22  ? 1.7311 1.5000 0.6373 0.8508  0.1529  0.0870  65  ALA   A O   
140  C CB  . ALA   A 22  ? 1.6864 1.4563 0.7608 0.7582  0.0909  0.0776  65  ALA   A CB  
141  N N   . GLU   A 23  ? 1.7285 1.4791 0.6663 0.7893  0.2198  0.1608  66  GLU   A N   
142  C CA  . GLU   A 23  ? 1.7170 1.4936 0.6502 0.7820  0.2799  0.1874  66  GLU   A CA  
143  C C   . GLU   A 23  ? 1.6361 1.4651 0.6672 0.7500  0.2710  0.1619  66  GLU   A C   
144  O O   . GLU   A 23  ? 1.5868 1.4309 0.7089 0.6982  0.2625  0.1616  66  GLU   A O   
145  C CB  . GLU   A 23  ? 1.7699 1.5324 0.7167 0.7409  0.3371  0.2409  66  GLU   A CB  
146  C CG  . GLU   A 23  ? 1.8536 1.6370 0.7743 0.7402  0.4078  0.2770  66  GLU   A CG  
147  C CD  . GLU   A 23  ? 1.9761 1.7325 0.9085 0.6965  0.4591  0.3292  66  GLU   A CD  
148  O OE1 . GLU   A 23  ? 1.9525 1.7204 0.9805 0.6410  0.4539  0.3304  66  GLU   A OE1 
149  O OE2 . GLU   A 23  ? 2.0616 1.7790 0.9024 0.7187  0.5031  0.3690  66  GLU   A OE2 
150  N N   . VAL   A 24  ? 1.6184 1.4705 0.6235 0.7857  0.2705  0.1391  67  VAL   A N   
151  C CA  . VAL   A 24  ? 1.5624 1.4555 0.6489 0.7648  0.2584  0.1137  67  VAL   A CA  
152  C C   . VAL   A 24  ? 1.5126 1.4538 0.6387 0.7412  0.3215  0.1441  67  VAL   A C   
153  O O   . VAL   A 24  ? 1.5237 1.4807 0.5908 0.7747  0.3644  0.1586  67  VAL   A O   
154  C CB  . VAL   A 24  ? 1.5839 1.4730 0.6306 0.8171  0.2155  0.0654  67  VAL   A CB  
155  C CG1 . VAL   A 24  ? 1.5514 1.4628 0.6835 0.7920  0.1899  0.0384  67  VAL   A CG1 
156  C CG2 . VAL   A 24  ? 1.6220 1.4672 0.6212 0.8461  0.1557  0.0347  67  VAL   A CG2 
157  N N   . THR   A 25  ? 1.4559 1.4235 0.6809 0.6840  0.3292  0.1541  68  THR   A N   
158  C CA  . THR   A 25  ? 1.4154 1.4369 0.6931 0.6576  0.3847  0.1790  68  THR   A CA  
159  C C   . THR   A 25  ? 1.3618 1.4175 0.7471 0.6141  0.3656  0.1650  68  THR   A C   
160  O O   . THR   A 25  ? 1.3642 1.3957 0.7726 0.6052  0.3145  0.1406  68  THR   A O   
161  C CB  . THR   A 25  ? 1.4433 1.4499 0.7017 0.6320  0.4380  0.2281  68  THR   A CB  
162  O OG1 . THR   A 25  ? 1.4309 1.4945 0.7190 0.6210  0.4990  0.2503  68  THR   A OG1 
163  C CG2 . THR   A 25  ? 1.4276 1.4101 0.7450 0.5774  0.4244  0.2409  68  THR   A CG2 
164  N N   . GLY   A 26  ? 1.3157 1.4287 0.7641 0.5900  0.4053  0.1789  69  GLY   A N   
165  C CA  . GLY   A 26  ? 1.2764 1.4217 0.8189 0.5543  0.3859  0.1660  69  GLY   A CA  
166  C C   . GLY   A 26  ? 1.2642 1.4357 0.8243 0.5861  0.3567  0.1301  69  GLY   A C   
167  O O   . GLY   A 26  ? 1.2962 1.4325 0.8036 0.6253  0.3202  0.1036  69  GLY   A O   
168  N N   . ASN   A 27  ? 1.2149 1.4453 0.8515 0.5701  0.3680  0.1264  70  ASN   A N   
169  C CA  . ASN   A 27  ? 1.2041 1.4587 0.8610 0.6028  0.3395  0.0928  70  ASN   A CA  
170  C C   . ASN   A 27  ? 1.1858 1.3995 0.8755 0.5816  0.2811  0.0757  70  ASN   A C   
171  O O   . ASN   A 27  ? 1.1961 1.3692 0.8898 0.5436  0.2663  0.0886  70  ASN   A O   
172  C CB  . ASN   A 27  ? 1.1917 1.5392 0.9106 0.6074  0.3819  0.0944  70  ASN   A CB  
173  C CG  . ASN   A 27  ? 1.2169 1.6029 1.0287 0.5531  0.3891  0.1074  70  ASN   A CG  
174  O OD1 . ASN   A 27  ? 1.2418 1.6056 1.0649 0.5071  0.4030  0.1336  70  ASN   A OD1 
175  N ND2 . ASN   A 27  ? 1.1906 1.6332 1.0687 0.5610  0.3760  0.0865  70  ASN   A ND2 
176  N N   . SER   A 28  ? 1.1588 1.3774 0.8633 0.6100  0.2484  0.0469  71  SER   A N   
177  C CA  . SER   A 28  ? 1.1515 1.3222 0.8740 0.5946  0.1958  0.0341  71  SER   A CA  
178  C C   . SER   A 28  ? 1.0987 1.3159 0.8828 0.5983  0.1874  0.0240  71  SER   A C   
179  O O   . SER   A 28  ? 1.1131 1.3173 0.8874 0.6375  0.1566  -0.0018 71  SER   A O   
180  C CB  . SER   A 28  ? 1.2065 1.3100 0.8711 0.6301  0.1514  0.0070  71  SER   A CB  
181  O OG  . SER   A 28  ? 1.2737 1.3483 0.8788 0.6430  0.1568  0.0072  71  SER   A OG  
182  N N   . PRO   A 29  ? 1.0400 1.3088 0.8878 0.5609  0.2098  0.0410  72  PRO   A N   
183  C CA  . PRO   A 29  ? 0.9896 1.3131 0.8993 0.5701  0.1990  0.0270  72  PRO   A CA  
184  C C   . PRO   A 29  ? 0.9938 1.2664 0.9086 0.5579  0.1480  0.0214  72  PRO   A C   
185  O O   . PRO   A 29  ? 1.0105 1.2397 0.9187 0.5164  0.1380  0.0383  72  PRO   A O   
186  C CB  . PRO   A 29  ? 0.9515 1.3543 0.9288 0.5346  0.2452  0.0449  72  PRO   A CB  
187  C CG  . PRO   A 29  ? 0.9849 1.3402 0.9350 0.4906  0.2608  0.0725  72  PRO   A CG  
188  C CD  . PRO   A 29  ? 1.0194 1.3007 0.8865 0.5129  0.2444  0.0702  72  PRO   A CD  
189  N N   . ARG   A 30  ? 0.9813 1.2571 0.9024 0.5977  0.1163  -0.0020 73  ARG   A N   
190  C CA  . ARG   A 30  ? 1.0010 1.2246 0.9184 0.5933  0.0680  -0.0052 73  ARG   A CA  
191  C C   . ARG   A 30  ? 0.9374 1.2338 0.9261 0.5790  0.0707  -0.0054 73  ARG   A C   
192  O O   . ARG   A 30  ? 0.8956 1.2706 0.9329 0.6107  0.0778  -0.0245 73  ARG   A O   
193  C CB  . ARG   A 30  ? 1.0611 1.2346 0.9392 0.6473  0.0272  -0.0301 73  ARG   A CB  
194  C CG  . ARG   A 30  ? 1.1836 1.2783 0.9944 0.6566  0.0172  -0.0339 73  ARG   A CG  
195  C CD  . ARG   A 30  ? 1.2973 1.3336 1.0682 0.7105  -0.0252 -0.0619 73  ARG   A CD  
196  N NE  . ARG   A 30  ? 1.3930 1.3774 1.1090 0.7284  -0.0301 -0.0751 73  ARG   A NE  
197  C CZ  . ARG   A 30  ? 1.4691 1.3617 1.1455 0.7028  -0.0565 -0.0699 73  ARG   A CZ  
198  N NH1 . ARG   A 30  ? 1.4804 1.3221 1.1619 0.6578  -0.0746 -0.0479 73  ARG   A NH1 
199  N NH2 . ARG   A 30  ? 1.4949 1.3496 1.1276 0.7225  -0.0647 -0.0880 73  ARG   A NH2 
200  N N   . LEU   A 31  ? 0.9262 1.2033 0.9247 0.5319  0.0660  0.0130  74  LEU   A N   
201  C CA  . LEU   A 31  ? 0.8734 1.2152 0.9382 0.5119  0.0658  0.0110  74  LEU   A CA  
202  C C   . LEU   A 31  ? 0.8872 1.1797 0.9319 0.5127  0.0171  0.0098  74  LEU   A C   
203  O O   . LEU   A 31  ? 0.9376 1.1417 0.9208 0.4984  -0.0009 0.0249  74  LEU   A O   
204  C CB  . LEU   A 31  ? 0.8604 1.2196 0.9486 0.4572  0.1022  0.0320  74  LEU   A CB  
205  C CG  . LEU   A 31  ? 0.8691 1.2618 0.9629 0.4517  0.1536  0.0416  74  LEU   A CG  
206  C CD1 . LEU   A 31  ? 0.8778 1.2546 0.9729 0.4014  0.1804  0.0649  74  LEU   A CD1 
207  C CD2 . LEU   A 31  ? 0.8231 1.3202 0.9861 0.4722  0.1815  0.0270  74  LEU   A CD2 
208  N N   . ASP   A 32  ? 0.8351 1.1882 0.9328 0.5281  -0.0028 -0.0075 75  ASP   A N   
209  C CA  . ASP   A 32  ? 0.8487 1.1589 0.9219 0.5324  -0.0494 -0.0080 75  ASP   A CA  
210  C C   . ASP   A 32  ? 0.7974 1.1297 0.8995 0.4825  -0.0390 0.0020  75  ASP   A C   
211  O O   . ASP   A 32  ? 0.7502 1.1733 0.9326 0.4715  -0.0263 -0.0124 75  ASP   A O   
212  C CB  . ASP   A 32  ? 0.8583 1.2283 0.9749 0.5819  -0.0823 -0.0373 75  ASP   A CB  
213  C CG  . ASP   A 32  ? 1.0020 1.3047 1.0592 0.6384  -0.1206 -0.0466 75  ASP   A CG  
214  O OD1 . ASP   A 32  ? 1.0781 1.2815 1.0605 0.6344  -0.1231 -0.0296 75  ASP   A OD1 
215  O OD2 . ASP   A 32  ? 1.0193 1.3677 1.1076 0.6873  -0.1506 -0.0728 75  ASP   A OD2 
216  N N   . VAL   A 33  ? 0.8026 1.0563 0.8448 0.4515  -0.0430 0.0243  76  VAL   A N   
217  C CA  . VAL   A 33  ? 0.7617 1.0302 0.8236 0.4077  -0.0329 0.0311  76  VAL   A CA  
218  C C   . VAL   A 33  ? 0.7744 0.9870 0.7830 0.4063  -0.0704 0.0368  76  VAL   A C   
219  O O   . VAL   A 33  ? 0.8174 0.9600 0.7601 0.4305  -0.0976 0.0454  76  VAL   A O   
220  C CB  . VAL   A 33  ? 0.7701 1.0170 0.8200 0.3674  0.0095  0.0512  76  VAL   A CB  
221  C CG1 . VAL   A 33  ? 0.7447 1.0347 0.8272 0.3731  0.0473  0.0500  76  VAL   A CG1 
222  C CG2 . VAL   A 33  ? 0.8292 0.9838 0.7990 0.3596  0.0029  0.0714  76  VAL   A CG2 
223  N N   . ALA   A 34  ? 0.7351 0.9745 0.7686 0.3783  -0.0714 0.0321  77  ALA   A N   
224  C CA  . ALA   A 34  ? 0.7577 0.9503 0.7362 0.3746  -0.1005 0.0369  77  ALA   A CA  
225  C C   . ALA   A 34  ? 0.7523 0.9248 0.7171 0.3299  -0.0729 0.0500  77  ALA   A C   
226  O O   . ALA   A 34  ? 0.7259 0.9389 0.7447 0.3036  -0.0415 0.0468  77  ALA   A O   
227  C CB  . ALA   A 34  ? 0.7226 0.9725 0.7438 0.3937  -0.1383 0.0086  77  ALA   A CB  
228  N N   . LEU   A 35  ? 0.7787 0.8862 0.6679 0.3233  -0.0820 0.0660  78  LEU   A N   
229  C CA  . LEU   A 35  ? 0.7779 0.8679 0.6501 0.2881  -0.0578 0.0753  78  LEU   A CA  
230  C C   . LEU   A 35  ? 0.7983 0.8818 0.6390 0.2903  -0.0851 0.0649  78  LEU   A C   
231  O O   . LEU   A 35  ? 0.8407 0.8810 0.6141 0.3134  -0.1119 0.0732  78  LEU   A O   
232  C CB  . LEU   A 35  ? 0.8061 0.8328 0.6191 0.2770  -0.0364 0.1028  78  LEU   A CB  
233  C CG  . LEU   A 35  ? 0.8246 0.8350 0.6157 0.2472  -0.0127 0.1113  78  LEU   A CG  
234  C CD1 . LEU   A 35  ? 0.7927 0.8453 0.6441 0.2261  0.0117  0.1001  78  LEU   A CD1 
235  C CD2 . LEU   A 35  ? 0.8567 0.8174 0.6020 0.2373  0.0052  0.1350  78  LEU   A CD2 
236  N N   . ASP   A 36  ? 0.7695 0.8924 0.6559 0.2698  -0.0819 0.0452  79  ASP   A N   
237  C CA  . ASP   A 36  ? 0.7903 0.9098 0.6471 0.2761  -0.1132 0.0280  79  ASP   A CA  
238  C C   . ASP   A 36  ? 0.8294 0.9002 0.6172 0.2599  -0.0956 0.0415  79  ASP   A C   
239  O O   . ASP   A 36  ? 0.8358 0.8852 0.6144 0.2407  -0.0597 0.0611  79  ASP   A O   
240  C CB  . ASP   A 36  ? 0.7596 0.9479 0.7050 0.2673  -0.1313 -0.0084 79  ASP   A CB  
241  C CG  . ASP   A 36  ? 0.7979 1.0001 0.7922 0.2284  -0.1029 -0.0157 79  ASP   A CG  
242  O OD1 . ASP   A 36  ? 0.8262 0.9883 0.7844 0.2124  -0.0700 0.0058  79  ASP   A OD1 
243  O OD2 . ASP   A 36  ? 0.7940 1.0455 0.8641 0.2142  -0.1159 -0.0441 79  ASP   A OD2 
244  N N   . GLU   A 37  ? 0.8507 0.9089 0.5900 0.2719  -0.1229 0.0280  80  GLU   A N   
245  C CA  . GLU   A 37  ? 0.8856 0.9062 0.5548 0.2647  -0.1095 0.0354  80  GLU   A CA  
246  C C   . GLU   A 37  ? 0.8575 0.8908 0.5686 0.2347  -0.0802 0.0261  80  GLU   A C   
247  O O   . GLU   A 37  ? 0.8852 0.8910 0.5483 0.2274  -0.0564 0.0382  80  GLU   A O   
248  C CB  . GLU   A 37  ? 0.9408 0.9540 0.5544 0.2901  -0.1505 0.0148  80  GLU   A CB  
249  C CG  . GLU   A 37  ? 1.0800 1.0424 0.5854 0.2978  -0.1372 0.0348  80  GLU   A CG  
250  C CD  . GLU   A 37  ? 1.1748 1.1342 0.6258 0.3208  -0.1726 0.0068  80  GLU   A CD  
251  O OE1 . GLU   A 37  ? 1.1930 1.1690 0.6669 0.3087  -0.1714 -0.0210 80  GLU   A OE1 
252  O OE2 . GLU   A 37  ? 1.2246 1.1601 0.6057 0.3539  -0.2047 0.0112  80  GLU   A OE2 
253  N N   . SER   A 38  ? 0.7993 0.8732 0.5998 0.2175  -0.0793 0.0067  81  SER   A N   
254  C CA  . SER   A 38  ? 0.7767 0.8505 0.6139 0.1901  -0.0516 0.0020  81  SER   A CA  
255  C C   . SER   A 38  ? 0.7625 0.8308 0.6204 0.1765  -0.0115 0.0289  81  SER   A C   
256  O O   . SER   A 38  ? 0.7576 0.8212 0.6426 0.1576  0.0113  0.0281  81  SER   A O   
257  C CB  . SER   A 38  ? 0.7561 0.8669 0.6765 0.1733  -0.0675 -0.0290 81  SER   A CB  
258  O OG  . SER   A 38  ? 0.8111 0.9242 0.7123 0.1852  -0.1083 -0.0606 81  SER   A OG  
259  N N   . GLY   A 39  ? 0.7583 0.8213 0.5990 0.1886  -0.0061 0.0508  82  GLY   A N   
260  C CA  . GLY   A 39  ? 0.7592 0.8171 0.6153 0.1804  0.0257  0.0715  82  GLY   A CA  
261  C C   . GLY   A 39  ? 0.7313 0.8274 0.6605 0.1744  0.0347  0.0669  82  GLY   A C   
262  O O   . GLY   A 39  ? 0.7224 0.8150 0.6633 0.1686  0.0618  0.0809  82  GLY   A O   
263  N N   . ASP   A 40  ? 0.7135 0.8508 0.6921 0.1779  0.0124  0.0468  83  ASP   A N   
264  C CA  . ASP   A 40  ? 0.6960 0.8818 0.7512 0.1707  0.0257  0.0422  83  ASP   A CA  
265  C C   . ASP   A 40  ? 0.7021 0.9120 0.7661 0.1974  0.0186  0.0464  83  ASP   A C   
266  O O   . ASP   A 40  ? 0.7047 0.9244 0.7586 0.2208  -0.0155 0.0350  83  ASP   A O   
267  C CB  . ASP   A 40  ? 0.6846 0.9140 0.8102 0.1534  0.0099  0.0144  83  ASP   A CB  
268  C CG  . ASP   A 40  ? 0.7725 0.9741 0.9022 0.1245  0.0222  0.0095  83  ASP   A CG  
269  O OD1 . ASP   A 40  ? 0.8024 0.9704 0.9106 0.1144  0.0549  0.0299  83  ASP   A OD1 
270  O OD2 . ASP   A 40  ? 0.8031 1.0131 0.9545 0.1153  -0.0044 -0.0172 83  ASP   A OD2 
271  N N   . PHE   A 41  ? 0.7030 0.9197 0.7812 0.1983  0.0487  0.0608  84  PHE   A N   
272  C CA  . PHE   A 41  ? 0.7043 0.9455 0.7940 0.2265  0.0445  0.0607  84  PHE   A CA  
273  C C   . PHE   A 41  ? 0.6964 1.0171 0.8739 0.2263  0.0442  0.0407  84  PHE   A C   
274  O O   . PHE   A 41  ? 0.6759 1.0278 0.9089 0.1968  0.0684  0.0382  84  PHE   A O   
275  C CB  . PHE   A 41  ? 0.6962 0.9154 0.7625 0.2315  0.0752  0.0796  84  PHE   A CB  
276  C CG  . PHE   A 41  ? 0.7324 0.8845 0.7239 0.2374  0.0691  0.0950  84  PHE   A CG  
277  C CD1 . PHE   A 41  ? 0.7584 0.8809 0.7104 0.2618  0.0423  0.0963  84  PHE   A CD1 
278  C CD2 . PHE   A 41  ? 0.7531 0.8715 0.7172 0.2182  0.0898  0.1078  84  PHE   A CD2 
279  C CE1 . PHE   A 41  ? 0.8050 0.8669 0.6972 0.2599  0.0402  0.1120  84  PHE   A CE1 
280  C CE2 . PHE   A 41  ? 0.7882 0.8575 0.6979 0.2202  0.0858  0.1196  84  PHE   A CE2 
281  C CZ  . PHE   A 41  ? 0.8061 0.8480 0.6829 0.2374  0.0628  0.1224  84  PHE   A CZ  
282  N N   . SER   A 42  ? 0.7134 1.0675 0.9070 0.2588  0.0171  0.0262  85  SER   A N   
283  C CA  . SER   A 42  ? 0.6903 1.1356 0.9780 0.2631  0.0158  0.0032  85  SER   A CA  
284  C C   . SER   A 42  ? 0.7290 1.2000 1.0183 0.3075  0.0089  -0.0018 85  SER   A C   
285  O O   . SER   A 42  ? 0.7836 1.1932 0.9984 0.3366  -0.0127 0.0067  85  SER   A O   
286  C CB  . SER   A 42  ? 0.6816 1.1598 1.0060 0.2612  -0.0264 -0.0246 85  SER   A CB  
287  O OG  . SER   A 42  ? 0.7426 1.1851 1.0045 0.2996  -0.0725 -0.0300 85  SER   A OG  
288  N N   . LEU   A 43  ? 0.6967 1.2567 1.0706 0.3128  0.0284  -0.0159 86  LEU   A N   
289  C CA  . LEU   A 43  ? 0.7144 1.3050 1.0919 0.3612  0.0226  -0.0255 86  LEU   A CA  
290  C C   . LEU   A 43  ? 0.7275 1.3553 1.1296 0.3996  -0.0294 -0.0543 86  LEU   A C   
291  O O   . LEU   A 43  ? 0.6817 1.3776 1.1589 0.3877  -0.0471 -0.0777 86  LEU   A O   
292  C CB  . LEU   A 43  ? 0.6607 1.3337 1.1082 0.3593  0.0722  -0.0269 86  LEU   A CB  
293  C CG  . LEU   A 43  ? 0.7006 1.3404 1.1183 0.3309  0.1267  0.0026  86  LEU   A CG  
294  C CD1 . LEU   A 43  ? 0.6711 1.3851 1.1335 0.3468  0.1709  0.0014  86  LEU   A CD1 
295  C CD2 . LEU   A 43  ? 0.7816 1.3149 1.0898 0.3439  0.1187  0.0227  86  LEU   A CD2 
296  N N   . VAL   A 44  ? 0.7881 1.3700 1.1282 0.4483  -0.0563 -0.0545 87  VAL   A N   
297  C CA  . VAL   A 44  ? 0.8057 1.4110 1.1541 0.4989  -0.1083 -0.0803 87  VAL   A CA  
298  C C   . VAL   A 44  ? 0.7963 1.4797 1.2011 0.5376  -0.0914 -0.0986 87  VAL   A C   
299  O O   . VAL   A 44  ? 0.8226 1.4706 1.1863 0.5479  -0.0627 -0.0842 87  VAL   A O   
300  C CB  . VAL   A 44  ? 0.8884 1.3730 1.1185 0.5280  -0.1482 -0.0644 87  VAL   A CB  
301  C CG1 . VAL   A 44  ? 0.8910 1.3877 1.1179 0.5883  -0.2047 -0.0891 87  VAL   A CG1 
302  C CG2 . VAL   A 44  ? 0.9343 1.3466 1.1039 0.4895  -0.1546 -0.0437 87  VAL   A CG2 
303  N N   . GLU   A 45  ? 0.7533 1.5498 1.2564 0.5590  -0.1070 -0.1328 88  GLU   A N   
304  C CA  . GLU   A 45  ? 0.7359 1.6211 1.2992 0.5998  -0.0879 -0.1535 88  GLU   A CA  
305  C C   . GLU   A 45  ? 0.7318 1.6661 1.3249 0.6653  -0.1443 -0.1906 88  GLU   A C   
306  O O   . GLU   A 45  ? 0.7310 1.7022 1.3354 0.7187  -0.1430 -0.2079 88  GLU   A O   
307  C CB  . GLU   A 45  ? 0.6987 1.7038 1.3766 0.5578  -0.0269 -0.1571 88  GLU   A CB  
308  C CG  . GLU   A 45  ? 0.8045 1.7572 1.4414 0.5085  0.0326  -0.1193 88  GLU   A CG  
309  C CD  . GLU   A 45  ? 0.8495 1.8837 1.5386 0.5077  0.0971  -0.1159 88  GLU   A CD  
310  O OE1 . GLU   A 45  ? 0.8261 1.9454 1.5644 0.5562  0.0970  -0.1423 88  GLU   A OE1 
311  O OE2 . GLU   A 45  ? 0.8814 1.8934 1.5575 0.4621  0.1483  -0.0868 88  GLU   A OE2 
312  N N   . GLU   B 8   ? 1.0426 1.0022 0.9098 0.3551  0.0445  -0.1160 17  GLU   B N   
313  C CA  . GLU   B 8   ? 1.0500 1.0081 0.9156 0.3602  0.0339  -0.1114 17  GLU   B CA  
