data_7HPD
# 
_entry.id   7HPD 
# 
_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   7HPD         pdb_00007hpd 10.2210/pdb7hpd/pdb 
WWPDB D_1001407763 ?            ?                   
# 
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                        7HPD 
_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 'N-(5-carbamoyl-1H-pyrrol-3-yl)-2-[(propan-2-yl)amino]-1H-1,3-benzimidazole-6-carboxamide' 326.353   1  ? ?    ? 
? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                       78.133    1  ? ?    ? 
? 
5 non-polymer syn 'SULFATE ION'                                                                              96.063    2  ? ?    ? 
? 
6 water       nat water                                                                                      18.015    80 ? ?    ? 
? 
# 
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 'N-(5-carbamoyl-1H-pyrrol-3-yl)-2-[(propan-2-yl)amino]-1H-1,3-benzimidazole-6-carboxamide' A1BGV 
4 'DIMETHYL SULFOXIDE'                                                                       DMS   
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 
A1BGV non-polymer         . 'N-(5-carbamoyl-1H-pyrrol-3-yl)-2-[(propan-2-yl)amino]-1H-1,3-benzimidazole-6-carboxamide' ? 
'C16 H18 N6 O2'  326.353 
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  16  GLY GLY 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        A1BGV 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BGV 
_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 A1BGV 1  301 301 A1BGV LIG B . 
D 4 DMS   1  302 302 DMS   DMS B . 
E 5 SO4   1  303 303 SO4   SO4 B . 
F 5 SO4   1  304 304 SO4   SO4 B . 
G 6 HOH   1  101 118 HOH   HOH A . 
G 6 HOH   2  102 16  HOH   HOH A . 
G 6 HOH   3  103 48  HOH   HOH A . 
G 6 HOH   4  104 34  HOH   HOH A . 
G 6 HOH   5  105 65  HOH   HOH A . 
G 6 HOH   6  106 98  HOH   HOH A . 
G 6 HOH   7  107 20  HOH   HOH A . 
G 6 HOH   8  108 148 HOH   HOH A . 
G 6 HOH   9  109 28  HOH   HOH A . 
G 6 HOH   10 110 49  HOH   HOH A . 
G 6 HOH   11 111 54  HOH   HOH A . 
G 6 HOH   12 112 119 HOH   HOH A . 
G 6 HOH   13 113 110 HOH   HOH A . 
G 6 HOH   14 114 105 HOH   HOH A . 
G 6 HOH   15 115 29  HOH   HOH A . 
G 6 HOH   16 116 120 HOH   HOH A . 
G 6 HOH   17 117 50  HOH   HOH A . 
H 6 HOH   1  401 9   HOH   HOH B . 
H 6 HOH   2  402 144 HOH   HOH B . 
H 6 HOH   3  403 11  HOH   HOH B . 
H 6 HOH   4  404 62  HOH   HOH B . 
H 6 HOH   5  405 46  HOH   HOH B . 
H 6 HOH   6  406 14  HOH   HOH B . 
H 6 HOH   7  407 135 HOH   HOH B . 
H 6 HOH   8  408 117 HOH   HOH B . 
H 6 HOH   9  409 58  HOH   HOH B . 
H 6 HOH   10 410 69  HOH   HOH B . 
H 6 HOH   11 411 139 HOH   HOH B . 
H 6 HOH   12 412 133 HOH   HOH B . 
H 6 HOH   13 413 5   HOH   HOH B . 
H 6 HOH   14 414 4   HOH   HOH B . 
H 6 HOH   15 415 126 HOH   HOH B . 
H 6 HOH   16 416 1   HOH   HOH B . 
H 6 HOH   17 417 100 HOH   HOH B . 
H 6 HOH   18 418 2   HOH   HOH B . 
H 6 HOH   19 419 147 HOH   HOH B . 
H 6 HOH   20 420 80  HOH   HOH B . 
H 6 HOH   21 421 132 HOH   HOH B . 
H 6 HOH   22 422 145 HOH   HOH B . 
H 6 HOH   23 423 12  HOH   HOH B . 
H 6 HOH   24 424 68  HOH   HOH B . 
H 6 HOH   25 425 125 HOH   HOH B . 
H 6 HOH   26 426 130 HOH   HOH B . 
H 6 HOH   27 427 32  HOH   HOH B . 
H 6 HOH   28 428 92  HOH   HOH B . 
H 6 HOH   29 429 128 HOH   HOH B . 
H 6 HOH   30 430 24  HOH   HOH B . 
H 6 HOH   31 431 23  HOH   HOH B . 
H 6 HOH   32 432 39  HOH   HOH B . 
H 6 HOH   33 433 136 HOH   HOH B . 
H 6 HOH   34 434 10  HOH   HOH B . 
H 6 HOH   35 435 116 HOH   HOH B . 
H 6 HOH   36 436 129 HOH   HOH B . 
H 6 HOH   37 437 137 HOH   HOH B . 
H 6 HOH   38 438 3   HOH   HOH B . 
H 6 HOH   39 439 143 HOH   HOH B . 
H 6 HOH   40 440 30  HOH   HOH B . 
H 6 HOH   41 441 18  HOH   HOH B . 
H 6 HOH   42 442 146 HOH   HOH B . 
H 6 HOH   43 443 107 HOH   HOH B . 
H 6 HOH   44 444 64  HOH   HOH B . 
H 6 HOH   45 445 102 HOH   HOH B . 
H 6 HOH   46 446 35  HOH   HOH B . 
H 6 HOH   47 447 138 HOH   HOH B . 
H 6 HOH   48 448 134 HOH   HOH B . 
H 6 HOH   49 449 82  HOH   HOH B . 
H 6 HOH   50 450 60  HOH   HOH B . 
H 6 HOH   51 451 124 HOH   HOH B . 
H 6 HOH   52 452 127 HOH   HOH B . 
H 6 HOH   53 453 90  HOH   HOH B . 
H 6 HOH   54 454 45  HOH   HOH B . 
H 6 HOH   55 455 67  HOH   HOH B . 
H 6 HOH   56 456 131 HOH   HOH B . 
H 6 HOH   57 457 87  HOH   HOH B . 
H 6 HOH   58 458 61  HOH   HOH B . 
H 6 HOH   59 459 73  HOH   HOH B . 
H 6 HOH   60 460 26  HOH   HOH B . 
H 6 HOH   61 461 42  HOH   HOH B . 
H 6 HOH   62 462 44  HOH   HOH B . 
H 6 HOH   63 463 109 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           7HPD 
_cell.length_a           42.584 
_cell.length_b           42.584 
_cell.length_c           216.536 
_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                         7HPD 
_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          7HPD 
_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   41.90 
_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   2023-11-22 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92124 
_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                     7HPD 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             216.51 
_reflns.d_resolution_high            1.61 
_reflns.number_obs                   27147 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.083 
_reflns.pdbx_netI_over_sigmaI        12.0 
_reflns.pdbx_redundancy              25.5 
_reflns.pdbx_Rrim_I_all              0.085 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     693357 
_reflns.pdbx_chi_squared             0.25 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.61 
_reflns_shell.d_res_low                   1.64 
_reflns_shell.number_measured_all         32517 
_reflns_shell.number_unique_obs           1301 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_chi_squared            0.07 
_reflns_shell.pdbx_redundancy             25.0 
_reflns_shell.percent_possible_obs        96.8 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             14.217 
_reflns_shell.pdbx_Rpim_I_all             2.818 
_reflns_shell.pdbx_CC_half                0.318 
_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                                 7HPD 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     21449 
_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                             23.12 
_refine.ls_d_res_high                            1.626 
_refine.ls_percent_reflns_obs                    81.5 
_refine.ls_R_factor_obs                          0.2464 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2452 
_refine.ls_R_factor_R_free                       0.2695 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.090 
_refine.ls_number_reflns_R_free                  1092 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.940 
_refine.correlation_coeff_Fo_to_Fc_free          0.941 
_refine.B_iso_mean                               67.59 
_refine.aniso_B[1][1]                            -8.19950 
_refine.aniso_B[2][2]                            -8.19950 
_refine.aniso_B[3][3]                            16.39890 
_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             0.140 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.129 
_refine.pdbx_overall_SU_R_Blow_DPI               0.148 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.132 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HPD 
_refine_analyze.Luzzati_coordinate_error_obs    0.42 
_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        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         38 
_refine_hist.number_atoms_solvent             80 
_refine_hist.number_atoms_total               1594 
_refine_hist.d_res_high                       1.626 
_refine_hist.d_res_low                        23.12 
# 
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  1580 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.03  ? 2.00  2154 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  536  '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  272  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1580 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.44  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           16.98 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  196  '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  1204 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.63 
_refine_ls_shell.d_res_low                        1.73 
_refine_ls_shell.number_reflns_R_work             401 
_refine_ls_shell.R_factor_R_work                  0.6503 
_refine_ls_shell.percent_reflns_obs               9.48 
_refine_ls_shell.R_factor_R_free                  0.5531 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            6.53 
_refine_ls_shell.number_reflns_R_free             28 
_refine_ls_shell.number_reflns_all                429 
_refine_ls_shell.R_factor_all                     0.6443 
# 
_struct.entry_id                  7HPD 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0015216-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HPD 
_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 5 ? 
F N N 5 ? 
G N N 6 ? 
H 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 7HPD A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HPD 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 7HPD SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HPD MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HPD MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HPD 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)' 4690 ? 
1 MORE         -43  ? 
1 'SSA (A^2)'  9680 ? 
# 
_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 
# 
_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 TRP B 41  ? LYS B 45  ? TRP B 50  LYS B 54  1 ? 5 
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  ? MET B 40  ? VAL B 45  MET B 49  
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 GLU A 11  ? N GLU A 54  O ARG B 15  ? O ARG B 24  
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                   7HPD 
_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 LEU B 30 ? ? -123.83 -155.68 
2 1 CYS B 80 ? ? 77.74   -15.52  
3 1 LEU B 92 ? ? -131.81 -44.49  
# 
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 432 ? H HOH . 
2 1 B HOH 454 ? H HOH . 
3 1 B HOH 462 ? H 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 -13.7413 -1.9497 -19.5339 0.0154 -0.2879 -0.2462 0.1722 0.1683 0.1855 6.9595 5.0276 7.8304 -2.4359 
0.6619 2.4448  0.5798 0.6638 0.3896 -0.7030 -0.4349 -0.4261 -0.2299 0.8045 -0.1449 
'X-RAY DIFFRACTION' 2 ? refined -18.3440 0.4743  -15.6734 0.1731 0.0754  -0.0903 0.2307 0.0345 0.0403 1.9089 1.2867 1.9365 -1.4058 
1.0086 -0.1048 0.4160 0.2241 0.1826 -0.2198 -0.4244 0.0593  0.0699  0.1985 0.0084  
# 
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 GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 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 
A1BGV N1   N N N 1   
A1BGV N3   N N N 2   
A1BGV C4   C Y N 3   
A1BGV C5   C Y N 4   
A1BGV C6   C Y N 5   
A1BGV C7   C Y N 6   
A1BGV C8   C Y N 7   
A1BGV C10  C Y N 8   
A1BGV C13  C N N 9   
A1BGV C15  C Y N 10  
A1BGV C1   C N N 11  
A1BGV C2   C N N 12  
A1BGV C3   C N N 13  
A1BGV N2   N Y N 14  
A1BGV C9   C N N 15  
A1BGV O1   O N N 16  
A1BGV C11  C Y N 17  
A1BGV N4   N Y N 18  
A1BGV C12  C Y N 19  
A1BGV N5   N N N 20  
A1BGV O2   O N N 21  
A1BGV C14  C Y N 22  
A1BGV C16  C Y N 23  
A1BGV N6   N Y N 24  
A1BGV H8   H N N 25  
A1BGV H11  H N N 26  
A1BGV H9   H N N 27  
A1BGV H10  H N N 28  
A1BGV H17  H N N 29  
A1BGV H2   H N N 30  
A1BGV H1   H N N 31  
A1BGV H3   H N N 32  
A1BGV H4   H N N 33  
A1BGV H5   H N N 34  
A1BGV H6   H N N 35  
A1BGV H7   H N N 36  
A1BGV H12  H N N 37  
A1BGV H13  H N N 38  
A1BGV H15  H N N 39  
A1BGV H14  H N N 40  
A1BGV H16  H N N 41  
A1BGV H18  H N N 42  
ALA   N    N N N 43  
ALA   CA   C N S 44  
ALA   C    C N N 45  
ALA   O    O N N 46  
ALA   CB   C N N 47  
ALA   OXT  O N N 48  
ALA   H    H N N 49  
ALA   H2   H N N 50  
ALA   HA   H N N 51  
ALA   HB1  H N N 52  
ALA   HB2  H N N 53  
ALA   HB3  H N N 54  
ALA   HXT  H N N 55  
ARG   N    N N N 56  
ARG   CA   C N S 57  
ARG   C    C N N 58  
ARG   O    O N N 59  
ARG   CB   C N N 60  
ARG   CG   C N N 61  
ARG   CD   C N N 62  
ARG   NE   N N N 63  
ARG   CZ   C N N 64  
ARG   NH1  N N N 65  
ARG   NH2  N N N 66  
ARG   OXT  O N N 67  
ARG   H    H N N 68  
ARG   H2   H N N 69  
ARG   HA   H N N 70  
ARG   HB2  H N N 71  
ARG   HB3  H N N 72  
ARG   HG2  H N N 73  
ARG   HG3  H N N 74  
ARG   HD2  H N N 75  
ARG   HD3  H N N 76  
ARG   HE   H N N 77  
ARG   HH11 H N N 78  
ARG   HH12 H N N 79  
ARG   HH21 H N N 80  
ARG   HH22 H N N 81  
ARG   HXT  H N N 82  
ASN   N    N N N 83  
ASN   CA   C N S 84  
ASN   C    C N N 85  
ASN   O    O N N 86  
ASN   CB   C N N 87  
ASN   CG   C N N 88  
ASN   OD1  O N N 89  
ASN   ND2  N N N 90  
ASN   OXT  O N N 91  
ASN   H    H N N 92  
ASN   H2   H N N 93  
ASN   HA   H N N 94  
ASN   HB2  H N N 95  
ASN   HB3  H N N 96  
ASN   HD21 H N N 97  
ASN   HD22 H N N 98  
ASN   HXT  H N N 99  
ASP   N    N N N 100 
ASP   CA   C N S 101 
ASP   C    C N N 102 
ASP   O    O N N 103 
ASP   CB   C N N 104 
ASP   CG   C N N 105 
ASP   OD1  O N N 106 
ASP   OD2  O N N 107 
ASP   OXT  O N N 108 
ASP   H    H N N 109 
ASP   H2   H N N 110 
ASP   HA   H N N 111 
ASP   HB2  H N N 112 
ASP   HB3  H N N 113 
ASP   HD2  H N N 114 
ASP   HXT  H N N 115 
CYS   N    N N N 116 
CYS   CA   C N R 117 
CYS   C    C N N 118 
CYS   O    O N N 119 
CYS   CB   C N N 120 
CYS   SG   S N N 121 
CYS   OXT  O N N 122 
CYS   H    H N N 123 
CYS   H2   H N N 124 
CYS   HA   H N N 125 
CYS   HB2  H N N 126 
CYS   HB3  H N N 127 
CYS   HG   H N N 128 
CYS   HXT  H N N 129 
DMS   S    S N N 130 
DMS   O    O N N 131 
DMS   C1   C N N 132 
DMS   C2   C N N 133 
DMS   H11  H N N 134 
DMS   H12  H N N 135 
DMS   H13  H N N 136 
DMS   H21  H N N 137 
DMS   H22  H N N 138 
DMS   H23  H N N 139 
GLN   N    N N N 140 
GLN   CA   C N S 141 
GLN   C    C N N 142 
GLN   O    O N N 143 
GLN   CB   C N N 144 
GLN   CG   C N N 145 
GLN   CD   C N N 146 
GLN   OE1  O N N 147 
GLN   NE2  N N N 148 
GLN   OXT  O N N 149 
GLN   H    H N N 150 
GLN   H2   H N N 151 
GLN   HA   H N N 152 
GLN   HB2  H N N 153 
GLN   HB3  H N N 154 
GLN   HG2  H N N 155 
GLN   HG3  H N N 156 
GLN   HE21 H N N 157 
GLN   HE22 H N N 158 
GLN   HXT  H N N 159 
GLU   N    N N N 160 
GLU   CA   C N S 161 
GLU   C    C N N 162 
GLU   O    O N N 163 
GLU   CB   C N N 164 
GLU   CG   C N N 165 
GLU   CD   C N N 166 
GLU   OE1  O N N 167 
GLU   OE2  O N N 168 
GLU   OXT  O N N 169 
GLU   H    H N N 170 
GLU   H2   H N N 171 
GLU   HA   H N N 172 
GLU   HB2  H N N 173 
GLU   HB3  H N N 174 
GLU   HG2  H N N 175 
GLU   HG3  H N N 176 
GLU   HE2  H N N 177 
GLU   HXT  H N N 178 
GLY   N    N N N 179 
GLY   CA   C N N 180 
GLY   C    C N N 181 
GLY   O    O N N 182 
GLY   OXT  O N N 183 
GLY   H    H N N 184 
GLY   H2   H N N 185 
GLY   HA2  H N N 186 
GLY   HA3  H N N 187 
GLY   HXT  H N N 188 
HIS   N    N N N 189 
HIS   CA   C N S 190 
HIS   C    C N N 191 
HIS   O    O N N 192 
HIS   CB   C N N 193 
HIS   CG   C Y N 194 
HIS   ND1  N Y N 195 
HIS   CD2  C Y N 196 
HIS   CE1  C Y N 197 
HIS   NE2  N Y N 198 
HIS   OXT  O N N 199 
HIS   H    H N N 200 
HIS   H2   H N N 201 
HIS   HA   H N N 202 
HIS   HB2  H N N 203 
HIS   HB3  H N N 204 
HIS   HD1  H N N 205 
HIS   HD2  H N N 206 
HIS   HE1  H N N 207 
HIS   HE2  H N N 208 
HIS   HXT  H N N 209 
HOH   O    O N N 210 
HOH   H1   H N N 211 
HOH   H2   H N N 212 
ILE   N    N N N 213 
ILE   CA   C N S 214 
ILE   C    C N N 215 
ILE   O    O N N 216 
ILE   CB   C N S 217 
ILE   CG1  C N N 218 
ILE   CG2  C N N 219 
ILE   CD1  C N N 220 
ILE   OXT  O N N 221 
ILE   H    H N N 222 
ILE   H2   H N N 223 
ILE   HA   H N N 224 
ILE   HB   H N N 225 
ILE   HG12 H N N 226 
ILE   HG13 H N N 227 
ILE   HG21 H N N 228 
ILE   HG22 H N N 229 
ILE   HG23 H N N 230 
ILE   HD11 H N N 231 
ILE   HD12 H N N 232 
ILE   HD13 H N N 233 
ILE   HXT  H N N 234 
LEU   N    N N N 235 
LEU   CA   C N S 236 
LEU   C    C N N 237 
LEU   O    O N N 238 
LEU   CB   C N N 239 
LEU   CG   C N N 240 
LEU   CD1  C N N 241 
LEU   CD2  C N N 242 
LEU   OXT  O N N 243 
LEU   H    H N N 244 
LEU   H2   H N N 245 
LEU   HA   H N N 246 
LEU   HB2  H N N 247 
LEU   HB3  H N N 248 
LEU   HG   H N N 249 
LEU   HD11 H N N 250 
LEU   HD12 H N N 251 
LEU   HD13 H N N 252 
LEU   HD21 H N N 253 
LEU   HD22 H N N 254 
LEU   HD23 H N N 255 
LEU   HXT  H N N 256 
LYS   N    N N N 257 
LYS   CA   C N S 258 
LYS   C    C N N 259 
LYS   O    O N N 260 
LYS   CB   C N N 261 
LYS   CG   C N N 262 
LYS   CD   C N N 263 
LYS   CE   C N N 264 
LYS   NZ   N N N 265 
LYS   OXT  O N N 266 
LYS   H    H N N 267 
LYS   H2   H N N 268 
LYS   HA   H N N 269 
LYS   HB2  H N N 270 
LYS   HB3  H N N 271 
LYS   HG2  H N N 272 
LYS   HG3  H N N 273 
LYS   HD2  H N N 274 
LYS   HD3  H N N 275 
LYS   HE2  H N N 276 
LYS   HE3  H N N 277 
LYS   HZ1  H N N 278 
LYS   HZ2  H N N 279 
LYS   HZ3  H N N 280 
LYS   HXT  H N N 281 
MET   N    N N N 282 
MET   CA   C N S 283 
MET   C    C N N 284 
MET   O    O N N 285 
MET   CB   C N N 286 
MET   CG   C N N 287 
MET   SD   S N N 288 
MET   CE   C N N 289 
MET   OXT  O N N 290 
MET   H    H N N 291 
MET   H2   H N N 292 
MET   HA   H N N 293 
MET   HB2  H N N 294 
MET   HB3  H N N 295 
MET   HG2  H N N 296 
MET   HG3  H N N 297 
MET   HE1  H N N 298 
MET   HE2  H N N 299 
MET   HE3  H N N 300 
MET   HXT  H N N 301 
PHE   N    N N N 302 
PHE   CA   C N S 303 
PHE   C    C N N 304 
PHE   O    O N N 305 
PHE   CB   C N N 306 
PHE   CG   C Y N 307 
PHE   CD1  C Y N 308 
PHE   CD2  C Y N 309 
PHE   CE1  C Y N 310 
PHE   CE2  C Y N 311 
PHE   CZ   C Y N 312 
PHE   OXT  O N N 313 
PHE   H    H N N 314 
PHE   H2   H N N 315 
PHE   HA   H N N 316 
PHE   HB2  H N N 317 
PHE   HB3  H N N 318 
PHE   HD1  H N N 319 
PHE   HD2  H N N 320 
PHE   HE1  H N N 321 
PHE   HE2  H N N 322 
PHE   HZ   H N N 323 
PHE   HXT  H N N 324 
PRO   N    N N N 325 
PRO   CA   C N S 326 
PRO   C    C N N 327 
PRO   O    O N N 328 
PRO   CB   C N N 329 
PRO   CG   C N N 330 
PRO   CD   C N N 331 
PRO   OXT  O N N 332 
PRO   H    H N N 333 
PRO   HA   H N N 334 
PRO   HB2  H N N 335 
PRO   HB3  H N N 336 
PRO   HG2  H N N 337 
PRO   HG3  H N N 338 
PRO   HD2  H N N 339 
PRO   HD3  H N N 340 
PRO   HXT  H N N 341 
SER   N    N N N 342 
SER   CA   C N S 343 
SER   C    C N N 344 
SER   O    O N N 345 
SER   CB   C N N 346 
SER   OG   O N N 347 
SER   OXT  O N N 348 
SER   H    H N N 349 
SER   H2   H N N 350 
SER   HA   H N N 351 
SER   HB2  H N N 352 
SER   HB3  H N N 353 
SER   HG   H N N 354 
SER   HXT  H N N 355 
SO4   S    S N N 356 
SO4   O1   O N N 357 
SO4   O2   O N N 358 
SO4   O3   O N N 359 
SO4   O4   O N N 360 
THR   N    N N N 361 
THR   CA   C N S 362 
THR   C    C N N 363 
THR   O    O N N 364 
THR   CB   C N R 365 
THR   OG1  O N N 366 
THR   CG2  C N N 367 
THR   OXT  O N N 368 
THR   H    H N N 369 
THR   H2   H N N 370 
THR   HA   H N N 371 
THR   HB   H N N 372 
THR   HG1  H N N 373 
THR   HG21 H N N 374 
THR   HG22 H N N 375 
THR   HG23 H N N 376 
THR   HXT  H N N 377 
TRP   N    N N N 378 
TRP   CA   C N S 379 
TRP   C    C N N 380 
TRP   O    O N N 381 
TRP   CB   C N N 382 
TRP   CG   C Y N 383 
TRP   CD1  C Y N 384 
TRP   CD2  C Y N 385 
TRP   NE1  N Y N 386 
TRP   CE2  C Y N 387 
TRP   CE3  C Y N 388 
TRP   CZ2  C Y N 389 
TRP   CZ3  C Y N 390 
TRP   CH2  C Y N 391 
TRP   OXT  O N N 392 
TRP   H    H N N 393 
TRP   H2   H N N 394 
TRP   HA   H N N 395 
TRP   HB2  H N N 396 
TRP   HB3  H N N 397 
TRP   HD1  H N N 398 
TRP   HE1  H N N 399 
TRP   HE3  H N N 400 
TRP   HZ2  H N N 401 
TRP   HZ3  H N N 402 
TRP   HH2  H N N 403 
TRP   HXT  H N N 404 
TYR   N    N N N 405 
TYR   CA   C N S 406 
TYR   C    C N N 407 
TYR   O    O N N 408 
TYR   CB   C N N 409 
TYR   CG   C Y N 410 
TYR   CD1  C Y N 411 
TYR   CD2  C Y N 412 
TYR   CE1  C Y N 413 
TYR   CE2  C Y N 414 
TYR   CZ   C Y N 415 
TYR   OH   O N N 416 
TYR   OXT  O N N 417 
TYR   H    H N N 418 
TYR   H2   H N N 419 
TYR   HA   H N N 420 
TYR   HB2  H N N 421 
TYR   HB3  H N N 422 
TYR   HD1  H N N 423 
TYR   HD2  H N N 424 
TYR   HE1  H N N 425 
TYR   HE2  H N N 426 
TYR   HH   H N N 427 
TYR   HXT  H N N 428 
VAL   N    N N N 429 
VAL   CA   C N S 430 
VAL   C    C N N 431 
VAL   O    O N N 432 
VAL   CB   C N N 433 
VAL   CG1  C N N 434 
VAL   CG2  C N N 435 
VAL   OXT  O N N 436 
VAL   H    H N N 437 
VAL   H2   H N N 438 
VAL   HA   H N N 439 
VAL   HB   H N N 440 
VAL   HG11 H N N 441 
VAL   HG12 H N N 442 
VAL   HG13 H N N 443 
VAL   HG21 H N N 444 
VAL   HG22 H N N 445 
VAL   HG23 H N N 446 
VAL   HXT  H N N 447 
# 
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 
A1BGV C1  C2   sing N N 1   
A1BGV C2  C3   sing N N 2   
A1BGV C2  N1   sing N N 3   
A1BGV N1  C4   sing N N 4   
A1BGV C4  N2   doub Y N 5   
A1BGV N2  C5   sing Y N 6   
A1BGV C5  C6   doub Y N 7   
A1BGV C6  C7   sing Y N 8   
A1BGV C7  C8   doub Y N 9   
A1BGV C8  C9   sing N N 10  
A1BGV C9  O1   doub N N 11  
A1BGV C9  N3   sing N N 12  
A1BGV N3  C10  sing N N 13  
A1BGV C10 C11  doub Y N 14  
A1BGV C11 N4   sing Y N 15  
A1BGV N4  C12  sing Y N 16  
A1BGV C12 C13  sing N N 17  
A1BGV C13 N5   sing N N 18  
A1BGV C13 O2   doub N N 19  
A1BGV C12 C14  doub Y N 20  
A1BGV C8  C15  sing Y N 21  
A1BGV C15 C16  doub Y N 22  
A1BGV C16 N6   sing Y N 23  
A1BGV C4  N6   sing Y N 24  
A1BGV C5  C16  sing Y N 25  
A1BGV C10 C14  sing Y N 26  
A1BGV N1  H8   sing N N 27  
A1BGV N3  H11  sing N N 28  
A1BGV C6  H9   sing N N 29  
A1BGV C7  H10  sing N N 30  
A1BGV C15 H17  sing N N 31  
A1BGV C1  H2   sing N N 32  
A1BGV C1  H1   sing N N 33  
A1BGV C1  H3   sing N N 34  
A1BGV C2  H4   sing N N 35  
A1BGV C3  H5   sing N N 36  
A1BGV C3  H6   sing N N 37  
A1BGV C3  H7   sing N N 38  
A1BGV C11 H12  sing N N 39  
A1BGV N4  H13  sing N N 40  
A1BGV N5  H15  sing N N 41  
A1BGV N5  H14  sing N N 42  
A1BGV C14 H16  sing N N 43  
A1BGV N6  H18  sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ARG   N   CA   sing N N 57  
ARG   N   H    sing N N 58  
ARG   N   H2   sing N N 59  
ARG   CA  C    sing N N 60  
ARG   CA  CB   sing N N 61  
ARG   CA  HA   sing N N 62  
ARG   C   O    doub N N 63  
ARG   C   OXT  sing N N 64  
ARG   CB  CG   sing N N 65  
ARG   CB  HB2  sing N N 66  
ARG   CB  HB3  sing N N 67  
ARG   CG  CD   sing N N 68  
ARG   CG  HG2  sing N N 69  
ARG   CG  HG3  sing N N 70  
ARG   CD  NE   sing N N 71  
ARG   CD  HD2  sing N N 72  
ARG   CD  HD3  sing N N 73  
ARG   NE  CZ   sing N N 74  
ARG   NE  HE   sing N N 75  
ARG   CZ  NH1  sing N N 76  
ARG   CZ  NH2  doub N N 77  
ARG   NH1 HH11 sing N N 78  
ARG   NH1 HH12 sing N N 79  
ARG   NH2 HH21 sing N N 80  
ARG   NH2 HH22 sing N N 81  
ARG   OXT HXT  sing N N 82  
ASN   N   CA   sing N N 83  
ASN   N   H    sing N N 84  
ASN   N   H2   sing N N 85  
ASN   CA  C    sing N N 86  
ASN   CA  CB   sing N N 87  
ASN   CA  HA   sing N N 88  
ASN   C   O    doub N N 89  
ASN   C   OXT  sing N N 90  
ASN   CB  CG   sing N N 91  
ASN   CB  HB2  sing N N 92  
ASN   CB  HB3  sing N N 93  
ASN   CG  OD1  doub N N 94  
ASN   CG  ND2  sing N N 95  
ASN   ND2 HD21 sing N N 96  
ASN   ND2 HD22 sing N N 97  
ASN   OXT HXT  sing N N 98  
ASP   N   CA   sing N N 99  
ASP   N   H    sing N N 100 
ASP   N   H2   sing N N 101 
ASP   CA  C    sing N N 102 
ASP   CA  CB   sing N N 103 
ASP   CA  HA   sing N N 104 
ASP   C   O    doub N N 105 
ASP   C   OXT  sing N N 106 
ASP   CB  CG   sing N N 107 
ASP   CB  HB2  sing N N 108 
ASP   CB  HB3  sing N N 109 
ASP   CG  OD1  doub N N 110 
ASP   CG  OD2  sing N N 111 
ASP   OD2 HD2  sing N N 112 
ASP   OXT HXT  sing N N 113 
CYS   N   CA   sing N N 114 
CYS   N   H    sing N N 115 
CYS   N   H2   sing N N 116 
CYS   CA  C    sing N N 117 
CYS   CA  CB   sing N N 118 
CYS   CA  HA   sing N N 119 
CYS   C   O    doub N N 120 
CYS   C   OXT  sing N N 121 
CYS   CB  SG   sing N N 122 
CYS   CB  HB2  sing N N 123 
CYS   CB  HB3  sing N N 124 
CYS   SG  HG   sing N N 125 
CYS   OXT HXT  sing N N 126 
DMS   S   O    doub N N 127 
DMS   S   C1   sing N N 128 
DMS   S   C2   sing N N 129 
DMS   C1  H11  sing N N 130 
DMS   C1  H12  sing N N 131 
DMS   C1  H13  sing N N 132 
DMS   C2  H21  sing N N 133 
DMS   C2  H22  sing N N 134 
DMS   C2  H23  sing N N 135 
GLN   N   CA   sing N N 136 
GLN   N   H    sing N N 137 
GLN   N   H2   sing N N 138 
GLN   CA  C    sing N N 139 
GLN   CA  CB   sing N N 140 
GLN   CA  HA   sing N N 141 
GLN   C   O    doub N N 142 
GLN   C   OXT  sing N N 143 
GLN   CB  CG   sing N N 144 
GLN   CB  HB2  sing N N 145 
GLN   CB  HB3  sing N N 146 
GLN   CG  CD   sing N N 147 
GLN   CG  HG2  sing N N 148 
GLN   CG  HG3  sing N N 149 
GLN   CD  OE1  doub N N 150 
GLN   CD  NE2  sing N N 151 
GLN   NE2 HE21 sing N N 152 
GLN   NE2 HE22 sing N N 153 
GLN   OXT HXT  sing N N 154 
GLU   N   CA   sing N N 155 
GLU   N   H    sing N N 156 
GLU   N   H2   sing N N 157 
GLU   CA  C    sing N N 158 
GLU   CA  CB   sing N N 159 
GLU   CA  HA   sing N N 160 
GLU   C   O    doub N N 161 
GLU   C   OXT  sing N N 162 
GLU   CB  CG   sing N N 163 
GLU   CB  HB2  sing N N 164 
GLU   CB  HB3  sing N N 165 
GLU   CG  CD   sing N N 166 
GLU   CG  HG2  sing N N 167 
GLU   CG  HG3  sing N N 168 
GLU   CD  OE1  doub N N 169 
GLU   CD  OE2  sing N N 170 
GLU   OE2 HE2  sing N N 171 
GLU   OXT HXT  sing N N 172 
GLY   N   CA   sing N N 173 
GLY   N   H    sing N N 174 
GLY   N   H2   sing N N 175 
GLY   CA  C    sing N N 176 
GLY   CA  HA2  sing N N 177 
GLY   CA  HA3  sing N N 178 
GLY   C   O    doub N N 179 
GLY   C   OXT  sing N N 180 
GLY   OXT HXT  sing N N 181 
HIS   N   CA   sing N N 182 
HIS   N   H    sing N N 183 
HIS   N   H2   sing N N 184 
HIS   CA  C    sing N N 185 
HIS   CA  CB   sing N N 186 
HIS   CA  HA   sing N N 187 
HIS   C   O    doub N N 188 
HIS   C   OXT  sing N N 189 
HIS   CB  CG   sing N N 190 
HIS   CB  HB2  sing N N 191 
HIS   CB  HB3  sing N N 192 
HIS   CG  ND1  sing Y N 193 
HIS   CG  CD2  doub Y N 194 
HIS   ND1 CE1  doub Y N 195 
HIS   ND1 HD1  sing N N 196 
HIS   CD2 NE2  sing Y N 197 
HIS   CD2 HD2  sing N N 198 
HIS   CE1 NE2  sing Y N 199 
HIS   CE1 HE1  sing N N 200 
HIS   NE2 HE2  sing N N 201 
HIS   OXT HXT  sing N N 202 
HOH   O   H1   sing N N 203 
HOH   O   H2   sing N N 204 
ILE   N   CA   sing N N 205 
ILE   N   H    sing N N 206 
ILE   N   H2   sing N N 207 
ILE   CA  C    sing N N 208 
ILE   CA  CB   sing N N 209 
ILE   CA  HA   sing N N 210 
ILE   C   O    doub N N 211 
ILE   C   OXT  sing N N 212 
ILE   CB  CG1  sing N N 213 
ILE   CB  CG2  sing N N 214 
ILE   CB  HB   sing N N 215 
ILE   CG1 CD1  sing N N 216 
ILE   CG1 HG12 sing N N 217 
ILE   CG1 HG13 sing N N 218 
ILE   CG2 HG21 sing N N 219 
ILE   CG2 HG22 sing N N 220 
ILE   CG2 HG23 sing N N 221 
ILE   CD1 HD11 sing N N 222 
ILE   CD1 HD12 sing N N 223 
ILE   CD1 HD13 sing N N 224 
ILE   OXT HXT  sing N N 225 
LEU   N   CA   sing N N 226 
LEU   N   H    sing N N 227 
LEU   N   H2   sing N N 228 
LEU   CA  C    sing N N 229 
LEU   CA  CB   sing N N 230 
LEU   CA  HA   sing N N 231 
LEU   C   O    doub N N 232 
LEU   C   OXT  sing N N 233 
LEU   CB  CG   sing N N 234 
LEU   CB  HB2  sing N N 235 
LEU   CB  HB3  sing N N 236 
LEU   CG  CD1  sing N N 237 
LEU   CG  CD2  sing N N 238 
LEU   CG  HG   sing N N 239 
LEU   CD1 HD11 sing N N 240 
LEU   CD1 HD12 sing N N 241 
LEU   CD1 HD13 sing N N 242 
LEU   CD2 HD21 sing N N 243 
LEU   CD2 HD22 sing N N 244 
LEU   CD2 HD23 sing N N 245 
LEU   OXT HXT  sing N N 246 
LYS   N   CA   sing N N 247 
LYS   N   H    sing N N 248 
LYS   N   H2   sing N N 249 
LYS   CA  C    sing N N 250 
LYS   CA  CB   sing N N 251 
LYS   CA  HA   sing N N 252 
LYS   C   O    doub N N 253 
LYS   C   OXT  sing N N 254 
LYS   CB  CG   sing N N 255 
LYS   CB  HB2  sing N N 256 
LYS   CB  HB3  sing N N 257 
LYS   CG  CD   sing N N 258 
LYS   CG  HG2  sing N N 259 
LYS   CG  HG3  sing N N 260 
LYS   CD  CE   sing N N 261 
LYS   CD  HD2  sing N N 262 
LYS   CD  HD3  sing N N 263 
LYS   CE  NZ   sing N N 264 
LYS   CE  HE2  sing N N 265 
LYS   CE  HE3  sing N N 266 
LYS   NZ  HZ1  sing N N 267 
LYS   NZ  HZ2  sing N N 268 
LYS   NZ  HZ3  sing N N 269 
LYS   OXT HXT  sing N N 270 
MET   N   CA   sing N N 271 
MET   N   H    sing N N 272 
MET   N   H2   sing N N 273 
MET   CA  C    sing N N 274 
MET   CA  CB   sing N N 275 
MET   CA  HA   sing N N 276 
MET   C   O    doub N N 277 
MET   C   OXT  sing N N 278 
MET   CB  CG   sing N N 279 
MET   CB  HB2  sing N N 280 
MET   CB  HB3  sing N N 281 
MET   CG  SD   sing N N 282 
MET   CG  HG2  sing N N 283 
MET   CG  HG3  sing N N 284 
MET   SD  CE   sing N N 285 
MET   CE  HE1  sing N N 286 
MET   CE  HE2  sing N N 287 
MET   CE  HE3  sing N N 288 
MET   OXT HXT  sing N N 289 
PHE   N   CA   sing N N 290 
PHE   N   H    sing N N 291 
PHE   N   H2   sing N N 292 
PHE   CA  C    sing N N 293 
PHE   CA  CB   sing N N 294 
PHE   CA  HA   sing N N 295 
PHE   C   O    doub N N 296 
PHE   C   OXT  sing N N 297 
PHE   CB  CG   sing N N 298 
PHE   CB  HB2  sing N N 299 
PHE   CB  HB3  sing N N 300 
PHE   CG  CD1  doub Y N 301 
PHE   CG  CD2  sing Y N 302 
PHE   CD1 CE1  sing Y N 303 
PHE   CD1 HD1  sing N N 304 
PHE   CD2 CE2  doub Y N 305 
PHE   CD2 HD2  sing N N 306 
PHE   CE1 CZ   doub Y N 307 
PHE   CE1 HE1  sing N N 308 
PHE   CE2 CZ   sing Y N 309 
PHE   CE2 HE2  sing N N 310 
PHE   CZ  HZ   sing N N 311 
PHE   OXT HXT  sing N N 312 
PRO   N   CA   sing N N 313 
PRO   N   CD   sing N N 314 
PRO   N   H    sing N N 315 
PRO   CA  C    sing N N 316 
PRO   CA  CB   sing N N 317 
PRO   CA  HA   sing N N 318 
PRO   C   O    doub N N 319 
PRO   C   OXT  sing N N 320 
PRO   CB  CG   sing N N 321 
PRO   CB  HB2  sing N N 322 
PRO   CB  HB3  sing N N 323 
PRO   CG  CD   sing N N 324 
PRO   CG  HG2  sing N N 325 
PRO   CG  HG3  sing N N 326 
PRO   CD  HD2  sing N N 327 
PRO   CD  HD3  sing N N 328 
PRO   OXT HXT  sing N N 329 
SER   N   CA   sing N N 330 
SER   N   H    sing N N 331 
SER   N   H2   sing N N 332 
SER   CA  C    sing N N 333 
SER   CA  CB   sing N N 334 
SER   CA  HA   sing N N 335 
SER   C   O    doub N N 336 
SER   C   OXT  sing N N 337 
SER   CB  OG   sing N N 338 
SER   CB  HB2  sing N N 339 
SER   CB  HB3  sing N N 340 
SER   OG  HG   sing N N 341 
SER   OXT HXT  sing N N 342 
SO4   S   O1   doub N N 343 
SO4   S   O2   doub N N 344 
SO4   S   O3   sing N N 345 
SO4   S   O4   sing N N 346 
THR   N   CA   sing N N 347 
THR   N   H    sing N N 348 
THR   N   H2   sing N N 349 
THR   CA  C    sing N N 350 
THR   CA  CB   sing N N 351 
THR   CA  HA   sing N N 352 
THR   C   O    doub N N 353 
THR   C   OXT  sing N N 354 
THR   CB  OG1  sing N N 355 
THR   CB  CG2  sing N N 356 
THR   CB  HB   sing N N 357 
THR   OG1 HG1  sing N N 358 
THR   CG2 HG21 sing N N 359 
THR   CG2 HG22 sing N N 360 
THR   CG2 HG23 sing N N 361 
THR   OXT HXT  sing N N 362 
TRP   N   CA   sing N N 363 
TRP   N   H    sing N N 364 
TRP   N   H2   sing N N 365 
TRP   CA  C    sing N N 366 
TRP   CA  CB   sing N N 367 
TRP   CA  HA   sing N N 368 
TRP   C   O    doub N N 369 
TRP   C   OXT  sing N N 370 
TRP   CB  CG   sing N N 371 
TRP   CB  HB2  sing N N 372 
TRP   CB  HB3  sing N N 373 
TRP   CG  CD1  doub Y N 374 
TRP   CG  CD2  sing Y N 375 
TRP   CD1 NE1  sing Y N 376 
TRP   CD1 HD1  sing N N 377 
TRP   CD2 CE2  doub Y N 378 
TRP   CD2 CE3  sing Y N 379 
TRP   NE1 CE2  sing Y N 380 
TRP   NE1 HE1  sing N N 381 
TRP   CE2 CZ2  sing Y N 382 
TRP   CE3 CZ3  doub Y N 383 
TRP   CE3 HE3  sing N N 384 
TRP   CZ2 CH2  doub Y N 385 
TRP   CZ2 HZ2  sing N N 386 
TRP   CZ3 CH2  sing Y N 387 
TRP   CZ3 HZ3  sing N N 388 
TRP   CH2 HH2  sing N N 389 
TRP   OXT HXT  sing N N 390 
TYR   N   CA   sing N N 391 
TYR   N   H    sing N N 392 
TYR   N   H2   sing N N 393 
TYR   CA  C    sing N N 394 
TYR   CA  CB   sing N N 395 
TYR   CA  HA   sing N N 396 
TYR   C   O    doub N N 397 
TYR   C   OXT  sing N N 398 
TYR   CB  CG   sing N N 399 
TYR   CB  HB2  sing N N 400 
TYR   CB  HB3  sing N N 401 
TYR   CG  CD1  doub Y N 402 
TYR   CG  CD2  sing Y N 403 
TYR   CD1 CE1  sing Y N 404 
TYR   CD1 HD1  sing N N 405 
TYR   CD2 CE2  doub Y N 406 
TYR   CD2 HD2  sing N N 407 
TYR   CE1 CZ   doub Y N 408 
TYR   CE1 HE1  sing N N 409 
TYR   CE2 CZ   sing Y N 410 
TYR   CE2 HE2  sing N N 411 
TYR   CZ  OH   sing N N 412 
TYR   OH  HH   sing N N 413 
TYR   OXT HXT  sing N N 414 
VAL   N   CA   sing N N 415 
VAL   N   H    sing N N 416 
VAL   N   H2   sing N N 417 
VAL   CA  C    sing N N 418 
VAL   CA  CB   sing N N 419 
VAL   CA  HA   sing N N 420 
VAL   C   O    doub N N 421 
VAL   C   OXT  sing N N 422 
VAL   CB  CG1  sing N N 423 
VAL   CB  CG2  sing N N 424 
VAL   CB  HB   sing N N 425 
VAL   CG1 HG11 sing N N 426 
VAL   CG1 HG12 sing N N 427 
VAL   CG1 HG13 sing N N 428 
VAL   CG2 HG21 sing N N 429 
VAL   CG2 HG22 sing N N 430 
VAL   CG2 HG23 sing N N 431 
VAL   OXT HXT  sing N N 432 
# 
_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                    7HPD 
_atom_sites.fract_transf_matrix[1][1]   0.023483 
_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]   0.023483 
_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]   0.004618 
_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   ? -20.933 18.889  -7.438  1.00 84.12  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.105 18.010  -7.461  1.00 83.94  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.124 17.231  -8.772  1.00 81.27  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -21.809 17.798  -9.817  1.00 82.33  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.384 18.855  -7.304  1.00 88.01  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.631 18.075  -6.937  1.00 96.57  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.510 17.061  -6.208  1.00 98.27  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.730 18.480  -7.370  1.00 100.42 ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.460 15.937  -8.727  1.00 77.95  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.472 15.115  -9.931  1.00 75.14  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.857 14.861  -10.496 1.00 73.20  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.795 14.662  -9.736  1.00 73.20  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.730 13.791  -9.709  1.00 73.70  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.255 13.967  -9.584  1.00 72.49  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.349 12.464  -9.170  1.00 70.01  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.752 13.213  -8.798  1.00 69.44  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -23.974 14.836  -11.834 1.00 71.06  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.234 14.619  -12.531 1.00 69.82  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.110 13.651  -13.682 1.00 68.20  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -24.025 13.493  -14.239 1.00 68.76  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.868 15.948  -12.978 1.00 70.79  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.079 16.748  -13.993 1.00 73.21  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.162 17.705  -13.589 1.00 74.86  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.349 16.644  -15.354 1.00 74.78  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.473 18.478  -14.512 1.00 76.30  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.653 17.402  -16.290 1.00 75.83  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.709 18.316  -15.864 1.00 77.83  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -23.077 19.151  -16.768 1.00 80.99  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.193 12.903  -13.973 1.00 65.62  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.197 11.921  -15.052 1.00 61.84  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.959 12.450  -16.277 1.00 58.90  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.778 13.378  -16.190 1.00 58.04  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.634 10.507  -14.621 1.00 62.03  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.064 10.481  -14.065 1.00 62.43  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.631 9.897   -13.636 1.00 62.24  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.604 9.044   -13.905 1.00 62.71  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.590 11.961  -17.447 1.00 57.36  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.101 12.452  -18.751 1.00 56.90  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.181 11.197  -19.621 1.00 57.07  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.133 10.582  -19.789 1.00 50.10  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -25.988 13.268  -19.360 1.00 57.27  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.371 14.736  -19.478 1.00 63.32  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.272 15.602  -20.042 1.00 71.93  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.280 15.073  -20.574 1.00 66.85  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.434 16.842  -20.005 1.00 73.68  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.336 10.898  -20.274 1.00 60.66  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.391 9.642   -21.051 1.00 64.07  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.432 9.712   -22.249 1.00 65.30  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.233 10.793  -22.795 1.00 65.50  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.833 9.307   -21.488 1.00 66.42  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.007 7.810   -21.762 1.00 69.32  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.460 7.353   -21.771 1.00 72.09  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.566 5.924   -22.084 1.00 73.54  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.580 5.439   -23.326 1.00 74.24  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.487 6.259   -24.368 1.00 75.73  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.645 4.129   -23.535 1.00 70.21  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.782 8.616   -22.585 1.00 65.59  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.843 8.580   -23.709 1.00 66.89  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.240 7.549   -24.780 1.00 67.40  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.713 7.629   -25.881 1.00 68.49  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.431 8.266   -23.217 1.00 67.83  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.111 6.590   -24.462 1.00 66.04  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.533 5.598   -25.443 1.00 65.35  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.168 4.340   -24.881 1.00 65.05  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.380 4.219   -23.666 1.00 63.25  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.506 3.405   -25.805 1.00 65.17  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.098 2.095   -25.539 1.00 65.77  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -27.995 1.081   -25.396 1.00 66.72  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -26.946 1.218   -26.030 1.00 67.48  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.004 1.635   -26.704 1.00 67.13  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.340 2.334   -26.776 1.00 74.34  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.539 3.312   -26.024 1.00 73.40  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.177 1.942   -27.633 1.00 78.62  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.249 0.028   -24.628 1.00 66.26  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.274 -1.027  -24.467 1.00 66.68  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.649 -2.151  -25.403 1.00 67.76  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.546 -2.939  -25.112 1.00 67.21  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.162 -1.433  -22.997 1.00 66.18  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.552 -0.264  -22.207 1.00 66.67  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.339 -2.699  -22.853 1.00 66.24  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.626 -0.416  -20.758 1.00 67.34  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -26.997 -2.190  -26.570 0.50 68.60  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -26.990 -2.199  -26.564 0.50 68.57  ? 60  THR   A N   1 
