data_7HP8
# 
_entry.id   7HP8 
# 
_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   7HP8         pdb_00007hp8 10.2210/pdb7hp8/pdb 
WWPDB D_1001407758 ?            ?                   
# 
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                        7HP8 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-07 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Ni, X.'              1  
'Marples, P.G.'       2  
'Godoy, A.S.'         3  
'Koekemoer, L.'       4  
'Aschenbrenner, J.C.' 5  
'Balcomb, B.H.'       6  
'Fairhead, M.'        7  
'Lithgo, R.M.'        8  
'Lee, A.'             9  
'Kenton, N.'          10 
'Thompson, W.'        11 
'Tomlinson, C.W.E.'   12 
'Wild, C.'            13 
'Winokan, M.'         14 
'Williams, E.P.'      15 
'Chandran, A.V.'      16 
'Walsh, M.A.'         17 
'Fearon, D.'          18 
'von Delft, F.'       19 
# 
_citation.id                        primary 
_citation.title                     'PanDDA analysis group deposition' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B'                                 5067.486  1   ?                           ?    ? 
? 
2 polymer     man 'Serine protease NS3'                                          18117.629 1   3.4.21.91,3.6.1.15,3.6.4.13 None ? 
? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                           78.133    3   ?                           ?    ? 
? 
4 non-polymer syn 'N-(3-methylpyridin-4-yl)-5-propanamidopyridine-3-carboxamide' 284.313   1   ?                           ?    ? 
? 
5 non-polymer syn 'SULFATE ION'                                                  96.063    1   ?                           ?    ? 
? 
6 water       nat water                                                          18.015    102 ?                           ?    ? 
? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                           DMS   
4 'N-(3-methylpyridin-4-yl)-5-propanamidopyridine-3-carboxamide' A1BGO 
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 
A1BGO non-polymer         . 'N-(3-methylpyridin-4-yl)-5-propanamidopyridine-3-carboxamide' ? 'C15 H16 N4 O2'  284.313 
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        A1BGO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BGO 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS   1  201 201 DMS   DMS B . 
D 3 DMS   1  202 202 DMS   DMS B . 
E 3 DMS   1  203 203 DMS   DMS B . 
F 4 A1BGO 1  204 201 A1BGO LIG B . 
G 5 SO4   1  205 202 SO4   SO4 B . 
H 6 HOH   1  101 103 HOH   HOH A . 
H 6 HOH   2  102 105 HOH   HOH A . 
H 6 HOH   3  103 34  HOH   HOH A . 
H 6 HOH   4  104 65  HOH   HOH A . 
H 6 HOH   5  105 54  HOH   HOH A . 
H 6 HOH   6  106 77  HOH   HOH A . 
H 6 HOH   7  107 98  HOH   HOH A . 
H 6 HOH   8  108 131 HOH   HOH A . 
H 6 HOH   9  109 16  HOH   HOH A . 
H 6 HOH   10 110 132 HOH   HOH A . 
H 6 HOH   11 111 50  HOH   HOH A . 
H 6 HOH   12 112 70  HOH   HOH A . 
H 6 HOH   13 113 118 HOH   HOH A . 
H 6 HOH   14 114 121 HOH   HOH A . 
H 6 HOH   15 115 110 HOH   HOH A . 
H 6 HOH   16 116 29  HOH   HOH A . 
H 6 HOH   17 117 36  HOH   HOH A . 
H 6 HOH   18 118 120 HOH   HOH A . 
H 6 HOH   19 119 134 HOH   HOH A . 
H 6 HOH   20 120 27  HOH   HOH A . 
H 6 HOH   21 121 85  HOH   HOH A . 
H 6 HOH   22 122 119 HOH   HOH A . 
H 6 HOH   23 123 135 HOH   HOH A . 
H 6 HOH   24 124 81  HOH   HOH A . 
I 6 HOH   1  301 11  HOH   HOH B . 
I 6 HOH   2  302 66  HOH   HOH B . 
I 6 HOH   3  303 51  HOH   HOH B . 
I 6 HOH   4  304 58  HOH   HOH B . 
I 6 HOH   5  305 92  HOH   HOH B . 
I 6 HOH   6  306 48  HOH   HOH B . 
I 6 HOH   7  307 5   HOH   HOH B . 