314  C C   . GLU   B 8   ? 1.0427 1.0156 0.9193 0.3362  0.0380  -0.1044 17  GLU   B C   
315  O O   . GLU   B 8   ? 1.0621 1.0199 0.9221 0.3231  0.0458  -0.0891 17  GLU   B O   
316  C CB  . GLU   B 8   ? 1.0940 1.0142 0.9249 0.3767  0.0298  -0.0970 17  GLU   B CB  
317  C CG  . GLU   B 8   ? 1.1376 1.0555 0.9637 0.3938  0.0148  -0.0986 17  GLU   B CG  
318  C CD  . GLU   B 8   ? 1.2174 1.0997 1.0069 0.4155  0.0113  -0.0857 17  GLU   B CD  
319  O OE1 . GLU   B 8   ? 1.2317 1.0905 1.0008 0.4112  0.0228  -0.0707 17  GLU   B OE1 
320  O OE2 . GLU   B 8   ? 1.2470 1.1245 1.0281 0.4372  -0.0032 -0.0907 17  GLU   B OE2 
321  N N   . THR   B 9   ? 1.0133 1.0153 0.9188 0.3308  0.0317  -0.1156 18  THR   B N   
322  C CA  . THR   B 9   ? 1.0019 1.0149 0.9179 0.3091  0.0331  -0.1097 18  THR   B CA  
323  C C   . THR   B 9   ? 0.9853 0.9942 0.9028 0.3186  0.0156  -0.1116 18  THR   B C   
324  O O   . THR   B 9   ? 0.9875 1.0093 0.9217 0.3025  0.0124  -0.1121 18  THR   B O   
325  C CB  . THR   B 9   ? 1.0057 1.0539 0.9543 0.2891  0.0420  -0.1184 18  THR   B CB  
326  O OG1 . THR   B 9   ? 1.0089 1.0831 0.9851 0.3021  0.0356  -0.1365 18  THR   B OG1 
327  C CG2 . THR   B 9   ? 1.0164 1.0641 0.9557 0.2741  0.0602  -0.1123 18  THR   B CG2 
328  N N   . THR   B 10  ? 0.9704 0.9595 0.8687 0.3450  0.0036  -0.1128 19  THR   B N   
329  C CA  . THR   B 10  ? 0.9536 0.9358 0.8482 0.3580  -0.0150 -0.1160 19  THR   B CA  
330  C C   . THR   B 10  ? 0.9379 0.9009 0.8095 0.3488  -0.0121 -0.0995 19  THR   B C   
331  O O   . THR   B 10  ? 0.9522 0.8965 0.7981 0.3484  -0.0003 -0.0845 19  THR   B O   
332  C CB  . THR   B 10  ? 0.9863 0.9479 0.8576 0.3918  -0.0270 -0.1196 19  THR   B CB  
333  O OG1 . THR   B 10  ? 1.0056 0.9786 0.8900 0.4024  -0.0265 -0.1320 19  THR   B OG1 
334  C CG2 . THR   B 10  ? 0.9900 0.9484 0.8608 0.4090  -0.0496 -0.1286 19  THR   B CG2 
335  N N   . ASP   B 11  ? 0.9105 0.8772 0.7913 0.3426  -0.0242 -0.1026 20  ASP   B N   
336  C CA  . ASP   B 11  ? 0.9130 0.8607 0.7709 0.3385  -0.0256 -0.0896 20  ASP   B CA  
337  C C   . ASP   B 11  ? 0.9240 0.8443 0.7420 0.3646  -0.0265 -0.0789 20  ASP   B C   
338  O O   . ASP   B 11  ? 0.9357 0.8490 0.7447 0.3890  -0.0351 -0.0855 20  ASP   B O   
339  C CB  . ASP   B 11  ? 0.9294 0.8797 0.8010 0.3376  -0.0459 -0.0994 20  ASP   B CB  
340  C CG  . ASP   B 11  ? 0.9791 0.9403 0.8715 0.3074  -0.0428 -0.0975 20  ASP   B CG  
341  O OD1 . ASP   B 11  ? 0.9606 0.9442 0.8780 0.2862  -0.0290 -0.0988 20  ASP   B OD1 
342  O OD2 . ASP   B 11  ? 1.0149 0.9607 0.8965 0.3060  -0.0543 -0.0945 20  ASP   B OD2 
343  N N   . GLY   B 12  ? 0.9130 0.8197 0.7082 0.3596  -0.0168 -0.0623 21  GLY   B N   
344  C CA  . GLY   B 12  ? 0.9094 0.7944 0.6695 0.3817  -0.0139 -0.0496 21  GLY   B CA  
345  C C   . GLY   B 12  ? 0.8890 0.7691 0.6366 0.3691  0.0053  -0.0310 21  GLY   B C   
346  O O   . GLY   B 12  ? 0.8695 0.7605 0.6323 0.3441  0.0142  -0.0287 21  GLY   B O   
347  N N   . VAL   B 13  ? 0.8842 0.7481 0.6040 0.3864  0.0116  -0.0173 22  VAL   B N   
348  C CA  . VAL   B 13  ? 0.8687 0.7295 0.5793 0.3755  0.0291  0.0011  22  VAL   B CA  
349  C C   . VAL   B 13  ? 0.8632 0.7172 0.5742 0.3740  0.0407  0.0059  22  VAL   B C   
350  O O   . VAL   B 13  ? 0.8711 0.7148 0.5741 0.3928  0.0357  0.0007  22  VAL   B O   
351  C CB  . VAL   B 13  ? 0.8757 0.7270 0.5588 0.3923  0.0303  0.0151  22  VAL   B CB  
352  C CG1 . VAL   B 13  ? 0.8897 0.7244 0.5463 0.4236  0.0264  0.0178  22  VAL   B CG1 
353  C CG2 . VAL   B 13  ? 0.8685 0.7232 0.5499 0.3779  0.0477  0.0332  22  VAL   B CG2 
354  N N   . TYR   B 14  ? 0.8492 0.7078 0.5705 0.3517  0.0539  0.0135  23  TYR   B N   
355  C CA  . TYR   B 14  ? 0.8566 0.7063 0.5801 0.3470  0.0632  0.0165  23  TYR   B CA  
356  C C   . TYR   B 14  ? 0.8625 0.7052 0.5798 0.3362  0.0772  0.0355  23  TYR   B C   
357  O O   . TYR   B 14  ? 0.8546 0.7074 0.5755 0.3236  0.0813  0.0428  23  TYR   B O   
358  C CB  . TYR   B 14  ? 0.8431 0.7061 0.5905 0.3284  0.0634  0.0021  23  TYR   B CB  
359  C CG  . TYR   B 14  ? 0.8350 0.7076 0.5952 0.3379  0.0520  -0.0171 23  TYR   B CG  
360  C CD1 . TYR   B 14  ? 0.8378 0.7233 0.6067 0.3396  0.0409  -0.0259 23  TYR   B CD1 
361  C CD2 . TYR   B 14  ? 0.8399 0.7100 0.6063 0.3439  0.0517  -0.0272 23  TYR   B CD2 
362  C CE1 . TYR   B 14  ? 0.8409 0.7389 0.6272 0.3467  0.0298  -0.0437 23  TYR   B CE1 
363  C CE2 . TYR   B 14  ? 0.8411 0.7248 0.6229 0.3537  0.0410  -0.0454 23  TYR   B CE2 
364  C CZ  . TYR   B 14  ? 0.8494 0.7489 0.6434 0.3539  0.0303  -0.0536 23  TYR   B CZ  
365  O OH  . TYR   B 14  ? 0.8581 0.7752 0.6735 0.3610  0.0193  -0.0719 23  TYR   B OH  
366  N N   . ARG   B 15  ? 0.8711 0.6964 0.5814 0.3398  0.0837  0.0425  24  ARG   B N   
367  C CA  . ARG   B 15  ? 0.8687 0.6871 0.5789 0.3262  0.0963  0.0597  24  ARG   B CA  
368  C C   . ARG   B 15  ? 0.8555 0.6776 0.5845 0.3033  0.0980  0.0513  24  ARG   B C   
369  O O   . ARG   B 15  ? 0.8535 0.6724 0.5876 0.3054  0.0929  0.0364  24  ARG   B O   
370  C CB  . ARG   B 15  ? 0.8846 0.6772 0.5771 0.3401  0.1018  0.0721  24  ARG   B CB  
371  C CG  . ARG   B 15  ? 0.9173 0.7030 0.5849 0.3656  0.1022  0.0829  24  ARG   B CG  
372  C CD  . ARG   B 15  ? 0.9664 0.7235 0.6139 0.3784  0.1089  0.0967  24  ARG   B CD  
373  N NE  . ARG   B 15  ? 1.0162 0.7641 0.6347 0.4083  0.1064  0.1023  24  ARG   B NE  
374  C CZ  . ARG   B 15  ? 1.0524 0.8018 0.6543 0.4174  0.1168  0.1217  24  ARG   B CZ  
375  N NH1 . ARG   B 15  ? 1.0299 0.7916 0.6451 0.3979  0.1308  0.1381  24  ARG   B NH1 
376  N NH2 . ARG   B 15  ? 1.0809 0.8210 0.6528 0.4475  0.1129  0.1242  24  ARG   B NH2 
377  N N   . VAL   B 16  ? 0.8484 0.6767 0.5866 0.2836  0.1047  0.0602  25  VAL   B N   
378  C CA  . VAL   B 16  ? 0.8596 0.6883 0.6117 0.2632  0.1056  0.0531  25  VAL   B CA  
379  C C   . VAL   B 16  ? 0.8768 0.6862 0.6280 0.2566  0.1122  0.0668  25  VAL   B C   
380  O O   . VAL   B 16  ? 0.8716 0.6837 0.6237 0.2523  0.1190  0.0840  25  VAL   B O   
381  C CB  . VAL   B 16  ? 0.8675 0.7171 0.6305 0.2458  0.1054  0.0510  25  VAL   B CB  
382  C CG1 . VAL   B 16  ? 0.8660 0.7143 0.6388 0.2274  0.1054  0.0424  25  VAL   B CG1 
383  C CG2 . VAL   B 16  ? 0.8713 0.7362 0.6340 0.2518  0.0989  0.0406  25  VAL   B CG2 
384  N N   . MET   B 17  ? 0.9015 0.6907 0.6510 0.2571  0.1100  0.0595  26  MET   B N   
385  C CA  . MET   B 17  ? 0.9303 0.6931 0.6769 0.2523  0.1140  0.0715  26  MET   B CA  
386  C C   . MET   B 17  ? 0.9625 0.7158 0.7200 0.2336  0.1108  0.0630  26  MET   B C   
387  O O   . MET   B 17  ? 0.9513 0.7143 0.7132 0.2304  0.1055  0.0449  26  MET   B O   
388  C CB  . MET   B 17  ? 0.9402 0.6770 0.6690 0.2738  0.1113  0.0695  26  MET   B CB  
389  C CG  . MET   B 17  ? 0.9424 0.6849 0.6566 0.2973  0.1102  0.0716  26  MET   B CG  
390  S SD  . MET   B 17  ? 0.9809 0.7218 0.6836 0.3023  0.1220  0.0999  26  MET   B SD  
391  C CE  . MET   B 17  ? 0.9658 0.6681 0.6605 0.2974  0.1288  0.1167  26  MET   B CE  
392  N N   . THR   B 18  ? 0.9992 0.7308 0.7595 0.2228  0.1137  0.0759  27  THR   B N   
393  C CA  . THR   B 18  ? 1.0381 0.7535 0.8057 0.2075  0.1078  0.0671  27  THR   B CA  
394  C C   . THR   B 18  ? 1.0850 0.7604 0.8461 0.2067  0.1075  0.0773  27  THR   B C   
395  O O   . THR   B 18  ? 1.0860 0.7515 0.8452 0.2068  0.1154  0.0987  27  THR   B O   
396  C CB  . THR   B 18  ? 1.0474 0.7826 0.8331 0.1852  0.1071  0.0681  27  THR   B CB  
397  O OG1 . THR   B 18  ? 1.0760 0.7930 0.8645 0.1741  0.0986  0.0551  27  THR   B OG1 
398  C CG2 . THR   B 18  ? 1.0383 0.7800 0.8368 0.1738  0.1148  0.0911  27  THR   B CG2 
399  N N   . ARG   B 19  ? 1.1186 0.7699 0.8746 0.2069  0.0984  0.0617  28  ARG   B N   
400  C CA  . ARG   B 19  ? 1.1656 0.7734 0.9145 0.2046  0.0950  0.0685  28  ARG   B CA  
401  C C   . ARG   B 19  ? 1.1833 0.7793 0.9489 0.1786  0.0893  0.0696  28  ARG   B C   
402  O O   . ARG   B 19  ? 1.1973 0.7541 0.9594 0.1729  0.0841  0.0738  28  ARG   B O   
403  C CB  . ARG   B 19  ? 1.2156 0.7989 0.9452 0.2250  0.0863  0.0500  28  ARG   B CB  
404  C CG  . ARG   B 19  ? 1.2855 0.8789 1.0009 0.2507  0.0894  0.0487  28  ARG   B CG  
405  C CD  . ARG   B 19  ? 1.3687 0.9300 1.0640 0.2728  0.0811  0.0369  28  ARG   B CD  
406  N NE  . ARG   B 19  ? 1.4341 0.9929 1.1131 0.2963  0.0838  0.0442  28  ARG   B NE  
407  C CZ  . ARG   B 19  ? 1.4744 1.0528 1.1494 0.3176  0.0795  0.0280  28  ARG   B CZ  
408  N NH1 . ARG   B 19  ? 1.4699 1.0737 1.1572 0.3175  0.0746  0.0048  28  ARG   B NH1 
409  N NH2 . ARG   B 19  ? 1.4769 1.0503 1.1359 0.3393  0.0799  0.0347  28  ARG   B NH2 
410  N N   . ARG   B 20  ? 1.1856 0.8138 0.9687 0.1634  0.0891  0.0657  29  ARG   B N   
411  C CA  . ARG   B 20  ? 1.2056 0.8298 1.0062 0.1399  0.0815  0.0638  29  ARG   B CA  
412  C C   . ARG   B 20  ? 1.2139 0.8279 1.0329 0.1218  0.0864  0.0885  29  ARG   B C   
413  O O   . ARG   B 20  ? 1.2272 0.8199 1.0589 0.1035  0.0774  0.0882  29  ARG   B O   
414  C CB  . ARG   B 20  ? 1.2201 0.8842 1.0310 0.1327  0.0807  0.0544  29  ARG   B CB  
415  C CG  . ARG   B 20  ? 1.2838 0.9461 1.1098 0.1117  0.0700  0.0480  29  ARG   B CG  
416  C CD  . ARG   B 20  ? 1.3298 1.0316 1.1642 0.1060  0.0709  0.0441  29  ARG   B CD  
417  N NE  . ARG   B 20  ? 1.3659 1.0952 1.2159 0.1017  0.0814  0.0647  29  ARG   B NE  
418  C CZ  . ARG   B 20  ? 1.3905 1.1408 1.2620 0.0856  0.0796  0.0719  29  ARG   B CZ  
419  N NH1 . ARG   B 20  ? 1.3954 1.1410 1.2752 0.0717  0.0663  0.0599  29  ARG   B NH1 
420  N NH2 . ARG   B 20  ? 1.3740 1.1510 1.2581 0.0853  0.0902  0.0900  29  ARG   B NH2 
421  N N   . LEU   B 21  ? 1.2014 0.8303 1.0218 0.1272  0.1006  0.1098  30  LEU   B N   
422  C CA  . LEU   B 21  ? 1.1945 0.8194 1.0326 0.1118  0.1095  0.1361  30  LEU   B CA  
423  C C   . LEU   B 21  ? 1.2065 0.7897 1.0255 0.1219  0.1150  0.1510  30  LEU   B C   
424  O O   . LEU   B 21  ? 1.2293 0.7812 1.0247 0.1374  0.1070  0.1371  30  LEU   B O   
425  C CB  . LEU   B 21  ? 1.1819 0.8530 1.0320 0.1129  0.1227  0.1504  30  LEU   B CB  
426  C CG  . LEU   B 21  ? 1.1862 0.8940 1.0653 0.0939  0.1199  0.1489  30  LEU   B CG  
427  C CD1 . LEU   B 21  ? 1.1958 0.8987 1.0779 0.0846  0.1024  0.1236  30  LEU   B CD1 
428  C CD2 . LEU   B 21  ? 1.1809 0.9311 1.0585 0.1058  0.1286  0.1522  30  LEU   B CD2 
429  N N   . LEU   B 22  ? 1.1895 0.7708 1.0185 0.1131  0.1284  0.1793  31  LEU   B N   
430  C CA  . LEU   B 22  ? 1.2038 0.7450 1.0121 0.1225  0.1357  0.1974  31  LEU   B CA  
431  C C   . LEU   B 22  ? 1.2094 0.7564 0.9857 0.1550  0.1414  0.1943  31  LEU   B C   
432  O O   . LEU   B 22  ? 1.2036 0.7916 0.9824 0.1636  0.1488  0.1952  31  LEU   B O   
433  C CB  . LEU   B 22  ? 1.1898 0.7393 1.0183 0.1056  0.1525  0.2302  31  LEU   B CB  
434  C CG  . LEU   B 22  ? 1.2217 0.7271 1.0301 0.1106  0.1616  0.2532  31  LEU   B CG  
435  C CD1 . LEU   B 22  ? 1.2301 0.6891 1.0510 0.0865  0.1511  0.2561  31  LEU   B CD1 
436  C CD2 . LEU   B 22  ? 1.2198 0.7507 1.0336 0.1110  0.1853  0.2850  31  LEU   B CD2 
437  N N   . GLY   B 23  ? 1.2181 0.7246 0.9649 0.1737  0.1351  0.1875  32  GLY   B N   
438  C CA  . GLY   B 23  ? 1.2180 0.7279 0.9354 0.2057  0.1367  0.1812  32  GLY   B CA  
439  C C   . GLY   B 23  ? 1.1893 0.7416 0.9113 0.2155  0.1314  0.1582  32  GLY   B C   
440  O O   . GLY   B 23  ? 1.1770 0.7470 0.9180 0.2010  0.1234  0.1416  32  GLY   B O   
441  N N   . SER   B 24  ? 1.1778 0.7456 0.8819 0.2399  0.1354  0.1577  33  SER   B N   
442  C CA  . SER   B 24  ? 1.1545 0.7613 0.8635 0.2484  0.1309  0.1385  33  SER   B CA  
443  C C   . SER   B 24  ? 1.1131 0.7554 0.8345 0.2418  0.1423  0.1541  33  SER   B C   
444  O O   . SER   B 24  ? 1.1092 0.7497 0.8177 0.2528  0.1532  0.1741  33  SER   B O   
445  C CB  . SER   B 24  ? 1.1965 0.7984 0.8808 0.2791  0.1258  0.1274  33  SER   B CB  
446  O OG  . SER   B 24  ? 1.2513 0.8217 0.9240 0.2882  0.1148  0.1121  33  SER   B OG  
447  N N   . THR   B 25  ? 1.0781 0.7517 0.8227 0.2247  0.1399  0.1457  34  THR   B N   
448  C CA  . THR   B 25  ? 1.0469 0.7555 0.8052 0.2181  0.1491  0.1588  34  THR   B CA  
449  C C   . THR   B 25  ? 1.0193 0.7581 0.7745 0.2296  0.1442  0.1433  34  THR   B C   
450  O O   . THR   B 25  ? 1.0212 0.7650 0.7810 0.2256  0.1341  0.1222  34  THR   B O   
451  C CB  . THR   B 25  ? 1.0453 0.7636 0.8333 0.1887  0.1492  0.1635  34  THR   B CB  
452  O OG1 . THR   B 25  ? 1.0746 0.7617 0.8668 0.1768  0.1530  0.1789  34  THR   B OG1 
453  C CG2 . THR   B 25  ? 1.0253 0.7824 0.8302 0.1823  0.1578  0.1759  34  THR   B CG2 
454  N N   . GLN   B 26  ? 0.9887 0.7462 0.7345 0.2446  0.1511  0.1535  35  GLN   B N   
455  C CA  . GLN   B 26  ? 0.9619 0.7449 0.7052 0.2542  0.1448  0.1393  35  GLN   B CA  
456  C C   . GLN   B 26  ? 0.9449 0.7581 0.7094 0.2364  0.1456  0.1403  35  GLN   B C   
457  O O   . GLN   B 26  ? 0.9423 0.7708 0.7140 0.2334  0.1552  0.1579  35  GLN   B O   
458  C CB  . GLN   B 26  ? 0.9456 0.7315 0.6658 0.2814  0.1474  0.1453  35  GLN   B CB  
459  C CG  . GLN   B 26  ? 0.9218 0.7303 0.6405 0.2898  0.1386  0.1301  35  GLN   B CG  
460  C CD  . GLN   B 26  ? 0.9785 0.7886 0.6739 0.3172  0.1385  0.1344  35  GLN   B CD  
461  O OE1 . GLN   B 26  ? 1.0137 0.8034 0.6885 0.3367  0.1374  0.1356  35  GLN   B OE1 
462  N NE2 . GLN   B 26  ? 0.9706 0.8029 0.6659 0.3212  0.1382  0.1361  35  GLN   B NE2 
463  N N   . VAL   B 27  ? 0.9250 0.7475 0.6988 0.2256  0.1361  0.1217  36  VAL   B N   
464  C CA  . VAL   B 27  ? 0.9017 0.7492 0.6917 0.2103  0.1344  0.1203  36  VAL   B CA  
465  C C   . VAL   B 27  ? 0.8814 0.7500 0.6637 0.2216  0.1311  0.1152  36  VAL   B C   
466  O O   . VAL   B 27  ? 0.8799 0.7691 0.6714 0.2140  0.1307  0.1180  36  VAL   B O   
467  C CB  . VAL   B 27  ? 0.9097 0.7526 0.7110 0.1915  0.1263  0.1050  36  VAL   B CB  
468  C CG1 . VAL   B 27  ? 0.9254 0.7474 0.7368 0.1779  0.1275  0.1111  36  VAL   B CG1 
469  C CG2 . VAL   B 27  ? 0.9178 0.7537 0.7082 0.1992  0.1190  0.0850  36  VAL   B CG2 
470  N N   . GLY   B 28  ? 0.8629 0.7252 0.6288 0.2399  0.1271  0.1070  37  GLY   B N   
471  C CA  . GLY   B 28  ? 0.8400 0.7168 0.5980 0.2505  0.1215  0.1009  37  GLY   B CA  
472  C C   . GLY   B 28  ? 0.8293 0.6969 0.5727 0.2696  0.1149  0.0902  37  GLY   B C   
473  O O   . GLY   B 28  ? 0.8372 0.6877 0.5730 0.2795  0.1158  0.0900  37  GLY   B O   
474  N N   . VAL   B 29  ? 0.8148 0.6926 0.5542 0.2752  0.1069  0.0814  38  VAL   B N   
475  C CA  . VAL   B 29  ? 0.8065 0.6801 0.5356 0.2927  0.0974  0.0700  38  VAL   B CA  
476  C C   . VAL   B 29  ? 0.7989 0.6828 0.5375 0.2812  0.0886  0.0551  38  VAL   B C   
477  O O   . VAL   B 29  ? 0.8015 0.6948 0.5470 0.2653  0.0898  0.0567  38  VAL   B O   
478  C CB  . VAL   B 29  ? 0.8049 0.6785 0.5149 0.3156  0.0964  0.0793  38  VAL   B CB  
479  C CG1 . VAL   B 29  ? 0.8068 0.6744 0.5058 0.3347  0.0834  0.0663  38  VAL   B CG1 
480  C CG2 . VAL   B 29  ? 0.8089 0.6744 0.5082 0.3261  0.1084  0.0975  38  VAL   B CG2 
481  N N   . GLY   B 30  ? 0.7853 0.6675 0.5245 0.2893  0.0797  0.0414  39  GLY   B N   
482  C CA  . GLY   B 30  ? 0.7718 0.6637 0.5212 0.2783  0.0724  0.0290  39  GLY   B CA  
483  C C   . GLY   B 30  ? 0.7686 0.6597 0.5174 0.2927  0.0601  0.0174  39  GLY   B C   
484  O O   . GLY   B 30  ? 0.7674 0.6498 0.5065 0.3131  0.0564  0.0167  39  GLY   B O   
485  N N   . VAL   B 31  ? 0.7590 0.6583 0.5183 0.2818  0.0531  0.0082  40  VAL   B N   
486  C CA  . VAL   B 31  ? 0.7636 0.6637 0.5277 0.2913  0.0391  -0.0039 40  VAL   B CA  
487  C C   . VAL   B 31  ? 0.7597 0.6737 0.5481 0.2771  0.0393  -0.0172 40  VAL   B C   
488  O O   . VAL   B 31  ? 0.7448 0.6670 0.5422 0.2560  0.0461  -0.0166 40  VAL   B O   