ATOM   84   C CA  A THR   A 1 17  ? -27.247 -3.207  -27.588 0.50 69.84  ? 60  THR   A CA  1 
ATOM   85   C CA  B THR   A 1 17  ? -27.302 -3.163  -27.614 0.50 69.78  ? 60  THR   A CA  1 
ATOM   86   C C   A THR   A 1 17  ? -25.949 -3.677  -28.221 0.50 71.22  ? 60  THR   A C   1 
ATOM   87   C C   B THR   A 1 17  ? -26.023 -3.623  -28.328 0.50 71.25  ? 60  THR   A C   1 
ATOM   88   O O   A THR   A 1 17  ? -24.995 -2.911  -28.331 0.50 71.29  ? 60  THR   A O   1 
ATOM   89   O O   B THR   A 1 17  ? -25.123 -2.810  -28.535 0.50 71.38  ? 60  THR   A O   1 
ATOM   90   C CB  A THR   A 1 17  ? -28.136 -2.657  -28.728 0.50 70.84  ? 60  THR   A CB  1 
ATOM   91   C CB  B THR   A 1 17  ? -28.301 -2.484  -28.585 0.50 70.67  ? 60  THR   A CB  1 
ATOM   92   O OG1 A THR   A 1 17  ? -27.508 -1.529  -29.338 0.50 71.58  ? 60  THR   A OG1 1 
ATOM   93   O OG1 B THR   A 1 17  ? -29.456 -2.070  -27.851 0.50 70.97  ? 60  THR   A OG1 1 
ATOM   94   C CG2 A THR   A 1 17  ? -29.554 -2.330  -28.285 0.50 71.15  ? 60  THR   A CG2 1 
ATOM   95   C CG2 B THR   A 1 17  ? -28.726 -3.374  -29.736 0.50 71.14  ? 60  THR   A CG2 1 
ATOM   96   N N   . TRP   A 1 18  ? -25.934 -4.919  -28.693 1.00 72.29  ? 61  TRP   A N   1 
ATOM   97   C CA  . TRP   A 1 18  ? -24.786 -5.452  -29.430 1.00 75.39  ? 61  TRP   A CA  1 
ATOM   98   C C   . TRP   A 1 18  ? -24.939 -4.890  -30.873 1.00 80.14  ? 61  TRP   A C   1 
ATOM   99   O O   . TRP   A 1 18  ? -26.036 -4.937  -31.437 1.00 81.14  ? 61  TRP   A O   1 
ATOM   100  C CB  . TRP   A 1 18  ? -24.863 -6.986  -29.478 1.00 74.62  ? 61  TRP   A CB  1 
ATOM   101  C CG  . TRP   A 1 18  ? -23.790 -7.659  -30.291 1.00 75.38  ? 61  TRP   A CG  1 
ATOM   102  C CD1 . TRP   A 1 18  ? -23.846 -7.987  -31.619 1.00 76.53  ? 61  TRP   A CD1 1 
ATOM   103  C CD2 . TRP   A 1 18  ? -22.569 -8.225  -29.789 1.00 75.20  ? 61  TRP   A CD2 1 
ATOM   104  N NE1 . TRP   A 1 18  ? -22.704 -8.661  -31.986 1.00 76.84  ? 61  TRP   A NE1 1 
ATOM   105  C CE2 . TRP   A 1 18  ? -21.901 -8.818  -30.882 1.00 76.07  ? 61  TRP   A CE2 1 
ATOM   106  C CE3 . TRP   A 1 18  ? -21.952 -8.249  -28.530 1.00 75.37  ? 61  TRP   A CE3 1 
ATOM   107  C CZ2 . TRP   A 1 18  ? -20.663 -9.454  -30.743 1.00 76.28  ? 61  TRP   A CZ2 1 
ATOM   108  C CZ3 . TRP   A 1 18  ? -20.730 -8.882  -28.394 1.00 75.99  ? 61  TRP   A CZ3 1 
ATOM   109  C CH2 . TRP   A 1 18  ? -20.094 -9.466  -29.491 1.00 76.03  ? 61  TRP   A CH2 1 
ATOM   110  N N   . GLU   A 1 19  ? -23.873 -4.323  -31.445 1.00 82.73  ? 62  GLU   A N   1 
ATOM   111  C CA  . GLU   A 1 19  ? -23.927 -3.795  -32.805 1.00 85.86  ? 62  GLU   A CA  1 
ATOM   112  C C   . GLU   A 1 19  ? -23.271 -4.789  -33.749 1.00 89.06  ? 62  GLU   A C   1 
ATOM   113  O O   . GLU   A 1 19  ? -22.074 -5.049  -33.628 1.00 88.67  ? 62  GLU   A O   1 
ATOM   114  C CB  . GLU   A 1 19  ? -23.210 -2.437  -32.914 1.00 88.85  ? 62  GLU   A CB  1 
ATOM   115  C CG  . GLU   A 1 19  ? -23.200 -1.890  -34.338 1.00 97.07  ? 62  GLU   A CG  1 
ATOM   116  C CD  . GLU   A 1 19  ? -22.120 -0.872  -34.651 1.00 106.52 ? 62  GLU   A CD  1 
ATOM   117  O OE1 . GLU   A 1 19  ? -21.514 -0.337  -33.695 1.00 110.00 ? 62  GLU   A OE1 1 
ATOM   118  O OE2 . GLU   A 1 19  ? -21.882 -0.607  -35.852 1.00 109.44 ? 62  GLU   A OE2 1 
ATOM   119  N N   . LYS   A 1 20  ? -24.024 -5.302  -34.730 1.00 91.92  ? 63  LYS   A N   1 
ATOM   120  C CA  . LYS   A 1 20  ? -23.448 -6.208  -35.726 1.00 95.08  ? 63  LYS   A CA  1 
ATOM   121  C C   . LYS   A 1 20  ? -22.439 -5.424  -36.574 1.00 97.46  ? 63  LYS   A C   1 
ATOM   122  O O   . LYS   A 1 20  ? -22.632 -4.228  -36.788 1.00 98.11  ? 63  LYS   A O   1 
ATOM   123  C CB  . LYS   A 1 20  ? -24.546 -6.812  -36.615 1.00 98.69  ? 63  LYS   A CB  1 
ATOM   124  C CG  . LYS   A 1 20  ? -25.095 -8.142  -36.108 1.00 104.46 ? 63  LYS   A CG  1 
ATOM   125  C CD  . LYS   A 1 20  ? -26.308 -8.607  -36.923 1.00 109.45 ? 63  LYS   A CD  1 
ATOM   126  C CE  . LYS   A 1 20  ? -27.587 -7.955  -36.438 1.00 114.38 ? 63  LYS   A CE  1 
ATOM   127  N NZ  . LYS   A 1 20  ? -28.736 -8.237  -37.348 1.00 117.68 ? 63  LYS   A NZ  1 
ATOM   128  N N   . ASP   A 1 21  ? -21.344 -6.062  -36.990 1.00 99.17  ? 64  ASP   A N   1 
ATOM   129  C CA  . ASP   A 1 21  ? -20.335 -5.383  -37.810 1.00 101.33 ? 64  ASP   A CA  1 
ATOM   130  C C   . ASP   A 1 21  ? -19.748 -4.136  -37.104 1.00 101.50 ? 64  ASP   A C   1 
ATOM   131  O O   . ASP   A 1 21  ? -19.624 -3.081  -37.723 1.00 101.92 ? 64  ASP   A O   1 
ATOM   132  C CB  . ASP   A 1 21  ? -20.907 -5.005  -39.200 1.00 105.78 ? 64  ASP   A CB  1 
ATOM   133  C CG  . ASP   A 1 21  ? -21.611 -6.129  -39.942 1.00 115.52 ? 64  ASP   A CG  1 
ATOM   134  O OD1 . ASP   A 1 21  ? -21.013 -7.217  -40.078 1.00 118.02 ? 64  ASP   A OD1 1 
ATOM   135  O OD2 . ASP   A 1 21  ? -22.752 -5.910  -40.410 1.00 119.26 ? 64  ASP   A OD2 1 
ATOM   136  N N   . ALA   A 1 22  ? -19.397 -4.252  -35.814 1.00 100.93 ? 65  ALA   A N   1 
ATOM   137  C CA  . ALA   A 1 22  ? -18.774 -3.136  -35.095 1.00 100.73 ? 65  ALA   A CA  1 
ATOM   138  C C   . ALA   A 1 22  ? -17.257 -3.109  -35.424 1.00 100.48 ? 65  ALA   A C   1 
ATOM   139  O O   . ALA   A 1 22  ? -16.748 -4.059  -36.025 1.00 100.29 ? 65  ALA   A O   1 
ATOM   140  C CB  . ALA   A 1 22  ? -19.006 -3.291  -33.591 1.00 101.02 ? 65  ALA   A CB  1 
ATOM   141  N N   . GLU   A 1 23  ? -16.540 -2.024  -35.078 1.00 100.57 ? 66  GLU   A N   1 
ATOM   142  C CA  . GLU   A 1 23  ? -15.093 -1.957  -35.314 1.00 101.19 ? 66  GLU   A CA  1 
ATOM   143  C C   . GLU   A 1 23  ? -14.414 -2.992  -34.398 1.00 99.88  ? 66  GLU   A C   1 
ATOM   144  O O   . GLU   A 1 23  ? -14.613 -2.939  -33.185 1.00 99.42  ? 66  GLU   A O   1 
ATOM   145  C CB  . GLU   A 1 23  ? -14.563 -0.548  -34.993 1.00 105.67 ? 66  GLU   A CB  1 
ATOM   146  C CG  . GLU   A 1 23  ? -13.045 -0.446  -34.930 1.00 113.56 ? 66  GLU   A CG  1 
ATOM   147  C CD  . GLU   A 1 23  ? -12.530 0.942   -34.604 1.00 123.04 ? 66  GLU   A CD  1 
ATOM   148  O OE1 . GLU   A 1 23  ? -13.199 1.659   -33.823 1.00 124.31 ? 66  GLU   A OE1 1 
ATOM   149  O OE2 . GLU   A 1 23  ? -11.460 1.316   -35.138 1.00 125.72 ? 66  GLU   A OE2 1 
ATOM   150  N N   . VAL   A 1 24  ? -13.653 -3.944  -34.974 1.00 98.59  ? 67  VAL   A N   1 
ATOM   151  C CA  . VAL   A 1 24  ? -12.992 -4.978  -34.168 1.00 97.64  ? 67  VAL   A CA  1 
ATOM   152  C C   . VAL   A 1 24  ? -11.515 -4.634  -33.978 1.00 95.80  ? 67  VAL   A C   1 
ATOM   153  O O   . VAL   A 1 24  ? -10.799 -4.490  -34.960 1.00 96.41  ? 67  VAL   A O   1 
ATOM   154  C CB  . VAL   A 1 24  ? -13.169 -6.404  -34.747 1.00 98.94  ? 67  VAL   A CB  1 
ATOM   155  C CG1 . VAL   A 1 24  ? -12.755 -7.448  -33.724 1.00 99.61  ? 67  VAL   A CG1 1 
ATOM   156  C CG2 . VAL   A 1 24  ? -14.605 -6.652  -35.204 1.00 99.61  ? 67  VAL   A CG2 1 
ATOM   157  N N   . THR   A 1 25  ? -11.059 -4.471  -32.721 1.00 93.70  ? 68  THR   A N   1 
ATOM   158  C CA  . THR   A 1 25  ? -9.673  -4.096  -32.406 1.00 92.16  ? 68  THR   A CA  1 
ATOM   159  C C   . THR   A 1 25  ? -9.239  -4.637  -31.016 1.00 90.32  ? 68  THR   A C   1 
ATOM   160  O O   . THR   A 1 25  ? -10.028 -5.287  -30.340 1.00 89.63  ? 68  THR   A O   1 
ATOM   161  C CB  . THR   A 1 25  ? -9.490  -2.561  -32.573 1.00 93.92  ? 68  THR   A CB  1 
ATOM   162  O OG1 . THR   A 1 25  ? -8.099  -2.246  -32.689 1.00 95.62  ? 68  THR   A OG1 1 
ATOM   163  C CG2 . THR   A 1 25  ? -10.116 -1.770  -31.458 1.00 93.94  ? 68  THR   A CG2 1 
ATOM   164  N N   . GLY   A 1 26  ? -7.982  -4.426  -30.636 1.00 89.13  ? 69  GLY   A N   1 
ATOM   165  C CA  . GLY   A 1 26  ? -7.472  -4.873  -29.351 1.00 88.47  ? 69  GLY   A CA  1 
ATOM   166  C C   . GLY   A 1 26  ? -7.029  -6.318  -29.328 1.00 87.35  ? 69  GLY   A C   1 
ATOM   167  O O   . GLY   A 1 26  ? -7.623  -7.178  -29.985 1.00 87.24  ? 69  GLY   A O   1 
ATOM   168  N N   . ASN   A 1 27  ? -5.991  -6.588  -28.539 1.00 86.11  ? 70  ASN   A N   1 
ATOM   169  C CA  . ASN   A 1 27  ? -5.443  -7.927  -28.387 1.00 85.35  ? 70  ASN   A CA  1 
ATOM   170  C C   . ASN   A 1 27  ? -5.987  -8.635  -27.091 1.00 82.99  ? 70  ASN   A C   1 
ATOM   171  O O   . ASN   A 1 27  ? -6.877  -8.090  -26.437 1.00 82.68  ? 70  ASN   A O   1 
ATOM   172  C CB  . ASN   A 1 27  ? -3.902  -7.891  -28.498 1.00 87.72  ? 70  ASN   A CB  1 
ATOM   173  C CG  . ASN   A 1 27  ? -3.169  -7.130  -27.413 1.00 92.19  ? 70  ASN   A CG  1 
ATOM   174  O OD1 . ASN   A 1 27  ? -3.710  -6.241  -26.759 1.00 92.83  ? 70  ASN   A OD1 1 
ATOM   175  N ND2 . ASN   A 1 27  ? -1.887  -7.452  -27.226 1.00 93.80  ? 70  ASN   A ND2 1 
ATOM   176  N N   . SER   A 1 28  ? -5.539  -9.876  -26.779 1.00 81.17  ? 71  SER   A N   1 
ATOM   177  C CA  . SER   A 1 28  ? -6.031  -10.641 -25.614 1.00 80.19  ? 71  SER   A CA  1 
ATOM   178  C C   . SER   A 1 28  ? -4.869  -11.130 -24.740 1.00 78.66  ? 71  SER   A C   1 
ATOM   179  O O   . SER   A 1 28  ? -4.540  -12.322 -24.734 1.00 78.51  ? 71  SER   A O   1 
ATOM   180  C CB  . SER   A 1 28  ? -6.874  -11.840 -26.061 1.00 81.75  ? 71  SER   A CB  1 
ATOM   181  O OG  . SER   A 1 28  ? -7.422  -11.728 -27.364 1.00 84.15  ? 71  SER   A OG  1 
ATOM   182  N N   . PRO   A 1 29  ? -4.199  -10.223 -24.025 1.00 77.60  ? 72  PRO   A N   1 
ATOM   183  C CA  . PRO   A 1 29  ? -3.028  -10.647 -23.242 1.00 77.39  ? 72  PRO   A CA  1 
ATOM   184  C C   . PRO   A 1 29  ? -3.371  -11.308 -21.913 1.00 76.77  ? 72  PRO   A C   1 
ATOM   185  O O   . PRO   A 1 29  ? -4.374  -10.970 -21.278 1.00 76.72  ? 72  PRO   A O   1 
ATOM   186  C CB  . PRO   A 1 29  ? -2.252  -9.350  -23.057 1.00 78.60  ? 72  PRO   A CB  1 
ATOM   187  C CG  . PRO   A 1 29  ? -3.366  -8.291  -22.971 1.00 78.94  ? 72  PRO   A CG  1 
ATOM   188  C CD  . PRO   A 1 29  ? -4.439  -8.770  -23.918 1.00 76.99  ? 72  PRO   A CD  1 
ATOM   189  N N   . ARG   A 1 30  ? -2.535  -12.270 -21.504 1.00 76.24  ? 73  ARG   A N   1 
ATOM   190  C CA  . ARG   A 1 30  ? -2.688  -12.979 -20.233 1.00 76.23  ? 73  ARG   A CA  1 
ATOM   191  C C   . ARG   A 1 30  ? -1.672  -12.381 -19.275 1.00 74.17  ? 73  ARG   A C   1 
ATOM   192  O O   . ARG   A 1 30  ? -0.473  -12.527 -19.485 1.00 73.32  ? 73  ARG   A O   1 
ATOM   193  C CB  . ARG   A 1 30  ? -2.459  -14.487 -20.421 1.00 79.12  ? 73  ARG   A CB  1 
ATOM   194  C CG  . ARG   A 1 30  ? -3.378  -15.038 -21.503 1.00 84.94  ? 73  ARG   A CG  1 
ATOM   195  C CD  . ARG   A 1 30  ? -3.444  -16.555 -21.593 1.00 90.50  ? 73  ARG   A CD  1 
ATOM   196  N NE  . ARG   A 1 30  ? -4.611  -16.920 -22.396 1.00 95.25  ? 73  ARG   A NE  1 
ATOM   197  C CZ  . ARG   A 1 30  ? -5.061  -18.158 -22.563 1.00 98.14  ? 73  ARG   A CZ  1 
ATOM   198  N NH1 . ARG   A 1 30  ? -4.437  -19.183 -21.988 1.00 97.44  ? 73  ARG   A NH1 1 
ATOM   199  N NH2 . ARG   A 1 30  ? -6.138  -18.383 -23.307 1.00 97.90  ? 73  ARG   A NH2 1 
ATOM   200  N N   . LEU   A 1 31  ? -2.155  -11.635 -18.281 1.00 72.74  ? 74  LEU   A N   1 
ATOM   201  C CA  . LEU   A 1 31  ? -1.294  -10.908 -17.366 1.00 72.32  ? 74  LEU   A CA  1 
ATOM   202  C C   . LEU   A 1 31  ? -1.444  -11.390 -15.936 1.00 71.90  ? 74  LEU   A C   1 
ATOM   203  O O   . LEU   A 1 31  ? -2.570  -11.478 -15.453 1.00 72.25  ? 74  LEU   A O   1 
ATOM   204  C CB  . LEU   A 1 31  ? -1.681  -9.423  -17.396 1.00 72.41  ? 74  LEU   A CB  1 
ATOM   205  C CG  . LEU   A 1 31  ? -1.706  -8.755  -18.763 1.00 73.93  ? 74  LEU   A CG  1 
ATOM   206  C CD1 . LEU   A 1 31  ? -2.477  -7.439  -18.712 1.00 74.08  ? 74  LEU   A CD1 1 
ATOM   207  C CD2 . LEU   A 1 31  ? -0.286  -8.593  -19.323 1.00 74.35  ? 74  LEU   A CD2 1 
ATOM   208  N N   . ASP   A 1 32  ? -0.322  -11.619 -15.238 1.00 70.84  ? 75  ASP   A N   1 
ATOM   209  C CA  . ASP   A 1 32  ? -0.341  -11.977 -13.827 1.00 71.07  ? 75  ASP   A CA  1 
ATOM   210  C C   . ASP   A 1 32  ? -0.517  -10.681 -13.037 1.00 68.97  ? 75  ASP   A C   1 
ATOM   211  O O   . ASP   A 1 32  ? 0.356   -9.814  -13.102 1.00 69.88  ? 75  ASP   A O   1 
ATOM   212  C CB  . ASP   A 1 32  ? 0.984   -12.628 -13.422 1.00 75.69  ? 75  ASP   A CB  1 
ATOM   213  C CG  . ASP   A 1 32  ? 1.116   -14.078 -13.829 1.00 85.45  ? 75  ASP   A CG  1 
ATOM   214  O OD1 . ASP   A 1 32  ? 0.074   -14.740 -14.009 1.00 87.14  ? 75  ASP   A OD1 1 
ATOM   215  O OD2 . ASP   A 1 32  ? 2.266   -14.556 -13.950 1.00 90.24  ? 75  ASP   A OD2 1 
ATOM   216  N N   . VAL   A 1 33  ? -1.645  -10.526 -12.317 1.00 65.72  ? 76  VAL   A N   1 
ATOM   217  C CA  . VAL   A 1 33  ? -1.918  -9.309  -11.558 1.00 63.69  ? 76  VAL   A CA  1 
ATOM   218  C C   . VAL   A 1 33  ? -2.226  -9.580  -10.058 1.00 63.32  ? 76  VAL   A C   1 
ATOM   219  O O   . VAL   A 1 33  ? -2.477  -10.721 -9.641  1.00 63.58  ? 76  VAL   A O   1 
ATOM   220  C CB  . VAL   A 1 33  ? -3.049  -8.443  -12.218 1.00 62.47  ? 76  VAL   A CB  1 
ATOM   221  C CG1 . VAL   A 1 33  ? -2.817  -8.229  -13.718 1.00 62.44  ? 76  VAL   A CG1 1 
ATOM   222  C CG2 . VAL   A 1 33  ? -4.412  -9.056  -11.963 1.00 62.06  ? 76  VAL   A CG2 1 
ATOM   223  N N   . ALA   A 1 34  ? -2.147  -8.517  -9.250  1.00 62.45  ? 77  ALA   A N   1 
ATOM   224  C CA  . ALA   A 1 34  ? -2.466  -8.537  -7.826  1.00 62.42  ? 77  ALA   A CA  1 
ATOM   225  C C   . ALA   A 1 34  ? -3.491  -7.431  -7.573  1.00 61.93  ? 77  ALA   A C   1 
ATOM   226  O O   . ALA   A 1 34  ? -3.497  -6.427  -8.283  1.00 62.04  ? 77  ALA   A O   1 
ATOM   227  C CB  . ALA   A 1 34  ? -1.215  -8.327  -6.984  1.00 62.88  ? 77  ALA   A CB  1 
ATOM   228  N N   . LEU   A 1 35  ? -4.408  -7.644  -6.631  1.00 61.21  ? 78  LEU   A N   1 
ATOM   229  C CA  . LEU   A 1 35  ? -5.448  -6.660  -6.341  1.00 60.84  ? 78  LEU   A CA  1 
ATOM   230  C C   . LEU   A 1 35  ? -5.291  -6.291  -4.874  1.00 60.71  ? 78  LEU   A C   1 
ATOM   231  O O   . LEU   A 1 35  ? -5.354  -7.175  -4.011  1.00 61.46  ? 78  LEU   A O   1 
ATOM   232  C CB  . LEU   A 1 35  ? -6.837  -7.252  -6.634  1.00 60.59  ? 78  LEU   A CB  1 
ATOM   233  C CG  . LEU   A 1 35  ? -8.032  -6.395  -6.197  1.00 61.72  ? 78  LEU   A CG  1 
ATOM   234  C CD1 . LEU   A 1 35  ? -8.099  -5.101  -6.970  1.00 61.49  ? 78  LEU   A CD1 1 
ATOM   235  C CD2 . LEU   A 1 35  ? -9.323  -7.160  -6.324  1.00 62.34  ? 78  LEU   A CD2 1 
ATOM   236  N N   . ASP   A 1 36  ? -4.976  -5.022  -4.593  1.00 59.48  ? 79  ASP   A N   1 
ATOM   237  C CA  . ASP   A 1 36  ? -4.744  -4.601  -3.220  1.00 59.88  ? 79  ASP   A CA  1 
ATOM   238  C C   . ASP   A 1 36  ? -6.075  -4.252  -2.475  1.00 59.31  ? 79  ASP   A C   1 
ATOM   239  O O   . ASP   A 1 36  ? -7.155  -4.290  -3.072  1.00 58.65  ? 79  ASP   A O   1 
ATOM   240  C CB  . ASP   A 1 36  ? -3.680  -3.476  -3.164  1.00 61.68  ? 79  ASP   A CB  1 
ATOM   241  C CG  . ASP   A 1 36  ? -4.129  -2.099  -3.609  1.00 65.29  ? 79  ASP   A CG  1 
ATOM   242  O OD1 . ASP   A 1 36  ? -5.323  -1.941  -3.938  1.00 65.85  ? 79  ASP   A OD1 1 
ATOM   243  O OD2 . ASP   A 1 36  ? -3.287  -1.175  -3.616  1.00 67.12  ? 79  ASP   A OD2 1 
ATOM   244  N N   . GLU   A 1 37  ? -5.988  -3.935  -1.179  1.00 58.98  ? 80  GLU   A N   1 
ATOM   245  C CA  . GLU   A 1 37  ? -7.158  -3.597  -0.384  1.00 59.47  ? 80  GLU   A CA  1 
ATOM   246  C C   . GLU   A 1 37  ? -7.898  -2.341  -0.895  1.00 59.48  ? 80  GLU   A C   1 
ATOM   247  O O   . GLU   A 1 37  ? -9.108  -2.237  -0.727  1.00 59.49  ? 80  GLU   A O   1 
ATOM   248  C CB  . GLU   A 1 37  ? -6.775  -3.473  1.099   1.00 61.71  ? 80  GLU   A CB  1 
ATOM   249  C CG  . GLU   A 1 37  ? -7.970  -3.564  2.034   1.00 68.31  ? 80  GLU   A CG  1 
ATOM   250  C CD  . GLU   A 1 37  ? -7.632  -3.371  3.497   1.00 75.77  ? 80  GLU   A CD  1 
ATOM   251  O OE1 . GLU   A 1 37  ? -7.635  -2.210  3.963   1.00 75.89  ? 80  GLU   A OE1 1 
ATOM   252  O OE2 . GLU   A 1 37  ? -7.352  -4.381  4.178   1.00 79.75  ? 80  GLU   A OE2 1 
ATOM   253  N N   . SER   A 1 38  ? -7.187  -1.410  -1.555  1.00 59.09  ? 81  SER   A N   1 
ATOM   254  C CA  . SER   A 1 38  ? -7.812  -0.191  -2.079  1.00 58.72  ? 81  SER   A CA  1 
ATOM   255  C C   . SER   A 1 38  ? -8.444  -0.344  -3.479  1.00 57.55  ? 81  SER   A C   1 
ATOM   256  O O   . SER   A 1 38  ? -8.880  0.649   -4.074  1.00 57.73  ? 81  SER   A O   1 
ATOM   257  C CB  . SER   A 1 38  ? -6.821  0.968   -2.066  1.00 60.59  ? 81  SER   A CB  1 
ATOM   258  O OG  . SER   A 1 38  ? -6.243  1.132   -0.780  1.00 64.67  ? 81  SER   A OG  1 
ATOM   259  N N   . GLY   A 1 39  ? -8.505  -1.568  -3.993  1.00 56.70  ? 82  GLY   A N   1 
ATOM   260  C CA  . GLY   A 1 39  ? -9.102  -1.816  -5.301  1.00 56.59  ? 82  GLY   A CA  1 
ATOM   261  C C   . GLY   A 1 39  ? -8.196  -1.502  -6.480  1.00 56.52  ? 82  GLY   A C   1 
ATOM   262  O O   . GLY   A 1 39  ? -8.672  -1.412  -7.607  1.00 55.36  ? 82  GLY   A O   1 
ATOM   263  N N   . ASP   A 1 40  ? -6.875  -1.378  -6.244  1.00 57.23  ? 83  ASP   A N   1 
ATOM   264  C CA  . ASP   A 1 40  ? -5.919  -1.104  -7.313  1.00 58.29  ? 83  ASP   A CA  1 
ATOM   265  C C   . ASP   A 1 40  ? -5.227  -2.377  -7.816  1.00 59.16  ? 83  ASP   A C   1 
ATOM   266  O O   . ASP   A 1 40  ? -4.623  -3.125  -7.033  1.00 58.87  ? 83  ASP   A O   1 
ATOM   267  C CB  . ASP   A 1 40  ? -4.851  -0.105  -6.843  1.00 60.37  ? 83  ASP   A CB  1 
ATOM   268  C CG  . ASP   A 1 40  ? -5.423  1.238   -6.451  1.00 66.58  ? 83  ASP   A CG  1 
ATOM   269  O OD1 . ASP   A 1 40  ? -6.247  1.776   -7.217  1.00 67.11  ? 83  ASP   A OD1 1 
ATOM   270  O OD2 . ASP   A 1 40  ? -5.048  1.751   -5.379  1.00 70.28  ? 83  ASP   A OD2 1 
ATOM   271  N N   . PHE   A 1 41  ? -5.291  -2.609  -9.126  1.00 59.37  ? 84  PHE   A N   1 
ATOM   272  C CA  . PHE   A 1 41  ? -4.580  -3.724  -9.730  1.00 59.97  ? 84  PHE   A CA  1 
ATOM   273  C C   . PHE   A 1 41  ? -3.136  -3.303  -9.980  1.00 62.71  ? 84  PHE   A C   1 
ATOM   274  O O   . PHE   A 1 41  ? -2.853  -2.132  -10.266 1.00 62.71  ? 84  PHE   A O   1 
ATOM   275  C CB  . PHE   A 1 41  ? -5.208  -4.137  -11.066 1.00 58.40  ? 84  PHE   A CB  1 
ATOM   276  C CG  . PHE   A 1 41  ? -6.502  -4.898  -10.958 1.00 57.22  ? 84  PHE   A CG  1 
ATOM   277  C CD1 . PHE   A 1 41  ? -6.516  -6.215  -10.535 1.00 57.26  ? 84  PHE   A CD1 1 
ATOM   278  C CD2 . PHE   A 1 41  ? -7.705  -4.303  -11.298 1.00 56.88  ? 84  PHE   A CD2 1 
ATOM   279  C CE1 . PHE   A 1 41  ? -7.717  -6.912  -10.445 1.00 57.49  ? 84  PHE   A CE1 1 
ATOM   280  C CE2 . PHE   A 1 41  ? -8.894  -5.006  -11.221 1.00 56.62  ? 84  PHE   A CE2 1 
ATOM   281  C CZ  . PHE   A 1 41  ? -8.895  -6.301  -10.806 1.00 56.46  ? 84  PHE   A CZ  1 
ATOM   282  N N   . SER   A 1 42  ? -2.226  -4.262  -9.887  1.00 64.63  ? 85  SER   A N   1 
ATOM   283  C CA  . SER   A 1 42  ? -0.823  -4.036  -10.202 1.00 67.50  ? 85  SER   A CA  1 
ATOM   284  C C   . SER   A 1 42  ? -0.278  -5.253  -10.941 1.00 70.61  ? 85  SER   A C   1 
ATOM   285  O O   . SER   A 1 42  ? -0.865  -6.333  -10.865 1.00 70.20  ? 85  SER   A O   1 
ATOM   286  C CB  . SER   A 1 42  ? -0.004  -3.753  -8.945  1.00 69.10  ? 85  SER   A CB  1 
ATOM   287  O OG  . SER   A 1 42  ? -0.152  -4.773  -7.970  1.00 71.41  ? 85  SER   A OG  1 
ATOM   288  N N   . LEU   A 1 43  ? 0.822   -5.084  -11.681 1.00 73.56  ? 86  LEU   A N   1 
ATOM   289  C CA  . LEU   A 1 43  ? 1.424   -6.203  -12.402 1.00 76.79  ? 86  LEU   A CA  1 
ATOM   290  C C   . LEU   A 1 43  ? 2.371   -6.967  -11.503 1.00 80.44  ? 86  LEU   A C   1 
ATOM   291  O O   . LEU   A 1 43  ? 3.196   -6.362  -10.818 1.00 80.35  ? 86  LEU   A O   1 
ATOM   292  C CB  . LEU   A 1 43  ? 2.216   -5.717  -13.622 1.00 77.12  ? 86  LEU   A CB  1 
ATOM   293  C CG  . LEU   A 1 43  ? 1.479   -5.561  -14.944 1.00 78.91  ? 86  LEU   A CG  1 
ATOM   294  C CD1 . LEU   A 1 43  ? 2.471   -5.254  -16.054 1.00 79.42  ? 86  LEU   A CD1 1 
ATOM   295  C CD2 . LEU   A 1 43  ? 0.719   -6.831  -15.315 1.00 79.75  ? 86  LEU   A CD2 1 
ATOM   296  N N   . VAL   A 1 44  ? 2.288   -8.301  -11.543 1.00 83.40  ? 87  VAL   A N   1 
ATOM   297  C CA  . VAL   A 1 44  ? 3.217   -9.190  -10.846 1.00 86.59  ? 87  VAL   A CA  1 
ATOM   298  C C   . VAL   A 1 44  ? 4.038   -9.749  -11.983 1.00 90.22  ? 87  VAL   A C   1 
ATOM   299  O O   . VAL   A 1 44  ? 3.472   -10.409 -12.861 1.00 90.92  ? 87  VAL   A O   1 
ATOM   300  C CB  . VAL   A 1 44  ? 2.505   -10.336 -10.094 1.00 87.20  ? 87  VAL   A CB  1 
ATOM   301  C CG1 . VAL   A 1 44  ? 3.524   -11.281 -9.459  1.00 87.58  ? 87  VAL   A CG1 1 
ATOM   302  C CG2 . VAL   A 1 44  ? 1.533   -9.793  -9.054  1.00 87.48  ? 87  VAL   A CG2 1 
ATOM   303  N N   . GLU   A 1 45  ? 5.337   -9.446  -12.026 1.00 92.47  ? 88  GLU   A N   1 
ATOM   304  C CA  . GLU   A 1 45  ? 6.144   -9.900  -13.157 1.00 95.06  ? 88  GLU   A CA  1 
ATOM   305  C C   . GLU   A 1 45  ? 7.170   -10.954 -12.812 1.00 96.32  ? 88  GLU   A C   1 
ATOM   306  O O   . GLU   A 1 45  ? 7.315   -11.895 -13.591 1.00 97.17  ? 88  GLU   A O   1 
ATOM   307  C CB  . GLU   A 1 45  ? 6.785   -8.720  -13.882 1.00 98.82  ? 88  GLU   A CB  1 
ATOM   308  C CG  . GLU   A 1 45  ? 5.794   -7.985  -14.772 1.00 103.66 ? 88  GLU   A CG  1 
ATOM   309  C CD  . GLU   A 1 45  ? 6.194   -7.922  -16.235 1.00 111.61 ? 88  GLU   A CD  1 
ATOM   310  O OE1 . GLU   A 1 45  ? 7.174   -8.601  -16.624 1.00 112.70 ? 88  GLU   A OE1 1 
ATOM   311  O OE2 . GLU   A 1 45  ? 5.523   -7.186  -16.995 1.00 114.41 ? 88  GLU   A OE2 1 
ATOM   312  N N   . GLY   B 2 7   ? -36.480 11.885  -11.673 1.00 74.95  ? 16  GLY   B N   1 
ATOM   313  C CA  . GLY   B 2 7   ? -35.446 11.925  -12.700 1.00 75.51  ? 16  GLY   B CA  1 
ATOM   314  C C   . GLY   B 2 7   ? -35.649 10.922  -13.823 1.00 75.56  ? 16  GLY   B C   1 
ATOM   315  O O   . GLY   B 2 7   ? -36.631 10.170  -13.819 1.00 76.23  ? 16  GLY   B O   1 
ATOM   316  N N   . GLU   B 2 8   ? -34.728 10.903  -14.807 1.00 74.35  ? 17  GLU   B N   1 
ATOM   317  C CA  . GLU   B 2 8   ? -34.824 9.950   -15.912 1.00 73.52  ? 17  GLU   B CA  1 
ATOM   318  C C   . GLU   B 2 8   ? -34.371 8.574   -15.414 1.00 71.95  ? 17  GLU   B C   1 
ATOM   319  O O   . GLU   B 2 8   ? -33.254 8.434   -14.911 1.00 71.96  ? 17  GLU   B O   1 
ATOM   320  C CB  . GLU   B 2 8   ? -33.989 10.407  -17.121 1.00 75.48  ? 17  GLU   B CB  1 
ATOM   321  C CG  . GLU   B 2 8   ? -34.131 9.478   -18.312 1.00 78.89  ? 17  GLU   B CG  1 
ATOM   322  C CD  . GLU   B 2 8   ? -33.410 9.935   -19.563 1.00 83.51  ? 17  GLU   B CD  1 
ATOM   323  O OE1 . GLU   B 2 8   ? -32.447 10.730  -19.442 1.00 82.85  ? 17  GLU   B OE1 1 
ATOM   324  O OE2 . GLU   B 2 8   ? -33.824 9.513   -20.669 1.00 85.87  ? 17  GLU   B OE2 1 
ATOM   325  N N   A THR   B 2 9   ? -35.247 7.575   -15.530 0.50 71.23  ? 18  THR   B N   1 
ATOM   326  N N   B THR   B 2 9   ? -35.243 7.566   -15.519 0.50 71.17  ? 18  THR   B N   1 
ATOM   327  C CA  A THR   B 2 9   ? -34.954 6.221   -15.042 0.50 70.99  ? 18  THR   B CA  1 
ATOM   328  C CA  B THR   B 2 9   ? -34.903 6.218   -15.056 0.50 70.83  ? 18  THR   B CA  1 
ATOM   329  C C   A THR   B 2 9   ? -34.931 5.158   -16.152 0.50 69.93  ? 18  THR   B C   1 
ATOM   330  C C   B THR   B 2 9   ? -34.927 5.158   -16.153 0.50 69.87  ? 18  THR   B C   1 
ATOM   331  O O   A THR   B 2 9   ? -34.862 3.970   -15.843 0.50 70.48  ? 18  THR   B O   1 
ATOM   332  O O   B THR   B 2 9   ? -34.873 3.971   -15.838 0.50 70.39  ? 18  THR   B O   1 
ATOM   333  C CB  A THR   B 2 9   ? -35.925 5.791   -13.896 0.50 72.69  ? 18  THR   B CB  1 
ATOM   334  C CB  B THR   B 2 9   ? -35.784 5.805   -13.873 0.50 72.36  ? 18  THR   B CB  1 
ATOM   335  O OG1 A THR   B 2 9   ? -36.702 6.891   -13.386 0.50 73.89  ? 18  THR   B OG1 1 
ATOM   336  O OG1 B THR   B 2 9   ? -37.159 6.033   -14.209 0.50 73.36  ? 18  THR   B OG1 1 
ATOM   337  C CG2 A THR   B 2 9   ? -35.207 5.079   -12.752 0.50 73.07  ? 18  THR   B CG2 1 
ATOM   338  C CG2 B THR   B 2 9   ? -35.408 6.538   -12.584 0.50 72.73  ? 18  THR   B CG2 1 
ATOM   339  N N   . THR   B 2 10  ? -34.986 5.564   -17.429 1.00 68.42  ? 19  THR   B N   1 
ATOM   340  C CA  . THR   B 2 10  ? -34.990 4.618   -18.541 1.00 66.12  ? 19  THR   B CA  1 
ATOM   341  C C   . THR   B 2 10  ? -33.682 3.814   -18.558 1.00 63.13  ? 19  THR   B C   1 
ATOM   342  O O   . THR   B 2 10  ? -32.620 4.380   -18.302 1.00 61.81  ? 19  THR   B O   1 
ATOM   343  C CB  . THR   B 2 10  ? -35.158 5.384   -19.885 1.00 67.32  ? 19  THR   B CB  1 
ATOM   344  O OG1 . THR   B 2 10  ? -36.240 6.315   -19.797 1.00 68.60  ? 19  THR   B OG1 1 
ATOM   345  C CG2 . THR   B 2 10  ? -35.389 4.457   -21.071 1.00 67.61  ? 19  THR   B CG2 1 
ATOM   346  N N   . ASP   B 2 11  ? -33.766 2.503   -18.857 1.00 61.93  ? 20  ASP   B N   1 
ATOM   347  C CA  . ASP   B 2 11  ? -32.610 1.620   -19.003 1.00 62.12  ? 20  ASP   B CA  1 
ATOM   348  C C   . ASP   B 2 11  ? -31.669 2.185   -20.074 1.00 61.80  ? 20  ASP   B C   1 
ATOM   349  O O   . ASP   B 2 11  ? -32.147 2.796   -21.034 1.00 62.63  ? 20  ASP   B O   1 
ATOM   350  C CB  . ASP   B 2 11  ? -33.054 0.219   -19.461 1.00 64.07  ? 20  ASP   B CB  1 
ATOM   351  C CG  . ASP   B 2 11  ? -33.505 -0.724  -18.369 1.00 68.64  ? 20  ASP   B CG  1 
ATOM   352  O OD1 . ASP   B 2 11  ? -33.695 -0.262  -17.235 1.00 67.28  ? 20  ASP   B OD1 1 
ATOM   353  O OD2 . ASP   B 2 11  ? -33.669 -1.941  -18.660 1.00 72.36  ? 20  ASP   B OD2 1 
ATOM   354  N N   . GLY   B 2 12  ? -30.366 1.989   -19.907 1.00 59.87  ? 21  GLY   B N   1 
ATOM   355  C CA  . GLY   B 2 12  ? -29.400 2.500   -20.864 1.00 58.76  ? 21  GLY   B CA  1 
ATOM   356  C C   . GLY   B 2 12  ? -28.090 2.953   -20.250 1.00 57.51  ? 21  GLY   B C   1 
ATOM   357  O O   . GLY   B 2 12  ? -27.850 2.774   -19.046 1.00 56.95  ? 21  GLY   B O   1 
ATOM   358  N N   . VAL   B 2 13  ? -27.204 3.491   -21.097 1.00 56.09  ? 22  VAL   B N   1 
ATOM   359  C CA  . VAL   B 2 13  ? -25.899 3.966   -20.653 1.00 55.51  ? 22  VAL   B CA  1 
ATOM   360  C C   . VAL   B 2 13  ? -25.947 5.490   -20.421 1.00 55.26  ? 22  VAL   B C   1 
ATOM   361  O O   . VAL   B 2 13  ? -26.621 6.193   -21.165 1.00 55.78  ? 22  VAL   B O   1 
ATOM   362  C CB  . VAL   B 2 13  ? -24.758 3.480   -21.586 1.00 55.93  ? 22  VAL   B CB  1 
ATOM   363  C CG1 . VAL   B 2 13  ? -24.905 4.021   -23.032 1.00 56.02  ? 22  VAL   B CG1 1 
ATOM   364  C CG2 . VAL   B 2 13  ? -23.390 3.799   -20.999 1.00 55.82  ? 22  VAL   B CG2 1 
ATOM   365  N N   . TYR   B 2 14  ? -25.317 5.982   -19.343 1.00 54.45  ? 23  TYR   B N   1 
ATOM   366  C CA  . TYR   B 2 14  ? -25.345 7.386   -18.941 1.00 54.91  ? 23  TYR   B CA  1 
ATOM   367  C C   . TYR   B 2 14  ? -23.954 7.963   -18.695 1.00 55.60  ? 23  TYR   B C   1 
ATOM   368  O O   . TYR   B 2 14  ? -23.053 7.263   -18.256 1.00 56.55  ? 23  TYR   B O   1 
ATOM   369  C CB  . TYR   B 2 14  ? -26.189 7.587   -17.648 1.00 54.57  ? 23  TYR   B CB  1 
ATOM   370  C CG  . TYR   B 2 14  ? -27.681 7.425   -17.839 1.00 55.35  ? 23  TYR   B CG  1 
ATOM   371  C CD1 . TYR   B 2 14  ? -28.234 6.186   -18.129 1.00 56.17  ? 23  TYR   B CD1 1 
ATOM   372  C CD2 . TYR   B 2 14  ? -28.544 8.500   -17.679 1.00 57.25  ? 23  TYR   B CD2 1 
ATOM   373  C CE1 . TYR   B 2 14  ? -29.597 6.029   -18.318 1.00 57.29  ? 23  TYR   B CE1 1 
ATOM   374  C CE2 . TYR   B 2 14  ? -29.916 8.358   -17.876 1.00 58.58  ? 23  TYR   B CE2 1 
ATOM   375  C CZ  . TYR   B 2 14  ? -30.435 7.120   -18.211 1.00 59.31  ? 23  TYR   B CZ  1 
ATOM   376  O OH  . TYR   B 2 14  ? -31.784 6.944   -18.392 1.00 61.50  ? 23  TYR   B OH  1 
ATOM   377  N N   . ARG   B 2 15  ? -23.804 9.268   -18.911 1.00 54.97  ? 24  ARG   B N   1 
ATOM   378  C CA  . ARG   B 2 15  ? -22.566 9.969   -18.614 1.00 54.36  ? 24  ARG   B CA  1 
ATOM   379  C C   . ARG   B 2 15  ? -22.647 10.465  -17.173 1.00 54.42  ? 24  ARG   B C   1 
ATOM   380  O O   . ARG   B 2 15  ? -23.708 10.902  -16.739 1.00 53.89  ? 24  ARG   B O   1 
ATOM   381  C CB  . ARG   B 2 15  ? -22.410 11.194  -19.534 1.00 54.51  ? 24  ARG   B CB  1 
ATOM   382  C CG  . ARG   B 2 15  ? -22.363 10.858  -21.019 1.00 56.31  ? 24  ARG   B CG  1 
ATOM   383  C CD  . ARG   B 2 15  ? -21.885 12.038  -21.818 1.00 59.13  ? 24  ARG   B CD  1 
ATOM   384  N NE  . ARG   B 2 15  ? -22.182 11.842  -23.231 1.00 61.87  ? 24  ARG   B NE  1 
ATOM   385  C CZ  . ARG   B 2 15  ? -21.298 11.451  -24.140 1.00 64.38  ? 24  ARG   B CZ  1 
ATOM   386  N NH1 . ARG   B 2 15  ? -20.020 11.286  -23.808 1.00 62.76  ? 24  ARG   B NH1 1 
ATOM   387  N NH2 . ARG   B 2 15  ? -21.673 11.259  -25.397 1.00 65.03  ? 24  ARG   B NH2 1 
ATOM   388  N N   . VAL   B 2 16  ? -21.528 10.456  -16.452 1.00 54.44  ? 25  VAL   B N   1 
ATOM   389  C CA  . VAL   B 2 16  ? -21.463 10.982  -15.091 1.00 55.42  ? 25  VAL   B CA  1 
ATOM   390  C C   . VAL   B 2 16  ? -20.632 12.260  -15.170 1.00 56.41  ? 25  VAL   B C   1 
ATOM   391  O O   . VAL   B 2 16  ? -19.461 12.225  -15.528 1.00 56.67  ? 25  VAL   B O   1 
ATOM   392  C CB  . VAL   B 2 16  ? -20.903 9.951   -14.065 1.00 55.82  ? 25  VAL   B CB  1 
ATOM   393  C CG1 . VAL   B 2 16  ? -20.913 10.534  -12.655 1.00 56.06  ? 25  VAL   B CG1 1 
ATOM   394  C CG2 . VAL   B 2 16  ? -21.686 8.645   -14.115 1.00 55.59  ? 25  VAL   B CG2 1 
ATOM   395  N N   . MET   B 2 17  ? -21.260 13.387  -14.908 1.00 57.32  ? 26  MET   B N   1 
ATOM   396  C CA  . MET   B 2 17  ? -20.674 14.710  -15.107 1.00 58.64  ? 26  MET   B CA  1 
ATOM   397  C C   . MET   B 2 17  ? -20.526 15.535  -13.836 1.00 60.96  ? 26  MET   B C   1 
ATOM   398  O O   . MET   B 2 17  ? -21.263 15.329  -12.878 1.00 60.93  ? 26  MET   B O   1 
ATOM   399  C CB  . MET   B 2 17  ? -21.594 15.509  -16.056 1.00 57.84  ? 26  MET   B CB  1 
ATOM   400  C CG  . MET   B 2 17  ? -21.973 14.785  -17.335 1.00 59.31  ? 26  MET   B CG  1 
ATOM   401  S SD  . MET   B 2 17  ? -20.636 14.770  -18.552 1.00 62.52  ? 26  MET   B SD  1 
ATOM   402  C CE  . MET   B 2 17  ? -20.413 16.538  -18.808 1.00 59.96  ? 26  MET   B CE  1 
ATOM   403  N N   . THR   B 2 18  ? -19.665 16.555  -13.875 1.00 62.97  ? 27  THR   B N   1 
ATOM   404  C CA  . THR   B 2 18  ? -19.528 17.493  -12.773 1.00 65.83  ? 27  THR   B CA  1 
ATOM   405  C C   . THR   B 2 18  ? -19.283 18.925  -13.271 1.00 68.25  ? 27  THR   B C   1 
ATOM   406  O O   . THR   B 2 18  ? -18.690 19.133  -14.333 1.00 67.71  ? 27  THR   B O   1 
ATOM   407  C CB  . THR   B 2 18  ? -18.448 17.048  -11.776 1.00 67.45  ? 27  THR   B CB  1 
ATOM   408  O OG1 . THR   B 2 18  ? -18.481 17.953  -10.669 1.00 69.34  ? 27  THR   B OG1 1 
ATOM   409  C CG2 . THR   B 2 18  ? -17.051 17.022  -12.390 1.00 67.28  ? 27  THR   B CG2 1 
ATOM   410  N N   . ARG   B 2 19  ? -19.733 19.912  -12.495 1.00 70.62  ? 28  ARG   B N   1 
ATOM   411  C CA  . ARG   B 2 19  ? -19.467 21.311  -12.806 1.00 73.53  ? 28  ARG   B CA  1 
ATOM   412  C C   . ARG   B 2 19  ? -18.495 21.950  -11.763 1.00 75.63  ? 28  ARG   B C   1 
ATOM   413  O O   . ARG   B 2 19  ? -18.361 23.175  -11.739 1.00 75.95  ? 28  ARG   B O   1 
ATOM   414  C CB  . ARG   B 2 19  ? -20.773 22.121  -12.978 1.00 76.14  ? 28  ARG   B CB  1 
ATOM   415  C CG  . ARG   B 2 19  ? -21.596 21.706  -14.199 1.00 81.21  ? 28  ARG   B CG  1 
ATOM   416  C CD  . ARG   B 2 19  ? -22.719 22.681  -14.501 1.00 86.45  ? 28  ARG   B CD  1 
ATOM   417  N NE  . ARG   B 2 19  ? -23.651 22.191  -15.524 1.00 91.15  ? 28  ARG   B NE  1 
ATOM   418  C CZ  . ARG   B 2 19  ? -24.856 21.684  -15.262 1.00 94.59  ? 28  ARG   B CZ  1 
ATOM   419  N NH1 . ARG   B 2 19  ? -25.281 21.574  -14.007 1.00 94.53  ? 28  ARG   B NH1 1 
ATOM   420  N NH2 . ARG   B 2 19  ? -25.637 21.267  -16.253 1.00 94.56  ? 28  ARG   B NH2 1 
ATOM   421  N N   . ARG   B 2 20  ? -17.793 21.120  -10.935 1.00 76.97  ? 29  ARG   B N   1 
ATOM   422  C CA  . ARG   B 2 20  ? -16.845 21.575  -9.895  1.00 78.72  ? 29  ARG   B CA  1 
ATOM   423  C C   . ARG   B 2 20  ? -15.422 21.901  -10.423 1.00 79.31  ? 29  ARG   B C   1 
ATOM   424  O O   . ARG   B 2 20  ? -14.536 22.252  -9.641  1.00 79.84  ? 29  ARG   B O   1 
ATOM   425  C CB  . ARG   B 2 20  ? -16.773 20.586  -8.703  1.00 80.76  ? 29  ARG   B CB  1 
ATOM   426  C CG  . ARG   B 2 20  ? -15.918 19.350  -8.956  1.00 86.10  ? 29  ARG   B CG  1 
ATOM   427  C CD  . ARG   B 2 20  ? -15.081 18.959  -7.744  1.00 91.00  ? 29  ARG   B CD  1 
ATOM   428  N NE  . ARG   B 2 20  ? -14.070 17.947  -8.073  1.00 95.08  ? 29  ARG   B NE  1 
ATOM   429  C CZ  . ARG   B 2 20  ? -12.756 18.121  -7.931  1.00 98.28  ? 29  ARG   B CZ  1 
ATOM   430  N NH1 . ARG   B 2 20  ? -12.277 19.269  -7.459  1.00 98.12  ? 29  ARG   B NH1 1 
ATOM   431  N NH2 . ARG   B 2 20  ? -11.912 17.146  -8.249  1.00 98.37  ? 29  ARG   B NH2 1 
ATOM   432  N N   . LEU   B 2 21  ? -15.201 21.764  -11.734 1.00 78.82  ? 30  LEU   B N   1 
ATOM   433  C CA  . LEU   B 2 21  ? -13.926 22.102  -12.368 1.00 78.39  ? 30  LEU   B CA  1 
ATOM   434  C C   . LEU   B 2 21  ? -14.240 23.135  -13.487 1.00 77.57  ? 30  LEU   B C   1 
ATOM   435  O O   . LEU   B 2 21  ? -15.247 23.841  -13.381 1.00 78.16  ? 30  LEU   B O   1 
ATOM   436  C CB  . LEU   B 2 21  ? -13.237 20.830  -12.910 1.00 78.88  ? 30  LEU   B CB  1 
ATOM   437  C CG  . LEU   B 2 21  ? -12.817 19.774  -11.900 1.00 81.01  ? 30  LEU   B CG  1 
ATOM   438  C CD1 . LEU   B 2 21  ? -12.158 18.613  -12.596 1.00 81.46  ? 30  LEU   B CD1 1 
ATOM   439  C CD2 . LEU   B 2 21  ? -11.856 20.338  -10.877 1.00 82.04  ? 30  LEU   B CD2 1 
ATOM   440  N N   . LEU   B 2 22  ? -13.398 23.258  -14.530 1.00 76.44  ? 31  LEU   B N   1 
ATOM   441  C CA  . LEU   B 2 22  ? -13.661 24.193  -15.622 1.00 75.84  ? 31  LEU   B CA  1 
ATOM   442  C C   . LEU   B 2 22  ? -14.753 23.618  -16.523 1.00 74.67  ? 31  LEU   B C   1 
ATOM   443  O O   . LEU   B 2 22  ? -14.646 22.464  -16.944 1.00 75.16  ? 31  LEU   B O   1 
ATOM   444  C CB  . LEU   B 2 22  ? -12.392 24.420  -16.436 1.00 75.92  ? 31  LEU   B CB  1 
ATOM   445  C CG  . LEU   B 2 22  ? -12.507 25.504  -17.469 1.00 77.15  ? 31  LEU   B CG  1 
ATOM   446  C CD1 . LEU   B 2 22  ? -12.171 26.868  -16.873 1.00 77.22  ? 31  LEU   B CD1 1 
ATOM   447  C CD2 . LEU   B 2 22  ? -11.621 25.203  -18.641 1.00 78.08  ? 31  LEU   B CD2 1 
ATOM   448  N N   . GLY   B 2 23  ? -15.798 24.402  -16.779 1.00 72.76  ? 32  GLY   B N   1 
ATOM   449  C CA  . GLY   B 2 23  ? -16.927 23.971  -17.597 1.00 71.61  ? 32  GLY   B CA  1 
ATOM   450  C C   . GLY   B 2 23  ? -17.608 22.731  -17.051 1.00 70.11  ? 32  GLY   B C   1 
ATOM   451  O O   . GLY   B 2 23  ? -17.706 22.556  -15.833 1.00 70.19  ? 32  GLY   B O   1 
ATOM   452  N N   . SER   B 2 24  ? -18.053 21.841  -17.941 1.00 68.65  ? 33  SER   B N   1 
ATOM   453  C CA  . SER   B 2 24  ? -18.674 20.580  -17.534 1.00 67.51  ? 33  SER   B CA  1 
ATOM   454  C C   . SER   B 2 24  ? -17.684 19.481  -17.861 1.00 65.66  ? 33  SER   B C   1 
ATOM   455  O O   . SER   B 2 24  ? -17.231 19.397  -18.997 1.00 65.82  ? 33  SER   B O   1 
ATOM   456  C CB  . SER   B 2 24  ? -19.980 20.347  -18.287 1.00 69.08  ? 33  SER   B CB  1 
ATOM   457  O OG  . SER   B 2 24  ? -20.894 21.409  -18.061 1.00 72.16  ? 33  SER   B OG  1 
ATOM   458  N N   . THR   B 2 25  ? -17.330 18.654  -16.880 1.00 63.79  ? 34  THR   B N   1 
ATOM   459  C CA  . THR   B 2 25  ? -16.348 17.592  -17.092 1.00 62.73  ? 34  THR   B CA  1 
ATOM   460  C C   . THR   B 2 25  ? -16.958 16.203  -16.865 1.00 61.24  ? 34  THR   B C   1 
ATOM   461  O O   . THR   B 2 25  ? -17.725 16.017  -15.917 1.00 60.06  ? 34  THR   B O   1 
ATOM   462  C CB  . THR   B 2 25  ? -15.104 17.828  -16.194 1.00 64.63  ? 34  THR   B CB  1 
ATOM   463  O OG1 . THR   B 2 25  ? -14.672 19.191  -16.313 1.00 66.67  ? 34  THR   B OG1 1 
ATOM   464  C CG2 . THR   B 2 25  ? -13.951 16.902  -16.546 1.00 64.84  ? 34  THR   B CG2 1 
ATOM   465  N N   . GLN   B 2 26  ? -16.616 15.227  -17.729 1.00 60.25  ? 35  GLN   B N   1 
ATOM   466  C CA  . GLN   B 2 26  ? -17.137 13.875  -17.572 1.00 60.06  ? 35  GLN   B CA  1 
ATOM   467  C C   . GLN   B 2 26  ? -16.163 13.051  -16.752 1.00 60.60  ? 35  GLN   B C   1 
ATOM   468  O O   . GLN   B 2 26  ? -15.050 12.786  -17.199 1.00 61.48  ? 35  GLN   B O   1 
ATOM   469  C CB  . GLN   B 2 26  ? -17.380 13.213  -18.931 1.00 60.04  ? 35  GLN   B CB  1 
ATOM   470  C CG  . GLN   B 2 26  ? -17.917 11.786  -18.822 1.00 60.88  ? 35  GLN   B CG  1 
ATOM   471  C CD  . GLN   B 2 26  ? -18.144 11.180  -20.183 1.00 61.30  ? 35  GLN   B CD  1 
ATOM   472  O OE1 . GLN   B 2 26  ? -18.703 11.816  -21.069 1.00 60.69  ? 35  GLN   B OE1 1 
ATOM   473  N NE2 . GLN   B 2 26  ? -17.731 9.934   -20.375 1.00 60.33  ? 35  GLN   B NE2 1 
ATOM   474  N N   . VAL   B 2 27  ? -16.563 12.664  -15.548 1.00 59.79  ? 36  VAL   B N   1 
ATOM   475  C CA  . VAL   B 2 27  ? -15.705 11.877  -14.662 1.00 58.94  ? 36  VAL   B CA  1 
ATOM   476  C C   . VAL   B 2 27  ? -15.854 10.353  -14.862 1.00 57.61  ? 36  VAL   B C   1 
ATOM   477  O O   . VAL   B 2 27  ? -14.961 9.578   -14.492 1.00 57.87  ? 36  VAL   B O   1 
ATOM   478  C CB  . VAL   B 2 27  ? -15.935 12.303  -13.192 1.00 59.98  ? 36  VAL   B CB  1 
ATOM   479  C CG1 . VAL   B 2 27  ? -15.470 13.741  -12.973 1.00 60.74  ? 36  VAL   B CG1 1 
ATOM   480  C CG2 . VAL   B 2 27  ? -17.403 12.154  -12.795 1.00 59.98  ? 36  VAL   B CG2 1 
ATOM   481  N N   . GLY   B 2 28  ? -16.961 9.936   -15.469 1.00 55.88  ? 37  GLY   B N   1 
ATOM   482  C CA  . GLY   B 2 28  ? -17.223 8.529   -15.718 1.00 54.26  ? 37  GLY   B CA  1 
ATOM   483  C C   . GLY   B 2 28  ? -18.529 8.298   -16.453 1.00 52.86  ? 37  GLY   B C   1 
ATOM   484  O O   . GLY   B 2 28  ? -19.120 9.223   -17.016 1.00 52.50  ? 37  GLY   B O   1 
ATOM   485  N N   . VAL   B 2 29  ? -18.965 7.029   -16.464 1.00 51.34  ? 38  VAL   B N   1 
ATOM   486  C CA  . VAL   B 2 29  ? -20.106 6.450   -17.164 1.00 50.03  ? 38  VAL   B CA  1 
ATOM   487  C C   . VAL   B 2 29  ? -20.808 5.442   -16.228 1.00 49.71  ? 38  VAL   B C   1 
ATOM   488  O O   . VAL   B 2 29  ? -20.201 4.949   -15.271 1.00 50.50  ? 38  VAL   B O   1 
ATOM   489  C CB  . VAL   B 2 29  ? -19.580 5.716   -18.446 1.00 50.31  ? 38  VAL   B CB  1 
ATOM   490  C CG1 . VAL   B 2 29  ? -20.707 5.053   -19.221 1.00 51.05  ? 38  VAL   B CG1 1 
ATOM   491  C CG2 . VAL   B 2 29  ? -18.809 6.652   -19.372 1.00 49.54  ? 38  VAL   B CG2 1 
ATOM   492  N N   . GLY   B 2 30  ? -22.064 5.127   -16.512 1.00 48.48  ? 39  GLY   B N   1 
ATOM   493  C CA  . GLY   B 2 30  ? -22.808 4.152   -15.736 1.00 47.98  ? 39  GLY   B CA  1 
ATOM   494  C C   . GLY   B 2 30  ? -23.949 3.517   -16.495 1.00 48.08  ? 39  GLY   B C   1 
ATOM   495  O O   . GLY   B 2 30  ? -24.291 3.948   -17.601 1.00 48.44  ? 39  GLY   B O   1 
ATOM   496  N N   . VAL   B 2 31  ? -24.523 2.465   -15.922 1.00 48.05  ? 40  VAL   B N   1 
ATOM   497  C CA  . VAL   B 2 31  ? -25.593 1.671   -16.518 1.00 48.90  ? 40  VAL   B CA  1 
ATOM   498  C C   . VAL   B 2 31  ? -26.848 1.729   -15.660 1.00 49.20  ? 40  VAL   B C   1 
ATOM   499  O O   . VAL   B 2 31  ? -26.821 1.323   -14.492 1.00 48.88  ? 40  VAL   B O   1 
ATOM   500  C CB  . VAL   B 2 31  ? -25.158 0.186   -16.663 1.00 50.92  ? 40  VAL   B CB  1 
ATOM   501  C CG1 . VAL   B 2 31  ? -26.325 -0.685  -17.133 1.00 52.38  ? 40  VAL   B CG1 1 
ATOM   502  C CG2 . VAL   B 2 31  ? -23.951 0.031   -17.600 1.00 51.86  ? 40  VAL   B CG2 1 
ATOM   503  N N   . MET   B 2 32  ? -27.959 2.141   -16.254 1.00 49.03  ? 41  MET   B N   1 
ATOM   504  C CA  . MET   B 2 32  ? -29.242 2.139   -15.578 1.00 49.55  ? 41  MET   B CA  1 
ATOM   505  C C   . MET   B 2 32  ? -29.933 0.839   -16.018 1.00 50.30  ? 41  MET   B C   1 
ATOM   506  O O   . MET   B 2 32  ? -30.068 0.596   -17.216 1.00 50.03  ? 41  MET   B O   1 
ATOM   507  C CB  . MET   B 2 32  ? -30.058 3.354   -16.036 1.00 49.98  ? 41  MET   B CB  1 
ATOM   508  C CG  . MET   B 2 32  ? -31.322 3.600   -15.236 1.00 52.49  ? 41  MET   B CG  1 
ATOM   509  S SD  . MET   B 2 32  ? -31.037 4.128   -13.509 1.00 56.46  ? 41  MET   B SD  1 
ATOM   510  C CE  . MET   B 2 32  ? -30.447 5.795   -13.761 1.00 54.49  ? 41  MET   B CE  1 
ATOM   511  N N   . GLN   B 2 33  ? -30.310 -0.007  -15.075 1.00 50.73  ? 42  GLN   B N   1 
ATOM   512  C CA  . GLN   B 2 33  ? -30.991 -1.260  -15.373 1.00 52.26  ? 42  GLN   B CA  1 