I 6 HOH   8  308 136 HOH   HOH B . 
I 6 HOH   9  309 57  HOH   HOH B . 
I 6 HOH   10 310 40  HOH   HOH B . 
I 6 HOH   11 311 14  HOH   HOH B . 
I 6 HOH   12 312 46  HOH   HOH B . 
I 6 HOH   13 313 62  HOH   HOH B . 
I 6 HOH   14 314 115 HOH   HOH B . 
I 6 HOH   15 315 4   HOH   HOH B . 
I 6 HOH   16 316 63  HOH   HOH B . 
I 6 HOH   17 317 24  HOH   HOH B . 
I 6 HOH   18 318 79  HOH   HOH B . 
I 6 HOH   19 319 30  HOH   HOH B . 
I 6 HOH   20 320 106 HOH   HOH B . 
I 6 HOH   21 321 1   HOH   HOH B . 
I 6 HOH   22 322 125 HOH   HOH B . 
I 6 HOH   23 323 117 HOH   HOH B . 
I 6 HOH   24 324 20  HOH   HOH B . 
I 6 HOH   25 325 32  HOH   HOH B . 
I 6 HOH   26 326 23  HOH   HOH B . 
I 6 HOH   27 327 89  HOH   HOH B . 
I 6 HOH   28 328 42  HOH   HOH B . 
I 6 HOH   29 329 102 HOH   HOH B . 
I 6 HOH   30 330 68  HOH   HOH B . 
I 6 HOH   31 331 107 HOH   HOH B . 
I 6 HOH   32 332 31  HOH   HOH B . 
I 6 HOH   33 333 90  HOH   HOH B . 
I 6 HOH   34 334 116 HOH   HOH B . 
I 6 HOH   35 335 17  HOH   HOH B . 
I 6 HOH   36 336 100 HOH   HOH B . 
I 6 HOH   37 337 73  HOH   HOH B . 
I 6 HOH   38 338 108 HOH   HOH B . 
I 6 HOH   39 339 39  HOH   HOH B . 
I 6 HOH   40 340 49  HOH   HOH B . 
I 6 HOH   41 341 35  HOH   HOH B . 
I 6 HOH   42 342 13  HOH   HOH B . 
I 6 HOH   43 343 126 HOH   HOH B . 
I 6 HOH   44 344 2   HOH   HOH B . 
I 6 HOH   45 345 28  HOH   HOH B . 
I 6 HOH   46 346 60  HOH   HOH B . 
I 6 HOH   47 347 21  HOH   HOH B . 
I 6 HOH   48 348 43  HOH   HOH B . 
I 6 HOH   49 349 127 HOH   HOH B . 
I 6 HOH   50 350 10  HOH   HOH B . 
I 6 HOH   51 351 12  HOH   HOH B . 
I 6 HOH   52 352 64  HOH   HOH B . 
I 6 HOH   53 353 83  HOH   HOH B . 
I 6 HOH   54 354 56  HOH   HOH B . 
I 6 HOH   55 355 9   HOH   HOH B . 
I 6 HOH   56 356 122 HOH   HOH B . 
I 6 HOH   57 357 123 HOH   HOH B . 
I 6 HOH   58 358 133 HOH   HOH B . 
I 6 HOH   59 359 72  HOH   HOH B . 
I 6 HOH   60 360 3   HOH   HOH B . 
I 6 HOH   61 361 18  HOH   HOH B . 
I 6 HOH   62 362 82  HOH   HOH B . 
I 6 HOH   63 363 129 HOH   HOH B . 
I 6 HOH   64 364 26  HOH   HOH B . 
I 6 HOH   65 365 130 HOH   HOH B . 
I 6 HOH   66 366 112 HOH   HOH B . 
I 6 HOH   67 367 69  HOH   HOH B . 
I 6 HOH   68 368 124 HOH   HOH B . 
I 6 HOH   69 369 67  HOH   HOH B . 
I 6 HOH   70 370 87  HOH   HOH B . 
I 6 HOH   71 371 45  HOH   HOH B . 
I 6 HOH   72 372 94  HOH   HOH B . 
I 6 HOH   73 373 80  HOH   HOH B . 
I 6 HOH   74 374 75  HOH   HOH B . 