489  C CB  . VAL   B 31  ? 0.7719 0.6683 0.5283 0.2901  0.0292  -0.0022 40  VAL   B CB  
490  C CG1 . VAL   B 31  ? 0.7755 0.6724 0.5425 0.2941  0.0129  -0.0163 40  VAL   B CG1 
491  C CG2 . VAL   B 31  ? 0.7838 0.6697 0.5153 0.3087  0.0287  0.0097  40  VAL   B CG2 
492  N N   . MET   B 32  ? 0.7647 0.6826 0.5632 0.2895  0.0313  -0.0293 41  MET   B N   
493  C CA  . MET   B 32  ? 0.7658 0.7024 0.5914 0.2776  0.0313  -0.0428 41  MET   B CA  
494  C C   . MET   B 32  ? 0.7705 0.7125 0.6091 0.2766  0.0160  -0.0516 41  MET   B C   
495  O O   . MET   B 32  ? 0.7774 0.7109 0.6092 0.2966  0.0016  -0.0565 41  MET   B O   
496  C CB  . MET   B 32  ? 0.7750 0.7149 0.6068 0.2922  0.0317  -0.0518 41  MET   B CB  
497  C CG  . MET   B 32  ? 0.7845 0.7485 0.6457 0.2822  0.0338  -0.0661 41  MET   B CG  
498  S SD  . MET   B 32  ? 0.8581 0.8317 0.7239 0.2596  0.0532  -0.0626 41  MET   B SD  
499  C CE  . MET   B 32  ? 0.8629 0.8165 0.7089 0.2758  0.0583  -0.0585 41  MET   B CE  
500  N N   . GLN   B 33  ? 0.7653 0.7182 0.6198 0.2537  0.0184  -0.0527 42  GLN   B N   
501  C CA  . GLN   B 33  ? 0.7737 0.7302 0.6441 0.2483  0.0038  -0.0604 42  GLN   B CA  
502  C C   . GLN   B 33  ? 0.7667 0.7456 0.6663 0.2230  0.0119  -0.0649 42  GLN   B C   
503  O O   . GLN   B 33  ? 0.7788 0.7600 0.6733 0.2059  0.0268  -0.0565 42  GLN   B O   
504  C CB  . GLN   B 33  ? 0.8135 0.7485 0.6620 0.2488  -0.0052 -0.0516 42  GLN   B CB  
505  C CG  . GLN   B 33  ? 0.8638 0.7965 0.7274 0.2448  -0.0240 -0.0607 42  GLN   B CG  
506  C CD  . GLN   B 33  ? 0.9370 0.8437 0.7744 0.2525  -0.0370 -0.0547 42  GLN   B CD  
507  O OE1 . GLN   B 33  ? 0.9539 0.8525 0.7944 0.2362  -0.0429 -0.0527 42  GLN   B OE1 
508  N NE2 . GLN   B 33  ? 0.9638 0.8563 0.7734 0.2782  -0.0411 -0.0510 42  GLN   B NE2 
509  N N   . GLU   B 34  ? 0.7469 0.7442 0.6775 0.2213  0.0028  -0.0782 43  GLU   B N   
510  C CA  . GLU   B 34  ? 0.7319 0.7561 0.6957 0.1976  0.0115  -0.0826 43  GLU   B CA  
511  C C   . GLU   B 34  ? 0.7292 0.7720 0.6969 0.1908  0.0332  -0.0816 43  GLU   B C   
512  O O   . GLU   B 34  ? 0.7303 0.7878 0.7094 0.1690  0.0468  -0.0780 43  GLU   B O   
513  C CB  . GLU   B 34  ? 0.7702 0.7849 0.7336 0.1742  0.0104  -0.0737 43  GLU   B CB  
514  C CG  . GLU   B 34  ? 0.8296 0.8283 0.7964 0.1788  -0.0135 -0.0783 43  GLU   B CG  
515  C CD  . GLU   B 34  ? 0.9572 0.9287 0.9036 0.1664  -0.0191 -0.0670 43  GLU   B CD  
516  O OE1 . GLU   B 34  ? 0.9743 0.9510 0.9352 0.1403  -0.0127 -0.0620 43  GLU   B OE1 
517  O OE2 . GLU   B 34  ? 1.0292 0.9737 0.9442 0.1837  -0.0299 -0.0630 43  GLU   B OE2 
518  N N   . GLY   B 35  ? 0.7258 0.7665 0.6830 0.2102  0.0358  -0.0853 44  GLY   B N   
519  C CA  . GLY   B 35  ? 0.7157 0.7695 0.6736 0.2077  0.0532  -0.0866 44  GLY   B CA  
520  C C   . GLY   B 35  ? 0.7200 0.7561 0.6491 0.1986  0.0660  -0.0729 44  GLY   B C   
521  O O   . GLY   B 35  ? 0.7233 0.7672 0.6501 0.1951  0.0794  -0.0741 44  GLY   B O   
522  N N   . VAL   B 36  ? 0.7136 0.7260 0.6201 0.1962  0.0604  -0.0609 45  VAL   B N   
523  C CA  . VAL   B 36  ? 0.7100 0.7068 0.5911 0.1878  0.0696  -0.0482 45  VAL   B CA  
524  C C   . VAL   B 36  ? 0.6977 0.6723 0.5553 0.2049  0.0646  -0.0410 45  VAL   B C   
525  O O   . VAL   B 36  ? 0.6932 0.6574 0.5450 0.2187  0.0521  -0.0403 45  VAL   B O   
526  C CB  . VAL   B 36  ? 0.7278 0.7191 0.6035 0.1684  0.0699  -0.0395 45  VAL   B CB  
527  C CG1 . VAL   B 36  ? 0.7546 0.7298 0.6034 0.1627  0.0766  -0.0274 45  VAL   B CG1 
528  C CG2 . VAL   B 36  ? 0.7172 0.7311 0.6155 0.1494  0.0789  -0.0439 45  VAL   B CG2 
529  N N   . PHE   B 37  ? 0.6844 0.6526 0.5292 0.2051  0.0741  -0.0362 46  PHE   B N   
530  C CA  . PHE   B 37  ? 0.6879 0.6376 0.5136 0.2181  0.0722  -0.0271 46  PHE   B CA  
531  C C   . PHE   B 37  ? 0.6812 0.6215 0.4911 0.2077  0.0740  -0.0145 46  PHE   B C   
532  O O   . PHE   B 37  ? 0.6570 0.6007 0.4652 0.1922  0.0815  -0.0127 46  PHE   B O   
533  C CB  . PHE   B 37  ? 0.6832 0.6287 0.5062 0.2239  0.0793  -0.0290 46  PHE   B CB  
534  C CG  . PHE   B 37  ? 0.6904 0.6172 0.4971 0.2379  0.0775  -0.0188 46  PHE   B CG  
535  C CD1 . PHE   B 37  ? 0.6940 0.6140 0.4956 0.2576  0.0690  -0.0187 46  PHE   B CD1 
536  C CD2 . PHE   B 37  ? 0.7005 0.6173 0.4970 0.2312  0.0844  -0.0086 46  PHE   B CD2 
537  C CE1 . PHE   B 37  ? 0.7058 0.6094 0.4902 0.2706  0.0699  -0.0069 46  PHE   B CE1 
538  C CE2 . PHE   B 37  ? 0.7102 0.6125 0.4948 0.2420  0.0847  0.0029  46  PHE   B CE2 
539  C CZ  . PHE   B 37  ? 0.7084 0.6044 0.4860 0.2618  0.0788  0.0045  46  PHE   B CZ  
540  N N   . HIS   B 38  ? 0.6902 0.6192 0.4871 0.2184  0.0667  -0.0063 47  HIS   B N   
541  C CA  . HIS   B 38  ? 0.7025 0.6249 0.4855 0.2118  0.0667  0.0046  47  HIS   B CA  
542  C C   . HIS   B 38  ? 0.7285 0.6439 0.5002 0.2217  0.0703  0.0152  47  HIS   B C   
543  O O   . HIS   B 38  ? 0.7351 0.6451 0.5016 0.2396  0.0671  0.0172  47  HIS   B O   
544  C CB  . HIS   B 38  ? 0.6996 0.6159 0.4765 0.2170  0.0547  0.0053  47  HIS   B CB  
545  C CG  . HIS   B 38  ? 0.7166 0.6388 0.5083 0.2077  0.0492  -0.0044 47  HIS   B CG  
546  N ND1 . HIS   B 38  ? 0.7207 0.6514 0.5293 0.2149  0.0451  -0.0157 47  HIS   B ND1 
547  C CD2 . HIS   B 38  ? 0.7265 0.6472 0.5193 0.1916  0.0470  -0.0037 47  HIS   B CD2 
548  C CE1 . HIS   B 38  ? 0.7132 0.6509 0.5369 0.2012  0.0414  -0.0215 47  HIS   B CE1 
549  N NE2 . HIS   B 38  ? 0.7263 0.6566 0.5401 0.1864  0.0429  -0.0137 47  HIS   B NE2 
550  N N   . THR   B 39  ? 0.7294 0.6452 0.4975 0.2105  0.0766  0.0223  48  THR   B N   
551  C CA  . THR   B 39  ? 0.7405 0.6530 0.5028 0.2175  0.0805  0.0338  48  THR   B CA  
552  C C   . THR   B 39  ? 0.7323 0.6482 0.4901 0.2066  0.0812  0.0415  48  THR   B C   
553  O O   . THR   B 39  ? 0.7261 0.6428 0.4802 0.1970  0.0775  0.0385  48  THR   B O   
554  C CB  . THR   B 39  ? 0.7567 0.6648 0.5250 0.2191  0.0873  0.0331  48  THR   B CB  
555  O OG1 . THR   B 39  ? 0.7724 0.6768 0.5366 0.2264  0.0914  0.0463  48  THR   B OG1 
556  C CG2 . THR   B 39  ? 0.7550 0.6646 0.5299 0.2024  0.0918  0.0271  48  THR   B CG2 
557  N N   . MET   B 40  ? 0.7282 0.6464 0.4864 0.2091  0.0854  0.0521  49  MET   B N   
558  C CA  . MET   B 40  ? 0.7260 0.6506 0.4837 0.2000  0.0850  0.0583  49  MET   B CA  
559  C C   . MET   B 40  ? 0.7334 0.6576 0.4991 0.1835  0.0886  0.0545  49  MET   B C   
560  O O   . MET   B 40  ? 0.7354 0.6544 0.5081 0.1824  0.0931  0.0521  49  MET   B O   
561  C CB  . MET   B 40  ? 0.7234 0.6553 0.4819 0.2108  0.0881  0.0714  49  MET   B CB  
562  C CG  . MET   B 40  ? 0.7403 0.6702 0.4869 0.2316  0.0848  0.0741  49  MET   B CG  
563  S SD  . MET   B 40  ? 0.9221 0.8621 0.6595 0.2408  0.0800  0.0819  49  MET   B SD  
564  C CE  . MET   B 40  ? 0.9628 0.8914 0.6881 0.2373  0.0677  0.0711  49  MET   B CE  
565  N N   . TRP   B 41  ? 0.7389 0.6660 0.5013 0.1721  0.0854  0.0531  50  TRP   B N   
566  C CA  A TRP   B 41  ? 0.7515 0.6767 0.5177 0.1580  0.0865  0.0479  50  TRP   B CA  
567  C CA  B TRP   B 41  ? 0.7466 0.6717 0.5128 0.1580  0.0866  0.0478  50  TRP   B CA  
568  C C   . TRP   B 41  ? 0.7568 0.6831 0.5366 0.1553  0.0892  0.0537  50  TRP   B C   
569  O O   . TRP   B 41  ? 0.7704 0.6889 0.5546 0.1481  0.0905  0.0475  50  TRP   B O   
570  C CB  A TRP   B 41  ? 0.7574 0.6843 0.5137 0.1491  0.0811  0.0464  50  TRP   B CB  
571  C CB  B TRP   B 41  ? 0.7453 0.6716 0.5012 0.1487  0.0812  0.0458  50  TRP   B CB  
572  C CG  A TRP   B 41  ? 0.7683 0.6899 0.5211 0.1372  0.0815  0.0374  50  TRP   B CG  
573  C CG  B TRP   B 41  ? 0.7452 0.6683 0.5014 0.1367  0.0806  0.0394  50  TRP   B CG  
574  C CD1 A TRP   B 41  ? 0.7832 0.7000 0.5262 0.1325  0.0844  0.0286  50  TRP   B CD1 
575  C CD1 B TRP   B 41  ? 0.7485 0.6747 0.5144 0.1310  0.0773  0.0417  50  TRP   B CD1 
576  C CD2 A TRP   B 41  ? 0.7710 0.6919 0.5304 0.1294  0.0791  0.0358  50  TRP   B CD2 
577  C CD2 B TRP   B 41  ? 0.7478 0.6643 0.4942 0.1297  0.0828  0.0287  50  TRP   B CD2 
578  N NE1 A TRP   B 41  ? 0.7921 0.7048 0.5312 0.1246  0.0844  0.0213  50  TRP   B NE1 
579  N NE1 B TRP   B 41  ? 0.7540 0.6724 0.5146 0.1219  0.0754  0.0319  50  TRP   B NE1 
580  C CE2 A TRP   B 41  ? 0.7853 0.6986 0.5341 0.1224  0.0796  0.0247  50  TRP   B CE2 
581  C CE2 B TRP   B 41  ? 0.7565 0.6694 0.5034 0.1220  0.0796  0.0241  50  TRP   B CE2 
582  C CE3 A TRP   B 41  ? 0.7735 0.7005 0.5478 0.1272  0.0760  0.0425  50  TRP   B CE3 
583  C CE3 B TRP   B 41  ? 0.7592 0.6741 0.4980 0.1294  0.0873  0.0227  50  TRP   B CE3 
584  C CZ2 A TRP   B 41  ? 0.7981 0.7060 0.5475 0.1151  0.0751  0.0187  50  TRP   B CZ2 
585  C CZ2 B TRP   B 41  ? 0.7714 0.6776 0.5062 0.1166  0.0809  0.0132  50  TRP   B CZ2 
586  C CZ3 A TRP   B 41  ? 0.7836 0.7061 0.5634 0.1173  0.0715  0.0370  50  TRP   B CZ3 
587  C CZ3 B TRP   B 41  ? 0.7727 0.6847 0.5028 0.1227  0.0909  0.0133  50  TRP   B CZ3 
588  C CH2 A TRP   B 41  ? 0.7957 0.7072 0.5614 0.1121  0.0699  0.0245  50  TRP   B CH2 
589  C CH2 B TRP   B 41  ? 0.7744 0.6812 0.5001 0.1176  0.0878  0.0085  50  TRP   B CH2 
590  N N   . HIS   B 42  ? 0.7485 0.6847 0.5355 0.1606  0.0899  0.0656  51  HIS   B N   
591  C CA  . HIS   B 42  ? 0.7532 0.6923 0.5571 0.1548  0.0932  0.0731  51  HIS   B CA  
592  C C   . HIS   B 42  ? 0.7665 0.6933 0.5749 0.1590  0.0998  0.0756  51  HIS   B C   
593  O O   . HIS   B 42  ? 0.7657 0.6885 0.5875 0.1506  0.1017  0.0802  51  HIS   B O   
594  C CB  . HIS   B 42  ? 0.7484 0.7063 0.5623 0.1586  0.0940  0.0860  51  HIS   B CB  
595  C CG  . HIS   B 42  ? 0.7590 0.7223 0.5692 0.1759  0.1005  0.0966  51  HIS   B CG  
596  N ND1 . HIS   B 42  ? 0.7859 0.7537 0.5811 0.1898  0.0971  0.0965  51  HIS   B ND1 
597  C CD2 . HIS   B 42  ? 0.7618 0.7245 0.5789 0.1820  0.1097  0.1077  51  HIS   B CD2 
598  C CE1 . HIS   B 42  ? 0.7822 0.7537 0.5752 0.2053  0.1038  0.1064  51  HIS   B CE1 
599  N NE2 . HIS   B 42  ? 0.7756 0.7443 0.5806 0.2013  0.1124  0.1140  51  HIS   B NE2 
600  N N   . VAL   B 43  ? 0.7697 0.6888 0.5671 0.1716  0.1018  0.0718  52  VAL   B N   
601  C CA  . VAL   B 43  ? 0.7740 0.6791 0.5715 0.1784  0.1064  0.0729  52  VAL   B CA  
602  C C   . VAL   B 43  ? 0.7892 0.6802 0.5882 0.1691  0.1043  0.0604  52  VAL   B C   
603  O O   . VAL   B 43  ? 0.7986 0.6763 0.6037 0.1655  0.1061  0.0634  52  VAL   B O   
604  C CB  . VAL   B 43  ? 0.7855 0.6885 0.5707 0.1968  0.1064  0.0709  52  VAL   B CB  
605  C CG1 . VAL   B 43  ? 0.7977 0.6841 0.5799 0.2054  0.1086  0.0675  52  VAL   B CG1 
606  C CG2 . VAL   B 43  ? 0.7837 0.6965 0.5641 0.2100  0.1087  0.0839  52  VAL   B CG2 
607  N N   . THR   B 44  ? 0.7823 0.6753 0.5747 0.1657  0.1007  0.0467  53  THR   B N   
608  C CA  . THR   B 44  ? 0.7900 0.6725 0.5808 0.1606  0.0995  0.0332  53  THR   B CA  
609  C C   . THR   B 44  ? 0.8050 0.6876 0.5957 0.1460  0.0953  0.0274  53  THR   B C   
610  O O   . THR   B 44  ? 0.8145 0.6856 0.6030 0.1425  0.0936  0.0171  53  THR   B O   
611  C CB  . THR   B 44  ? 0.7947 0.6818 0.5793 0.1679  0.1002  0.0215  53  THR   B CB  
612  O OG1 . THR   B 44  ? 0.8013 0.7001 0.5809 0.1609  0.0989  0.0186  53  THR   B OG1 
613  C CG2 . THR   B 44  ? 0.8044 0.6925 0.5883 0.1838  0.1011  0.0252  53  THR   B CG2 
614  N N   . LYS   B 45  ? 0.8086 0.7028 0.5992 0.1395  0.0924  0.0326  54  LYS   B N   
615  C CA  . LYS   B 45  ? 0.8333 0.7279 0.6196 0.1279  0.0866  0.0259  54  LYS   B CA  
616  C C   . LYS   B 45  ? 0.8466 0.7387 0.6177 0.1276  0.0879  0.0119  54  LYS   B C   
617  O O   . LYS   B 45  ? 0.8546 0.7413 0.6177 0.1208  0.0840  0.0033  54  LYS   B O   
618  C CB  . LYS   B 45  ? 0.8715 0.7555 0.6683 0.1188  0.0816  0.0251  54  LYS   B CB  
619  C CG  . LYS   B 45  ? 0.9417 0.8296 0.7576 0.1166  0.0826  0.0401  54  LYS   B CG  
620  C CD  . LYS   B 45  ? 1.0238 0.9323 0.8457 0.1152  0.0809  0.0496  54  LYS   B CD  
621  C CE  . LYS   B 45  ? 1.1034 1.0201 0.9469 0.1134  0.0846  0.0653  54  LYS   B CE  
622  N NZ  . LYS   B 45  ? 1.1509 1.0894 0.9967 0.1216  0.0879  0.0766  54  LYS   B NZ  
623  N N   . GLY   B 46  ? 0.8455 0.7424 0.6133 0.1352  0.0932  0.0096  55  GLY   B N   
624  C CA  . GLY   B 46  ? 0.8543 0.7538 0.6123 0.1344  0.0971  -0.0019 55  GLY   B CA  
625  C C   . GLY   B 46  ? 0.8651 0.7575 0.6247 0.1394  0.0999  -0.0134 55  GLY   B C   
626  O O   . GLY   B 46  ? 0.8732 0.7709 0.6259 0.1398  0.1044  -0.0236 55  GLY   B O   
627  N N   . ALA   B 47  ? 0.8661 0.7464 0.6339 0.1440  0.0976  -0.0116 56  ALA   B N   
628  C CA  . ALA   B 47  ? 0.8703 0.7391 0.6375 0.1511  0.0982  -0.0228 56  ALA   B CA  
629  C C   . ALA   B 47  ? 0.8648 0.7430 0.6359 0.1632  0.1034  -0.0287 56  ALA   B C   
630  O O   . ALA   B 47  ? 0.8599 0.7473 0.6368 0.1673  0.1046  -0.0215 56  ALA   B O   
631  C CB  . ALA   B 47  ? 0.8719 0.7210 0.6458 0.1520  0.0939  -0.0165 56  ALA   B CB  
632  N N   . ALA   B 48  ? 0.8681 0.7435 0.6367 0.1704  0.1050  -0.0425 57  ALA   B N   
633  C CA  . ALA   B 48  ? 0.8686 0.7553 0.6445 0.1832  0.1086  -0.0499 57  ALA   B CA  
634  C C   . ALA   B 48  ? 0.8770 0.7504 0.6580 0.1949  0.1047  -0.0437 57  ALA   B C   
635  O O   . ALA   B 48  ? 0.8846 0.7366 0.6623 0.1938  0.1009  -0.0362 57  ALA   B O   
636  C CB  . ALA   B 48  ? 0.8719 0.7605 0.6435 0.1900  0.1111  -0.0669 57  ALA   B CB  
637  N N   . LEU   B 49  ? 0.8780 0.7639 0.6671 0.2061  0.1054  -0.0465 58  LEU   B N   
638  C CA  . LEU   B 49  ? 0.9075 0.7805 0.6972 0.2203  0.1014  -0.0410 58  LEU   B CA  
639  C C   . LEU   B 49  ? 0.9436 0.8185 0.7369 0.2374  0.0996  -0.0553 58  LEU   B C   
640  O O   . LEU   B 49  ? 0.9443 0.8411 0.7463 0.2384  0.1026  -0.0682 58  LEU   B O   
641  C CB  . LEU   B 49  ? 0.8977 0.7811 0.6911 0.2220  0.1003  -0.0306 58  LEU   B CB  
642  C CG  . LEU   B 49  ? 0.9125 0.7987 0.7030 0.2077  0.1015  -0.0179 58  LEU   B CG  
643  C CD1 . LEU   B 49  ? 0.9196 0.8162 0.7119 0.2121  0.0991  -0.0113 58  LEU   B CD1 
644  C CD2 . LEU   B 49  ? 0.9266 0.7938 0.7117 0.2035  0.1013  -0.0060 58  LEU   B CD2 
645  N N   . ARG   B 50  ? 0.9762 0.8292 0.7631 0.2513  0.0951  -0.0526 59  ARG   B N   
646  C CA  . ARG   B 50  ? 1.0070 0.8583 0.7952 0.2709  0.0912  -0.0660 59  ARG   B CA  
647  C C   . ARG   B 50  ? 1.0185 0.8762 0.8104 0.2855  0.0866  -0.0630 59  ARG   B C   
648  O O   . ARG   B 50  ? 1.0169 0.8656 0.8022 0.2844  0.0861  -0.0479 59  ARG   B O   
649  C CB  . ARG   B 50  ? 1.0616 0.8763 0.8350 0.2778  0.0874  -0.0649 59  ARG   B CB  
650  C CG  . ARG   B 50  ? 1.1480 0.9535 0.9178 0.3008  0.0815  -0.0781 59  ARG   B CG  
651  C CD  . ARG   B 50  ? 1.2276 0.9932 0.9808 0.3063  0.0768  -0.0794 59  ARG   B CD  
652  N NE  . ARG   B 50  ? 1.2908 1.0222 1.0316 0.3028  0.0755  -0.0593 59  ARG   B NE  
653  C CZ  . ARG   B 50  ? 1.3235 1.0380 1.0545 0.3184  0.0727  -0.0503 59  ARG   B CZ  
654  N NH1 . ARG   B 50  ? 1.2997 1.0285 1.0327 0.3391  0.0685  -0.0608 59  ARG   B NH1 
655  N NH2 . ARG   B 50  ? 1.3412 1.0258 1.0607 0.3135  0.0743  -0.0303 59  ARG   B NH2 
656  N N   . SER   B 51  ? 1.0279 0.9035 0.8310 0.2999  0.0828  -0.0779 60  SER   B N   
657  C CA  . SER   B 51  ? 1.0529 0.9327 0.8589 0.3167  0.0751  -0.0783 60  SER   B CA  
658  C C   . SER   B 51  ? 1.0914 0.9692 0.8991 0.3394  0.0684  -0.0943 60  SER   B C   
659  O O   . SER   B 51  ? 1.0852 0.9932 0.9135 0.3456  0.0659  -0.1100 60  SER   B O   
660  C CB  . SER   B 51  ? 1.0409 0.9533 0.8662 0.3086  0.0747  -0.0817 60  SER   B CB  
661  O OG  . SER   B 51  ? 1.0563 0.9698 0.8830 0.3261  0.0644  -0.0834 60  SER   B OG  
662  N N   . GLY   B 52  ? 1.1219 0.9644 0.9091 0.3510  0.0656  -0.0903 61  GLY   B N   
663  C CA  . GLY   B 52  ? 1.1393 0.9728 0.9229 0.3737  0.0585  -0.1051 61  GLY   B CA  