ATOM   513  C C   . GLN   B 2 33  ? -31.935 -1.575  -14.241 1.00 54.31  ? 42  GLN   B C   1 
ATOM   514  O O   . GLN   B 2 33  ? -31.531 -1.480  -13.083 1.00 55.62  ? 42  GLN   B O   1 
ATOM   515  C CB  . GLN   B 2 33  ? -30.001 -2.427  -15.578 1.00 53.98  ? 42  GLN   B CB  1 
ATOM   516  C CG  . GLN   B 2 33  ? -30.742 -3.672  -16.071 1.00 58.38  ? 42  GLN   B CG  1 
ATOM   517  C CD  . GLN   B 2 33  ? -29.865 -4.761  -16.628 1.00 62.85  ? 42  GLN   B CD  1 
ATOM   518  O OE1 . GLN   B 2 33  ? -30.013 -5.936  -16.279 1.00 65.76  ? 42  GLN   B OE1 1 
ATOM   519  N NE2 . GLN   B 2 33  ? -28.929 -4.406  -17.489 1.00 61.37  ? 42  GLN   B NE2 1 
ATOM   520  N N   . GLU   B 2 34  ? -33.198 -1.889  -14.540 1.00 54.49  ? 43  GLU   B N   1 
ATOM   521  C CA  . GLU   B 2 34  ? -34.178 -2.163  -13.486 1.00 55.11  ? 43  GLU   B CA  1 
ATOM   522  C C   . GLU   B 2 34  ? -34.261 -1.057  -12.361 1.00 54.84  ? 43  GLU   B C   1 
ATOM   523  O O   . GLU   B 2 34  ? -34.433 -1.377  -11.184 1.00 54.54  ? 43  GLU   B O   1 
ATOM   524  C CB  . GLU   B 2 34  ? -33.949 -3.557  -12.881 1.00 57.50  ? 43  GLU   B CB  1 
ATOM   525  C CG  . GLU   B 2 34  ? -34.044 -4.679  -13.906 1.00 61.78  ? 43  GLU   B CG  1 
ATOM   526  C CD  . GLU   B 2 34  ? -33.296 -5.963  -13.581 1.00 68.08  ? 43  GLU   B CD  1 
ATOM   527  O OE1 . GLU   B 2 34  ? -33.637 -6.617  -12.571 1.00 70.08  ? 43  GLU   B OE1 1 
ATOM   528  O OE2 . GLU   B 2 34  ? -32.367 -6.318  -14.343 1.00 70.40  ? 43  GLU   B OE2 1 
ATOM   529  N N   . GLY   B 2 35  ? -34.179 0.216   -12.740 1.00 53.91  ? 44  GLY   B N   1 
ATOM   530  C CA  . GLY   B 2 35  ? -34.289 1.319   -11.786 1.00 53.56  ? 44  GLY   B CA  1 
ATOM   531  C C   . GLY   B 2 35  ? -33.085 1.538   -10.879 1.00 52.68  ? 44  GLY   B C   1 
ATOM   532  O O   . GLY   B 2 35  ? -33.130 2.385   -9.985  1.00 52.87  ? 44  GLY   B O   1 
ATOM   533  N N   . VAL   B 2 36  ? -31.997 0.787   -11.114 1.00 51.03  ? 45  VAL   B N   1 
ATOM   534  C CA  . VAL   B 2 36  ? -30.755 0.859   -10.360 1.00 50.36  ? 45  VAL   B CA  1 
ATOM   535  C C   . VAL   B 2 36  ? -29.635 1.405   -11.255 1.00 49.03  ? 45  VAL   B C   1 
ATOM   536  O O   . VAL   B 2 36  ? -29.475 0.950   -12.408 1.00 49.51  ? 45  VAL   B O   1 
ATOM   537  C CB  . VAL   B 2 36  ? -30.410 -0.554  -9.781  1.00 52.22  ? 45  VAL   B CB  1 
ATOM   538  C CG1 . VAL   B 2 36  ? -28.958 -0.639  -9.291  1.00 53.19  ? 45  VAL   B CG1 1 
ATOM   539  C CG2 . VAL   B 2 36  ? -31.366 -0.913  -8.649  1.00 52.59  ? 45  VAL   B CG2 1 
ATOM   540  N N   . PHE   B 2 37  ? -28.886 2.402   -10.756 1.00 47.22  ? 46  PHE   B N   1 
ATOM   541  C CA  . PHE   B 2 37  ? -27.771 2.951   -11.525 1.00 47.55  ? 46  PHE   B CA  1 
ATOM   542  C C   . PHE   B 2 37  ? -26.489 2.261   -11.035 1.00 47.31  ? 46  PHE   B C   1 
ATOM   543  O O   . PHE   B 2 37  ? -26.252 2.209   -9.826  1.00 46.90  ? 46  PHE   B O   1 
ATOM   544  C CB  . PHE   B 2 37  ? -27.684 4.483   -11.361 1.00 47.94  ? 46  PHE   B CB  1 
ATOM   545  C CG  . PHE   B 2 37  ? -26.680 5.112   -12.309 1.00 48.54  ? 46  PHE   B CG  1 
ATOM   546  C CD1 . PHE   B 2 37  ? -26.875 5.070   -13.677 1.00 49.69  ? 46  PHE   B CD1 1 
ATOM   547  C CD2 . PHE   B 2 37  ? -25.551 5.749   -11.824 1.00 49.23  ? 46  PHE   B CD2 1 
ATOM   548  C CE1 . PHE   B 2 37  ? -25.951 5.638   -14.548 1.00 50.62  ? 46  PHE   B CE1 1 
ATOM   549  C CE2 . PHE   B 2 37  ? -24.624 6.305   -12.689 1.00 49.77  ? 46  PHE   B CE2 1 
ATOM   550  C CZ  . PHE   B 2 37  ? -24.840 6.267   -14.048 1.00 50.30  ? 46  PHE   B CZ  1 
ATOM   551  N N   . HIS   B 2 38  ? -25.695 1.699   -11.947 1.00 46.59  ? 47  HIS   B N   1 
ATOM   552  C CA  . HIS   B 2 38  ? -24.474 0.975   -11.631 1.00 46.76  ? 47  HIS   B CA  1 
ATOM   553  C C   . HIS   B 2 38  ? -23.268 1.728   -12.171 1.00 48.07  ? 47  HIS   B C   1 
ATOM   554  O O   . HIS   B 2 38  ? -23.249 2.043   -13.362 1.00 47.42  ? 47  HIS   B O   1 
ATOM   555  C CB  . HIS   B 2 38  ? -24.503 -0.399  -12.321 1.00 46.58  ? 47  HIS   B CB  1 
ATOM   556  C CG  . HIS   B 2 38  ? -25.725 -1.211  -12.030 1.00 48.31  ? 47  HIS   B CG  1 
ATOM   557  N ND1 . HIS   B 2 38  ? -26.982 -0.832  -12.494 1.00 49.86  ? 47  HIS   B ND1 1 
ATOM   558  C CD2 . HIS   B 2 38  ? -25.851 -2.354  -11.315 1.00 49.08  ? 47  HIS   B CD2 1 
ATOM   559  C CE1 . HIS   B 2 38  ? -27.818 -1.763  -12.064 1.00 50.09  ? 47  HIS   B CE1 1 
ATOM   560  N NE2 . HIS   B 2 38  ? -27.179 -2.707  -11.363 1.00 50.19  ? 47  HIS   B NE2 1 
ATOM   561  N N   . THR   B 2 39  ? -22.220 1.958   -11.339 1.00 48.11  ? 48  THR   B N   1 
ATOM   562  C CA  . THR   B 2 39  ? -20.994 2.589   -11.871 1.00 48.82  ? 48  THR   B CA  1 
ATOM   563  C C   . THR   B 2 39  ? -19.745 2.028   -11.120 1.00 48.73  ? 48  THR   B C   1 
ATOM   564  O O   . THR   B 2 39  ? -19.884 1.144   -10.264 1.00 48.75  ? 48  THR   B O   1 
ATOM   565  C CB  . THR   B 2 39  ? -21.120 4.152   -11.916 1.00 50.02  ? 48  THR   B CB  1 
ATOM   566  O OG1 . THR   B 2 39  ? -20.016 4.697   -12.662 1.00 50.94  ? 48  THR   B OG1 1 
ATOM   567  C CG2 . THR   B 2 39  ? -21.161 4.787   -10.531 1.00 49.57  ? 48  THR   B CG2 1 
ATOM   568  N N   . MET   B 2 40  ? -18.542 2.515   -11.456 1.00 47.97  ? 49  MET   B N   1 
ATOM   569  C CA  . MET   B 2 40  ? -17.347 2.144   -10.724 1.00 48.29  ? 49  MET   B CA  1 
ATOM   570  C C   . MET   B 2 40  ? -17.188 3.115   -9.541  1.00 48.75  ? 49  MET   B C   1 
ATOM   571  O O   . MET   B 2 40  ? -17.492 4.301   -9.651  1.00 49.46  ? 49  MET   B O   1 
ATOM   572  C CB  . MET   B 2 40  ? -16.098 2.132   -11.607 1.00 48.75  ? 49  MET   B CB  1 
ATOM   573  C CG  . MET   B 2 40  ? -16.304 1.396   -12.943 1.00 51.94  ? 49  MET   B CG  1 
ATOM   574  S SD  . MET   B 2 40  ? -14.876 0.444   -13.404 1.00 59.52  ? 49  MET   B SD  1 
ATOM   575  C CE  . MET   B 2 40  ? -15.041 -0.907  -12.335 1.00 55.61  ? 49  MET   B CE  1 
ATOM   576  N N   . TRP   B 2 41  ? -16.734 2.602   -8.400  1.00 49.03  ? 50  TRP   B N   1 
ATOM   577  C CA  A TRP   B 2 41  ? -16.560 3.407   -7.198  0.50 49.29  ? 50  TRP   B CA  1 
ATOM   578  C CA  B TRP   B 2 41  ? -16.544 3.391   -7.190  0.50 48.80  ? 50  TRP   B CA  1 
ATOM   579  C C   . TRP   B 2 41  ? -15.636 4.601   -7.408  1.00 49.03  ? 50  TRP   B C   1 
ATOM   580  O O   . TRP   B 2 41  ? -15.960 5.692   -6.944  1.00 48.89  ? 50  TRP   B O   1 
ATOM   581  C CB  A TRP   B 2 41  ? -16.091 2.552   -6.004  0.50 49.77  ? 50  TRP   B CB  1 
ATOM   582  C CB  B TRP   B 2 41  ? -15.996 2.516   -6.043  0.50 48.52  ? 50  TRP   B CB  1 
ATOM   583  C CG  A TRP   B 2 41  ? -16.317 3.238   -4.697  0.50 51.21  ? 50  TRP   B CG  1 
ATOM   584  C CG  B TRP   B 2 41  ? -15.862 3.283   -4.774  0.50 48.96  ? 50  TRP   B CG  1 
ATOM   585  C CD1 A TRP   B 2 41  ? -17.444 3.192   -3.934  0.50 52.18  ? 50  TRP   B CD1 1 
ATOM   586  C CD1 B TRP   B 2 41  ? -14.843 4.116   -4.417  0.50 49.84  ? 50  TRP   B CD1 1 
ATOM   587  C CD2 A TRP   B 2 41  ? -15.411 4.122   -4.026  0.50 51.81  ? 50  TRP   B CD2 1 
ATOM   588  C CD2 B TRP   B 2 41  ? -16.827 3.355   -3.726  0.50 48.81  ? 50  TRP   B CD2 1 
ATOM   589  N NE1 A TRP   B 2 41  ? -17.279 3.958   -2.806  0.50 52.85  ? 50  TRP   B NE1 1 
ATOM   590  N NE1 B TRP   B 2 41  ? -15.108 4.686   -3.197  0.50 49.82  ? 50  TRP   B NE1 1 
ATOM   591  C CE2 A TRP   B 2 41  ? -16.041 4.545   -2.841  0.50 52.68  ? 50  TRP   B CE2 1 
ATOM   592  C CE2 B TRP   B 2 41  ? -16.312 4.220   -2.741  0.50 49.60  ? 50  TRP   B CE2 1 
ATOM   593  C CE3 A TRP   B 2 41  ? -14.116 4.579   -4.300  0.50 52.58  ? 50  TRP   B CE3 1 
ATOM   594  C CE3 B TRP   B 2 41  ? -18.066 2.748   -3.509  0.50 49.38  ? 50  TRP   B CE3 1 
ATOM   595  C CZ2 A TRP   B 2 41  ? -15.433 5.425   -1.947  0.50 53.44  ? 50  TRP   B CZ2 1 
ATOM   596  C CZ2 B TRP   B 2 41  ? -17.009 4.519   -1.574  0.50 50.20  ? 50  TRP   B CZ2 1 
ATOM   597  C CZ3 A TRP   B 2 41  ? -13.505 5.421   -3.393  0.50 53.52  ? 50  TRP   B CZ3 1 
ATOM   598  C CZ3 B TRP   B 2 41  ? -18.738 3.020   -2.335  0.50 50.41  ? 50  TRP   B CZ3 1 
ATOM   599  C CH2 A TRP   B 2 41  ? -14.166 5.845   -2.241  0.50 53.54  ? 50  TRP   B CH2 1 
ATOM   600  C CH2 B TRP   B 2 41  ? -18.211 3.902   -1.386  0.50 50.44  ? 50  TRP   B CH2 1 
ATOM   601  N N   . HIS   B 2 42  ? -14.485 4.413   -8.079  1.00 49.32  ? 51  HIS   B N   1 
ATOM   602  C CA  . HIS   B 2 42  ? -13.562 5.538   -8.302  1.00 50.24  ? 51  HIS   B CA  1 
ATOM   603  C C   . HIS   B 2 42  ? -14.163 6.723   -9.084  1.00 52.04  ? 51  HIS   B C   1 
ATOM   604  O O   . HIS   B 2 42  ? -13.580 7.805   -9.073  1.00 53.47  ? 51  HIS   B O   1 
ATOM   605  C CB  . HIS   B 2 42  ? -12.246 5.093   -8.932  1.00 49.47  ? 51  HIS   B CB  1 
ATOM   606  C CG  . HIS   B 2 42  ? -12.322 4.714   -10.375 1.00 50.20  ? 51  HIS   B CG  1 
ATOM   607  N ND1 . HIS   B 2 42  ? -12.505 3.400   -10.761 1.00 51.19  ? 51  HIS   B ND1 1 
ATOM   608  C CD2 . HIS   B 2 42  ? -12.106 5.470   -11.482 1.00 51.12  ? 51  HIS   B CD2 1 
ATOM   609  C CE1 . HIS   B 2 42  ? -12.466 3.410   -12.087 1.00 51.46  ? 51  HIS   B CE1 1 
ATOM   610  N NE2 . HIS   B 2 42  ? -12.247 4.639   -12.560 1.00 51.41  ? 51  HIS   B NE2 1 
ATOM   611  N N   . VAL   B 2 43  ? -15.327 6.544   -9.725  1.00 51.43  ? 52  VAL   B N   1 
ATOM   612  C CA  . VAL   B 2 43  ? -15.980 7.602   -10.493 1.00 50.76  ? 52  VAL   B CA  1 
ATOM   613  C C   . VAL   B 2 43  ? -16.704 8.593   -9.570  1.00 51.69  ? 52  VAL   B C   1 
ATOM   614  O O   . VAL   B 2 43  ? -16.545 9.806   -9.728  1.00 52.95  ? 52  VAL   B O   1 
ATOM   615  C CB  . VAL   B 2 43  ? -16.949 6.989   -11.537 1.00 50.78  ? 52  VAL   B CB  1 
ATOM   616  C CG1 . VAL   B 2 43  ? -17.870 8.058   -12.157 1.00 52.09  ? 52  VAL   B CG1 1 
ATOM   617  C CG2 . VAL   B 2 43  ? -16.185 6.239   -12.619 1.00 50.86  ? 52  VAL   B CG2 1 
ATOM   618  N N   . THR   B 2 44  ? -17.536 8.089   -8.648  1.00 50.56  ? 53  THR   B N   1 
ATOM   619  C CA  . THR   B 2 44  ? -18.309 8.961   -7.774  1.00 51.41  ? 53  THR   B CA  1 
ATOM   620  C C   . THR   B 2 44  ? -17.742 9.091   -6.364  1.00 52.54  ? 53  THR   B C   1 
ATOM   621  O O   . THR   B 2 44  ? -18.071 10.039  -5.670  1.00 53.38  ? 53  THR   B O   1 
ATOM   622  C CB  . THR   B 2 44  ? -19.770 8.490   -7.732  1.00 51.66  ? 53  THR   B CB  1 
ATOM   623  O OG1 . THR   B 2 44  ? -19.848 7.258   -7.007  1.00 51.66  ? 53  THR   B OG1 1 
ATOM   624  C CG2 . THR   B 2 44  ? -20.385 8.332   -9.149  1.00 51.66  ? 53  THR   B CG2 1 
ATOM   625  N N   . LYS   B 2 45  ? -16.925 8.128   -5.937  1.00 53.09  ? 54  LYS   B N   1 
ATOM   626  C CA  . LYS   B 2 45  ? -16.395 7.984   -4.576  1.00 54.47  ? 54  LYS   B CA  1 
ATOM   627  C C   . LYS   B 2 45  ? -17.563 7.790   -3.581  1.00 54.86  ? 54  LYS   B C   1 
ATOM   628  O O   . LYS   B 2 45  ? -17.451 8.224   -2.440  1.00 55.53  ? 54  LYS   B O   1 
ATOM   629  C CB  . LYS   B 2 45  ? -15.514 9.181   -4.140  1.00 57.06  ? 54  LYS   B CB  1 
ATOM   630  C CG  . LYS   B 2 45  ? -14.394 9.531   -5.105  1.00 63.55  ? 54  LYS   B CG  1 
ATOM   631  C CD  . LYS   B 2 45  ? -13.329 8.469   -5.096  1.00 70.11  ? 54  LYS   B CD  1 
ATOM   632  C CE  . LYS   B 2 45  ? -12.231 8.707   -6.109  1.00 75.45  ? 54  LYS   B CE  1 
ATOM   633  N NZ  . LYS   B 2 45  ? -11.198 7.626   -6.045  1.00 78.34  ? 54  LYS   B NZ  1 
ATOM   634  N N   . GLY   B 2 46  ? -18.662 7.165   -4.022  1.00 54.43  ? 55  GLY   B N   1 
ATOM   635  C CA  . GLY   B 2 46  ? -19.840 6.957   -3.192  1.00 55.23  ? 55  GLY   B CA  1 
ATOM   636  C C   . GLY   B 2 46  ? -20.741 8.163   -2.997  1.00 56.40  ? 55  GLY   B C   1 
ATOM   637  O O   . GLY   B 2 46  ? -21.720 8.072   -2.260  1.00 56.56  ? 55  GLY   B O   1 
ATOM   638  N N   . ALA   B 2 47  ? -20.477 9.291   -3.689  1.00 56.98  ? 56  ALA   B N   1 
ATOM   639  C CA  . ALA   B 2 47  ? -21.305 10.504  -3.535  1.00 57.31  ? 56  ALA   B CA  1 
ATOM   640  C C   . ALA   B 2 47  ? -22.669 10.425  -4.209  1.00 56.97  ? 56  ALA   B C   1 
ATOM   641  O O   . ALA   B 2 47  ? -22.803 9.753   -5.226  1.00 56.62  ? 56  ALA   B O   1 
ATOM   642  C CB  . ALA   B 2 47  ? -20.553 11.726  -4.058  1.00 57.61  ? 56  ALA   B CB  1 
ATOM   643  N N   . ALA   B 2 48  ? -23.666 11.176  -3.687  1.00 56.45  ? 57  ALA   B N   1 
ATOM   644  C CA  . ALA   B 2 48  ? -25.006 11.229  -4.275  1.00 57.01  ? 57  ALA   B CA  1 
ATOM   645  C C   . ALA   B 2 48  ? -24.961 11.836  -5.683  1.00 58.05  ? 57  ALA   B C   1 
ATOM   646  O O   . ALA   B 2 48  ? -24.049 12.602  -6.001  1.00 58.66  ? 57  ALA   B O   1 
ATOM   647  C CB  . ALA   B 2 48  ? -25.943 12.037  -3.386  1.00 57.50  ? 57  ALA   B CB  1 
ATOM   648  N N   . LEU   B 2 49  ? -25.928 11.465  -6.540  1.00 57.82  ? 58  LEU   B N   1 
ATOM   649  C CA  . LEU   B 2 49  ? -25.993 11.939  -7.917  1.00 58.48  ? 58  LEU   B CA  1 
ATOM   650  C C   . LEU   B 2 49  ? -27.318 12.619  -8.201  1.00 60.46  ? 58  LEU   B C   1 
ATOM   651  O O   . LEU   B 2 49  ? -28.326 12.324  -7.567  1.00 60.89  ? 58  LEU   B O   1 
ATOM   652  C CB  . LEU   B 2 49  ? -25.835 10.763  -8.898  1.00 57.52  ? 58  LEU   B CB  1 
ATOM   653  C CG  . LEU   B 2 49  ? -24.584 9.920   -8.771  1.00 57.35  ? 58  LEU   B CG  1 
ATOM   654  C CD1 . LEU   B 2 49  ? -24.678 8.708   -9.652  1.00 57.24  ? 58  LEU   B CD1 1 
ATOM   655  C CD2 . LEU   B 2 49  ? -23.345 10.719  -9.099  1.00 57.33  ? 58  LEU   B CD2 1 
ATOM   656  N N   . ARG   B 2 50  ? -27.320 13.519  -9.164  1.00 61.65  ? 59  ARG   B N   1 
ATOM   657  C CA  . ARG   B 2 50  ? -28.517 14.215  -9.592  1.00 63.69  ? 59  ARG   B CA  1 
ATOM   658  C C   . ARG   B 2 50  ? -28.921 13.691  -10.994 1.00 64.78  ? 59  ARG   B C   1 
ATOM   659  O O   . ARG   B 2 50  ? -28.065 13.367  -11.806 1.00 63.69  ? 59  ARG   B O   1 
ATOM   660  C CB  . ARG   B 2 50  ? -28.274 15.745  -9.535  1.00 66.29  ? 59  ARG   B CB  1 
ATOM   661  C CG  . ARG   B 2 50  ? -28.742 16.576  -10.731 1.00 72.09  ? 59  ARG   B CG  1 
ATOM   662  C CD  . ARG   B 2 50  ? -28.787 18.071  -10.428 1.00 77.04  ? 59  ARG   B CD  1 
ATOM   663  N NE  . ARG   B 2 50  ? -27.454 18.677  -10.426 1.00 81.37  ? 59  ARG   B NE  1 
ATOM   664  C CZ  . ARG   B 2 50  ? -26.901 19.279  -11.476 1.00 84.97  ? 59  ARG   B CZ  1 
ATOM   665  N NH1 . ARG   B 2 50  ? -27.561 19.362  -12.627 1.00 84.79  ? 59  ARG   B NH1 1 
ATOM   666  N NH2 . ARG   B 2 50  ? -25.684 19.801  -11.383 1.00 85.58  ? 59  ARG   B NH2 1 
ATOM   667  N N   . SER   B 2 51  ? -30.218 13.540  -11.239 1.00 66.77  ? 60  SER   B N   1 
ATOM   668  C CA  . SER   B 2 51  ? -30.724 13.112  -12.542 1.00 69.28  ? 60  SER   B CA  1 
ATOM   669  C C   . SER   B 2 51  ? -31.855 14.081  -12.828 1.00 71.74  ? 60  SER   B C   1 
ATOM   670  O O   . SER   B 2 51  ? -32.962 13.884  -12.334 1.00 72.45  ? 60  SER   B O   1 
ATOM   671  C CB  . SER   B 2 51  ? -31.255 11.684  -12.477 1.00 70.37  ? 60  SER   B CB  1 
ATOM   672  O OG  . SER   B 2 51  ? -31.803 11.297  -13.727 1.00 72.48  ? 60  SER   B OG  1 
ATOM   673  N N   . GLY   B 2 52  ? -31.547 15.174  -13.515 1.00 72.96  ? 61  GLY   B N   1 
ATOM   674  C CA  . GLY   B 2 52  ? -32.522 16.234  -13.745 1.00 74.50  ? 61  GLY   B CA  1 
ATOM   675  C C   . GLY   B 2 52  ? -32.752 16.951  -12.431 1.00 76.21  ? 61  GLY   B C   1 
ATOM   676  O O   . GLY   B 2 52  ? -31.790 17.409  -11.804 1.00 76.43  ? 61  GLY   B O   1 
ATOM   677  N N   . GLU   B 2 53  ? -34.006 16.970  -11.947 1.00 76.92  ? 62  GLU   B N   1 
ATOM   678  C CA  . GLU   B 2 53  ? -34.284 17.546  -10.627 1.00 77.86  ? 62  GLU   B CA  1 
ATOM   679  C C   . GLU   B 2 53  ? -34.465 16.469  -9.528  1.00 77.25  ? 62  GLU   B C   1 
ATOM   680  O O   . GLU   B 2 53  ? -34.973 16.775  -8.448  1.00 77.74  ? 62  GLU   B O   1 
ATOM   681  C CB  . GLU   B 2 53  ? -35.461 18.530  -10.665 1.00 81.91  ? 62  GLU   B CB  1 
ATOM   682  C CG  . GLU   B 2 53  ? -35.012 19.963  -10.892 1.00 89.76  ? 62  GLU   B CG  1 
ATOM   683  C CD  . GLU   B 2 53  ? -36.103 21.003  -10.735 1.00 100.61 ? 62  GLU   B CD  1 
ATOM   684  O OE1 . GLU   B 2 53  ? -37.294 20.629  -10.838 1.00 103.72 ? 62  GLU   B OE1 1 
ATOM   685  O OE2 . GLU   B 2 53  ? -35.769 22.193  -10.523 1.00 104.02 ? 62  GLU   B OE2 1 
ATOM   686  N N   . GLY   B 2 54  ? -34.009 15.242  -9.796  1.00 75.94  ? 63  GLY   B N   1 
ATOM   687  C CA  . GLY   B 2 54  ? -34.110 14.132  -8.856  1.00 75.05  ? 63  GLY   B CA  1 
ATOM   688  C C   . GLY   B 2 54  ? -32.786 13.713  -8.240  1.00 73.42  ? 63  GLY   B C   1 
ATOM   689  O O   . GLY   B 2 54  ? -31.711 13.988  -8.784  1.00 73.52  ? 63  GLY   B O   1 
ATOM   690  N N   . ARG   B 2 55  ? -32.855 13.042  -7.090  1.00 71.34  ? 64  ARG   B N   1 
ATOM   691  C CA  . ARG   B 2 55  ? -31.657 12.608  -6.387  1.00 69.45  ? 64  ARG   B CA  1 
ATOM   692  C C   . ARG   B 2 55  ? -31.512 11.078  -6.365  1.00 66.65  ? 64  ARG   B C   1 
ATOM   693  O O   . ARG   B 2 55  ? -32.459 10.352  -6.054  1.00 66.89  ? 64  ARG   B O   1 
ATOM   694  C CB  . ARG   B 2 55  ? -31.654 13.190  -4.965  1.00 70.97  ? 64  ARG   B CB  1 
ATOM   695  C CG  . ARG   B 2 55  ? -30.371 12.984  -4.183  1.00 74.20  ? 64  ARG   B CG  1 
ATOM   696  C CD  . ARG   B 2 55  ? -30.578 13.401  -2.732  1.00 78.31  ? 64  ARG   B CD  1 
ATOM   697  N NE  . ARG   B 2 55  ? -29.414 13.100  -1.901  1.00 81.69  ? 64  ARG   B NE  1 
ATOM   698  C CZ  . ARG   B 2 55  ? -28.639 14.016  -1.324  1.00 84.32  ? 64  ARG   B CZ  1 
ATOM   699  N NH1 . ARG   B 2 55  ? -28.905 15.309  -1.471  1.00 84.00  ? 64  ARG   B NH1 1 
ATOM   700  N NH2 . ARG   B 2 55  ? -27.595 13.645  -0.592  1.00 84.17  ? 64  ARG   B NH2 1 
ATOM   701  N N   . LEU   B 2 56  ? -30.322 10.599  -6.696  1.00 63.59  ? 65  LEU   B N   1 
ATOM   702  C CA  . LEU   B 2 56  ? -29.996 9.187   -6.637  1.00 61.48  ? 65  LEU   B CA  1 
ATOM   703  C C   . LEU   B 2 56  ? -29.041 9.033   -5.457  1.00 58.97  ? 65  LEU   B C   1 
ATOM   704  O O   . LEU   B 2 56  ? -27.945 9.596   -5.468  1.00 58.64  ? 65  LEU   B O   1 
ATOM   705  C CB  . LEU   B 2 56  ? -29.276 8.686   -7.927  1.00 61.40  ? 65  LEU   B CB  1 
ATOM   706  C CG  . LEU   B 2 56  ? -29.901 8.932   -9.305  1.00 62.98  ? 65  LEU   B CG  1 
ATOM   707  C CD1 . LEU   B 2 56  ? -29.224 8.045   -10.362 1.00 63.54  ? 65  LEU   B CD1 1 
ATOM   708  C CD2 . LEU   B 2 56  ? -31.409 8.659   -9.314  1.00 63.37  ? 65  LEU   B CD2 1 
ATOM   709  N N   . ASP   B 2 57  ? -29.446 8.281   -4.442  1.00 57.44  ? 66  ASP   B N   1 
ATOM   710  C CA  . ASP   B 2 57  ? -28.597 8.014   -3.290  1.00 56.32  ? 66  ASP   B CA  1 
ATOM   711  C C   . ASP   B 2 57  ? -27.876 6.667   -3.461  1.00 54.40  ? 66  ASP   B C   1 
ATOM   712  O O   . ASP   B 2 57  ? -28.462 5.715   -3.992  1.00 54.67  ? 66  ASP   B O   1 
ATOM   713  C CB  . ASP   B 2 57  ? -29.449 7.954   -2.021  1.00 60.00  ? 66  ASP   B CB  1 
ATOM   714  C CG  . ASP   B 2 57  ? -30.168 9.246   -1.715  1.00 68.76  ? 66  ASP   B CG  1 
ATOM   715  O OD1 . ASP   B 2 57  ? -29.614 10.313  -2.026  1.00 70.86  ? 66  ASP   B OD1 1 
ATOM   716  O OD2 . ASP   B 2 57  ? -31.293 9.186   -1.168  1.00 71.81  ? 66  ASP   B OD2 1 
ATOM   717  N N   . PRO   B 2 58  ? -26.613 6.543   -3.007  1.00 52.92  ? 67  PRO   B N   1 
ATOM   718  C CA  . PRO   B 2 58  ? -25.952 5.226   -3.066  1.00 52.04  ? 67  PRO   B CA  1 
ATOM   719  C C   . PRO   B 2 58  ? -26.710 4.193   -2.216  1.00 51.46  ? 67  PRO   B C   1 
ATOM   720  O O   . PRO   B 2 58  ? -27.378 4.549   -1.234  1.00 52.42  ? 67  PRO   B O   1 
ATOM   721  C CB  . PRO   B 2 58  ? -24.550 5.501   -2.510  1.00 53.04  ? 67  PRO   B CB  1 
ATOM   722  C CG  . PRO   B 2 58  ? -24.696 6.702   -1.655  1.00 53.87  ? 67  PRO   B CG  1 
ATOM   723  C CD  . PRO   B 2 58  ? -25.783 7.541   -2.302  1.00 52.58  ? 67  PRO   B CD  1 
ATOM   724  N N   . TYR   B 2 59  ? -26.655 2.924   -2.620  1.00 49.99  ? 68  TYR   B N   1 
ATOM   725  C CA  . TYR   B 2 59  ? -27.335 1.823   -1.949  1.00 49.29  ? 68  TYR   B CA  1 
ATOM   726  C C   . TYR   B 2 59  ? -26.311 0.774   -1.495  1.00 48.51  ? 68  TYR   B C   1 
ATOM   727  O O   . TYR   B 2 59  ? -26.403 0.271   -0.398  1.00 48.05  ? 68  TYR   B O   1 
ATOM   728  C CB  . TYR   B 2 59  ? -28.365 1.181   -2.907  1.00 48.93  ? 68  TYR   B CB  1 
ATOM   729  C CG  . TYR   B 2 59  ? -29.196 0.074   -2.282  1.00 48.84  ? 68  TYR   B CG  1 
ATOM   730  C CD1 . TYR   B 2 59  ? -28.713 -1.230  -2.208  1.00 48.65  ? 68  TYR   B CD1 1 
ATOM   731  C CD2 . TYR   B 2 59  ? -30.488 0.317   -1.832  1.00 49.94  ? 68  TYR   B CD2 1 
ATOM   732  C CE1 . TYR   B 2 59  ? -29.485 -2.255  -1.686  1.00 49.21  ? 68  TYR   B CE1 1 
ATOM   733  C CE2 . TYR   B 2 59  ? -31.269 -0.701  -1.301  1.00 50.51  ? 68  TYR   B CE2 1 
ATOM   734  C CZ  . TYR   B 2 59  ? -30.767 -1.990  -1.248  1.00 51.36  ? 68  TYR   B CZ  1 
ATOM   735  O OH  . TYR   B 2 59  ? -31.523 -2.991  -0.698  1.00 54.41  ? 68  TYR   B OH  1 
ATOM   736  N N   . TRP   B 2 60  ? -25.389 0.394   -2.367  1.00 47.82  ? 69  TRP   B N   1 
ATOM   737  C CA  . TRP   B 2 60  ? -24.349 -0.598  -2.048  1.00 46.71  ? 69  TRP   B CA  1 
ATOM   738  C C   . TRP   B 2 60  ? -23.049 -0.122  -2.656  1.00 46.44  ? 69  TRP   B C   1 
ATOM   739  O O   . TRP   B 2 60  ? -23.058 0.422   -3.765  1.00 46.25  ? 69  TRP   B O   1 
ATOM   740  C CB  . TRP   B 2 60  ? -24.722 -1.991  -2.601  1.00 45.99  ? 69  TRP   B CB  1 
ATOM   741  C CG  . TRP   B 2 60  ? -23.588 -2.981  -2.575  1.00 47.06  ? 69  TRP   B CG  1 
ATOM   742  C CD1 . TRP   B 2 60  ? -23.153 -3.705  -1.497  1.00 48.66  ? 69  TRP   B CD1 1 
ATOM   743  C CD2 . TRP   B 2 60  ? -22.675 -3.258  -3.642  1.00 47.25  ? 69  TRP   B CD2 1 
ATOM   744  N NE1 . TRP   B 2 60  ? -22.029 -4.426  -1.835  1.00 48.73  ? 69  TRP   B NE1 1 
ATOM   745  C CE2 . TRP   B 2 60  ? -21.716 -4.171  -3.147  1.00 48.27  ? 69  TRP   B CE2 1 
ATOM   746  C CE3 . TRP   B 2 60  ? -22.542 -2.785  -4.960  1.00 48.21  ? 69  TRP   B CE3 1 
ATOM   747  C CZ2 . TRP   B 2 60  ? -20.658 -4.637  -3.933  1.00 48.53  ? 69  TRP   B CZ2 1 
ATOM   748  C CZ3 . TRP   B 2 60  ? -21.520 -3.280  -5.749  1.00 48.80  ? 69  TRP   B CZ3 1 
ATOM   749  C CH2 . TRP   B 2 60  ? -20.588 -4.188  -5.232  1.00 48.65  ? 69  TRP   B CH2 1 
ATOM   750  N N   . GLY   B 2 61  ? -21.933 -0.426  -2.006  1.00 46.82  ? 70  GLY   B N   1 
ATOM   751  C CA  . GLY   B 2 61  ? -20.633 -0.104  -2.589  1.00 47.63  ? 70  GLY   B CA  1 
ATOM   752  C C   . GLY   B 2 61  ? -19.510 -0.904  -1.991  1.00 47.87  ? 70  GLY   B C   1 
ATOM   753  O O   . GLY   B 2 61  ? -19.623 -1.351  -0.844  1.00 47.31  ? 70  GLY   B O   1 
ATOM   754  N N   . ASP   B 2 62  ? -18.399 -1.042  -2.721  1.00 47.81  ? 71  ASP   B N   1 
ATOM   755  C CA  . ASP   B 2 62  ? -17.226 -1.733  -2.195  1.00 49.81  ? 71  ASP   B CA  1 
ATOM   756  C C   . ASP   B 2 62  ? -15.990 -1.212  -2.911  1.00 50.57  ? 71  ASP   B C   1 
ATOM   757  O O   . ASP   B 2 62  ? -15.910 -1.297  -4.140  1.00 50.85  ? 71  ASP   B O   1 
ATOM   758  C CB  . ASP   B 2 62  ? -17.356 -3.260  -2.323  1.00 53.12  ? 71  ASP   B CB  1 
ATOM   759  C CG  . ASP   B 2 62  ? -16.252 -4.028  -1.627  1.00 60.28  ? 71  ASP   B CG  1 
ATOM   760  O OD1 . ASP   B 2 62  ? -15.303 -4.433  -2.297  1.00 62.55  ? 71  ASP   B OD1 1 
ATOM   761  O OD2 . ASP   B 2 62  ? -16.350 -4.231  -0.418  1.00 65.57  ? 71  ASP   B OD2 1 
ATOM   762  N N   . VAL   B 2 63  ? -15.066 -0.599  -2.161  1.00 50.47  ? 72  VAL   B N   1 
ATOM   763  C CA  . VAL   B 2 63  ? -13.832 -0.031  -2.710  1.00 51.00  ? 72  VAL   B CA  1 
ATOM   764  C C   . VAL   B 2 63  ? -12.947 -1.113  -3.328  1.00 51.64  ? 72  VAL   B C   1 
ATOM   765  O O   . VAL   B 2 63  ? -12.360 -0.885  -4.394  1.00 52.82  ? 72  VAL   B O   1 
ATOM   766  C CB  . VAL   B 2 63  ? -13.107 0.834   -1.629  1.00 52.00  ? 72  VAL   B CB  1 
ATOM   767  C CG1 . VAL   B 2 63  ? -11.607 0.951   -1.876  1.00 52.67  ? 72  VAL   B CG1 1 
ATOM   768  C CG2 . VAL   B 2 63  ? -13.740 2.217   -1.543  1.00 52.35  ? 72  VAL   B CG2 1 
ATOM   769  N N   . LYS   B 2 64  ? -12.884 -2.292  -2.711  1.00 51.62  ? 73  LYS   B N   1 
ATOM   770  C CA  . LYS   B 2 64  ? -12.051 -3.366  -3.255  1.00 51.85  ? 73  LYS   B CA  1 
ATOM   771  C C   . LYS   B 2 64  ? -12.569 -3.885  -4.598  1.00 51.47  ? 73  LYS   B C   1 
ATOM   772  O O   . LYS   B 2 64  ? -11.779 -4.091  -5.514  1.00 51.36  ? 73  LYS   B O   1 
ATOM   773  C CB  . LYS   B 2 64  ? -11.817 -4.509  -2.256  1.00 52.31  ? 73  LYS   B CB  1 
ATOM   774  C CG  . LYS   B 2 64  ? -10.753 -5.458  -2.811  1.00 55.43  ? 73  LYS   B CG  1 
ATOM   775  C CD  . LYS   B 2 64  ? -10.273 -6.465  -1.825  1.00 59.13  ? 73  LYS   B CD  1 
ATOM   776  C CE  . LYS   B 2 64  ? -9.401  -7.455  -2.542  1.00 63.66  ? 73  LYS   B CE  1 
ATOM   777  N NZ  . LYS   B 2 64  ? -8.750  -8.379  -1.581  1.00 66.97  ? 73  LYS   B NZ  1 
ATOM   778  N N   . GLN   B 2 65  ? -13.895 -4.063  -4.737  1.00 51.45  ? 74  GLN   B N   1 
ATOM   779  C CA  . GLN   B 2 65  ? -14.453 -4.453  -6.042  1.00 51.29  ? 74  GLN   B CA  1 
ATOM   780  C C   . GLN   B 2 65  ? -14.501 -3.283  -7.044  1.00 49.89  ? 74  GLN   B C   1 
ATOM   781  O O   . GLN   B 2 65  ? -14.592 -3.514  -8.253  1.00 49.23  ? 74  GLN   B O   1 
ATOM   782  C CB  . GLN   B 2 65  ? -15.816 -5.130  -5.913  1.00 54.41  ? 74  GLN   B CB  1 
ATOM   783  C CG  . GLN   B 2 65  ? -15.843 -6.339  -4.973  1.00 61.94  ? 74  GLN   B CG  1 
ATOM   784  C CD  . GLN   B 2 65  ? -14.636 -7.281  -5.037  1.00 72.71  ? 74  GLN   B CD  1 
ATOM   785  O OE1 . GLN   B 2 65  ? -13.983 -7.569  -4.001  1.00 75.74  ? 74  GLN   B OE1 1 
ATOM   786  N NE2 . GLN   B 2 65  ? -14.315 -7.794  -6.244  1.00 74.98  ? 74  GLN   B NE2 1 
ATOM   787  N N   . ASP   B 2 66  ? -14.426 -2.039  -6.519  1.00 48.98  ? 75  ASP   B N   1 
ATOM   788  C CA  . ASP   B 2 66  ? -14.472 -0.772  -7.231  1.00 47.98  ? 75  ASP   B CA  1 
ATOM   789  C C   . ASP   B 2 66  ? -15.836 -0.625  -7.916  1.00 47.40  ? 75  ASP   B C   1 
ATOM   790  O O   . ASP   B 2 66  ? -15.894 -0.190  -9.069  1.00 46.58  ? 75  ASP   B O   1 
ATOM   791  C CB  . ASP   B 2 66  ? -13.309 -0.621  -8.262  1.00 48.73  ? 75  ASP   B CB  1 
ATOM   792  C CG  . ASP   B 2 66  ? -13.224 0.776   -8.842  1.00 49.55  ? 75  ASP   B CG  1 
ATOM   793  O OD1 . ASP   B 2 66  ? -13.622 1.725   -8.148  1.00 47.39  ? 75  ASP   B OD1 1 
ATOM   794  O OD2 . ASP   B 2 66  ? -12.803 0.913   -10.021 1.00 50.75  ? 75  ASP   B OD2 1 
ATOM   795  N N   . LEU   B 2 67  ? -16.924 -0.973  -7.221  1.00 46.08  ? 76  LEU   B N   1 
ATOM   796  C CA  . LEU   B 2 67  ? -18.277 -0.846  -7.766  1.00 46.10  ? 76  LEU   B CA  1 
ATOM   797  C C   . LEU   B 2 67  ? -19.197 -0.139  -6.764  1.00 46.93  ? 76  LEU   B C   1 
ATOM   798  O O   . LEU   B 2 67  ? -18.948 -0.157  -5.548  1.00 47.10  ? 76  LEU   B O   1 
ATOM   799  C CB  . LEU   B 2 67  ? -18.839 -2.238  -8.045  1.00 45.94  ? 76  LEU   B CB  1 
ATOM   800  C CG  . LEU   B 2 67  ? -18.097 -3.004  -9.129  1.00 47.56  ? 76  LEU   B CG  1 
ATOM   801  C CD1 . LEU   B 2 67  ? -18.526 -4.426  -9.143  1.00 48.70  ? 76  LEU   B CD1 1 
ATOM   802  C CD2 . LEU   B 2 67  ? -18.264 -2.321  -10.489 1.00 47.78  ? 76  LEU   B CD2 1 
ATOM   803  N N   . VAL   B 2 68  ? -20.276 0.459   -7.281  1.00 46.25  ? 77  VAL   B N   1 
ATOM   804  C CA  . VAL   B 2 68  ? -21.286 1.138   -6.472  1.00 46.52  ? 77  VAL   B CA  1 
ATOM   805  C C   . VAL   B 2 68  ? -22.617 1.084   -7.239  1.00 45.46  ? 77  VAL   B C   1 
ATOM   806  O O   . VAL   B 2 68  ? -22.649 1.160   -8.477  1.00 44.02  ? 77  VAL   B O   1 
ATOM   807  C CB  . VAL   B 2 68  ? -20.860 2.603   -6.085  1.00 47.47  ? 77  VAL   B CB  1 
ATOM   808  C CG1 . VAL   B 2 68  ? -20.560 3.439   -7.341  1.00 48.06  ? 77  VAL   B CG1 1 
ATOM   809  C CG2 . VAL   B 2 68  ? -21.894 3.296   -5.192  1.00 48.08  ? 77  VAL   B CG2 1 
ATOM   810  N N   . SER   B 2 69  ? -23.709 0.929   -6.506  1.00 45.27  ? 78  SER   B N   1 
ATOM   811  C CA  . SER   B 2 69  ? -25.044 0.925   -7.087  1.00 46.12  ? 78  SER   B CA  1 
ATOM   812  C C   . SER   B 2 69  ? -25.879 1.973   -6.366  1.00 46.53  ? 78  SER   B C   1 
ATOM   813  O O   . SER   B 2 69  ? -25.659 2.260   -5.161  1.00 45.59  ? 78  SER   B O   1 
ATOM   814  C CB  . SER   B 2 69  ? -25.692 -0.456  -7.003  1.00 48.11  ? 78  SER   B CB  1 
ATOM   815  O OG  . SER   B 2 69  ? -26.078 -0.794  -5.678  1.00 51.72  ? 78  SER   B OG  1 
ATOM   816  N N   . TYR   B 2 70  ? -26.851 2.536   -7.099  1.00 46.79  ? 79  TYR   B N   1 
ATOM   817  C CA  . TYR   B 2 70  ? -27.726 3.611   -6.613  1.00 48.05  ? 79  TYR   B CA  1 
ATOM   818  C C   . TYR   B 2 70  ? -29.176 3.197   -6.767  1.00 49.08  ? 79  TYR   B C   1 
ATOM   819  O O   . TYR   B 2 70  ? -29.522 2.580   -7.792  1.00 49.40  ? 79  TYR   B O   1 
ATOM   820  C CB  . TYR   B 2 70  ? -27.487 4.886   -7.456  1.00 48.03  ? 79  TYR   B CB  1 
ATOM   821  C CG  . TYR   B 2 70  ? -26.149 5.552   -7.197  1.00 48.32  ? 79  TYR   B CG  1 
ATOM   822  C CD1 . TYR   B 2 70  ? -24.974 5.046   -7.745  1.00 48.12  ? 79  TYR   B CD1 1 
ATOM   823  C CD2 . TYR   B 2 70  ? -26.060 6.684   -6.405  1.00 49.80  ? 79  TYR   B CD2 1 
ATOM   824  C CE1 . TYR   B 2 70  ? -23.743 5.637   -7.480  1.00 49.01  ? 79  TYR   B CE1 1 
ATOM   825  C CE2 . TYR   B 2 70  ? -24.835 7.266   -6.110  1.00 50.38  ? 79  TYR   B CE2 1 
ATOM   826  C CZ  . TYR   B 2 70  ? -23.679 6.742   -6.651  1.00 50.09  ? 79  TYR   B CZ  1 
ATOM   827  O OH  . TYR   B 2 70  ? -22.487 7.332   -6.323  1.00 51.09  ? 79  TYR   B OH  1 
ATOM   828  N N   . CYS   B 2 71  ? -30.019 3.518   -5.747  1.00 49.17  ? 80  CYS   B N   1 
ATOM   829  C CA  . CYS   B 2 71  ? -31.476 3.295   -5.689  1.00 50.66  ? 80  CYS   B CA  1 
ATOM   830  C C   . CYS   B 2 71  ? -31.874 1.852   -5.375  1.00 51.00  ? 80  CYS   B C   1 
ATOM   831  O O   . CYS   B 2 71  ? -33.018 1.608   -5.003  1.00 52.62  ? 80  CYS   B O   1 
ATOM   832  C CB  . CYS   B 2 71  ? -32.183 3.804   -6.947  1.00 53.27  ? 80  CYS   B CB  1 
ATOM   833  S SG  . CYS   B 2 71  ? -31.639 5.451   -7.494  1.00 60.19  ? 80  CYS   B SG  1 
ATOM   834  N N   . GLY   B 2 72  ? -30.948 0.918   -5.500  1.00 49.38  ? 81  GLY   B N   1 
ATOM   835  C CA  . GLY   B 2 72  ? -31.229 -0.478  -5.227  1.00 48.82  ? 81  GLY   B CA  1 
ATOM   836  C C   . GLY   B 2 72  ? -29.985 -1.333  -5.311  1.00 47.95  ? 81  GLY   B C   1 
ATOM   837  O O   . GLY   B 2 72  ? -28.878 -0.836  -5.544  1.00 47.27  ? 81  GLY   B O   1 
ATOM   838  N N   . PRO   B 2 73  ? -30.159 -2.635  -5.063  1.00 47.71  ? 82  PRO   B N   1 
ATOM   839  C CA  . PRO   B 2 73  ? -29.009 -3.541  -5.099  1.00 48.05  ? 82  PRO   B CA  1 
ATOM   840  C C   . PRO   B 2 73  ? -28.510 -3.813  -6.516  1.00 48.28  ? 82  PRO   B C   1 
ATOM   841  O O   . PRO   B 2 73  ? -29.279 -3.684  -7.477  1.00 47.56  ? 82  PRO   B O   1 
ATOM   842  C CB  . PRO   B 2 73  ? -29.540 -4.817  -4.433  1.00 49.13  ? 82  PRO   B CB  1 
ATOM   843  C CG  . PRO   B 2 73  ? -31.007 -4.789  -4.677  1.00 49.52  ? 82  PRO   B CG  1 
ATOM   844  C CD  . PRO   B 2 73  ? -31.412 -3.338  -4.720  1.00 47.79  ? 82  PRO   B CD  1 
ATOM   845  N N   . TRP   B 2 74  ? -27.224 -4.214  -6.647  1.00 48.42  ? 83  TRP   B N   1 
ATOM   846  C CA  . TRP   B 2 74  ? -26.587 -4.533  -7.927  1.00 49.02  ? 83  TRP   B CA  1 
ATOM   847  C C   . TRP   B 2 74  ? -27.441 -5.552  -8.709  1.00 50.48  ? 83  TRP   B C   1 
ATOM   848  O O   . TRP   B 2 74  ? -27.845 -6.569  -8.140  1.00 50.41  ? 83  TRP   B O   1 
ATOM   849  C CB  . TRP   B 2 74  ? -25.160 -5.062  -7.672  1.00 48.48  ? 83  TRP   B CB  1 
ATOM   850  C CG  . TRP   B 2 74  ? -24.357 -5.256  -8.931  1.00 47.41  ? 83  TRP   B CG  1 
ATOM   851  C CD1 . TRP   B 2 74  ? -24.317 -6.367  -9.717  1.00 47.51  ? 83  TRP   B CD1 1 
ATOM   852  C CD2 . TRP   B 2 74  ? -23.486 -4.293  -9.547  1.00 47.14  ? 83  TRP   B CD2 1 
ATOM   853  N NE1 . TRP   B 2 74  ? -23.471 -6.160  -10.784 1.00 47.87  ? 83  TRP   B NE1 1 
ATOM   854  C CE2 . TRP   B 2 74  ? -22.963 -4.886  -10.713 1.00 47.68  ? 83  TRP   B CE2 1 
ATOM   855  C CE3 . TRP   B 2 74  ? -23.127 -2.968  -9.241  1.00 47.15  ? 83  TRP   B CE3 1 
ATOM   856  C CZ2 . TRP   B 2 74  ? -22.125 -4.193  -11.592 1.00 48.10  ? 83  TRP   B CZ2 1 
ATOM   857  C CZ3 . TRP   B 2 74  ? -22.254 -2.305  -10.079 1.00 47.58  ? 83  TRP   B CZ3 1 
ATOM   858  C CH2 . TRP   B 2 74  ? -21.765 -2.912  -11.244 1.00 48.03  ? 83  TRP   B CH2 1 
ATOM   859  N N   . LYS   B 2 75  ? -27.797 -5.215  -9.973  1.00 51.34  ? 84  LYS   B N   1 
ATOM   860  C CA  . LYS   B 2 75  ? -28.699 -6.003  -10.807 1.00 52.52  ? 84  LYS   B CA  1 
ATOM   861  C C   . LYS   B 2 75  ? -28.009 -6.809  -11.904 1.00 53.97  ? 84  LYS   B C   1 
ATOM   862  O O   . LYS   B 2 75  ? -28.640 -7.693  -12.470 1.00 54.97  ? 84  LYS   B O   1 
ATOM   863  C CB  . LYS   B 2 75  ? -29.724 -5.071  -11.484 1.00 54.14  ? 84  LYS   B CB  1 
ATOM   864  C CG  . LYS   B 2 75  ? -30.599 -4.241  -10.540 1.00 55.86  ? 84  LYS   B CG  1 
ATOM   865  C CD  . LYS   B 2 75  ? -31.607 -5.106  -9.805  1.00 58.03  ? 84  LYS   B CD  1 
ATOM   866  C CE  . LYS   B 2 75  ? -32.413 -4.286  -8.838  1.00 61.27  ? 84  LYS   B CE  1 
ATOM   867  N NZ  . LYS   B 2 75  ? -33.534 -5.054  -8.233  1.00 64.38  ? 84  LYS   B NZ  1 
ATOM   868  N N   . LEU   B 2 76  ? -26.763 -6.480  -12.255 1.00 53.77  ? 85  LEU   B N   1 
ATOM   869  C CA  . LEU   B 2 76  ? -26.078 -7.108  -13.386 1.00 54.63  ? 85  LEU   B CA  1 
ATOM   870  C C   . LEU   B 2 76  ? -25.399 -8.409  -12.984 1.00 56.34  ? 85  LEU   B C   1 
ATOM   871  O O   . LEU   B 2 76  ? -24.514 -8.379  -12.143 1.00 55.75  ? 85  LEU   B O   1 
ATOM   872  C CB  . LEU   B 2 76  ? -25.065 -6.123  -14.012 1.00 54.09  ? 85  LEU   B CB  1 
ATOM   873  C CG  . LEU   B 2 76  ? -25.512 -4.650  -14.132 1.00 54.58  ? 85  LEU   B CG  1 
ATOM   874  C CD1 . LEU   B 2 76  ? -24.448 -3.783  -14.747 1.00 55.28  ? 85  LEU   B CD1 1 
ATOM   875  C CD2 . LEU   B 2 76  ? -26.763 -4.522  -14.918 1.00 54.91  ? 85  LEU   B CD2 1 
ATOM   876  N N   . ASP   B 2 77  ? -25.810 -9.550  -13.579 1.00 58.47  ? 86  ASP   B N   1 
ATOM   877  C CA  . ASP   B 2 77  ? -25.239 -10.854 -13.214 1.00 61.52  ? 86  ASP   B CA  1 
ATOM   878  C C   . ASP   B 2 77  ? -24.654 -11.675 -14.368 1.00 62.47  ? 86  ASP   B C   1 
ATOM   879  O O   . ASP   B 2 77  ? -24.115 -12.757 -14.109 1.00 62.83  ? 86  ASP   B O   1 
ATOM   880  C CB  . ASP   B 2 77  ? -26.254 -11.711 -12.438 1.00 65.70  ? 86  ASP   B CB  1 
ATOM   881  C CG  . ASP   B 2 77  ? -27.590 -11.920 -13.131 1.00 75.07  ? 86  ASP   B CG  1 
ATOM   882  O OD1 . ASP   B 2 77  ? -27.773 -11.390 -14.252 1.00 77.09  ? 86  ASP   B OD1 1 
ATOM   883  O OD2 . ASP   B 2 77  ? -28.454 -12.617 -12.555 1.00 79.21  ? 86  ASP   B OD2 1 
ATOM   884  N N   . ALA   B 2 78  ? -24.729 -11.179 -15.619 1.00 62.22  ? 87  ALA   B N   1 
ATOM   885  C CA  . ALA   B 2 78  ? -24.152 -11.913 -16.735 1.00 62.63  ? 87  ALA   B CA  1 
ATOM   886  C C   . ALA   B 2 78  ? -22.622 -11.973 -16.591 1.00 62.99  ? 87  ALA   B C   1 
ATOM   887  O O   . ALA   B 2 78  ? -22.003 -11.056 -16.022 1.00 62.82  ? 87  ALA   B O   1 
ATOM   888  C CB  . ALA   B 2 78  ? -24.546 -11.287 -18.063 1.00 62.32  ? 87  ALA   B CB  1 
ATOM   889  N N   . ALA   B 2 79  ? -22.027 -13.079 -17.064 1.00 62.45  ? 88  ALA   B N   1 
ATOM   890  C CA  . ALA   B 2 79  ? -20.592 -13.276 -17.009 1.00 63.15  ? 88  ALA   B CA  1 
ATOM   891  C C   . ALA   B 2 79  ? -20.012 -13.579 -18.392 1.00 63.84  ? 88  ALA   B C   1 
ATOM   892  O O   . ALA   B 2 79  ? -20.682 -14.201 -19.210 1.00 63.27  ? 88  ALA   B O   1 
ATOM   893  C CB  . ALA   B 2 79  ? -20.276 -14.437 -16.079 1.00 63.36  ? 88  ALA   B CB  1 
ATOM   894  N N   . TRP   B 2 80  ? -18.742 -13.203 -18.634 1.00 65.08  ? 89  TRP   B N   1 
ATOM   895  C CA  . TRP   B 2 80  ? -18.045 -13.543 -19.877 1.00 67.30  ? 89  TRP   B CA  1 
ATOM   896  C C   . TRP   B 2 80  ? -17.890 -15.082 -19.907 1.00 69.05  ? 89  TRP   B C   1 
ATOM   897  O O   . TRP   B 2 80  ? -17.590 -15.668 -18.867 1.00 67.92  ? 89  TRP   B O   1 
ATOM   898  C CB  . TRP   B 2 80  ? -16.670 -12.854 -19.934 1.00 67.49  ? 89  TRP   B CB  1 
ATOM   899  C CG  . TRP   B 2 80  ? -15.859 -13.223 -21.145 1.00 68.37  ? 89  TRP   B CG  1 
ATOM   900  C CD1 . TRP   B 2 80  ? -16.279 -13.248 -22.445 1.00 69.51  ? 89  TRP   B CD1 1 
ATOM   901  C CD2 . TRP   B 2 80  ? -14.485 -13.636 -21.159 1.00 68.44  ? 89  TRP   B CD2 1 
ATOM   902  N NE1 . TRP   B 2 80  ? -15.249 -13.638 -23.267 1.00 69.78  ? 89  TRP   B NE1 1 
ATOM   903  C CE2 . TRP   B 2 80  ? -14.139 -13.899 -22.500 1.00 69.26  ? 89  TRP   B CE2 1 
ATOM   904  C CE3 . TRP   B 2 80  ? -13.511 -13.801 -20.173 1.00 68.72  ? 89  TRP   B CE3 1 
ATOM   905  C CZ2 . TRP   B 2 80  ? -12.862 -14.314 -22.872 1.00 69.57  ? 89  TRP   B CZ2 1 
ATOM   906  C CZ3 . TRP   B 2 80  ? -12.251 -14.235 -20.545 1.00 69.63  ? 89  TRP   B CZ3 1 
ATOM   907  C CH2 . TRP   B 2 80  ? -11.936 -14.469 -21.884 1.00 69.58  ? 89  TRP   B CH2 1 
ATOM   908  N N   . ASP   B 2 81  ? -18.189 -15.738 -21.054 1.00 71.02  ? 90  ASP   B N   1 
ATOM   909  C CA  . ASP   B 2 81  ? -18.133 -17.209 -21.094 1.00 73.78  ? 90  ASP   B CA  1 
ATOM   910  C C   . ASP   B 2 81  ? -16.724 -17.806 -21.220 1.00 76.75  ? 90  ASP   B C   1 
ATOM   911  O O   . ASP   B 2 81  ? -16.589 -19.027 -21.213 1.00 77.73  ? 90  ASP   B O   1 
ATOM   912  C CB  . ASP   B 2 81  ? -19.056 -17.793 -22.168 1.00 75.29  ? 90  ASP   B CB  1 
ATOM   913  C CG  . ASP   B 2 81  ? -18.729 -17.412 -23.590 1.00 79.70  ? 90  ASP   B CG  1 
ATOM   914  O OD1 . ASP   B 2 81  ? -17.678 -16.763 -23.809 1.00 80.20  ? 90  ASP   B OD1 1 
ATOM   915  O OD2 . ASP   B 2 81  ? -19.529 -17.757 -24.496 1.00 82.58  ? 90  ASP   B OD2 1 
ATOM   916  N N   . GLY   B 2 82  ? -15.704 -16.956 -21.301 1.00 78.15  ? 91  GLY   B N   1 
ATOM   917  C CA  . GLY   B 2 82  ? -14.313 -17.369 -21.426 1.00 79.66  ? 91  GLY   B CA  1 
ATOM   918  C C   . GLY   B 2 82  ? -13.896 -17.733 -22.842 1.00 81.40  ? 91  GLY   B C   1 
ATOM   919  O O   . GLY   B 2 82  ? -12.757 -18.154 -23.052 1.00 82.05  ? 91  GLY   B O   1 
ATOM   920  N N   . LEU   B 2 83  ? -14.801 -17.601 -23.823 1.00 81.77  ? 92  LEU   B N   1 
ATOM   921  C CA  . LEU   B 2 83  ? -14.515 -17.987 -25.205 1.00 82.96  ? 92  LEU   B CA  1 
ATOM   922  C C   . LEU   B 2 83  ? -14.878 -16.969 -26.270 1.00 82.60  ? 92  LEU   B C   1 
ATOM   923  O O   . LEU   B 2 83  ? -14.126 -16.806 -27.230 1.00 83.20  ? 92  LEU   B O   1 
ATOM   924  C CB  . LEU   B 2 83  ? -15.236 -19.298 -25.534 1.00 84.34  ? 92  LEU   B CB  1 
ATOM   925  C CG  . LEU   B 2 83  ? -14.583 -20.531 -24.971 1.00 88.21  ? 92  LEU   B CG  1 
ATOM   926  C CD1 . LEU   B 2 83  ? -15.621 -21.552 -24.567 1.00 89.89  ? 92  LEU   B CD1 1 
ATOM   927  C CD2 . LEU   B 2 83  ? -13.583 -21.103 -25.957 1.00 89.00  ? 92  LEU   B CD2 1 
ATOM   928  N N   . SER   B 2 84  ? -16.064 -16.360 -26.175 1.00 81.59  ? 93  SER   B N   1 
ATOM   929  C CA  . SER   B 2 84  ? -16.547 -15.458 -27.215 1.00 80.95  ? 93  SER   B CA  1 
ATOM   930  C C   . SER   B 2 84  ? -16.027 -14.023 -27.128 1.00 79.22  ? 93  SER   B C   1 
ATOM   931  O O   . SER   B 2 84  ? -15.620 -13.551 -26.054 1.00 79.14  ? 93  SER   B O   1 
ATOM   932  C CB  . SER   B 2 84  ? -18.080 -15.440 -27.263 1.00 83.20  ? 93  SER   B CB  1 
ATOM   933  O OG  . SER   B 2 84  ? -18.699 -16.551 -26.633 1.00 86.35  ? 93  SER   B OG  1 
ATOM   934  N N   . GLU   B 2 85  ? -16.079 -13.320 -28.271 1.00 77.26  ? 94  GLU   B N   1 
ATOM   935  C CA  . GLU   B 2 85  ? -15.734 -11.909 -28.337 1.00 76.05  ? 94  GLU   B CA  1 
ATOM   936  C C   . GLU   B 2 85  ? -16.856 -11.103 -27.628 1.00 72.83  ? 94  GLU   B C   1 
ATOM   937  O O   . GLU   B 2 85  ? -17.974 -11.587 -27.423 1.00 72.90  ? 94  GLU   B O   1 
ATOM   938  C CB  . GLU   B 2 85  ? -15.538 -11.428 -29.806 1.00 79.63  ? 94  GLU   B CB  1 
ATOM   939  C CG  . GLU   B 2 85  ? -14.235 -11.913 -30.458 1.00 84.68  ? 94  GLU   B CG  1 
ATOM   940  C CD  . GLU   B 2 85  ? -13.809 -11.180 -31.723 1.00 91.21  ? 94  GLU   B CD  1 
ATOM   941  O OE1 . GLU   B 2 85  ? -14.679 -10.566 -32.385 1.00 91.87  ? 94  GLU   B OE1 1 
ATOM   942  O OE2 . GLU   B 2 85  ? -12.599 -11.211 -32.049 1.00 92.92  ? 94  GLU   B OE2 1 
ATOM   943  N N   . VAL   B 2 86  ? -16.525 -9.894  -27.213 1.00 69.37  ? 95  VAL   B N   1 
ATOM   944  C CA  . VAL   B 2 86  ? -17.439 -9.023  -26.479 1.00 65.90  ? 95  VAL   B CA  1 
ATOM   945  C C   . VAL   B 2 86  ? -17.386 -7.608  -27.058 1.00 64.15  ? 95  VAL   B C   1 