I 6 HOH   75 375 61  HOH   HOH B . 
I 6 HOH   76 376 109 HOH   HOH B . 
I 6 HOH   77 377 59  HOH   HOH B . 
I 6 HOH   78 378 44  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0267 ? 1 
refinement       BUSTER  .        ? 2 
'data scaling'   Aimless .        ? 3 
phasing          PHASER  .        ? 4 
'data reduction' XDS     .        ? 5 
'data reduction' XDS     .        ? 6 
'data reduction' XDS     .        ? 7 
'data reduction' XDS     .        ? 8 
'data reduction' XDS     .        ? 9 
# 
_cell.entry_id           7HP8 
_cell.length_a           42.254 
_cell.length_b           42.254 
_cell.length_c           216.509 
_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                         7HP8 
_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          7HP8 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.08 
_exptl_crystal.density_percent_sol   40.98 
_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   2023-10-06 
_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                     7HP8 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             216.58 
_reflns.d_resolution_high            1.74 
_reflns.number_obs                   21391 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.175 
_reflns.pdbx_netI_over_sigmaI        6.4 
_reflns.pdbx_redundancy              25.3 
_reflns.pdbx_Rrim_I_all              0.179 
_reflns.pdbx_Rpim_I_all              0.036 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     541365 
_reflns.pdbx_chi_squared             0.21 
_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                  1.74 
_reflns_shell.d_res_low                   1.78 
_reflns_shell.number_measured_all         31296 
_reflns_shell.number_unique_obs           1248 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_chi_squared            0.08 
_reflns_shell.pdbx_redundancy             25.1 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             10.558 
_reflns_shell.pdbx_Rpim_I_all             2.086 
_reflns_shell.pdbx_CC_half                0.510 
_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                                 7HP8 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     16379 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             54.13 
_refine.ls_d_res_high                            1.74 
_refine.ls_percent_reflns_obs                    80.82 
_refine.ls_R_factor_obs                          0.23928 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.23643 
_refine.ls_R_factor_R_free                       0.29430 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_number_reflns_R_free                  839 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.940 
_refine.B_iso_mean                               57.885 
_refine.aniso_B[1][1]                            1.28 
_refine.aniso_B[2][2]                            1.28 
_refine.aniso_B[3][3]                            -2.56 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            -0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.227 
_refine.pdbx_overall_ESU_R_Free                  0.199 
_refine.overall_SU_ML                            0.297 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             24.379 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_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             102 
_refine_hist.number_atoms_total               1616 
_refine_hist.d_res_high                       1.74 
_refine_hist.d_res_low                        54.13 
# 
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 
r_bond_refined_d             0.009  0.014  ? 2295 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.015  ? 1838 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.626  1.643  ? 2699 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.211  1.591  ? 4257 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.642  5.000  ? 265  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       35.490 23.023 ? 86   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       16.630 15.000 ? 322  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       20.828 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.070  0.200  ? 240  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 2346 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 438  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  1.969  3.693  ? 1150 'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.998  3.502  ? 1087 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 3.634  5.160  ? 1269 'X-RAY DIFFRACTION' ? 
r_mcangle_other              3.637  5.164  ? 1270 'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.058  4.353  ? 1145 'X-RAY DIFFRACTION' ? 
r_scbond_other               2.066  4.288  ? 1133 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              3.703  5.868  ? 1419 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       13.855 38.943 ? 2036 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         13.851 38.949 ? 2037 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.741 
_refine_ls_shell.d_res_low                        1.786 
_refine_ls_shell.number_reflns_R_work             55 
_refine_ls_shell.R_factor_R_work                  0.643 
_refine_ls_shell.percent_reflns_obs               3.65 
_refine_ls_shell.R_factor_R_free                  0.108 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             1 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HP8 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0014942-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HP8 
_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 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I 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 7HP8 A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HP8 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 7HP8 SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HP8 MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HP8 MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HP8 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)' 4720 ? 