664  C C   . GLY   B 52  ? 1.1526 0.9948 0.9425 0.3664  0.0637  -0.1180 61  GLY   B C   
665  O O   . GLY   B 52  ? 1.1701 0.9945 0.9497 0.3506  0.0690  -0.1102 61  GLY   B O   
666  N N   . GLU   B 53  ? 1.1371 1.0097 0.9449 0.3775  0.0624  -0.1381 62  GLU   B N   
667  C CA  . GLU   B 53  ? 1.1306 1.0168 0.9434 0.3728  0.0690  -0.1515 62  GLU   B CA  
668  C C   . GLU   B 53  ? 1.1044 1.0222 0.9320 0.3471  0.0809  -0.1481 62  GLU   B C   
669  O O   . GLU   B 53  ? 1.1117 1.0288 0.9330 0.3375  0.0877  -0.1516 62  GLU   B O   
670  C CB  . GLU   B 53  ? 1.1550 1.0675 0.9834 0.3953  0.0651  -0.1740 62  GLU   B CB  
671  C CG  . GLU   B 53  ? 1.2569 1.1338 1.0644 0.4208  0.0549  -0.1824 62  GLU   B CG  
672  C CD  . GLU   B 53  ? 1.3421 1.2489 1.1656 0.4439  0.0517  -0.2068 62  GLU   B CD  
673  O OE1 . GLU   B 53  ? 1.3554 1.2694 1.1868 0.4653  0.0412  -0.2142 62  GLU   B OE1 
674  O OE2 . GLU   B 53  ? 1.3580 1.2825 1.1859 0.4421  0.0593  -0.2189 62  GLU   B OE2 
675  N N   . GLY   B 54  ? 1.0711 1.0133 0.9156 0.3375  0.0822  -0.1417 63  GLY   B N   
676  C CA  . GLY   B 54  ? 1.0427 1.0132 0.9006 0.3144  0.0924  -0.1376 63  GLY   B CA  
677  C C   . GLY   B 54  ? 1.0351 0.9856 0.8760 0.2936  0.0976  -0.1219 63  GLY   B C   
678  O O   . GLY   B 54  ? 1.0589 0.9772 0.8828 0.2931  0.0930  -0.1090 63  GLY   B O   
679  N N   . ARG   B 55  ? 0.9963 0.9675 0.8424 0.2763  0.1075  -0.1224 64  ARG   B N   
680  C CA  . ARG   B 55  ? 0.9847 0.9413 0.8159 0.2570  0.1115  -0.1094 64  ARG   B CA  
681  C C   . ARG   B 55  ? 0.9430 0.9196 0.7849 0.2407  0.1151  -0.0999 64  ARG   B C   
682  O O   . ARG   B 55  ? 0.9327 0.9402 0.7940 0.2383  0.1195  -0.1064 64  ARG   B O   
683  C CB  . ARG   B 55  ? 1.0094 0.9676 0.8305 0.2522  0.1187  -0.1181 64  ARG   B CB  
684  C CG  . ARG   B 55  ? 1.0680 1.0079 0.8715 0.2350  0.1200  -0.1075 64  ARG   B CG  
685  C CD  . ARG   B 55  ? 1.1135 1.0543 0.9041 0.2344  0.1252  -0.1188 64  ARG   B CD  
686  N NE  . ARG   B 55  ? 1.1727 1.1008 0.9475 0.2180  0.1256  -0.1105 64  ARG   B NE  
687  C CZ  . ARG   B 55  ? 1.2343 1.1350 0.9912 0.2174  0.1195  -0.1133 64  ARG   B CZ  
688  N NH1 . ARG   B 55  ? 1.2513 1.1312 1.0022 0.2318  0.1129  -0.1236 64  ARG   B NH1 
689  N NH2 . ARG   B 55  ? 1.2392 1.1318 0.9840 0.2029  0.1184  -0.1066 64  ARG   B NH2 
690  N N   . LEU   B 56  ? 0.9125 0.8715 0.7431 0.2300  0.1127  -0.0846 65  LEU   B N   
691  C CA  . LEU   B 56  ? 0.8802 0.8515 0.7156 0.2154  0.1145  -0.0753 65  LEU   B CA  
692  C C   . LEU   B 56  ? 0.8619 0.8263 0.6823 0.1995  0.1200  -0.0694 65  LEU   B C   
693  O O   . LEU   B 56  ? 0.8753 0.8167 0.6818 0.1982  0.1167  -0.0630 65  LEU   B O   
694  C CB  . LEU   B 56  ? 0.8872 0.8435 0.7183 0.2187  0.1063  -0.0624 65  LEU   B CB  
695  C CG  . LEU   B 56  ? 0.9003 0.8544 0.7380 0.2372  0.0979  -0.0652 65  LEU   B CG  
696  C CD1 . LEU   B 56  ? 0.9141 0.8563 0.7436 0.2387  0.0919  -0.0516 65  LEU   B CD1 
697  C CD2 . LEU   B 56  ? 0.8897 0.8718 0.7501 0.2411  0.0966  -0.0781 65  LEU   B CD2 
698  N N   . ASP   B 57  ? 0.8304 0.8140 0.6534 0.1874  0.1281  -0.0711 66  ASP   B N   
699  C CA  . ASP   B 57  ? 0.8335 0.8094 0.6386 0.1740  0.1321  -0.0657 66  ASP   B CA  
700  C C   . ASP   B 57  ? 0.8079 0.7822 0.6092 0.1612  0.1301  -0.0522 66  ASP   B C   
701  O O   . ASP   B 57  ? 0.7943 0.7810 0.6087 0.1590  0.1295  -0.0498 66  ASP   B O   
702  C CB  . ASP   B 57  ? 0.8793 0.8729 0.6817 0.1708  0.1434  -0.0756 66  ASP   B CB  
703  C CG  . ASP   B 57  ? 0.9907 0.9815 0.7907 0.1852  0.1441  -0.0899 66  ASP   B CG  
704  O OD1 . ASP   B 57  ? 1.0186 0.9832 0.8064 0.1904  0.1363  -0.0900 66  ASP   B OD1 
705  O OD2 . ASP   B 57  ? 1.0383 1.0534 0.8499 0.1915  0.1521  -0.1010 66  ASP   B OD2 
706  N N   . PRO   B 58  ? 0.8011 0.7590 0.5853 0.1536  0.1272  -0.0438 67  PRO   B N   
707  C CA  . PRO   B 58  ? 0.7941 0.7497 0.5726 0.1437  0.1243  -0.0318 67  PRO   B CA  
708  C C   . PRO   B 58  ? 0.7744 0.7441 0.5513 0.1325  0.1321  -0.0316 67  PRO   B C   
709  O O   . PRO   B 58  ? 0.7746 0.7544 0.5484 0.1302  0.1414  -0.0389 67  PRO   B O   
710  C CB  . PRO   B 58  ? 0.8153 0.7543 0.5775 0.1393  0.1198  -0.0261 67  PRO   B CB  
711  C CG  . PRO   B 58  ? 0.8255 0.7608 0.5811 0.1415  0.1230  -0.0369 67  PRO   B CG  
712  C CD  . PRO   B 58  ? 0.8015 0.7430 0.5716 0.1536  0.1251  -0.0462 67  PRO   B CD  
713  N N   . TYR   B 59  ? 0.7572 0.7268 0.5357 0.1261  0.1287  -0.0230 68  TYR   B N   
714  C CA  . TYR   B 59  ? 0.7424 0.7220 0.5204 0.1135  0.1359  -0.0204 68  TYR   B CA  
715  C C   . TYR   B 59  ? 0.7470 0.7101 0.5037 0.1044  0.1313  -0.0086 68  TYR   B C   
716  O O   . TYR   B 59  ? 0.7554 0.7177 0.4968 0.0944  0.1385  -0.0055 68  TYR   B O   
717  C CB  . TYR   B 59  ? 0.7207 0.7145 0.5241 0.1139  0.1341  -0.0228 68  TYR   B CB  
718  C CG  . TYR   B 59  ? 0.7057 0.7105 0.5148 0.0984  0.1415  -0.0191 68  TYR   B CG  
719  C CD1 . TYR   B 59  ? 0.7146 0.7037 0.5109 0.0880  0.1363  -0.0077 68  TYR   B CD1 
720  C CD2 . TYR   B 59  ? 0.6932 0.7246 0.5224 0.0945  0.1534  -0.0266 68  TYR   B CD2 
721  C CE1 . TYR   B 59  ? 0.7190 0.7144 0.5200 0.0721  0.1431  -0.0025 68  TYR   B CE1 
722  C CE2 . TYR   B 59  ? 0.6937 0.7369 0.5319 0.0782  0.1615  -0.0213 68  TYR   B CE2 
723  C CZ  . TYR   B 59  ? 0.7172 0.7403 0.5412 0.0661  0.1560  -0.0087 68  TYR   B CZ  
724  O OH  . TYR   B 59  ? 0.7372 0.7679 0.5693 0.0481  0.1640  -0.0017 68  TYR   B OH  
725  N N   . TRP   B 60  ? 0.7412 0.6914 0.4954 0.1095  0.1198  -0.0020 69  TRP   B N   
726  C CA  . TRP   B 60  ? 0.7471 0.6817 0.4813 0.1045  0.1133  0.0082  69  TRP   B CA  
727  C C   . TRP   B 60  ? 0.7630 0.6890 0.4944 0.1147  0.1040  0.0116  69  TRP   B C   
728  O O   . TRP   B 60  ? 0.7523 0.6812 0.4976 0.1252  0.1009  0.0098  69  TRP   B O   
729  C CB  . TRP   B 60  ? 0.7347 0.6643 0.4713 0.0996  0.1080  0.0141  69  TRP   B CB  
730  C CG  . TRP   B 60  ? 0.7493 0.6601 0.4652 0.0996  0.0980  0.0238  69  TRP   B CG  
731  C CD1 . TRP   B 60  ? 0.7735 0.6721 0.4656 0.0906  0.0987  0.0303  69  TRP   B CD1 
732  C CD2 . TRP   B 60  ? 0.7452 0.6477 0.4599 0.1117  0.0858  0.0277  69  TRP   B CD2 
733  N NE1 . TRP   B 60  ? 0.7814 0.6647 0.4593 0.0966  0.0864  0.0372  69  TRP   B NE1 
734  C CE2 . TRP   B 60  ? 0.7650 0.6523 0.4571 0.1098  0.0791  0.0356  69  TRP   B CE2 
735  C CE3 . TRP   B 60  ? 0.7465 0.6531 0.4749 0.1257  0.0804  0.0255  69  TRP   B CE3 
736  C CZ2 . TRP   B 60  ? 0.7766 0.6562 0.4623 0.1217  0.0677  0.0404  69  TRP   B CZ2 
737  C CZ3 . TRP   B 60  ? 0.7601 0.6584 0.4802 0.1371  0.0705  0.0315  69  TRP   B CZ3 
738  C CH2 . TRP   B 60  ? 0.7729 0.6593 0.4732 0.1352  0.0643  0.0384  69  TRP   B CH2 
739  N N   . GLY   B 61  ? 0.7771 0.6932 0.4907 0.1121  0.0995  0.0175  70  GLY   B N   
740  C CA  . GLY   B 61  ? 0.7812 0.6935 0.4951 0.1200  0.0915  0.0222  70  GLY   B CA  
741  C C   . GLY   B 61  ? 0.7822 0.6858 0.4772 0.1170  0.0847  0.0287  70  GLY   B C   
742  O O   . GLY   B 61  ? 0.7993 0.6971 0.4770 0.1088  0.0868  0.0284  70  GLY   B O   
743  N N   . ASP   B 62  ? 0.7696 0.6733 0.4669 0.1248  0.0769  0.0345  71  ASP   B N   
744  C CA  . ASP   B 62  ? 0.7801 0.6783 0.4620 0.1251  0.0685  0.0400  71  ASP   B CA  
745  C C   . ASP   B 62  ? 0.7698 0.6780 0.4654 0.1334  0.0640  0.0440  71  ASP   B C   
746  O O   . ASP   B 62  ? 0.7452 0.6585 0.4517 0.1430  0.0640  0.0478  71  ASP   B O   
747  C CB  . ASP   B 62  ? 0.8153 0.7025 0.4838 0.1278  0.0626  0.0453  71  ASP   B CB  
748  C CG  . ASP   B 62  ? 0.9092 0.7862 0.5557 0.1284  0.0533  0.0501  71  ASP   B CG  
749  O OD1 . ASP   B 62  ? 0.9448 0.8285 0.5945 0.1373  0.0462  0.0531  71  ASP   B OD1 
750  O OD2 . ASP   B 62  ? 0.9460 0.8086 0.5720 0.1207  0.0533  0.0514  71  ASP   B OD2 
751  N N   . VAL   B 63  ? 0.7775 0.6892 0.4728 0.1297  0.0600  0.0432  72  VAL   B N   
752  C CA  . VAL   B 63  ? 0.7736 0.6985 0.4869 0.1347  0.0567  0.0479  72  VAL   B CA  
753  C C   . VAL   B 63  ? 0.7890 0.7194 0.4987 0.1459  0.0499  0.0557  72  VAL   B C   
754  O O   . VAL   B 63  ? 0.7955 0.7390 0.5213 0.1543  0.0515  0.0617  72  VAL   B O   
755  C CB  . VAL   B 63  ? 0.7729 0.7010 0.4912 0.1264  0.0524  0.0433  72  VAL   B CB  
756  C CG1 . VAL   B 63  ? 0.7675 0.7119 0.5028 0.1298  0.0457  0.0494  72  VAL   B CG1 
757  C CG2 . VAL   B 63  ? 0.7719 0.6969 0.5015 0.1202  0.0588  0.0369  72  VAL   B CG2 
758  N N   . LYS   B 64  ? 0.7983 0.7174 0.4853 0.1474  0.0429  0.0561  73  LYS   B N   
759  C CA  . LYS   B 64  ? 0.7984 0.7203 0.4791 0.1605  0.0346  0.0621  73  LYS   B CA  
760  C C   . LYS   B 64  ? 0.7908 0.7109 0.4735 0.1717  0.0370  0.0653  73  LYS   B C   
761  O O   . LYS   B 64  ? 0.7779 0.7104 0.4682 0.1854  0.0354  0.0704  73  LYS   B O   
762  C CB  . LYS   B 64  ? 0.8302 0.7359 0.4828 0.1601  0.0245  0.0617  73  LYS   B CB  
763  C CG  . LYS   B 64  ? 0.8839 0.7943 0.5308 0.1761  0.0140  0.0665  73  LYS   B CG  
764  C CD  . LYS   B 64  ? 0.9735 0.8670 0.5919 0.1770  0.0022  0.0661  73  LYS   B CD  
765  C CE  . LYS   B 64  ? 1.0398 0.9322 0.6483 0.1955  -0.0084 0.0699  73  LYS   B CE  
766  N NZ  . LYS   B 64  ? 1.0900 0.9580 0.6650 0.1981  -0.0211 0.0701  73  LYS   B NZ  
767  N N   . GLN   B 65  ? 0.7980 0.7045 0.4750 0.1669  0.0408  0.0618  74  GLN   B N   
768  C CA  . GLN   B 65  ? 0.7998 0.7032 0.4794 0.1777  0.0411  0.0626  74  GLN   B CA  
769  C C   . GLN   B 65  ? 0.7891 0.7070 0.4897 0.1830  0.0496  0.0637  74  GLN   B C   
770  O O   . GLN   B 65  ? 0.7995 0.7183 0.5013 0.1970  0.0490  0.0658  74  GLN   B O   
771  C CB  . GLN   B 65  ? 0.8292 0.7168 0.5020 0.1689  0.0420  0.0577  74  GLN   B CB  
772  C CG  . GLN   B 65  ? 0.9089 0.7770 0.5586 0.1629  0.0344  0.0589  74  GLN   B CG  
773  C CD  . GLN   B 65  ? 1.0155 0.8712 0.6643 0.1529  0.0364  0.0557  74  GLN   B CD  
774  O OE1 . GLN   B 65  ? 1.0315 0.8871 0.6907 0.1589  0.0349  0.0530  74  GLN   B OE1 
775  N NE2 . GLN   B 65  ? 1.0467 0.8923 0.6832 0.1377  0.0399  0.0562  74  GLN   B NE2 
776  N N   . ASP   B 66  ? 0.7729 0.6987 0.4871 0.1725  0.0569  0.0619  75  ASP   B N   
777  C CA  . ASP   B 66  ? 0.7526 0.6872 0.4849 0.1748  0.0651  0.0634  75  ASP   B CA  
778  C C   . ASP   B 66  ? 0.7292 0.6560 0.4620 0.1787  0.0684  0.0587  75  ASP   B C   
779  O O   . ASP   B 66  ? 0.7167 0.6466 0.4556 0.1902  0.0715  0.0620  75  ASP   B O   
780  C CB  . ASP   B 66  ? 0.7557 0.7052 0.4973 0.1876  0.0663  0.0733  75  ASP   B CB  
781  C CG  . ASP   B 66  ? 0.7881 0.7447 0.5482 0.1861  0.0757  0.0774  75  ASP   B CG  
782  O OD1 . ASP   B 66  ? 0.8102 0.7627 0.5781 0.1728  0.0783  0.0725  75  ASP   B OD1 
783  O OD2 . ASP   B 66  ? 0.7844 0.7485 0.5486 0.1994  0.0804  0.0858  75  ASP   B OD2 
784  N N   . LEU   B 67  ? 0.7230 0.6411 0.4501 0.1693  0.0681  0.0510  76  LEU   B N   
785  C CA  . LEU   B 67  ? 0.7140 0.6286 0.4462 0.1716  0.0705  0.0447  76  LEU   B CA  
786  C C   . LEU   B 67  ? 0.7169 0.6325 0.4547 0.1586  0.0774  0.0365  76  LEU   B C   
787  O O   . LEU   B 67  ? 0.7132 0.6276 0.4440 0.1471  0.0788  0.0351  76  LEU   B O   
788  C CB  . LEU   B 67  ? 0.7157 0.6212 0.4382 0.1739  0.0627  0.0432  76  LEU   B CB  
789  C CG  . LEU   B 67  ? 0.7335 0.6351 0.4474 0.1907  0.0541  0.0484  76  LEU   B CG  
790  C CD1 . LEU   B 67  ? 0.7462 0.6335 0.4491 0.1900  0.0440  0.0457  76  LEU   B CD1 
791  C CD2 . LEU   B 67  ? 0.7326 0.6390 0.4539 0.2070  0.0561  0.0490  76  LEU   B CD2 
792  N N   . VAL   B 68  ? 0.7100 0.6278 0.4584 0.1623  0.0810  0.0302  77  VAL   B N   
793  C CA  . VAL   B 68  ? 0.7018 0.6233 0.4562 0.1533  0.0878  0.0210  77  VAL   B CA  
794  C C   . VAL   B 68  ? 0.6903 0.6163 0.4565 0.1596  0.0878  0.0137  77  VAL   B C   
795  O O   . VAL   B 68  ? 0.6740 0.5982 0.4438 0.1730  0.0833  0.0150  77  VAL   B O   
796  C CB  . VAL   B 68  ? 0.6971 0.6183 0.4557 0.1520  0.0925  0.0191  77  VAL   B CB  
797  C CG1 . VAL   B 68  ? 0.6973 0.6165 0.4644 0.1648  0.0925  0.0221  77  VAL   B CG1 
798  C CG2 . VAL   B 68  ? 0.6854 0.6098 0.4460 0.1452  0.0989  0.0085  77  VAL   B CG2 
799  N N   . SER   B 69  ? 0.6917 0.6251 0.4640 0.1505  0.0926  0.0061  78  SER   B N   
800  C CA  . SER   B 69  ? 0.6947 0.6375 0.4834 0.1547  0.0923  -0.0024 78  SER   B CA  
801  C C   . SER   B 69  ? 0.7050 0.6594 0.5035 0.1526  0.1017  -0.0124 78  SER   B C   
802  O O   . SER   B 69  ? 0.7081 0.6631 0.4983 0.1437  0.1088  -0.0131 78  SER   B O   
803  C CB  . SER   B 69  ? 0.6975 0.6422 0.4894 0.1456  0.0888  -0.0020 78  SER   B CB  
804  O OG  . SER   B 69  ? 0.7124 0.6630 0.5017 0.1292  0.0980  -0.0024 78  SER   B OG  
805  N N   . TYR   B 70  ? 0.7040 0.6667 0.5181 0.1632  0.1006  -0.0210 79  TYR   B N   
806  C CA  . TYR   B 70  ? 0.7075 0.6811 0.5308 0.1658  0.1080  -0.0320 79  TYR   B CA  
807  C C   . TYR   B 70  ? 0.7080 0.7030 0.5536 0.1651  0.1091  -0.0415 79  TYR   B C   
808  O O   . TYR   B 70  ? 0.7053 0.7019 0.5616 0.1713  0.0999  -0.0424 79  TYR   B O   
809  C CB  . TYR   B 70  ? 0.7102 0.6730 0.5321 0.1823  0.1045  -0.0342 79  TYR   B CB  
810  C CG  . TYR   B 70  ? 0.7283 0.6737 0.5343 0.1802  0.1054  -0.0262 79  TYR   B CG  
811  C CD1 . TYR   B 70  ? 0.7464 0.6811 0.5430 0.1797  0.1009  -0.0136 79  TYR   B CD1 
812  C CD2 . TYR   B 70  ? 0.7405 0.6814 0.5420 0.1785  0.1101  -0.0319 79  TYR   B CD2 
813  C CE1 . TYR   B 70  ? 0.7658 0.6892 0.5533 0.1757  0.1016  -0.0063 79  TYR   B CE1 
814  C CE2 . TYR   B 70  ? 0.7618 0.6871 0.5521 0.1740  0.1091  -0.0253 79  TYR   B CE2 
815  C CZ  . TYR   B 70  ? 0.7841 0.7024 0.5696 0.1716  0.1052  -0.0121 79  TYR   B CZ  
816  O OH  . TYR   B 70  ? 0.8085 0.7157 0.5884 0.1660  0.1038  -0.0057 79  TYR   B OH  
817  N N   . CYS   B 71  ? 0.7035 0.7160 0.5567 0.1584  0.1201  -0.0491 80  CYS   B N   
818  C CA  . CYS   B 71  ? 0.7079 0.7484 0.5874 0.1561  0.1246  -0.0587 80  CYS   B CA  
819  C C   . CYS   B 71  ? 0.6969 0.7464 0.5856 0.1385  0.1260  -0.0527 80  CYS   B C   
820  O O   . CYS   B 71  ? 0.6866 0.7625 0.5994 0.1317  0.1327  -0.0588 80  CYS   B O   
821  C CB  . CYS   B 71  ? 0.7294 0.7771 0.6278 0.1737  0.1152  -0.0688 80  CYS   B CB  
822  S SG  . CYS   B 71  ? 0.8341 0.8615 0.7171 0.1949  0.1111  -0.0725 80  CYS   B SG  
823  N N   . GLY   B 72  ? 0.6938 0.7223 0.5650 0.1313  0.1199  -0.0408 81  GLY   B N   
824  C CA  . GLY   B 72  ? 0.6851 0.7152 0.5613 0.1146  0.1196  -0.0341 81  GLY   B CA  
825  C C   . GLY   B 72  ? 0.6881 0.6908 0.5397 0.1108  0.1111  -0.0218 81  GLY   B C   
826  O O   . GLY   B 72  ? 0.6943 0.6802 0.5269 0.1208  0.1062  -0.0180 81  GLY   B O   
827  N N   . PRO   B 73  ? 0.6793 0.6777 0.5316 0.0956  0.1097  -0.0151 82  PRO   B N   
828  C CA  . PRO   B 73  ? 0.7004 0.6713 0.5278 0.0934  0.1002  -0.0041 82  PRO   B CA  
829  C C   . PRO   B 73  ? 0.7174 0.6744 0.5437 0.1097  0.0828  -0.0052 82  PRO   B C   
830  O O   . PRO   B 73  ? 0.7152 0.6819 0.5626 0.1186  0.0757  -0.0140 82  PRO   B O   
831  C CB  . PRO   B 73  ? 0.7072 0.6756 0.5386 0.0734  0.1022  0.0023  82  PRO   B CB  
832  C CG  . PRO   B 73  ? 0.6877 0.6841 0.5560 0.0679  0.1066  -0.0068 82  PRO   B CG  
833  C CD  . PRO   B 73  ? 0.6517 0.6700 0.5289 0.0797  0.1165  -0.0169 82  PRO   B CD  
834  N N   . TRP   B 74  ? 0.7336 0.6684 0.5343 0.1146  0.0753  0.0035  83  TRP   B N   
835  C CA  . TRP   B 74  ? 0.7476 0.6680 0.5408 0.1315  0.0602  0.0043  83  TRP   B CA  
836  C C   . TRP   B 74  ? 0.7579 0.6741 0.5653 0.1308  0.0468  -0.0004 83  TRP   B C   
837  O O   . TRP   B 74  ? 0.7596 0.6697 0.5691 0.1142  0.0457  0.0028  83  TRP   B O   
838  C CB  . TRP   B 74  ? 0.7571 0.6583 0.5221 0.1339  0.0559  0.0147  83  TRP   B CB  