ATOM   946  O O   . VAL   B 2 86  ? -16.480 -7.287  -27.831 1.00 65.25  ? 95  VAL   B O   1 
ATOM   947  C CB  . VAL   B 2 86  ? -17.037 -9.007  -24.967 1.00 64.40  ? 95  VAL   B CB  1 
ATOM   948  C CG1 . VAL   B 2 86  ? -16.931 -10.416 -24.399 1.00 63.78  ? 95  VAL   B CG1 1 
ATOM   949  C CG2 . VAL   B 2 86  ? -15.732 -8.250  -24.759 1.00 64.21  ? 95  VAL   B CG2 1 
ATOM   950  N N   . GLN   B 2 87  ? -18.343 -6.748  -26.669 1.00 61.99  ? 96  GLN   B N   1 
ATOM   951  C CA  . GLN   B 2 87  ? -18.329 -5.368  -27.109 1.00 61.75  ? 96  GLN   B CA  1 
ATOM   952  C C   . GLN   B 2 87  ? -18.199 -4.393  -25.957 1.00 61.12  ? 96  GLN   B C   1 
ATOM   953  O O   . GLN   B 2 87  ? -18.948 -4.479  -25.010 1.00 61.94  ? 96  GLN   B O   1 
ATOM   954  C CB  . GLN   B 2 87  ? -19.538 -5.032  -28.006 1.00 62.34  ? 96  GLN   B CB  1 
ATOM   955  C CG  . GLN   B 2 87  ? -19.346 -5.620  -29.398 1.00 66.26  ? 96  GLN   B CG  1 
ATOM   956  C CD  . GLN   B 2 87  ? -20.431 -5.263  -30.376 1.00 72.45  ? 96  GLN   B CD  1 
ATOM   957  O OE1 . GLN   B 2 87  ? -21.339 -4.465  -30.109 1.00 72.25  ? 96  GLN   B OE1 1 
ATOM   958  N NE2 . GLN   B 2 87  ? -20.353 -5.853  -31.552 1.00 74.36  ? 96  GLN   B NE2 1 
ATOM   959  N N   . LEU   B 2 88  ? -17.237 -3.480  -26.041 1.00 59.96  ? 97  LEU   B N   1 
ATOM   960  C CA  . LEU   B 2 88  ? -17.112 -2.402  -25.096 1.00 59.81  ? 97  LEU   B CA  1 
ATOM   961  C C   . LEU   B 2 88  ? -17.992 -1.297  -25.672 1.00 59.16  ? 97  LEU   B C   1 
ATOM   962  O O   . LEU   B 2 88  ? -17.734 -0.819  -26.787 1.00 59.54  ? 97  LEU   B O   1 
ATOM   963  C CB  . LEU   B 2 88  ? -15.659 -1.893  -24.963 1.00 59.71  ? 97  LEU   B CB  1 
ATOM   964  C CG  . LEU   B 2 88  ? -15.524 -0.577  -24.153 1.00 60.41  ? 97  LEU   B CG  1 
ATOM   965  C CD1 . LEU   B 2 88  ? -16.045 -0.746  -22.698 1.00 59.80  ? 97  LEU   B CD1 1 
ATOM   966  C CD2 . LEU   B 2 88  ? -14.102 -0.052  -24.177 1.00 61.20  ? 97  LEU   B CD2 1 
ATOM   967  N N   . LEU   B 2 89  ? -19.042 -0.917  -24.942 1.00 58.37  ? 98  LEU   B N   1 
ATOM   968  C CA  . LEU   B 2 89  ? -19.891 0.175   -25.383 1.00 58.87  ? 98  LEU   B CA  1 
ATOM   969  C C   . LEU   B 2 89  ? -19.254 1.398   -24.748 1.00 60.23  ? 98  LEU   B C   1 
ATOM   970  O O   . LEU   B 2 89  ? -19.605 1.800   -23.636 1.00 60.73  ? 98  LEU   B O   1 
ATOM   971  C CB  . LEU   B 2 89  ? -21.366 -0.054  -25.016 1.00 58.46  ? 98  LEU   B CB  1 
ATOM   972  C CG  . LEU   B 2 89  ? -22.391 1.124   -25.110 1.00 60.64  ? 98  LEU   B CG  1 
ATOM   973  C CD1 . LEU   B 2 89  ? -22.144 2.052   -26.264 1.00 61.21  ? 98  LEU   B CD1 1 
ATOM   974  C CD2 . LEU   B 2 89  ? -23.802 0.600   -25.155 1.00 61.64  ? 98  LEU   B CD2 1 
ATOM   975  N N   . ALA   B 2 90  ? -18.232 1.940   -25.443 1.00 60.37  ? 99  ALA   B N   1 
ATOM   976  C CA  . ALA   B 2 90  ? -17.478 3.064   -24.916 1.00 60.57  ? 99  ALA   B CA  1 
ATOM   977  C C   . ALA   B 2 90  ? -18.232 4.371   -25.033 1.00 60.63  ? 99  ALA   B C   1 
ATOM   978  O O   . ALA   B 2 90  ? -18.818 4.663   -26.083 1.00 59.83  ? 99  ALA   B O   1 
ATOM   979  C CB  . ALA   B 2 90  ? -16.135 3.178   -25.609 1.00 60.45  ? 99  ALA   B CB  1 
ATOM   980  N N   . VAL   B 2 91  ? -18.226 5.154   -23.932 1.00 60.06  ? 100 VAL   B N   1 
ATOM   981  C CA  . VAL   B 2 91  ? -18.840 6.477   -23.940 1.00 60.21  ? 100 VAL   B CA  1 
ATOM   982  C C   . VAL   B 2 91  ? -17.725 7.480   -23.571 1.00 60.98  ? 100 VAL   B C   1 
ATOM   983  O O   . VAL   B 2 91  ? -17.574 7.845   -22.406 1.00 60.68  ? 100 VAL   B O   1 
ATOM   984  C CB  . VAL   B 2 91  ? -20.081 6.545   -23.012 1.00 59.46  ? 100 VAL   B CB  1 
ATOM   985  C CG1 . VAL   B 2 91  ? -20.730 7.928   -23.050 1.00 59.27  ? 100 VAL   B CG1 1 
ATOM   986  C CG2 . VAL   B 2 91  ? -21.094 5.462   -23.380 1.00 59.11  ? 100 VAL   B CG2 1 
ATOM   987  N N   . PRO   B 2 92  ? -16.902 7.902   -24.558 1.00 61.73  ? 101 PRO   B N   1 
ATOM   988  C CA  . PRO   B 2 92  ? -15.784 8.804   -24.240 1.00 62.38  ? 101 PRO   B CA  1 
ATOM   989  C C   . PRO   B 2 92  ? -16.212 10.249  -24.002 1.00 63.84  ? 101 PRO   B C   1 
ATOM   990  O O   . PRO   B 2 92  ? -17.254 10.678  -24.484 1.00 63.97  ? 101 PRO   B O   1 
ATOM   991  C CB  . PRO   B 2 92  ? -14.830 8.654   -25.454 1.00 63.32  ? 101 PRO   B CB  1 
ATOM   992  C CG  . PRO   B 2 92  ? -15.469 7.636   -26.382 1.00 63.69  ? 101 PRO   B CG  1 
ATOM   993  C CD  . PRO   B 2 92  ? -16.924 7.551   -25.991 1.00 62.04  ? 101 PRO   B CD  1 
ATOM   994  N N   . PRO   B 2 93  ? -15.396 11.035  -23.285 1.00 65.02  ? 102 PRO   B N   1 
ATOM   995  C CA  . PRO   B 2 93  ? -15.774 12.431  -23.014 1.00 65.95  ? 102 PRO   B CA  1 
ATOM   996  C C   . PRO   B 2 93  ? -15.907 13.305  -24.268 1.00 67.02  ? 102 PRO   B C   1 
ATOM   997  O O   . PRO   B 2 93  ? -15.009 13.332  -25.110 1.00 67.36  ? 102 PRO   B O   1 
ATOM   998  C CB  . PRO   B 2 93  ? -14.674 12.909  -22.055 1.00 66.52  ? 102 PRO   B CB  1 
ATOM   999  C CG  . PRO   B 2 93  ? -14.120 11.614  -21.422 1.00 66.93  ? 102 PRO   B CG  1 
ATOM   1000 C CD  . PRO   B 2 93  ? -14.131 10.682  -22.613 1.00 65.14  ? 102 PRO   B CD  1 
ATOM   1001 N N   . GLY   B 2 94  ? -17.055 13.978  -24.394 1.00 67.01  ? 103 GLY   B N   1 
ATOM   1002 C CA  . GLY   B 2 94  ? -17.391 14.848  -25.519 1.00 66.98  ? 103 GLY   B CA  1 
ATOM   1003 C C   . GLY   B 2 94  ? -17.621 14.136  -26.848 1.00 67.22  ? 103 GLY   B C   1 
ATOM   1004 O O   . GLY   B 2 94  ? -17.746 14.774  -27.891 1.00 67.36  ? 103 GLY   B O   1 
ATOM   1005 N N   . GLU   B 2 95  ? -17.662 12.805  -26.832 1.00 67.46  ? 104 GLU   B N   1 
ATOM   1006 C CA  . GLU   B 2 95  ? -17.814 11.999  -28.044 1.00 68.00  ? 104 GLU   B CA  1 
ATOM   1007 C C   . GLU   B 2 95  ? -19.004 11.060  -27.903 1.00 68.03  ? 104 GLU   B C   1 
ATOM   1008 O O   . GLU   B 2 95  ? -19.392 10.696  -26.788 1.00 67.46  ? 104 GLU   B O   1 
ATOM   1009 C CB  . GLU   B 2 95  ? -16.525 11.182  -28.299 1.00 70.22  ? 104 GLU   B CB  1 
ATOM   1010 C CG  . GLU   B 2 95  ? -15.317 12.062  -28.575 1.00 75.65  ? 104 GLU   B CG  1 
ATOM   1011 C CD  . GLU   B 2 95  ? -13.965 11.374  -28.636 1.00 82.40  ? 104 GLU   B CD  1 
ATOM   1012 O OE1 . GLU   B 2 95  ? -13.899 10.142  -28.420 1.00 81.53  ? 104 GLU   B OE1 1 
ATOM   1013 O OE2 . GLU   B 2 95  ? -12.965 12.077  -28.913 1.00 86.35  ? 104 GLU   B OE2 1 
ATOM   1014 N N   . ARG   B 2 96  ? -19.587 10.669  -29.034 1.00 68.16  ? 105 ARG   B N   1 
ATOM   1015 C CA  . ARG   B 2 96  ? -20.755 9.798   -29.038 1.00 69.25  ? 105 ARG   B CA  1 
ATOM   1016 C C   . ARG   B 2 96  ? -20.421 8.379   -28.598 1.00 68.70  ? 105 ARG   B C   1 
ATOM   1017 O O   . ARG   B 2 96  ? -19.284 7.932   -28.767 1.00 68.96  ? 105 ARG   B O   1 
ATOM   1018 C CB  . ARG   B 2 96  ? -21.344 9.757   -30.456 1.00 72.92  ? 105 ARG   B CB  1 
ATOM   1019 C CG  . ARG   B 2 96  ? -22.845 9.466   -30.506 1.00 78.65  ? 105 ARG   B CG  1 
ATOM   1020 C CD  . ARG   B 2 96  ? -23.490 9.807   -31.848 1.00 83.16  ? 105 ARG   B CD  1 
ATOM   1021 N NE  . ARG   B 2 96  ? -22.722 9.325   -32.999 1.00 88.85  ? 105 ARG   B NE  1 
ATOM   1022 C CZ  . ARG   B 2 96  ? -22.125 10.120  -33.885 1.00 93.74  ? 105 ARG   B CZ  1 
ATOM   1023 N NH1 . ARG   B 2 96  ? -22.209 11.442  -33.767 1.00 93.59  ? 105 ARG   B NH1 1 
ATOM   1024 N NH2 . ARG   B 2 96  ? -21.445 9.599   -34.901 1.00 95.26  ? 105 ARG   B NH2 1 
ATOM   1025 N N   . ALA   B 2 97  ? -21.431 7.657   -28.053 1.00 67.46  ? 106 ALA   B N   1 
ATOM   1026 C CA  . ALA   B 2 97  ? -21.349 6.251   -27.670 1.00 66.80  ? 106 ALA   B CA  1 
ATOM   1027 C C   . ALA   B 2 97  ? -20.948 5.437   -28.906 1.00 66.66  ? 106 ALA   B C   1 
ATOM   1028 O O   . ALA   B 2 97  ? -21.458 5.687   -30.005 1.00 65.37  ? 106 ALA   B O   1 
ATOM   1029 C CB  . ALA   B 2 97  ? -22.699 5.776   -27.171 1.00 66.67  ? 106 ALA   B CB  1 
ATOM   1030 N N   . LYS   B 2 98  ? -20.018 4.489   -28.734 1.00 67.08  ? 107 LYS   B N   1 
ATOM   1031 C CA  . LYS   B 2 98  ? -19.494 3.718   -29.850 1.00 68.51  ? 107 LYS   B CA  1 
ATOM   1032 C C   . LYS   B 2 98  ? -19.125 2.302   -29.393 1.00 68.29  ? 107 LYS   B C   1 
ATOM   1033 O O   . LYS   B 2 98  ? -18.508 2.144   -28.331 1.00 68.94  ? 107 LYS   B O   1 
ATOM   1034 C CB  . LYS   B 2 98  ? -18.275 4.484   -30.381 1.00 72.76  ? 107 LYS   B CB  1 
ATOM   1035 C CG  . LYS   B 2 98  ? -17.442 3.819   -31.461 1.00 80.31  ? 107 LYS   B CG  1 
ATOM   1036 C CD  . LYS   B 2 98  ? -16.062 4.517   -31.574 1.00 86.61  ? 107 LYS   B CD  1 
ATOM   1037 C CE  . LYS   B 2 98  ? -15.392 4.734   -30.220 1.00 90.57  ? 107 LYS   B CE  1 
ATOM   1038 N NZ  . LYS   B 2 98  ? -13.926 4.961   -30.348 1.00 93.63  ? 107 LYS   B NZ  1 
ATOM   1039 N N   . ASN   B 2 99  ? -19.567 1.272   -30.143 1.00 66.94  ? 108 ASN   B N   1 
ATOM   1040 C CA  . ASN   B 2 99  ? -19.334 -0.138  -29.815 1.00 67.64  ? 108 ASN   B CA  1 
ATOM   1041 C C   . ASN   B 2 99  ? -18.014 -0.613  -30.414 1.00 68.40  ? 108 ASN   B C   1 
ATOM   1042 O O   . ASN   B 2 99  ? -17.776 -0.405  -31.605 1.00 68.98  ? 108 ASN   B O   1 
ATOM   1043 C CB  . ASN   B 2 99  ? -20.461 -1.022  -30.368 1.00 68.46  ? 108 ASN   B CB  1 
ATOM   1044 C CG  . ASN   B 2 99  ? -21.789 -0.900  -29.673 1.00 70.10  ? 108 ASN   B CG  1 
ATOM   1045 O OD1 . ASN   B 2 99  ? -22.441 0.144   -29.702 1.00 72.02  ? 108 ASN   B OD1 1 
ATOM   1046 N ND2 . ASN   B 2 99  ? -22.241 -1.979  -29.069 1.00 69.10  ? 108 ASN   B ND2 1 
ATOM   1047 N N   . ILE   B 2 100 ? -17.161 -1.238  -29.613 1.00 68.15  ? 109 ILE   B N   1 
ATOM   1048 C CA  . ILE   B 2 100 ? -15.871 -1.733  -30.083 1.00 68.98  ? 109 ILE   B CA  1 
ATOM   1049 C C   . ILE   B 2 100 ? -15.773 -3.197  -29.723 1.00 69.52  ? 109 ILE   B C   1 
ATOM   1050 O O   . ILE   B 2 100 ? -15.861 -3.547  -28.545 1.00 69.37  ? 109 ILE   B O   1 
ATOM   1051 C CB  . ILE   B 2 100 ? -14.711 -0.961  -29.427 1.00 70.00  ? 109 ILE   B CB  1 
ATOM   1052 C CG1 . ILE   B 2 100 ? -14.909 0.562   -29.488 1.00 71.42  ? 109 ILE   B CG1 1 
ATOM   1053 C CG2 . ILE   B 2 100 ? -13.381 -1.395  -30.003 1.00 70.53  ? 109 ILE   B CG2 1 
ATOM   1054 C CD1 . ILE   B 2 100 ? -14.835 1.160   -30.895 1.00 73.29  ? 109 ILE   B CD1 1 
ATOM   1055 N N   . GLN   B 2 101 ? -15.593 -4.058  -30.711 1.00 69.89  ? 110 GLN   B N   1 
ATOM   1056 C CA  . GLN   B 2 101 ? -15.527 -5.492  -30.485 1.00 71.10  ? 110 GLN   B CA  1 
ATOM   1057 C C   . GLN   B 2 101 ? -14.108 -5.933  -30.270 1.00 73.04  ? 110 GLN   B C   1 
ATOM   1058 O O   . GLN   B 2 101 ? -13.203 -5.421  -30.930 1.00 74.16  ? 110 GLN   B O   1 
ATOM   1059 C CB  . GLN   B 2 101 ? -16.129 -6.233  -31.674 1.00 72.80  ? 110 GLN   B CB  1 
ATOM   1060 C CG  . GLN   B 2 101 ? -16.396 -7.699  -31.413 1.00 75.40  ? 110 GLN   B CG  1 
ATOM   1061 C CD  . GLN   B 2 101 ? -17.368 -8.217  -32.432 1.00 79.22  ? 110 GLN   B CD  1 
ATOM   1062 O OE1 . GLN   B 2 101 ? -18.369 -7.564  -32.756 1.00 77.83  ? 110 GLN   B OE1 1 
ATOM   1063 N NE2 . GLN   B 2 101 ? -17.088 -9.399  -32.963 1.00 81.20  ? 110 GLN   B NE2 1 
ATOM   1064 N N   . THR   B 2 102 ? -13.904 -6.886  -29.343 1.00 72.93  ? 111 THR   B N   1 
ATOM   1065 C CA  . THR   B 2 102 ? -12.596 -7.430  -29.020 1.00 73.24  ? 111 THR   B CA  1 
ATOM   1066 C C   . THR   B 2 102 ? -12.742 -8.805  -28.366 1.00 74.18  ? 111 THR   B C   1 
ATOM   1067 O O   . THR   B 2 102 ? -13.827 -9.149  -27.892 1.00 75.51  ? 111 THR   B O   1 
ATOM   1068 C CB  . THR   B 2 102 ? -11.863 -6.462  -28.072 1.00 74.40  ? 111 THR   B CB  1 
ATOM   1069 O OG1 . THR   B 2 102 ? -10.492 -6.857  -27.949 1.00 75.84  ? 111 THR   B OG1 1 
ATOM   1070 C CG2 . THR   B 2 102 ? -12.536 -6.361  -26.687 1.00 74.36  ? 111 THR   B CG2 1 
ATOM   1071 N N   . LEU   B 2 103 ? -11.656 -9.595  -28.324 1.00 73.08  ? 112 LEU   B N   1 
ATOM   1072 C CA  . LEU   B 2 103 ? -11.670 -10.861 -27.604 1.00 72.76  ? 112 LEU   B CA  1 
ATOM   1073 C C   . LEU   B 2 103 ? -10.904 -10.577 -26.314 1.00 72.07  ? 112 LEU   B C   1 
ATOM   1074 O O   . LEU   B 2 103 ? -9.724  -10.213 -26.349 1.00 71.46  ? 112 LEU   B O   1 
ATOM   1075 C CB  . LEU   B 2 103 ? -10.980 -12.027 -28.356 1.00 72.73  ? 112 LEU   B CB  1 
ATOM   1076 C CG  . LEU   B 2 103 ? -10.929 -13.306 -27.498 1.00 74.56  ? 112 LEU   B CG  1 
ATOM   1077 C CD1 . LEU   B 2 103 ? -12.180 -14.095 -27.609 1.00 75.36  ? 112 LEU   B CD1 1 
ATOM   1078 C CD2 . LEU   B 2 103 ? -9.751  -14.136 -27.797 1.00 75.47  ? 112 LEU   B CD2 1 
ATOM   1079 N N   . PRO   B 2 104 ? -11.546 -10.772 -25.161 1.00 72.26  ? 113 PRO   B N   1 
ATOM   1080 C CA  . PRO   B 2 104 ? -10.864 -10.456 -23.907 1.00 72.10  ? 113 PRO   B CA  1 
ATOM   1081 C C   . PRO   B 2 104 ? -9.675  -11.350 -23.601 1.00 72.62  ? 113 PRO   B C   1 
ATOM   1082 O O   . PRO   B 2 104 ? -9.672  -12.544 -23.877 1.00 73.19  ? 113 PRO   B O   1 
ATOM   1083 C CB  . PRO   B 2 104 ? -11.950 -10.627 -22.839 1.00 72.38  ? 113 PRO   B CB  1 
ATOM   1084 C CG  . PRO   B 2 104 ? -13.223 -10.612 -23.557 1.00 72.94  ? 113 PRO   B CG  1 
ATOM   1085 C CD  . PRO   B 2 104 ? -12.957 -11.137 -24.946 1.00 71.85  ? 113 PRO   B CD  1 
ATOM   1086 N N   . GLY   B 2 105 ? -8.673  -10.743 -23.006 1.00 72.46  ? 114 GLY   B N   1 
ATOM   1087 C CA  . GLY   B 2 105 ? -7.546  -11.444 -22.428 1.00 72.24  ? 114 GLY   B CA  1 
ATOM   1088 C C   . GLY   B 2 105 ? -7.908  -11.869 -21.008 1.00 72.60  ? 114 GLY   B C   1 
ATOM   1089 O O   . GLY   B 2 105 ? -9.092  -11.944 -20.654 1.00 72.37  ? 114 GLY   B O   1 
ATOM   1090 N N   . ILE   B 2 106 ? -6.900  -12.134 -20.177 1.00 72.66  ? 115 ILE   B N   1 
ATOM   1091 C CA  . ILE   B 2 106 ? -7.099  -12.619 -18.802 1.00 73.43  ? 115 ILE   B CA  1 
ATOM   1092 C C   . ILE   B 2 106 ? -6.250  -11.864 -17.762 1.00 72.99  ? 115 ILE   B C   1 
ATOM   1093 O O   . ILE   B 2 106 ? -5.117  -11.498 -18.035 1.00 74.04  ? 115 ILE   B O   1 
ATOM   1094 C CB  . ILE   B 2 106 ? -6.693  -14.129 -18.751 1.00 75.49  ? 115 ILE   B CB  1 
ATOM   1095 C CG1 . ILE   B 2 106 ? -7.484  -15.003 -19.740 1.00 78.36  ? 115 ILE   B CG1 1 
ATOM   1096 C CG2 . ILE   B 2 106 ? -6.757  -14.703 -17.359 1.00 75.98  ? 115 ILE   B CG2 1 
ATOM   1097 C CD1 . ILE   B 2 106 ? -8.950  -15.123 -19.418 1.00 80.68  ? 115 ILE   B CD1 1 
ATOM   1098 N N   . PHE   B 2 107 ? -6.779  -11.676 -16.562 1.00 71.51  ? 116 PHE   B N   1 
ATOM   1099 C CA  . PHE   B 2 107 ? -6.030  -11.148 -15.430 1.00 70.94  ? 116 PHE   B CA  1 
ATOM   1100 C C   . PHE   B 2 107 ? -5.930  -12.358 -14.520 1.00 71.08  ? 116 PHE   B C   1 
ATOM   1101 O O   . PHE   B 2 107 ? -6.956  -12.783 -14.001 1.00 71.22  ? 116 PHE   B O   1 
ATOM   1102 C CB  . PHE   B 2 107 ? -6.819  -10.060 -14.681 1.00 70.05  ? 116 PHE   B CB  1 
ATOM   1103 C CG  . PHE   B 2 107 ? -6.556  -8.624  -15.061 1.00 70.17  ? 116 PHE   B CG  1 
ATOM   1104 C CD1 . PHE   B 2 107 ? -5.798  -8.311  -16.178 1.00 70.73  ? 116 PHE   B CD1 1 
ATOM   1105 C CD2 . PHE   B 2 107 ? -7.123  -7.585  -14.339 1.00 70.97  ? 116 PHE   B CD2 1 
ATOM   1106 C CE1 . PHE   B 2 107 ? -5.594  -6.990  -16.553 1.00 71.42  ? 116 PHE   B CE1 1 
ATOM   1107 C CE2 . PHE   B 2 107 ? -6.909  -6.264  -14.709 1.00 71.68  ? 116 PHE   B CE2 1 
ATOM   1108 C CZ  . PHE   B 2 107 ? -6.142  -5.974  -15.808 1.00 71.63  ? 116 PHE   B CZ  1 
ATOM   1109 N N   . LYS   B 2 108 ? -4.740  -12.941 -14.351 1.00 71.19  ? 117 LYS   B N   1 
ATOM   1110 C CA  . LYS   B 2 108 ? -4.569  -14.091 -13.464 1.00 71.51  ? 117 LYS   B CA  1 
ATOM   1111 C C   . LYS   B 2 108 ? -4.276  -13.565 -12.075 1.00 70.78  ? 117 LYS   B C   1 
ATOM   1112 O O   . LYS   B 2 108 ? -3.297  -12.845 -11.900 1.00 71.16  ? 117 LYS   B O   1 
ATOM   1113 C CB  . LYS   B 2 108 ? -3.393  -14.987 -13.919 1.00 74.76  ? 117 LYS   B CB  1 
ATOM   1114 C CG  . LYS   B 2 108 ? -3.504  -15.474 -15.365 1.00 82.61  ? 117 LYS   B CG  1 
ATOM   1115 C CD  . LYS   B 2 108 ? -2.403  -16.491 -15.735 1.00 90.35  ? 117 LYS   B CD  1 
ATOM   1116 C CE  . LYS   B 2 108 ? -2.571  -16.993 -17.157 1.00 96.75  ? 117 LYS   B CE  1 
ATOM   1117 N NZ  . LYS   B 2 108 ? -1.445  -17.867 -17.617 1.00 99.96  ? 117 LYS   B NZ  1 
ATOM   1118 N N   . THR   B 2 109 ? -5.118  -13.885 -11.092 1.00 69.81  ? 118 THR   B N   1 
ATOM   1119 C CA  . THR   B 2 109 ? -4.880  -13.442 -9.713  1.00 69.59  ? 118 THR   B CA  1 
ATOM   1120 C C   . THR   B 2 109 ? -4.716  -14.658 -8.782  1.00 70.12  ? 118 THR   B C   1 
ATOM   1121 O O   . THR   B 2 109 ? -5.050  -15.775 -9.172  1.00 69.98  ? 118 THR   B O   1 
ATOM   1122 C CB  . THR   B 2 109 ? -5.990  -12.458 -9.209  1.00 69.42  ? 118 THR   B CB  1 
ATOM   1123 O OG1 . THR   B 2 109 ? -7.072  -13.191 -8.626  1.00 69.62  ? 118 THR   B OG1 1 
ATOM   1124 C CG2 . THR   B 2 109 ? -6.488  -11.485 -10.286 1.00 69.35  ? 118 THR   B CG2 1 
ATOM   1125 N N   . LYS   B 2 110 ? -4.257  -14.433 -7.534  1.00 70.50  ? 119 LYS   B N   1 
ATOM   1126 C CA  . LYS   B 2 110 ? -4.150  -15.512 -6.553  1.00 71.23  ? 119 LYS   B CA  1 
ATOM   1127 C C   . LYS   B 2 110 ? -5.548  -16.072 -6.185  1.00 72.54  ? 119 LYS   B C   1 
ATOM   1128 O O   . LYS   B 2 110 ? -5.633  -17.193 -5.679  1.00 73.72  ? 119 LYS   B O   1 
ATOM   1129 C CB  . LYS   B 2 110 ? -3.422  -15.021 -5.287  1.00 72.33  ? 119 LYS   B CB  1 
ATOM   1130 C CG  . LYS   B 2 110 ? -4.174  -13.936 -4.522  1.00 75.46  ? 119 LYS   B CG  1 
ATOM   1131 C CD  . LYS   B 2 110 ? -3.493  -13.636 -3.185  1.00 80.05  ? 119 LYS   B CD  1 
ATOM   1132 C CE  . LYS   B 2 110 ? -4.459  -13.208 -2.103  1.00 84.04  ? 119 LYS   B CE  1 
ATOM   1133 N NZ  . LYS   B 2 110 ? -4.854  -11.783 -2.228  1.00 87.00  ? 119 LYS   B NZ  1 
ATOM   1134 N N   . ASP   B 2 111 ? -6.633  -15.300 -6.430  1.00 71.91  ? 120 ASP   B N   1 
ATOM   1135 C CA  . ASP   B 2 111 ? -7.992  -15.723 -6.126  1.00 72.54  ? 120 ASP   B CA  1 
ATOM   1136 C C   . ASP   B 2 111 ? -8.817  -16.105 -7.350  1.00 73.17  ? 120 ASP   B C   1 
ATOM   1137 O O   . ASP   B 2 111 ? -10.041 -16.163 -7.248  1.00 74.34  ? 120 ASP   B O   1 
ATOM   1138 C CB  . ASP   B 2 111 ? -8.729  -14.637 -5.328  1.00 74.22  ? 120 ASP   B CB  1 
ATOM   1139 C CG  . ASP   B 2 111 ? -8.059  -14.310 -4.012  1.00 79.45  ? 120 ASP   B CG  1 
ATOM   1140 O OD1 . ASP   B 2 111 ? -7.674  -15.254 -3.294  1.00 81.03  ? 120 ASP   B OD1 1 
ATOM   1141 O OD2 . ASP   B 2 111 ? -7.916  -13.109 -3.701  1.00 81.40  ? 120 ASP   B OD2 1 
ATOM   1142 N N   . GLY   B 2 112 ? -8.175  -16.331 -8.491  1.00 72.34  ? 121 GLY   B N   1 
ATOM   1143 C CA  . GLY   B 2 112 ? -8.887  -16.716 -9.701  1.00 72.06  ? 121 GLY   B CA  1 
ATOM   1144 C C   . GLY   B 2 112 ? -8.665  -15.822 -10.907 1.00 71.27  ? 121 GLY   B C   1 
ATOM   1145 O O   . GLY   B 2 112 ? -8.103  -14.732 -10.787 1.00 71.62  ? 121 GLY   B O   1 
ATOM   1146 N N   . ASP   B 2 113 ? -9.107  -16.281 -12.080 1.00 70.13  ? 122 ASP   B N   1 
ATOM   1147 C CA  . ASP   B 2 113 ? -8.967  -15.528 -13.327 1.00 69.91  ? 122 ASP   B CA  1 
ATOM   1148 C C   . ASP   B 2 113 ? -10.185 -14.626 -13.573 1.00 69.05  ? 122 ASP   B C   1 
ATOM   1149 O O   . ASP   B 2 113 ? -11.306 -14.972 -13.204 1.00 68.72  ? 122 ASP   B O   1 
ATOM   1150 C CB  . ASP   B 2 113 ? -8.825  -16.468 -14.532 1.00 72.16  ? 122 ASP   B CB  1 
ATOM   1151 C CG  . ASP   B 2 113 ? -7.545  -17.276 -14.618 1.00 79.45  ? 122 ASP   B CG  1 
ATOM   1152 O OD1 . ASP   B 2 113 ? -6.695  -17.146 -13.710 1.00 80.84  ? 122 ASP   B OD1 1 
ATOM   1153 O OD2 . ASP   B 2 113 ? -7.401  -18.051 -15.592 1.00 83.01  ? 122 ASP   B OD2 1 
ATOM   1154 N N   . ILE   B 2 114 ? -9.951  -13.478 -14.219 1.00 68.13  ? 123 ILE   B N   1 
ATOM   1155 C CA  . ILE   B 2 114 ? -10.974 -12.496 -14.575 1.00 67.89  ? 123 ILE   B CA  1 
ATOM   1156 C C   . ILE   B 2 114 ? -10.719 -12.095 -16.030 1.00 66.84  ? 123 ILE   B C   1 
ATOM   1157 O O   . ILE   B 2 114 ? -9.565  -11.881 -16.394 1.00 66.86  ? 123 ILE   B O   1 
ATOM   1158 C CB  . ILE   B 2 114 ? -10.859 -11.205 -13.701 1.00 68.82  ? 123 ILE   B CB  1 
ATOM   1159 C CG1 . ILE   B 2 114 ? -10.641 -11.495 -12.214 1.00 70.43  ? 123 ILE   B CG1 1 
ATOM   1160 C CG2 . ILE   B 2 114 ? -12.052 -10.270 -13.912 1.00 69.12  ? 123 ILE   B CG2 1 
ATOM   1161 C CD1 . ILE   B 2 114 ? -10.306 -10.223 -11.352 1.00 71.94  ? 123 ILE   B CD1 1 
ATOM   1162 N N   . GLY   B 2 115 ? -11.776 -11.905 -16.822 1.00 65.63  ? 124 GLY   B N   1 
ATOM   1163 C CA  . GLY   B 2 115 ? -11.631 -11.416 -18.191 1.00 65.08  ? 124 GLY   B CA  1 
ATOM   1164 C C   . GLY   B 2 115 ? -11.111 -9.988  -18.186 1.00 64.32  ? 124 GLY   B C   1 
ATOM   1165 O O   . GLY   B 2 115 ? -11.300 -9.252  -17.204 1.00 63.30  ? 124 GLY   B O   1 
ATOM   1166 N N   . ALA   B 2 116 ? -10.408 -9.594  -19.251 1.00 64.25  ? 125 ALA   B N   1 
ATOM   1167 C CA  . ALA   B 2 116 ? -9.841  -8.253  -19.336 1.00 64.64  ? 125 ALA   B CA  1 
ATOM   1168 C C   . ALA   B 2 116 ? -9.892  -7.720  -20.759 1.00 65.40  ? 125 ALA   B C   1 
ATOM   1169 O O   . ALA   B 2 116 ? -9.637  -8.470  -21.684 1.00 65.41  ? 125 ALA   B O   1 
ATOM   1170 C CB  . ALA   B 2 116 ? -8.407  -8.258  -18.840 1.00 64.36  ? 125 ALA   B CB  1 
ATOM   1171 N N   . VAL   B 2 117 ? -10.203 -6.431  -20.939 1.00 66.01  ? 126 VAL   B N   1 
ATOM   1172 C CA  A VAL   B 2 117 ? -10.265 -5.842  -22.276 0.50 67.50  ? 126 VAL   B CA  1 
ATOM   1173 C CA  B VAL   B 2 117 ? -10.311 -5.804  -22.248 0.50 67.73  ? 126 VAL   B CA  1 
ATOM   1174 C C   . VAL   B 2 117 ? -9.061  -4.942  -22.558 1.00 68.91  ? 126 VAL   B C   1 
ATOM   1175 O O   . VAL   B 2 117 ? -8.739  -4.027  -21.785 1.00 69.52  ? 126 VAL   B O   1 
ATOM   1176 C CB  A VAL   B 2 117 ? -11.609 -5.145  -22.593 0.50 67.83  ? 126 VAL   B CB  1 
ATOM   1177 C CB  B VAL   B 2 117 ? -11.676 -5.046  -22.309 0.50 68.49  ? 126 VAL   B CB  1 
ATOM   1178 C CG1 A VAL   B 2 117 ? -12.701 -6.176  -22.847 0.50 68.38  ? 126 VAL   B CG1 1 
ATOM   1179 C CG1 B VAL   B 2 117 ? -11.560 -3.611  -22.813 0.50 69.17  ? 126 VAL   B CG1 1 
ATOM   1180 C CG2 A VAL   B 2 117 ? -12.016 -4.179  -21.486 0.50 68.04  ? 126 VAL   B CG2 1 
ATOM   1181 C CG2 B VAL   B 2 117 ? -12.706 -5.838  -23.103 0.50 68.94  ? 126 VAL   B CG2 1 
ATOM   1182 N N   . ALA   B 2 118 ? -8.350  -5.241  -23.659 1.00 69.94  ? 127 ALA   B N   1 
ATOM   1183 C CA  . ALA   B 2 118 ? -7.170  -4.464  -24.013 1.00 71.84  ? 127 ALA   B CA  1 
ATOM   1184 C C   . ALA   B 2 118 ? -7.546  -3.332  -24.932 1.00 73.16  ? 127 ALA   B C   1 
ATOM   1185 O O   . ALA   B 2 118 ? -7.192  -3.306  -26.105 1.00 73.81  ? 127 ALA   B O   1 
ATOM   1186 C CB  . ALA   B 2 118 ? -6.093  -5.344  -24.621 1.00 72.38  ? 127 ALA   B CB  1 
ATOM   1187 N N   . LEU   B 2 119 ? -8.381  -2.430  -24.417 1.00 73.02  ? 128 LEU   B N   1 
ATOM   1188 C CA  . LEU   B 2 119 ? -8.816  -1.251  -25.150 1.00 73.19  ? 128 LEU   B CA  1 
ATOM   1189 C C   . LEU   B 2 119 ? -8.455  -0.065  -24.270 1.00 73.70  ? 128 LEU   B C   1 
ATOM   1190 O O   . LEU   B 2 119 ? -8.583  -0.133  -23.035 1.00 73.95  ? 128 LEU   B O   1 
ATOM   1191 C CB  . LEU   B 2 119 ? -10.320 -1.290  -25.469 1.00 72.91  ? 128 LEU   B CB  1 
ATOM   1192 C CG  . LEU   B 2 119 ? -10.758 -2.455  -26.351 1.00 73.54  ? 128 LEU   B CG  1 
ATOM   1193 C CD1 . LEU   B 2 119 ? -12.259 -2.562  -26.405 1.00 73.35  ? 128 LEU   B CD1 1 
ATOM   1194 C CD2 . LEU   B 2 119 ? -10.171 -2.336  -27.762 1.00 74.60  ? 128 LEU   B CD2 1 
ATOM   1195 N N   . ASP   B 2 120 ? -7.937  0.990   -24.888 1.00 73.56  ? 129 ASP   B N   1 
ATOM   1196 C CA  . ASP   B 2 120 ? -7.474  2.144   -24.145 1.00 73.77  ? 129 ASP   B CA  1 
ATOM   1197 C C   . ASP   B 2 120 ? -8.260  3.418   -24.405 1.00 73.35  ? 129 ASP   B C   1 
ATOM   1198 O O   . ASP   B 2 120 ? -8.098  4.056   -25.432 1.00 73.80  ? 129 ASP   B O   1 
ATOM   1199 C CB  . ASP   B 2 120 ? -5.986  2.357   -24.422 1.00 75.92  ? 129 ASP   B CB  1 
ATOM   1200 C CG  . ASP   B 2 120 ? -5.299  3.243   -23.415 1.00 80.71  ? 129 ASP   B CG  1 
ATOM   1201 O OD1 . ASP   B 2 120 ? -5.981  4.114   -22.819 1.00 81.75  ? 129 ASP   B OD1 1 
ATOM   1202 O OD2 . ASP   B 2 120 ? -4.085  3.064   -23.205 1.00 82.46  ? 129 ASP   B OD2 1 
ATOM   1203 N N   . TYR   B 2 121 ? -9.042  3.827   -23.424 1.00 72.65  ? 130 TYR   B N   1 
ATOM   1204 C CA  . TYR   B 2 121 ? -9.834  5.053   -23.428 1.00 72.46  ? 130 TYR   B CA  1 
ATOM   1205 C C   . TYR   B 2 121 ? -9.492  5.852   -22.173 1.00 71.74  ? 130 TYR   B C   1 
ATOM   1206 O O   . TYR   B 2 121 ? -9.127  5.271   -21.142 1.00 71.72  ? 130 TYR   B O   1 
ATOM   1207 C CB  . TYR   B 2 121 ? -11.330 4.721   -23.424 1.00 72.80  ? 130 TYR   B CB  1 
ATOM   1208 C CG  . TYR   B 2 121 ? -11.812 4.235   -24.763 1.00 74.25  ? 130 TYR   B CG  1 
ATOM   1209 C CD1 . TYR   B 2 121 ? -12.302 5.124   -25.709 1.00 75.41  ? 130 TYR   B CD1 1 
ATOM   1210 C CD2 . TYR   B 2 121 ? -11.690 2.899   -25.126 1.00 75.47  ? 130 TYR   B CD2 1 
ATOM   1211 C CE1 . TYR   B 2 121 ? -12.682 4.694   -26.971 1.00 76.64  ? 130 TYR   B CE1 1 
ATOM   1212 C CE2 . TYR   B 2 121 ? -12.061 2.459   -26.391 1.00 76.57  ? 130 TYR   B CE2 1 
ATOM   1213 C CZ  . TYR   B 2 121 ? -12.566 3.361   -27.306 1.00 77.96  ? 130 TYR   B CZ  1 
ATOM   1214 O OH  . TYR   B 2 121 ? -12.978 2.946   -28.543 1.00 80.49  ? 130 TYR   B OH  1 
ATOM   1215 N N   . PRO   B 2 122 ? -9.637  7.189   -22.222 1.00 71.00  ? 131 PRO   B N   1 
ATOM   1216 C CA  . PRO   B 2 122 ? -9.320  7.994   -21.036 1.00 70.17  ? 131 PRO   B CA  1 
ATOM   1217 C C   . PRO   B 2 122 ? -10.150 7.617   -19.819 1.00 68.34  ? 131 PRO   B C   1 
ATOM   1218 O O   . PRO   B 2 122 ? -11.210 7.000   -19.944 1.00 68.34  ? 131 PRO   B O   1 
ATOM   1219 C CB  . PRO   B 2 122 ? -9.587  9.435   -21.492 1.00 71.01  ? 131 PRO   B CB  1 
ATOM   1220 C CG  . PRO   B 2 122 ? -10.467 9.309   -22.679 1.00 71.50  ? 131 PRO   B CG  1 
ATOM   1221 C CD  . PRO   B 2 122 ? -10.058 8.040   -23.350 1.00 70.42  ? 131 PRO   B CD  1 
ATOM   1222 N N   . ALA   B 2 123 ? -9.644  7.966   -18.635 1.00 66.39  ? 132 ALA   B N   1 
ATOM   1223 C CA  . ALA   B 2 123 ? -10.282 7.674   -17.356 1.00 64.44  ? 132 ALA   B CA  1 
ATOM   1224 C C   . ALA   B 2 123 ? -11.751 8.151   -17.255 1.00 62.28  ? 132 ALA   B C   1 
ATOM   1225 O O   . ALA   B 2 123 ? -12.549 7.510   -16.570 1.00 62.17  ? 132 ALA   B O   1 
ATOM   1226 C CB  . ALA   B 2 123 ? -9.447  8.243   -16.234 1.00 64.48  ? 132 ALA   B CB  1 
ATOM   1227 N N   . GLY   B 2 124 ? -12.120 9.204   -17.990 1.00 60.13  ? 133 GLY   B N   1 
ATOM   1228 C CA  . GLY   B 2 124 ? -13.508 9.675   -18.014 1.00 58.69  ? 133 GLY   B CA  1 
ATOM   1229 C C   . GLY   B 2 124 ? -14.490 8.694   -18.653 1.00 57.08  ? 133 GLY   B C   1 
ATOM   1230 O O   . GLY   B 2 124 ? -15.704 8.867   -18.538 1.00 56.99  ? 133 GLY   B O   1 
ATOM   1231 N N   . THR   B 2 125 ? -13.970 7.639   -19.310 1.00 55.59  ? 134 THR   B N   1 
ATOM   1232 C CA  . THR   B 2 125 ? -14.735 6.535   -19.917 1.00 55.41  ? 134 THR   B CA  1 
ATOM   1233 C C   . THR   B 2 125 ? -15.064 5.409   -18.876 1.00 53.68  ? 134 THR   B C   1 
ATOM   1234 O O   . THR   B 2 125 ? -15.849 4.498   -19.166 1.00 53.63  ? 134 THR   B O   1 
ATOM   1235 C CB  . THR   B 2 125 ? -13.956 5.991   -21.148 1.00 57.67  ? 134 THR   B CB  1 
ATOM   1236 O OG1 . THR   B 2 125 ? -13.597 7.085   -22.008 1.00 59.26  ? 134 THR   B OG1 1 
ATOM   1237 C CG2 . THR   B 2 125 ? -14.747 4.975   -21.972 1.00 58.38  ? 134 THR   B CG2 1 
ATOM   1238 N N   . SER   B 2 126 ? -14.468 5.479   -17.662 1.00 51.43  ? 135 SER   B N   1 
ATOM   1239 C CA  . SER   B 2 126 ? -14.692 4.498   -16.594 1.00 50.95  ? 135 SER   B CA  1 
ATOM   1240 C C   . SER   B 2 126 ? -16.171 4.328   -16.291 1.00 50.60  ? 135 SER   B C   1 
ATOM   1241 O O   . SER   B 2 126 ? -16.847 5.318   -16.078 1.00 50.97  ? 135 SER   B O   1 
ATOM   1242 C CB  . SER   B 2 126 ? -13.980 4.939   -15.320 1.00 51.00  ? 135 SER   B CB  1 
ATOM   1243 O OG  . SER   B 2 126 ? -12.567 4.835   -15.445 1.00 51.82  ? 135 SER   B OG  1 
ATOM   1244 N N   . GLY   B 2 127 ? -16.649 3.090   -16.289 1.00 50.07  ? 136 GLY   B N   1 
ATOM   1245 C CA  . GLY   B 2 127 ? -18.045 2.747   -16.055 1.00 50.31  ? 136 GLY   B CA  1 
ATOM   1246 C C   . GLY   B 2 127 ? -18.779 2.275   -17.302 1.00 50.94  ? 136 GLY   B C   1 
ATOM   1247 O O   . GLY   B 2 127 ? -19.901 1.774   -17.208 1.00 51.22  ? 136 GLY   B O   1 
ATOM   1248 N N   . SER   B 2 128 ? -18.164 2.441   -18.491 1.00 50.56  ? 137 SER   B N   1 
ATOM   1249 C CA  . SER   B 2 128 ? -18.748 2.001   -19.755 1.00 51.28  ? 137 SER   B CA  1 
ATOM   1250 C C   . SER   B 2 128 ? -18.974 0.483   -19.727 1.00 52.28  ? 137 SER   B C   1 
ATOM   1251 O O   . SER   B 2 128 ? -18.072 -0.266  -19.356 1.00 53.01  ? 137 SER   B O   1 
ATOM   1252 C CB  . SER   B 2 128 ? -17.814 2.365   -20.910 1.00 52.26  ? 137 SER   B CB  1 
ATOM   1253 O OG  . SER   B 2 128 ? -17.842 3.763   -21.149 1.00 53.58  ? 137 SER   B OG  1 
ATOM   1254 N N   . PRO   B 2 129 ? -20.178 0.017   -20.088 1.00 52.33  ? 138 PRO   B N   1 
ATOM   1255 C CA  . PRO   B 2 129 ? -20.437 -1.436  -20.072 1.00 52.66  ? 138 PRO   B CA  1 
ATOM   1256 C C   . PRO   B 2 129 ? -19.763 -2.281  -21.154 1.00 53.88  ? 138 PRO   B C   1 
ATOM   1257 O O   . PRO   B 2 129 ? -19.552 -1.848  -22.299 1.00 53.88  ? 138 PRO   B O   1 
ATOM   1258 C CB  . PRO   B 2 129 ? -21.956 -1.519  -20.246 1.00 52.89  ? 138 PRO   B CB  1 
ATOM   1259 C CG  . PRO   B 2 129 ? -22.300 -0.281  -21.070 1.00 52.95  ? 138 PRO   B CG  1 
ATOM   1260 C CD  . PRO   B 2 129 ? -21.368 0.782   -20.517 1.00 51.49  ? 138 PRO   B CD  1 
ATOM   1261 N N   . ILE   B 2 130 ? -19.519 -3.542  -20.803 1.00 54.50  ? 139 ILE   B N   1 
ATOM   1262 C CA  . ILE   B 2 130 ? -18.999 -4.573  -21.684 1.00 55.80  ? 139 ILE   B CA  1 
ATOM   1263 C C   . ILE   B 2 130 ? -20.154 -5.565  -21.862 1.00 57.52  ? 139 ILE   B C   1 
ATOM   1264 O O   . ILE   B 2 130 ? -20.757 -5.974  -20.873 1.00 57.00  ? 139 ILE   B O   1 
ATOM   1265 C CB  . ILE   B 2 130 ? -17.742 -5.217  -21.072 1.00 55.91  ? 139 ILE   B CB  1 
ATOM   1266 C CG1 . ILE   B 2 130 ? -16.665 -4.145  -20.840 1.00 56.90  ? 139 ILE   B CG1 1 
ATOM   1267 C CG2 . ILE   B 2 130 ? -17.220 -6.343  -21.970 1.00 56.14  ? 139 ILE   B CG2 1 
ATOM   1268 C CD1 . ILE   B 2 130 ? -15.680 -4.514  -19.815 1.00 58.68  ? 139 ILE   B CD1 1 
ATOM   1269 N N   . LEU   B 2 131 ? -20.507 -5.904  -23.119 1.00 59.39  ? 140 LEU   B N   1 
ATOM   1270 C CA  . LEU   B 2 131 ? -21.691 -6.731  -23.403 1.00 61.62  ? 140 LEU   B CA  1 
ATOM   1271 C C   . LEU   B 2 131 ? -21.435 -8.079  -24.057 1.00 62.29  ? 140 LEU   B C   1 
ATOM   1272 O O   . LEU   B 2 131 ? -20.544 -8.179  -24.883 1.00 62.82  ? 140 LEU   B O   1 
ATOM   1273 C CB  . LEU   B 2 131 ? -22.644 -5.976  -24.358 1.00 62.96  ? 140 LEU   B CB  1 
ATOM   1274 C CG  . LEU   B 2 131 ? -22.676 -4.473  -24.259 1.00 65.61  ? 140 LEU   B CG  1 
ATOM   1275 C CD1 . LEU   B 2 131 ? -23.444 -3.883  -25.385 1.00 66.58  ? 140 LEU   B CD1 1 
ATOM   1276 C CD2 . LEU   B 2 131 ? -23.185 -4.041  -22.891 1.00 66.50  ? 140 LEU   B CD2 1 
ATOM   1277 N N   . ASP   B 2 132 ? -22.328 -9.070  -23.810 1.00 62.62  ? 141 ASP   B N   1 
ATOM   1278 C CA  . ASP   B 2 132 ? -22.306 -10.350 -24.531 1.00 63.74  ? 141 ASP   B CA  1 
ATOM   1279 C C   . ASP   B 2 132 ? -23.192 -10.253 -25.823 1.00 65.90  ? 141 ASP   B C   1 
ATOM   1280 O O   . ASP   B 2 132 ? -23.845 -9.219  -26.060 1.00 65.53  ? 141 ASP   B O   1 
ATOM   1281 C CB  . ASP   B 2 132 ? -22.706 -11.538 -23.630 1.00 63.30  ? 141 ASP   B CB  1 
ATOM   1282 C CG  . ASP   B 2 132 ? -24.149 -11.602 -23.155 1.00 66.55  ? 141 ASP   B CG  1 
ATOM   1283 O OD1 . ASP   B 2 132 ? -25.002 -10.879 -23.720 1.00 65.44  ? 141 ASP   B OD1 1 
ATOM   1284 O OD2 . ASP   B 2 132 ? -24.430 -12.388 -22.223 1.00 69.35  ? 141 ASP   B OD2 1 
ATOM   1285 N N   . LYS   B 2 133 ? -23.255 -11.341 -26.616 1.00 67.64  ? 142 LYS   B N   1 
ATOM   1286 C CA  . LYS   B 2 133 ? -23.991 -11.419 -27.889 1.00 69.87  ? 142 LYS   B CA  1 
ATOM   1287 C C   . LYS   B 2 133 ? -25.485 -11.105 -27.787 1.00 70.00  ? 142 LYS   B C   1 
ATOM   1288 O O   . LYS   B 2 133 ? -26.043 -10.595 -28.749 1.00 70.38  ? 142 LYS   B O   1 
ATOM   1289 C CB  . LYS   B 2 133 ? -23.764 -12.779 -28.573 1.00 73.80  ? 142 LYS   B CB  1 
ATOM   1290 C CG  . LYS   B 2 133 ? -22.322 -12.955 -29.021 1.00 81.12  ? 142 LYS   B CG  1 
ATOM   1291 C CD  . LYS   B 2 133 ? -22.136 -14.193 -29.910 1.00 88.23  ? 142 LYS   B CD  1 
ATOM   1292 C CE  . LYS   B 2 133 ? -21.453 -15.326 -29.179 1.00 93.56  ? 142 LYS   B CE  1 
ATOM   1293 N NZ  . LYS   B 2 133 ? -21.243 -16.502 -30.074 1.00 96.81  ? 142 LYS   B NZ  1 
ATOM   1294 N N   . CYS   B 2 134 ? -26.137 -11.420 -26.647 1.00 69.69  ? 143 CYS   B N   1 
ATOM   1295 C CA  . CYS   B 2 134 ? -27.557 -11.053 -26.455 1.00 69.62  ? 143 CYS   B CA  1 
ATOM   1296 C C   . CYS   B 2 134 ? -27.738 -9.646  -25.902 1.00 67.20  ? 143 CYS   B C   1 
ATOM   1297 O O   . CYS   B 2 134 ? -28.872 -9.253  -25.626 1.00 67.21  ? 143 CYS   B O   1 
ATOM   1298 C CB  . CYS   B 2 134 ? -28.311 -12.052 -25.588 1.00 72.62  ? 143 CYS   B CB  1 
ATOM   1299 S SG  . CYS   B 2 134 ? -27.682 -13.735 -25.670 1.00 82.45  ? 143 CYS   B SG  1 
ATOM   1300 N N   . GLY   B 2 135 ? -26.656 -8.898  -25.750 1.00 65.00  ? 144 GLY   B N   1 
ATOM   1301 C CA  . GLY   B 2 135 ? -26.734 -7.535  -25.258 1.00 63.97  ? 144 GLY   B CA  1 
ATOM   1302 C C   . GLY   B 2 135 ? -26.750 -7.424  -23.748 1.00 62.33  ? 144 GLY   B C   1 
ATOM   1303 O O   . GLY   B 2 135 ? -27.029 -6.349  -23.233 1.00 62.36  ? 144 GLY   B O   1 
ATOM   1304 N N   . ARG   B 2 136 ? -26.416 -8.501  -23.024 1.00 61.00  ? 145 ARG   B N   1 
ATOM   1305 C CA  . ARG   B 2 136 ? -26.394 -8.452  -21.561 1.00 60.56  ? 145 ARG   B CA  1 
ATOM   1306 C C   . ARG   B 2 136 ? -25.075 -7.878  -21.031 1.00 58.35  ? 145 ARG   B C   1 
ATOM   1307 O O   . ARG   B 2 136 ? -24.001 -8.210  -21.552 1.00 57.54  ? 145 ARG   B O   1 
ATOM   1308 C CB  . ARG   B 2 136 ? -26.665 -9.837  -20.968 1.00 63.33  ? 145 ARG   B CB  1 
ATOM   1309 C CG  . ARG   B 2 136 ? -28.114 -10.285 -21.139 1.00 69.21  ? 145 ARG   B CG  1 
ATOM   1310 C CD  . ARG   B 2 136 ? -28.332 -11.649 -20.520 1.00 74.93  ? 145 ARG   B CD  1 
ATOM   1311 N NE  . ARG   B 2 136 ? -27.564 -12.668 -21.230 1.00 80.51  ? 145 ARG   B NE  1 
ATOM   1312 C CZ  . ARG   B 2 136 ? -26.949 -13.695 -20.651 1.00 84.75  ? 145 ARG   B CZ  1 
ATOM   1313 N NH1 . ARG   B 2 136 ? -27.002 -13.856 -19.332 1.00 84.70  ? 145 ARG   B NH1 1 
ATOM   1314 N NH2 . ARG   B 2 136 ? -26.262 -14.560 -21.384 1.00 86.35  ? 145 ARG   B NH2 1 
ATOM   1315 N N   . VAL   B 2 137 ? -25.142 -7.040  -19.965 1.00 56.46  ? 146 VAL   B N   1 
ATOM   1316 C CA  . VAL   B 2 137 ? -23.924 -6.463  -19.397 1.00 55.18  ? 146 VAL   B CA  1 
ATOM   1317 C C   . VAL   B 2 137 ? -23.151 -7.473  -18.545 1.00 54.58  ? 146 VAL   B C   1 
ATOM   1318 O O   . VAL   B 2 137 ? -23.622 -7.903  -17.489 1.00 53.84  ? 146 VAL   B O   1 
ATOM   1319 C CB  . VAL   B 2 137 ? -24.179 -5.138  -18.643 1.00 55.15  ? 146 VAL   B CB  1 
ATOM   1320 C CG1 . VAL   B 2 137 ? -22.884 -4.579  -18.066 1.00 54.98  ? 146 VAL   B CG1 1 
ATOM   1321 C CG2 . VAL   B 2 137 ? -24.839 -4.119  -19.568 1.00 55.80  ? 146 VAL   B CG2 1 
ATOM   1322 N N   . ILE   B 2 138 ? -21.958 -7.828  -19.000 1.00 53.56  ? 147 ILE   B N   1 
ATOM   1323 C CA  . ILE   B 2 138 ? -21.098 -8.763  -18.291 1.00 53.12  ? 147 ILE   B CA  1 
ATOM   1324 C C   . ILE   B 2 138 ? -20.057 -8.071  -17.368 1.00 52.67  ? 147 ILE   B C   1 
ATOM   1325 O O   . ILE   B 2 138 ? -19.315 -8.773  -16.667 1.00 53.20  ? 147 ILE   B O   1 
ATOM   1326 C CB  . ILE   B 2 138 ? -20.395 -9.736  -19.287 1.00 53.15  ? 147 ILE   B CB  1 
ATOM   1327 C CG1 . ILE   B 2 138 ? -19.482 -8.969  -20.234 1.00 54.36  ? 147 ILE   B CG1 1 
ATOM   1328 C CG2 . ILE   B 2 138 ? -21.392 -10.627 -20.024 1.00 53.03  ? 147 ILE   B CG2 1 
ATOM   1329 C CD1 . ILE   B 2 138 ? -18.577 -9.845  -21.073 1.00 56.69  ? 147 ILE   B CD1 1 
ATOM   1330 N N   . GLY   B 2 139 ? -20.007 -6.737  -17.371 1.00 51.43  ? 148 GLY   B N   1 
ATOM   1331 C CA  . GLY   B 2 139 ? -19.082 -6.006  -16.517 1.00 51.41  ? 148 GLY   B CA  1 
ATOM   1332 C C   . GLY   B 2 139 ? -18.860 -4.569  -16.935 1.00 51.70  ? 148 GLY   B C   1 
ATOM   1333 O O   . GLY   B 2 139 ? -19.363 -4.146  -17.982 1.00 52.85  ? 148 GLY   B O   1 
ATOM   1334 N N   . LEU   B 2 140 ? -18.065 -3.812  -16.155 1.00 50.81  ? 149 LEU   B N   1 
ATOM   1335 C CA  . LEU   B 2 140 ? -17.782 -2.402  -16.444 1.00 51.35  ? 149 LEU   B CA  1 
ATOM   1336 C C   . LEU   B 2 140 ? -16.296 -2.183  -16.666 1.00 52.79  ? 149 LEU   B C   1 
ATOM   1337 O O   . LEU   B 2 140 ? -15.466 -2.818  -16.021 1.00 52.87  ? 149 LEU   B O   1 
ATOM   1338 C CB  . LEU   B 2 140 ? -18.264 -1.484  -15.308 1.00 51.22  ? 149 LEU   B CB  1 
ATOM   1339 C CG  . LEU   B 2 140 ? -19.730 -1.585  -14.870 1.00 52.59  ? 149 LEU   B CG  1 
ATOM   1340 C CD1 . LEU   B 2 140 ? -20.039 -0.558  -13.770 1.00 53.63  ? 149 LEU   B CD1 1 
ATOM   1341 C CD2 . LEU   B 2 140 ? -20.701 -1.456  -16.058 1.00 52.81  ? 149 LEU   B CD2 1 
ATOM   1342 N N   . TYR   B 2 141 ? -15.973 -1.267  -17.571 1.00 53.84  ? 150 TYR   B N   1 
ATOM   1343 C CA  . TYR   B 2 141 ? -14.614 -0.918  -17.974 1.00 55.52  ? 150 TYR   B CA  1 
ATOM   1344 C C   . TYR   B 2 141 ? -14.054 0.192   -17.084 1.00 55.86  ? 150 TYR   B C   1 
ATOM   1345 O O   . TYR   B 2 141 ? -14.809 1.077   -16.708 1.00 56.54  ? 150 TYR   B O   1 
ATOM   1346 C CB  . TYR   B 2 141 ? -14.676 -0.404  -19.447 1.00 56.79  ? 150 TYR   B CB  1 
ATOM   1347 C CG  . TYR   B 2 141 ? -13.374 0.164   -19.961 1.00 58.92  ? 150 TYR   B CG  1 
ATOM   1348 C CD1 . TYR   B 2 141 ? -13.092 1.523   -19.853 1.00 60.12  ? 150 TYR   B CD1 1 
ATOM   1349 C CD2 . TYR   B 2 141 ? -12.425 -0.654  -20.566 1.00 60.27  ? 150 TYR   B CD2 1 
ATOM   1350 C CE1 . TYR   B 2 141 ? -11.879 2.042   -20.292 1.00 61.69  ? 150 TYR   B CE1 1 
ATOM   1351 C CE2 . TYR   B 2 141 ? -11.231 -0.137  -21.057 1.00 61.06  ? 150 TYR   B CE2 1 
ATOM   1352 C CZ  . TYR   B 2 141 ? -10.967 1.215   -20.935 1.00 62.62  ? 150 TYR   B CZ  1 
ATOM   1353 O OH  . TYR   B 2 141 ? -9.782  1.730   -21.413 1.00 64.50  ? 150 TYR   B OH  1 
ATOM   1354 N N   . GLY   B 2 142 ? -12.740 0.212   -16.849 1.00 54.99  ? 151 GLY   B N   1 
ATOM   1355 C CA  . GLY   B 2 142 ? -12.136 1.313   -16.104 1.00 55.39  ? 151 GLY   B CA  1 
ATOM   1356 C C   . GLY   B 2 142 ? -11.208 1.013   -14.942 1.00 55.68  ? 151 GLY   B C   1 
ATOM   1357 O O   . GLY   B 2 142 ? -10.522 1.932   -14.485 1.00 56.35  ? 151 GLY   B O   1 
ATOM   1358 N N   . ASN   B 2 143 ? -11.170 -0.250  -14.434 1.00 54.52  ? 152 ASN   B N   1 
ATOM   1359 C CA  . ASN   B 2 143 ? -10.240 -0.581  -13.354 1.00 54.85  ? 152 ASN   B CA  1 
ATOM   1360 C C   . ASN   B 2 143 ? -9.226  -1.600  -13.877 1.00 56.11  ? 152 ASN   B C   1 
ATOM   1361 O O   . ASN   B 2 143 ? -9.557  -2.773  -14.057 1.00 55.65  ? 152 ASN   B O   1 
ATOM   1362 C CB  . ASN   B 2 143 ? -10.953 -1.117  -12.107 1.00 54.33  ? 152 ASN   B CB  1 
ATOM   1363 C CG  . ASN   B 2 143 ? -10.042 -1.157  -10.881 1.00 56.42  ? 152 ASN   B CG  1 
ATOM   1364 O OD1 . ASN   B 2 143 ? -9.088  -0.366  -10.758 1.00 56.70  ? 152 ASN   B OD1 1 
ATOM   1365 N ND2 . ASN   B 2 143 ? -10.311 -2.075  -9.941  1.00 55.90  ? 152 ASN   B ND2 1 
ATOM   1366 N N   . GLY   B 2 144 ? -8.008  -1.142  -14.099 1.00 57.27  ? 153 GLY   B N   1 
ATOM   1367 C CA  . GLY   B 2 144 ? -6.993  -2.006  -14.655 1.00 60.19  ? 153 GLY   B CA  1 
ATOM   1368 C C   . GLY   B 2 144 ? -5.566  -1.643  -14.361 1.00 62.65  ? 153 GLY   B C   1 
ATOM   1369 O O   . GLY   B 2 144 ? -5.241  -1.149  -13.275 1.00 62.87  ? 153 GLY   B O   1 
ATOM   1370 N N   . VAL   B 2 145 ? -4.702  -1.896  -15.359 1.00 64.01  ? 154 VAL   B N   1 
ATOM   1371 C CA  . VAL   B 2 145 ? -3.282  -1.720  -15.189 1.00 65.92  ? 154 VAL   B CA  1 
ATOM   1372 C C   . VAL   B 2 145 ? -2.597  -1.122  -16.440 1.00 68.10  ? 154 VAL   B C   1 
ATOM   1373 O O   . VAL   B 2 145 ? -3.158  -1.135  -17.531 1.00 68.00  ? 154 VAL   B O   1 
ATOM   1374 C CB  . VAL   B 2 145 ? -2.720  -3.113  -14.779 1.00 66.67  ? 154 VAL   B CB  1 
ATOM   1375 C CG1 . VAL   B 2 145 ? -2.279  -3.947  -15.974 1.00 66.62  ? 154 VAL   B CG1 1 
ATOM   1376 C CG2 . VAL   B 2 145 ? -1.632  -2.998  -13.726 1.00 67.82  ? 154 VAL   B CG2 1 
ATOM   1377 N N   . VAL   B 2 146 ? -1.396  -0.581  -16.260 1.00 69.82  ? 155 VAL   B N   1 
ATOM   1378 C CA  . VAL   B 2 146 ? -0.605  -0.039  -17.346 1.00 72.71  ? 155 VAL   B CA  1 