1 MORE         -33  ? 
1 'SSA (A^2)'  9870 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            134 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            134 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             143 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             143 
_struct_conn.ptnr2_symmetry                8_444 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.384 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       134 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      134 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        143 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       143 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          8_444 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA2 5 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N GLU A 11  ? N GLU A 54  O ARG B 15  ? O ARG B 24  
AA1 4 5 N THR B 18  ? N THR B 27  O THR B 25  ? O THR B 34  
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 TRP B 60  ? N TRP B 69  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O LYS B 98  ? O LYS B 107 N ALA B 90  ? N ALA B 99  
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                   7HP8 
_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   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 64 ? C 90.43   50.29   
2 1 ASP A 64 ? D 90.43   50.29   
3 1 GLU A 66 ? A -59.56  93.22   
4 1 GLU A 66 ? B -59.56  93.22   
5 1 ASP B 20 ? ? -48.08  156.24  
6 1 LEU B 30 ? ? -101.12 -168.19 
7 1 ASP B 71 ? ? -161.48 107.99  
8 1 CYS B 80 ? A 82.14   -12.54  
9 1 CYS B 80 ? B 82.14   -12.54  
# 
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 339 ? I HOH . 
2 1 B HOH 371 ? I 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 -13.3944 -1.8811 -19.3265 0.2625 0.2656 0.0319 0.1482 0.0554 0.0509 1.8129 2.1262 1.0960 -0.5191 
0.0609 0.1427  0.2700 0.2752 0.1976 -0.2814 -0.2603 -0.1933 0.0405 0.1191 -0.0097 
'X-RAY DIFFRACTION' 2 ? refined -18.2197 0.6886  -15.9789 0.3090 0.3233 0.1063 0.1305 0.0398 0.0090 0.5287 0.3527 0.6530 -0.3199 
0.3839 -0.0684 0.2045 0.1326 0.0420 -0.1387 -0.2086 0.0302  0.1527 0.0846 0.0041  
# 
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 50 ? ? A 88  ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 16 ? ? B 203 ? ? ? ? 
# 
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 
A1BGO N1   N N N 1   
A1BGO N3   N N N 2   
A1BGO C4   C Y N 3   
A1BGO C5   C Y N 4   
A1BGO C6   C Y N 5   
A1BGO C7   C Y N 6   
A1BGO C8   C N N 7   
A1BGO C10  C Y N 8   
A1BGO C13  C Y N 9   
A1BGO C15  C Y N 10  
A1BGO C1   C N N 11  
A1BGO C2   C N N 12  
A1BGO C3   C N N 13  
A1BGO O1   O N N 14  
A1BGO N2   N Y N 15  
A1BGO O2   O N N 16  
A1BGO C9   C Y N 17  
A1BGO C11  C Y N 18  
A1BGO N4   N Y N 19  
A1BGO C12  C Y N 20  
A1BGO C14  C N N 21  
A1BGO H6   H N N 22  
A1BGO H9   H N N 23  
A1BGO H7   H N N 24  
A1BGO H8   H N N 25  
A1BGO H10  H N N 26  
A1BGO H16  H N N 27  
A1BGO H3   H N N 28  
A1BGO H1   H N N 29  