839  C CG  . TRP   B 74  ? 0.7571 0.6476 0.5120 0.1543  0.0437  0.0163  83  TRP   B CG  
840  C CD1 . TRP   B 74  ? 0.7689 0.6432 0.5161 0.1619  0.0284  0.0166  83  TRP   B CD1 
841  C CD2 . TRP   B 74  ? 0.7522 0.6471 0.5027 0.1703  0.0460  0.0182  83  TRP   B CD2 
842  N NE1 . TRP   B 74  ? 0.7762 0.6466 0.5126 0.1837  0.0221  0.0182  83  TRP   B NE1 
843  C CE2 . TRP   B 74  ? 0.7635 0.6474 0.5032 0.1883  0.0337  0.0201  83  TRP   B CE2 
844  C CE3 . TRP   B 74  ? 0.7458 0.6513 0.4996 0.1710  0.0572  0.0189  83  TRP   B CE3 
845  C CZ2 . TRP   B 74  ? 0.7674 0.6540 0.5006 0.2066  0.0348  0.0241  83  TRP   B CZ2 
846  C CZ3 . TRP   B 74  ? 0.7478 0.6534 0.4972 0.1867  0.0570  0.0231  83  TRP   B CZ3 
847  C CH2 . TRP   B 74  ? 0.7593 0.6571 0.4989 0.2043  0.0472  0.0263  83  TRP   B CH2 
848  N N   . LYS   B 75  ? 0.7617 0.6810 0.5797 0.1482  0.0368  -0.0085 84  LYS   B N   
849  C CA  . LYS   B 75  ? 0.7670 0.6835 0.6012 0.1498  0.0213  -0.0161 84  LYS   B CA  
850  C C   . LYS   B 75  ? 0.8057 0.6976 0.6198 0.1669  0.0026  -0.0148 84  LYS   B C   
851  O O   . LYS   B 75  ? 0.8147 0.6963 0.6363 0.1655  -0.0132 -0.0199 84  LYS   B O   
852  C CB  . LYS   B 75  ? 0.7542 0.6915 0.6137 0.1606  0.0203  -0.0288 84  LYS   B CB  
853  C CG  . LYS   B 75  ? 0.7524 0.7169 0.6339 0.1479  0.0375  -0.0330 84  LYS   B CG  
854  C CD  . LYS   B 75  ? 0.7820 0.7593 0.6885 0.1247  0.0400  -0.0344 84  LYS   B CD  
855  C CE  . LYS   B 75  ? 0.7974 0.8074 0.7292 0.1157  0.0570  -0.0405 84  LYS   B CE  
856  N NZ  . LYS   B 75  ? 0.8071 0.8305 0.7600 0.0902  0.0643  -0.0375 84  LYS   B NZ  
857  N N   . LEU   B 76  ? 0.8247 0.7085 0.6151 0.1843  0.0036  -0.0090 85  LEU   B N   
858  C CA  . LEU   B 76  ? 0.8545 0.7188 0.6240 0.2055  -0.0123 -0.0083 85  LEU   B CA  
859  C C   . LEU   B 76  ? 0.8976 0.7394 0.6477 0.1987  -0.0209 -0.0015 85  LEU   B C   
860  O O   . LEU   B 76  ? 0.9011 0.7407 0.6373 0.1907  -0.0116 0.0080  85  LEU   B O   
861  C CB  . LEU   B 76  ? 0.8579 0.7259 0.6117 0.2264  -0.0055 -0.0031 85  LEU   B CB  
862  C CG  . LEU   B 76  ? 0.8546 0.7410 0.6236 0.2308  0.0059  -0.0071 85  LEU   B CG  
863  C CD1 . LEU   B 76  ? 0.8609 0.7472 0.6139 0.2475  0.0135  0.0011  85  LEU   B CD1 
864  C CD2 . LEU   B 76  ? 0.8510 0.7408 0.6348 0.2418  -0.0055 -0.0198 85  LEU   B CD2 
865  N N   . ASP   B 77  ? 0.9227 0.7458 0.6711 0.2023  -0.0404 -0.0072 86  ASP   B N   
866  C CA  . ASP   B 77  ? 0.9596 0.7561 0.6884 0.1960  -0.0510 -0.0017 86  ASP   B CA  
867  C C   . ASP   B 77  ? 0.9793 0.7506 0.6835 0.2214  -0.0727 -0.0051 86  ASP   B C   
868  O O   . ASP   B 77  ? 1.0082 0.7548 0.6916 0.2199  -0.0825 -0.0005 86  ASP   B O   
869  C CB  . ASP   B 77  ? 0.9954 0.7860 0.7433 0.1678  -0.0536 -0.0027 86  ASP   B CB  
870  C CG  . ASP   B 77  ? 1.0868 0.8833 0.8642 0.1654  -0.0659 -0.0154 86  ASP   B CG  
871  O OD1 . ASP   B 77  ? 1.0962 0.8993 0.8764 0.1880  -0.0741 -0.0248 86  ASP   B OD1 
872  O OD2 . ASP   B 77  ? 1.1277 0.9226 0.9259 0.1410  -0.0675 -0.0157 86  ASP   B OD2 
873  N N   . ALA   B 78  ? 0.9653 0.7408 0.6678 0.2464  -0.0804 -0.0129 87  ALA   B N   
874  C CA  . ALA   B 78  ? 0.9774 0.7292 0.6524 0.2738  -0.1004 -0.0167 87  ALA   B CA  
875  C C   . ALA   B 78  ? 0.9864 0.7360 0.6326 0.2879  -0.0931 -0.0056 87  ALA   B C   
876  O O   . ALA   B 78  ? 0.9651 0.7360 0.6150 0.2831  -0.0729 0.0033  87  ALA   B O   
877  C CB  . ALA   B 78  ? 0.9668 0.7233 0.6423 0.2995  -0.1094 -0.0270 87  ALA   B CB  
878  N N   . ALA   B 79  ? 1.0100 0.7337 0.6286 0.3055  -0.1109 -0.0070 88  ALA   B N   
879  C CA  . ALA   B 79  ? 1.0317 0.7545 0.6239 0.3216  -0.1066 0.0021  88  ALA   B CA  
880  C C   . ALA   B 79  ? 1.0646 0.7768 0.6296 0.3591  -0.1205 -0.0028 88  ALA   B C   
881  O O   . ALA   B 79  ? 1.0737 0.7643 0.6323 0.3703  -0.1414 -0.0144 88  ALA   B O   
882  C CB  . ALA   B 79  ? 1.0425 0.7423 0.6227 0.3063  -0.1139 0.0065  88  ALA   B CB  
883  N N   . TRP   B 80  ? 1.0823 0.8097 0.6308 0.3791  -0.1095 0.0058  89  TRP   B N   
884  C CA  . TRP   B 80  ? 1.1161 0.8371 0.6348 0.4174  -0.1192 0.0034  89  TRP   B CA  
885  C C   . TRP   B 80  ? 1.1462 0.8306 0.6403 0.4261  -0.1446 -0.0038 89  TRP   B C   
886  O O   . TRP   B 80  ? 1.1395 0.8134 0.6333 0.4077  -0.1459 0.0006  89  TRP   B O   
887  C CB  . TRP   B 80  ? 1.1163 0.8645 0.6277 0.4304  -0.1001 0.0165  89  TRP   B CB  
888  C CG  . TRP   B 80  ? 1.1400 0.8876 0.6214 0.4708  -0.1059 0.0157  89  TRP   B CG  
889  C CD1 . TRP   B 80  ? 1.1626 0.9025 0.6282 0.4978  -0.1145 0.0082  89  TRP   B CD1 
890  C CD2 . TRP   B 80  ? 1.1493 0.9089 0.6131 0.4905  -0.1013 0.0232  89  TRP   B CD2 
891  N NE1 . TRP   B 80  ? 1.1767 0.9207 0.6127 0.5337  -0.1154 0.0107  89  TRP   B NE1 
892  C CE2 . TRP   B 80  ? 1.1681 0.9261 0.6045 0.5298  -0.1069 0.0199  89  TRP   B CE2 
893  C CE3 . TRP   B 80  ? 1.1532 0.9244 0.6207 0.4805  -0.0946 0.0312  89  TRP   B CE3 
894  C CZ2 . TRP   B 80  ? 1.1751 0.9455 0.5896 0.5590  -0.1043 0.0248  89  TRP   B CZ2 
895  C CZ3 . TRP   B 80  ? 1.1632 0.9471 0.6113 0.5090  -0.0936 0.0354  89  TRP   B CZ3 
896  C CH2 . TRP   B 80  ? 1.1658 0.9517 0.5892 0.5474  -0.0969 0.0328  89  TRP   B CH2 
897  N N   . ASP   B 81  ? 1.1807 0.8425 0.6524 0.4542  -0.1660 -0.0153 90  ASP   B N   
898  C CA  . ASP   B 81  ? 1.2306 0.8521 0.6773 0.4630  -0.1932 -0.0236 90  ASP   B CA  
899  C C   . ASP   B 81  ? 1.2708 0.8904 0.6857 0.4892  -0.1942 -0.0183 90  ASP   B C   
900  O O   . ASP   B 81  ? 1.3013 0.8850 0.6920 0.4982  -0.2170 -0.0247 90  ASP   B O   
901  C CB  . ASP   B 81  ? 1.2580 0.8502 0.6928 0.4812  -0.2206 -0.0405 90  ASP   B CB  
902  C CG  . ASP   B 81  ? 1.3324 0.9332 0.7431 0.5231  -0.2221 -0.0452 90  ASP   B CG  
903  O OD1 . ASP   B 81  ? 1.3396 0.9706 0.7426 0.5391  -0.2000 -0.0338 90  ASP   B OD1 
904  O OD2 . ASP   B 81  ? 1.3807 0.9583 0.7805 0.5399  -0.2452 -0.0602 90  ASP   B OD2 
905  N N   . GLY   B 82  ? 1.2620 0.9198 0.6789 0.5004  -0.1703 -0.0069 91  GLY   B N   
906  C CA  . GLY   B 82  ? 1.2781 0.9451 0.6716 0.5256  -0.1677 -0.0013 91  GLY   B CA  
907  C C   . GLY   B 82  ? 1.3018 0.9612 0.6604 0.5720  -0.1797 -0.0087 91  GLY   B C   
908  O O   . GLY   B 82  ? 1.3152 0.9813 0.6517 0.5977  -0.1801 -0.0060 91  GLY   B O   
909  N N   . LEU   B 83  ? 1.3031 0.9485 0.6552 0.5846  -0.1909 -0.0191 92  LEU   B N   
910  C CA  . LEU   B 83  ? 1.3263 0.9598 0.6414 0.6301  -0.2047 -0.0282 92  LEU   B CA  
911  C C   . LEU   B 83  ? 1.3272 0.9847 0.6431 0.6472  -0.1898 -0.0257 92  LEU   B C   
912  O O   . LEU   B 83  ? 1.3414 1.0166 0.6333 0.6825  -0.1802 -0.0211 92  LEU   B O   
913  C CB  . LEU   B 83  ? 1.3563 0.9372 0.6526 0.6360  -0.2418 -0.0473 92  LEU   B CB  
914  C CG  . LEU   B 83  ? 1.4124 0.9537 0.6889 0.6355  -0.2662 -0.0536 92  LEU   B CG  
915  C CD1 . LEU   B 83  ? 1.4479 0.9384 0.6994 0.6531  -0.3037 -0.0737 92  LEU   B CD1 
916  C CD2 . LEU   B 83  ? 1.4245 0.9796 0.6738 0.6656  -0.2597 -0.0472 92  LEU   B CD2 
917  N N   . SER   B 84  ? 1.3118 0.9674 0.6519 0.6253  -0.1895 -0.0295 93  SER   B N   
918  C CA  . SER   B 84  ? 1.2981 0.9657 0.6332 0.6443  -0.1820 -0.0303 93  SER   B CA  
919  C C   . SER   B 84  ? 1.2599 0.9703 0.6153 0.6354  -0.1466 -0.0120 93  SER   B C   
920  O O   . SER   B 84  ? 1.2436 0.9760 0.6271 0.6057  -0.1280 -0.0002 93  SER   B O   
921  C CB  . SER   B 84  ? 1.3260 0.9699 0.6752 0.6306  -0.2023 -0.0456 93  SER   B CB  
922  O OG  . SER   B 84  ? 1.3600 0.9834 0.7327 0.5954  -0.2170 -0.0519 93  SER   B OG  
923  N N   . GLU   B 85  ? 1.2495 0.9688 0.5880 0.6627  -0.1388 -0.0101 94  GLU   B N   
924  C CA  . GLU   B 85  ? 1.2316 0.9844 0.5861 0.6563  -0.1078 0.0067  94  GLU   B CA  
925  C C   . GLU   B 85  ? 1.2006 0.9547 0.5935 0.6183  -0.1043 0.0047  94  GLU   B C   
926  O O   . GLU   B 85  ? 1.2050 0.9358 0.6082 0.6044  -0.1262 -0.0107 94  GLU   B O   
927  C CB  . GLU   B 85  ? 1.2649 1.0202 0.5849 0.6980  -0.1021 0.0094  94  GLU   B CB  
928  C CG  . GLU   B 85  ? 1.3169 1.0894 0.6075 0.7315  -0.0903 0.0197  94  GLU   B CG  
929  C CD  . GLU   B 85  ? 1.4006 1.1817 0.6563 0.7721  -0.0776 0.0274  94  GLU   B CD  
930  O OE1 . GLU   B 85  ? 1.3794 1.1449 0.6248 0.7810  -0.0838 0.0215  94  GLU   B OE1 
931  O OE2 . GLU   B 85  ? 1.4391 1.2436 0.6775 0.7959  -0.0609 0.0397  94  GLU   B OE2 
932  N N   . VAL   B 86  ? 1.1632 0.9458 0.5791 0.6003  -0.0767 0.0204  95  VAL   B N   
933  C CA  . VAL   B 86  ? 1.1291 0.9175 0.5808 0.5657  -0.0694 0.0203  95  VAL   B CA  
934  C C   . VAL   B 86  ? 1.1158 0.9207 0.5682 0.5732  -0.0478 0.0323  95  VAL   B C   
935  O O   . VAL   B 86  ? 1.1388 0.9549 0.5685 0.5991  -0.0342 0.0442  95  VAL   B O   
936  C CB  . VAL   B 86  ? 1.0978 0.9007 0.5804 0.5281  -0.0583 0.0276  95  VAL   B CB  
937  C CG1 . VAL   B 86  ? 1.1091 0.8936 0.5849 0.5234  -0.0777 0.0192  95  VAL   B CG1 
938  C CG2 . VAL   B 86  ? 1.0802 0.9140 0.5690 0.5268  -0.0311 0.0471  95  VAL   B CG2 
939  N N   . GLN   B 87  ? 1.0819 0.8886 0.5599 0.5506  -0.0434 0.0301  96  GLN   B N   
940  C CA  . GLN   B 87  ? 1.0555 0.8732 0.5342 0.5552  -0.0238 0.0416  96  GLN   B CA  
941  C C   . GLN   B 87  ? 1.0196 0.8552 0.5342 0.5190  -0.0048 0.0511  96  GLN   B C   
942  O O   . GLN   B 87  ? 1.0028 0.8360 0.5431 0.4920  -0.0118 0.0416  96  GLN   B O   
943  C CB  . GLN   B 87  ? 1.0639 0.8632 0.5313 0.5723  -0.0383 0.0289  96  GLN   B CB  
944  C CG  . GLN   B 87  ? 1.1283 0.9139 0.5512 0.6166  -0.0477 0.0268  96  GLN   B CG  
945  C CD  . GLN   B 87  ? 1.1623 0.9289 0.5684 0.6388  -0.0634 0.0142  96  GLN   B CD  
946  O OE1 . GLN   B 87  ? 1.1588 0.9259 0.5852 0.6246  -0.0619 0.0108  96  GLN   B OE1 
947  N NE2 . GLN   B 87  ? 1.1838 0.9331 0.5501 0.6771  -0.0796 0.0064  96  GLN   B NE2 
948  N N   . LEU   B 88  ? 0.9996 0.8531 0.5156 0.5189  0.0192  0.0699  97  LEU   B N   
949  C CA  . LEU   B 88  ? 0.9765 0.8436 0.5228 0.4885  0.0364  0.0789  97  LEU   B CA  
950  C C   . LEU   B 88  ? 0.9786 0.8352 0.5209 0.4957  0.0399  0.0788  97  LEU   B C   
951  O O   . LEU   B 88  ? 0.9948 0.8477 0.5115 0.5220  0.0474  0.0882  97  LEU   B O   
952  C CB  . LEU   B 88  ? 0.9631 0.8535 0.5143 0.4854  0.0590  0.0995  97  LEU   B CB  
953  C CG  . LEU   B 88  ? 0.9541 0.8555 0.5333 0.4578  0.0773  0.1105  97  LEU   B CG  
954  C CD1 . LEU   B 88  ? 0.9303 0.8321 0.5375 0.4251  0.0707  0.1000  97  LEU   B CD1 
955  C CD2 . LEU   B 88  ? 0.9502 0.8752 0.5351 0.4575  0.0990  0.1317  97  LEU   B CD2 
956  N N   . LEU   B 89  ? 0.9608 0.8119 0.5252 0.4752  0.0341  0.0678  98  LEU   B N   
957  C CA  . LEU   B 89  ? 0.9658 0.8076 0.5286 0.4810  0.0372  0.0671  98  LEU   B CA  
958  C C   . LEU   B 89  ? 0.9672 0.8202 0.5478 0.4596  0.0597  0.0833  98  LEU   B C   
959  O O   . LEU   B 89  ? 0.9516 0.8104 0.5595 0.4317  0.0616  0.0788  98  LEU   B O   
960  C CB  . LEU   B 89  ? 0.9615 0.7955 0.5418 0.4708  0.0196  0.0462  98  LEU   B CB  
961  C CG  . LEU   B 89  ? 0.9809 0.8066 0.5648 0.4748  0.0198  0.0413  98  LEU   B CG  
962  C CD1 . LEU   B 89  ? 1.0157 0.8274 0.5654 0.5080  0.0217  0.0488  98  LEU   B CD1 
963  C CD2 . LEU   B 89  ? 0.9823 0.8051 0.5823 0.4715  -0.0012 0.0187  98  LEU   B CD2 
964  N N   . ALA   B 90  ? 0.9799 0.8372 0.5453 0.4722  0.0769  0.1029  99  ALA   B N   
965  C CA  . ALA   B 90  ? 0.9756 0.8432 0.5587 0.4522  0.0979  0.1204  99  ALA   B CA  
966  C C   . ALA   B 90  ? 0.9799 0.8315 0.5647 0.4488  0.1024  0.1217  99  ALA   B C   
967  O O   . ALA   B 90  ? 1.0016 0.8373 0.5604 0.4738  0.1014  0.1240  99  ALA   B O   
968  C CB  . ALA   B 90  ? 0.9735 0.8536 0.5421 0.4667  0.1153  0.1419  99  ALA   B CB  
969  N N   . VAL   B 91  ? 0.9568 0.8107 0.5691 0.4201  0.1073  0.1206  100 VAL   B N   
970  C CA  . VAL   B 91  ? 0.9583 0.7949 0.5719 0.4168  0.1114  0.1219  100 VAL   B CA  
971  C C   . VAL   B 91  ? 0.9631 0.8040 0.5903 0.3979  0.1308  0.1421  100 VAL   B C   
972  O O   . VAL   B 91  ? 0.9522 0.7997 0.6055 0.3710  0.1324  0.1392  100 VAL   B O   
973  C CB  . VAL   B 91  ? 0.9504 0.7836 0.5831 0.4022  0.0981  0.1004  100 VAL   B CB  
974  C CG1 . VAL   B 91  ? 0.9662 0.7801 0.5975 0.4031  0.1004  0.0997  100 VAL   B CG1 
975  C CG2 . VAL   B 91  ? 0.9440 0.7774 0.5700 0.4168  0.0788  0.0815  100 VAL   B CG2 
976  N N   . PRO   B 92  ? 0.9807 0.8186 0.5905 0.4119  0.1455  0.1632  101 PRO   B N   
977  C CA  . PRO   B 92  ? 0.9846 0.8292 0.6115 0.3921  0.1641  0.1841  101 PRO   B CA  
978  C C   . PRO   B 92  ? 1.0093 0.8291 0.6414 0.3799  0.1676  0.1873  101 PRO   B C   
979  O O   . PRO   B 92  ? 1.0298 0.8254 0.6425 0.3956  0.1599  0.1794  101 PRO   B O   
980  C CB  . PRO   B 92  ? 1.0065 0.8579 0.6108 0.4143  0.1796  0.2061  101 PRO   B CB  
981  C CG  . PRO   B 92  ? 1.0220 0.8681 0.5938 0.4476  0.1668  0.1944  101 PRO   B CG  
982  C CD  . PRO   B 92  ? 0.9984 0.8273 0.5718 0.4464  0.1462  0.1696  101 PRO   B CD  
983  N N   . PRO   B 93  ? 1.0021 0.8263 0.6602 0.3526  0.1773  0.1977  102 PRO   B N   
984  C CA  . PRO   B 93  ? 1.0143 0.8103 0.6761 0.3407  0.1786  0.1999  102 PRO   B CA  
985  C C   . PRO   B 93  ? 1.0509 0.8200 0.6833 0.3605  0.1885  0.2175  102 PRO   B C   
986  O O   . PRO   B 93  ? 1.0557 0.8325 0.6787 0.3683  0.2045  0.2401  102 PRO   B O   
987  C CB  . PRO   B 93  ? 1.0035 0.8117 0.6986 0.3089  0.1867  0.2097  102 PRO   B CB  
988  C CG  . PRO   B 93  ? 0.9919 0.8366 0.7037 0.3028  0.1848  0.2050  102 PRO   B CG  
989  C CD  . PRO   B 93  ? 0.9759 0.8298 0.6615 0.3322  0.1850  0.2063  102 PRO   B CD  
990  N N   . GLY   B 94  ? 1.0732 0.8118 0.6893 0.3709  0.1788  0.2069  103 GLY   B N   
991  C CA  . GLY   B 94  ? 1.1014 0.8078 0.6846 0.3920  0.1850  0.2210  103 GLY   B CA  
992  C C   . GLY   B 94  ? 1.1212 0.8286 0.6687 0.4275  0.1841  0.2231  103 GLY   B C   
993  O O   . GLY   B 94  ? 1.1380 0.8178 0.6526 0.4489  0.1887  0.2348  103 GLY   B O   
994  N N   . GLU   B 95  ? 1.1200 0.8558 0.6707 0.4353  0.1774  0.2119  104 GLU   B N   
995  C CA  . GLU   B 95  ? 1.1439 0.8799 0.6595 0.4702  0.1743  0.2121  104 GLU   B CA  
996  C C   . GLU   B 95  ? 1.1468 0.8853 0.6599 0.4834  0.1500  0.1824  104 GLU   B C   
997  O O   . GLU   B 95  ? 1.1262 0.8780 0.6691 0.4627  0.1395  0.1644  104 GLU   B O   
998  C CB  . GLU   B 95  ? 1.1695 0.9352 0.6859 0.4727  0.1884  0.2279  104 GLU   B CB  
999  C CG  . GLU   B 95  ? 1.2341 1.0048 0.7605 0.4568  0.2137  0.2582  104 GLU   B CG  
1000 C CD  . GLU   B 95  ? 1.3055 1.1118 0.8382 0.4587  0.2289  0.2736  104 GLU   B CD  
1001 O OE1 . GLU   B 95  ? 1.3127 1.1372 0.8379 0.4745  0.2186  0.2602  104 GLU   B OE1 
1002 O OE2 . GLU   B 95  ? 1.3336 1.1498 0.8793 0.4448  0.2506  0.2991  104 GLU   B OE2 
1003 N N   . ARG   B 96  ? 1.1635 0.8889 0.6409 0.5180  0.1409  0.1775  105 ARG   B N   
1004 C CA  . ARG   B 96  ? 1.1772 0.9044 0.6524 0.5325  0.1163  0.1498  105 ARG   B CA  
1005 C C   . ARG   B 96  ? 1.1611 0.9170 0.6522 0.5258  0.1093  0.1396  105 ARG   B C   
1006 O O   . ARG   B 96  ? 1.1618 0.9336 0.6511 0.5239  0.1230  0.1555  105 ARG   B O   
1007 C CB  . ARG   B 96  ? 1.2357 0.9393 0.6656 0.5731  0.1081  0.1490  105 ARG   B CB  
1008 C CG  . ARG   B 96  ? 1.3061 1.0116 0.7312 0.5922  0.0811  0.1212  105 ARG   B CG  
1009 C CD  . ARG   B 96  ? 1.3962 1.0737 0.7912 0.6228  0.0670  0.1122  105 ARG   B CD  
1010 N NE  . ARG   B 96  ? 1.4727 1.1276 0.8189 0.6531  0.0786  0.1333  105 ARG   B NE  
1011 C CZ  . ARG   B 96  ? 1.5475 1.2014 0.8585 0.6836  0.0750  0.1355  105 ARG   B CZ  
1012 N NH1 . ARG   B 96  ? 1.5446 1.2175 0.8654 0.6864  0.0594  0.1182  105 ARG   B NH1 
1013 N NH2 . ARG   B 96  ? 1.5716 1.2040 0.8356 0.7119  0.0874  0.1559  105 ARG   B NH2 