ATOM   1379 C C   . VAL   B 2 146 ? 0.435   -1.111  -17.662 1.00 75.50  ? 155 VAL   B C   1 
ATOM   1380 O O   . VAL   B 2 146 ? 1.124   -1.575  -16.752 1.00 75.75  ? 155 VAL   B O   1 
ATOM   1381 C CB  . VAL   B 2 146 ? 0.030   1.318   -16.952 1.00 73.71  ? 155 VAL   B CB  1 
ATOM   1382 C CG1 . VAL   B 2 146 ? 1.195   1.676   -17.865 1.00 74.62  ? 155 VAL   B CG1 1 
ATOM   1383 C CG2 . VAL   B 2 146 ? -1.016  2.427   -16.959 1.00 74.16  ? 155 VAL   B CG2 1 
ATOM   1384 N N   . ILE   B 2 147 ? 0.517   -1.547  -18.929 1.00 77.46  ? 156 ILE   B N   1 
ATOM   1385 C CA  . ILE   B 2 147 ? 1.470   -2.596  -19.298 1.00 79.57  ? 156 ILE   B CA  1 
ATOM   1386 C C   . ILE   B 2 147 ? 2.837   -1.994  -19.759 1.00 81.70  ? 156 ILE   B C   1 
ATOM   1387 O O   . ILE   B 2 147 ? 3.006   -0.780  -19.682 1.00 81.77  ? 156 ILE   B O   1 
ATOM   1388 C CB  . ILE   B 2 147 ? 0.804   -3.574  -20.302 1.00 80.07  ? 156 ILE   B CB  1 
ATOM   1389 C CG1 . ILE   B 2 147 ? 0.347   -2.858  -21.577 1.00 81.09  ? 156 ILE   B CG1 1 
ATOM   1390 C CG2 . ILE   B 2 147 ? -0.378  -4.275  -19.622 1.00 80.39  ? 156 ILE   B CG2 1 
ATOM   1391 C CD1 . ILE   B 2 147 ? -0.161  -3.803  -22.658 1.00 82.12  ? 156 ILE   B CD1 1 
ATOM   1392 N N   . LYS   B 2 148 ? 3.832   -2.839  -20.145 1.00 83.39  ? 157 LYS   B N   1 
ATOM   1393 C CA  . LYS   B 2 148 ? 5.184   -2.414  -20.544 1.00 85.13  ? 157 LYS   B CA  1 
ATOM   1394 C C   . LYS   B 2 148 ? 5.214   -1.285  -21.572 1.00 85.81  ? 157 LYS   B C   1 
ATOM   1395 O O   . LYS   B 2 148 ? 5.986   -0.328  -21.426 1.00 85.93  ? 157 LYS   B O   1 
ATOM   1396 C CB  . LYS   B 2 148 ? 6.014   -3.618  -21.036 1.00 88.55  ? 157 LYS   B CB  1 
ATOM   1397 C CG  . LYS   B 2 148 ? 7.421   -3.270  -21.553 1.00 94.36  ? 157 LYS   B CG  1 
ATOM   1398 C CD  . LYS   B 2 148 ? 8.355   -4.488  -21.607 1.00 100.17 ? 157 LYS   B CD  1 
ATOM   1399 C CE  . LYS   B 2 148 ? 8.679   -5.052  -20.232 1.00 104.70 ? 157 LYS   B CE  1 
ATOM   1400 N NZ  . LYS   B 2 148 ? 10.015  -4.609  -19.725 1.00 106.91 ? 157 LYS   B NZ  1 
ATOM   1401 N N   . ASN   B 2 149 ? 4.367   -1.378  -22.605 1.00 85.89  ? 158 ASN   B N   1 
ATOM   1402 C CA  . ASN   B 2 149 ? 4.332   -0.367  -23.647 1.00 86.60  ? 158 ASN   B CA  1 
ATOM   1403 C C   . ASN   B 2 149 ? 3.552   0.925   -23.268 1.00 85.59  ? 158 ASN   B C   1 
ATOM   1404 O O   . ASN   B 2 149 ? 3.358   1.797   -24.124 1.00 86.12  ? 158 ASN   B O   1 
ATOM   1405 C CB  . ASN   B 2 149 ? 3.810   -0.974  -24.959 1.00 90.02  ? 158 ASN   B CB  1 
ATOM   1406 C CG  . ASN   B 2 149 ? 2.537   -1.788  -24.809 1.00 95.93  ? 158 ASN   B CG  1 
ATOM   1407 O OD1 . ASN   B 2 149 ? 2.424   -2.924  -25.300 1.00 98.36  ? 158 ASN   B OD1 1 
ATOM   1408 N ND2 . ASN   B 2 149 ? 1.551   -1.219  -24.137 1.00 96.10  ? 158 ASN   B ND2 1 
ATOM   1409 N N   . GLY   B 2 150 ? 3.105   1.026   -22.017 1.00 83.64  ? 159 GLY   B N   1 
ATOM   1410 C CA  . GLY   B 2 150 ? 2.404   2.201   -21.521 1.00 82.03  ? 159 GLY   B CA  1 
ATOM   1411 C C   . GLY   B 2 150 ? 0.918   2.262   -21.792 1.00 79.68  ? 159 GLY   B C   1 
ATOM   1412 O O   . GLY   B 2 150 ? 0.261   3.209   -21.350 1.00 80.08  ? 159 GLY   B O   1 
ATOM   1413 N N   . SER   B 2 151 ? 0.366   1.273   -22.529 1.00 76.88  ? 160 SER   B N   1 
ATOM   1414 C CA  A SER   B 2 151 ? -1.069  1.211   -22.835 0.50 75.81  ? 160 SER   B CA  1 
ATOM   1415 C CA  B SER   B 2 151 ? -1.070  1.267   -22.810 0.50 75.57  ? 160 SER   B CA  1 
ATOM   1416 C C   . SER   B 2 151 ? -1.864  0.695   -21.619 1.00 74.21  ? 160 SER   B C   1 
ATOM   1417 O O   . SER   B 2 151 ? -1.277  0.103   -20.715 1.00 73.95  ? 160 SER   B O   1 
ATOM   1418 C CB  A SER   B 2 151 ? -1.312  0.317   -24.052 0.50 77.12  ? 160 SER   B CB  1 
ATOM   1419 C CB  B SER   B 2 151 ? -1.374  0.515   -24.104 0.50 76.19  ? 160 SER   B CB  1 
ATOM   1420 O OG  A SER   B 2 151 ? -2.678  -0.015  -24.244 0.50 79.42  ? 160 SER   B OG  1 
ATOM   1421 O OG  B SER   B 2 151 ? -1.061  -0.862  -23.997 0.50 77.22  ? 160 SER   B OG  1 
ATOM   1422 N N   . TYR   B 2 152 ? -3.192  0.894   -21.604 1.00 72.09  ? 161 TYR   B N   1 
ATOM   1423 C CA  . TYR   B 2 152 ? -4.066  0.446   -20.508 1.00 70.79  ? 161 TYR   B CA  1 
ATOM   1424 C C   . TYR   B 2 152 ? -4.792  -0.842  -20.837 1.00 69.18  ? 161 TYR   B C   1 
ATOM   1425 O O   . TYR   B 2 152 ? -5.324  -0.986  -21.939 1.00 70.08  ? 161 TYR   B O   1 
ATOM   1426 C CB  . TYR   B 2 152 ? -5.144  1.513   -20.194 1.00 70.56  ? 161 TYR   B CB  1 
ATOM   1427 C CG  . TYR   B 2 152 ? -5.628  1.491   -18.756 1.00 70.71  ? 161 TYR   B CG  1 
ATOM   1428 C CD1 . TYR   B 2 152 ? -4.800  1.888   -17.716 1.00 71.24  ? 161 TYR   B CD1 1 
ATOM   1429 C CD2 . TYR   B 2 152 ? -6.930  1.118   -18.442 1.00 71.26  ? 161 TYR   B CD2 1 
ATOM   1430 C CE1 . TYR   B 2 152 ? -5.238  1.876   -16.396 1.00 71.96  ? 161 TYR   B CE1 1 
ATOM   1431 C CE2 . TYR   B 2 152 ? -7.377  1.093   -17.121 1.00 71.70  ? 161 TYR   B CE2 1 
ATOM   1432 C CZ  . TYR   B 2 152 ? -6.535  1.499   -16.103 1.00 72.61  ? 161 TYR   B CZ  1 
ATOM   1433 O OH  . TYR   B 2 152 ? -6.964  1.513   -14.790 1.00 74.25  ? 161 TYR   B OH  1 
ATOM   1434 N N   . VAL   B 2 153 ? -4.860  -1.752  -19.864 1.00 66.61  ? 162 VAL   B N   1 
ATOM   1435 C CA  . VAL   B 2 153 ? -5.620  -2.989  -19.984 1.00 64.86  ? 162 VAL   B CA  1 
ATOM   1436 C C   . VAL   B 2 153 ? -6.572  -3.040  -18.772 1.00 62.06  ? 162 VAL   B C   1 
ATOM   1437 O O   . VAL   B 2 153 ? -6.121  -2.994  -17.629 1.00 61.48  ? 162 VAL   B O   1 
ATOM   1438 C CB  . VAL   B 2 153 ? -4.721  -4.243  -20.127 1.00 65.85  ? 162 VAL   B CB  1 
ATOM   1439 C CG1 . VAL   B 2 153 ? -5.558  -5.517  -20.083 1.00 65.83  ? 162 VAL   B CG1 1 
ATOM   1440 C CG2 . VAL   B 2 153 ? -3.916  -4.175  -21.435 1.00 67.05  ? 162 VAL   B CG2 1 
ATOM   1441 N N   . SER   B 2 154 ? -7.882  -3.064  -19.020 1.00 60.29  ? 163 SER   B N   1 
ATOM   1442 C CA  . SER   B 2 154 ? -8.879  -3.015  -17.942 1.00 58.97  ? 163 SER   B CA  1 
ATOM   1443 C C   . SER   B 2 154 ? -9.488  -4.368  -17.606 1.00 58.25  ? 163 SER   B C   1 
ATOM   1444 O O   . SER   B 2 154 ? -9.772  -5.128  -18.515 1.00 59.21  ? 163 SER   B O   1 
ATOM   1445 C CB  . SER   B 2 154 ? -10.017 -2.087  -18.362 1.00 59.14  ? 163 SER   B CB  1 
ATOM   1446 O OG  . SER   B 2 154 ? -11.130 -2.141  -17.477 1.00 61.68  ? 163 SER   B OG  1 
ATOM   1447 N N   . ALA   B 2 155 ? -9.840  -4.599  -16.339 1.00 56.88  ? 164 ALA   B N   1 
ATOM   1448 C CA  . ALA   B 2 155 ? -10.557 -5.818  -15.960 1.00 56.00  ? 164 ALA   B CA  1 
ATOM   1449 C C   . ALA   B 2 155 ? -11.997 -5.702  -16.502 1.00 55.80  ? 164 ALA   B C   1 
ATOM   1450 O O   . ALA   B 2 155 ? -12.487 -4.601  -16.775 1.00 55.66  ? 164 ALA   B O   1 
ATOM   1451 C CB  . ALA   B 2 155 ? -10.607 -5.942  -14.425 1.00 56.05  ? 164 ALA   B CB  1 
ATOM   1452 N N   . ILE   B 2 156 ? -12.677 -6.836  -16.657 1.00 55.75  ? 165 ILE   B N   1 
ATOM   1453 C CA  . ILE   B 2 156 ? -14.106 -6.844  -16.933 1.00 55.33  ? 165 ILE   B CA  1 
ATOM   1454 C C   . ILE   B 2 156 ? -14.655 -6.975  -15.478 1.00 54.12  ? 165 ILE   B C   1 
ATOM   1455 O O   . ILE   B 2 156 ? -14.649 -8.074  -14.911 1.00 53.95  ? 165 ILE   B O   1 
ATOM   1456 C CB  . ILE   B 2 156 ? -14.582 -8.030  -17.797 1.00 56.00  ? 165 ILE   B CB  1 
ATOM   1457 C CG1 . ILE   B 2 156 ? -13.905 -8.006  -19.202 1.00 58.20  ? 165 ILE   B CG1 1 
ATOM   1458 C CG2 . ILE   B 2 156 ? -16.115 -7.958  -17.922 1.00 56.19  ? 165 ILE   B CG2 1 
ATOM   1459 C CD1 . ILE   B 2 156 ? -14.349 -9.132  -20.145 1.00 60.28  ? 165 ILE   B CD1 1 
ATOM   1460 N N   . THR   B 2 157 ? -15.023 -5.844  -14.843 1.00 52.93  ? 166 THR   B N   1 
ATOM   1461 C CA  . THR   B 2 157 ? -15.476 -5.878  -13.439 1.00 51.59  ? 166 THR   B CA  1 
ATOM   1462 C C   . THR   B 2 157 ? -16.980 -6.052  -13.303 1.00 50.34  ? 166 THR   B C   1 
ATOM   1463 O O   . THR   B 2 157 ? -17.737 -5.165  -13.710 1.00 49.16  ? 166 THR   B O   1 
ATOM   1464 C CB  . THR   B 2 157 ? -15.033 -4.635  -12.666 1.00 51.38  ? 166 THR   B CB  1 
ATOM   1465 O OG1 . THR   B 2 157 ? -13.619 -4.447  -12.757 1.00 50.96  ? 166 THR   B OG1 1 
ATOM   1466 C CG2 . THR   B 2 157 ? -15.467 -4.681  -11.208 1.00 51.25  ? 166 THR   B CG2 1 
ATOM   1467 N N   . GLN   B 2 158 ? -17.400 -7.165  -12.701 1.00 49.84  ? 167 GLN   B N   1 
ATOM   1468 C CA  . GLN   B 2 158 ? -18.803 -7.511  -12.497 1.00 50.57  ? 167 GLN   B CA  1 
ATOM   1469 C C   . GLN   B 2 158 ? -19.125 -7.676  -10.976 1.00 52.39  ? 167 GLN   B C   1 
ATOM   1470 O O   . GLN   B 2 158 ? -18.309 -8.202  -10.226 1.00 51.69  ? 167 GLN   B O   1 
ATOM   1471 C CB  . GLN   B 2 158 ? -19.131 -8.812  -13.270 1.00 50.41  ? 167 GLN   B CB  1 
ATOM   1472 C CG  . GLN   B 2 158 ? -20.607 -9.229  -13.286 1.00 51.37  ? 167 GLN   B CG  1 
ATOM   1473 C CD  . GLN   B 2 158 ? -21.558 -8.143  -13.800 1.00 51.94  ? 167 GLN   B CD  1 
ATOM   1474 O OE1 . GLN   B 2 158 ? -21.689 -7.063  -13.205 1.00 51.80  ? 167 GLN   B OE1 1 
ATOM   1475 N NE2 . GLN   B 2 158 ? -22.290 -8.429  -14.870 1.00 48.38  ? 167 GLN   B NE2 1 
ATOM   1476 N N   . GLY   B 2 159 ? -20.301 -7.223  -10.554 1.00 54.45  ? 168 GLY   B N   1 
ATOM   1477 C CA  . GLY   B 2 159 ? -20.747 -7.374  -9.173  1.00 57.85  ? 168 GLY   B CA  1 
ATOM   1478 C C   . GLY   B 2 159 ? -21.554 -8.643  -8.983  1.00 61.53  ? 168 GLY   B C   1 
ATOM   1479 O O   . GLY   B 2 159 ? -21.674 -9.470  -9.896  1.00 62.08  ? 168 GLY   B O   1 
ATOM   1480 N N   . LYS   B 2 160 ? -22.104 -8.817  -7.790  1.00 64.58  ? 169 LYS   B N   1 
ATOM   1481 C CA  . LYS   B 2 160 ? -22.885 -10.007 -7.452  1.00 67.51  ? 169 LYS   B CA  1 
ATOM   1482 C C   . LYS   B 2 160 ? -24.339 -9.596  -7.300  1.00 69.91  ? 169 LYS   B C   1 
ATOM   1483 O O   . LYS   B 2 160 ? -24.622 -8.594  -6.637  1.00 70.61  ? 169 LYS   B O   1 
ATOM   1484 C CB  . LYS   B 2 160 ? -22.395 -10.643 -6.122  1.00 70.23  ? 169 LYS   B CB  1 
ATOM   1485 C CG  . LYS   B 2 160 ? -20.894 -10.490 -5.822  1.00 75.47  ? 169 LYS   B CG  1 
ATOM   1486 C CD  . LYS   B 2 160 ? -20.015 -11.302 -6.776  1.00 79.69  ? 169 LYS   B CD  1 
ATOM   1487 C CE  . LYS   B 2 160 ? -18.556 -10.900 -6.697  1.00 83.80  ? 169 LYS   B CE  1 
ATOM   1488 N NZ  . LYS   B 2 160 ? -18.303 -9.570  -7.325  1.00 86.70  ? 169 LYS   B NZ  1 
ATOM   1489 N N   . ARG   B 2 161 ? -25.261 -10.356 -7.898  1.00 70.99  ? 170 ARG   B N   1 
ATOM   1490 C CA  . ARG   B 2 161 ? -26.689 -10.063 -7.773  1.00 72.53  ? 170 ARG   B CA  1 
ATOM   1491 C C   . ARG   B 2 161 ? -27.239 -10.945 -6.632  1.00 74.80  ? 170 ARG   B C   1 
ATOM   1492 O O   . ARG   B 2 161 ? -27.039 -12.161 -6.641  1.00 74.98  ? 170 ARG   B O   1 
ATOM   1493 C CB  . ARG   B 2 161 ? -27.421 -10.332 -9.107  1.00 72.91  ? 170 ARG   B CB  1 
ATOM   1494 C CG  . ARG   B 2 161 ? -28.846 -9.807  -9.159  1.00 74.55  ? 170 ARG   B CG  1 
ATOM   1495 C CD  . ARG   B 2 161 ? -29.590 -10.299 -10.392 1.00 76.52  ? 170 ARG   B CD  1 
ATOM   1496 N NE  . ARG   B 2 161 ? -31.042 -10.173 -10.248 1.00 78.81  ? 170 ARG   B NE  1 
ATOM   1497 C CZ  . ARG   B 2 161 ? -31.790 -9.278  -10.891 1.00 80.24  ? 170 ARG   B CZ  1 
ATOM   1498 N NH1 . ARG   B 2 161 ? -31.235 -8.430  -11.747 1.00 78.36  ? 170 ARG   B NH1 1 
ATOM   1499 N NH2 . ARG   B 2 161 ? -33.102 -9.235  -10.692 1.00 80.23  ? 170 ARG   B NH2 1 
ATOM   1500 N N   . GLU   B 2 162 ? -27.869 -10.328 -5.622  1.00 76.36  ? 171 GLU   B N   1 
ATOM   1501 C CA  . GLU   B 2 162 ? -28.421 -11.058 -4.481  1.00 78.25  ? 171 GLU   B CA  1 
ATOM   1502 C C   . GLU   B 2 162 ? -29.783 -11.670 -4.831  1.00 79.42  ? 171 GLU   B C   1 
ATOM   1503 O O   . GLU   B 2 162 ? -30.167 -12.697 -4.264  1.00 80.16  ? 171 GLU   B O   1 
ATOM   1504 C CB  . GLU   B 2 162 ? -28.546 -10.126 -3.266  1.00 81.42  ? 171 GLU   B CB  1 
ATOM   1505 C CG  . GLU   B 2 162 ? -27.249 -9.425  -2.899  1.00 88.00  ? 171 GLU   B CG  1 
ATOM   1506 C CD  . GLU   B 2 162 ? -26.292 -10.268 -2.078  1.00 97.41  ? 171 GLU   B CD  1 
ATOM   1507 O OE1 . GLU   B 2 162 ? -25.076 -9.963  -2.083  1.00 98.76  ? 171 GLU   B OE1 1 
ATOM   1508 O OE2 . GLU   B 2 162 ? -26.758 -11.234 -1.428  1.00 100.76 ? 171 GLU   B OE2 1 
HETATM 1509 N N1  . A1BGV C 3 .   ? -4.936  5.447   -20.571 0.89 68.93  ? 301 A1BGV B N1  1 
HETATM 1510 N N3  . A1BGV C 3 .   ? -8.788  4.024   -13.408 0.89 63.09  ? 301 A1BGV B N3  1 
HETATM 1511 C C4  . A1BGV C 3 .   ? -5.694  5.161   -19.490 0.89 67.62  ? 301 A1BGV B C4  1 
HETATM 1512 C C5  . A1BGV C 3 .   ? -7.412  4.733   -18.280 0.89 66.05  ? 301 A1BGV B C5  1 
HETATM 1513 C C6  . A1BGV C 3 .   ? -8.656  4.360   -17.772 0.89 65.41  ? 301 A1BGV B C6  1 
HETATM 1514 C C7  . A1BGV C 3 .   ? -8.820  4.343   -16.406 0.89 64.99  ? 301 A1BGV B C7  1 
HETATM 1515 C C8  . A1BGV C 3 .   ? -7.807  4.770   -15.533 0.89 64.74  ? 301 A1BGV B C8  1 
HETATM 1516 C C10 . A1BGV C 3 .   ? -8.902  4.004   -12.005 0.89 62.77  ? 301 A1BGV B C10 1 
HETATM 1517 C C13 . A1BGV C 3 .   ? -9.281  2.747   -8.561  0.89 62.51  ? 301 A1BGV B C13 1 
HETATM 1518 C C15 . A1BGV C 3 .   ? -6.580  5.155   -16.038 0.89 65.34  ? 301 A1BGV B C15 1 
HETATM 1519 C C1  . A1BGV C 3 .   ? -2.875  6.767   -20.244 0.89 71.05  ? 301 A1BGV B C1  1 
HETATM 1520 C C2  . A1BGV C 3 .   ? -3.467  5.442   -20.690 0.89 70.20  ? 301 A1BGV B C2  1 
HETATM 1521 C C3  . A1BGV C 3 .   ? -2.845  4.261   -19.967 0.89 70.01  ? 301 A1BGV B C3  1 
HETATM 1522 N N2  . A1BGV C 3 .   ? -6.958  4.794   -19.599 0.89 66.96  ? 301 A1BGV B N2  1 
HETATM 1523 C C9  . A1BGV C 3 .   ? -7.934  4.876   -14.043 0.89 64.26  ? 301 A1BGV B C9  1 
HETATM 1524 O O1  . A1BGV C 3 .   ? -7.224  5.654   -13.427 0.89 64.72  ? 301 A1BGV B O1  1 
HETATM 1525 C C11 . A1BGV C 3 .   ? -8.698  5.094   -11.196 0.89 62.67  ? 301 A1BGV B C11 1 
HETATM 1526 N N4  . A1BGV C 3 .   ? -8.834  4.708   -9.912  0.89 62.64  ? 301 A1BGV B N4  1 
HETATM 1527 C C12 . A1BGV C 3 .   ? -9.090  3.364   -9.872  0.89 62.58  ? 301 A1BGV B C12 1 
HETATM 1528 N N5  . A1BGV C 3 .   ? -9.474  1.437   -8.530  0.89 61.70  ? 301 A1BGV B N5  1 
HETATM 1529 O O2  . A1BGV C 3 .   ? -9.272  3.445   -7.539  0.89 63.54  ? 301 A1BGV B O2  1 
HETATM 1530 C C14 . A1BGV C 3 .   ? -9.135  2.900   -11.168 0.89 62.43  ? 301 A1BGV B C14 1 
HETATM 1531 C C16 . A1BGV C 3 .   ? -6.395  5.129   -17.407 0.89 66.17  ? 301 A1BGV B C16 1 
HETATM 1532 N N6  . A1BGV C 3 .   ? -5.316  5.436   -18.213 0.89 66.81  ? 301 A1BGV B N6  1 
HETATM 1533 S S   . DMS   D 4 .   ? -13.629 11.881  -9.401  1.00 152.80 ? 302 DMS   B S   1 
HETATM 1534 O O   . DMS   D 4 .   ? -14.608 11.158  -8.587  1.00 152.85 ? 302 DMS   B O   1 
HETATM 1535 C C1  . DMS   D 4 .   ? -12.083 11.616  -8.577  1.00 152.79 ? 302 DMS   B C1  1 
HETATM 1536 C C2  . DMS   D 4 .   ? -13.377 10.861  -10.819 1.00 152.74 ? 302 DMS   B C2  1 
HETATM 1537 S S   . SO4   E 5 .   ? -14.372 -22.038 -20.532 1.00 170.68 ? 303 SO4   B S   1 
HETATM 1538 O O1  . SO4   E 5 .   ? -15.746 -21.744 -20.945 1.00 170.72 ? 303 SO4   B O1  1 
HETATM 1539 O O2  . SO4   E 5 .   ? -14.255 -21.919 -19.078 1.00 170.64 ? 303 SO4   B O2  1 
HETATM 1540 O O3  . SO4   E 5 .   ? -14.020 -23.400 -20.942 1.00 170.67 ? 303 SO4   B O3  1 
HETATM 1541 O O4  . SO4   E 5 .   ? -13.468 -21.086 -21.173 1.00 170.66 ? 303 SO4   B O4  1 
HETATM 1542 S S   . SO4   F 5 .   ? -18.894 11.238  -0.315  1.00 129.23 ? 304 SO4   B S   1 
HETATM 1543 O O1  . SO4   F 5 .   ? -19.697 10.022  -0.175  1.00 129.13 ? 304 SO4   B O1  1 
HETATM 1544 O O2  . SO4   F 5 .   ? -17.506 10.867  -0.623  1.00 129.20 ? 304 SO4   B O2  1 
HETATM 1545 O O3  . SO4   F 5 .   ? -19.426 12.082  -1.381  1.00 129.29 ? 304 SO4   B O3  1 
HETATM 1546 O O4  . SO4   F 5 .   ? -18.949 12.007  0.927   1.00 129.32 ? 304 SO4   B O4  1 
HETATM 1547 O O   . HOH   G 6 .   ? -4.140  -14.586 -25.501 1.00 62.51  ? 101 HOH   A O   1 
HETATM 1548 O O   . HOH   G 6 .   ? -29.023 15.270  -15.094 1.00 63.90  ? 102 HOH   A O   1 
HETATM 1549 O O   . HOH   G 6 .   ? -7.986  0.261   3.444   1.00 62.16  ? 103 HOH   A O   1 
HETATM 1550 O O   . HOH   G 6 .   ? -2.173  -4.329  -6.354  1.00 58.34  ? 104 HOH   A O   1 
HETATM 1551 O O   . HOH   G 6 .   ? -24.112 9.128   -27.369 1.00 58.53  ? 105 HOH   A O   1 
HETATM 1552 O O   . HOH   G 6 .   ? -23.852 19.036  -19.376 1.00 62.15  ? 106 HOH   A O   1 
HETATM 1553 O O   . HOH   G 6 .   ? -6.670  -9.417  -3.168  1.00 61.83  ? 107 HOH   A O   1 
HETATM 1554 O O   . HOH   G 6 .   ? -8.222  1.328   1.127   1.00 66.34  ? 108 HOH   A O   1 
HETATM 1555 O O   . HOH   G 6 .   ? -2.793  -11.943 -7.140  1.00 53.36  ? 109 HOH   A O   1 
HETATM 1556 O O   . HOH   G 6 .   ? -8.337  -2.329  6.747   1.00 62.93  ? 110 HOH   A O   1 
HETATM 1557 O O   . HOH   G 6 .   ? 6.916   -4.649  -17.034 1.00 68.18  ? 111 HOH   A O   1 
HETATM 1558 O O   . HOH   G 6 .   ? -4.191  -0.864  -0.198  1.00 72.04  ? 112 HOH   A O   1 
HETATM 1559 O O   . HOH   G 6 .   ? -3.490  -4.578  0.208   1.00 72.80  ? 113 HOH   A O   1 
HETATM 1560 O O   . HOH   G 6 .   ? -28.358 -6.507  -28.188 1.00 65.42  ? 114 HOH   A O   1 
HETATM 1561 O O   . HOH   G 6 .   ? -4.397  -10.483 -5.627  1.00 53.92  ? 115 HOH   A O   1 
HETATM 1562 O O   . HOH   G 6 .   ? -21.628 -9.103  -34.838 1.00 66.14  ? 116 HOH   A O   1 
HETATM 1563 O O   . HOH   G 6 .   ? -31.000 -0.097  -22.987 1.00 66.59  ? 117 HOH   A O   1 
HETATM 1564 O O   . HOH   H 6 .   ? -15.285 -5.263  1.529   1.00 50.87  ? 401 HOH   B O   1 
HETATM 1565 O O   . HOH   H 6 .   ? 1.434   -1.379  -14.296 1.00 73.01  ? 402 HOH   B O   1 
HETATM 1566 O O   . HOH   H 6 .   ? -33.984 1.409   -15.376 1.00 63.79  ? 403 HOH   B O   1 
HETATM 1567 O O   . HOH   H 6 .   ? -14.686 -7.267  -1.501  1.00 61.27  ? 404 HOH   B O   1 
HETATM 1568 O O   . HOH   H 6 .   ? -16.459 20.515  -14.277 1.00 67.67  ? 405 HOH   B O   1 
HETATM 1569 O O   . HOH   H 6 .   ? -6.407  -0.691  -10.950 1.00 47.80  ? 406 HOH   B O   1 
HETATM 1570 O O   . HOH   H 6 .   ? -3.255  6.250   -16.756 1.00 73.63  ? 407 HOH   B O   1 
HETATM 1571 O O   . HOH   H 6 .   ? -9.453  -7.124  -25.520 1.00 60.09  ? 408 HOH   B O   1 
HETATM 1572 O O   . HOH   H 6 .   ? -17.185 12.533  -5.322  1.00 58.46  ? 409 HOH   B O   1 
HETATM 1573 O O   . HOH   H 6 .   ? -6.955  -11.176 -5.282  1.00 61.39  ? 410 HOH   B O   1 
HETATM 1574 O O   . HOH   H 6 .   ? -6.636  -10.754 -0.465  1.00 76.38  ? 411 HOH   B O   1 
HETATM 1575 O O   . HOH   H 6 .   ? -5.381  2.622   -12.889 1.00 73.08  ? 412 HOH   B O   1 
HETATM 1576 O O   . HOH   H 6 .   ? -26.108 -8.555  -16.595 1.00 49.99  ? 413 HOH   B O   1 
HETATM 1577 O O   . HOH   H 6 .   ? -17.848 -11.082 -16.623 1.00 56.76  ? 414 HOH   B O   1 
HETATM 1578 O O   . HOH   H 6 .   ? -24.072 -6.748  -4.667  1.00 58.64  ? 415 HOH   B O   1 
HETATM 1579 O O   . HOH   H 6 .   ? -12.937 -2.646  -14.859 1.00 44.03  ? 416 HOH   B O   1 
HETATM 1580 O O   . HOH   H 6 .   ? -35.437 3.530   -8.905  1.00 72.52  ? 417 HOH   B O   1 
HETATM 1581 O O   . HOH   H 6 .   ? -27.895 -6.757  -18.601 1.00 54.99  ? 418 HOH   B O   1 
HETATM 1582 O O   . HOH   H 6 .   ? -9.330  7.556   -8.130  1.00 82.90  ? 419 HOH   B O   1 
HETATM 1583 O O   . HOH   H 6 .   ? -32.519 -7.383  -7.033  1.00 65.30  ? 420 HOH   B O   1 
HETATM 1584 O O   . HOH   H 6 .   ? -22.199 14.743  -5.989  1.00 64.38  ? 421 HOH   B O   1 
HETATM 1585 O O   . HOH   H 6 .   ? -16.999 8.449   -30.367 1.00 69.61  ? 422 HOH   B O   1 
HETATM 1586 O O   . HOH   H 6 .   ? -7.265  -7.028  0.431   1.00 71.64  ? 423 HOH   B O   1 
HETATM 1587 O O   . HOH   H 6 .   ? -21.883 -14.336 -21.789 1.00 67.82  ? 424 HOH   B O   1 
HETATM 1588 O O   . HOH   H 6 .   ? -14.879 12.903  -6.352  1.00 79.67  ? 425 HOH   B O   1 
HETATM 1589 O O   . HOH   H 6 .   ? -24.867 12.777  -23.562 1.00 65.53  ? 426 HOH   B O   1 
HETATM 1590 O O   . HOH   H 6 .   ? -12.442 -4.041  -10.177 1.00 50.73  ? 427 HOH   B O   1 
HETATM 1591 O O   . HOH   H 6 .   ? -15.620 -10.754 -15.204 1.00 62.14  ? 428 HOH   B O   1 
HETATM 1592 O O   . HOH   H 6 .   ? -27.958 19.759  -15.468 1.00 81.52  ? 429 HOH   B O   1 
HETATM 1593 O O   . HOH   H 6 .   ? -16.044 -7.340  -8.505  1.00 69.67  ? 430 HOH   B O   1 
HETATM 1594 O O   . HOH   H 6 .   ? -31.930 6.815   -4.432  1.00 66.24  ? 431 HOH   B O   1 
HETATM 1595 O O   . HOH   H 6 .   ? -21.292 6.321   0.000   0.50 59.98  ? 432 HOH   B O   1 
HETATM 1596 O O   . HOH   H 6 .   ? 3.699   -5.629  -19.377 1.00 98.34  ? 433 HOH   B O   1 
HETATM 1597 O O   . HOH   H 6 .   ? -18.720 14.805  -22.140 1.00 60.81  ? 434 HOH   B O   1 
HETATM 1598 O O   . HOH   H 6 .   ? -14.523 -12.891 -16.503 1.00 61.25  ? 435 HOH   B O   1 
HETATM 1599 O O   . HOH   H 6 .   ? -6.816  8.832   -18.485 1.00 73.04  ? 436 HOH   B O   1 
HETATM 1600 O O   B HOH   H 6 .   ? -28.554 6.345   0.814   0.50 45.43  ? 437 HOH   B O   1 
HETATM 1601 O O   . HOH   H 6 .   ? -25.972 -5.152  -4.110  1.00 51.72  ? 438 HOH   B O   1 
HETATM 1602 O O   . HOH   H 6 .   ? -18.773 -7.053  -5.762  1.00 69.72  ? 439 HOH   B O   1 
HETATM 1603 O O   . HOH   H 6 .   ? -10.790 11.741  -19.006 1.00 59.72  ? 440 HOH   B O   1 
HETATM 1604 O O   . HOH   H 6 .   ? -19.586 -13.956 -23.084 1.00 57.17  ? 441 HOH   B O   1 
HETATM 1605 O O   . HOH   H 6 .   ? -7.645  3.523   -4.964  1.00 78.25  ? 442 HOH   B O   1 
HETATM 1606 O O   . HOH   H 6 .   ? -9.064  -11.069 -7.645  1.00 67.84  ? 443 HOH   B O   1 
HETATM 1607 O O   . HOH   H 6 .   ? -19.759 -6.252  -0.834  1.00 57.08  ? 444 HOH   B O   1 
HETATM 1608 O O   . HOH   H 6 .   ? -30.816 4.223   -2.581  1.00 62.32  ? 445 HOH   B O   1 
HETATM 1609 O O   . HOH   H 6 .   ? -15.898 -14.868 -31.028 1.00 73.16  ? 446 HOH   B O   1 
HETATM 1610 O O   . HOH   H 6 .   ? -15.030 -8.995  -11.644 1.00 72.52  ? 447 HOH   B O   1 
HETATM 1611 O O   . HOH   H 6 .   ? -6.624  7.117   -23.667 1.00 69.60  ? 448 HOH   B O   1 
HETATM 1612 O O   . HOH   H 6 .   ? -11.711 -5.711  -8.301  1.00 53.02  ? 449 HOH   B O   1 
HETATM 1613 O O   . HOH   H 6 .   ? -19.950 6.639   -32.704 1.00 71.28  ? 450 HOH   B O   1 
HETATM 1614 O O   . HOH   H 6 .   ? -10.695 8.809   -10.248 1.00 79.86  ? 451 HOH   B O   1 
HETATM 1615 O O   . HOH   H 6 .   ? -17.906 -16.393 -30.750 1.00 69.04  ? 452 HOH   B O   1 
HETATM 1616 O O   . HOH   H 6 .   ? -21.964 -14.440 -25.859 1.00 78.84  ? 453 HOH   B O   1 
HETATM 1617 O O   . HOH   H 6 .   ? -31.429 -11.155 -27.067 0.50 81.10  ? 454 HOH   B O   1 
HETATM 1618 O O   . HOH   H 6 .   ? -24.356 -15.682 -17.803 1.00 82.62  ? 455 HOH   B O   1 
HETATM 1619 O O   . HOH   H 6 .   ? -10.999 -12.913 -8.616  1.00 81.77  ? 456 HOH   B O   1 
HETATM 1620 O O   . HOH   H 6 .   ? -1.216  -15.369 -10.188 1.00 84.28  ? 457 HOH   B O   1 
HETATM 1621 O O   . HOH   H 6 .   ? -29.471 -6.071  -1.087  1.00 59.00  ? 458 HOH   B O   1 
HETATM 1622 O O   . HOH   H 6 .   ? -10.634 7.949   -13.156 1.00 65.66  ? 459 HOH   B O   1 
HETATM 1623 O O   . HOH   H 6 .   ? -17.114 16.651  -21.780 1.00 62.86  ? 460 HOH   B O   1 
HETATM 1624 O O   . HOH   H 6 .   ? -20.458 -8.227  -2.648  1.00 75.58  ? 461 HOH   B O   1 
HETATM 1625 O O   . HOH   H 6 .   ? -21.292 3.573   -0.000  0.50 75.22  ? 462 HOH   B O   1 
HETATM 1626 O O   . HOH   H 6 .   ? -11.229 -7.675  2.265   1.00 68.00  ? 463 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   ? 1.4439 0.3712 1.3811 0.1464  0.0008  -0.2297 50  ASP   A N   
2    C CA  . ASP   A 7   ? 1.4196 0.4392 1.3304 0.1915  -0.0005 -0.2292 50  ASP   A CA  
3    C C   . ASP   A 7   ? 1.3927 0.4166 1.2787 0.1902  0.0190  -0.1633 50  ASP   A C   
4    O O   . ASP   A 7   ? 1.4460 0.3687 1.3133 0.1867  0.0269  -0.1219 50  ASP   A O   
5    C CB  . ASP   A 7   ? 1.4912 0.4705 1.3821 0.2552  -0.0228 -0.2672 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 1.5635 0.6610 1.4448 0.2984  -0.0261 -0.2883 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 1.5418 0.7555 1.4364 0.2775  -0.0165 -0.2991 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 1.6265 0.7015 1.4877 0.3532  -0.0380 -0.2940 50  ASP   A OD2 
9    N N   . MET   A 8   ? 1.3144 0.4503 1.1972 0.1920  0.0274  -0.1527 51  MET   A N   
10   C CA  . MET   A 8   ? 1.2824 0.4295 1.1429 0.1921  0.0427  -0.0982 51  MET   A CA  
11   C C   . MET   A 8   ? 1.2586 0.4301 1.0926 0.2456  0.0332  -0.0972 51  MET   A C   
12   O O   . MET   A 8   ? 1.2315 0.4743 1.0754 0.2711  0.0227  -0.1373 51  MET   A O   
13   C CB  . MET   A 8   ? 1.2282 0.4677 1.1044 0.1537  0.0581  -0.0817 51  MET   A CB  
14   C CG  . MET   A 8   ? 1.2114 0.4288 1.1140 0.1032  0.0690  -0.0712 51  MET   A CG  
15   S SD  . MET   A 8   ? 1.1377 0.4639 1.0585 0.0680  0.0808  -0.0595 51  MET   A SD  
16   C CE  . MET   A 8   ? 1.1262 0.4196 1.0924 0.0163  0.0847  -0.0692 51  MET   A CE  
17   N N   . TYR   A 9   ? 1.2589 0.3811 1.0600 0.2624  0.0378  -0.0524 52  TYR   A N   
18   C CA  . TYR   A 9   ? 1.2439 0.3889 1.0201 0.3158  0.0248  -0.0512 52  TYR   A CA  
19   C C   . TYR   A 9   ? 1.2225 0.3930 0.9759 0.3124  0.0356  -0.0070 52  TYR   A C   
20   O O   . TYR   A 9   ? 1.2452 0.3790 0.9883 0.2784  0.0545  0.0329  52  TYR   A O   
21   C CB  . TYR   A 9   ? 1.3013 0.3415 1.0470 0.3675  0.0056  -0.0561 52  TYR   A CB  
22   C CG  . TYR   A 9   ? 1.3895 0.2958 1.0963 0.3596  0.0154  -0.0044 52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 1.4380 0.2499 1.1566 0.3250  0.0226  -0.0038 52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 1.4389 0.3085 1.0941 0.3910  0.0162  0.0412  52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 1.5102 0.1943 1.1944 0.3128  0.0364  0.0469  52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 1.5088 0.2531 1.1194 0.3846  0.0299  0.0944  52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 1.5602 0.2101 1.1868 0.3423  0.0426  0.0996  52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 1.6591 0.1759 1.2423 0.3327  0.0598  0.1547  52  TYR   A OH  
29   N N   . ILE   A 10  ? 1.1642 0.4125 0.9167 0.3440  0.0247  -0.0195 53  ILE   A N   
30   C CA  . ILE   A 10  ? 1.1123 0.3926 0.8447 0.3459  0.0296  0.0121  53  ILE   A CA  
31   C C   . ILE   A 10  ? 1.1071 0.3379 0.7929 0.4046  0.0116  0.0273  53  ILE   A C   
32   O O   . ILE   A 10  ? 1.1106 0.3073 0.7873 0.4510  -0.0087 0.0052  53  ILE   A O   
33   C CB  . ILE   A 10  ? 1.0639 0.4630 0.8299 0.3279  0.0319  -0.0077 53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 1.0349 0.5087 0.8284 0.3602  0.0150  -0.0548 53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 1.0467 0.4782 0.8401 0.2724  0.0509  -0.0071 53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 0.9919 0.5744 0.8163 0.3408  0.0194  -0.0673 53  ILE   A CD1 
37   N N   . GLU   A 11  ? 1.1050 0.3209 0.7537 0.4070  0.0185  0.0670  54  GLU   A N   
38   C CA  . GLU   A 11  ? 1.1384 0.2976 0.7259 0.4638  0.0032  0.0916  54  GLU   A CA  
39   C C   . GLU   A 11  ? 1.1204 0.3509 0.6970 0.4652  0.0029  0.1017  54  GLU   A C   
40   O O   . GLU   A 11  ? 1.0314 0.2650 0.6072 0.4228  0.0268  0.1284  54  GLU   A O   
41   C CB  . GLU   A 11  ? 1.1972 0.2419 0.7370 0.4468  0.0253  0.1448  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 1.3237 0.2553 0.8270 0.4873  0.0118  0.1507  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 1.4917 0.2895 0.9516 0.4665  0.0375  0.2089  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 1.4274 0.2359 0.8768 0.4267  0.0666  0.2465  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 1.5601 0.2458 0.9936 0.4897  0.0295  0.2160  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 1.1539 0.4331 0.7179 0.5174  -0.0253 0.0811  55  ARG   A N   
47   C CA  . ARG   A 12  ? 1.1756 0.5239 0.7350 0.5148  -0.0281 0.0825  55  ARG   A CA  
48   C C   . ARG   A 12  ? 1.2375 0.5174 0.7263 0.5189  -0.0117 0.1375  55  ARG   A C   
49   O O   . ARG   A 12  ? 1.2910 0.4754 0.7224 0.5471  -0.0089 0.1723  55  ARG   A O   
50   C CB  . ARG   A 12  ? 1.1767 0.6010 0.7462 0.5672  -0.0646 0.0416  55  ARG   A CB  
51   C CG  . ARG   A 12  ? 1.1719 0.6900 0.7719 0.5453  -0.0682 0.0217  55  ARG   A CG  
52   C CD  . ARG   A 12  ? 1.1576 0.7775 0.8039 0.5746  -0.1003 -0.0335 55  ARG   A CD  
53   N NE  . ARG   A 12  ? 1.1408 0.8359 0.8174 0.5478  -0.1036 -0.0523 55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 1.1622 0.8618 0.7969 0.5769  -0.1209 -0.0477 55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 1.2287 0.8652 0.7836 0.6345  -0.1337 -0.0198 55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 1.0802 0.8406 0.7468 0.5494  -0.1249 -0.0697 55  ARG   A NH2 
57   N N   . ALA   A 13  ? 1.2258 0.5481 0.7183 0.4889  0.0025  0.1470  56  ALA   A N   
58   C CA  . ALA   A 13  ? 1.2792 0.5551 0.7073 0.4926  0.0220  0.1956  56  ALA   A CA  
59   C C   . ALA   A 13  ? 1.2754 0.6108 0.6749 0.5244  0.0039  0.1845  56  ALA   A C   
60   O O   . ALA   A 13  ? 1.3236 0.6243 0.6545 0.5459  0.0145  0.2216  56  ALA   A O   
61   C CB  . ALA   A 13  ? 1.2847 0.5536 0.7387 0.4294  0.0590  0.2184  56  ALA   A CB  
62   N N   . GLY   A 14  ? 1.2115 0.6351 0.6628 0.5242  -0.0206 0.1344  57  GLY   A N   
63   C CA  . GLY   A 14  ? 1.1902 0.6702 0.6225 0.5520  -0.0423 0.1147  57  GLY   A CA  
64   C C   . GLY   A 14  ? 1.1308 0.7024 0.6383 0.5247  -0.0581 0.0625  57  GLY   A C   
65   O O   . GLY   A 14  ? 1.0769 0.6755 0.6507 0.4853  -0.0512 0.0423  57  GLY   A O   
66   N N   . ASP   A 15  ? 1.1216 0.7395 0.6151 0.5471  -0.0800 0.0397  58  ASP   A N   
67   C CA  . ASP   A 15  ? 1.0815 0.7776 0.6398 0.5220  -0.0970 -0.0095 58  ASP   A CA  
68   C C   . ASP   A 15  ? 1.0946 0.7813 0.6591 0.4779  -0.0734 0.0041  58  ASP   A C   
69   O O   . ASP   A 15  ? 1.1380 0.7812 0.6448 0.4869  -0.0547 0.0412  58  ASP   A O   
70   C CB  . ASP   A 15  ? 1.0886 0.8350 0.6270 0.5729  -0.1380 -0.0471 58  ASP   A CB  
71   C CG  . ASP   A 15  ? 1.1617 0.9476 0.7152 0.6182  -0.1714 -0.0790 58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 1.1537 0.9153 0.7200 0.6185  -0.1618 -0.0669 58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 1.1984 1.0408 0.7480 0.6595  -0.2100 -0.1190 58  ASP   A OD2 
74   N N   . ILE   A 16  ? 1.0520 0.7814 0.6842 0.4337  -0.0746 -0.0262 59  ILE   A N   
75   C CA  . ILE   A 16  ? 1.0591 0.7768 0.6976 0.3977  -0.0577 -0.0174 59  ILE   A CA  
76   C C   . ILE   A 16  ? 1.0630 0.8130 0.6985 0.4147  -0.0850 -0.0538 59  ILE   A C   
77   O O   . ILE   A 16  ? 1.0219 0.8167 0.7151 0.3952  -0.1042 -0.0961 59  ILE   A O   
78   C CB  . ILE   A 16  ? 1.0294 0.7549 0.7302 0.3400  -0.0392 -0.0191 59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 1.0509 0.7392 0.7433 0.3290  -0.0136 0.0158  59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 1.0313 0.7459 0.7398 0.3097  -0.0300 -0.0167 59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 1.0371 0.7402 0.7815 0.2838  0.0006  0.0110  59  ILE   A CD1 
82   N N   A THR   A 17  ? 1.1031 0.8328 0.6706 0.4523  -0.0867 -0.0394 60  THR   A N   
83   N N   B THR   A 17  ? 1.1026 0.8322 0.6705 0.4518  -0.0865 -0.0394 60  THR   A N   
84   C CA  A THR   A 17  ? 1.1147 0.8718 0.6671 0.4774  -0.1151 -0.0771 60  THR   A CA  
85   C CA  B THR   A 17  ? 1.1136 0.8721 0.6656 0.4794  -0.1165 -0.0780 60  THR   A CA  
86   C C   A THR   A 17  ? 1.1595 0.8876 0.6589 0.4870  -0.0971 -0.0544 60  THR   A C   
87   C C   B THR   A 17  ? 1.1608 0.8910 0.6556 0.4925  -0.0998 -0.0558 60  THR   A C   
88   O O   A THR   A 17  ? 1.1871 0.8815 0.6401 0.4941  -0.0666 -0.0063 60  THR   A O   
89   O O   B THR   A 17  ? 1.1906 0.8876 0.6339 0.5044  -0.0710 -0.0079 60  THR   A O   
90   C CB  A THR   A 17  ? 1.1335 0.9179 0.6404 0.5411  -0.1488 -0.0970 60  THR   A CB  
91   C CB  B THR   A 17  ? 1.1280 0.9148 0.6425 0.5397  -0.1493 -0.0970 60  THR   A CB  
92   O OG1 A THR   A 17  ? 1.1853 0.9259 0.6084 0.5800  -0.1301 -0.0460 60  THR   A OG1 
93   O OG1 B THR   A 17  ? 1.0990 0.9222 0.6753 0.5286  -0.1635 -0.1212 60  THR   A OG1 
94   C CG2 A THR   A 17  ? 1.1016 0.9351 0.6667 0.5424  -0.1752 -0.1337 60  THR   A CG2 
95   C CG2 B THR   A 17  ? 1.1279 0.9531 0.6221 0.5762  -0.1870 -0.1444 60  THR   A CG2 
96   N N   . TRP   A 18  ? 1.1653 0.9091 0.6723 0.4892  -0.1166 -0.0921 61  TRP   A N   
97   C CA  . TRP   A 18  ? 1.2273 0.9552 0.6819 0.5095  -0.1045 -0.0812 61  TRP   A CA  
98   C C   . TRP   A 18  ? 1.3112 1.0539 0.6798 0.5771  -0.1181 -0.0795 61  TRP   A C   
99   O O   . TRP   A 18  ? 1.3137 1.0890 0.6802 0.6076  -0.1563 -0.1187 61  TRP   A O   
100  C CB  . TRP   A 18  ? 1.2038 0.9378 0.6936 0.4959  -0.1279 -0.1306 61  TRP   A CB  
101  C CG  . TRP   A 18  ? 1.2337 0.9584 0.6722 0.5251  -0.1221 -0.1324 61  TRP   A CG  
102  C CD1 . TRP   A 18  ? 1.2604 1.0072 0.6404 0.5801  -0.1452 -0.1623 61  TRP   A CD1 
103  C CD2 . TRP   A 18  ? 1.2376 0.9359 0.6838 0.5037  -0.0961 -0.1125 61  TRP   A CD2 
104  N NE1 . TRP   A 18  ? 1.2778 1.0145 0.6271 0.5945  -0.1310 -0.1604 61  TRP   A NE1 
105  C CE2 . TRP   A 18  ? 1.2636 0.9715 0.6552 0.5489  -0.1015 -0.1302 61  TRP   A CE2 
106  C CE3 . TRP   A 18  ? 1.2336 0.9063 0.7238 0.4560  -0.0698 -0.0825 61  TRP   A CE3 
107  C CZ2 . TRP   A 18  ? 1.2722 0.9673 0.6589 0.5479  -0.0819 -0.1211 61  TRP   A CZ2 
108  C CZ3 . TRP   A 18  ? 1.2484 0.9070 0.7319 0.4557  -0.0531 -0.0725 61  TRP   A CZ3 
109  C CH2 . TRP   A 18  ? 1.2610 0.9318 0.6959 0.5014  -0.0587 -0.0918 61  TRP   A CH2 
110  N N   . GLU   A 19  ? 1.3739 1.0971 0.6723 0.6005  -0.0863 -0.0333 62  GLU   A N   
111  C CA  . GLU   A 19  ? 1.4421 1.1743 0.6458 0.6653  -0.0931 -0.0229 62  GLU   A CA  
112  C C   . GLU   A 19  ? 1.4900 1.2442 0.6496 0.6964  -0.0975 -0.0471 62  GLU   A C   
113  O O   . GLU   A 19  ? 1.4899 1.2355 0.6437 0.6809  -0.0630 -0.0227 62  GLU   A O   
114  C CB  . GLU   A 19  ? 1.5120 1.2057 0.6582 0.6715  -0.0501 0.0492  62  GLU   A CB  
115  C CG  . GLU   A 19  ? 1.6531 1.3481 0.6869 0.7396  -0.0511 0.0701  62  GLU   A CG  
116  C CD  . GLU   A 19  ? 1.8078 1.4639 0.7756 0.7409  0.0026  0.1448  62  GLU   A CD  
117  O OE1 . GLU   A 19  ? 1.8469 1.4704 0.8623 0.6881  0.0372  0.1806  62  GLU   A OE1 
118  O OE2 . GLU   A 19  ? 1.8768 1.5364 0.7449 0.7937  0.0108  0.1668  62  GLU   A OE2 
119  N N   . LYS   A 20  ? 1.5260 1.3142 0.6524 0.7452  -0.1408 -0.0979 63  LYS   A N   
120  C CA  . LYS   A 20  ? 1.5755 1.3867 0.6505 0.7845  -0.1488 -0.1275 63  LYS   A CA  
121  C C   . LYS   A 20  ? 1.6408 1.4488 0.6135 0.8231  -0.1062 -0.0687 63  LYS   A C   
122  O O   . LYS   A 20  ? 1.6718 1.4614 0.5947 0.8396  -0.0909 -0.0203 63  LYS   A O   
123  C CB  . LYS   A 20  ? 1.6132 1.4651 0.6717 0.8317  -0.2085 -0.1987 63  LYS   A CB  
124  C CG  . LYS   A 20  ? 1.6526 1.5123 0.8042 0.7955  -0.2459 -0.2703 63  LYS   A CG  
125  C CD  . LYS   A 20  ? 1.7001 1.6070 0.8515 0.8350  -0.3082 -0.3456 63  LYS   A CD  
126  C CE  . LYS   A 20  ? 1.7368 1.6657 0.9433 0.8189  -0.3308 -0.3541 63  LYS   A CE  
127  N NZ  . LYS   A 20  ? 1.7609 1.7503 0.9600 0.8673  -0.3924 -0.4256 63  LYS   A NZ  
128  N N   . ASP   A 21  ? 1.6668 1.4894 0.6117 0.8342  -0.0836 -0.0694 64  ASP   A N   
129  C CA  . ASP   A 21  ? 1.7223 1.5535 0.5742 0.8666  -0.0366 -0.0137 64  ASP   A CA  
130  C C   . ASP   A 21  ? 1.7334 1.5259 0.5972 0.8221  0.0164  0.0653  64  ASP   A C   
131  O O   . ASP   A 21  ? 1.7700 1.5475 0.5549 0.8471  0.0427  0.1188  64  ASP   A O   
132  C CB  . ASP   A 21  ? 1.8091 1.6626 0.5476 0.9437  -0.0581 -0.0183 64  ASP   A CB  
133  C CG  . ASP   A 21  ? 1.9229 1.8176 0.6486 0.9911  -0.1178 -0.1035 64  ASP   A CG  
134  O OD1 . ASP   A 21  ? 1.9422 1.8581 0.6841 0.9941  -0.1210 -0.1446 64  ASP   A OD1 
135  O OD2 . ASP   A 21  ? 1.9752 1.8820 0.6740 1.0287  -0.1632 -0.1321 64  ASP   A OD2 
136  N N   . ALA   A 22  ? 1.7012 1.4735 0.6602 0.7570  0.0308  0.0720  65  ALA   A N   
137  C CA  . ALA   A 22  ? 1.7032 1.4422 0.6821 0.7121  0.0779  0.1373  65  ALA   A CA  
138  C C   . ALA   A 22  ? 1.6991 1.4644 0.6543 0.7069  0.1322  0.1734  65  ALA   A C   
139  O O   . ALA   A 22  ? 1.6886 1.4980 0.6238 0.7362  0.1294  0.1419  65  ALA   A O   
140  C CB  . ALA   A 22  ? 1.6787 1.3953 0.7642 0.6497  0.0690  0.1251  65  ALA   A CB  
141  N N   . GLU   A 23  ? 1.7067 1.4492 0.6653 0.6713  0.1814  0.2358  66  GLU   A N   
142  C CA  . GLU   A 23  ? 1.7041 1.4839 0.6567 0.6579  0.2363  0.2685  66  GLU   A CA  
143  C C   . GLU   A 23  ? 1.6458 1.4593 0.6897 0.6257  0.2310  0.2306  66  GLU   A C   
144  O O   . GLU   A 23  ? 1.6232 1.4093 0.7451 0.5791  0.2189  0.2247  66  GLU   A O   
145  C CB  . GLU   A 23  ? 1.7728 1.5141 0.7280 0.6147  0.2864  0.3386  66  GLU   A CB  
146  C CG  . GLU   A 23  ? 1.8476 1.6358 0.8315 0.5814  0.3444  0.3681  66  GLU   A CG  
147  C CD  . GLU   A 23  ? 1.9774 1.7242 0.9733 0.5309  0.3932  0.4332  66  GLU   A CD  
148  O OE1 . GLU   A 23  ? 2.0064 1.6854 1.0316 0.5033  0.3762  0.4432  66  GLU   A OE1 
149  O OE2 . GLU   A 23  ? 2.0050 1.7885 0.9833 0.5182  0.4495  0.4722  66  GLU   A OE2 
150  N N   . VAL   A 24  ? 1.6152 1.4866 0.6442 0.6560  0.2371  0.2033  67  VAL   A N   
151  C CA  . VAL   A 24  ? 1.5685 1.4666 0.6749 0.6363  0.2282  0.1668  67  VAL   A CA  
152  C C   . VAL   A 24  ? 1.5179 1.4673 0.6549 0.6100  0.2835  0.2003  67  VAL   A C   
153  O O   . VAL   A 24  ? 1.5261 1.5272 0.6099 0.6383  0.3201  0.2177  67  VAL   A O   
154  C CB  . VAL   A 24  ? 1.5838 1.5058 0.6698 0.6874  0.1891  0.1021  67  VAL   A CB  
155  C CG1 . VAL   A 24  ? 1.5660 1.4863 0.7325 0.6652  0.1699  0.0662  67  VAL   A CG1 
156  C CG2 . VAL   A 24  ? 1.6161 1.5026 0.6658 0.7168  0.1377  0.0670  67  VAL   A CG2 
157  N N   . THR   A 25  ? 1.4651 1.4073 0.6878 0.5560  0.2906  0.2087  68  THR   A N   
158  C CA  . THR   A 25  ? 1.4111 1.4099 0.6805 0.5244  0.3391  0.2350  68  THR   A CA  
159  C C   . THR   A 25  ? 1.3546 1.3589 0.7181 0.4897  0.3207  0.2106  68  THR   A C   
160  O O   . THR   A 25  ? 1.3545 1.3122 0.7389 0.4891  0.2752  0.1798  68  THR   A O   
161  C CB  . THR   A 25  ? 1.4451 1.4249 0.6986 0.4873  0.3868  0.2989  68  THR   A CB  
162  O OG1 . THR   A 25  ? 1.4315 1.4846 0.7169 0.4645  0.4410  0.3226  68  THR   A OG1 
163  C CG2 . THR   A 25  ? 1.4528 1.3629 0.7537 0.4376  0.3721  0.3140  68  THR   A CG2 
164  N N   . GLY   A 26  ? 1.3007 1.3674 0.7184 0.4641  0.3558  0.2229  69  GLY   A N   
165  C CA  . GLY   A 26  ? 1.2604 1.3408 0.7604 0.4374  0.3387  0.2019  69  GLY   A CA  
166  C C   . GLY   A 26  ? 1.2310 1.3462 0.7415 0.4811  0.3112  0.1539  69  GLY   A C   
167  O O   . GLY   A 26  ? 1.2546 1.3451 0.7151 0.5269  0.2823  0.1239  69  GLY   A O   
168  N N   . ASN   A 27  ? 1.1749 1.3444 0.7523 0.4684  0.3165  0.1434  70  ASN   A N   
169  C CA  . ASN   A 27  ? 1.1503 1.3499 0.7428 0.5121  0.2896  0.0995  70  ASN   A CA  
170  C C   . ASN   A 27  ? 1.1346 1.2619 0.7568 0.5013  0.2399  0.0799  70  ASN   A C   
171  O O   . ASN   A 27  ? 1.1506 1.2132 0.7776 0.4620  0.2286  0.0980  70  ASN   A O   
172  C CB  . ASN   A 27  ? 1.1249 1.4427 0.7655 0.5187  0.3256  0.0962  70  ASN   A CB  
173  C CG  . ASN   A 27  ? 1.1407 1.4988 0.8631 0.4644  0.3424  0.1139  70  ASN   A CG  
174  O OD1 . ASN   A 27  ? 1.1614 1.4661 0.8995 0.4135  0.3430  0.1403  70  ASN   A OD1 
175  N ND2 . ASN   A 27  ? 1.1079 1.5695 0.8868 0.4772  0.3556  0.0948  70  ASN   A ND2 
176  N N   . SER   A 28  ? 1.1064 1.2379 0.7398 0.5402  0.2098  0.0436  71  SER   A N   
177  C CA  . SER   A 28  ? 1.1142 1.1694 0.7631 0.5340  0.1655  0.0301  71  SER   A CA  
178  C C   . SER   A 28  ? 1.0620 1.1665 0.7603 0.5473  0.1573  0.0174  71  SER   A C   
179  O O   . SER   A 28  ? 1.0677 1.1595 0.7558 0.5960  0.1291  -0.0139 71  SER   A O   
180  C CB  . SER   A 28  ? 1.1754 1.1539 0.7769 0.5726  0.1264  -0.0025 71  SER   A CB  
181  O OG  . SER   A 28  ? 1.2227 1.2023 0.7725 0.5947  0.1341  -0.0106 71  SER   A OG  
182  N N   . PRO   A 29  ? 1.0109 1.1741 0.7633 0.5086  0.1796  0.0378  72  PRO   A N   
183  C CA  . PRO   A 29  ? 0.9701 1.1978 0.7726 0.5264  0.1696  0.0210  72  PRO   A CA  
184  C C   . PRO   A 29  ? 0.9865 1.1403 0.7904 0.5259  0.1263  0.0172  72  PRO   A C   
185  O O   . PRO   A 29  ? 1.0158 1.0926 0.8066 0.4869  0.1162  0.0367  72  PRO   A O   
186  C CB  . PRO   A 29  ? 0.9344 1.2551 0.7970 0.4797  0.2103  0.0412  72  PRO   A CB  
187  C CG  . PRO   A 29  ? 0.9690 1.2178 0.8126 0.4241  0.2225  0.0748  72  PRO   A CG  
188  C CD  . PRO   A 29  ? 0.9931 1.1672 0.7650 0.4496  0.2124  0.0730  72  PRO   A CD  
189  N N   . ARG   A 30  ? 0.9676 1.1459 0.7834 0.5735  0.1010  -0.0075 73  ARG   A N   