A1BGO H2   H N N 30  
A1BGO H4   H N N 31  
A1BGO H5   H N N 32  
A1BGO H11  H N N 33  
A1BGO H12  H N N 34  
A1BGO H13  H N N 35  
A1BGO H15  H N N 36  
A1BGO H14  H N N 37  
ALA   N    N N N 38  
ALA   CA   C N S 39  
ALA   C    C N N 40  
ALA   O    O N N 41  
ALA   CB   C N N 42  
ALA   OXT  O N N 43  
ALA   H    H N N 44  
ALA   H2   H N N 45  
ALA   HA   H N N 46  
ALA   HB1  H N N 47  
ALA   HB2  H N N 48  
ALA   HB3  H N N 49  
ALA   HXT  H N N 50  
ARG   N    N N N 51  
ARG   CA   C N S 52  
ARG   C    C N N 53  
ARG   O    O N N 54  
ARG   CB   C N N 55  
ARG   CG   C N N 56  
ARG   CD   C N N 57  
ARG   NE   N N N 58  
ARG   CZ   C N N 59  
ARG   NH1  N N N 60  
ARG   NH2  N N N 61  
ARG   OXT  O N N 62  
ARG   H    H N N 63  
ARG   H2   H N N 64  
ARG   HA   H N N 65  
ARG   HB2  H N N 66  
ARG   HB3  H N N 67  
ARG   HG2  H N N 68  
ARG   HG3  H N N 69  
ARG   HD2  H N N 70  
ARG   HD3  H N N 71  
ARG   HE   H N N 72  
ARG   HH11 H N N 73  
ARG   HH12 H N N 74  
ARG   HH21 H N N 75  
ARG   HH22 H N N 76  
ARG   HXT  H N N 77  
ASN   N    N N N 78  
ASN   CA   C N S 79  
ASN   C    C N N 80  
ASN   O    O N N 81  
ASN   CB   C N N 82  
ASN   CG   C N N 83  
ASN   OD1  O N N 84  
ASN   ND2  N N N 85  
ASN   OXT  O N N 86  
ASN   H    H N N 87  
ASN   H2   H N N 88  
ASN   HA   H N N 89  
ASN   HB2  H N N 90  
ASN   HB3  H N N 91  
ASN   HD21 H N N 92  
ASN   HD22 H N N 93  
ASN   HXT  H N N 94  
ASP   N    N N N 95  
ASP   CA   C N S 96  
ASP   C    C N N 97  
ASP   O    O N N 98  
ASP   CB   C N N 99  
ASP   CG   C N N 100 
ASP   OD1  O N N 101 
ASP   OD2  O N N 102 
ASP   OXT  O N N 103 
ASP   H    H N N 104 
ASP   H2   H N N 105 
ASP   HA   H N N 106 
ASP   HB2  H N N 107 
ASP   HB3  H N N 108 
ASP   HD2  H N N 109 
ASP   HXT  H N N 110 
CYS   N    N N N 111 
CYS   CA   C N R 112 
CYS   C    C N N 113 
CYS   O    O N N 114 
CYS   CB   C N N 115 
CYS   SG   S N N 116 
CYS   OXT  O N N 117 
CYS   H    H N N 118 
CYS   H2   H N N 119 
CYS   HA   H N N 120 
CYS   HB2  H N N 121 
CYS   HB3  H N N 122 
CYS   HG   H N N 123 
CYS   HXT  H N N 124 
DMS   S    S N N 125 
DMS   O    O N N 126 
DMS   C1   C N N 127 
DMS   C2   C N N 128 
DMS   H11  H N N 129 
DMS   H12  H N N 130 
DMS   H13  H N N 131 
DMS   H21  H N N 132 
DMS   H22  H N N 133 
DMS   H23  H N N 134 
GLN   N    N N N 135 
GLN   CA   C N S 136 
GLN   C    C N N 137 
GLN   O    O N N 138 
GLN   CB   C N N 139 
GLN   CG   C N N 140 
GLN   CD   C N N 141 
GLN   OE1  O N N 142 
GLN   NE2  N N N 143 
GLN   OXT  O N N 144 
GLN   H    H N N 145 
GLN   H2   H N N 146 
GLN   HA   H N N 147 
GLN   HB2  H N N 148 
GLN   HB3  H N N 149 
GLN   HG2  H N N 150 
GLN   HG3  H N N 151 
GLN   HE21 H N N 152 
GLN   HE22 H N N 153 
GLN   HXT  H N N 154 
GLU   N    N N N 155 
GLU   CA   C N S 156 
GLU   C    C N N 157 
GLU   O    O N N 158 
GLU   CB   C N N 159 
GLU   CG   C N N 160 
GLU   CD   C N N 161 
GLU   OE1  O N N 162 
GLU   OE2  O N N 163 
GLU   OXT  O N N 164 
GLU   H    H N N 165 
GLU   H2   H N N 166 
GLU   HA   H N N 167 