1014 N N   . ALA   B 97  ? 1.1410 0.9039 0.6495 0.5211  0.0884  0.1139  106 ALA   B N   
1015 C CA  . ALA   B 97  ? 1.1274 0.9106 0.6488 0.5153  0.0782  0.1023  106 ALA   B CA  
1016 C C   . ALA   B 97  ? 1.1546 0.9359 0.6413 0.5471  0.0749  0.1068  106 ALA   B C   
1017 O O   . ALA   B 97  ? 1.1754 0.9381 0.6304 0.5774  0.0670  0.1041  106 ALA   B O   
1018 C CB  . ALA   B 97  ? 1.1108 0.8957 0.6513 0.5096  0.0561  0.0756  106 ALA   B CB  
1019 N N   . LYS   B 98  ? 1.1578 0.9573 0.6478 0.5428  0.0799  0.1129  107 LYS   B N   
1020 C CA  . LYS   B 98  ? 1.1824 0.9814 0.6375 0.5749  0.0781  0.1176  107 LYS   B CA  
1021 C C   . LYS   B 98  ? 1.1702 0.9828 0.6347 0.5705  0.0649  0.1053  107 LYS   B C   
1022 O O   . LYS   B 98  ? 1.1620 0.9921 0.6558 0.5425  0.0714  0.1080  107 LYS   B O   
1023 C CB  . LYS   B 98  ? 1.2231 1.0314 0.6663 0.5788  0.1058  0.1464  107 LYS   B CB  
1024 C CG  . LYS   B 98  ? 1.3236 1.1291 0.7228 0.6178  0.1101  0.1562  107 LYS   B CG  
1025 C CD  . LYS   B 98  ? 1.3931 1.2144 0.7881 0.6169  0.1416  0.1873  107 LYS   B CD  
1026 C CE  . LYS   B 98  ? 1.4043 1.2569 0.8400 0.5844  0.1542  0.1955  107 LYS   B CE  
1027 N NZ  . LYS   B 98  ? 1.3988 1.2523 0.8698 0.5481  0.1660  0.2044  107 LYS   B NZ  
1028 N N   . ASN   B 99  ? 1.1729 0.9750 0.6115 0.5984  0.0450  0.0914  108 ASN   B N   
1029 C CA  . ASN   B 99  ? 1.1717 0.9807 0.6154 0.5961  0.0303  0.0797  108 ASN   B CA  
1030 C C   . ASN   B 99  ? 1.1808 1.0009 0.6001 0.6165  0.0424  0.0946  108 ASN   B C   
1031 O O   . ASN   B 99  ? 1.2136 1.0258 0.5960 0.6496  0.0472  0.1025  108 ASN   B O   
1032 C CB  . ASN   B 99  ? 1.1899 0.9796 0.6198 0.6152  -0.0005 0.0552  108 ASN   B CB  
1033 C CG  . ASN   B 99  ? 1.2286 1.0128 0.6877 0.5952  -0.0155 0.0372  108 ASN   B CG  
1034 O OD1 . ASN   B 99  ? 1.2432 1.0218 0.7055 0.5954  -0.0114 0.0377  108 ASN   B OD1 
1035 N ND2 . ASN   B 99  ? 1.2196 1.0045 0.6995 0.5796  -0.0341 0.0204  108 ASN   B ND2 
1036 N N   . ILE   B 100 ? 1.1564 0.9951 0.5939 0.5996  0.0471  0.0982  109 ILE   B N   
1037 C CA  . ILE   B 100 ? 1.1553 1.0094 0.5735 0.6193  0.0577  0.1106  109 ILE   B CA  
1038 C C   . ILE   B 100 ? 1.1516 1.0022 0.5669 0.6229  0.0360  0.0943  109 ILE   B C   
1039 O O   . ILE   B 100 ? 1.1361 0.9917 0.5813 0.5930  0.0302  0.0877  109 ILE   B O   
1040 C CB  . ILE   B 100 ? 1.1477 1.0310 0.5920 0.5965  0.0854  0.1327  109 ILE   B CB  
1041 C CG1 . ILE   B 100 ? 1.1653 1.0479 0.6151 0.5885  0.1062  0.1496  109 ILE   B CG1 
1042 C CG2 . ILE   B 100 ? 1.1522 1.0571 0.5803 0.6179  0.0962  0.1445  109 ILE   B CG2 
1043 C CD1 . ILE   B 100 ? 1.2011 1.0748 0.6093 0.6253  0.1166  0.1623  109 ILE   B CD1 
1044 N N   . GLN   B 101 ? 1.1623 1.0026 0.5394 0.6601  0.0243  0.0885  110 GLN   B N   
1045 C CA  . GLN   B 101 ? 1.1779 1.0090 0.5467 0.6676  0.0014  0.0727  110 GLN   B CA  
1046 C C   . GLN   B 101 ? 1.1758 1.0314 0.5435 0.6723  0.0148  0.0849  110 GLN   B C   
1047 O O   . GLN   B 101 ? 1.1854 1.0576 0.5325 0.6970  0.0333  0.1002  110 GLN   B O   
1048 C CB  . GLN   B 101 ? 1.2243 1.0278 0.5499 0.7080  -0.0224 0.0570  110 GLN   B CB  
1049 C CG  . GLN   B 101 ? 1.2666 1.0522 0.5834 0.7144  -0.0511 0.0379  110 GLN   B CG  
1050 C CD  . GLN   B 101 ? 1.3430 1.0954 0.6309 0.7415  -0.0814 0.0168  110 GLN   B CD  
1051 O OE1 . GLN   B 101 ? 1.3296 1.0715 0.6229 0.7386  -0.0876 0.0101  110 GLN   B OE1 
1052 N NE2 . GLN   B 101 ? 1.3946 1.1294 0.6508 0.7700  -0.1026 0.0047  110 GLN   B NE2 
1053 N N   . THR   B 102 ? 1.1611 1.0191 0.5492 0.6509  0.0050  0.0779  111 THR   B N   
1054 C CA  . THR   B 102 ? 1.1581 1.0393 0.5467 0.6560  0.0141  0.0868  111 THR   B CA  
1055 C C   . THR   B 102 ? 1.1702 1.0331 0.5559 0.6525  -0.0118 0.0700  111 THR   B C   
1056 O O   . THR   B 102 ? 1.1849 1.0222 0.5798 0.6345  -0.0319 0.0548  111 THR   B O   
1057 C CB  . THR   B 102 ? 1.1593 1.0729 0.5877 0.6228  0.0400  0.1046  111 THR   B CB  
1058 O OG1 . THR   B 102 ? 1.1623 1.1052 0.5916 0.6328  0.0519  0.1154  111 THR   B OG1 
1059 C CG2 . THR   B 102 ? 1.1515 1.0581 0.6159 0.5798  0.0322  0.0967  111 THR   B CG2 
1060 N N   . LEU   B 103 ? 1.1626 1.0381 0.5356 0.6698  -0.0116 0.0728  112 LEU   B N   
1061 C CA  . LEU   B 103 ? 1.1715 1.0277 0.5413 0.6648  -0.0353 0.0589  112 LEU   B CA  
1062 C C   . LEU   B 103 ? 1.1481 1.0316 0.5532 0.6333  -0.0204 0.0698  112 LEU   B C   
1063 O O   . LEU   B 103 ? 1.1304 1.0496 0.5431 0.6402  0.0007  0.0848  112 LEU   B O   
1064 C CB  . LEU   B 103 ? 1.1956 1.0427 0.5253 0.7067  -0.0499 0.0516  112 LEU   B CB  
1065 C CG  . LEU   B 103 ? 1.2293 1.0511 0.5572 0.6970  -0.0755 0.0380  112 LEU   B CG  
1066 C CD1 . LEU   B 103 ? 1.2599 1.0346 0.5706 0.6998  -0.1069 0.0180  112 LEU   B CD1 
1067 C CD2 . LEU   B 103 ? 1.2465 1.0798 0.5523 0.7264  -0.0776 0.0392  112 LEU   B CD2 
1068 N N   . PRO   B 104 ? 1.1432 1.0113 0.5704 0.5989  -0.0313 0.0625  113 PRO   B N   
1069 C CA  . PRO   B 104 ? 1.1292 1.0208 0.5873 0.5695  -0.0187 0.0718  113 PRO   B CA  
1070 C C   . PRO   B 104 ? 1.1474 1.0504 0.5967 0.5829  -0.0231 0.0730  113 PRO   B C   
1071 O O   . PRO   B 104 ? 1.1733 1.0526 0.5933 0.6057  -0.0441 0.0619  113 PRO   B O   
1072 C CB  . PRO   B 104 ? 1.1318 0.9992 0.6083 0.5339  -0.0310 0.0622  113 PRO   B CB  
1073 C CG  . PRO   B 104 ? 1.1530 0.9938 0.6182 0.5406  -0.0439 0.0510  113 PRO   B CG  
1074 C CD  . PRO   B 104 ? 1.1441 0.9757 0.5717 0.5840  -0.0536 0.0466  113 PRO   B CD  
1075 N N   . GLY   B 105 ? 1.1261 1.0643 0.6027 0.5670  -0.0047 0.0856  114 GLY   B N   
1076 C CA  . GLY   B 105 ? 1.1217 1.0761 0.5997 0.5722  -0.0077 0.0871  114 GLY   B CA  
1077 C C   . GLY   B 105 ? 1.1301 1.0621 0.6185 0.5414  -0.0222 0.0797  114 GLY   B C   
1078 O O   . GLY   B 105 ? 1.1394 1.0394 0.6266 0.5230  -0.0332 0.0713  114 GLY   B O   
1079 N N   . ILE   B 106 ? 1.1226 1.0714 0.6202 0.5367  -0.0226 0.0825  115 ILE   B N   
1080 C CA  . ILE   B 106 ? 1.1303 1.0568 0.6315 0.5112  -0.0363 0.0766  115 ILE   B CA  
1081 C C   . ILE   B 106 ? 1.1018 1.0622 0.6336 0.4908  -0.0236 0.0853  115 ILE   B C   
1082 O O   . ILE   B 106 ? 1.0909 1.0876 0.6315 0.5066  -0.0150 0.0919  115 ILE   B O   
1083 C CB  . ILE   B 106 ? 1.1705 1.0672 0.6371 0.5339  -0.0613 0.0664  115 ILE   B CB  
1084 C CG1 . ILE   B 106 ? 1.2258 1.0806 0.6610 0.5518  -0.0799 0.0549  115 ILE   B CG1 
1085 C CG2 . ILE   B 106 ? 1.1855 1.0624 0.6528 0.5110  -0.0735 0.0635  115 ILE   B CG2 
1086 C CD1 . ILE   B 106 ? 1.2634 1.0823 0.7020 0.5235  -0.0899 0.0484  115 ILE   B CD1 
1087 N N   . PHE   B 107 ? 1.0901 1.0381 0.6367 0.4572  -0.0244 0.0841  116 PHE   B N   
1088 C CA  . PHE   B 107 ? 1.0693 1.0400 0.6390 0.4377  -0.0189 0.0888  116 PHE   B CA  
1089 C C   . PHE   B 107 ? 1.0936 1.0330 0.6391 0.4381  -0.0404 0.0808  116 PHE   B C   
1090 O O   . PHE   B 107 ? 1.1148 1.0148 0.6454 0.4242  -0.0513 0.0747  116 PHE   B O   
1091 C CB  . PHE   B 107 ? 1.0512 1.0214 0.6457 0.4022  -0.0082 0.0909  116 PHE   B CB  
1092 C CG  . PHE   B 107 ? 1.0273 1.0308 0.6520 0.3945  0.0135  0.1007  116 PHE   B CG  
1093 C CD1 . PHE   B 107 ? 1.0180 1.0494 0.6462 0.4179  0.0252  0.1087  116 PHE   B CD1 
1094 C CD2 . PHE   B 107 ? 1.0180 1.0227 0.6652 0.3647  0.0225  0.1022  116 PHE   B CD2 
1095 C CE1 . PHE   B 107 ? 1.0058 1.0638 0.6603 0.4094  0.0457  0.1196  116 PHE   B CE1 
1096 C CE2 . PHE   B 107 ? 1.0057 1.0354 0.6787 0.3575  0.0410  0.1113  116 PHE   B CE2 
1097 C CZ  . PHE   B 107 ? 0.9955 1.0506 0.6722 0.3787  0.0526  0.1207  116 PHE   B CZ  
1098 N N   . LYS   B 108 ? 1.0883 1.0442 0.6295 0.4541  -0.0467 0.0813  117 LYS   B N   
1099 C CA  . LYS   B 108 ? 1.1093 1.0335 0.6252 0.4552  -0.0675 0.0747  117 LYS   B CA  
1100 C C   . LYS   B 108 ? 1.0899 1.0267 0.6260 0.4283  -0.0636 0.0776  117 LYS   B C   
1101 O O   . LYS   B 108 ? 1.0624 1.0429 0.6262 0.4287  -0.0530 0.0827  117 LYS   B O   
1102 C CB  . LYS   B 108 ? 1.1524 1.0859 0.6490 0.4916  -0.0790 0.0719  117 LYS   B CB  
1103 C CG  . LYS   B 108 ? 1.2418 1.1711 0.7185 0.5242  -0.0810 0.0691  117 LYS   B CG  
1104 C CD  . LYS   B 108 ? 1.3251 1.2745 0.7872 0.5628  -0.0885 0.0669  117 LYS   B CD  
1105 C CE  . LYS   B 108 ? 1.3681 1.3774 0.8566 0.5796  -0.0659 0.0758  117 LYS   B CE  
1106 N NZ  . LYS   B 108 ? 1.4107 1.4375 0.8796 0.6233  -0.0726 0.0724  117 LYS   B NZ  
1107 N N   . THR   B 109 ? 1.0975 0.9976 0.6214 0.4045  -0.0713 0.0746  118 THR   B N   
1108 C CA  . THR   B 109 ? 1.0951 1.0010 0.6308 0.3807  -0.0694 0.0761  118 THR   B CA  
1109 C C   . THR   B 109 ? 1.1288 0.9960 0.6299 0.3821  -0.0896 0.0723  118 THR   B C   
1110 O O   . THR   B 109 ? 1.1558 0.9859 0.6260 0.3952  -0.1040 0.0687  118 THR   B O   
1111 C CB  . THR   B 109 ? 1.0941 0.9971 0.6489 0.3484  -0.0555 0.0779  118 THR   B CB  
1112 O OG1 . THR   B 109 ? 1.1218 0.9803 0.6538 0.3333  -0.0631 0.0747  118 THR   B OG1 
1113 C CG2 . THR   B 109 ? 1.0750 1.0008 0.6539 0.3485  -0.0387 0.0812  118 THR   B CG2 
1114 N N   . LYS   B 110 ? 1.1241 0.9965 0.6287 0.3685  -0.0916 0.0728  119 LYS   B N   
1115 C CA  . LYS   B 110 ? 1.1589 0.9917 0.6277 0.3683  -0.1094 0.0707  119 LYS   B CA  
1116 C C   . LYS   B 110 ? 1.1960 0.9794 0.6425 0.3474  -0.1111 0.0714  119 LYS   B C   
1117 O O   . LYS   B 110 ? 1.2225 0.9633 0.6339 0.3492  -0.1263 0.0712  119 LYS   B O   
1118 C CB  . LYS   B 110 ? 1.1634 1.0137 0.6406 0.3582  -0.1106 0.0708  119 LYS   B CB  
1119 C CG  . LYS   B 110 ? 1.1960 1.0514 0.6921 0.3267  -0.0961 0.0726  119 LYS   B CG  
1120 C CD  . LYS   B 110 ? 1.2499 1.1050 0.7393 0.3174  -0.1027 0.0710  119 LYS   B CD  
1121 C CE  . LYS   B 110 ? 1.2867 1.1363 0.7838 0.2884  -0.0907 0.0717  119 LYS   B CE  
1122 N NZ  . LYS   B 110 ? 1.2914 1.1853 0.8286 0.2802  -0.0813 0.0700  119 LYS   B NZ  
1123 N N   . ASP   B 111 ? 1.1898 0.9793 0.6576 0.3282  -0.0956 0.0727  120 ASP   B N   
1124 C CA  . ASP   B 111 ? 1.2122 0.9652 0.6685 0.3072  -0.0945 0.0733  120 ASP   B CA  
1125 C C   . ASP   B 111 ? 1.2224 0.9604 0.6773 0.3153  -0.0973 0.0705  120 ASP   B C   
1126 O O   . ASP   B 111 ? 1.2373 0.9547 0.6934 0.2963  -0.0939 0.0704  120 ASP   B O   
1127 C CB  . ASP   B 111 ? 1.2236 0.9942 0.7046 0.2799  -0.0764 0.0750  120 ASP   B CB  
1128 C CG  . ASP   B 111 ? 1.2808 1.0570 0.7577 0.2692  -0.0757 0.0763  120 ASP   B CG  
1129 O OD1 . ASP   B 111 ? 1.3023 1.0451 0.7479 0.2654  -0.0859 0.0780  120 ASP   B OD1 
1130 O OD2 . ASP   B 111 ? 1.3016 1.1135 0.8055 0.2646  -0.0657 0.0757  120 ASP   B OD2 
1131 N N   . GLY   B 112 ? 1.2110 0.9608 0.6639 0.3436  -0.1033 0.0677  121 GLY   B N   
1132 C CA  . GLY   B 112 ? 1.2155 0.9498 0.6635 0.3551  -0.1085 0.0635  121 GLY   B CA  
1133 C C   . GLY   B 112 ? 1.1941 0.9669 0.6647 0.3712  -0.0965 0.0632  121 GLY   B C   
1134 O O   . GLY   B 112 ? 1.1724 0.9859 0.6679 0.3689  -0.0814 0.0676  121 GLY   B O   
1135 N N   . ASP   B 113 ? 1.2018 0.9600 0.6622 0.3882  -0.1038 0.0583  122 ASP   B N   
1136 C CA  . ASP   B 113 ? 1.1900 0.9790 0.6642 0.4071  -0.0932 0.0585  122 ASP   B CA  
1137 C C   . ASP   B 113 ? 1.1741 0.9679 0.6701 0.3884  -0.0807 0.0583  122 ASP   B C   
1138 O O   . ASP   B 113 ? 1.1907 0.9553 0.6839 0.3707  -0.0874 0.0542  122 ASP   B O   
1139 C CB  . ASP   B 113 ? 1.2395 1.0091 0.6855 0.4411  -0.1099 0.0519  122 ASP   B CB  
1140 C CG  . ASP   B 113 ? 1.3456 1.1156 0.7696 0.4675  -0.1219 0.0509  122 ASP   B CG  
1141 O OD1 . ASP   B 113 ? 1.3685 1.1558 0.8006 0.4592  -0.1178 0.0556  122 ASP   B OD1 
1142 O OD2 . ASP   B 113 ? 1.3995 1.1523 0.7970 0.4983  -0.1367 0.0444  122 ASP   B OD2 
1143 N N   . ILE   B 114 ? 1.1360 0.9672 0.6545 0.3927  -0.0627 0.0632  123 ILE   B N   
1144 C CA  . ILE   B 114 ? 1.1189 0.9575 0.6578 0.3783  -0.0501 0.0634  123 ILE   B CA  
1145 C C   . ILE   B 114 ? 1.1001 0.9552 0.6370 0.4055  -0.0442 0.0646  123 ILE   B C   
1146 O O   . ILE   B 114 ? 1.0916 0.9724 0.6274 0.4257  -0.0382 0.0703  123 ILE   B O   
1147 C CB  . ILE   B 114 ? 1.1047 0.9709 0.6728 0.3531  -0.0316 0.0701  123 ILE   B CB  
1148 C CG1 . ILE   B 114 ? 1.1310 0.9840 0.6965 0.3308  -0.0364 0.0697  123 ILE   B CG1 
1149 C CG2 . ILE   B 114 ? 1.1010 0.9728 0.6888 0.3389  -0.0193 0.0697  123 ILE   B CG2 
1150 C CD1 . ILE   B 114 ? 1.1349 1.0164 0.7235 0.3140  -0.0226 0.0752  123 ILE   B CD1 
1151 N N   . GLY   B 115 ? 1.0874 0.9303 0.6246 0.4065  -0.0454 0.0596  124 GLY   B N   
1152 C CA  . GLY   B 115 ? 1.0801 0.9364 0.6120 0.4325  -0.0389 0.0614  124 GLY   B CA  
1153 C C   . GLY   B 115 ? 1.0502 0.9446 0.6066 0.4266  -0.0147 0.0735  124 GLY   B C   
1154 O O   . GLY   B 115 ? 1.0474 0.9525 0.6272 0.3990  -0.0049 0.0773  124 GLY   B O   
1155 N N   . ALA   B 116 ? 1.0317 0.9463 0.5823 0.4521  -0.0048 0.0802  125 ALA   B N   
1156 C CA  . ALA   B 116 ? 1.0098 0.9592 0.5845 0.4455  0.0187  0.0937  125 ALA   B CA  
1157 C C   . ALA   B 116 ? 1.0244 0.9813 0.5882 0.4701  0.0289  0.0994  125 ALA   B C   
1158 O O   . ALA   B 116 ? 1.0468 0.9963 0.5830 0.5011  0.0205  0.0959  125 ALA   B O   
1159 C CB  . ALA   B 116 ? 0.9882 0.9682 0.5754 0.4459  0.0258  0.1019  125 ALA   B CB  
1160 N N   . VAL   B 117 ? 1.0201 0.9886 0.6020 0.4581  0.0460  0.1079  126 VAL   B N   
1161 C CA  A VAL   B 117 ? 1.0342 1.0073 0.6032 0.4809  0.0572  0.1153  126 VAL   B CA  
1162 C CA  B VAL   B 117 ? 1.0352 1.0078 0.6048 0.4800  0.0571  0.1151  126 VAL   B CA  
1163 C C   . VAL   B 117 ? 1.0314 1.0416 0.6187 0.4810  0.0820  0.1345  126 VAL   B C   
1164 O O   . VAL   B 117 ? 1.0188 1.0439 0.6370 0.4533  0.0933  0.1417  126 VAL   B O   
1165 C CB  A VAL   B 117 ? 1.0451 0.9947 0.6116 0.4748  0.0545  0.1091  126 VAL   B CB  
1166 C CB  B VAL   B 117 ? 1.0460 0.9955 0.6180 0.4678  0.0544  0.1085  126 VAL   B CB  
1167 C CG1 A VAL   B 117 ? 1.0672 0.9839 0.6120 0.4847  0.0295  0.0910  126 VAL   B CG1 
1168 C CG1 B VAL   B 117 ? 1.0497 1.0076 0.6206 0.4772  0.0725  0.1209  126 VAL   B CG1 
1169 C CG2 A VAL   B 117 ? 1.0373 0.9891 0.6350 0.4388  0.0621  0.1104  126 VAL   B CG2 
1170 C CG2 B VAL   B 117 ? 1.0679 0.9850 0.6158 0.4814  0.0307  0.0913  126 VAL   B CG2 
1171 N N   . ALA   B 118 ? 1.0488 1.0747 0.6172 0.5128  0.0899  0.1427  127 ALA   B N   
1172 C CA  . ALA   B 118 ? 1.0483 1.1134 0.6348 0.5150  0.1146  0.1625  127 ALA   B CA  
1173 C C   . ALA   B 118 ? 1.0643 1.1283 0.6473 0.5191  0.1329  0.1757  127 ALA   B C   
1174 O O   . ALA   B 118 ? 1.0747 1.1491 0.6363 0.5483  0.1446  0.1859  127 ALA   B O   
1175 C CB  . ALA   B 118 ? 1.0495 1.1379 0.6196 0.5474  0.1159  0.1656  127 ALA   B CB  
1176 N N   . LEU   B 119 ? 1.0634 1.1129 0.6648 0.4910  0.1351  0.1754  128 LEU   B N   
1177 C CA  . LEU   B 119 ? 1.0704 1.1130 0.6683 0.4921  0.1508  0.1876  128 LEU   B CA  
1178 C C   . LEU   B 119 ? 1.0494 1.1054 0.6869 0.4568  0.1652  0.1990  128 LEU   B C   
1179 O O   . LEU   B 119 ? 1.0475 1.0975 0.7065 0.4295  0.1550  0.1886  128 LEU   B O   
1180 C CB  . LEU   B 119 ? 1.0998 1.1031 0.6759 0.4969  0.1346  0.1723  128 LEU   B CB  
1181 C CG  . LEU   B 119 ? 1.1429 1.1276 0.6787 0.5325  0.1180  0.1601  128 LEU   B CG  
1182 C CD1 . LEU   B 119 ? 1.1653 1.1147 0.6895 0.5312  0.0989  0.1425  128 LEU   B CD1 
1183 C CD2 . LEU   B 119 ? 1.1597 1.1550 0.6671 0.5674  0.1334  0.1748  128 LEU   B CD2 
1184 N N   . ASP   B 120 ? 1.0331 1.1059 0.6792 0.4572  0.1884  0.2203  129 ASP   B N   
1185 C CA  . ASP   B 120 ? 1.0169 1.0988 0.7006 0.4235  0.2008  0.2314  129 ASP   B CA  
1186 C C   . ASP   B 120 ? 1.0090 1.0601 0.6844 0.4170  0.2048  0.2345  129 ASP   B C   
1187 O O   . ASP   B 120 ? 1.0263 1.0667 0.6744 0.4397  0.2141  0.2444  129 ASP   B O   
1188 C CB  . ASP   B 120 ? 1.0380 1.1612 0.7468 0.4205  0.2236  0.2540  129 ASP   B CB  