190  C CA  . ARG   A 30  ? 0.9923 1.1031 0.8010 0.5822  0.0604  -0.0078 73  ARG   A CA  
191  C C   . ARG   A 30  ? 0.9155 1.1179 0.7848 0.5680  0.0641  -0.0065 73  ARG   A C   
192  O O   . ARG   A 30  ? 0.8569 1.1633 0.7657 0.6019  0.0693  -0.0291 73  ARG   A O   
193  C CB  . ARG   A 30  ? 1.0567 1.1195 0.8299 0.6516  0.0248  -0.0361 73  ARG   A CB  
194  C CG  . ARG   A 30  ? 1.1729 1.1599 0.8944 0.6661  0.0211  -0.0473 73  ARG   A CG  
195  C CD  . ARG   A 30  ? 1.2860 1.1862 0.9664 0.7248  -0.0197 -0.0750 73  ARG   A CD  
196  N NE  . ARG   A 30  ? 1.3897 1.2024 1.0268 0.7178  -0.0265 -0.0833 73  ARG   A NE  
197  C CZ  . ARG   A 30  ? 1.4739 1.1824 1.0726 0.7513  -0.0616 -0.1068 73  ARG   A CZ  
198  N NH1 . ARG   A 30  ? 1.4819 1.1486 1.0719 0.7988  -0.0930 -0.1199 73  ARG   A NH1 
199  N NH2 . ARG   A 30  ? 1.5025 1.1455 1.0717 0.7390  -0.0678 -0.1192 73  ARG   A NH2 
200  N N   . LEU   A 31  ? 0.9026 1.0776 0.7837 0.5169  0.0629  0.0157  74  LEU   A N   
201  C CA  . LEU   A 31  ? 0.8480 1.1104 0.7892 0.4955  0.0655  0.0132  74  LEU   A CA  
202  C C   . LEU   A 31  ? 0.8664 1.0768 0.7887 0.5045  0.0260  0.0170  74  LEU   A C   
203  O O   . LEU   A 31  ? 0.9202 1.0275 0.7974 0.4817  0.0159  0.0380  74  LEU   A O   
204  C CB  . LEU   A 31  ? 0.8329 1.1136 0.8049 0.4254  0.0999  0.0336  74  LEU   A CB  
205  C CG  . LEU   A 31  ? 0.8391 1.1533 0.8167 0.4076  0.1435  0.0422  74  LEU   A CG  
206  C CD1 . LEU   A 31  ? 0.8514 1.1299 0.8333 0.3437  0.1679  0.0691  74  LEU   A CD1 
207  C CD2 . LEU   A 31  ? 0.7787 1.2304 0.8161 0.4230  0.1691  0.0232  74  LEU   A CD2 
208  N N   . ASP   A 32  ? 0.8147 1.1044 0.7727 0.5359  0.0058  -0.0029 75  ASP   A N   
209  C CA  . ASP   A 32  ? 0.8371 1.0903 0.7729 0.5483  -0.0315 0.0021  75  ASP   A CA  
210  C C   . ASP   A 32  ? 0.7863 1.0748 0.7595 0.4860  -0.0190 0.0100  75  ASP   A C   
211  O O   . ASP   A 32  ? 0.7347 1.1388 0.7817 0.4649  -0.0024 -0.0086 75  ASP   A O   
212  C CB  . ASP   A 32  ? 0.8585 1.1967 0.8205 0.6115  -0.0609 -0.0269 75  ASP   A CB  
213  C CG  . ASP   A 32  ? 1.0197 1.2966 0.9303 0.6850  -0.0875 -0.0356 75  ASP   A CG  
214  O OD1 . ASP   A 32  ? 1.1087 1.2507 0.9516 0.6854  -0.0941 -0.0150 75  ASP   A OD1 
215  O OD2 . ASP   A 32  ? 1.0408 1.4056 0.9823 0.7430  -0.1031 -0.0662 75  ASP   A OD2 
216  N N   . VAL   A 33  ? 0.7926 0.9851 0.7192 0.4550  -0.0252 0.0347  76  VAL   A N   
217  C CA  . VAL   A 33  ? 0.7500 0.9653 0.7048 0.4001  -0.0156 0.0386  76  VAL   A CA  
218  C C   . VAL   A 33  ? 0.7737 0.9468 0.6855 0.4084  -0.0481 0.0467  76  VAL   A C   
219  O O   . VAL   A 33  ? 0.8225 0.9227 0.6707 0.4493  -0.0736 0.0603  76  VAL   A O   
220  C CB  . VAL   A 33  ? 0.7545 0.9153 0.7036 0.3449  0.0182  0.0581  76  VAL   A CB  
221  C CG1 . VAL   A 33  ? 0.7358 0.9281 0.7086 0.3424  0.0504  0.0561  76  VAL   A CG1 
222  C CG2 . VAL   A 33  ? 0.8141 0.8529 0.6912 0.3428  0.0088  0.0823  76  VAL   A CG2 
223  N N   . ALA   A 34  ? 0.7358 0.9559 0.6810 0.3711  -0.0469 0.0375  77  ALA   A N   
224  C CA  . ALA   A 34  ? 0.7575 0.9520 0.6622 0.3739  -0.0729 0.0426  77  ALA   A CA  
225  C C   . ALA   A 34  ? 0.7620 0.9226 0.6683 0.3145  -0.0512 0.0511  77  ALA   A C   
226  O O   . ALA   A 34  ? 0.7358 0.9260 0.6955 0.2739  -0.0235 0.0432  77  ALA   A O   
227  C CB  . ALA   A 34  ? 0.7125 1.0166 0.6599 0.3978  -0.1012 0.0098  77  ALA   A CB  
228  N N   . LEU   A 35  ? 0.7965 0.8891 0.6400 0.3113  -0.0612 0.0698  78  LEU   A N   
229  C CA  . LEU   A 35  ? 0.8025 0.8648 0.6442 0.2625  -0.0425 0.0747  78  LEU   A CA  
230  C C   . LEU   A 35  ? 0.7950 0.8908 0.6207 0.2658  -0.0654 0.0608  78  LEU   A C   
231  O O   . LEU   A 35  ? 0.8358 0.9026 0.5967 0.3010  -0.0876 0.0759  78  LEU   A O   
232  C CB  . LEU   A 35  ? 0.8540 0.8115 0.6367 0.2536  -0.0284 0.1073  78  LEU   A CB  
233  C CG  . LEU   A 35  ? 0.8818 0.8090 0.6541 0.2126  -0.0124 0.1120  78  LEU   A CG  
234  C CD1 . LEU   A 35  ? 0.8496 0.8048 0.6818 0.1755  0.0099  0.0961  78  LEU   A CD1 
235  C CD2 . LEU   A 35  ? 0.9371 0.7763 0.6554 0.2075  -0.0024 0.1410  78  LEU   A CD2 
236  N N   . ASP   A 36  ? 0.7395 0.8979 0.6227 0.2335  -0.0624 0.0303  79  ASP   A N   
237  C CA  . ASP   A 36  ? 0.7335 0.9355 0.6060 0.2392  -0.0878 0.0072  79  ASP   A CA  
238  C C   . ASP   A 36  ? 0.7652 0.9065 0.5818 0.2189  -0.0788 0.0205  79  ASP   A C   
239  O O   . ASP   A 36  ? 0.7865 0.8582 0.5838 0.1976  -0.0528 0.0455  79  ASP   A O   
240  C CB  . ASP   A 36  ? 0.6915 0.9951 0.6569 0.2164  -0.0947 -0.0401 79  ASP   A CB  
241  C CG  . ASP   A 36  ? 0.7227 1.0165 0.7415 0.1588  -0.0677 -0.0534 79  ASP   A CG  
242  O OD1 . ASP   A 36  ? 0.7686 0.9822 0.7511 0.1402  -0.0454 -0.0283 79  ASP   A OD1 
243  O OD2 . ASP   A 36  ? 0.6956 1.0609 0.7939 0.1326  -0.0700 -0.0901 79  ASP   A OD2 
244  N N   . GLU   A 37  ? 0.7581 0.9340 0.5490 0.2293  -0.1013 0.0008  80  GLU   A N   
245  C CA  . GLU   A 37  ? 0.7952 0.9311 0.5332 0.2153  -0.0925 0.0084  80  GLU   A CA  
246  C C   . GLU   A 37  ? 0.7844 0.9047 0.5709 0.1671  -0.0667 -0.0075 80  GLU   A C   
247  O O   . GLU   A 37  ? 0.8137 0.8846 0.5620 0.1541  -0.0489 0.0083  80  GLU   A O   
248  C CB  . GLU   A 37  ? 0.8191 1.0077 0.5179 0.2423  -0.1241 -0.0153 80  GLU   A CB  
249  C CG  . GLU   A 37  ? 0.9443 1.0902 0.5610 0.2428  -0.1139 0.0043  80  GLU   A CG  
250  C CD  . GLU   A 37  ? 1.0360 1.2378 0.6052 0.2722  -0.1440 -0.0211 80  GLU   A CD  
251  O OE1 . GLU   A 37  ? 1.0101 1.2587 0.6145 0.2541  -0.1509 -0.0677 80  GLU   A OE1 
252  O OE2 . GLU   A 37  ? 1.1138 1.3093 0.6070 0.3163  -0.1625 0.0045  80  GLU   A OE2 
253  N N   . SER   A 38  ? 0.7381 0.8982 0.6087 0.1411  -0.0633 -0.0366 81  SER   A N   
254  C CA  . SER   A 38  ? 0.7288 0.8615 0.6410 0.0991  -0.0406 -0.0487 81  SER   A CA  
255  C C   . SER   A 38  ? 0.7324 0.8034 0.6508 0.0838  -0.0094 -0.0150 81  SER   A C   
256  O O   . SER   A 38  ? 0.7329 0.7767 0.6840 0.0539  0.0090  -0.0206 81  SER   A O   
257  C CB  . SER   A 38  ? 0.7048 0.8967 0.7006 0.0726  -0.0493 -0.0937 81  SER   A CB  
258  O OG  . SER   A 38  ? 0.7362 0.9919 0.7291 0.0887  -0.0830 -0.1325 81  SER   A OG  
259  N N   . GLY   A 39  ? 0.7419 0.7871 0.6253 0.1071  -0.0059 0.0179  82  GLY   A N   
260  C CA  . GLY   A 39  ? 0.7582 0.7503 0.6417 0.0983  0.0189  0.0450  82  GLY   A CA  
261  C C   . GLY   A 39  ? 0.7287 0.7481 0.6706 0.0883  0.0314  0.0416  82  GLY   A C   
262  O O   . GLY   A 39  ? 0.7263 0.7068 0.6705 0.0787  0.0531  0.0593  82  GLY   A O   
263  N N   . ASP   A 40  ? 0.6976 0.7909 0.6860 0.0926  0.0183  0.0184  83  ASP   A N   
264  C CA  . ASP   A 40  ? 0.6767 0.8122 0.7259 0.0811  0.0346  0.0147  83  ASP   A CA  
265  C C   . ASP   A 40  ? 0.6829 0.8441 0.7210 0.1206  0.0283  0.0258  83  ASP   A C   
266  O O   . ASP   A 40  ? 0.6712 0.8703 0.6955 0.1544  0.0003  0.0154  83  ASP   A O   
267  C CB  . ASP   A 40  ? 0.6517 0.8656 0.7766 0.0553  0.0275  -0.0234 83  ASP   A CB  
268  C CG  . ASP   A 40  ? 0.7343 0.9172 0.8782 0.0156  0.0334  -0.0399 83  ASP   A CG  
269  O OD1 . ASP   A 40  ? 0.7668 0.8829 0.9000 -0.0044 0.0584  -0.0192 83  ASP   A OD1 
270  O OD2 . ASP   A 40  ? 0.7595 0.9842 0.9265 0.0088  0.0103  -0.0762 83  ASP   A OD2 
271  N N   . PHE   A 41  ? 0.6915 0.8323 0.7319 0.1213  0.0523  0.0449  84  PHE   A N   
272  C CA  . PHE   A 41  ? 0.6913 0.8602 0.7270 0.1604  0.0479  0.0491  84  PHE   A CA  
273  C C   . PHE   A 41  ? 0.6641 0.9402 0.7787 0.1542  0.0537  0.0241  84  PHE   A C   
274  O O   . PHE   A 41  ? 0.6348 0.9416 0.8063 0.1100  0.0758  0.0153  84  PHE   A O   
275  C CB  . PHE   A 41  ? 0.7000 0.8133 0.7058 0.1669  0.0704  0.0734  84  PHE   A CB  
276  C CG  . PHE   A 41  ? 0.7394 0.7596 0.6752 0.1796  0.0620  0.0939  84  PHE   A CG  
277  C CD1 . PHE   A 41  ? 0.7645 0.7559 0.6553 0.2183  0.0382  0.0996  84  PHE   A CD1 
278  C CD2 . PHE   A 41  ? 0.7608 0.7219 0.6783 0.1527  0.0778  0.1070  84  PHE   A CD2 
279  C CE1 . PHE   A 41  ? 0.8150 0.7202 0.6491 0.2212  0.0341  0.1187  84  PHE   A CE1 
280  C CE2 . PHE   A 41  ? 0.7990 0.6881 0.6642 0.1601  0.0714  0.1216  84  PHE   A CE2 
281  C CZ  . PHE   A 41  ? 0.8190 0.6807 0.6457 0.1900  0.0516  0.1277  84  PHE   A CZ  
282  N N   . SER   A 42  ? 0.6676 1.0002 0.7880 0.1982  0.0343  0.0121  85  SER   A N   
283  C CA  . SER   A 42  ? 0.6378 1.0885 0.8383 0.1988  0.0402  -0.0147 85  SER   A CA  
284  C C   . SER   A 42  ? 0.6748 1.1487 0.8594 0.2534  0.0366  -0.0126 85  SER   A C   
285  O O   . SER   A 42  ? 0.7196 1.1166 0.8311 0.2939  0.0181  0.0041  85  SER   A O   
286  C CB  . SER   A 42  ? 0.6158 1.1492 0.8604 0.2011  0.0080  -0.0509 85  SER   A CB  
287  O OG  . SER   A 42  ? 0.6757 1.1819 0.8558 0.2532  -0.0330 -0.0501 85  SER   A OG  
288  N N   . LEU   A 43  ? 0.6546 1.2322 0.9082 0.2536  0.0561  -0.0303 86  LEU   A N   
289  C CA  . LEU   A 43  ? 0.6871 1.2998 0.9307 0.3110  0.0527  -0.0357 86  LEU   A CA  
290  C C   . LEU   A 43  ? 0.7040 1.3893 0.9632 0.3647  0.0092  -0.0659 86  LEU   A C   
291  O O   . LEU   A 43  ? 0.6461 1.4315 0.9755 0.3484  -0.0015 -0.0959 86  LEU   A O   
292  C CB  . LEU   A 43  ? 0.6382 1.3439 0.9480 0.2917  0.0968  -0.0421 86  LEU   A CB  
293  C CG  . LEU   A 43  ? 0.6960 1.3363 0.9659 0.2762  0.1369  -0.0108 86  LEU   A CG  
294  C CD1 . LEU   A 43  ? 0.6450 1.3968 0.9759 0.2689  0.1794  -0.0185 86  LEU   A CD1 
295  C CD2 . LEU   A 43  ? 0.7681 1.3130 0.9489 0.3311  0.1171  0.0019  86  LEU   A CD2 
296  N N   . VAL   A 44  ? 0.7791 1.4149 0.9749 0.4310  -0.0174 -0.0607 87  VAL   A N   
297  C CA  . VAL   A 44  ? 0.7987 1.4941 0.9972 0.4980  -0.0610 -0.0866 87  VAL   A CA  
298  C C   . VAL   A 44  ? 0.8086 1.5787 1.0407 0.5378  -0.0459 -0.1045 87  VAL   A C   
299  O O   . VAL   A 44  ? 0.8620 1.5520 1.0403 0.5575  -0.0336 -0.0864 87  VAL   A O   
300  C CB  . VAL   A 44  ? 0.8838 1.4516 0.9777 0.5472  -0.1006 -0.0637 87  VAL   A CB  
301  C CG1 . VAL   A 44  ? 0.8718 1.4949 0.9609 0.6261  -0.1472 -0.0880 87  VAL   A CG1 
302  C CG2 . VAL   A 44  ? 0.9277 1.4174 0.9787 0.5057  -0.1074 -0.0416 87  VAL   A CG2 
303  N N   . GLU   A 45  ? 0.7530 1.6825 1.0780 0.5467  -0.0443 -0.1430 88  GLU   A N   
304  C CA  . GLU   A 45  ? 0.7437 1.7616 1.1066 0.5829  -0.0232 -0.1625 88  GLU   A CA  
305  C C   . GLU   A 45  ? 0.7302 1.8257 1.1040 0.6712  -0.0663 -0.1985 88  GLU   A C   
306  O O   . GLU   A 45  ? 0.7567 1.8368 1.0986 0.7292  -0.0672 -0.2036 88  GLU   A O   
307  C CB  . GLU   A 45  ? 0.7144 1.8605 1.1799 0.5190  0.0302  -0.1744 88  GLU   A CB  
308  C CG  . GLU   A 45  ? 0.8161 1.8724 1.2501 0.4563  0.0797  -0.1340 88  GLU   A CG  
309  C CD  . GLU   A 45  ? 0.8865 2.0088 1.3455 0.4548  0.1308  -0.1323 88  GLU   A CD  
310  O OE1 . GLU   A 45  ? 0.8524 2.0834 1.3461 0.5098  0.1277  -0.1635 88  GLU   A OE1 
311  O OE2 . GLU   A 45  ? 0.9465 2.0140 1.3865 0.4025  0.1738  -0.0998 88  GLU   A OE2 
312  N N   . GLY   B 7   ? 1.0118 0.9776 0.8585 0.2555  0.0258  -0.1133 16  GLY   B N   
313  C CA  . GLY   B 7   ? 1.0320 0.9692 0.8679 0.2579  0.0247  -0.1024 16  GLY   B CA  
314  C C   . GLY   B 7   ? 1.0314 0.9704 0.8691 0.2613  0.0208  -0.0990 16  GLY   B C   
315  O O   . GLY   B 7   ? 1.0284 0.9895 0.8784 0.2603  0.0176  -0.1056 16  GLY   B O   
316  N N   . GLU   B 8   ? 1.0274 0.9439 0.8535 0.2663  0.0204  -0.0886 17  GLU   B N   
317  C CA  . GLU   B 8   ? 1.0176 0.9338 0.8420 0.2727  0.0152  -0.0861 17  GLU   B CA  
318  C C   . GLU   B 8   ? 0.9919 0.9181 0.8238 0.2567  0.0156  -0.0811 17  GLU   B C   
319  O O   . GLU   B 8   ? 0.9959 0.9147 0.8237 0.2462  0.0209  -0.0717 17  GLU   B O   
320  C CB  . GLU   B 8   ? 1.0562 0.9481 0.8636 0.2860  0.0155  -0.0757 17  GLU   B CB  
321  C CG  . GLU   B 8   ? 1.1011 0.9929 0.9035 0.2972  0.0087  -0.0751 17  GLU   B CG  
322  C CD  . GLU   B 8   ? 1.1724 1.0443 0.9563 0.3140  0.0098  -0.0644 17  GLU   B CD  
323  O OE1 . GLU   B 8   ? 1.1709 1.0289 0.9482 0.3111  0.0175  -0.0525 17  GLU   B OE1 
324  O OE2 . GLU   B 8   ? 1.2050 1.0761 0.9814 0.3307  0.0026  -0.0676 17  GLU   B OE2 
325  N N   A THR   B 9   ? 0.9733 0.9160 0.8172 0.2546  0.0092  -0.0874 18  THR   B N   
326  N N   B THR   B 9   ? 0.9725 0.9152 0.8164 0.2544  0.0092  -0.0873 18  THR   B N   
327  C CA  A THR   B 9   ? 0.9648 0.9155 0.8169 0.2392  0.0078  -0.0829 18  THR   B CA  
328  C CA  B THR   B 9   ? 0.9633 0.9131 0.8148 0.2393  0.0079  -0.0824 18  THR   B CA  
329  C C   A THR   B 9   ? 0.9547 0.8981 0.8042 0.2463  -0.0027 -0.0823 18  THR   B C   
330  C C   B THR   B 9   ? 0.9540 0.8974 0.8035 0.2463  -0.0027 -0.0823 18  THR   B C   
331  O O   A THR   B 9   ? 0.9574 0.9057 0.8149 0.2348  -0.0069 -0.0801 18  THR   B O   
332  O O   B THR   B 9   ? 0.9561 0.9046 0.8138 0.2347  -0.0069 -0.0802 18  THR   B O   
333  C CB  A THR   B 9   ? 0.9705 0.9485 0.8429 0.2252  0.0092  -0.0884 18  THR   B CB  
334  C CB  B THR   B 9   ? 0.9674 0.9435 0.8383 0.2248  0.0098  -0.0873 18  THR   B CB  
335  O OG1 A THR   B 9   ? 0.9801 0.9709 0.8566 0.2302  0.0133  -0.0966 18  THR   B OG1 
336  O OG1 B THR   B 9   ? 0.9705 0.9632 0.8537 0.2330  0.0046  -0.0985 18  THR   B OG1 
337  C CG2 A THR   B 9   ? 0.9730 0.9555 0.8480 0.2065  0.0151  -0.0799 18  THR   B CG2 
338  C CG2 B THR   B 9   ? 0.9710 0.9524 0.8402 0.2161  0.0200  -0.0855 18  THR   B CG2 
339  N N   . THR   B 10  ? 0.9437 0.8746 0.7812 0.2662  -0.0078 -0.0844 19  THR   B N   
340  C CA  . THR   B 10  ? 0.9187 0.8424 0.7510 0.2772  -0.0195 -0.0859 19  THR   B CA  
341  C C   . THR   B 10  ? 0.8886 0.8004 0.7097 0.2721  -0.0186 -0.0748 19  THR   B C   
342  O O   . THR   B 10  ? 0.8783 0.7817 0.6885 0.2698  -0.0084 -0.0646 19  THR   B O   
343  C CB  . THR   B 10  ? 0.9430 0.8551 0.7596 0.3027  -0.0231 -0.0887 19  THR   B CB  
344  O OG1 . THR   B 10  ? 0.9537 0.8751 0.7777 0.3083  -0.0227 -0.0984 19  THR   B OG1 
345  C CG2 . THR   B 10  ? 0.9504 0.8574 0.7613 0.3183  -0.0377 -0.0941 19  THR   B CG2 
346  N N   . ASP   B 11  ? 0.8724 0.7834 0.6972 0.2707  -0.0302 -0.0774 20  ASP   B N   
347  C CA  . ASP   B 11  ? 0.8829 0.7821 0.6952 0.2698  -0.0324 -0.0690 20  ASP   B CA  
348  C C   . ASP   B 11  ? 0.8913 0.7773 0.6797 0.2905  -0.0290 -0.0617 20  ASP   B C   
349  O O   . ASP   B 11  ? 0.9051 0.7883 0.6863 0.3093  -0.0317 -0.0660 20  ASP   B O   
350  C CB  . ASP   B 11  ? 0.9067 0.8031 0.7248 0.2716  -0.0501 -0.0761 20  ASP   B CB  
351  C CG  . ASP   B 11  ? 0.9543 0.8599 0.7936 0.2479  -0.0535 -0.0768 20  ASP   B CG  
352  O OD1 . ASP   B 11  ? 0.9290 0.8477 0.7798 0.2313  -0.0417 -0.0735 20  ASP   B OD1 
353  O OD2 . ASP   B 11  ? 1.0022 0.9011 0.8461 0.2469  -0.0687 -0.0804 20  ASP   B OD2 
354  N N   . GLY   B 12  ? 0.8727 0.7525 0.6494 0.2877  -0.0226 -0.0502 21  GLY   B N   
355  C CA  . GLY   B 12  ? 0.8682 0.7398 0.6245 0.3060  -0.0175 -0.0402 21  GLY   B CA  
356  C C   . GLY   B 12  ? 0.8538 0.7251 0.6063 0.2956  -0.0038 -0.0260 21  GLY   B C   
357  O O   . GLY   B 12  ? 0.8416 0.7173 0.6049 0.2749  0.0006  -0.0249 21  GLY   B O   
358  N N   . VAL   B 13  ? 0.8423 0.7094 0.5795 0.3107  0.0026  -0.0144 22  VAL   B N   
359  C CA  . VAL   B 13  ? 0.8350 0.7034 0.5708 0.3021  0.0150  0.0005  22  VAL   B CA  
360  C C   . VAL   B 13  ? 0.8305 0.6959 0.5730 0.2974  0.0256  0.0061  22  VAL   B C   
361  O O   . VAL   B 13  ? 0.8402 0.7008 0.5783 0.3111  0.0248  0.0041  22  VAL   B O   
362  C CB  . VAL   B 13  ? 0.8459 0.7154 0.5638 0.3189  0.0158  0.0119  22  VAL   B CB  
363  C CG1 . VAL   B 13  ? 0.8531 0.7199 0.5553 0.3457  0.0162  0.0169  22  VAL   B CG1 
364  C CG2 . VAL   B 13  ? 0.8417 0.7164 0.5627 0.3068  0.0275  0.0266  22  VAL   B CG2 
365  N N   . TYR   B 14  ? 0.8162 0.6831 0.5695 0.2784  0.0336  0.0114  23  TYR   B N   
366  C CA  . TYR   B 14  ? 0.8212 0.6825 0.5827 0.2716  0.0410  0.0148  23  TYR   B CA  
367  C C   . TYR   B 14  ? 0.8291 0.6895 0.5939 0.2634  0.0502  0.0308  23  TYR   B C   
368  O O   . TYR   B 14  ? 0.8385 0.7060 0.6042 0.2553  0.0516  0.0354  23  TYR   B O   
369  C CB  . TYR   B 14  ? 0.8112 0.6754 0.5868 0.2552  0.0391  0.0015  23  TYR   B CB  
370  C CG  . TYR   B 14  ? 0.8194 0.6866 0.5972 0.2620  0.0316  -0.0132 23  TYR   B CG  
371  C CD1 . TYR   B 14  ? 0.8279 0.7016 0.6046 0.2657  0.0229  -0.0207 23  TYR   B CD1 
372  C CD2 . TYR   B 14  ? 0.8429 0.7070 0.6255 0.2643  0.0321  -0.0202 23  TYR   B CD2 
373  C CE1 . TYR   B 14  ? 0.8384 0.7172 0.6210 0.2709  0.0152  -0.0339 23  TYR   B CE1 
374  C CE2 . TYR   B 14  ? 0.8564 0.7268 0.6425 0.2713  0.0252  -0.0338 23  TYR   B CE2 
375  C CZ  . TYR   B 14  ? 0.8625 0.7412 0.6498 0.2742  0.0169  -0.0403 23  TYR   B CZ  
376  O OH  . TYR   B 14  ? 0.8849 0.7722 0.6796 0.2797  0.0092  -0.0536 23  TYR   B OH  
377  N N   . ARG   B 15  ? 0.8230 0.6743 0.5911 0.2646  0.0557  0.0389  24  ARG   B N   
378  C CA  . ARG   B 15  ? 0.8129 0.6627 0.5896 0.2542  0.0634  0.0540  24  ARG   B CA  
379  C C   . ARG   B 15  ? 0.8098 0.6564 0.6014 0.2344  0.0621  0.0449  24  ARG   B C   
380  O O   . ARG   B 15  ? 0.8041 0.6452 0.5982 0.2335  0.0578  0.0316  24  ARG   B O   
381  C CB  . ARG   B 15  ? 0.8192 0.6578 0.5940 0.2641  0.0688  0.0682  24  ARG   B CB  
382  C CG  . ARG   B 15  ? 0.8467 0.6889 0.6041 0.2874  0.0709  0.0783  24  ARG   B CG  
383  C CD  . ARG   B 15  ? 0.8853 0.7190 0.6424 0.2942  0.0789  0.0982  24  ARG   B CD  
384  N NE  . ARG   B 15  ? 0.9260 0.7616 0.6632 0.3203  0.0799  0.1045  24  ARG   B NE  
385  C CZ  . ARG   B 15  ? 0.9570 0.8051 0.6840 0.3337  0.0865  0.1216  24  ARG   B CZ  
386  N NH1 . ARG   B 15  ? 0.9289 0.7896 0.6661 0.3221  0.0935  0.1357  24  ARG   B NH1 
387  N NH2 . ARG   B 15  ? 0.9716 0.8213 0.6778 0.3603  0.0860  0.1248  24  ARG   B NH2 
388  N N   . VAL   B 16  ? 0.8053 0.6564 0.6066 0.2203  0.0652  0.0518  25  VAL   B N   
389  C CA  . VAL   B 16  ? 0.8145 0.6622 0.6289 0.2034  0.0631  0.0435  25  VAL   B CA  
390  C C   . VAL   B 16  ? 0.8268 0.6635 0.6531 0.1976  0.0662  0.0566  25  VAL   B C   
391  O O   . VAL   B 16  ? 0.8264 0.6689 0.6579 0.1948  0.0713  0.0726  25  VAL   B O   
392  C CB  . VAL   B 16  ? 0.8146 0.6750 0.6313 0.1914  0.0620  0.0386  25  VAL   B CB  
393  C CG1 . VAL   B 16  ? 0.8150 0.6723 0.6427 0.1772  0.0591  0.0285  25  VAL   B CG1 
394  C CG2 . VAL   B 16  ? 0.8125 0.6814 0.6185 0.1967  0.0583  0.0288  25  VAL   B CG2 
395  N N   . MET   B 17  ? 0.8419 0.6629 0.6729 0.1967  0.0626  0.0503  26  MET   B N   
396  C CA  . MET   B 17  ? 0.8603 0.6651 0.7028 0.1925  0.0633  0.0624  26  MET   B CA  
397  C C   . MET   B 17  ? 0.8885 0.6825 0.7452 0.1784  0.0562  0.0525  26  MET   B C   
398  O O   . MET   B 17  ? 0.8883 0.6848 0.7419 0.1767  0.0508  0.0337  26  MET   B O   
399  C CB  . MET   B 17  ? 0.8583 0.6474 0.6918 0.2074  0.0626  0.0637  26  MET   B CB  
400  C CG  . MET   B 17  ? 0.8797 0.6773 0.6964 0.2255  0.0671  0.0696  26  MET   B CG  
401  S SD  . MET   B 17  ? 0.9181 0.7226 0.7348 0.2307  0.0776  0.0990  26  MET   B SD  
402  C CE  . MET   B 17  ? 0.8902 0.6693 0.7188 0.2268  0.0783  0.1136  26  MET   B CE  
403  N N   . THR   B 18  ? 0.9132 0.6941 0.7853 0.1699  0.0555  0.0652  27  THR   B N   
404  C CA  . THR   B 18  ? 0.9499 0.7156 0.8356 0.1585  0.0459  0.0554  27  THR   B CA  
405  C C   . THR   B 18  ? 0.9854 0.7251 0.8826 0.1567  0.0425  0.0677  27  THR   B C   
406  O O   . THR   B 18  ? 0.9774 0.7163 0.8790 0.1580  0.0500  0.0902  27  THR   B O   
407  C CB  . THR   B 18  ? 0.9618 0.7402 0.8608 0.1434  0.0442  0.0540  27  THR   B CB  
408  O OG1 . THR   B 18  ? 0.9876 0.7501 0.8969 0.1356  0.0325  0.0404  27  THR   B OG1 
409  C CG2 . THR   B 18  ? 0.9520 0.7384 0.8660 0.1353  0.0508  0.0776  27  THR   B CG2 
410  N N   . ARG   B 19  ? 1.0210 0.7394 0.9228 0.1544  0.0308  0.0535  28  ARG   B N   
411  C CA  . ARG   B 19  ? 1.0635 0.7526 0.9779 0.1508  0.0244  0.0638  28  ARG   B CA  
412  C C   . ARG   B 19  ? 1.0856 0.7642 1.0239 0.1330  0.0133  0.0612  28  ARG   B C   
413  O O   . ARG   B 19  ? 1.0951 0.7450 1.0456 0.1286  0.0033  0.0644  28  ARG   B O   
414  C CB  . ARG   B 19  ? 1.1089 0.7752 1.0088 0.1654  0.0172  0.0512  28  ARG   B CB  
415  C CG  . ARG   B 19  ? 1.1775 0.8503 1.0577 0.1829  0.0268  0.0573  28  ARG   B CG  
416  C CD  . ARG   B 19  ? 1.2561 0.9043 1.1244 0.1973  0.0193  0.0481  28  ARG   B CD  
417  N NE  . ARG   B 19  ? 1.3193 0.9766 1.1675 0.2158  0.0265  0.0486  28  ARG   B NE  
418  C CZ  . ARG   B 19  ? 1.3633 1.0332 1.1974 0.2276  0.0244  0.0277  28  ARG   B CZ  
419  N NH1 . ARG   B 19  ? 1.3597 1.0364 1.1957 0.2234  0.0171  0.0061  28  ARG   B NH1 
420  N NH2 . ARG   B 19  ? 1.3657 1.0431 1.1841 0.2440  0.0294  0.0286  28  ARG   B NH2 
421  N N   . ARG   B 20  ? 1.0929 0.7936 1.0380 0.1232  0.0141  0.0556  29  ARG   B N   
422  C CA  . ARG   B 20  ? 1.1095 0.8047 1.0767 0.1074  0.0029  0.0509  29  ARG   B CA  
423  C C   . ARG   B 20  ? 1.1071 0.8042 1.1019 0.0919  0.0063  0.0769  29  ARG   B C   
424  O O   . ARG   B 20  ? 1.1073 0.8021 1.1242 0.0776  -0.0032 0.0747  29  ARG   B O   
425  C CB  . ARG   B 20  ? 1.1300 0.8477 1.0906 0.1056  0.0012  0.0321  29  ARG   B CB  
426  C CG  . ARG   B 20  ? 1.1871 0.9350 1.1492 0.1005  0.0134  0.0445  29  ARG   B CG  
427  C CD  . ARG   B 20  ? 1.2416 1.0018 1.2141 0.0899  0.0069  0.0345  29  ARG   B CD  
428  N NE  . ARG   B 20  ? 1.2829 1.0695 1.2603 0.0844  0.0173  0.0491  29  ARG   B NE  
429  C CZ  . ARG   B 20  ? 1.3129 1.1066 1.3147 0.0709  0.0152  0.0601  29  ARG   B CZ  
430  N NH1 . ARG   B 20  ? 1.3093 1.0839 1.3348 0.0600  0.0021  0.0585  29  ARG   B NH1 
431  N NH2 . ARG   B 20  ? 1.3048 1.1248 1.3081 0.0688  0.0249  0.0723  29  ARG   B NH2 
432  N N   . LEU   B 21  ? 1.0989 0.8028 1.0929 0.0955  0.0199  0.1015  30  LEU   B N   
433  C CA  . LEU   B 21  ? 1.0829 0.7924 1.1030 0.0825  0.0256  0.1299  30  LEU   B CA  
434  C C   . LEU   B 21  ? 1.0803 0.7654 1.1018 0.0872  0.0283  0.1494  30  LEU   B C   
435  O O   . LEU   B 21  ? 1.1010 0.7583 1.1105 0.0957  0.0192  0.1361  30  LEU   B O   
436  C CB  . LEU   B 21  ? 1.0780 0.8252 1.0937 0.0847  0.0415  0.1436  30  LEU   B CB  
437  C CG  . LEU   B 21  ? 1.0977 0.8685 1.1118 0.0801  0.0397  0.1280  30  LEU   B CG  
438  C CD1 . LEU   B 21  ? 1.0941 0.8983 1.1027 0.0845  0.0544  0.1434  30  LEU   B CD1 
439  C CD2 . LEU   B 21  ? 1.1025 0.8688 1.1459 0.0616  0.0273  0.1239  30  LEU   B CD2 
440  N N   . LEU   B 22  ? 1.0578 0.7532 1.0933 0.0829  0.0403  0.1809  31  LEU   B N   
441  C CA  . LEU   B 22  ? 1.0575 0.7311 1.0929 0.0883  0.0442  0.2023  31  LEU   B CA  
442  C C   . LEU   B 22  ? 1.0530 0.7319 1.0523 0.1126  0.0544  0.1992  31  LEU   B C   
443  O O   . LEU   B 22  ? 1.0537 0.7635 1.0387 0.1219  0.0663  0.2014  31  LEU   B O   
444  C CB  . LEU   B 22  ? 1.0447 0.7336 1.1062 0.0769  0.0558  0.2388  31  LEU   B CB  
445  C CG  . LEU   B 22  ? 1.0669 0.7314 1.1332 0.0791  0.0592  0.2645  31  LEU   B CG  
446  C CD1 . LEU   B 22  ? 1.0693 0.6976 1.1670 0.0591  0.0419  0.2670  31  LEU   B CD1 
447  C CD2 . LEU   B 22  ? 1.0663 0.7604 1.1401 0.0807  0.0792  0.3009  31  LEU   B CD2 
448  N N   . GLY   B 23  ? 1.0437 0.6922 1.0286 0.1236  0.0480  0.1923  32  GLY   B N   
449  C CA  . GLY   B 23  ? 1.0393 0.6900 0.9915 0.1473  0.0549  0.1868  32  GLY   B CA  
450  C C   . GLY   B 23  ? 1.0196 0.6927 0.9516 0.1564  0.0550  0.1606  32  GLY   B C   
451  O O   . GLY   B 23  ? 1.0186 0.6924 0.9557 0.1478  0.0452  0.1385  32  GLY   B O   
452  N N   . SER   B 24  ? 1.0023 0.6943 0.9117 0.1740  0.0658  0.1635  33  SER   B N   
453  C CA  . SER   B 24  ? 0.9864 0.7000 0.8786 0.1818  0.0661  0.1417  33  SER   B CA  
454  C C   . SER   B 24  ? 0.9517 0.6967 0.8463 0.1796  0.0769  0.1552  33  SER   B C   
455  O O   . SER   B 24  ? 0.9519 0.7064 0.8427 0.1883  0.0876  0.1779  33  SER   B O   
456  C CB  . SER   B 24  ? 1.0163 0.7268 0.8818 0.2042  0.0671  0.1324  33  SER   B CB  
457  O OG  . SER   B 24  ? 1.0659 0.7478 0.9279 0.2086  0.0573  0.1209  33  SER   B OG  
458  N N   . THR   B 25  ? 0.9207 0.6825 0.8204 0.1697  0.0741  0.1418  34  THR   B N   
459  C CA  . THR   B 25  ? 0.8969 0.6881 0.7985 0.1679  0.0828  0.1528  34  THR   B CA  
460  C C   . THR   B 25  ? 0.8791 0.6873 0.7603 0.1774  0.0824  0.1344  34  THR   B C   
461  O O   . THR   B 25  ? 0.8675 0.6701 0.7445 0.1744  0.0743  0.1117  34  THR   B O   
462  C CB  . THR   B 25  ? 0.9098 0.7071 0.8390 0.1463  0.0800  0.1579  34  THR   B CB  
463  O OG1 . THR   B 25  ? 0.9351 0.7120 0.8860 0.1358  0.0773  0.1730  34  THR   B OG1 
464  C CG2 . THR   B 25  ? 0.9006 0.7290 0.8340 0.1453  0.0897  0.1733  34  THR   B CG2 
465  N N   . GLN   B 26  ? 0.8639 0.6928 0.7326 0.1894  0.0906  0.1446  35  GLN   B N   
466  C CA  . GLN   B 26  ? 0.8630 0.7053 0.7137 0.1978  0.0885  0.1286  35  GLN   B CA  
467  C C   . GLN   B 26  ? 0.8610 0.7213 0.7201 0.1858  0.0884  0.1268  35  GLN   B C   
468  O O   . GLN   B 26  ? 0.8648 0.7418 0.7295 0.1858  0.0953  0.1441  35  GLN   B O   
469  C CB  . GLN   B 26  ? 0.8665 0.7184 0.6963 0.2202  0.0941  0.1369  35  GLN   B CB  
470  C CG  . GLN   B 26  ? 0.8791 0.7422 0.6918 0.2287  0.0896  0.1205  35  GLN   B CG  
471  C CD  . GLN   B 26  ? 0.8890 0.7594 0.6808 0.2527  0.0925  0.1272  35  GLN   B CD  
472  O OE1 . GLN   B 26  ? 0.8872 0.7479 0.6710 0.2661  0.0942  0.1326  35  GLN   B OE1 
473  N NE2 . GLN   B 26  ? 0.8748 0.7615 0.6559 0.2603  0.0918  0.1260  35  GLN   B NE2 
474  N N   . VAL   B 27  ? 0.8513 0.7097 0.7110 0.1765  0.0811  0.1068  36  VAL   B N   
475  C CA  . VAL   B 27  ? 0.8334 0.7069 0.6990 0.1657  0.0799  0.1032  36  VAL   B CA  
476  C C   . VAL   B 27  ? 0.8182 0.7062 0.6647 0.1758  0.0802  0.0974  36  VAL   B C   
477  O O   . VAL   B 27  ? 0.8160 0.7188 0.6638 0.1716  0.0808  0.0995  36  VAL   B O   
478  C CB  . VAL   B 27  ? 0.8463 0.7103 0.7224 0.1509  0.0716  0.0862  36  VAL   B CB  
479  C CG1 . VAL   B 27  ? 0.8536 0.7031 0.7511 0.1400  0.0690  0.0931  36  VAL   B CG1 
480  C CG2 . VAL   B 27  ? 0.8538 0.7085 0.7167 0.1565  0.0664  0.0666  36  VAL   B CG2 
481  N N   . GLY   B 28  ? 0.8035 0.6865 0.6332 0.1895  0.0785  0.0899  37  GLY   B N   
482  C CA  . GLY   B 28  ? 0.7856 0.6779 0.5981 0.1994  0.0760  0.0835  37  GLY   B CA  
483  C C   . GLY   B 28  ? 0.7752 0.6598 0.5735 0.2141  0.0724  0.0750  37  GLY   B C   
484  O O   . GLY   B 28  ? 0.7740 0.6481 0.5728 0.2203  0.0737  0.0772  37  GLY   B O   
485  N N   . VAL   B 29  ? 0.7586 0.6477 0.5445 0.2199  0.0668  0.0652  38  VAL   B N   
486  C CA  . VAL   B 29  ? 0.7477 0.6327 0.5207 0.2340  0.0608  0.0559  38  VAL   B CA  
487  C C   . VAL   B 29  ? 0.7434 0.6292 0.5163 0.2250  0.0532  0.0403  38  VAL   B C   
488  O O   . VAL   B 29  ? 0.7503 0.6413 0.5271 0.2126  0.0532  0.0393  38  VAL   B O   
489  C CB  . VAL   B 29  ? 0.7542 0.6461 0.5110 0.2542  0.0608  0.0653  38  VAL   B CB  
490  C CG1 . VAL   B 29  ? 0.7698 0.6566 0.5132 0.2705  0.0519  0.0543  38  VAL   B CG1 
491  C CG2 . VAL   B 29  ? 0.7433 0.6386 0.5003 0.2635  0.0703  0.0843  38  VAL   B CG2 
492  N N   . GLY   B 30  ? 0.7303 0.6122 0.4996 0.2315  0.0468  0.0291  39  GLY   B N   
493  C CA  . GLY   B 30  ? 0.7225 0.6065 0.4939 0.2230  0.0398  0.0168  39  GLY   B CA  
494  C C   . GLY   B 30  ? 0.7264 0.6079 0.4925 0.2348  0.0307  0.0077  39  GLY   B C   
495  O O   . GLY   B 30  ? 0.7344 0.6121 0.4941 0.2510  0.0297  0.0089  39  GLY   B O   
496  N N   . VAL   B 31  ? 0.7243 0.6079 0.4936 0.2270  0.0234  -0.0008 40  VAL   B N   
497  C CA  . VAL   B 31  ? 0.7359 0.6176 0.5044 0.2350  0.0122  -0.0101 40  VAL   B CA  
498  C C   . VAL   B 31  ? 0.7323 0.6205 0.5168 0.2220  0.0107  -0.0200 40  VAL   B C   
499  O O   . VAL   B 31  ? 0.7238 0.6175 0.5158 0.2055  0.0127  -0.0204 40  VAL   B O   
500  C CB  . VAL   B 31  ? 0.7656 0.6435 0.5256 0.2370  0.0024  -0.0102 40  VAL   B CB  
501  C CG1 . VAL   B 31  ? 0.7841 0.6584 0.5477 0.2420  -0.0119 -0.0210 40  VAL   B CG1 
502  C CG2 . VAL   B 31  ? 0.7843 0.6594 0.5267 0.2536  0.0030  -0.0011 40  VAL   B CG2 
503  N N   . MET   B 32  ? 0.7281 0.6175 0.5172 0.2308  0.0067  -0.0278 41  MET   B N   
504  C CA  . MET   B 32  ? 0.7258 0.6257 0.5313 0.2210  0.0047  -0.0373 41  MET   B CA  
505  C C   . MET   B 32  ? 0.7338 0.6334 0.5439 0.2227  -0.0092 -0.0434 41  MET   B C   
506  O O   . MET   B 32  ? 0.7357 0.6277 0.5375 0.2398  -0.0182 -0.0466 41  MET   B O   
507  C CB  . MET   B 32  ? 0.7297 0.6315 0.5379 0.2313  0.0069  -0.0430 41  MET   B CB  
508  C CG  . MET   B 32  ? 0.7508 0.6677 0.5761 0.2223  0.0073  -0.0524 41  MET   B CG  
509  S SD  . MET   B 32  ? 0.7951 0.7225 0.6277 0.2035  0.0188  -0.0501 41  MET   B SD  
510  C CE  . MET   B 32  ? 0.7774 0.6925 0.6005 0.2127  0.0260  -0.0475 41  MET   B CE  
511  N N   . GLN   B 33  ? 0.7326 0.6396 0.5552 0.2059  -0.0116 -0.0443 42  GLN   B N   
512  C CA  . GLN   B 33  ? 0.7498 0.6551 0.5809 0.2040  -0.0261 -0.0492 42  GLN   B CA  
513  C C   . GLN   B 33  ? 0.7628 0.6847 0.6160 0.1845  -0.0241 -0.0505 42  GLN   B C   
514  O O   . GLN   B 33  ? 0.7768 0.7055 0.6312 0.1707  -0.0138 -0.0442 42  GLN   B O   
515  C CB  . GLN   B 33  ? 0.7808 0.6712 0.5988 0.2051  -0.0339 -0.0441 42  GLN   B CB  
516  C CG  . GLN   B 33  ? 0.8359 0.7197 0.6625 0.2059  -0.0526 -0.0507 42  GLN   B CG  
517  C CD  . GLN   B 33  ? 0.9045 0.7695 0.7142 0.2147  -0.0648 -0.0490 42  GLN   B CD  
518  O OE1 . GLN   B 33  ? 0.9416 0.7991 0.7580 0.2045  -0.0761 -0.0490 42  GLN   B OE1 
519  N NE2 . GLN   B 33  ? 0.8955 0.7531 0.6831 0.2342  -0.0630 -0.0469 42  GLN   B NE2 
520  N N   . GLU   B 34  ? 0.7560 0.6870 0.6273 0.1837  -0.0333 -0.0582 43  GLU   B N   
521  C CA  . GLU   B 34  ? 0.7488 0.7009 0.6441 0.1652  -0.0302 -0.0576 43  GLU   B CA  
522  C C   . GLU   B 34  ? 0.7384 0.7091 0.6360 0.1585  -0.0127 -0.0554 43  GLU   B C   
523  O O   . GLU   B 34  ? 0.7265 0.7117 0.6342 0.1424  -0.0059 -0.0497 43  GLU   B O   
524  C CB  . GLU   B 34  ? 0.7787 0.7256 0.6803 0.1488  -0.0363 -0.0500 43  GLU   B CB  
525  C CG  . GLU   B 34  ? 0.8388 0.7675 0.7411 0.1551  -0.0565 -0.0542 43  GLU   B CG  
526  C CD  . GLU   B 34  ? 0.9267 0.8377 0.8224 0.1460  -0.0643 -0.0466 43  GLU   B CD  
527  O OE1 . GLU   B 34  ? 0.9441 0.8634 0.8553 0.1260  -0.0623 -0.0390 43  GLU   B OE1 
528  O OE2 . GLU   B 34  ? 0.9704 0.8599 0.8445 0.1600  -0.0724 -0.0477 43  GLU   B OE2 
529  N N   . GLY   B 35  ? 0.7303 0.6998 0.6182 0.1718  -0.0067 -0.0601 44  GLY   B N   
530  C CA  . GLY   B 35  ? 0.7209 0.7044 0.6096 0.1687  0.0065  -0.0606 44  GLY   B CA  
531  C C   . GLY   B 35  ? 0.7164 0.6934 0.5920 0.1616  0.0162  -0.0527 44  GLY   B C   
532  O O   . GLY   B 35  ? 0.7152 0.7029 0.5909 0.1590  0.0254  -0.0540 44  GLY   B O   
533  N N   . VAL   B 36  ? 0.7052 0.6650 0.5688 0.1599  0.0130  -0.0457 45  VAL   B N   
534  C CA  . VAL   B 36  ? 0.7031 0.6560 0.5545 0.1539  0.0202  -0.0384 45  VAL   B CA  
535  C C   . VAL   B 36  ? 0.6978 0.6323 0.5328 0.1663  0.0202  -0.0356 45  VAL   B C   
536  O O   . VAL   B 36  ? 0.7099 0.6329 0.5385 0.1769  0.0122  -0.0354 45  VAL   B O   
537  C CB  . VAL   B 36  ? 0.7270 0.6782 0.5790 0.1410  0.0168  -0.0312 45  VAL   B CB  
538  C CG1 . VAL   B 36  ? 0.7480 0.6886 0.5844 0.1383  0.0213  -0.0242 45  VAL   B CG1 
539  C CG2 . VAL   B 36  ? 0.7191 0.6918 0.5874 0.1269  0.0209  -0.0301 45  VAL   B CG2 
540  N N   . PHE   B 37  ? 0.6776 0.6100 0.5067 0.1660  0.0286  -0.0335 46  PHE   B N   
541  C CA  . PHE   B 37  ? 0.6905 0.6084 0.5076 0.1754  0.0300  -0.0280 46  PHE   B CA  
542  C C   . PHE   B 37  ? 0.6916 0.6051 0.5009 0.1681  0.0315  -0.0200 46  PHE   B C   
543  O O   . PHE   B 37  ? 0.6833 0.6035 0.4951 0.1566  0.0358  -0.0196 46  PHE   B O   
544  C CB  . PHE   B 37  ? 0.6959 0.6118 0.5138 0.1788  0.0363  -0.0299 46  PHE   B CB  
545  C CG  . PHE   B 37  ? 0.7111 0.6131 0.5201 0.1884  0.0379  -0.0220 46  PHE   B CG  
546  C CD1 . PHE   B 37  ? 0.7301 0.6253 0.5327 0.2033  0.0340  -0.0203 46  PHE   B CD1 
547  C CD2 . PHE   B 37  ? 0.7217 0.6192 0.5296 0.1831  0.0432  -0.0157 46  PHE   B CD2 
548  C CE1 . PHE   B 37  ? 0.7477 0.6333 0.5421 0.2128  0.0371  -0.0105 46  PHE   B CE1 
549  C CE2 . PHE   B 37  ? 0.7334 0.6213 0.5364 0.1904  0.0456  -0.0059 46  PHE   B CE2 
550  C CZ  . PHE   B 37  ? 0.7441 0.6268 0.5400 0.2054  0.0434  -0.0025 46  PHE   B CZ  
551  N N   . HIS   B 38  ? 0.6892 0.5931 0.4880 0.1764  0.0275  -0.0143 47  HIS   B N   
552  C CA  . HIS   B 38  ? 0.6953 0.5959 0.4855 0.1724  0.0276  -0.0073 47  HIS   B CA  
553  C C   . HIS   B 38  ? 0.7153 0.6120 0.4991 0.1798  0.0327  0.0005  47  HIS   B C   
554  O O   . HIS   B 38  ? 0.7102 0.6025 0.4889 0.1937  0.0316  0.0032  47  HIS   B O   
555  C CB  . HIS   B 38  ? 0.6978 0.5917 0.4803 0.1785  0.0170  -0.0069 47  HIS   B CB  
556  C CG  . HIS   B 38  ? 0.7158 0.6121 0.5078 0.1714  0.0098  -0.0130 47  HIS   B CG  
557  N ND1 . HIS   B 38  ? 0.7304 0.6313 0.5329 0.1753  0.0070  -0.0202 47  HIS   B ND1 
558  C CD2 . HIS   B 38  ? 0.7250 0.6207 0.5191 0.1603  0.0050  -0.0119 47  HIS   B CD2 
559  C CE1 . HIS   B 38  ? 0.7286 0.6333 0.5414 0.1656  0.0006  -0.0228 47  HIS   B CE1 
560  N NE2 . HIS   B 38  ? 0.7328 0.6333 0.5408 0.1561  -0.0008 -0.0172 47  HIS   B NE2 
561  N N   . THR   B 39  ? 0.7148 0.6142 0.4988 0.1712  0.0380  0.0051  48  THR   B N   
562  C CA  . THR   B 39  ? 0.7250 0.6234 0.5065 0.1766  0.0426  0.0145  48  THR   B CA  
563  C C   . THR   B 39  ? 0.7234 0.6263 0.5018 0.1693  0.0436  0.0192  48  THR   B C   
564  O O   . THR   B 39  ? 0.7243 0.6283 0.4998 0.1617  0.0405  0.0152  48  THR   B O   
565  C CB  . THR   B 39  ? 0.7376 0.6339 0.5289 0.1761  0.0482  0.0152  48  THR   B CB  
566  O OG1 . THR   B 39  ? 0.7497 0.6453 0.5405 0.1820  0.0525  0.0272  48  THR   B OG1 
567  C CG2 . THR   B 39  ? 0.7280 0.6268 0.5286 0.1626  0.0505  0.0093  48  THR   B CG2 
568  N N   . MET   B 40  ? 0.7123 0.6185 0.4917 0.1720  0.0480  0.0285  49  MET   B N   
569  C CA  . MET   B 40  ? 0.7144 0.6270 0.4933 0.1654  0.0489  0.0322  49  MET   B CA  
570  C C   . MET   B 40  ? 0.7154 0.6296 0.5072 0.1521  0.0521  0.0283  49  MET   B C   
571  O O   . MET   B 40  ? 0.7222 0.6329 0.5242 0.1507  0.0547  0.0279  49  MET   B O   
572  C CB  . MET   B 40  ? 0.7189 0.6386 0.4948 0.1747  0.0516  0.0442  49  MET   B CB  
573  C CG  . MET   B 40  ? 0.7646 0.6826 0.5262 0.1926  0.0481  0.0474  49  MET   B CG  
574  S SD  . MET   B 40  ? 0.8612 0.7902 0.6103 0.2037  0.0468  0.0561  49  MET   B SD  
575  C CE  . MET   B 40  ? 0.8171 0.7392 0.5565 0.1963  0.0380  0.0460  49  MET   B CE  
576  N N   . TRP   B 41  ? 0.7182 0.6364 0.5082 0.1436  0.0506  0.0247  50  TRP   B N   
577  C CA  A TRP   B 41  ? 0.7176 0.6377 0.5173 0.1332  0.0516  0.0190  50  TRP   B CA  
578  C CA  B TRP   B 41  ? 0.7115 0.6317 0.5111 0.1332  0.0515  0.0190  50  TRP   B CA  
579  C C   . TRP   B 41  ? 0.7092 0.6303 0.5232 0.1309  0.0538  0.0248  50  TRP   B C   
580  O O   . TRP   B 41  ? 0.7056 0.6218 0.5300 0.1261  0.0534  0.0195  50  TRP   B O   
581  C CB  A TRP   B 41  ? 0.7245 0.6495 0.5169 0.1272  0.0493  0.0152  50  TRP   B CB  
582  C CB  B TRP   B 41  ? 0.7087 0.6340 0.5009 0.1274  0.0493  0.0158  50  TRP   B CB  
583  C CG  A TRP   B 41  ? 0.7404 0.6670 0.5385 0.1195  0.0490  0.0061  50  TRP   B CG  
584  C CG  B TRP   B 41  ? 0.7110 0.6386 0.5106 0.1194  0.0489  0.0082  50  TRP   B CG  
585  C CD1 A TRP   B 41  ? 0.7535 0.6806 0.5485 0.1172  0.0493  -0.0020 50  TRP   B CD1 
586  C CD1 B TRP   B 41  ? 0.7174 0.6477 0.5285 0.1153  0.0480  0.0087  50  TRP   B CD1 
587  C CD2 A TRP   B 41  ? 0.7437 0.6727 0.5522 0.1146  0.0477  0.0038  50  TRP   B CD2 
588  C CD2 B TRP   B 41  ? 0.7098 0.6381 0.5067 0.1159  0.0486  -0.0014 50  TRP   B CD2 
589  N NE1 A TRP   B 41  ? 0.7595 0.6894 0.5590 0.1132  0.0482  -0.0098 50  TRP   B NE1 
590  N NE1 B TRP   B 41  ? 0.7163 0.6465 0.5303 0.1105  0.0456  -0.0019 50  TRP   B NE1 
591  C CE2 A TRP   B 41  ? 0.7546 0.6840 0.5628 0.1113  0.0462  -0.0073 50  TRP   B CE2 
592  C CE2 B TRP   B 41  ? 0.7168 0.6470 0.5207 0.1117  0.0467  -0.0079 50  TRP   B CE2 
593  C CE3 A TRP   B 41  ? 0.7487 0.6811 0.5680 0.1128  0.0471  0.0102  50  TRP   B CE3 
594  C CE3 B TRP   B 41  ? 0.7190 0.6481 0.5091 0.1161  0.0495  -0.0048 50  TRP   B CE3 
595  C CZ2 A TRP   B 41  ? 0.7614 0.6912 0.5781 0.1076  0.0423  -0.0141 50  TRP   B CZ2 
596  C CZ2 B TRP   B 41  ? 0.7243 0.6574 0.5255 0.1104  0.0460  -0.0183 50  TRP   B CZ2 
597  C CZ3 A TRP   B 41  ? 0.7564 0.6900 0.5872 0.1066  0.0434  0.0044  50  TRP   B CZ3 
598  C CZ3 B TRP   B 41  ? 0.7304 0.6652 0.5198 0.1131  0.0504  -0.0130 50  TRP   B CZ3 
599  C CH2 A TRP   B 41  ? 0.7583 0.6890 0.5871 0.1046  0.0401  -0.0085 50  TRP   B CH2 
600  C CH2 B TRP   B 41  ? 0.7287 0.6656 0.5220 0.1116  0.0488  -0.0200 50  TRP   B CH2 
601  N N   . HIS   B 42  ? 0.7100 0.6381 0.5257 0.1343  0.0556  0.0358  51  HIS   B N   
602  C CA  . HIS   B 42  ? 0.7147 0.6460 0.5484 0.1302  0.0580  0.0441  51  HIS   B CA  
603  C C   . HIS   B 42  ? 0.7378 0.6592 0.5805 0.1325  0.0605  0.0481  51  HIS   B C   
604  O O   . HIS   B 42  ? 0.7506 0.6703 0.6107 0.1262  0.0610  0.0537  51  HIS   B O   
605  C CB  . HIS   B 42  ? 0.6997 0.6452 0.5349 0.1344  0.0608  0.0571  51  HIS   B CB  
606  C CG  . HIS   B 42  ? 0.7111 0.6597 0.5367 0.1485  0.0648  0.0677  51  HIS   B CG  
607  N ND1 . HIS   B 42  ? 0.7297 0.6800 0.5352 0.1594  0.0622  0.0659  51  HIS   B ND1 
608  C CD2 . HIS   B 42  ? 0.7193 0.6705 0.5525 0.1543  0.0704  0.0810  51  HIS   B CD2 
609  C CE1 . HIS   B 42  ? 0.7337 0.6875 0.5340 0.1730  0.0657  0.0760  51  HIS   B CE1 
610  N NE2 . HIS   B 42  ? 0.7273 0.6826 0.5433 0.1706  0.0716  0.0860  51  HIS   B NE2 
611  N N   . VAL   B 43  ? 0.7359 0.6500 0.5681 0.1410  0.0610  0.0451  52  VAL   B N   
612  C CA  . VAL   B 43  ? 0.7290 0.6329 0.5666 0.1454  0.0629  0.0482  52  VAL   B CA  
613  C C   . VAL   B 43  ? 0.7418 0.6348 0.5874 0.1380  0.0590  0.0361  52  VAL   B C   
614  O O   . VAL   B 43  ? 0.7567 0.6405 0.6148 0.1353  0.0587  0.0398  52  VAL   B O   
615  C CB  . VAL   B 43  ? 0.7351 0.6365 0.5577 0.1592  0.0633  0.0479  52  VAL   B CB  
616  C CG1 . VAL   B 43  ? 0.7547 0.6441 0.5803 0.1647  0.0641  0.0473  52  VAL   B CG1 
617  C CG2 . VAL   B 43  ? 0.7360 0.6466 0.5498 0.1704  0.0662  0.0604  52  VAL   B CG2 
618  N N   . THR   B 44  ? 0.7296 0.6237 0.5677 0.1360  0.0559  0.0222  53  THR   B N   
619  C CA  . THR   B 44  ? 0.7412 0.6283 0.5840 0.1326  0.0522  0.0096  53  THR   B CA  
620  C C   . THR   B 44  ? 0.7527 0.6431 0.6003 0.1235  0.0482  0.0014  53  THR   B C   
621  O O   . THR   B 44  ? 0.7639 0.6473 0.6171 0.1218  0.0437  -0.0081 53  THR   B O   
622  C CB  . THR   B 44  ? 0.7471 0.6360 0.5798 0.1384  0.0521  -0.0001 53  THR   B CB  
623  O OG1 . THR   B 44  ? 0.7462 0.6461 0.5707 0.1349  0.0521  -0.0038 53  THR   B OG1 
624  C CG2 . THR   B 44  ? 0.7500 0.6355 0.5775 0.1492  0.0541  0.0059  53  THR   B CG2 
625  N N   . LYS   B 45  ? 0.7577 0.6584 0.6012 0.1197  0.0488  0.0041  54  LYS   B N   
626  C CA  . LYS   B 45  ? 0.7732 0.6794 0.6170 0.1133  0.0449  -0.0041 54  LYS   B CA  
627  C C   . LYS   B 45  ? 0.7806 0.6894 0.6145 0.1151  0.0438  -0.0174 54  LYS   B C   
628  O O   . LYS   B 45  ? 0.7884 0.6981 0.6235 0.1129  0.0395  -0.0274 54  LYS   B O   
629  C CB  . LYS   B 45  ? 0.8023 0.7025 0.6633 0.1071  0.0393  -0.0056 54  LYS   B CB  
630  C CG  . LYS   B 45  ? 0.8795 0.7799 0.7551 0.1039  0.0413  0.0098  54  LYS   B CG  
631  C CD  . LYS   B 45  ? 0.9589 0.8741 0.8310 0.1026  0.0437  0.0171  54  LYS   B CD  
632  C CE  . LYS   B 45  ? 1.0196 0.9413 0.9058 0.1012  0.0473  0.0341  54  LYS   B CE  
633  N NZ  . LYS   B 45  ? 1.0522 0.9908 0.9335 0.1020  0.0490  0.0395  54  LYS   B NZ  
634  N N   . GLY   B 46  ? 0.7772 0.6886 0.6024 0.1197  0.0473  -0.0175 55  GLY   B N   
635  C CA  . GLY   B 46  ? 0.7872 0.7055 0.6058 0.1212  0.0478  -0.0274 55  GLY   B CA  
636  C C   . GLY   B 46  ? 0.8019 0.7158 0.6251 0.1258  0.0457  -0.0373 55  GLY   B C   
637  O O   . GLY   B 46  ? 0.8023 0.7259 0.6207 0.1284  0.0467  -0.0456 55  GLY   B O   
638  N N   . ALA   B 47  ? 0.8107 0.7109 0.6432 0.1277  0.0429  -0.0357 56  ALA   B N   
639  C CA  . ALA   B 47  ? 0.8164 0.7090 0.6522 0.1335  0.0390  -0.0458 56  ALA   B CA  
640  C C   . ALA   B 47  ? 0.8123 0.7079 0.6442 0.1411  0.0421  -0.0478 56  ALA   B C   
641  O O   . ALA   B 47  ? 0.8081 0.7047 0.6385 0.1423  0.0458  -0.0390 56  ALA   B O   
642  C CB  . ALA   B 47  ? 0.8224 0.6963 0.6701 0.1321  0.0341  -0.0419 56  ALA   B CB  
643  N N   . ALA   B 48  ? 0.8056 0.7028 0.6363 0.1479  0.0393  -0.0602 57  ALA   B N   
644  C CA  . ALA   B 48  ? 0.8116 0.7138 0.6405 0.1561  0.0412  -0.0637 57  ALA   B CA  
645  C C   . ALA   B 48  ? 0.8295 0.7141 0.6618 0.1608  0.0403  -0.0565 57  ALA   B C   
646  O O   . ALA   B 48  ? 0.8412 0.7088 0.6788 0.1585  0.0373  -0.0510 57  ALA   B O   
647  C CB  . ALA   B 48  ? 0.8167 0.7248 0.6431 0.1643  0.0378  -0.0789 57  ALA   B CB  
648  N N   . LEU   B 49  ? 0.8256 0.7154 0.6558 0.1674  0.0427  -0.0556 58  LEU   B N   
649  C CA  . LEU   B 49  ? 0.8388 0.7140 0.6692 0.1746  0.0423  -0.0488 58  LEU   B CA  
650  C C   . LEU   B 49  ? 0.8644 0.7396 0.6933 0.1863  0.0398  -0.0588 58  LEU   B C   
651  O O   . LEU   B 49  ? 0.8640 0.7569 0.6925 0.1886  0.0401  -0.0690 58  LEU   B O   
652  C CB  . LEU   B 49  ? 0.8259 0.7064 0.6533 0.1747  0.0459  -0.0383 58  LEU   B CB  
653  C CG  . LEU   B 49  ? 0.8231 0.7059 0.6500 0.1657  0.0483  -0.0283 58  LEU   B CG  
654  C CD1 . LEU   B 49  ? 0.8216 0.7101 0.6432 0.1689  0.0495  -0.0219 58  LEU   B CD1 
655  C CD2 . LEU   B 49  ? 0.8261 0.6947 0.6576 0.1631  0.0484  -0.0184 58  LEU   B CD2 
656  N N   . ARG   B 50  ? 0.8859 0.7425 0.7138 0.1942  0.0376  -0.0551 59  ARG   B N   
657  C CA  . ARG   B 50  ? 0.9138 0.7677 0.7386 0.2074  0.0344  -0.0640 59  ARG   B CA  
658  C C   . ARG   B 50  ? 0.9287 0.7829 0.7497 0.2157  0.0365  -0.0570 59  ARG   B C   
659  O O   . ARG   B 50  ? 0.9181 0.7645 0.7374 0.2142  0.0392  -0.0434 59  ARG   B O   
660  C CB  . ARG   B 50  ? 0.9549 0.7841 0.7797 0.2120  0.0283  -0.0665 59  ARG   B CB  
661  C CG  . ARG   B 50  ? 1.0361 0.8469 0.8562 0.2250  0.0260  -0.0633 59  ARG   B CG  
662  C CD  . ARG   B 50  ? 1.1070 0.8937 0.9266 0.2303  0.0177  -0.0697 59  ARG   B CD  
663  N NE  . ARG   B 50  ? 1.1666 0.9314 0.9936 0.2200  0.0158  -0.0574 59  ARG   B NE  
664  C CZ  . ARG   B 50  ? 1.2190 0.9622 1.0472 0.2214  0.0165  -0.0418 59  ARG   B CZ  
665  N NH1 . ARG   B 50  ? 1.2211 0.9602 1.0404 0.2346  0.0190  -0.0374 59  ARG   B NH1 
666  N NH2 . ARG   B 50  ? 1.2286 0.9555 1.0676 0.2099  0.0148  -0.0298 59  ARG   B NH2 
667  N N   . SER   B 51  ? 0.9503 0.8164 0.7702 0.2253  0.0348  -0.0667 60  SER   B N   
668  C CA  . SER   B 51  ? 0.9834 0.8496 0.7994 0.2358  0.0343  -0.0633 60  SER   B CA  
669  C C   . SER   B 51  ? 1.0168 0.8793 0.8299 0.2503  0.0299  -0.0742 60  SER   B C   
670  O O   . SER   B 51  ? 1.0176 0.8999 0.8353 0.2531  0.0282  -0.0868 60  SER   B O   
671  C CB  . SER   B 51  ? 0.9881 0.8769 0.8087 0.2313  0.0349  -0.0658 60  SER   B CB  
672  O OG  . SER   B 51  ? 1.0162 0.9046 0.8333 0.2431  0.0317  -0.0653 60  SER   B OG  
673  N N   . GLY   B 52  ? 1.0426 0.8806 0.8490 0.2592  0.0280  -0.0691 61  GLY   B N   
674  C CA  . GLY   B 52  ? 1.0663 0.8963 0.8679 0.2742  0.0227  -0.0795 61  GLY   B CA  
675  C C   . GLY   B 52  ? 1.0864 0.9182 0.8911 0.2709  0.0194  -0.0918 61  GLY   B C   
676  O O   . GLY   B 52  ? 1.0930 0.9112 0.8998 0.2614  0.0189  -0.0873 61  GLY   B O   
677  N N   . GLU   B 53  ? 1.0880 0.9403 0.8942 0.2789  0.0168  -0.1077 62  GLU   B N   
678  C CA  . GLU   B 53  ? 1.0972 0.9567 0.9046 0.2785  0.0138  -0.1205 62  GLU   B CA  
679  C C   . GLU   B 53  ? 1.0754 0.9683 0.8913 0.2671  0.0192  -0.1241 62  GLU   B C   
680  O O   . GLU   B 53  ? 1.0764 0.9849 0.8926 0.2702  0.0178  -0.1361 62  GLU   B O   
681  C CB  . GLU   B 53  ? 1.1506 1.0098 0.9519 0.2974  0.0070  -0.1358 62  GLU   B CB  
682  C CG  . GLU   B 53  ? 1.2659 1.0867 1.0580 0.3053  -0.0009 -0.1356 62  GLU   B CG  
683  C CD  . GLU   B 53  ? 1.4069 1.2250 1.1909 0.3249  -0.0094 -0.1527 62  GLU   B CD  
684  O OE1 . GLU   B 53  ? 1.4364 1.2826 1.2218 0.3350  -0.0083 -0.1628 62  GLU   B OE1 
685  O OE2 . GLU   B 53  ? 1.4624 1.2503 1.2394 0.3305  -0.0181 -0.1561 62  GLU   B OE2 
686  N N   . GLY   B 54  ? 1.0538 0.9564 0.8752 0.2550  0.0248  -0.1133 63  GLY   B N   
687  C CA  . GLY   B 54  ? 1.0304 0.9613 0.8596 0.2431  0.0300  -0.1134 63  GLY   B CA  
688  C C   . GLY   B 54  ? 1.0126 0.9358 0.8413 0.2282  0.0332  -0.1040 63  GLY   B C   
689  O O   . GLY   B 54  ? 1.0230 0.9220 0.8484 0.2249  0.0324  -0.0942 63  GLY   B O   
690  N N   . ARG   B 55  ? 0.9775 0.9233 0.8100 0.2198  0.0370  -0.1062 64  ARG   B N   
691  C CA  . ARG   B 55  ? 0.9555 0.8966 0.7867 0.2070  0.0395  -0.0990 64  ARG   B CA  
692  C C   . ARG   B 55  ? 0.9132 0.8701 0.7490 0.1951  0.0447  -0.0896 64  ARG   B C   
693  O O   . ARG   B 55  ? 0.9057 0.8877 0.7479 0.1935  0.0476  -0.0919 64  ARG   B O   
694  C CB  . ARG   B 55  ? 0.9732 0.9224 0.8010 0.2087  0.0382  -0.1091 64  ARG   B CB  
695  C CG  . ARG   B 55  ? 1.0174 0.9591 0.8429 0.1980  0.0386  -0.1042 64  ARG   B CG  
696  C CD  . ARG   B 55  ? 1.0665 1.0217 0.8871 0.2026  0.0370  -0.1161 64  ARG   B CD  
697  N NE  . ARG   B 55  ? 1.1116 1.0627 0.9295 0.1934  0.0369  -0.1127 64  ARG   B NE  
698  C CZ  . ARG   B 55  ? 1.1518 1.0854 0.9666 0.1956  0.0290  -0.1194 64  ARG   B CZ  
699  N NH1 . ARG   B 55  ? 1.1541 1.0702 0.9674 0.2064  0.0202  -0.1296 64  ARG   B NH1 
700  N NH2 . ARG   B 55  ? 1.1508 1.0832 0.9642 0.1873  0.0285  -0.1166 64  ARG   B NH2 
701  N N   . LEU   B 56  ? 0.8800 0.8224 0.7136 0.1867  0.0454  -0.0787 65  LEU   B N   
702  C CA  . LEU   B 56  ? 0.8496 0.8015 0.6849 0.1762  0.0486  -0.0700 65  LEU   B CA  
703  C C   . LEU   B 56  ? 0.8185 0.7717 0.6504 0.1672  0.0507  -0.0681 65  LEU   B C   
704  O O   . LEU   B 56  ? 0.8212 0.7569 0.6500 0.1657  0.0488  -0.0653 65  LEU   B O   
705  C CB  . LEU   B 56  ? 0.8548 0.7903 0.6876 0.1762  0.0471  -0.0593 65  LEU   B CB  
706  C CG  . LEU   B 56  ? 0.8775 0.8055 0.7101 0.1877  0.0438  -0.0597 65  LEU   B CG  
707  C CD1 . LEU   B 56  ? 0.8889 0.8079 0.7172 0.1880  0.0426  -0.0493 65  LEU   B CD1 
708  C CD2 . LEU   B 56  ? 0.8735 0.8208 0.7136 0.1921  0.0423  -0.0687 65  LEU   B CD2 
709  N N   . ASP   B 57  ? 0.7918 0.7661 0.6248 0.1614  0.0544  -0.0691 66  ASP   B N   
710  C CA  . ASP   B 57  ? 0.7783 0.7555 0.6059 0.1544  0.0564  -0.0674 66  ASP   B CA  
711  C C   . ASP   B 57  ? 0.7552 0.7305 0.5811 0.1441  0.0579  -0.0558 66  ASP   B C   
712  O O   . ASP   B 57  ? 0.7549 0.7369 0.5853 0.1412  0.0584  -0.0509 66  ASP   B O   
713  C CB  . ASP   B 57  ? 0.8165 0.8195 0.6438 0.1560  0.0603  -0.0739 66  ASP   B CB  
714  C CG  . ASP   B 57  ? 0.9263 0.9333 0.7528 0.1686  0.0578  -0.0871 66  ASP   B CG  
715  O OD1 . ASP   B 57  ? 0.9613 0.9462 0.7850 0.1740  0.0519  -0.0921 66  ASP   B OD1 
716  O OD2 . ASP   B 57  ? 0.9555 0.9882 0.7848 0.1734  0.0615  -0.0920 66  ASP   B OD2 
717  N N   . PRO   B 58  ? 0.7415 0.7078 0.5615 0.1391  0.0575  -0.0519 67  PRO   B N   
718  C CA  . PRO   B 58  ? 0.7319 0.6972 0.5482 0.1309  0.0583  -0.0418 67  PRO   B CA  
719  C C   . PRO   B 58  ? 0.7181 0.7029 0.5344 0.1251  0.0622  -0.0395 67  PRO   B C   
720  O O   . PRO   B 58  ? 0.7244 0.7261 0.5411 0.1270  0.0658  -0.0451 67  PRO   B O   
721  C CB  . PRO   B 58  ? 0.7495 0.7057 0.5602 0.1282  0.0570  -0.0407 67  PRO   B CB  
722  C CG  . PRO   B 58  ? 0.7590 0.7176 0.5702 0.1329  0.0558  -0.0514 67  PRO   B CG  
723  C CD  . PRO   B 58  ? 0.7409 0.6990 0.5578 0.1408  0.0549  -0.0576 67  PRO   B CD  
724  N N   . TYR   B 59  ? 0.7001 0.6830 0.5164 0.1189  0.0612  -0.0307 68  TYR   B N   
725  C CA  . TYR   B 59  ? 0.6853 0.6835 0.5039 0.1112  0.0641  -0.0252 68  TYR   B CA  
726  C C   . TYR   B 59  ? 0.6816 0.6719 0.4898 0.1044  0.0632  -0.0167 68  TYR   B C   
727  O O   . TYR   B 59  ? 0.6731 0.6751 0.4773 0.0994  0.0674  -0.0130 68  TYR   B O   
728  C CB  . TYR   B 59  ? 0.6761 0.6766 0.5064 0.1096  0.0606  -0.0228 68  TYR   B CB  
729  C CG  . TYR   B 59  ? 0.6668 0.6839 0.5050 0.0997  0.0629  -0.0155 68  TYR   B CG  
730  C CD1 . TYR   B 59  ? 0.6690 0.6766 0.5029 0.0911  0.0596  -0.0056 68  TYR   B CD1 
731  C CD2 . TYR   B 59  ? 0.6680 0.7104 0.5190 0.0990  0.0678  -0.0176 68  TYR   B CD2 
732  C CE1 . TYR   B 59  ? 0.6688 0.6891 0.5120 0.0805  0.0609  0.0031  68  TYR   B CE1 
733  C CE2 . TYR   B 59  ? 0.6659 0.7257 0.5277 0.0884  0.0705  -0.0084 68  TYR   B CE2 
734  C CZ  . TYR   B 59  ? 0.6818 0.7291 0.5404 0.0784  0.0668  0.0026  68  TYR   B CZ  
735  O OH  . TYR   B 59  ? 0.7113 0.7740 0.5820 0.0664  0.0692  0.0137  68  TYR   B OH  
736  N N   . TRP   B 60  ? 0.6807 0.6525 0.4838 0.1054  0.0578  -0.0131 69  TRP   B N   
737  C CA  . TRP   B 60  ? 0.6733 0.6363 0.4651 0.1011  0.0557  -0.0060 69  TRP   B CA  
738  C C   . TRP   B 60  ? 0.6763 0.6257 0.4624 0.1066  0.0528  -0.0068 69  TRP   B C   
739  O O   . TRP   B 60  ? 0.6748 0.6170 0.4653 0.1126  0.0506  -0.0083 69  TRP   B O   
740  C CB  . TRP   B 60  ? 0.6662 0.6224 0.4589 0.0964  0.0501  0.0014  69  TRP   B CB  
741  C CG  . TRP   B 60  ? 0.6888 0.6312 0.4681 0.0952  0.0454  0.0076  69  TRP   B CG  
742  C CD1 . TRP   B 60  ? 0.7119 0.6556 0.4814 0.0896  0.0471  0.0130  69  TRP   B CD1 
743  C CD2 . TRP   B 60  ? 0.6989 0.6254 0.4710 0.1022  0.0386  0.0086  69  TRP   B CD2 
744  N NE1 . TRP   B 60  ? 0.7220 0.6505 0.4790 0.0924  0.0409  0.0164  69  TRP   B NE1 
745  C CE2 . TRP   B 60  ? 0.7188 0.6378 0.4773 0.1004  0.0358  0.0138  69  TRP   B CE2 
746  C CE3 . TRP   B 60  ? 0.7127 0.6321 0.4871 0.1115  0.0352  0.0060  69  TRP   B CE3 
747  C CZ2 . TRP   B 60  ? 0.7298 0.6362 0.4779 0.1079  0.0294  0.0157  69  TRP   B CZ2 
748  C CZ3 . TRP   B 60  ? 0.7275 0.6352 0.4915 0.1190  0.0295  0.0091  69  TRP   B CZ3 
749  C CH2 . TRP   B 60  ? 0.7317 0.6338 0.4830 0.1173  0.0266  0.0135  69  TRP   B CH2 
750  N N   . GLY   B 61  ? 0.6853 0.6320 0.4616 0.1048  0.0526  -0.0044 70  GLY   B N   
751  C CA  . GLY   B 61  ? 0.6997 0.6370 0.4728 0.1091  0.0500  -0.0032 70  GLY   B CA  
752  C C   . GLY   B 61  ? 0.7075 0.6425 0.4690 0.1073  0.0481  0.0008  70  GLY   B C   
753  O O   . GLY   B 61  ? 0.7006 0.6414 0.4556 0.1030  0.0499  0.0008  70  GLY   B O   
754  N N   . ASP   B 62  ? 0.7100 0.6384 0.4682 0.1117  0.0449  0.0044  71  ASP   B N   
755  C CA  . ASP   B 62  ? 0.7393 0.6669 0.4865 0.1117  0.0424  0.0073  71  ASP   B CA  
756  C C   . ASP   B 62  ? 0.7475 0.6754 0.4985 0.1168  0.0414  0.0094  71  ASP   B C   
757  O O   . ASP   B 62  ? 0.7520 0.6759 0.5041 0.1230  0.0401  0.0137  71  ASP   B O   
758  C CB  . ASP   B 62  ? 0.7883 0.7075 0.5227 0.1118  0.0375  0.0128  71  ASP   B CB  
759  C CG  . ASP   B 62  ? 0.8841 0.8017 0.6045 0.1125  0.0346  0.0152  71  ASP   B CG  
760  O OD1 . ASP   B 62  ? 0.9161 0.8299 0.6304 0.1192  0.0303  0.0179  71  ASP   B OD1 
761  O OD2 . ASP   B 62  ? 0.9518 0.8732 0.6662 0.1079  0.0367  0.0144  71  ASP   B OD2 
762  N N   . VAL   B 63  ? 0.7429 0.6772 0.4974 0.1146  0.0420  0.0065  72  VAL   B N   
763  C CA  . VAL   B 63  ? 0.7454 0.6840 0.5082 0.1172  0.0415  0.0098  72  VAL   B CA  
764  C C   . VAL   B 63  ? 0.7572 0.6960 0.5088 0.1239  0.0384  0.0166  72  VAL   B C   
765  O O   . VAL   B 63  ? 0.7693 0.7116 0.5261 0.1297  0.0392  0.0229  72  VAL   B O   
766  C CB  . VAL   B 63  ? 0.7531 0.6984 0.5244 0.1124  0.0406  0.0035  72  VAL   B CB  
767  C CG1 . VAL   B 63  ? 0.7567 0.7099 0.5347 0.1136  0.0386  0.0078  72  VAL   B CG1 
768  C CG2 . VAL   B 63  ? 0.7532 0.6965 0.5392 0.1093  0.0419  -0.0022 72  VAL   B CG2 
769  N N   . LYS   B 64  ? 0.7636 0.6987 0.4990 0.1244  0.0349  0.0162  73  LYS   B N   
770  C CA  . LYS   B 64  ? 0.7714 0.7050 0.4937 0.1327  0.0302  0.0213  73  LYS   B CA  
771  C C   . LYS   B 64  ? 0.7709 0.6963 0.4884 0.1409  0.0277  0.0255  73  LYS   B C   
772  O O   . LYS   B 64  ? 0.7691 0.6989 0.4833 0.1510  0.0260  0.0302  73  LYS   B O   
773  C CB  . LYS   B 64  ? 0.7849 0.7133 0.4893 0.1321  0.0257  0.0200  73  LYS   B CB  
774  C CG  . LYS   B 64  ? 0.8290 0.7571 0.5201 0.1427  0.0198  0.0240  73  LYS   B CG  
775  C CD  . LYS   B 64  ? 0.8834 0.8066 0.5566 0.1435  0.0148  0.0228  73  LYS   B CD  
776  C CE  . LYS   B 64  ? 0.9468 0.8671 0.6050 0.1564  0.0075  0.0260  73  LYS   B CE  
777  N NZ  . LYS   B 64  ? 0.9963 0.9121 0.6361 0.1588  0.0020  0.0246  73  LYS   B NZ  
778  N N   . GLN   B 65  ? 0.7738 0.6896 0.4916 0.1378  0.0271  0.0237  74  GLN   B N   
779  C CA  . GLN   B 65  ? 0.7753 0.6832 0.4902 0.1465  0.0231  0.0258  74  GLN   B CA  
780  C C   . GLN   B 65  ? 0.7510 0.6657 0.4789 0.1512  0.0284  0.0278  74  GLN   B C   
781  O O   . GLN   B 65  ? 0.7452 0.6568 0.4686 0.1627  0.0255  0.0305  74  GLN   B O   
782  C CB  . GLN   B 65  ? 0.8193 0.7156 0.5324 0.1416  0.0190  0.0234  74  GLN   B CB  
783  C CG  . GLN   B 65  ? 0.9218 0.8093 0.6225 0.1362  0.0137  0.0243  74  GLN   B CG  
784  C CD  . GLN   B 65  ? 1.0656 0.9481 0.7489 0.1449  0.0069  0.0267  74  GLN   B CD  
785  O OE1 . GLN   B 65  ? 1.1058 0.9905 0.7815 0.1412  0.0076  0.0272  74  GLN   B OE1 
786  N NE2 . GLN   B 65  ? 1.0991 0.9755 0.7742 0.1585  -0.0006 0.0276  74  GLN   B NE2 
787  N N   . ASP   B 66  ? 0.7319 0.6545 0.4746 0.1434  0.0353  0.0263  75  ASP   B N   
788  C CA  . ASP   B 66  ? 0.7132 0.6400 0.4699 0.1450  0.0406  0.0288  75  ASP   B CA  
789  C C   . ASP   B 66  ? 0.7080 0.6268 0.4662 0.1479  0.0400  0.0262  75  ASP   B C   
790  O O   . ASP   B 66  ? 0.6970 0.6155 0.4573 0.1569  0.0414  0.0305  75  ASP   B O   
791  C CB  . ASP   B 66  ? 0.7194 0.6551 0.4769 0.1550  0.0423  0.0383  75  ASP   B CB  
792  C CG  . ASP   B 66  ? 0.7228 0.6629 0.4969 0.1543  0.0487  0.0435  75  ASP   B CG  
793  O OD1 . ASP   B 66  ? 0.6923 0.6297 0.4788 0.1443  0.0506  0.0387  75  ASP   B OD1 
794  O OD2 . ASP   B 66  ? 0.7363 0.6818 0.5100 0.1650  0.0512  0.0527  75  ASP   B OD2 
795  N N   . LEU   B 67  ? 0.6931 0.6073 0.4505 0.1411  0.0383  0.0198  76  LEU   B N   
796  C CA  . LEU   B 67  ? 0.6935 0.6030 0.4550 0.1430  0.0372  0.0162  76  LEU   B CA  
797  C C   . LEU   B 67  ? 0.6994 0.6132 0.4706 0.1333  0.0412  0.0096  76  LEU   B C   
798  O O   . LEU   B 67  ? 0.7001 0.6187 0.4707 0.1255  0.0431  0.0074  76  LEU   B O   
799  C CB  . LEU   B 67  ? 0.6973 0.5989 0.4492 0.1455  0.0292  0.0157  76  LEU   B CB  
800  C CG  . LEU   B 67  ? 0.7239 0.6200 0.4633 0.1589  0.0229  0.0200  76  LEU   B CG  
801  C CD1 . LEU   B 67  ? 0.7453 0.6301 0.4750 0.1596  0.0124  0.0183  76  LEU   B CD1 
802  C CD2 . LEU   B 67  ? 0.7258 0.6222 0.4674 0.1716  0.0239  0.0216  76  LEU   B CD2 
803  N N   . VAL   B 68  ? 0.6885 0.6016 0.4672 0.1359  0.0420  0.0060  77  VAL   B N   
804  C CA  . VAL   B 68  ? 0.6871 0.6064 0.4743 0.1300  0.0454  -0.0010 77  VAL   B CA  
805  C C   . VAL   B 68  ? 0.6722 0.5909 0.4643 0.1344  0.0430  -0.0043 77  VAL   B C   
806  O O   . VAL   B 68  ? 0.6565 0.5687 0.4473 0.1439  0.0403  -0.0024 77  VAL   B O   
807  C CB  . VAL   B 68  ? 0.6961 0.6167 0.4907 0.1292  0.0494  -0.0039 77  VAL   B CB  
808  C CG1 . VAL   B 68  ? 0.7046 0.6181 0.5032 0.1373  0.0499  0.0003  77  VAL   B CG1 
809  C CG2 . VAL   B 68  ? 0.6997 0.6272 0.5002 0.1261  0.0516  -0.0129 77  VAL   B CG2 
810  N N   . SER   B 69  ? 0.6649 0.5925 0.4628 0.1284  0.0441  -0.0089 78  SER   B N   
811  C CA  . SER   B 69  ? 0.6717 0.6027 0.4778 0.1314  0.0418  -0.0130 78  SER   B CA  
812  C C   . SER   B 69  ? 0.6701 0.6132 0.4846 0.1301  0.0471  -0.0202 78  SER   B C   
813  O O   . SER   B 69  ? 0.6559 0.6070 0.4692 0.1246  0.0516  -0.0218 78  SER   B O   
814  C CB  . SER   B 69  ? 0.6956 0.6286 0.5037 0.1255  0.0366  -0.0107 78  SER   B CB  
815  O OG  . SER   B 69  ? 0.7359 0.6816 0.5475 0.1146  0.0410  -0.0096 78  SER   B OG  
816  N N   . TYR   B 70  ? 0.6705 0.6154 0.4919 0.1370  0.0457  -0.0254 79  TYR   B N   
817  C CA  . TYR   B 70  ? 0.6806 0.6362 0.5089 0.1394  0.0492  -0.0335 79  TYR   B CA  
818  C C   . TYR   B 70  ? 0.6852 0.6553 0.5245 0.1393  0.0476  -0.0374 79  TYR   B C   
819  O O   . TYR   B 70  ? 0.6901 0.6548 0.5321 0.1425  0.0415  -0.0362 79  TYR   B O   
820  C CB  . TYR   B 70  ? 0.6852 0.6281 0.5118 0.1500  0.0485  -0.0363 79  TYR   B CB  
821  C CG  . TYR   B 70  ? 0.6944 0.6259 0.5157 0.1487  0.0503  -0.0328 79  TYR   B CG  
822  C CD1 . TYR   B 70  ? 0.6970 0.6188 0.5125 0.1481  0.0494  -0.0237 79  TYR   B CD1 
823  C CD2 . TYR   B 70  ? 0.7126 0.6441 0.5355 0.1488  0.0517  -0.0389 79  TYR   B CD2 
824  C CE1 . TYR   B 70  ? 0.7110 0.6259 0.5254 0.1456  0.0509  -0.0197 79  TYR   B CE1 
825  C CE2 . TYR   B 70  ? 0.7237 0.6451 0.5453 0.1461  0.0515  -0.0360 79  TYR   B CE2 
826  C CZ  . TYR   B 70  ? 0.7234 0.6377 0.5422 0.1436  0.0516  -0.0259 79  TYR   B CZ  
827  O OH  . TYR   B 70  ? 0.7375 0.6451 0.5585 0.1399  0.0512  -0.0229 79  TYR   B OH  
828  N N   . CYS   B 71  ? 0.6773 0.6676 0.5234 0.1364  0.0524  -0.0421 80  CYS   B N   
829  C CA  . CYS   B 71  ? 0.6844 0.6958 0.5445 0.1358  0.0526  -0.0458 80  CYS   B CA  
830  C C   . CYS   B 71  ? 0.6822 0.7042 0.5512 0.1236  0.0516  -0.0378 80  CYS   B C   
831  O O   . CYS   B 71  ? 0.6903 0.7354 0.5738 0.1196  0.0536  -0.0384 80  CYS   B O   
832  C CB  . CYS   B 71  ? 0.7174 0.7239 0.5827 0.1469  0.0471  -0.0523 80  CYS   B CB  
833  S SG  . CYS   B 71  ? 0.8150 0.8026 0.6692 0.1609  0.0470  -0.0585 80  CYS   B SG  
834  N N   . GLY   B 72  ? 0.6696 0.6758 0.5308 0.1177  0.0483  -0.0300 81  GLY   B N   
835  C CA  . GLY   B 72  ? 0.6587 0.6692 0.5271 0.1058  0.0454  -0.0216 81  GLY   B CA  
836  C C   . GLY   B 72  ? 0.6594 0.6488 0.5138 0.1024  0.0413  -0.0144 81  GLY   B C   
837  O O   . GLY   B 72  ? 0.6603 0.6352 0.5007 0.1090  0.0418  -0.0155 81  GLY   B O   
838  N N   . PRO   B 73  ? 0.6551 0.6435 0.5142 0.0918  0.0371  -0.0063 82  PRO   B N   
839  C CA  . PRO   B 73  ? 0.6712 0.6390 0.5156 0.0897  0.0320  0.0001  82  PRO   B CA  
840  C C   . PRO   B 73  ? 0.6838 0.6295 0.5211 0.1000  0.0207  -0.0031 82  PRO   B C   
841  O O   . PRO   B 73  ? 0.6716 0.6170 0.5185 0.1059  0.0144  -0.0087 82  PRO   B O   
842  C CB  . PRO   B 73  ? 0.6803 0.6528 0.5335 0.0754  0.0298  0.0098  82  PRO   B CB  
843  C CG  . PRO   B 73  ? 0.6715 0.6620 0.5482 0.0713  0.0286  0.0079  82  PRO   B CG  
844  C CD  . PRO   B 73  ? 0.6435 0.6498 0.5226 0.0810  0.0365  -0.0019 82  PRO   B CD  
845  N N   . TRP   B 74  ? 0.6970 0.6258 0.5169 0.1036  0.0179  0.0003  83  TRP   B N   
846  C CA  . TRP   B 74  ? 0.7143 0.6244 0.5238 0.1159  0.0079  -0.0015 83  TRP   B CA  
847  C C   . TRP   B 74  ? 0.7326 0.6343 0.5510 0.1159  -0.0062 -0.0032 83  TRP   B C   
848  O O   . TRP   B 74  ? 0.7299 0.6302 0.5552 0.1038  -0.0109 0.0019  83  TRP   B O   
849  C CB  . TRP   B 74  ? 0.7176 0.6157 0.5088 0.1175  0.0070  0.0038  83  TRP   B CB  
850  C CG  . TRP   B 74  ? 0.7132 0.5968 0.4914 0.1329  -0.0011 0.0025  83  TRP   B CG  
851  C CD1 . TRP   B 74  ? 0.7219 0.5898 0.4934 0.1394  -0.0152 0.0020  83  TRP   B CD1 
852  C CD2 . TRP   B 74  ? 0.7120 0.5967 0.4825 0.1447  0.0043  0.0021  83  TRP   B CD2 
853  N NE1 . TRP   B 74  ? 0.7331 0.5945 0.4911 0.1567  -0.0182 0.0009  83  TRP   B NE1 
854  C CE2 . TRP   B 74  ? 0.7269 0.5994 0.4852 0.1594  -0.0055 0.0022  83  TRP   B CE2 
855  C CE3 . TRP   B 74  ? 0.7079 0.6023 0.4815 0.1446  0.0157  0.0020  83  TRP   B CE3 
856  C CZ2 . TRP   B 74  ? 0.7347 0.6082 0.4845 0.1738  -0.0021 0.0040  83  TRP   B CZ2 
857  C CZ3 . TRP   B 74  ? 0.7161 0.6085 0.4831 0.1564  0.0180  0.0043  83  TRP   B CZ3 
858  C CH2 . TRP   B 74  ? 0.7286 0.6123 0.4840 0.1707  0.0103  0.0062  83  TRP   B CH2 
859  N N   . LYS   B 75  ? 0.7447 0.6416 0.5644 0.1292  -0.0130 -0.0102 84  LYS   B N   
860  C CA  . LYS   B 75  ? 0.7585 0.6485 0.5885 0.1316  -0.0281 -0.0148 84  LYS   B CA  
861  C C   . LYS   B 75  ? 0.7897 0.6573 0.6035 0.1461  -0.0430 -0.0171 84  LYS   B C   
862  O O   . LYS   B 75  ? 0.8033 0.6609 0.6244 0.1472  -0.0589 -0.0211 84  LYS   B O   
863  C CB  . LYS   B 75  ? 0.7710 0.6726 0.6135 0.1392  -0.0271 -0.0233 84  LYS   B CB  
864  C CG  . LYS   B 75  ? 0.7791 0.7049 0.6383 0.1285  -0.0144 -0.0235 84  LYS   B CG  
865  C CD  . LYS   B 75  ? 0.7955 0.7332 0.6761 0.1113  -0.0175 -0.0198 84  LYS   B CD  
866  C CE  . LYS   B 75  ? 0.8226 0.7881 0.7172 0.1032  -0.0038 -0.0193 84  LYS   B CE  
867  N NZ  . LYS   B 75  ? 0.8479 0.8310 0.7673 0.0872  -0.0056 -0.0143 84  LYS   B NZ  
868  N N   . LEU   B 76  ? 0.7962 0.6573 0.5895 0.1585  -0.0391 -0.0150 85  LEU   B N   
869  C CA  . LEU   B 76  ? 0.8187 0.6628 0.5941 0.1769  -0.0520 -0.0175 85  LEU   B CA  
870  C C   . LEU   B 76  ? 0.8491 0.6778 0.6137 0.1729  -0.0616 -0.0135 85  LEU   B C   
871  O O   . LEU   B 76  ? 0.8434 0.6748 0.5999 0.1664  -0.0524 -0.0067 85  LEU   B O   
872  C CB  . LEU   B 76  ? 0.8156 0.6641 0.5756 0.1930  -0.0422 -0.0154 85  LEU   B CB  
873  C CG  . LEU   B 76  ? 0.8141 0.6765 0.5830 0.1944  -0.0294 -0.0166 85  LEU   B CG  
874  C CD1 . LEU   B 76  ? 0.8267 0.6914 0.5821 0.2083  -0.0207 -0.0115 85  LEU   B CD1 
875  C CD2 . LEU   B 76  ? 0.8147 0.6777 0.5940 0.2012  -0.0375 -0.0251 85  LEU   B CD2 
876  N N   . ASP   B 77  ? 0.8820 0.6931 0.6463 0.1774  -0.0814 -0.0183 86  ASP   B N   
877  C CA  . ASP   B 77  ? 0.9305 0.7228 0.6842 0.1740  -0.0933 -0.0150 86  ASP   B CA  
878  C C   . ASP   B 77  ? 0.9565 0.7280 0.6893 0.1969  -0.1126 -0.0215 86  ASP   B C   
879  O O   . ASP   B 77  ? 0.9709 0.7245 0.6919 0.1966  -0.1238 -0.0196 86  ASP   B O   
880  C CB  . ASP   B 77  ? 0.9783 0.7651 0.7529 0.1522  -0.1010 -0.0120 86  ASP   B CB  
881  C CG  . ASP   B 77  ? 1.0903 0.8757 0.8862 0.1514  -0.1145 -0.0199 86  ASP   B CG  
882  O OD1 . ASP   B 77  ? 1.1167 0.9036 0.9087 0.1697  -0.1189 -0.0292 86  ASP   B OD1 
883  O OD2 . ASP   B 77  ? 1.1364 0.9197 0.9534 0.1325  -0.1210 -0.0161 86  ASP   B OD2 
884  N N   . ALA   B 78  ? 0.9547 0.7285 0.6807 0.2185  -0.1166 -0.0291 87  ALA   B N   
885  C CA  . ALA   B 78  ? 0.9731 0.7301 0.6766 0.2440  -0.1345 -0.0358 87  ALA   B CA  
886  C C   . ALA   B 78  ? 0.9852 0.7440 0.6641 0.2544  -0.1272 -0.0292 87  ALA   B C   
887  O O   . ALA   B 78  ? 0.9766 0.7539 0.6563 0.2476  -0.1064 -0.0208 87  ALA   B O   
888  C CB  . ALA   B 78  ? 0.9688 0.7309 0.6684 0.2666  -0.1383 -0.0441 87  ALA   B CB  
889  N N   . ALA   B 79  ? 0.9916 0.7312 0.6501 0.2706  -0.1456 -0.0335 88  ALA   B N   
890  C CA  . ALA   B 79  ? 1.0075 0.7497 0.6422 0.2833  -0.1415 -0.0286 88  ALA   B CA  
891  C C   . ALA   B 79  ? 1.0261 0.7643 0.6355 0.3183  -0.1543 -0.0355 88  ALA   B C   
892  O O   . ALA   B 79  ? 1.0256 0.7466 0.6319 0.3315  -0.1753 -0.0466 88  ALA   B O   
893  C CB  . ALA   B 79  ? 1.0184 0.7410 0.6481 0.2711  -0.1518 -0.0264 88  ALA   B CB  
894  N N   . TRP   B 80  ? 1.0423 0.7970 0.6335 0.3340  -0.1429 -0.0292 89  TRP   B N   
895  C CA  . TRP   B 80  ? 1.0792 0.8346 0.6434 0.3695  -0.1534 -0.0339 89  TRP   B CA  
896  C C   . TRP   B 80  ? 1.1170 0.8429 0.6637 0.3794  -0.1804 -0.0433 89  TRP   B C   
897  O O   . TRP   B 80  ? 1.1055 0.8208 0.6542 0.3617  -0.1816 -0.0397 89  TRP   B O   
898  C CB  . TRP   B 80  ? 1.0761 0.8592 0.6288 0.3800  -0.1337 -0.0224 89  TRP   B CB  
899  C CG  . TRP   B 80  ? 1.0949 0.8840 0.6187 0.4178  -0.1424 -0.0251 89  TRP   B CG  
900  C CD1 . TRP   B 80  ? 1.1142 0.9012 0.6255 0.4454  -0.1535 -0.0328 89  TRP   B CD1 
901  C CD2 . TRP   B 80  ? 1.0990 0.8995 0.6018 0.4342  -0.1410 -0.0205 89  TRP   B CD2 
902  N NE1 . TRP   B 80  ? 1.1237 0.9210 0.6065 0.4788  -0.1583 -0.0327 89  TRP   B NE1 
903  C CE2 . TRP   B 80  ? 1.1159 0.9221 0.5936 0.4724  -0.1510 -0.0252 89  TRP   B CE2 
904  C CE3 . TRP   B 80  ? 1.1001 0.9085 0.6026 0.4218  -0.1325 -0.0132 89  TRP   B CE3 
905  C CZ2 . TRP   B 80  ? 1.1230 0.9443 0.5760 0.4981  -0.1518 -0.0221 89  TRP   B CZ2 
906  C CZ3 . TRP   B 80  ? 1.1150 0.9368 0.5940 0.4465  -0.1345 -0.0110 89  TRP   B CZ3 
907  C CH2 . TRP   B 80  ? 1.1196 0.9492 0.5747 0.4841  -0.1433 -0.0150 89  TRP   B CH2 
908  N N   . ASP   B 81  ? 1.1525 0.8627 0.6831 0.4069  -0.2035 -0.0560 90  ASP   B N   
909  C CA  . ASP   B 81  ? 1.2036 0.8808 0.7188 0.4160  -0.2326 -0.0664 90  ASP   B CA  
910  C C   . ASP   B 81  ? 1.2512 0.9301 0.7350 0.4394  -0.2368 -0.0655 90  ASP   B C   
911  O O   . ASP   B 81  ? 1.2784 0.9282 0.7468 0.4484  -0.2617 -0.0743 90  ASP   B O   
912  C CB  . ASP   B 81  ? 1.2314 0.8862 0.7430 0.4350  -0.2604 -0.0828 90  ASP   B CB  
913  C CG  . ASP   B 81  ? 1.2901 0.9596 0.7786 0.4745  -0.2628 -0.0889 90  ASP   B CG  
914  O OD1 . ASP   B 81  ? 1.2920 0.9898 0.7654 0.4891  -0.2430 -0.0790 90  ASP   B OD1 
915  O OD2 . ASP   B 81  ? 1.3325 0.9864 0.8187 0.4913  -0.2845 -0.1031 90  ASP   B OD2 
916  N N   . GLY   B 82  ? 1.2602 0.9727 0.7364 0.4482  -0.2134 -0.0547 91  GLY   B N   
917  C CA  . GLY   B 82  ? 1.2848 1.0078 0.7340 0.4707  -0.2136 -0.0522 91  GLY   B CA  
918  C C   . GLY   B 82  ? 1.3157 1.0426 0.7346 0.5153  -0.2281 -0.0610 91  GLY   B C   
919  O O   . GLY   B 82  ? 1.3286 1.0660 0.7227 0.5386  -0.2302 -0.0601 91  GLY   B O   
920  N N   . LEU   B 83  ? 1.3227 1.0421 0.7419 0.5295  -0.2391 -0.0703 92  LEU   B N   
921  C CA  . LEU   B 83  ? 1.3475 1.0687 0.7358 0.5749  -0.2555 -0.0806 92  LEU   B CA  
922  C C   . LEU   B 83  ? 1.3348 1.0799 0.7238 0.5923  -0.2434 -0.0779 92  LEU   B C   
923  O O   . LEU   B 83  ? 1.3430 1.1113 0.7070 0.6280  -0.2397 -0.0755 92  LEU   B O   
924  C CB  . LEU   B 83  ? 1.3833 1.0602 0.7610 0.5862  -0.2941 -0.1010 92  LEU   B CB  
925  C CG  . LEU   B 83  ? 1.4465 1.0985 0.8067 0.5891  -0.3131 -0.1063 92  LEU   B CG  
926  C CD1 . LEU   B 83  ? 1.4797 1.0838 0.8519 0.5713  -0.3428 -0.1189 92  LEU   B CD1 
927  C CD2 . LEU   B 83  ? 1.4677 1.1270 0.7868 0.6376  -0.3266 -0.1141 92  LEU   B CD2 
928  N N   . SER   B 84  ? 1.3154 1.0543 0.7306 0.5706  -0.2394 -0.0790 93  SER   B N   
929  C CA  . SER   B 84  ? 1.3016 1.0578 0.7163 0.5882  -0.2314 -0.0783 93  SER   B CA  
930  C C   . SER   B 84  ? 1.2632 1.0578 0.6889 0.5795  -0.1957 -0.0577 93  SER   B C   
931  O O   . SER   B 84  ? 1.2522 1.0578 0.6970 0.5490  -0.1759 -0.0449 93  SER   B O   
932  C CB  . SER   B 84  ? 1.3304 1.0637 0.7672 0.5726  -0.2450 -0.0902 93  SER   B CB  
933  O OG  . SER   B 84  ? 1.3787 1.0764 0.8257 0.5549  -0.2699 -0.1023 93  SER   B OG  
934  N N   . GLU   B 85  ? 1.2360 1.0496 0.6499 0.6067  -0.1886 -0.0546 94  GLU   B N   
935  C CA  . GLU   B 85  ? 1.2059 1.0523 0.6315 0.5995  -0.1569 -0.0348 94  GLU   B CA  
936  C C   . GLU   B 85  ? 1.1567 0.9942 0.6165 0.5623  -0.1475 -0.0338 94  GLU   B C   
937  O O   . GLU   B 85  ? 1.1625 0.9735 0.6338 0.5504  -0.1658 -0.0486 94  GLU   B O   
938  C CB  . GLU   B 85  ? 1.2521 1.1197 0.6538 0.6408  -0.1529 -0.0308 94  GLU   B CB  
939  C CG  . GLU   B 85  ? 1.3194 1.2089 0.6893 0.6772  -0.1531 -0.0254 94  GLU   B CG  
940  C CD  . GLU   B 85  ? 1.3979 1.3195 0.7481 0.7131  -0.1389 -0.0129 94  GLU   B CD  
941  O OE1 . GLU   B 85  ? 1.4068 1.3251 0.7588 0.7202  -0.1381 -0.0148 94  GLU   B OE1 
942  O OE2 . GLU   B 85  ? 1.4152 1.3669 0.7485 0.7344  -0.1281 -0.0001 94  GLU   B OE2 
943  N N   . VAL   B 86  ? 1.0994 0.9596 0.5766 0.5438  -0.1198 -0.0161 95  VAL   B N   
944  C CA  . VAL   B 86  ? 1.0467 0.9025 0.5547 0.5101  -0.1084 -0.0138 95  VAL   B CA  
945  C C   . VAL   B 86  ? 1.0155 0.8937 0.5281 0.5154  -0.0861 0.0009  95  VAL   B C   
946  O O   . VAL   B 86  ? 1.0277 0.9282 0.5234 0.5395  -0.0757 0.0132  95  VAL   B O   
947  C CB  . VAL   B 86  ? 1.0208 0.8766 0.5495 0.4732  -0.0978 -0.0071 95  VAL   B CB  
948  C CG1 . VAL   B 86  ? 1.0228 0.8568 0.5440 0.4696  -0.1185 -0.0185 95  VAL   B CG1 
949  C CG2 . VAL   B 86  ? 1.0085 0.8933 0.5380 0.4714  -0.0743 0.0121  95  VAL   B CG2 
950  N N   . GLN   B 87  ? 0.9821 0.8555 0.5179 0.4931  -0.0784 0.0008  96  GLN   B N   
951  C CA  . GLN   B 87  ? 0.9714 0.8617 0.5130 0.4951  -0.0579 0.0151  96  GLN   B CA  
952  C C   . GLN   B 87  ? 0.9522 0.8488 0.5212 0.4595  -0.0384 0.0264  96  GLN   B C   
953  O O   . GLN   B 87  ? 0.9608 0.8440 0.5487 0.4335  -0.0425 0.0176  96  GLN   B O   
954  C CB  . GLN   B 87  ? 0.9833 0.8642 0.5213 0.5107  -0.0664 0.0053  96  GLN   B CB  
955  C CG  . GLN   B 87  ? 1.0428 0.9260 0.5487 0.5541  -0.0796 0.0000  96  GLN   B CG  
956  C CD  . GLN   B 87  ? 1.1259 1.0019 0.6250 0.5741  -0.0881 -0.0094 96  GLN   B CD  
957  O OE1 . GLN   B 87  ? 1.1186 0.9896 0.6368 0.5570  -0.0825 -0.0108 96  GLN   B OE1 
958  N NE2 . GLN   B 87  ? 1.1598 1.0357 0.6299 0.6133  -0.1029 -0.0171 96  GLN   B NE2 
959  N N   . LEU   B 88  ? 0.9295 0.8475 0.5013 0.4592  -0.0179 0.0459  97  LEU   B N   
960  C CA  . LEU   B 88  ? 0.9173 0.8406 0.5147 0.4290  -0.0005 0.0565  97  LEU   B CA  
961  C C   . LEU   B 88  ? 0.9083 0.8284 0.5111 0.4325  0.0057  0.0589  97  LEU   B C   
962  O O   . LEU   B 88  ? 0.9142 0.8451 0.5030 0.4568  0.0121  0.0695  97  LEU   B O   
963  C CB  . LEU   B 88  ? 0.9067 0.8544 0.5077 0.4266  0.0171  0.0770  97  LEU   B CB  
964  C CG  . LEU   B 88  ? 0.9049 0.8572 0.5331 0.3982  0.0344  0.0889  97  LEU   B CG  
965  C CD1 . LEU   B 88  ? 0.8959 0.8331 0.5430 0.3665  0.0297  0.0765  97  LEU   B CD1 
966  C CD2 . LEU   B 88  ? 0.9044 0.8821 0.5387 0.3973  0.0504  0.1101  97  LEU   B CD2 
967  N N   . LEU   B 89  ? 0.8969 0.8029 0.5180 0.4105  0.0036  0.0491  98  LEU   B N   
968  C CA  . LEU   B 89  ? 0.9026 0.8048 0.5294 0.4128  0.0092  0.0505  98  LEU   B CA  
969  C C   . LEU   B 89  ? 0.9110 0.8217 0.5558 0.3924  0.0283  0.0671  98  LEU   B C   
970  O O   . LEU   B 89  ? 0.9128 0.8173 0.5775 0.3659  0.0310  0.0627  98  LEU   B O   
971  C CB  . LEU   B 89  ? 0.8996 0.7852 0.5364 0.4030  -0.0038 0.0310  98  LEU   B CB  
972  C CG  . LEU   B 89  ? 0.9251 0.8056 0.5731 0.3983  0.0015  0.0293  98  LEU   B CG  
973  C CD1 . LEU   B 89  ? 0.9348 0.8209 0.5699 0.4204  0.0113  0.0428  98  LEU   B CD1 
974  C CD2 . LEU   B 89  ? 0.9402 0.8094 0.5924 0.3994  -0.0150 0.0091  98  LEU   B CD2 
975  N N   . ALA   B 90  ? 0.9097 0.8363 0.5476 0.4055  0.0411  0.0869  99  ALA   B N   
976  C CA  . ALA   B 90  ? 0.9031 0.8382 0.5600 0.3864  0.0579  0.1044  99  ALA   B CA  
977  C C   . ALA   B 90  ? 0.9040 0.8286 0.5711 0.3806  0.0642  0.1079  99  ALA   B C   
978  O O   . ALA   B 90  ? 0.8997 0.8205 0.5529 0.4022  0.0629  0.1087  99  ALA   B O   
979  C CB  . ALA   B 90  ? 0.8963 0.8544 0.5460 0.4007  0.0696  0.1262  99  ALA   B CB  
980  N N   . VAL   B 91  ? 0.8909 0.8098 0.5812 0.3527  0.0699  0.1088  100 VAL   B N   
981  C CA  . VAL   B 91  ? 0.8933 0.8005 0.5940 0.3461  0.0754  0.1125  100 VAL   B CA  
982  C C   . VAL   B 91  ? 0.8945 0.8090 0.6136 0.3302  0.0889  0.1331  100 VAL   B C   
983  O O   . VAL   B 91  ? 0.8858 0.7956 0.6242 0.3057  0.0893  0.1292  100 VAL   B O   
984  C CB  . VAL   B 91  ? 0.8856 0.7770 0.5965 0.3304  0.0665  0.0916  100 VAL   B CB  
985  C CG1 . VAL   B 91  ? 0.8846 0.7633 0.6039 0.3265  0.0708  0.0940  100 VAL   B CG1 
986  C CG2 . VAL   B 91  ? 0.8872 0.7742 0.5844 0.3442  0.0524  0.0729  100 VAL   B CG2 
987  N N   . PRO   B 92  ? 0.9014 0.8289 0.6151 0.3446  0.0996  0.1558  101 PRO   B N   
988  C CA  . PRO   B 92  ? 0.8995 0.8360 0.6345 0.3282  0.1119  0.1772  101 PRO   B CA  
989  C C   . PRO   B 92  ? 0.9189 0.8366 0.6701 0.3145  0.1153  0.1826  101 PRO   B C   
990  O O   . PRO   B 92  ? 0.9292 0.8310 0.6703 0.3252  0.1120  0.1763  101 PRO   B O   
991  C CB  . PRO   B 92  ? 0.9075 0.8678 0.6304 0.3506  0.1223  0.2005  101 PRO   B CB  
992  C CG  . PRO   B 92  ? 0.9221 0.8836 0.6141 0.3807  0.1139  0.1886  101 PRO   B CG  
993  C CD  . PRO   B 92  ? 0.9106 0.8472 0.5994 0.3768  0.1009  0.1634  101 PRO   B CD  
994  N N   . PRO   B 93  ? 0.9250 0.8439 0.7016 0.2918  0.1210  0.1943  102 PRO   B N   
995  C CA  . PRO   B 93  ? 0.9386 0.8360 0.7311 0.2787  0.1219  0.1987  102 PRO   B CA  
996  C C   . PRO   B 93  ? 0.9567 0.8488 0.7411 0.2953  0.1301  0.2192  102 PRO   B C   
997  O O   . PRO   B 93  ? 0.9551 0.8664 0.7380 0.3054  0.1411  0.2434  102 PRO   B O   
998  C CB  . PRO   B 93  ? 0.9342 0.8373 0.7560 0.2526  0.1246  0.2076  102 PRO   B CB  
999  C CG  . PRO   B 93  ? 0.9339 0.8561 0.7530 0.2491  0.1212  0.1964  102 PRO   B CG  
1000 C CD  . PRO   B 93  ? 0.9146 0.8528 0.7077 0.2767  0.1245  0.2016  102 PRO   B CD  
1001 N N   . GLY   B 94  ? 0.9669 0.8347 0.7446 0.2999  0.1247  0.2093  103 GLY   B N   
1002 C CA  . GLY   B 94  ? 0.9736 0.8308 0.7406 0.3167  0.1305  0.2255  103 GLY   B CA  
1003 C C   . GLY   B 94  ? 0.9818 0.8527 0.7194 0.3492  0.1337  0.2300  103 GLY   B C   
1004 O O   . GLY   B 94  ? 0.9889 0.8557 0.7149 0.3666  0.1404  0.2470  103 GLY   B O   
1005 N N   . GLU   B 95  ? 0.9842 0.8706 0.7084 0.3589  0.1282  0.2150  104 GLU   B N   
1006 C CA  . GLU   B 95  ? 0.9961 0.8960 0.6915 0.3913  0.1283  0.2164  104 GLU   B CA  
1007 C C   . GLU   B 95  ? 1.0044 0.8956 0.6847 0.4008  0.1127  0.1854  104 GLU   B C   
1008 O O   . GLU   B 95  ? 0.9954 0.8796 0.6881 0.3810  0.1040  0.1656  104 GLU   B O   
1009 C CB  . GLU   B 95  ? 1.0148 0.9450 0.7083 0.3970  0.1356  0.2306  104 GLU   B CB  
1010 C CG  . GLU   B 95  ? 1.0731 1.0178 0.7834 0.3892  0.1521  0.2642  104 GLU   B CG  
1011 C CD  . GLU   B 95  ? 1.1460 1.1241 0.8608 0.3904  0.1601  0.2790  104 GLU   B CD  
1012 O OE1 . GLU   B 95  ? 1.1355 1.1241 0.8383 0.3977  0.1520  0.2620  104 GLU   B OE1 
1013 O OE2 . GLU   B 95  ? 1.1852 1.1795 0.9163 0.3843  0.1742  0.3083  104 GLU   B OE2 
1014 N N   . ARG   B 96  ? 1.0144 0.9070 0.6685 0.4314  0.1087  0.1816  105 ARG   B N   
1015 C CA  . ARG   B 96  ? 1.0351 0.9196 0.6765 0.4419  0.0924  0.1530  105 ARG   B CA  
1016 C C   . ARG   B 96  ? 1.0248 0.9213 0.6643 0.4392  0.0839  0.1397  105 ARG   B C   
1017 O O   . ARG   B 96  ? 1.0229 0.9378 0.6596 0.4428  0.0905  0.1535  105 ARG   B O   
1018 C CB  . ARG   B 96  ? 1.0912 0.9751 0.7044 0.4782  0.0894  0.1535  105 ARG   B CB  
1019 C CG  . ARG   B 96  ? 1.1711 1.0397 0.7775 0.4864  0.0733  0.1260  105 ARG   B CG  
1020 C CD  . ARG   B 96  ? 1.2382 1.1023 0.8191 0.5207  0.0712  0.1277  105 ARG   B CD  
1021 N NE  . ARG   B 96  ? 1.3127 1.1941 0.8692 0.5507  0.0758  0.1424  105 ARG   B NE  
1022 C CZ  . ARG   B 96  ? 1.3766 1.2643 0.9210 0.5671  0.0906  0.1694  105 ARG   B CZ  
1023 N NH1 . ARG   B 96  ? 1.3753 1.2499 0.9306 0.5554  0.1009  0.1845  105 ARG   B NH1 
1024 N NH2 . ARG   B 96  ? 1.3970 1.3042 0.9181 0.5964  0.0947  0.1820  105 ARG   B NH2 
1025 N N   . ALA   B 97  ? 1.0117 0.8985 0.6529 0.4337  0.0689  0.1133  106 ALA   B N   
1026 C CA  . ALA   B 97  ? 1.0024 0.8950 0.6405 0.4323  0.0574  0.0982  106 ALA   B CA  
1027 C C   . ALA   B 97  ? 1.0059 0.9099 0.6170 0.4657  0.0535  0.1018  106 ALA   B C   
1028 O O   . ALA   B 97  ? 0.9964 0.8979 0.5893 0.4921  0.0514  0.1024  106 ALA   B O   
1029 C CB  . ALA   B 97  ? 1.0034 0.8830 0.6469 0.4256  0.0421  0.0722  106 ALA   B CB  
1030 N N   . LYS   B 98  ? 1.0083 0.9251 0.6152 0.4665  0.0522  0.1041  107 LYS   B N   
1031 C CA  . LYS   B 98  ? 1.0310 0.9609 0.6112 0.4996  0.0487  0.1081  107 LYS   B CA  
1032 C C   . LYS   B 98  ? 1.0288 0.9613 0.6046 0.4980  0.0359  0.0948  107 LYS   B C   
1033 O O   . LYS   B 98  ? 1.0302 0.9662 0.6230 0.4726  0.0401  0.0973  107 LYS   B O   
1034 C CB  . LYS   B 98  ? 1.0786 1.0292 0.6567 0.5068  0.0688  0.1382  107 LYS   B CB  
1035 C CG  . LYS   B 98  ? 1.1759 1.1481 0.7273 0.5410  0.0701  0.1483  107 LYS   B CG  
1036 C CD  . LYS   B 98  ? 1.2441 1.2422 0.8044 0.5368  0.0919  0.1798  107 LYS   B CD  
1037 C CE  . LYS   B 98  ? 1.2833 1.2833 0.8747 0.4983  0.0982  0.1838  107 LYS   B CE  
1038 N NZ  . LYS   B 98  ? 1.3095 1.3398 0.9082 0.4979  0.1147  0.2104  107 LYS   B NZ  
1039 N N   . ASN   B 99  ? 1.0207 0.9487 0.5742 0.5248  0.0183  0.0792  108 ASN   B N   
1040 C CA  . ASN   B 99  ? 1.0327 0.9579 0.5794 0.5265  0.0024  0.0647  108 ASN   B CA  
1041 C C   . ASN   B 99  ? 1.0418 0.9885 0.5686 0.5493  0.0075  0.0782  108 ASN   B C   
1042 O O   . ASN   B 99  ? 1.0524 1.0115 0.5572 0.5816  0.0113  0.0876  108 ASN   B O   
1043 C CB  . ASN   B 99  ? 1.0533 0.9612 0.5865 0.5453  -0.0219 0.0403  108 ASN   B CB  
1044 C CG  . ASN   B 99  ? 1.0732 0.9626 0.6277 0.5224  -0.0310 0.0234  108 ASN   B CG  
1045 O OD1 . ASN   B 99  ? 1.0951 0.9818 0.6595 0.5161  -0.0229 0.0263  108 ASN   B OD1 
1046 N ND2 . ASN   B 99  ? 1.0624 0.9390 0.6240 0.5109  -0.0486 0.0058  108 ASN   B ND2 
1047 N N   . ILE   B 100 ? 1.0344 0.9874 0.5676 0.5347  0.0078  0.0796  109 ILE   B N   
1048 C CA  . ILE   B 100 ? 1.0430 1.0192 0.5587 0.5557  0.0124  0.0916  109 ILE   B CA  
1049 C C   . ILE   B 100 ? 1.0570 1.0226 0.5619 0.5596  -0.0080 0.0730  109 ILE   B C   
1050 O O   . ILE   B 100 ? 1.0531 1.0066 0.5759 0.5301  -0.0122 0.0651  109 ILE   B O   
1051 C CB  . ILE   B 100 ? 1.0419 1.0398 0.5780 0.5335  0.0347  0.1147  109 ILE   B CB  
1052 C CG1 . ILE   B 100 ? 1.0528 1.0536 0.6073 0.5198  0.0531  0.1321  109 ILE   B CG1 
1053 C CG2 . ILE   B 100 ? 1.0442 1.0720 0.5636 0.5573  0.0411  0.1291  109 ILE   B CG2 
1054 C CD1 . ILE   B 100 ? 1.0782 1.0930 0.6134 0.5522  0.0622  0.1479  109 ILE   B CD1 
1055 N N   . GLN   B 101 ? 1.0705 1.0395 0.5453 0.5966  -0.0215 0.0659  110 GLN   B N   
1056 C CA  . GLN   B 101 ? 1.0951 1.0500 0.5564 0.6043  -0.0443 0.0471  110 GLN   B CA  
1057 C C   . GLN   B 101 ? 1.1150 1.0920 0.5683 0.6100  -0.0374 0.0581  110 GLN   B C   
1058 O O   . GLN   B 101 ? 1.1221 1.1296 0.5661 0.6288  -0.0210 0.0775  110 GLN   B O   
1059 C CB  . GLN   B 101 ? 1.1302 1.0738 0.5619 0.6437  -0.0666 0.0303  110 GLN   B CB  
1060 C CG  . GLN   B 101 ? 1.1748 1.0936 0.5966 0.6481  -0.0954 0.0069  110 GLN   B CG  
1061 C CD  . GLN   B 101 ? 1.2356 1.1362 0.6381 0.6783  -0.1197 -0.0130 110 GLN   B CD  
1062 O OE1 . GLN   B 101 ? 1.2175 1.1109 0.6287 0.6760  -0.1191 -0.0167 110 GLN   B OE1 
1063 N NE2 . GLN   B 101 ? 1.2725 1.1649 0.6479 0.7085  -0.1427 -0.0272 110 GLN   B NE2 
1064 N N   . THR   B 102 ? 1.1169 1.0799 0.5742 0.5941  -0.0499 0.0467  111 THR   B N   
1065 C CA  . THR   B 102 ? 1.1172 1.0987 0.5668 0.5987  -0.0464 0.0539  111 THR   B CA  
1066 C C   . THR   B 102 ? 1.1406 1.0952 0.5828 0.5938  -0.0706 0.0337  111 THR   B C   
1067 O O   . THR   B 102 ? 1.1642 1.0881 0.6169 0.5760  -0.0851 0.0182  111 THR   B O   
1068 C CB  . THR   B 102 ? 1.1156 1.1171 0.5943 0.5657  -0.0215 0.0735  111 THR   B CB  
1069 O OG1 . THR   B 102 ? 1.1276 1.1551 0.5987 0.5750  -0.0157 0.0833  111 THR   B OG1 
1070 C CG2 . THR   B 102 ? 1.1139 1.0913 0.6202 0.5234  -0.0235 0.0650  111 THR   B CG2 
1071 N N   . LEU   B 103 ? 1.1283 1.0948 0.5534 0.6092  -0.0751 0.0345  112 LEU   B N   
1072 C CA  . LEU   B 103 ? 1.1353 1.0755 0.5537 0.6026  -0.0968 0.0179  112 LEU   B CA  
1073 C C   . LEU   B 103 ? 1.1155 1.0670 0.5560 0.5697  -0.0809 0.0291  112 LEU   B C   
1074 O O   . LEU   B 103 ? 1.0969 1.0816 0.5367 0.5759  -0.0646 0.0447  112 LEU   B O   
1075 C CB  . LEU   B 103 ? 1.1465 1.0887 0.5282 0.6439  -0.1158 0.0086  112 LEU   B CB  
1076 C CG  . LEU   B 103 ? 1.1815 1.0937 0.5577 0.6339  -0.1379 -0.0068 112 LEU   B CG  
1077 C CD1 . LEU   B 103 ? 1.2069 1.0764 0.5799 0.6335  -0.1659 -0.0281 112 LEU   B CD1 
1078 C CD2 . LEU   B 103 ? 1.1979 1.1240 0.5455 0.6644  -0.1457 -0.0080 112 LEU   B CD2 
1079 N N   . PRO   B 104 ? 1.1198 1.0457 0.5799 0.5355  -0.0861 0.0214  113 PRO   B N   
1080 C CA  . PRO   B 104 ? 1.1076 1.0438 0.5878 0.5052  -0.0715 0.0310  113 PRO   B CA  
1081 C C   . PRO   B 104 ? 1.1170 1.0617 0.5804 0.5168  -0.0775 0.0306  113 PRO   B C   
1082 O O   . PRO   B 104 ? 1.1387 1.0643 0.5779 0.5368  -0.0997 0.0170  113 PRO   B O   
1083 C CB  . PRO   B 104 ? 1.1152 1.0200 0.6147 0.4717  -0.0790 0.0209  113 PRO   B CB  
1084 C CG  . PRO   B 104 ? 1.1289 1.0149 0.6275 0.4789  -0.0902 0.0107  113 PRO   B CG  
1085 C CD  . PRO   B 104 ? 1.1238 1.0142 0.5920 0.5216  -0.1029 0.0057  113 PRO   B CD  
1086 N N   . GLY   B 105 ? 1.1010 1.0736 0.5787 0.5036  -0.0584 0.0451  114 GLY   B N   
1087 C CA  . GLY   B 105 ? 1.0979 1.0804 0.5665 0.5067  -0.0612 0.0454  114 GLY   B CA  
1088 C C   . GLY   B 105 ? 1.1075 1.0625 0.5885 0.4745  -0.0678 0.0373  114 GLY   B C   
1089 O O   . GLY   B 105 ? 1.1114 1.0369 0.6014 0.4569  -0.0756 0.0287  114 GLY   B O   
1090 N N   . ILE   B 106 ? 1.1041 1.0707 0.5861 0.4671  -0.0644 0.0406  115 ILE   B N   
1091 C CA  . ILE   B 106 ? 1.1193 1.0620 0.6088 0.4402  -0.0705 0.0339  115 ILE   B CA  
1092 C C   . ILE   B 106 ? 1.0982 1.0654 0.6099 0.4173  -0.0523 0.0446  115 ILE   B C   
1093 O O   . ILE   B 106 ? 1.0994 1.1012 0.6126 0.4284  -0.0414 0.0546  115 ILE   B O   
1094 C CB  . ILE   B 106 ? 1.1621 1.0848 0.6214 0.4597  -0.0932 0.0222  115 ILE   B CB  