1189 C CG  . ASP   B 120 ? 1.1129 1.2535 0.8694 0.3827  0.2263  0.2575  129 ASP   B CG  
1190 O OD1 . ASP   B 120 ? 1.1304 1.2453 0.8965 0.3587  0.2165  0.2478  129 ASP   B OD1 
1191 O OD2 . ASP   B 120 ? 1.1327 1.3136 0.9170 0.3781  0.2370  0.2689  129 ASP   B OD2 
1192 N N   . TYR   B 121 ? 0.9843 1.0203 0.6811 0.3877  0.1974  0.2260  130 TYR   B N   
1193 C CA  . TYR   B 121 ? 0.9857 0.9911 0.6771 0.3799  0.1986  0.2263  130 TYR   B CA  
1194 C C   . TYR   B 121 ? 0.9607 0.9669 0.6886 0.3437  0.2018  0.2290  130 TYR   B C   
1195 O O   . TYR   B 121 ? 0.9485 0.9737 0.7022 0.3252  0.1966  0.2236  130 TYR   B O   
1196 C CB  . TYR   B 121 ? 1.0074 0.9835 0.6766 0.3891  0.1778  0.2034  130 TYR   B CB  
1197 C CG  . TYR   B 121 ? 1.0371 1.0000 0.6668 0.4250  0.1744  0.2019  130 TYR   B CG  
1198 C CD1 . TYR   B 121 ? 1.0638 1.0067 0.6721 0.4395  0.1827  0.2114  130 TYR   B CD1 
1199 C CD2 . TYR   B 121 ? 1.0556 1.0239 0.6668 0.4461  0.1621  0.1913  130 TYR   B CD2 
1200 C CE1 . TYR   B 121 ? 1.0989 1.0296 0.6679 0.4751  0.1790  0.2100  130 TYR   B CE1 
1201 C CE2 . TYR   B 121 ? 1.0855 1.0405 0.6586 0.4810  0.1572  0.1889  130 TYR   B CE2 
1202 C CZ  . TYR   B 121 ? 1.1173 1.0548 0.6692 0.4960  0.1660  0.1983  130 TYR   B CZ  
1203 O OH  . TYR   B 121 ? 1.1625 1.0855 0.6736 0.5326  0.1598  0.1952  130 TYR   B OH  
1204 N N   . PRO   B 122 ? 0.9488 0.9313 0.6772 0.3344  0.2081  0.2357  131 PRO   B N   
1205 C CA  . PRO   B 122 ? 0.9149 0.8940 0.6759 0.3012  0.2086  0.2365  131 PRO   B CA  
1206 C C   . PRO   B 122 ? 0.8841 0.8578 0.6557 0.2850  0.1896  0.2129  131 PRO   B C   
1207 O O   . PRO   B 122 ? 0.8890 0.8511 0.6406 0.2978  0.1765  0.1962  131 PRO   B O   
1208 C CB  . PRO   B 122 ? 0.9499 0.8952 0.6978 0.3018  0.2143  0.2435  131 PRO   B CB  
1209 C CG  . PRO   B 122 ? 0.9772 0.9197 0.6919 0.3335  0.2259  0.2578  131 PRO   B CG  
1210 C CD  . PRO   B 122 ? 0.9656 0.9219 0.6629 0.3552  0.2144  0.2434  131 PRO   B CD  
1211 N N   . ALA   B 123 ? 0.8479 0.8304 0.6510 0.2571  0.1880  0.2119  132 ALA   B N   
1212 C CA  . ALA   B 123 ? 0.8358 0.8138 0.6486 0.2403  0.1721  0.1917  132 ALA   B CA  
1213 C C   . ALA   B 123 ? 0.8442 0.7916 0.6374 0.2447  0.1615  0.1745  132 ALA   B C   
1214 O O   . ALA   B 123 ? 0.8361 0.7826 0.6232 0.2448  0.1490  0.1574  132 ALA   B O   
1215 C CB  . ALA   B 123 ? 0.8224 0.8046 0.6674 0.2116  0.1728  0.1950  132 ALA   B CB  
1216 N N   . GLY   B 124 ? 0.8444 0.7679 0.6279 0.2494  0.1670  0.1801  133 GLY   B N   
1217 C CA  . GLY   B 124 ? 0.8484 0.7448 0.6156 0.2558  0.1582  0.1651  133 GLY   B CA  
1218 C C   . GLY   B 124 ? 0.8431 0.7375 0.5862 0.2796  0.1503  0.1545  133 GLY   B C   
1219 O O   . GLY   B 124 ? 0.8372 0.7150 0.5711 0.2848  0.1414  0.1398  133 GLY   B O   
1220 N N   . THR   B 125 ? 0.8373 0.7494 0.5711 0.2951  0.1525  0.1610  134 THR   B N   
1221 C CA  . THR   B 125 ? 0.8537 0.7632 0.5651 0.3175  0.1422  0.1499  134 THR   B CA  
1222 C C   . THR   B 125 ? 0.8337 0.7514 0.5526 0.3072  0.1285  0.1327  134 THR   B C   
1223 O O   . THR   B 125 ? 0.8389 0.7510 0.5436 0.3206  0.1172  0.1209  134 THR   B O   
1224 C CB  . THR   B 125 ? 0.8914 0.8115 0.5841 0.3422  0.1497  0.1637  134 THR   B CB  
1225 O OG1 . THR   B 125 ? 0.9120 0.8246 0.5981 0.3487  0.1651  0.1824  134 THR   B OG1 
1226 C CG2 . THR   B 125 ? 0.9150 0.8258 0.5804 0.3688  0.1370  0.1519  134 THR   B CG2 
1227 N N   . SER   B 126 ? 0.8148 0.7441 0.5554 0.2834  0.1288  0.1316  135 SER   B N   
1228 C CA  . SER   B 126 ? 0.8065 0.7413 0.5519 0.2721  0.1175  0.1178  135 SER   B CA  
1229 C C   . SER   B 126 ? 0.8017 0.7215 0.5413 0.2715  0.1074  0.1005  135 SER   B C   
1230 O O   . SER   B 126 ? 0.8059 0.7144 0.5505 0.2653  0.1090  0.0957  135 SER   B O   
1231 C CB  . SER   B 126 ? 0.8154 0.7589 0.5822 0.2474  0.1193  0.1184  135 SER   B CB  
1232 O OG  . SER   B 126 ? 0.8385 0.8024 0.6157 0.2464  0.1259  0.1321  135 SER   B OG  
1233 N N   . GLY   B 127 ? 0.7916 0.7119 0.5221 0.2777  0.0969  0.0913  136 GLY   B N   
1234 C CA  . GLY   B 127 ? 0.7895 0.7000 0.5182 0.2766  0.0872  0.0755  136 GLY   B CA  
1235 C C   . GLY   B 127 ? 0.7945 0.6963 0.5075 0.3001  0.0796  0.0713  136 GLY   B C   
1236 O O   . GLY   B 127 ? 0.7926 0.6890 0.5064 0.3004  0.0694  0.0579  136 GLY   B O   
1237 N N   . SER   B 128 ? 0.7999 0.7004 0.4984 0.3207  0.0844  0.0825  137 SER   B N   
1238 C CA  . SER   B 128 ? 0.8210 0.7113 0.4996 0.3468  0.0757  0.0781  137 SER   B CA  
1239 C C   . SER   B 128 ? 0.8372 0.7261 0.5087 0.3516  0.0601  0.0677  137 SER   B C   
1240 O O   . SER   B 128 ? 0.8379 0.7343 0.5081 0.3472  0.0597  0.0719  137 SER   B O   
1241 C CB  . SER   B 128 ? 0.8495 0.7406 0.5101 0.3684  0.0856  0.0941  137 SER   B CB  
1242 O OG  . SER   B 128 ? 0.8721 0.7571 0.5346 0.3676  0.0978  0.1037  137 SER   B OG  
1243 N N   . PRO   B 129 ? 0.8516 0.7298 0.5189 0.3608  0.0459  0.0536  138 PRO   B N   
1244 C CA  . PRO   B 129 ? 0.8589 0.7315 0.5209 0.3632  0.0294  0.0435  138 PRO   B CA  
1245 C C   . PRO   B 129 ? 0.8936 0.7594 0.5288 0.3907  0.0213  0.0463  138 PRO   B C   
1246 O O   . PRO   B 129 ? 0.8941 0.7559 0.5104 0.4156  0.0238  0.0514  138 PRO   B O   
1247 C CB  . PRO   B 129 ? 0.8611 0.7269 0.5331 0.3623  0.0171  0.0273  138 PRO   B CB  
1248 C CG  . PRO   B 129 ? 0.8653 0.7278 0.5311 0.3786  0.0229  0.0296  138 PRO   B CG  
1249 C CD  . PRO   B 129 ? 0.8412 0.7113 0.5103 0.3688  0.0429  0.0455  138 PRO   B CD  
1250 N N   . ILE   B 130 ? 0.9122 0.7745 0.5431 0.3873  0.0107  0.0426  139 ILE   B N   
1251 C CA  . ILE   B 130 ? 0.9351 0.7882 0.5397 0.4127  -0.0008 0.0419  139 ILE   B CA  
1252 C C   . ILE   B 130 ? 0.9538 0.7880 0.5570 0.4143  -0.0241 0.0246  139 ILE   B C   
1253 O O   . ILE   B 130 ? 0.9356 0.7682 0.5591 0.3892  -0.0290 0.0175  139 ILE   B O   
1254 C CB  . ILE   B 130 ? 0.9437 0.8053 0.5447 0.4081  0.0035  0.0507  139 ILE   B CB  
1255 C CG1 . ILE   B 130 ? 0.9429 0.8266 0.5528 0.4032  0.0261  0.0672  139 ILE   B CG1 
1256 C CG2 . ILE   B 130 ? 0.9660 0.8164 0.5377 0.4367  -0.0105 0.0479  139 ILE   B CG2 
1257 C CD1 . ILE   B 130 ? 0.9535 0.8493 0.5695 0.3910  0.0295  0.0734  139 ILE   B CD1 
1258 N N   . LEU   B 131 ? 0.9806 0.8011 0.5612 0.4437  -0.0380 0.0176  140 LEU   B N   
1259 C CA  . LEU   B 131 ? 1.0106 0.8130 0.5931 0.4460  -0.0624 -0.0003 140 LEU   B CA  
1260 C C   . LEU   B 131 ? 1.0375 0.8188 0.5918 0.4700  -0.0839 -0.0078 140 LEU   B C   
1261 O O   . LEU   B 131 ? 1.0515 0.8322 0.5772 0.4969  -0.0805 -0.0006 140 LEU   B O   
1262 C CB  . LEU   B 131 ? 1.0228 0.8239 0.6098 0.4570  -0.0667 -0.0089 140 LEU   B CB  
1263 C CG  . LEU   B 131 ? 1.0452 0.8591 0.6323 0.4618  -0.0456 0.0024  140 LEU   B CG  
1264 C CD1 . LEU   B 131 ? 1.0547 0.8584 0.6267 0.4888  -0.0555 -0.0056 140 LEU   B CD1 
1265 C CD2 . LEU   B 131 ? 1.0410 0.8703 0.6614 0.4286  -0.0310 0.0050  140 LEU   B CD2 
1266 N N   . ASP   B 132 ? 1.0460 0.8099 0.6090 0.4605  -0.1065 -0.0225 141 ASP   B N   
1267 C CA  . ASP   B 132 ? 1.0775 0.8150 0.6145 0.4826  -0.1322 -0.0330 141 ASP   B CA  
1268 C C   . ASP   B 132 ? 1.1068 0.8317 0.6308 0.5105  -0.1508 -0.0474 141 ASP   B C   
1269 O O   . ASP   B 132 ? 1.1062 0.8438 0.6439 0.5096  -0.1429 -0.0483 141 ASP   B O   
1270 C CB  . ASP   B 132 ? 1.0785 0.7995 0.6304 0.4566  -0.1480 -0.0401 141 ASP   B CB  
1271 C CG  . ASP   B 132 ? 1.0928 0.8123 0.6787 0.4324  -0.1591 -0.0525 141 ASP   B CG  
1272 O OD1 . ASP   B 132 ? 1.0772 0.8089 0.6762 0.4370  -0.1567 -0.0578 141 ASP   B OD1 
1273 O OD2 . ASP   B 132 ? 1.1252 0.8317 0.7247 0.4092  -0.1699 -0.0562 141 ASP   B OD2 
1274 N N   . LYS   B 133 ? 1.1381 0.8367 0.6352 0.5357  -0.1770 -0.0595 142 LYS   B N   
1275 C CA  . LYS   B 133 ? 1.1688 0.8534 0.6489 0.5659  -0.1972 -0.0743 142 LYS   B CA  
1276 C C   . LYS   B 133 ? 1.1632 0.8487 0.6790 0.5474  -0.2118 -0.0896 142 LYS   B C   
1277 O O   . LYS   B 133 ? 1.1692 0.8497 0.6759 0.5707  -0.2246 -0.1007 142 LYS   B O   
1278 C CB  . LYS   B 133 ? 1.2400 0.8938 0.6810 0.5987  -0.2243 -0.0856 142 LYS   B CB  
1279 C CG  . LYS   B 133 ? 1.3474 1.0054 0.7473 0.6300  -0.2092 -0.0719 142 LYS   B CG  
1280 C CD  . LYS   B 133 ? 1.4565 1.0841 0.8151 0.6633  -0.2351 -0.0830 142 LYS   B CD  
1281 C CE  . LYS   B 133 ? 1.5229 1.1583 0.8636 0.6692  -0.2200 -0.0688 142 LYS   B CE  
1282 N NZ  . LYS   B 133 ? 1.5891 1.1908 0.8994 0.6899  -0.2489 -0.0818 142 LYS   B NZ  
1283 N N   . CYS   B 134 ? 1.1421 0.8366 0.6984 0.5068  -0.2085 -0.0898 143 CYS   B N   
1284 C CA  . CYS   B 134 ? 1.1245 0.8287 0.7209 0.4871  -0.2174 -0.1026 143 CYS   B CA  
1285 C C   . CYS   B 134 ? 1.0808 0.8156 0.7010 0.4729  -0.1905 -0.0938 143 CYS   B C   
1286 O O   . CYS   B 134 ? 1.0676 0.8154 0.7224 0.4573  -0.1951 -0.1039 143 CYS   B O   
1287 C CB  . CYS   B 134 ? 1.1477 0.8449 0.7762 0.4524  -0.2301 -0.1090 143 CYS   B CB  
1288 S SG  . CYS   B 134 ? 1.2811 0.9358 0.8815 0.4651  -0.2628 -0.1185 143 CYS   B SG  
1289 N N   . GLY   B 135 ? 1.0618 0.8084 0.6658 0.4772  -0.1639 -0.0759 144 GLY   B N   
1290 C CA  . GLY   B 135 ? 1.0380 0.8091 0.6622 0.4633  -0.1392 -0.0671 144 GLY   B CA  
1291 C C   . GLY   B 135 ? 1.0064 0.7940 0.6627 0.4236  -0.1227 -0.0600 144 GLY   B C   
1292 O O   . GLY   B 135 ? 0.9931 0.8000 0.6697 0.4094  -0.1050 -0.0557 144 GLY   B O   
1293 N N   . ARG   B 136 ? 0.9962 0.7739 0.6542 0.4068  -0.1288 -0.0586 145 ARG   B N   
1294 C CA  . ARG   B 136 ? 0.9800 0.7698 0.6621 0.3709  -0.1138 -0.0509 145 ARG   B CA  
1295 C C   . ARG   B 136 ? 0.9635 0.7622 0.6308 0.3692  -0.0905 -0.0332 145 ARG   B C   
1296 O O   . ARG   B 136 ? 0.9758 0.7649 0.6138 0.3891  -0.0913 -0.0263 145 ARG   B O   
1297 C CB  . ARG   B 136 ? 1.0077 0.7791 0.6944 0.3540  -0.1306 -0.0554 145 ARG   B CB  
1298 C CG  . ARG   B 136 ? 1.0626 0.8287 0.7743 0.3473  -0.1530 -0.0725 145 ARG   B CG  
1299 C CD  . ARG   B 136 ? 1.1417 0.8866 0.8586 0.3277  -0.1686 -0.0748 145 ARG   B CD  
1300 N NE  . ARG   B 136 ? 1.2401 0.9541 0.9178 0.3511  -0.1852 -0.0747 145 ARG   B NE  
1301 C CZ  . ARG   B 136 ? 1.3122 1.0025 0.9783 0.3399  -0.1935 -0.0706 145 ARG   B CZ  
1302 N NH1 . ARG   B 136 ? 1.3049 0.9978 0.9945 0.3041  -0.1856 -0.0646 145 ARG   B NH1 
1303 N NH2 . ARG   B 136 ? 1.3516 1.0145 0.9799 0.3658  -0.2092 -0.0719 145 ARG   B NH2 
1304 N N   . VAL   B 137 ? 0.9361 0.7543 0.6243 0.3469  -0.0703 -0.0266 146 VAL   B N   
1305 C CA  . VAL   B 137 ? 0.9224 0.7509 0.6029 0.3412  -0.0492 -0.0111 146 VAL   B CA  
1306 C C   . VAL   B 137 ? 0.9175 0.7375 0.5913 0.3268  -0.0511 -0.0055 146 VAL   B C   
1307 O O   . VAL   B 137 ? 0.9255 0.7442 0.6158 0.3020  -0.0529 -0.0084 146 VAL   B O   
1308 C CB  . VAL   B 137 ? 0.9145 0.7629 0.6187 0.3226  -0.0306 -0.0087 146 VAL   B CB  
1309 C CG1 . VAL   B 137 ? 0.9236 0.7812 0.6218 0.3160  -0.0112 0.0061  146 VAL   B CG1 
1310 C CG2 . VAL   B 137 ? 0.9112 0.7641 0.6199 0.3388  -0.0313 -0.0154 146 VAL   B CG2 
1311 N N   . ILE   B 138 ? 0.9061 0.7198 0.5544 0.3441  -0.0514 0.0024  147 ILE   B N   
1312 C CA  . ILE   B 138 ? 0.9012 0.7057 0.5381 0.3361  -0.0544 0.0081  147 ILE   B CA  
1313 C C   . ILE   B 138 ? 0.8837 0.7061 0.5239 0.3243  -0.0342 0.0212  147 ILE   B C   
1314 O O   . ILE   B 138 ? 0.8943 0.7113 0.5256 0.3177  -0.0358 0.0261  147 ILE   B O   
1315 C CB  . ILE   B 138 ? 0.9174 0.7032 0.5234 0.3652  -0.0710 0.0061  147 ILE   B CB  
1316 C CG1 . ILE   B 138 ? 0.9343 0.7328 0.5238 0.3940  -0.0610 0.0132  147 ILE   B CG1 
1317 C CG2 . ILE   B 138 ? 0.9269 0.6898 0.5308 0.3718  -0.0953 -0.0088 147 ILE   B CG2 
1318 C CD1 . ILE   B 138 ? 0.9763 0.7602 0.5322 0.4282  -0.0750 0.0110  147 ILE   B CD1 
1319 N N   . GLY   B 139 ? 0.8595 0.7010 0.5124 0.3217  -0.0173 0.0262  148 GLY   B N   
1320 C CA  . GLY   B 139 ? 0.8499 0.7076 0.5093 0.3093  -0.0003 0.0371  148 GLY   B CA  
1321 C C   . GLY   B 139 ? 0.8390 0.7121 0.5063 0.3146  0.0152  0.0434  148 GLY   B C   
1322 O O   . GLY   B 139 ? 0.8416 0.7119 0.5054 0.3309  0.0134  0.0402  148 GLY   B O   
1323 N N   . LEU   B 140 ? 0.8223 0.7096 0.4993 0.3012  0.0292  0.0523  149 LEU   B N   
1324 C CA  . LEU   B 140 ? 0.8123 0.7116 0.4985 0.3020  0.0442  0.0599  149 LEU   B CA  
1325 C C   . LEU   B 140 ? 0.8233 0.7366 0.5062 0.3093  0.0536  0.0737  149 LEU   B C   
1326 O O   . LEU   B 140 ? 0.8263 0.7453 0.5077 0.3041  0.0514  0.0766  149 LEU   B O   
1327 C CB  . LEU   B 140 ? 0.7925 0.6963 0.4981 0.2777  0.0523  0.0568  149 LEU   B CB  
1328 C CG  . LEU   B 140 ? 0.7948 0.6921 0.5098 0.2674  0.0467  0.0438  149 LEU   B CG  
1329 C CD1 . LEU   B 140 ? 0.7922 0.6964 0.5235 0.2464  0.0569  0.0416  149 LEU   B CD1 
1330 C CD2 . LEU   B 140 ? 0.7928 0.6839 0.5052 0.2856  0.0406  0.0372  149 LEU   B CD2 
1331 N N   . TYR   B 141 ? 0.8261 0.7456 0.5085 0.3215  0.0642  0.0825  150 TYR   B N   
1332 C CA  . TYR   B 141 ? 0.8287 0.7653 0.5121 0.3289  0.0762  0.0976  150 TYR   B CA  
1333 C C   . TYR   B 141 ? 0.8123 0.7607 0.5188 0.3059  0.0877  0.1042  150 TYR   B C   
1334 O O   . TYR   B 141 ? 0.8231 0.7633 0.5394 0.2926  0.0901  0.0995  150 TYR   B O   
1335 C CB  . TYR   B 141 ? 0.8460 0.7800 0.5161 0.3523  0.0831  0.1050  150 TYR   B CB  
1336 C CG  . TYR   B 141 ? 0.8612 0.8144 0.5338 0.3601  0.0994  0.1233  150 TYR   B CG  
1337 C CD1 . TYR   B 141 ? 0.8720 0.8292 0.5593 0.3491  0.1144  0.1344  150 TYR   B CD1 
1338 C CD2 . TYR   B 141 ? 0.8748 0.8418 0.5352 0.3793  0.1000  0.1297  150 TYR   B CD2 
1339 C CE1 . TYR   B 141 ? 0.8822 0.8582 0.5751 0.3541  0.1306  0.1530  150 TYR   B CE1 
1340 C CE2 . TYR   B 141 ? 0.8807 0.8702 0.5461 0.3871  0.1171  0.1476  150 TYR   B CE2 
1341 C CZ  . TYR   B 141 ? 0.8895 0.8842 0.5729 0.3729  0.1330  0.1600  150 TYR   B CZ  
1342 O OH  . TYR   B 141 ? 0.8867 0.9049 0.5786 0.3778  0.1513  0.1795  150 TYR   B OH  
1343 N N   . GLY   B 142 ? 0.7928 0.7605 0.5086 0.3024  0.0938  0.1142  151 GLY   B N   
1344 C CA  . GLY   B 142 ? 0.7923 0.7708 0.5320 0.2807  0.1029  0.1201  151 GLY   B CA  
1345 C C   . GLY   B 142 ? 0.7997 0.7918 0.5519 0.2655  0.0988  0.1191  151 GLY   B C   
1346 O O   . GLY   B 142 ? 0.7991 0.8019 0.5723 0.2495  0.1052  0.1244  151 GLY   B O   
1347 N N   . ASN   B 143 ? 0.8018 0.7913 0.5410 0.2703  0.0870  0.1120  152 ASN   B N   
1348 C CA  . ASN   B 143 ? 0.8167 0.8189 0.5643 0.2597  0.0821  0.1116  152 ASN   B CA  
1349 C C   . ASN   B 143 ? 0.8476 0.8647 0.5862 0.2802  0.0790  0.1168  152 ASN   B C   
1350 O O   . ASN   B 143 ? 0.8637 0.8670 0.5796 0.2945  0.0685  0.1108  152 ASN   B O   
1351 C CB  . ASN   B 143 ? 0.8171 0.8020 0.5563 0.2452  0.0710  0.0995  152 ASN   B CB  
1352 C CG  . ASN   B 143 ? 0.8162 0.8125 0.5656 0.2315  0.0671  0.0992  152 ASN   B CG  
1353 O OD1 . ASN   B 143 ? 0.8094 0.8273 0.5794 0.2276  0.0730  0.1066  152 ASN   B OD1 
1354 N ND2 . ASN   B 143 ? 0.7874 0.7692 0.5225 0.2239  0.0568  0.0910  152 ASN   B ND2 
1355 N N   . GLY   B 144 ? 0.8532 0.8985 0.6103 0.2823  0.0879  0.1278  153 GLY   B N   
1356 C CA  . GLY   B 144 ? 0.8824 0.9477 0.6332 0.3042  0.0869  0.1331  153 GLY   B CA  
1357 C C   . GLY   B 144 ? 0.8943 0.9959 0.6734 0.2991  0.0935  0.1423  153 GLY   B C   
1358 O O   . GLY   B 144 ? 0.8824 0.9898 0.6822 0.2771  0.0910  0.1400  153 GLY   B O   
1359 N N   . VAL   B 145 ? 0.9109 1.0386 0.6914 0.3206  0.1017  0.1523  154 VAL   B N   
1360 C CA  . VAL   B 145 ? 0.9228 1.0917 0.7328 0.3191  0.1077  0.1610  154 VAL   B CA  
1361 C C   . VAL   B 145 ? 0.9459 1.1459 0.7678 0.3345  0.1281  0.1784  154 VAL   B C   
1362 O O   . VAL   B 145 ? 0.9563 1.1437 0.7548 0.3531  0.1351  0.1825  154 VAL   B O   
1363 C CB  . VAL   B 145 ? 0.9349 1.1086 0.7307 0.3336  0.0912  0.1518  154 VAL   B CB  
1364 C CG1 . VAL   B 145 ? 0.9455 1.1197 0.7124 0.3683  0.0903  0.1526  154 VAL   B CG1 
1365 C CG2 . VAL   B 145 ? 0.9238 1.1360 0.7530 0.3253  0.0903  0.1548  154 VAL   B CG2 
1366 N N   . VAL   B 146 ? 0.9502 1.1918 0.8092 0.3267  0.1375  0.1888  155 VAL   B N   
1367 C CA  . VAL   B 146 ? 0.9662 1.2442 0.8418 0.3389  0.1590  0.2075  155 VAL   B CA  
1368 C C   . VAL   B 146 ? 0.9923 1.3068 0.8689 0.3634  0.1563  0.2073  155 VAL   B C   
1369 O O   . VAL   B 146 ? 0.9811 1.3158 0.8794 0.3547  0.1455  0.2010  155 VAL   B O   
1370 C CB  . VAL   B 146 ? 0.9538 1.2542 0.8759 0.3098  0.1726  0.2206  155 VAL   B CB  
1371 C CG1 . VAL   B 146 ? 0.9449 1.2893 0.8887 0.3209  0.1963  0.2419  155 VAL   B CG1 
1372 C CG2 . VAL   B 146 ? 0.9757 1.2367 0.8917 0.2901  0.1752  0.2206  155 VAL   B CG2 
1373 N N   . ILE   B 147 ? 1.0259 1.3468 0.8756 0.3966  0.1641  0.2125  156 ILE   B N   
1374 C CA  . ILE   B 147 ? 1.0492 1.4022 0.8942 0.4250  0.1604  0.2106  156 ILE   B CA  
1375 C C   . ILE   B 147 ? 1.0427 1.4582 0.9288 0.4281  0.1826  0.2289  156 ILE   B C   
1376 O O   . ILE   B 147 ? 1.0301 1.4591 0.9453 0.4078  0.2016  0.2447  156 ILE   B O   
1377 C CB  . ILE   B 147 ? 1.0874 1.4129 0.8792 0.4618  0.1537  0.2036  156 ILE   B CB  
1378 C CG1 . ILE   B 147 ? 1.1015 1.4237 0.8777 0.4756  0.1743  0.2176  156 ILE   B CG1 
1379 C CG2 . ILE   B 147 ? 1.1297 1.3999 0.8896 0.4553  0.1292  0.1846  156 ILE   B CG2 
1380 C CD1 . ILE   B 147 ? 1.1375 1.4371 0.8619 0.5155  0.1672  0.2105  156 ILE   B CD1 
1381 N N   . LYS   B 148 ? 1.0466 1.5010 0.9368 0.4532  0.1800  0.2271  157 LYS   B N   
1382 C CA  . LYS   B 148 ? 1.0328 1.5539 0.9636 0.4601  0.2014  0.2438  157 LYS   B CA  
1383 C C   . LYS   B 148 ? 1.0476 1.5831 0.9754 0.4704  0.2317  0.2658  157 LYS   B C   
1384 O O   . LYS   B 148 ? 1.0265 1.6149 0.9960 0.4647  0.2546  0.2844  157 LYS   B O   
1385 C CB  . LYS   B 148 ? 1.0568 1.6095 0.9786 0.4947  0.1921  0.2355  157 LYS   B CB  
1386 C CG  . LYS   B 148 ? 1.0868 1.6850 1.0578 0.4805  0.1838  0.2316  157 LYS   B CG  
1387 C CD  . LYS   B 148 ? 1.1383 1.7677 1.0986 0.5182  0.1738  0.2227  157 LYS   B CD  
1388 C CE  . LYS   B 148 ? 1.1688 1.8463 1.1298 0.5514  0.1992  0.2378  157 LYS   B CE  
1389 N NZ  . LYS   B 148 ? 1.1521 1.8925 1.1762 0.5308  0.2276  0.2598  157 LYS   B NZ  
1390 N N   . ASN   B 149 ? 1.0793 1.5686 0.9579 0.4860  0.2317  0.2639  158 ASN   B N   
1391 C CA  . ASN   B 149 ? 1.0851 1.5755 0.9495 0.4976  0.2576  0.2833  158 ASN   B CA  
1392 C C   . ASN   B 149 ? 1.0670 1.5512 0.9646 0.4586  0.2729  0.2988  158 ASN   B C   
1393 O O   . ASN   B 149 ? 1.0667 1.5643 0.9673 0.4617  0.2991  0.3205  158 ASN   B O   
1394 C CB  . ASN   B 149 ? 1.1526 1.5846 0.9552 0.5199  0.2455  0.2718  158 ASN   B CB  
1395 C CG  . ASN   B 149 ? 1.2292 1.6628 0.9861 0.5680  0.2425  0.2663  158 ASN   B CG  
1396 O OD1 . ASN   B 149 ? 1.2401 1.7226 1.0060 0.5918  0.2556  0.2747  158 ASN   B OD1 
1397 N ND2 . ASN   B 149 ? 1.2679 1.6477 0.9749 0.5842  0.2248  0.2517  158 ASN   B ND2 
1398 N N   . GLY   B 150 ? 1.0521 1.5085 0.9663 0.4250  0.2554  0.2869  159 GLY   B N   
1399 C CA  . GLY   B 150 ? 1.0383 1.4751 0.9754 0.3893  0.2630  0.2959  159 GLY   B CA  
1400 C C   . GLY   B 150 ? 1.0538 1.4278 0.9479 0.3896  0.2528  0.2861  159 GLY   B C   
1401 O O   . GLY   B 150 ? 1.0663 1.4133 0.9726 0.3607  0.2514  0.2865  159 GLY   B O   
1402 N N   . SER   B 151 ? 1.0486 1.3986 0.8923 0.4231  0.2442  0.2760  160 SER   B N   
1403 C CA  . SER   B 151 ? 1.0562 1.3507 0.8597 0.4272  0.2329  0.2651  160 SER   B CA  
1404 C C   . SER   B 151 ? 1.0198 1.2810 0.8201 0.4088  0.2059  0.2421  160 SER   B C   
1405 O O   . SER   B 151 ? 1.0052 1.2818 0.8226 0.4008  0.1932  0.2326  160 SER   B O   
1406 C CB  . SER   B 151 ? 1.1062 1.3890 0.8599 0.4696  0.2326  0.2628  160 SER   B CB  
1407 O OG  . SER   B 151 ? 1.1486 1.4462 0.8911 0.4916  0.2186  0.2505  160 SER   B OG  
1408 N N   . TYR   B 152 ? 1.0012 1.2173 0.7792 0.4027  0.1982  0.2339  161 TYR   B N   
1409 C CA  . TYR   B 152 ? 0.9750 1.1574 0.7481 0.3847  0.1766  0.2144  161 TYR   B CA  
1410 C C   . TYR   B 152 ? 0.9593 1.1119 0.6909 0.4080  0.1578  0.1975  161 TYR   B C   
1411 O O   . TYR   B 152 ? 0.9716 1.1097 0.6729 0.4325  0.1602  0.1988  161 TYR   B O   
1412 C CB  . TYR   B 152 ? 0.9768 1.1324 0.7573 0.3614  0.1811  0.2165  161 TYR   B CB  
1413 C CG  . TYR   B 152 ? 0.9857 1.1113 0.7652 0.3410  0.1623  0.1978  161 TYR   B CG  
1414 C CD1 . TYR   B 152 ? 0.9793 1.1153 0.7846 0.3174  0.1540  0.1914  161 TYR   B CD1 
1415 C CD2 . TYR   B 152 ? 1.0129 1.1016 0.7656 0.3463  0.1529  0.1864  161 TYR   B CD2 
1416 C CE1 . TYR   B 152 ? 0.9985 1.1079 0.7994 0.3006  0.1386  0.1752  161 TYR   B CE1 
1417 C CE2 . TYR   B 152 ? 1.0324 1.0979 0.7853 0.3283  0.1379  0.1702  161 TYR   B CE2 
1418 C CZ  . TYR   B 152 ? 1.0309 1.1063 0.8063 0.3057  0.1318  0.1653  161 TYR   B CZ  
1419 O OH  . TYR   B 152 ? 1.0594 1.1127 0.8325 0.2890  0.1191  0.1506  161 TYR   B OH  
1420 N N   . VAL   B 153 ? 0.9325 1.0743 0.6620 0.4003  0.1382  0.1817  162 VAL   B N   
1421 C CA  . VAL   B 153 ? 0.9326 1.0433 0.6266 0.4174  0.1183  0.1656  162 VAL   B CA  
1422 C C   . VAL   B 153 ? 0.9103 0.9922 0.6086 0.3902  0.1040  0.1519  162 VAL   B C   
1423 O O   . VAL   B 153 ? 0.8962 0.9872 0.6145 0.3700  0.0998  0.1493  162 VAL   B O   
1424 C CB  . VAL   B 153 ? 0.9424 1.0689 0.6236 0.4411  0.1089  0.1616  162 VAL   B CB  
1425 C CG1 . VAL   B 153 ? 0.9713 1.0602 0.6179 0.4538  0.0852  0.1442  162 VAL   B CG1 
1426 C CG2 . VAL   B 153 ? 0.9436 1.1000 0.6174 0.4718  0.1247  0.1748  162 VAL   B CG2 
1427 N N   . SER   B 154 ? 0.9066 0.9561 0.5876 0.3898  0.0975  0.1435  163 SER   B N   
1428 C CA  . SER   B 154 ? 0.8964 0.9217 0.5823 0.3649  0.0867  0.1314  163 SER   B CA  
1429 C C   . SER   B 154 ? 0.8915 0.8924 0.5543 0.3715  0.0664  0.1172  163 SER   B C   
1430 O O   . SER   B 154 ? 0.9034 0.8917 0.5415 0.3958  0.0589  0.1133  163 SER   B O   
1431 C CB  . SER   B 154 ? 0.9031 0.9106 0.5895 0.3580  0.0922  0.1306  163 SER   B CB  
1432 O OG  . SER   B 154 ? 0.9068 0.8895 0.5907 0.3427  0.0805  0.1168  163 SER   B OG  
1433 N N   . ALA   B 155 ? 0.8682 0.8581 0.5375 0.3492  0.0574  0.1092  164 ALA   B N   
1434 C CA  . ALA   B 155 ? 0.8693 0.8313 0.5181 0.3505  0.0392  0.0971  164 ALA   B CA  
1435 C C   . ALA   B 155 ? 0.8652 0.8034 0.5066 0.3498  0.0349  0.0892  164 ALA   B C   
1436 O O   . ALA   B 155 ? 0.8512 0.7929 0.5050 0.3428  0.0456  0.0916  164 ALA   B O   
1437 C CB  . ALA   B 155 ? 0.8714 0.8283 0.5285 0.3255  0.0338  0.0929  164 ALA   B CB  
1438 N N   . ILE   B 156 ? 0.8762 0.7897 0.4978 0.3580  0.0182  0.0793  165 ILE   B N   
1439 C CA  . ILE   B 156 ? 0.8821 0.7744 0.5017 0.3534  0.0110  0.0697  165 ILE   B CA  
1440 C C   . ILE   B 156 ? 0.8683 0.7523 0.4997 0.3233  0.0086  0.0652  165 ILE   B C   
1441 O O   . ILE   B 156 ? 0.8704 0.7389 0.4899 0.3197  -0.0036 0.0617  165 ILE   B O   
1442 C CB  . ILE   B 156 ? 0.9021 0.7715 0.4965 0.3765  -0.0074 0.0611  165 ILE   B CB  
1443 C CG1 . ILE   B 156 ? 0.9104 0.7903 0.4896 0.4090  -0.0026 0.0665  165 ILE   B CG1 
1444 C CG2 . ILE   B 156 ? 0.9149 0.7643 0.5141 0.3668  -0.0171 0.0496  165 ILE   B CG2 
1445 C CD1 . ILE   B 156 ? 0.9351 0.7923 0.4866 0.4359  -0.0210 0.0570  165 ILE   B CD1 
1446 N N   . THR   B 157 ? 0.8528 0.7469 0.5053 0.3029  0.0211  0.0665  166 THR   B N   
1447 C CA  . THR   B 157 ? 0.8443 0.7335 0.5059 0.2761  0.0216  0.0630  166 THR   B CA  
1448 C C   . THR   B 157 ? 0.8458 0.7203 0.5116 0.2655  0.0164  0.0534  166 THR   B C   
1449 O O   . THR   B 157 ? 0.8494 0.7288 0.5272 0.2652  0.0223  0.0503  166 THR   B O   
1450 C CB  . THR   B 157 ? 0.8314 0.7387 0.5118 0.2606  0.0361  0.0680  166 THR   B CB  
1451 O OG1 . THR   B 157 ? 0.8277 0.7526 0.5100 0.2686  0.0408  0.0771  166 THR   B OG1 
1452 C CG2 . THR   B 157 ? 0.8366 0.7386 0.5210 0.2367  0.0364  0.0641  166 THR   B CG2 
1453 N N   . GLN   B 158 ? 0.8443 0.7014 0.5017 0.2562  0.0058  0.0493  167 GLN   B N   
1454 C CA  . GLN   B 158 ? 0.8536 0.6994 0.5191 0.2433  0.0012  0.0410  167 GLN   B CA  
1455 C C   . GLN   B 158 ? 0.8694 0.7138 0.5399 0.2170  0.0071  0.0420  167 GLN   B C   
1456 O O   . GLN   B 158 ? 0.8606 0.7000 0.5181 0.2124  0.0061  0.0473  167 GLN   B O   
1457 C CB  . GLN   B 158 ? 0.8736 0.6963 0.5244 0.2546  -0.0178 0.0357  167 GLN   B CB  
1458 C CG  . GLN   B 158 ? 0.8941 0.7067 0.5582 0.2418  -0.0249 0.0267  167 GLN   B CG  
1459 C CD  . GLN   B 158 ? 0.8926 0.7216 0.5781 0.2431  -0.0181 0.0204  167 GLN   B CD  
1460 O OE1 . GLN   B 158 ? 0.8785 0.7252 0.5785 0.2322  -0.0027 0.0222  167 GLN   B OE1 
1461 N NE2 . GLN   B 158 ? 0.8693 0.6908 0.5563 0.2570  -0.0310 0.0118  167 GLN   B NE2 
1462 N N   . GLY   B 159 ? 0.8837 0.7335 0.5716 0.2019  0.0135  0.0365  168 GLY   B N   
1463 C CA  . GLY   B 159 ? 0.9219 0.7711 0.6128 0.1787  0.0205  0.0373  168 GLY   B CA  
1464 C C   . GLY   B 159 ? 0.9813 0.8106 0.6668 0.1682  0.0105  0.0361  168 GLY   B C   
1465 O O   . GLY   B 159 ? 0.9936 0.8074 0.6726 0.1793  -0.0044 0.0336  168 GLY   B O   
1466 N N   . LYS   B 160 ? 1.0135 0.8420 0.7008 0.1469  0.0186  0.0381  169 LYS   B N   
1467 C CA  . LYS   B 160 ? 1.0588 0.8687 0.7433 0.1323  0.0120  0.0394  169 LYS   B CA  
1468 C C   . LYS   B 160 ? 1.0715 0.8989 0.7845 0.1166  0.0219  0.0336  169 LYS   B C   
1469 O O   . LYS   B 160 ? 1.0673 0.9145 0.7896 0.1090  0.0376  0.0328  169 LYS   B O   
1470 C CB  . LYS   B 160 ? 1.1098 0.9032 0.7696 0.1206  0.0142  0.0487  169 LYS   B CB  
1471 C CG  . LYS   B 160 ? 1.1995 0.9694 0.8534 0.1033  0.0089  0.0529  169 LYS   B CG  
1472 C CD  . LYS   B 160 ? 1.2952 1.0419 0.9164 0.0973  0.0079  0.0631  169 LYS   B CD  
1473 C CE  . LYS   B 160 ? 1.3708 1.0857 0.9808 0.0823  -0.0005 0.0693  169 LYS   B CE  
1474 N NZ  . LYS   B 160 ? 1.4011 1.1248 1.0256 0.0565  0.0159  0.0733  169 LYS   B NZ  
1475 N N   . ARG   B 161 ? 1.0834 0.9048 0.8117 0.1136  0.0114  0.0284  170 ARG   B N   
1476 C CA  . ARG   B 161 ? 1.0868 0.9280 0.8467 0.0987  0.0192  0.0225  170 ARG   B CA  
1477 C C   . ARG   B 161 ? 1.1184 0.9486 0.8761 0.0729  0.0246  0.0307  170 ARG   B C   
1478 O O   . ARG   B 161 ? 1.1318 0.9334 0.8763 0.0686  0.0108  0.0353  170 ARG   B O   
1479 C CB  . ARG   B 161 ? 1.0886 0.9302 0.8688 0.1090  0.0029  0.0117  170 ARG   B CB  
1480 C CG  . ARG   B 161 ? 1.0937 0.9530 0.9101 0.0913  0.0057  0.0053  170 ARG   B CG  
1481 C CD  . ARG   B 161 ? 1.1148 0.9836 0.9539 0.1064  -0.0084 -0.0084 170 ARG   B CD  
1482 N NE  . ARG   B 161 ? 1.1217 1.0184 1.0013 0.0914  -0.0026 -0.0161 170 ARG   B NE  
1483 C CZ  . ARG   B 161 ? 1.1314 1.0488 1.0364 0.1038  -0.0081 -0.0294 170 ARG   B CZ  
1484 N NH1 . ARG   B 161 ? 1.1202 1.0309 1.0110 0.1313  -0.0186 -0.0353 170 ARG   B NH1 
1485 N NH2 . ARG   B 161 ? 1.1104 1.0566 1.0548 0.0896  -0.0026 -0.0365 170 ARG   B NH2 
1486 N N   . GLU   B 162 ? 1.1277 0.9783 0.8949 0.0571  0.0446  0.0332  171 GLU   B N   
1487 C CA  . GLU   B 162 ? 1.1606 1.0030 0.9249 0.0324  0.0532  0.0429  171 GLU   B CA  
1488 C C   . GLU   B 162 ? 1.1574 1.0088 0.9576 0.0167  0.0499  0.0391  171 GLU   B C   
1489 O O   . GLU   B 162 ? 1.1696 1.0072 0.9696 -0.0046 0.0518  0.0483  171 GLU   B O   
1490 C CB  . GLU   B 162 ? 1.2048 1.0660 0.9627 0.0233  0.0766  0.0471  171 GLU   B CB  
1491 C CG  . GLU   B 162 ? 1.3194 1.1618 1.0372 0.0301  0.0777  0.0548  171 GLU   B CG  
1492 C CD  . GLU   B 162 ? 1.4622 1.2708 1.1503 0.0181  0.0733  0.0680  171 GLU   B CD  
1493 O OE1 . GLU   B 162 ? 1.5023 1.3114 1.1804 0.0017  0.0889  0.0764  171 GLU   B OE1 
1494 O OE2 . GLU   B 162 ? 1.5044 1.2848 1.1768 0.0265  0.0545  0.0702  171 GLU   B OE2 
1495 S S   . DMS   C .   ? 1.2242 1.0705 0.9704 0.1206  0.0758  -0.0323 201 DMS   B S   
1496 O O   . DMS   C .   ? 1.2181 1.0832 0.9591 0.1236  0.0847  -0.0284 201 DMS   B O   
1497 C C1  . DMS   C .   ? 1.2285 1.0610 0.9786 0.1318  0.0793  -0.0394 201 DMS   B C1  
1498 C C2  . DMS   C .   ? 1.2122 1.0591 0.9820 0.1160  0.0736  -0.0143 201 DMS   B C2  
1499 N N1  . A1BGW D .   ? 0.7804 0.7902 0.7150 0.0458  0.0370  0.0472  202 A1BGW B N1  
1500 N N3  . A1BGW D .   ? 0.7695 0.7760 0.6937 0.0583  0.0384  0.0524  202 A1BGW B N3  
1501 C C4  . A1BGW D .   ? 0.7749 0.7737 0.7009 0.0609  0.0332  0.0486  202 A1BGW B C4  
1502 C C5  . A1BGW D .   ? 0.7702 0.7731 0.6966 0.0562  0.0413  0.0544  202 A1BGW B C5  
1503 C C6  . A1BGW D .   ? 0.7708 0.7754 0.6985 0.0542  0.0415  0.0543  202 A1BGW B C6  
1504 C C7  . A1BGW D .   ? 0.7721 0.7786 0.6970 0.0550  0.0385  0.0525  202 A1BGW B C7  
1505 C C8  . A1BGW D .   ? 0.7733 0.7815 0.6942 0.0562  0.0345  0.0510  202 A1BGW B C8  
1506 C C10 . A1BGW D .   ? 0.7818 0.7783 0.6790 0.0593  0.0321  0.0462  202 A1BGW B C10 
1507 C C13 . A1BGW D .   ? 0.7744 0.7770 0.7055 0.0483  0.0432  0.0559  202 A1BGW B C13 
1508 C C15 . A1BGW D .   ? 0.7790 0.7799 0.7070 0.0542  0.0338  0.0490  202 A1BGW B C15 
1509 C C1  . A1BGW D .   ? 0.7876 0.8073 0.7289 0.0300  0.0430  0.0419  202 A1BGW B C1  
1510 C C2  . A1BGW D .   ? 0.7810 0.7936 0.7155 0.0420  0.0397  0.0471  202 A1BGW B C2  
1511 C C3  . A1BGW D .   ? 0.7783 0.7811 0.7079 0.0537  0.0343  0.0485  202 A1BGW B C3  
1512 N N2  . A1BGW D .   ? 0.7713 0.7733 0.6961 0.0606  0.0364  0.0507  202 A1BGW B N2  
1513 O O1  . A1BGW D .   ? 0.7704 0.7716 0.6973 0.0526  0.0444  0.0580  202 A1BGW B O1  
1514 C C9  . A1BGW D .   ? 0.7792 0.7805 0.6916 0.0554  0.0348  0.0490  202 A1BGW B C9  
1515 C C11 . A1BGW D .   ? 0.7790 0.7785 0.6727 0.0627  0.0267  0.0478  202 A1BGW B C11 
1516 N N4  . A1BGW D .   ? 0.7751 0.7771 0.6766 0.0647  0.0265  0.0486  202 A1BGW B N4  
1517 C C12 . A1BGW D .   ? 0.7707 0.7800 0.6862 0.0618  0.0299  0.0504  202 A1BGW B C12 
1518 N N5  . A1BGW D .   ? 0.7746 0.7792 0.7051 0.0492  0.0415  0.0544  202 A1BGW B N5  
1519 C C14 . A1BGW D .   ? 0.7788 0.7757 0.7128 0.0416  0.0449  0.0592  202 A1BGW B C14 
1520 N N6  . A1BGW D .   ? 0.7804 0.7874 0.7096 0.0468  0.0378  0.0489  202 A1BGW B N6  
1521 S S   . DMS   E .   ? 1.6626 1.3007 1.1404 0.5209  -0.2229 -0.0724 203 DMS   B S   
1522 O O   . DMS   E .   ? 1.6578 1.3194 1.1208 0.5308  -0.1952 -0.0542 203 DMS   B O   
1523 C C1  . DMS   E .   ? 1.6682 1.2820 1.1569 0.4891  -0.2360 -0.0729 203 DMS   B C1  
1524 C C2  . DMS   E .   ? 1.6914 1.2935 1.1231 0.5676  -0.2564 -0.0890 203 DMS   B C2  
1525 S S   . SO4   F .   ? 2.2593 1.8512 1.5646 0.6333  0.1500  0.2203  204 SO4   B S   
1526 O O1  . SO4   F .   ? 2.2449 1.8620 1.5689 0.6109  0.1748  0.2439  204 SO4   B O1  
1527 O O2  . SO4   F .   ? 2.2571 1.8338 1.5883 0.6099  0.1449  0.2125  204 SO4   B O2  
1528 O O3  . SO4   F .   ? 2.2872 1.8460 1.5359 0.6712  0.1529  0.2337  204 SO4   B O3  
1529 O O4  . SO4   F .   ? 2.2483 1.8626 1.5652 0.6422  0.1266  0.1908  204 SO4   B O4  
1530 S S   . DMS   G .   ? 1.9917 1.6522 1.2434 0.7488  -0.1900 -0.0417 205 DMS   B S   
1531 O O   . DMS   G .   ? 2.0081 1.6255 1.2541 0.7472  -0.2286 -0.0642 205 DMS   B O   
1532 C C1  . DMS   G .   ? 2.0001 1.6650 1.2181 0.7910  -0.1836 -0.0410 205 DMS   B C1  
1533 C C2  . DMS   G .   ? 2.0001 1.6697 1.2167 0.7828  -0.1844 -0.0347 205 DMS   B C2  
1534 S S   . DMS   H .   ? 1.6181 1.4682 1.4051 0.2908  -0.0837 -0.0587 206 DMS   B S   
1535 O O   . DMS   H .   ? 1.6276 1.4703 1.3827 0.3035  -0.0716 -0.0447 206 DMS   B O   
1536 C C1  . DMS   H .   ? 1.6238 1.4525 1.4120 0.2736  -0.1012 -0.0601 206 DMS   B C1  
1537 C C2  . DMS   H .   ? 1.6225 1.4636 1.4032 0.3237  -0.1080 -0.0744 206 DMS   B C2  
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