1095 C CG1 . ILE   B 106 ? 1.2155 1.1102 0.6518 0.4839  -0.1161 0.0091  115 ILE   B CG1 
1096 C CG2 . ILE   B 106 ? 1.1746 1.0743 0.6379 0.4353  -0.0992 0.0175  115 ILE   B CG2 
1097 C CD1 . ILE   B 106 ? 1.2527 1.1115 0.7015 0.4625  -0.1256 0.0010  115 ILE   B CD1 
1098 N N   . PHE   B 107 ? 1.0794 1.0297 0.6080 0.3867  -0.0500 0.0421  116 PHE   B N   
1099 C CA  . PHE   B 107 ? 1.0605 1.0278 0.6069 0.3659  -0.0376 0.0483  116 PHE   B CA  
1100 C C   . PHE   B 107 ? 1.0761 1.0190 0.6057 0.3629  -0.0528 0.0386  116 PHE   B C   
1101 O O   . PHE   B 107 ? 1.0884 0.9999 0.6176 0.3489  -0.0616 0.0316  116 PHE   B O   
1102 C CB  . PHE   B 107 ? 1.0412 1.0042 0.6161 0.3351  -0.0254 0.0511  116 PHE   B CB  
1103 C CG  . PHE   B 107 ? 1.0256 1.0164 0.6243 0.3291  -0.0068 0.0634  116 PHE   B CG  
1104 C CD1 . PHE   B 107 ? 1.0244 1.0431 0.6199 0.3505  0.0000  0.0736  116 PHE   B CD1 
1105 C CD2 . PHE   B 107 ? 1.0282 1.0162 0.6520 0.3030  0.0032  0.0653  116 PHE   B CD2 
1106 C CE1 . PHE   B 107 ? 1.0176 1.0597 0.6362 0.3439  0.0169  0.0871  116 PHE   B CE1 
1107 C CE2 . PHE   B 107 ? 1.0228 1.0319 0.6686 0.2973  0.0184  0.0768  116 PHE   B CE2 
1108 C CZ  . PHE   B 107 ? 1.0141 1.0494 0.6580 0.3166  0.0253  0.0884  116 PHE   B CZ  
1109 N N   . LYS   B 108 ? 1.0775 1.0344 0.5929 0.3767  -0.0563 0.0388  117 LYS   B N   
1110 C CA  . LYS   B 108 ? 1.0956 1.0285 0.5931 0.3750  -0.0709 0.0304  117 LYS   B CA  
1111 C C   . LYS   B 108 ? 1.0778 1.0177 0.5940 0.3486  -0.0601 0.0335  117 LYS   B C   
1112 O O   . LYS   B 108 ? 1.0667 1.0401 0.5970 0.3468  -0.0474 0.0404  117 LYS   B O   
1113 C CB  . LYS   B 108 ? 1.1416 1.0864 0.6125 0.4051  -0.0811 0.0277  117 LYS   B CB  
1114 C CG  . LYS   B 108 ? 1.2487 1.1920 0.6979 0.4375  -0.0921 0.0241  117 LYS   B CG  
1115 C CD  . LYS   B 108 ? 1.3541 1.3057 0.7730 0.4695  -0.1052 0.0192  117 LYS   B CD  
1116 C CE  . LYS   B 108 ? 1.4442 1.3929 0.8390 0.5043  -0.1179 0.0139  117 LYS   B CE  
1117 N NZ  . LYS   B 108 ? 1.4899 1.4535 0.8547 0.5397  -0.1291 0.0096  117 LYS   B NZ  
1118 N N   . THR   B 109 ? 1.0747 0.9853 0.5925 0.3283  -0.0651 0.0289  118 THR   B N   
1119 C CA  . THR   B 109 ? 1.0653 0.9814 0.5973 0.3056  -0.0562 0.0306  118 THR   B CA  
1120 C C   . THR   B 109 ? 1.0876 0.9787 0.5977 0.3056  -0.0697 0.0250  118 THR   B C   
1121 O O   . THR   B 109 ? 1.1024 0.9662 0.5902 0.3182  -0.0863 0.0201  118 THR   B O   
1122 C CB  . THR   B 109 ? 1.0566 0.9674 0.6136 0.2797  -0.0453 0.0326  118 THR   B CB  
1123 O OG1 . THR   B 109 ? 1.0727 0.9501 0.6224 0.2685  -0.0546 0.0282  118 THR   B OG1 
1124 C CG2 . THR   B 109 ? 1.0462 0.9694 0.6192 0.2818  -0.0365 0.0369  118 THR   B CG2 
1125 N N   . LYS   B 110 ? 1.0882 0.9862 0.6044 0.2915  -0.0637 0.0257  119 LYS   B N   
1126 C CA  . LYS   B 110 ? 1.1124 0.9862 0.6078 0.2902  -0.0750 0.0219  119 LYS   B CA  
1127 C C   . LYS   B 110 ? 1.1425 0.9791 0.6348 0.2758  -0.0821 0.0214  119 LYS   B C   
1128 O O   . LYS   B 110 ? 1.1736 0.9824 0.6452 0.2778  -0.0951 0.0197  119 LYS   B O   
1129 C CB  . LYS   B 110 ? 1.1177 1.0090 0.6216 0.2784  -0.0660 0.0225  119 LYS   B CB  
1130 C CG  . LYS   B 110 ? 1.1471 1.0435 0.6765 0.2536  -0.0525 0.0248  119 LYS   B CG  
1131 C CD  . LYS   B 110 ? 1.2000 1.1086 0.7328 0.2449  -0.0476 0.0231  119 LYS   B CD  
1132 C CE  . LYS   B 110 ? 1.2511 1.1486 0.7934 0.2239  -0.0413 0.0234  119 LYS   B CE  
1133 N NZ  . LYS   B 110 ? 1.2725 1.1886 0.8444 0.2109  -0.0284 0.0245  119 LYS   B NZ  
1134 N N   . ASP   B 111 ? 1.1274 0.9641 0.6409 0.2613  -0.0737 0.0236  120 ASP   B N   
1135 C CA  . ASP   B 111 ? 1.1442 0.9521 0.6601 0.2467  -0.0789 0.0242  120 ASP   B CA  
1136 C C   . ASP   B 111 ? 1.1583 0.9495 0.6724 0.2555  -0.0897 0.0215  120 ASP   B C   
1137 O O   . ASP   B 111 ? 1.1748 0.9498 0.6998 0.2414  -0.0912 0.0224  120 ASP   B O   
1138 C CB  . ASP   B 111 ? 1.1533 0.9726 0.6940 0.2233  -0.0630 0.0274  120 ASP   B CB  
1139 C CG  . ASP   B 111 ? 1.2151 1.0471 0.7565 0.2145  -0.0547 0.0285  120 ASP   B CG  
1140 O OD1 . ASP   B 111 ? 1.2466 1.0638 0.7685 0.2171  -0.0627 0.0286  120 ASP   B OD1 
1141 O OD2 . ASP   B 111 ? 1.2255 1.0811 0.7864 0.2059  -0.0413 0.0288  120 ASP   B OD2 
1142 N N   . GLY   B 112 ? 1.1498 0.9474 0.6515 0.2794  -0.0969 0.0182  121 GLY   B N   
1143 C CA  . GLY   B 112 ? 1.1529 0.9349 0.6501 0.2919  -0.1091 0.0138  121 GLY   B CA  
1144 C C   . GLY   B 112 ? 1.1316 0.9400 0.6365 0.3064  -0.1007 0.0144  121 GLY   B C   
1145 O O   . GLY   B 112 ? 1.1206 0.9599 0.6406 0.3018  -0.0832 0.0198  121 GLY   B O   
1146 N N   . ASP   B 113 ? 1.1248 0.9203 0.6194 0.3245  -0.1141 0.0090  122 ASP   B N   
1147 C CA  . ASP   B 113 ? 1.1133 0.9318 0.6113 0.3418  -0.1074 0.0101  122 ASP   B CA  
1148 C C   . ASP   B 113 ? 1.0945 0.9132 0.6161 0.3265  -0.0988 0.0115  122 ASP   B C   
1149 O O   . ASP   B 113 ? 1.0959 0.8901 0.6249 0.3111  -0.1063 0.0080  122 ASP   B O   
1150 C CB  . ASP   B 113 ? 1.1547 0.9604 0.6266 0.3737  -0.1274 0.0022  122 ASP   B CB  
1151 C CG  . ASP   B 113 ? 1.2542 1.0650 0.6995 0.3974  -0.1365 -0.0002 122 ASP   B CG  
1152 O OD1 . ASP   B 113 ? 1.2663 1.0917 0.7137 0.3887  -0.1273 0.0046  122 ASP   B OD1 
1153 O OD2 . ASP   B 113 ? 1.3107 1.1110 0.7323 0.4261  -0.1541 -0.0079 122 ASP   B OD2 
1154 N N   . ILE   B 114 ? 1.0694 0.9164 0.6028 0.3313  -0.0833 0.0173  123 ILE   B N   
1155 C CA  . ILE   B 114 ? 1.0583 0.9089 0.6121 0.3208  -0.0741 0.0189  123 ILE   B CA  
1156 C C   . ILE   B 114 ? 1.0421 0.9092 0.5884 0.3468  -0.0724 0.0208  123 ILE   B C   
1157 O O   . ILE   B 114 ? 1.0363 0.9284 0.5756 0.3619  -0.0652 0.0272  123 ILE   B O   
1158 C CB  . ILE   B 114 ? 1.0548 0.9261 0.6339 0.2972  -0.0528 0.0269  123 ILE   B CB  
1159 C CG1 . ILE   B 114 ? 1.0760 0.9413 0.6586 0.2769  -0.0512 0.0269  123 ILE   B CG1 
1160 C CG2 . ILE   B 114 ? 1.0525 0.9224 0.6514 0.2849  -0.0454 0.0270  123 ILE   B CG2 
1161 C CD1 . ILE   B 114 ? 1.0804 0.9677 0.6855 0.2578  -0.0324 0.0331  123 ILE   B CD1 
1162 N N   . GLY   B 115 ? 1.0290 0.8859 0.5786 0.3515  -0.0771 0.0165  124 GLY   B N   
1163 C CA  . GLY   B 115 ? 1.0191 0.8921 0.5614 0.3764  -0.0740 0.0193  124 GLY   B CA  
1164 C C   . GLY   B 115 ? 0.9930 0.8972 0.5538 0.3685  -0.0501 0.0329  124 GLY   B C   
1165 O O   . GLY   B 115 ? 0.9718 0.8790 0.5544 0.3416  -0.0382 0.0368  124 GLY   B O   
1166 N N   . ALA   B 116 ? 0.9870 0.9152 0.5391 0.3922  -0.0432 0.0409  125 ALA   B N   
1167 C CA  . ALA   B 116 ? 0.9759 0.9337 0.5467 0.3853  -0.0212 0.0563  125 ALA   B CA  
1168 C C   . ALA   B 116 ? 0.9830 0.9557 0.5461 0.4100  -0.0161 0.0634  125 ALA   B C   
1169 O O   . ALA   B 116 ? 0.9908 0.9654 0.5291 0.4400  -0.0267 0.0598  125 ALA   B O   
1170 C CB  . ALA   B 116 ? 0.9632 0.9462 0.5360 0.3844  -0.0129 0.0652  125 ALA   B CB  
1171 N N   . VAL   B 117 ? 0.9809 0.9638 0.5635 0.3994  -0.0005 0.0736  126 VAL   B N   
1172 C CA  A VAL   B 117 ? 0.9974 0.9946 0.5726 0.4226  0.0061  0.0826  126 VAL   B CA  
1173 C CA  B VAL   B 117 ? 1.0002 0.9967 0.5764 0.4214  0.0064  0.0825  126 VAL   B CA  
1174 C C   . VAL   B 117 ? 0.9993 1.0333 0.5856 0.4253  0.0261  0.1042  126 VAL   B C   
1175 O O   . VAL   B 117 ? 0.9953 1.0381 0.6079 0.3996  0.0394  0.1135  126 VAL   B O   
1176 C CB  A VAL   B 117 ? 1.0045 0.9842 0.5883 0.4162  0.0063  0.0784  126 VAL   B CB  
1177 C CB  B VAL   B 117 ? 1.0118 0.9894 0.6010 0.4085  0.0074  0.0780  126 VAL   B CB  
1178 C CG1 A VAL   B 117 ? 1.0265 0.9770 0.5945 0.4258  -0.0156 0.0588  126 VAL   B CG1 
1179 C CG1 B VAL   B 117 ? 1.0095 1.0048 0.6136 0.4063  0.0264  0.0951  126 VAL   B CG1 
1180 C CG2 A VAL   B 117 ? 0.9993 0.9733 0.6125 0.3812  0.0168  0.0808  126 VAL   B CG2 
1181 C CG2 B VAL   B 117 ? 1.0315 0.9872 0.6008 0.4288  -0.0112 0.0626  126 VAL   B CG2 
1182 N N   . ALA   B 118 ? 1.0115 1.0683 0.5777 0.4575  0.0274  0.1122  127 ALA   B N   
1183 C CA  . ALA   B 118 ? 1.0187 1.1148 0.5962 0.4618  0.0468  0.1350  127 ALA   B CA  
1184 C C   . ALA   B 118 ? 1.0303 1.1351 0.6142 0.4680  0.0601  0.1498  127 ALA   B C   
1185 O O   . ALA   B 118 ? 1.0372 1.1632 0.6041 0.4981  0.0649  0.1605  127 ALA   B O   
1186 C CB  . ALA   B 118 ? 1.0245 1.1468 0.5786 0.4929  0.0434  0.1382  127 ALA   B CB  
1187 N N   . LEU   B 119 ? 1.0276 1.1134 0.6334 0.4416  0.0647  0.1490  128 LEU   B N   
1188 C CA  . LEU   B 119 ? 1.0259 1.1148 0.6401 0.4433  0.0770  0.1628  128 LEU   B CA  
1189 C C   . LEU   B 119 ? 1.0187 1.1130 0.6686 0.4096  0.0911  0.1755  128 LEU   B C   
1190 O O   . LEU   B 119 ? 1.0216 1.1013 0.6868 0.3830  0.0863  0.1645  128 LEU   B O   
1191 C CB  . LEU   B 119 ? 1.0366 1.0934 0.6403 0.4476  0.0656  0.1467  128 LEU   B CB  
1192 C CG  . LEU   B 119 ? 1.0588 1.1066 0.6288 0.4808  0.0482  0.1317  128 LEU   B CG  
1193 C CD1 . LEU   B 119 ? 1.0686 1.0835 0.6349 0.4782  0.0346  0.1131  128 LEU   B CD1 
1194 C CD2 . LEU   B 119 ? 1.0701 1.1451 0.6192 0.5175  0.0558  0.1472  128 LEU   B CD2 
1195 N N   . ASP   B 120 ? 1.0053 1.1213 0.6683 0.4114  0.1079  0.1991  129 ASP   B N   
1196 C CA  . ASP   B 120 ? 0.9942 1.1161 0.6926 0.3809  0.1200  0.2128  129 ASP   B CA  
1197 C C   . ASP   B 120 ? 0.9899 1.0955 0.7015 0.3708  0.1269  0.2207  129 ASP   B C   
1198 O O   . ASP   B 120 ? 0.9916 1.1112 0.7012 0.3853  0.1382  0.2405  129 ASP   B O   
1199 C CB  . ASP   B 120 ? 1.0032 1.1669 0.7144 0.3850  0.1337  0.2366  129 ASP   B CB  
1200 C CG  . ASP   B 120 ? 1.0486 1.2197 0.7985 0.3516  0.1414  0.2465  129 ASP   B CG  
1201 O OD1 . ASP   B 120 ? 1.0640 1.2098 0.8321 0.3282  0.1407  0.2423  129 ASP   B OD1 
1202 O OD2 . ASP   B 120 ? 1.0562 1.2586 0.8184 0.3496  0.1469  0.2572  129 ASP   B OD2 
1203 N N   . TYR   B 121 ? 0.9856 1.0633 0.7116 0.3457  0.1209  0.2066  130 TYR   B N   
1204 C CA  . TYR   B 121 ? 0.9850 1.0432 0.7251 0.3329  0.1250  0.2104  130 TYR   B CA  
1205 C C   . TYR   B 121 ? 0.9669 1.0194 0.7395 0.2993  0.1270  0.2109  130 TYR   B C   
1206 O O   . TYR   B 121 ? 0.9643 1.0178 0.7429 0.2858  0.1207  0.1991  130 TYR   B O   
1207 C CB  . TYR   B 121 ? 1.0051 1.0327 0.7283 0.3380  0.1125  0.1877  130 TYR   B CB  
1208 C CG  . TYR   B 121 ? 1.0327 1.0619 0.7265 0.3712  0.1097  0.1875  130 TYR   B CG  
1209 C CD1 . TYR   B 121 ? 1.0502 1.0753 0.7399 0.3833  0.1165  0.1990  130 TYR   B CD1 
1210 C CD2 . TYR   B 121 ? 1.0543 1.0897 0.7234 0.3928  0.0996  0.1768  130 TYR   B CD2 
1211 C CE1 . TYR   B 121 ? 1.0741 1.1027 0.7353 0.4167  0.1138  0.1991  130 TYR   B CE1 
1212 C CE2 . TYR   B 121 ? 1.0767 1.1147 0.7179 0.4262  0.0956  0.1761  130 TYR   B CE2 
1213 C CZ  . TYR   B 121 ? 1.0966 1.1319 0.7338 0.4384  0.1028  0.1869  130 TYR   B CZ  
1214 O OH  . TYR   B 121 ? 1.1378 1.1747 0.7459 0.4731  0.0978  0.1847  130 TYR   B OH  
1215 N N   . PRO   B 122 ? 0.9536 0.9977 0.7465 0.2863  0.1343  0.2235  131 PRO   B N   
1216 C CA  . PRO   B 122 ? 0.9354 0.9717 0.7592 0.2557  0.1337  0.2224  131 PRO   B CA  
1217 C C   . PRO   B 122 ? 0.9208 0.9333 0.7424 0.2417  0.1208  0.1950  131 PRO   B C   
1218 O O   . PRO   B 122 ? 0.9331 0.9302 0.7334 0.2524  0.1131  0.1784  131 PRO   B O   
1219 C CB  . PRO   B 122 ? 0.9447 0.9691 0.7840 0.2495  0.1408  0.2384  131 PRO   B CB  
1220 C CG  . PRO   B 122 ? 0.9624 0.9795 0.7747 0.2751  0.1422  0.2395  131 PRO   B CG  
1221 C CD  . PRO   B 122 ? 0.9493 0.9892 0.7372 0.2996  0.1423  0.2393  131 PRO   B CD  
1222 N N   . ALA   B 123 ? 0.8887 0.9004 0.7332 0.2183  0.1183  0.1909  132 ALA   B N   
1223 C CA  . ALA   B 123 ? 0.8702 0.8636 0.7146 0.2041  0.1076  0.1673  132 ALA   B CA  
1224 C C   . ALA   B 123 ? 0.8543 0.8199 0.6922 0.2033  0.1023  0.1535  132 ALA   B C   
1225 O O   . ALA   B 123 ? 0.8603 0.8144 0.6873 0.2014  0.0940  0.1339  132 ALA   B O   
1226 C CB  . ALA   B 123 ? 0.8602 0.8578 0.7320 0.1813  0.1063  0.1680  132 ALA   B CB  
1227 N N   . GLY   B 124 ? 0.8284 0.7847 0.6715 0.2065  0.1072  0.1647  133 GLY   B N   
1228 C CA  . GLY   B 124 ? 0.8208 0.7528 0.6563 0.2089  0.1023  0.1521  133 GLY   B CA  
1229 C C   . GLY   B 124 ? 0.8104 0.7392 0.6191 0.2286  0.0979  0.1404  133 GLY   B C   
1230 O O   . GLY   B 124 ? 0.8170 0.7288 0.6195 0.2302  0.0923  0.1264  133 GLY   B O   
1231 N N   . THR   B 125 ? 0.7912 0.7368 0.5843 0.2443  0.0991  0.1451  134 THR   B N   
1232 C CA  . THR   B 125 ? 0.7981 0.7413 0.5661 0.2637  0.0921  0.1334  134 THR   B CA  
1233 C C   . THR   B 125 ? 0.7790 0.7179 0.5425 0.2549  0.0817  0.1135  134 THR   B C   
1234 O O   . THR   B 125 ? 0.7860 0.7187 0.5331 0.2663  0.0732  0.1012  134 THR   B O   
1235 C CB  . THR   B 125 ? 0.8254 0.7883 0.5777 0.2873  0.0971  0.1483  134 THR   B CB  
1236 O OG1 . THR   B 125 ? 0.8415 0.8101 0.6001 0.2933  0.1084  0.1697  134 THR   B OG1 
1237 C CG2 . THR   B 125 ? 0.8448 0.8029 0.5703 0.3113  0.0880  0.1367  134 THR   B CG2 
1238 N N   . SER   B 126 ? 0.7445 0.6864 0.5233 0.2347  0.0819  0.1110  135 SER   B N   
1239 C CA  . SER   B 126 ? 0.7408 0.6791 0.5158 0.2253  0.0736  0.0950  135 SER   B CA  
1240 C C   . SER   B 126 ? 0.7435 0.6654 0.5136 0.2236  0.0663  0.0784  135 SER   B C   
1241 O O   . SER   B 126 ? 0.7481 0.6606 0.5280 0.2169  0.0679  0.0755  135 SER   B O   
1242 C CB  . SER   B 126 ? 0.7341 0.6759 0.5276 0.2043  0.0753  0.0946  135 SER   B CB  
1243 O OG  . SER   B 126 ? 0.7363 0.6969 0.5356 0.2046  0.0803  0.1079  135 SER   B OG  
1244 N N   . GLY   B 127 ? 0.7424 0.6614 0.4986 0.2298  0.0578  0.0681  136 GLY   B N   
1245 C CA  . GLY   B 127 ? 0.7503 0.6574 0.5039 0.2282  0.0502  0.0534  136 GLY   B CA  
1246 C C   . GLY   B 127 ? 0.7646 0.6669 0.5039 0.2485  0.0439  0.0504  136 GLY   B C   
1247 O O   . GLY   B 127 ? 0.7713 0.6658 0.5092 0.2483  0.0356  0.0381  136 GLY   B O   
1248 N N   . SER   B 128 ? 0.7609 0.6696 0.4904 0.2669  0.0476  0.0619  137 SER   B N   
1249 C CA  . SER   B 128 ? 0.7767 0.6819 0.4897 0.2903  0.0409  0.0590  137 SER   B CA  
1250 C C   . SER   B 128 ? 0.7952 0.6955 0.4957 0.2963  0.0269  0.0474  137 SER   B C   
1251 O O   . SER   B 128 ? 0.8043 0.7100 0.4999 0.2944  0.0255  0.0500  137 SER   B O   
1252 C CB  . SER   B 128 ? 0.7887 0.7057 0.4915 0.3097  0.0488  0.0757  137 SER   B CB  
1253 O OG  . SER   B 128 ? 0.8018 0.7188 0.5151 0.3066  0.0596  0.0867  137 SER   B OG  
1254 N N   . PRO   B 129 ? 0.8006 0.6902 0.4974 0.3029  0.0155  0.0344  138 PRO   B N   
1255 C CA  . PRO   B 129 ? 0.8107 0.6924 0.4980 0.3075  -0.0002 0.0235  138 PRO   B CA  
1256 C C   . PRO   B 129 ? 0.8332 0.7164 0.4976 0.3338  -0.0082 0.0254  138 PRO   B C   
1257 O O   . PRO   B 129 ? 0.8351 0.7245 0.4875 0.3561  -0.0050 0.0317  138 PRO   B O   
1258 C CB  . PRO   B 129 ? 0.8147 0.6864 0.5085 0.3073  -0.0101 0.0100  138 PRO   B CB  
1259 C CG  . PRO   B 129 ? 0.8145 0.6894 0.5081 0.3190  -0.0021 0.0146  138 PRO   B CG  
1260 C CD  . PRO   B 129 ? 0.7901 0.6738 0.4922 0.3065  0.0149  0.0286  138 PRO   B CD  
1261 N N   . ILE   B 130 ? 0.8458 0.7222 0.5028 0.3330  -0.0202 0.0190  139 ILE   B N   
1262 C CA  . ILE   B 130 ? 0.8707 0.7448 0.5047 0.3582  -0.0326 0.0165  139 ILE   B CA  
1263 C C   . ILE   B 130 ? 0.8995 0.7539 0.5320 0.3612  -0.0537 -0.0003 139 ILE   B C   
1264 O O   . ILE   B 130 ? 0.8912 0.7360 0.5384 0.3386  -0.0585 -0.0064 139 ILE   B O   
1265 C CB  . ILE   B 130 ? 0.8723 0.7524 0.4996 0.3543  -0.0310 0.0223  139 ILE   B CB  
1266 C CG1 . ILE   B 130 ? 0.8752 0.7766 0.5102 0.3482  -0.0104 0.0389  139 ILE   B CG1 
1267 C CG2 . ILE   B 130 ? 0.8851 0.7619 0.4862 0.3829  -0.0459 0.0179  139 ILE   B CG2 
1268 C CD1 . ILE   B 130 ? 0.8946 0.8019 0.5330 0.3339  -0.0069 0.0429  139 ILE   B CD1 
1269 N N   . LEU   B 131 ? 0.9304 0.7796 0.5466 0.3890  -0.0664 -0.0074 140 LEU   B N   
1270 C CA  . LEU   B 131 ? 0.9642 0.7948 0.5824 0.3926  -0.0883 -0.0242 140 LEU   B CA  
1271 C C   . LEU   B 131 ? 0.9845 0.8012 0.5813 0.4152  -0.1110 -0.0341 140 LEU   B C   
1272 O O   . LEU   B 131 ? 0.9963 0.8210 0.5696 0.4420  -0.1106 -0.0297 140 LEU   B O   
1273 C CB  . LEU   B 131 ? 0.9802 0.8124 0.5995 0.4072  -0.0892 -0.0292 140 LEU   B CB  
1274 C CG  . LEU   B 131 ? 1.0054 0.8519 0.6355 0.3991  -0.0673 -0.0180 140 LEU   B CG  
1275 C CD1 . LEU   B 131 ? 1.0198 0.8663 0.6438 0.4203  -0.0704 -0.0228 140 LEU   B CD1 
1276 C CD2 . LEU   B 131 ? 1.0078 0.8545 0.6645 0.3644  -0.0585 -0.0176 140 LEU   B CD2 
1277 N N   . ASP   B 132 ? 0.9927 0.7887 0.5979 0.4070  -0.1322 -0.0480 141 ASP   B N   
1278 C CA  . ASP   B 132 ? 1.0194 0.7965 0.6058 0.4299  -0.1591 -0.0609 141 ASP   B CA  
1279 C C   . ASP   B 132 ? 1.0507 0.8230 0.6304 0.4560  -0.1739 -0.0736 141 ASP   B C   
1280 O O   . ASP   B 132 ? 1.0384 0.8218 0.6294 0.4536  -0.1625 -0.0718 141 ASP   B O   
1281 C CB  . ASP   B 132 ? 1.0171 0.7718 0.6161 0.4080  -0.1765 -0.0681 141 ASP   B CB  
1282 C CG  . ASP   B 132 ? 1.0512 0.7969 0.6803 0.3842  -0.1843 -0.0756 141 ASP   B CG  
1283 O OD1 . ASP   B 132 ? 1.0316 0.7848 0.6700 0.3894  -0.1825 -0.0803 141 ASP   B OD1 
1284 O OD2 . ASP   B 132 ? 1.0865 0.8186 0.7301 0.3607  -0.1924 -0.0761 141 ASP   B OD2 
1285 N N   . LYS   B 133 ? 1.0847 0.8391 0.6461 0.4812  -0.2009 -0.0878 142 LYS   B N   
1286 C CA  . LYS   B 133 ? 1.1186 0.8666 0.6693 0.5109  -0.2193 -0.1023 142 LYS   B CA  
1287 C C   . LYS   B 133 ? 1.1123 0.8555 0.6918 0.4942  -0.2256 -0.1119 142 LYS   B C   
1288 O O   . LYS   B 133 ? 1.1175 0.8656 0.6909 0.5157  -0.2289 -0.1186 142 LYS   B O   
1289 C CB  . LYS   B 133 ? 1.1836 0.9093 0.7110 0.5384  -0.2508 -0.1178 142 LYS   B CB  
1290 C CG  . LYS   B 133 ? 1.2842 1.0207 0.7774 0.5660  -0.2448 -0.1098 142 LYS   B CG  
1291 C CD  . LYS   B 133 ? 1.3906 1.1065 0.8552 0.6020  -0.2776 -0.1273 142 LYS   B CD  
1292 C CE  . LYS   B 133 ? 1.4661 1.1640 0.9246 0.5933  -0.2899 -0.1286 142 LYS   B CE  
1293 N NZ  . LYS   B 133 ? 1.5246 1.2005 0.9531 0.6309  -0.3236 -0.1469 142 LYS   B NZ  
1294 N N   . CYS   B 134 ? 1.1008 0.8360 0.7109 0.4577  -0.2273 -0.1123 143 CYS   B N   
1295 C CA  . CYS   B 134 ? 1.0892 0.8259 0.7301 0.4397  -0.2304 -0.1195 143 CYS   B CA  
1296 C C   . CYS   B 134 ? 1.0458 0.8057 0.7016 0.4217  -0.2006 -0.1070 143 CYS   B C   
1297 O O   . CYS   B 134 ? 1.0357 0.8006 0.7172 0.4059  -0.2002 -0.1117 143 CYS   B O   
1298 C CB  . CYS   B 134 ? 1.1235 0.8437 0.7922 0.4108  -0.2473 -0.1254 143 CYS   B CB  
1299 S SG  . CYS   B 134 ? 1.2639 0.9532 0.9156 0.4205  -0.2765 -0.1331 143 CYS   B SG  
1300 N N   . GLY   B 135 ? 1.0183 0.7923 0.6593 0.4247  -0.1773 -0.0917 144 GLY   B N   
1301 C CA  . GLY   B 135 ? 0.9948 0.7876 0.6482 0.4095  -0.1509 -0.0801 144 GLY   B CA  
1302 C C   . GLY   B 135 ? 0.9647 0.7621 0.6414 0.3724  -0.1376 -0.0719 144 GLY   B C   
1303 O O   . GLY   B 135 ? 0.9560 0.7668 0.6465 0.3580  -0.1192 -0.0654 144 GLY   B O   
1304 N N   . ARG   B 136 ? 0.9508 0.7368 0.6300 0.3585  -0.1466 -0.0718 145 ARG   B N   
1305 C CA  . ARG   B 136 ? 0.9372 0.7281 0.6359 0.3252  -0.1339 -0.0634 145 ARG   B CA  
1306 C C   . ARG   B 136 ? 0.9093 0.7114 0.5963 0.3217  -0.1128 -0.0489 145 ARG   B C   
1307 O O   . ARG   B 136 ? 0.9075 0.7076 0.5713 0.3405  -0.1147 -0.0455 145 ARG   B O   
1308 C CB  . ARG   B 136 ? 0.9753 0.7484 0.6827 0.3108  -0.1524 -0.0681 145 ARG   B CB  
1309 C CG  . ARG   B 136 ? 1.0441 0.8105 0.7751 0.3032  -0.1701 -0.0798 145 ARG   B CG  
1310 C CD  . ARG   B 136 ? 1.1192 0.8666 0.8610 0.2867  -0.1882 -0.0816 145 ARG   B CD  
1311 N NE  . ARG   B 136 ? 1.2059 0.9310 0.9219 0.3090  -0.2084 -0.0875 145 ARG   B NE  
1312 C CZ  . ARG   B 136 ? 1.2678 0.9757 0.9766 0.3013  -0.2171 -0.0838 145 ARG   B CZ  
1313 N NH1 . ARG   B 136 ? 1.2607 0.9714 0.9861 0.2711  -0.2064 -0.0731 145 ARG   B NH1 
1314 N NH2 . ARG   B 136 ? 1.3033 0.9914 0.9862 0.3255  -0.2365 -0.0909 145 ARG   B NH2 
1315 N N   . VAL   B 137 ? 0.8755 0.6904 0.5792 0.2980  -0.0937 -0.0409 146 VAL   B N   
1316 C CA  . VAL   B 137 ? 0.8582 0.6837 0.5546 0.2928  -0.0754 -0.0282 146 VAL   B CA  
1317 C C   . VAL   B 137 ? 0.8549 0.6729 0.5459 0.2819  -0.0793 -0.0247 146 VAL   B C   
1318 O O   . VAL   B 137 ? 0.8419 0.6562 0.5476 0.2595  -0.0805 -0.0251 146 VAL   B O   
1319 C CB  . VAL   B 137 ? 0.8475 0.6876 0.5605 0.2755  -0.0555 -0.0223 146 VAL   B CB  
1320 C CG1 . VAL   B 137 ? 0.8439 0.6935 0.5514 0.2701  -0.0394 -0.0101 146 VAL   B CG1 
1321 C CG2 . VAL   B 137 ? 0.8534 0.6987 0.5679 0.2893  -0.0521 -0.0251 146 VAL   B CG2 
1322 N N   . ILE   B 138 ? 0.8494 0.6669 0.5189 0.2989  -0.0806 -0.0205 147 ILE   B N   
1323 C CA  . ILE   B 138 ? 0.8490 0.6595 0.5096 0.2928  -0.0847 -0.0174 147 ILE   B CA  
1324 C C   . ILE   B 138 ? 0.8373 0.6637 0.5001 0.2800  -0.0649 -0.0058 147 ILE   B C   
1325 O O   . ILE   B 138 ? 0.8477 0.6701 0.5035 0.2741  -0.0669 -0.0030 147 ILE   B O   
1326 C CB  . ILE   B 138 ? 0.8617 0.6619 0.4960 0.3208  -0.1012 -0.0217 147 ILE   B CB  
1327 C CG1 . ILE   B 138 ? 0.8762 0.6944 0.4949 0.3444  -0.0900 -0.0146 147 ILE   B CG1 
1328 C CG2 . ILE   B 138 ? 0.8674 0.6473 0.5001 0.3318  -0.1256 -0.0354 147 ILE   B CG2 
1329 C CD1 . ILE   B 138 ? 0.9162 0.7308 0.5069 0.3736  -0.1027 -0.0169 147 ILE   B CD1 
1330 N N   . GLY   B 139 ? 0.8131 0.6556 0.4855 0.2764  -0.0477 0.0003  148 GLY   B N   
1331 C CA  . GLY   B 139 ? 0.8063 0.6628 0.4841 0.2638  -0.0310 0.0101  148 GLY   B CA  
1332 C C   . GLY   B 139 ? 0.8029 0.6741 0.4874 0.2671  -0.0156 0.0175  148 GLY   B C   
1333 O O   . GLY   B 139 ? 0.8184 0.6896 0.5001 0.2820  -0.0169 0.0161  148 GLY   B O   
1334 N N   . LEU   B 140 ? 0.7848 0.6679 0.4779 0.2544  -0.0019 0.0256  149 LEU   B N   
1335 C CA  . LEU   B 140 ? 0.7846 0.6794 0.4869 0.2546  0.0121  0.0341  149 LEU   B CA  
1336 C C   . LEU   B 140 ? 0.7995 0.7092 0.4971 0.2615  0.0201  0.0463  149 LEU   B C   
1337 O O   . LEU   B 140 ? 0.8006 0.7139 0.4944 0.2567  0.0186  0.0474  149 LEU   B O   
1338 C CB  . LEU   B 140 ? 0.7762 0.6720 0.4979 0.2322  0.0203  0.0324  149 LEU   B CB  
1339 C CG  . LEU   B 140 ? 0.7936 0.6807 0.5240 0.2225  0.0151  0.0216  149 LEU   B CG  
1340 C CD1 . LEU   B 140 ? 0.7998 0.6914 0.5467 0.2044  0.0244  0.0206  149 LEU   B CD1 
1341 C CD2 . LEU   B 140 ? 0.7991 0.6809 0.5264 0.2378  0.0092  0.0168  149 LEU   B CD2 
1342 N N   . TYR   B 141 ? 0.8091 0.7286 0.5078 0.2726  0.0288  0.0563  150 TYR   B N   
1343 C CA  . TYR   B 141 ? 0.8245 0.7627 0.5221 0.2804  0.0381  0.0710  150 TYR   B CA  
1344 C C   . TYR   B 141 ? 0.8188 0.7652 0.5384 0.2595  0.0497  0.0786  150 TYR   B C   
1345 O O   . TYR   B 141 ? 0.8258 0.7639 0.5587 0.2473  0.0528  0.0757  150 TYR   B O   
1346 C CB  . TYR   B 141 ? 0.8414 0.7860 0.5304 0.3030  0.0423  0.0800  150 TYR   B CB  
1347 C CG  . TYR   B 141 ? 0.8598 0.8274 0.5515 0.3105  0.0547  0.0989  150 TYR   B CG  
1348 C CD1 . TYR   B 141 ? 0.8660 0.8406 0.5778 0.2983  0.0677  0.1119  150 TYR   B CD1 
1349 C CD2 . TYR   B 141 ? 0.8773 0.8605 0.5524 0.3303  0.0529  0.1044  150 TYR   B CD2 
1350 C CE1 . TYR   B 141 ? 0.8759 0.8735 0.5946 0.3027  0.0794  0.1314  150 TYR   B CE1 
1351 C CE2 . TYR   B 141 ? 0.8770 0.8863 0.5566 0.3376  0.0655  0.1235  150 TYR   B CE2 
1352 C CZ  . TYR   B 141 ? 0.8864 0.9036 0.5893 0.3230  0.0791  0.1380  150 TYR   B CZ  
1353 O OH  . TYR   B 141 ? 0.8982 0.9430 0.6095 0.3281  0.0918  0.1590  150 TYR   B OH  
1354 N N   . GLY   B 142 ? 0.8007 0.7641 0.5247 0.2575  0.0553  0.0884  151 GLY   B N   
1355 C CA  . GLY   B 142 ? 0.7954 0.7668 0.5425 0.2388  0.0646  0.0960  151 GLY   B CA  
1356 C C   . GLY   B 142 ? 0.7937 0.7733 0.5487 0.2248  0.0640  0.0942  151 GLY   B C   
1357 O O   . GLY   B 142 ? 0.7922 0.7813 0.5676 0.2119  0.0706  0.1016  151 GLY   B O   
1358 N N   . ASN   B 143 ? 0.7855 0.7605 0.5254 0.2270  0.0550  0.0844  152 ASN   B N   
1359 C CA  . ASN   B 143 ? 0.7854 0.7686 0.5301 0.2162  0.0541  0.0828  152 ASN   B CA  
1360 C C   . ASN   B 143 ? 0.8020 0.7994 0.5305 0.2335  0.0510  0.0873  152 ASN   B C   
1361 O O   . ASN   B 143 ? 0.8069 0.7934 0.5141 0.2448  0.0411  0.0794  152 ASN   B O   
1362 C CB  . ASN   B 143 ? 0.7856 0.7520 0.5268 0.2027  0.0469  0.0686  152 ASN   B CB  
1363 C CG  . ASN   B 143 ? 0.8069 0.7814 0.5555 0.1903  0.0470  0.0668  152 ASN   B CG  
1364 O OD1 . ASN   B 143 ? 0.7994 0.7900 0.5648 0.1850  0.0531  0.0745  152 ASN   B OD1 
1365 N ND2 . ASN   B 143 ? 0.8077 0.7716 0.5448 0.1855  0.0399  0.0572  152 ASN   B ND2 
1366 N N   . GLY   B 144 ? 0.8049 0.8267 0.5446 0.2354  0.0587  0.0998  153 GLY   B N   
1367 C CA  . GLY   B 144 ? 0.8405 0.8809 0.5656 0.2541  0.0570  0.1050  153 GLY   B CA  
1368 C C   . GLY   B 144 ? 0.8564 0.9258 0.5982 0.2497  0.0639  0.1157  153 GLY   B C   
1369 O O   . GLY   B 144 ? 0.8526 0.9232 0.6132 0.2299  0.0649  0.1130  153 GLY   B O   
1370 N N   . VAL   B 145 ? 0.8674 0.9622 0.6024 0.2697  0.0682  0.1276  154 VAL   B N   
1371 C CA  . VAL   B 145 ? 0.8755 1.0033 0.6258 0.2686  0.0743  0.1385  154 VAL   B CA  
1372 C C   . VAL   B 145 ? 0.8895 1.0493 0.6488 0.2825  0.0870  0.1601  154 VAL   B C   
1373 O O   . VAL   B 145 ? 0.8943 1.0505 0.6390 0.2997  0.0892  0.1648  154 VAL   B O   
1374 C CB  . VAL   B 145 ? 0.8922 1.0219 0.6191 0.2810  0.0635  0.1278  154 VAL   B CB  
1375 C CG1 . VAL   B 145 ? 0.8943 1.0407 0.5964 0.3124  0.0619  0.1330  154 VAL   B CG1 
1376 C CG2 . VAL   B 145 ? 0.8948 1.0424 0.6396 0.2671  0.0641  0.1276  154 VAL   B CG2 
1377 N N   . VAL   B 146 ? 0.8920 1.0841 0.6768 0.2748  0.0953  0.1736  155 VAL   B N   
1378 C CA  . VAL   B 146 ? 0.9125 1.1409 0.7094 0.2864  0.1086  0.1970  155 VAL   B CA  
1379 C C   . VAL   B 146 ? 0.9435 1.2023 0.7228 0.3097  0.1067  0.1985  155 VAL   B C   
1380 O O   . VAL   B 146 ? 0.9428 1.2092 0.7263 0.3028  0.1007  0.1903  155 VAL   B O   
1381 C CB  . VAL   B 146 ? 0.9046 1.1501 0.7458 0.2609  0.1186  0.2127  155 VAL   B CB  
1382 C CG1 . VAL   B 146 ? 0.8948 1.1877 0.7527 0.2714  0.1324  0.2388  155 VAL   B CG1 
1383 C CG2 . VAL   B 146 ? 0.9156 1.1322 0.7700 0.2446  0.1211  0.2140  155 VAL   B CG2 
1384 N N   . ILE   B 147 ? 0.9704 1.2456 0.7273 0.3395  0.1103  0.2073  156 ILE   B N   
1385 C CA  . ILE   B 147 ? 0.9942 1.2986 0.7306 0.3659  0.1074  0.2076  156 ILE   B CA  
1386 C C   . ILE   B 147 ? 0.9935 1.3537 0.7569 0.3689  0.1233  0.2331  156 ILE   B C   
1387 O O   . ILE   B 147 ? 0.9787 1.3497 0.7784 0.3467  0.1350  0.2494  156 ILE   B O   
1388 C CB  . ILE   B 147 ? 1.0199 1.3094 0.7132 0.3994  0.0985  0.1988  156 ILE   B CB  
1389 C CG1 . ILE   B 147 ? 1.0307 1.3277 0.7225 0.4128  0.1098  0.2151  156 ILE   B CG1 
1390 C CG2 . ILE   B 147 ? 1.0478 1.2858 0.7210 0.3919  0.0811  0.1736  156 ILE   B CG2 
1391 C CD1 . ILE   B 147 ? 1.0607 1.3492 0.7102 0.4501  0.1005  0.2069  156 ILE   B CD1 
1392 N N   . LYS   B 148 ? 1.0082 1.4040 0.7561 0.3945  0.1228  0.2360  157 LYS   B N   
1393 C CA  . LYS   B 148 ? 1.0023 1.4568 0.7756 0.3992  0.1376  0.2598  157 LYS   B CA  
1394 C C   . LYS   B 148 ? 0.9956 1.4746 0.7902 0.3991  0.1566  0.2885  157 LYS   B C   
1395 O O   . LYS   B 148 ? 0.9725 1.4830 0.8094 0.3792  0.1694  0.3093  157 LYS   B O   
1396 C CB  . LYS   B 148 ? 1.0451 1.5312 0.7881 0.4354  0.1330  0.2567  157 LYS   B CB  
1397 C CG  . LYS   B 148 ? 1.0880 1.6420 0.8551 0.4451  0.1492  0.2825  157 LYS   B CG  
1398 C CD  . LYS   B 148 ? 1.1600 1.7441 0.9019 0.4749  0.1415  0.2740  157 LYS   B CD  
1399 C CE  . LYS   B 148 ? 1.2219 1.7890 0.9673 0.4580  0.1269  0.2527  157 LYS   B CE  
1400 N NZ  . LYS   B 148 ? 1.2194 1.8373 1.0054 0.4439  0.1357  0.2659  157 LYS   B NZ  
1401 N N   . ASN   B 149 ? 1.0112 1.4746 0.7777 0.4208  0.1577  0.2901  158 ASN   B N   
1402 C CA  . ASN   B 149 ? 1.0084 1.4926 0.7893 0.4245  0.1756  0.3177  158 ASN   B CA  
1403 C C   . ASN   B 149 ? 0.9963 1.4486 0.8072 0.3903  0.1800  0.3231  158 ASN   B C   
1404 O O   . ASN   B 149 ? 0.9970 1.4579 0.8174 0.3925  0.1936  0.3452  158 ASN   B O   
1405 C CB  . ASN   B 149 ? 1.0667 1.5503 0.8034 0.4655  0.1747  0.3175  158 ASN   B CB  
1406 C CG  . ASN   B 149 ? 1.1723 1.6007 0.8721 0.4738  0.1548  0.2872  158 ASN   B CG  
1407 O OD1 . ASN   B 149 ? 1.2175 1.6421 0.8774 0.5064  0.1429  0.2729  158 ASN   B OD1 
1408 N ND2 . ASN   B 149 ? 1.1844 1.5694 0.8975 0.4449  0.1501  0.2770  158 ASN   B ND2 
1409 N N   . GLY   B 150 ? 0.9796 1.3955 0.8029 0.3615  0.1684  0.3032  159 GLY   B N   
1410 C CA  . GLY   B 150 ? 0.9603 1.3454 0.8110 0.3300  0.1701  0.3049  159 GLY   B CA  
1411 C C   . GLY   B 150 ? 0.9542 1.2926 0.7807 0.3338  0.1636  0.2916  159 GLY   B C   
1412 O O   . GLY   B 150 ? 0.9619 1.2726 0.8082 0.3095  0.1636  0.2906  159 GLY   B O   
1413 N N   . SER   B 151 ? 0.9359 1.2652 0.7202 0.3650  0.1568  0.2805  160 SER   B N   
1414 C CA  A SER   B 151 ? 0.9444 1.2312 0.7049 0.3710  0.1488  0.2660  160 SER   B CA  
1415 C CA  B SER   B 151 ? 0.9409 1.2274 0.7031 0.3696  0.1492  0.2665  160 SER   B CA  
1416 C C   . SER   B 151 ? 0.9399 1.1852 0.6946 0.3529  0.1320  0.2371  160 SER   B C   
1417 O O   . SER   B 151 ? 0.9340 1.1839 0.6920 0.3446  0.1252  0.2270  160 SER   B O   
1418 C CB  A SER   B 151 ? 0.9724 1.2657 0.6919 0.4115  0.1455  0.2638  160 SER   B CB  
1419 C CB  B SER   B 151 ? 0.9598 1.2524 0.6826 0.4094  0.1474  0.2664  160 SER   B CB  
1420 O OG  A SER   B 151 ? 1.0238 1.2756 0.7183 0.4189  0.1332  0.2445  160 SER   B OG  
1421 O OG  B SER   B 151 ? 0.9811 1.2771 0.6757 0.4298  0.1345  0.2497  160 SER   B OG  
1422 N N   . TYR   B 152 ? 0.9290 1.1357 0.6743 0.3481  0.1255  0.2245  161 TYR   B N   
1423 C CA  . TYR   B 152 ? 0.9269 1.0959 0.6670 0.3315  0.1111  0.1993  161 TYR   B CA  
1424 C C   . TYR   B 152 ? 0.9256 1.0743 0.6287 0.3537  0.0963  0.1803  161 TYR   B C   
1425 O O   . TYR   B 152 ? 0.9448 1.0902 0.6278 0.3768  0.0956  0.1820  161 TYR   B O   
1426 C CB  . TYR   B 152 ? 0.9284 1.0683 0.6844 0.3106  0.1125  0.1965  161 TYR   B CB  
1427 C CG  . TYR   B 152 ? 0.9354 1.0496 0.7018 0.2846  0.1033  0.1778  161 TYR   B CG  
1428 C CD1 . TYR   B 152 ? 0.9299 1.0548 0.7220 0.2628  0.1052  0.1798  161 TYR   B CD1 
1429 C CD2 . TYR   B 152 ? 0.9583 1.0392 0.7101 0.2824  0.0928  0.1588  161 TYR   B CD2 
1430 C CE1 . TYR   B 152 ? 0.9440 1.0468 0.7431 0.2418  0.0969  0.1628  161 TYR   B CE1 
1431 C CE2 . TYR   B 152 ? 0.9677 1.0286 0.7280 0.2603  0.0857  0.1434  161 TYR   B CE2 
1432 C CZ  . TYR   B 152 ? 0.9683 1.0398 0.7510 0.2408  0.0881  0.1454  161 TYR   B CZ  
1433 O OH  . TYR   B 152 ? 0.9928 1.0461 0.7823 0.2213  0.0814  0.1304  161 TYR   B OH  
1434 N N   . VAL   B 153 ? 0.9011 1.0338 0.5959 0.3462  0.0836  0.1621  162 VAL   B N   
1435 C CA  . VAL   B 153 ? 0.8977 1.0050 0.5617 0.3617  0.0670  0.1429  162 VAL   B CA  
1436 C C   . VAL   B 153 ? 0.8709 0.9446 0.5426 0.3357  0.0585  0.1262  162 VAL   B C   
1437 O O   . VAL   B 153 ? 0.8586 0.9332 0.5442 0.3159  0.0587  0.1231  162 VAL   B O   
1438 C CB  . VAL   B 153 ? 0.9132 1.0349 0.5540 0.3839  0.0585  0.1387  162 VAL   B CB  
1439 C CG1 . VAL   B 153 ? 0.9335 1.0221 0.5457 0.3952  0.0385  0.1178  162 VAL   B CG1 
1440 C CG2 . VAL   B 153 ? 0.9200 1.0771 0.5504 0.4138  0.0673  0.1553  162 VAL   B CG2 
1441 N N   . SER   B 154 ? 0.8601 0.9067 0.5241 0.3361  0.0519  0.1163  163 SER   B N   
1442 C CA  . SER   B 154 ? 0.8495 0.8684 0.5225 0.3124  0.0459  0.1026  163 SER   B CA  
1443 C C   . SER   B 154 ? 0.8552 0.8503 0.5076 0.3169  0.0288  0.0856  163 SER   B C   
1444 O O   . SER   B 154 ? 0.8768 0.8654 0.5076 0.3396  0.0191  0.0809  163 SER   B O   
1445 C CB  . SER   B 154 ? 0.8534 0.8590 0.5348 0.3078  0.0498  0.1028  163 SER   B CB  
1446 O OG  . SER   B 154 ? 0.8918 0.8727 0.5790 0.2894  0.0432  0.0889  163 SER   B OG  
1447 N N   . ALA   B 155 ? 0.8405 0.8202 0.5004 0.2952  0.0245  0.0763  164 ALA   B N   
1448 C CA  . ALA   B 155 ? 0.8431 0.7976 0.4872 0.2956  0.0088  0.0622  164 ALA   B CA  
1449 C C   . ALA   B 155 ? 0.8469 0.7826 0.4908 0.2971  0.0035  0.0552  164 ALA   B C   
1450 O O   . ALA   B 155 ? 0.8390 0.7786 0.4972 0.2915  0.0129  0.0597  164 ALA   B O   
1451 C CB  . ALA   B 155 ? 0.8432 0.7891 0.4975 0.2710  0.0085  0.0568  164 ALA   B CB  
1452 N N   . ILE   B 156 ? 0.8584 0.7729 0.4870 0.3046  -0.0128 0.0442  165 ILE   B N   
1453 C CA  . ILE   B 156 ? 0.8579 0.7540 0.4903 0.3018  -0.0199 0.0357  165 ILE   B CA  
1454 C C   . ILE   B 156 ? 0.8419 0.7265 0.4880 0.2739  -0.0200 0.0309  165 ILE   B C   
1455 O O   . ILE   B 156 ? 0.8474 0.7180 0.4846 0.2704  -0.0312 0.0256  165 ILE   B O   
1456 C CB  . ILE   B 156 ? 0.8791 0.7574 0.4912 0.3226  -0.0396 0.0257  165 ILE   B CB  
1457 C CG1 . ILE   B 156 ? 0.9086 0.8007 0.5020 0.3546  -0.0401 0.0302  165 ILE   B CG1 
1458 C CG2 . ILE   B 156 ? 0.8837 0.7452 0.5062 0.3149  -0.0466 0.0169  165 ILE   B CG2 
1459 C CD1 . ILE   B 156 ? 0.9483 0.8224 0.5195 0.3795  -0.0619 0.0184  165 ILE   B CD1 
1460 N N   . THR   B 157 ? 0.8177 0.7093 0.4841 0.2554  -0.0073 0.0338  166 THR   B N   
1461 C CA  . THR   B 157 ? 0.7990 0.6843 0.4770 0.2318  -0.0056 0.0302  166 THR   B CA  
1462 C C   . THR   B 157 ? 0.7851 0.6567 0.4710 0.2230  -0.0117 0.0224  166 THR   B C   
1463 O O   . THR   B 157 ? 0.7655 0.6401 0.4622 0.2224  -0.0066 0.0215  166 THR   B O   
1464 C CB  . THR   B 157 ? 0.7859 0.6858 0.4806 0.2171  0.0091  0.0355  166 THR   B CB  
1465 O OG1 . THR   B 157 ? 0.7762 0.6918 0.4682 0.2232  0.0147  0.0435  166 THR   B OG1 
1466 C CG2 . THR   B 157 ? 0.7829 0.6784 0.4862 0.1964  0.0106  0.0312  166 THR   B CG2 
1467 N N   . GLN   B 158 ? 0.7850 0.6422 0.4667 0.2157  -0.0222 0.0179  167 GLN   B N   
1468 C CA  . GLN   B 158 ? 0.7945 0.6406 0.4863 0.2057  -0.0291 0.0120  167 GLN   B CA  
1469 C C   . GLN   B 158 ? 0.8144 0.6607 0.5156 0.1831  -0.0244 0.0133  167 GLN   B C   
1470 O O   . GLN   B 158 ? 0.8090 0.6537 0.5013 0.1793  -0.0244 0.0166  167 GLN   B O   
1471 C CB  . GLN   B 158 ? 0.8029 0.6299 0.4825 0.2180  -0.0486 0.0064  167 GLN   B CB  
1472 C CG  . GLN   B 158 ? 0.8143 0.6302 0.5075 0.2091  -0.0584 0.0003  167 GLN   B CG  
1473 C CD  . GLN   B 158 ? 0.8129 0.6392 0.5213 0.2095  -0.0517 -0.0029 167 GLN   B CD  
1474 O OE1 . GLN   B 158 ? 0.8024 0.6432 0.5226 0.1987  -0.0365 0.0001  167 GLN   B OE1 
1475 N NE2 . GLN   B 158 ? 0.7707 0.5887 0.4788 0.2224  -0.0644 -0.0101 167 GLN   B NE2 
1476 N N   . GLY   B 159 ? 0.8336 0.6837 0.5517 0.1705  -0.0204 0.0110  168 GLY   B N   
1477 C CA  . GLY   B 159 ? 0.8726 0.7259 0.5994 0.1514  -0.0155 0.0130  168 GLY   B CA  
1478 C C   . GLY   B 159 ? 0.9232 0.7625 0.6521 0.1441  -0.0278 0.0130  168 GLY   B C   
1479 O O   . GLY   B 159 ? 0.9373 0.7613 0.6599 0.1541  -0.0425 0.0099  168 GLY   B O   
1480 N N   . LYS   B 160 ? 0.9572 0.8015 0.6951 0.1271  -0.0227 0.0169  169 LYS   B N   
1481 C CA  . LYS   B 160 ? 0.9964 0.8289 0.7399 0.1165  -0.0329 0.0202  169 LYS   B CA  
1482 C C   . LYS   B 160 ? 1.0145 0.8602 0.7817 0.1056  -0.0289 0.0191  169 LYS   B C   
1483 O O   . LYS   B 160 ? 1.0139 0.8795 0.7895 0.0999  -0.0145 0.0193  169 LYS   B O   
1484 C CB  . LYS   B 160 ? 1.0344 0.8646 0.7696 0.1053  -0.0291 0.0284  169 LYS   B CB  
1485 C CG  . LYS   B 160 ? 1.1075 0.9375 0.8226 0.1138  -0.0249 0.0291  169 LYS   B CG  
1486 C CD  . LYS   B 160 ? 1.1733 0.9846 0.8701 0.1296  -0.0390 0.0266  169 LYS   B CD  
1487 C CE  . LYS   B 160 ? 1.2281 1.0464 0.9095 0.1400  -0.0333 0.0265  169 LYS   B CE  
1488 N NZ  . LYS   B 160 ? 1.2567 1.0923 0.9453 0.1475  -0.0234 0.0232  169 LYS   B NZ  
1489 N N   . ARG   B 161 ? 1.0276 0.8633 0.8063 0.1033  -0.0424 0.0174  170 ARG   B N   
1490 C CA  . ARG   B 161 ? 1.0337 0.8845 0.8378 0.0926  -0.0398 0.0167  170 ARG   B CA  
1491 C C   . ARG   B 161 ? 1.0581 0.9108 0.8732 0.0728  -0.0391 0.0278  170 ARG   B C   
1492 O O   . ARG   B 161 ? 1.0692 0.9005 0.8792 0.0690  -0.0522 0.0326  170 ARG   B O   
1493 C CB  . ARG   B 161 ? 1.0386 0.8796 0.8520 0.1015  -0.0558 0.0080  170 ARG   B CB  
1494 C CG  . ARG   B 161 ? 1.0440 0.9044 0.8840 0.0942  -0.0527 0.0048  170 ARG   B CG  
1495 C CD  . ARG   B 161 ? 1.0694 0.9182 0.9198 0.1017  -0.0718 -0.0039 170 ARG   B CD  
1496 N NE  . ARG   B 161 ? 1.0821 0.9494 0.9628 0.0898  -0.0718 -0.0048 170 ARG   B NE  
1497 C CZ  . ARG   B 161 ? 1.0918 0.9738 0.9833 0.0981  -0.0698 -0.0140 170 ARG   B CZ  
1498 N NH1 . ARG   B 161 ? 1.0751 0.9532 0.9489 0.1180  -0.0675 -0.0219 170 ARG   B NH1 
1499 N NH2 . ARG   B 161 ? 1.0756 0.9770 0.9959 0.0869  -0.0700 -0.0145 170 ARG   B NH2 
1500 N N   . GLU   B 162 ? 1.0650 0.9431 0.8933 0.0614  -0.0236 0.0327  171 GLU   B N   
1501 C CA  . GLU   B 162 ? 1.0829 0.9683 0.9219 0.0432  -0.0197 0.0457  171 GLU   B CA  
1502 C C   . GLU   B 162 ? 1.0870 0.9759 0.9548 0.0317  -0.0293 0.0483  171 GLU   B C   
1503 O O   . GLU   B 162 ? 1.0947 0.9785 0.9725 0.0166  -0.0339 0.0605  171 GLU   B O   
1504 C CB  . GLU   B 162 ? 1.1131 1.0274 0.9530 0.0388  0.0007  0.0494  171 GLU   B CB  
1505 C CG  . GLU   B 162 ? 1.2053 1.1176 1.0208 0.0494  0.0089  0.0454  171 GLU   B CG  
1506 C CD  . GLU   B 162 ? 1.3353 1.2343 1.1317 0.0461  0.0084  0.0544  171 GLU   B CD  
1507 O OE1 . GLU   B 162 ? 1.3617 1.2526 1.1381 0.0563  0.0094  0.0500  171 GLU   B OE1 
1508 O OE2 . GLU   B 162 ? 1.3764 1.2735 1.1786 0.0334  0.0069  0.0664  171 GLU   B OE2 
1509 N N1  . A1BGV C .   ? 0.8795 1.0255 0.7141 0.2672  0.1427  0.2451  301 A1BGV B N1  
1510 N N3  . A1BGV C .   ? 0.8531 0.8634 0.6808 0.1808  0.0818  0.1185  301 A1BGV B N3  
1511 C C4  . A1BGV C .   ? 0.8737 0.9906 0.7049 0.2531  0.1304  0.2207  301 A1BGV B C4  
1512 C C5  . A1BGV C .   ? 0.8751 0.9433 0.6913 0.2404  0.1129  0.1846  301 A1BGV B C5  
1513 C C6  . A1BGV C .   ? 0.8811 0.9206 0.6835 0.2376  0.1028  0.1634  301 A1BGV B C6  
1514 C C7  . A1BGV C .   ? 0.8766 0.9037 0.6889 0.2175  0.0960  0.1486  301 A1BGV B C7  
1515 C C8  . A1BGV C .   ? 0.8615 0.9010 0.6973 0.2000  0.0976  0.1527  301 A1BGV B C8  
1516 C C10 . A1BGV C .   ? 0.8500 0.8514 0.6835 0.1652  0.0756  0.1044  301 A1BGV B C10 
1517 C C13 . A1BGV C .   ? 0.8566 0.8405 0.6780 0.1420  0.0583  0.0669  301 A1BGV B C13 
1518 C C15 . A1BGV C .   ? 0.8546 0.9214 0.7066 0.2013  0.1064  0.1728  301 A1BGV B C15 
1519 C C1  . A1BGV C .   ? 0.8706 1.0628 0.7662 0.2394  0.1585  0.2806  301 A1BGV B C1  
1520 C C2  . A1BGV C .   ? 0.8760 1.0624 0.7288 0.2670  0.1517  0.2643  301 A1BGV B C2  
1521 C C3  . A1BGV C .   ? 0.8729 1.0712 0.7159 0.2699  0.1432  0.2495  301 A1BGV B C3  
1522 N N2  . A1BGV C .   ? 0.8821 0.9713 0.6909 0.2610  0.1223  0.2040  301 A1BGV B N2  
1523 C C9  . A1BGV C .   ? 0.8561 0.8830 0.7024 0.1800  0.0903  0.1370  301 A1BGV B C9  
1524 O O1  . A1BGV C .   ? 0.8515 0.8850 0.7227 0.1643  0.0914  0.1415  301 A1BGV B O1  
1525 C C11 . A1BGV C .   ? 0.8420 0.8400 0.6990 0.1481  0.0752  0.1031  301 A1BGV B C11 
1526 N N4  . A1BGV C .   ? 0.8450 0.8366 0.6986 0.1393  0.0683  0.0879  301 A1BGV B N4  
1527 C C12 . A1BGV C .   ? 0.8525 0.8431 0.6820 0.1490  0.0649  0.0812  301 A1BGV B C12 
1528 N N5  . A1BGV C .   ? 0.8546 0.8358 0.6538 0.1503  0.0544  0.0623  301 A1BGV B N5  
1529 O O2  . A1BGV C .   ? 0.8666 0.8468 0.7008 0.1297  0.0560  0.0598  301 A1BGV B O2  
1530 C C14 . A1BGV C .   ? 0.8532 0.8487 0.6703 0.1650  0.0683  0.0904  301 A1BGV B C14 
1531 C C16 . A1BGV C .   ? 0.8633 0.9453 0.7057 0.2212  0.1148  0.1895  301 A1BGV B C16 
1532 N N6  . A1BGV C .   ? 0.8572 0.9702 0.7111 0.2284  0.1259  0.2130  301 A1BGV B N6  
1533 S S   . DMS   D .   ? 2.0046 1.8874 1.9136 0.1112  0.0563  0.0634  302 DMS   B S   
1534 O O   . DMS   D .   ? 2.0113 1.8937 1.9027 0.1147  0.0530  0.0450  302 DMS   B O   
1535 C C1  . DMS   D .   ? 1.9937 1.8923 1.9193 0.0989  0.0534  0.0661  302 DMS   B C1  
1536 C C2  . DMS   D .   ? 2.0031 1.9017 1.8986 0.1240  0.0666  0.0798  302 DMS   B C2  
1537 S S   . SO4   E .   ? 2.4961 2.0912 1.8979 0.4816  -0.3076 -0.0846 303 SO4   B S   
1538 O O1  . SO4   E .   ? 2.4918 2.0775 1.9175 0.4702  -0.3136 -0.0899 303 SO4   B O1  
1539 O O2  . SO4   E .   ? 2.4893 2.0857 1.9084 0.4459  -0.2910 -0.0715 303 SO4   B O2  
1540 O O3  . SO4   E .   ? 2.5174 2.0780 1.8894 0.5079  -0.3410 -0.0981 303 SO4   B O3  
1541 O O4  . SO4   E .   ? 2.4852 2.1238 1.8754 0.5040  -0.2856 -0.0787 303 SO4   B O4  
1542 S S   . SO4   F .   ? 1.7251 1.6185 1.5666 0.1231  0.0219  -0.0651 304 SO4   B S   
1543 O O1  . SO4   F .   ? 1.7228 1.6329 1.5506 0.1252  0.0305  -0.0630 304 SO4   B O1  
1544 O O2  . SO4   F .   ? 1.7220 1.6147 1.5722 0.1145  0.0217  -0.0544 304 SO4   B O2  
1545 O O3  . SO4   F .   ? 1.7280 1.6078 1.5766 0.1260  0.0217  -0.0619 304 SO4   B O3  
1546 O O4  . SO4   F .   ? 1.7275 1.6190 1.5671 0.1278  0.0126  -0.0813 304 SO4   B O4  
# 