GLU   HB2  H N N 168 
GLU   HB3  H N N 169 
GLU   HG2  H N N 170 
GLU   HG3  H N N 171 
GLU   HE2  H N N 172 
GLU   HXT  H N N 173 
GLY   N    N N N 174 
GLY   CA   C N N 175 
GLY   C    C N N 176 
GLY   O    O N N 177 
GLY   OXT  O N N 178 
GLY   H    H N N 179 
GLY   H2   H N N 180 
GLY   HA2  H N N 181 
GLY   HA3  H N N 182 
GLY   HXT  H N N 183 
HIS   N    N N N 184 
HIS   CA   C N S 185 
HIS   C    C N N 186 
HIS   O    O N N 187 
HIS   CB   C N N 188 
HIS   CG   C Y N 189 
HIS   ND1  N Y N 190 
HIS   CD2  C Y N 191 
HIS   CE1  C Y N 192 
HIS   NE2  N Y N 193 
HIS   OXT  O N N 194 
HIS   H    H N N 195 
HIS   H2   H N N 196 
HIS   HA   H N N 197 
HIS   HB2  H N N 198 
HIS   HB3  H N N 199 
HIS   HD1  H N N 200 
HIS   HD2  H N N 201 
HIS   HE1  H N N 202 
HIS   HE2  H N N 203 
HIS   HXT  H N N 204 
HOH   O    O N N 205 
HOH   H1   H N N 206 
HOH   H2   H N N 207 
ILE   N    N N N 208 
ILE   CA   C N S 209 
ILE   C    C N N 210 
ILE   O    O N N 211 
ILE   CB   C N S 212 
ILE   CG1  C N N 213 
ILE   CG2  C N N 214 
ILE   CD1  C N N 215 
ILE   OXT  O N N 216 
ILE   H    H N N 217 
ILE   H2   H N N 218 
ILE   HA   H N N 219 
ILE   HB   H N N 220 
ILE   HG12 H N N 221 
ILE   HG13 H N N 222 
ILE   HG21 H N N 223 
ILE   HG22 H N N 224 
ILE   HG23 H N N 225 
ILE   HD11 H N N 226 
ILE   HD12 H N N 227 
ILE   HD13 H N N 228 
ILE   HXT  H N N 229 
LEU   N    N N N 230 
LEU   CA   C N S 231 
LEU   C    C N N 232 
LEU   O    O N N 233 
LEU   CB   C N N 234 
LEU   CG   C N N 235 
LEU   CD1  C N N 236 
LEU   CD2  C N N 237 
LEU   OXT  O N N 238 
LEU   H    H N N 239 
LEU   H2   H N N 240 
LEU   HA   H N N 241 
LEU   HB2  H N N 242 
LEU   HB3  H N N 243 
LEU   HG   H N N 244 
LEU   HD11 H N N 245 
LEU   HD12 H N N 246 
LEU   HD13 H N N 247 
LEU   HD21 H N N 248 
LEU   HD22 H N N 249 
LEU   HD23 H N N 250 
LEU   HXT  H N N 251 
LYS   N    N N N 252 
LYS   CA   C N S 253 
LYS   C    C N N 254 
LYS   O    O N N 255 
LYS   CB   C N N 256 
LYS   CG   C N N 257 
LYS   CD   C N N 258 
LYS   CE   C N N 259 
LYS   NZ   N N N 260 
LYS   OXT  O N N 261 
LYS   H    H N N 262 
LYS   H2   H N N 263 
LYS   HA   H N N 264 
LYS   HB2  H N N 265 
LYS   HB3  H N N 266 
LYS   HG2  H N N 267 
LYS   HG3  H N N 268 
LYS   HD2  H N N 269 
LYS   HD3  H N N 270 
LYS   HE2  H N N 271 
LYS   HE3  H N N 272 
LYS   HZ1  H N N 273 
LYS   HZ2  H N N 274 
LYS   HZ3  H N N 275 
LYS   HXT  H N N 276 
MET   N    N N N 277 
MET   CA   C N S 278 
MET   C    C N N 279 
MET   O    O N N 280 
MET   CB   C N N 281 
MET   CG   C N N 282 
MET   SD   S N N 283 
MET   CE   C N N 284 
MET   OXT  O N N 285 
MET   H    H N N 286 
MET   H2   H N N 287 
MET   HA   H N N 288 
MET   HB2  H N N 289 
MET   HB3  H N N 290 
MET   HG2  H N N 291 
MET   HG3  H N N 292 
MET   HE1  H N N 293 
MET   HE2  H N N 294 
MET   HE3  H N N 295 
MET   HXT  H N N 296 
PHE   N    N N N 297 
PHE   CA   C N S 298 
PHE   C    C N N 299 
PHE   O    O N N 300 
PHE   CB   C N N 301 
PHE   CG   C Y N 302 
PHE   CD1  C Y N 303 
PHE   CD2  C Y N 304 
PHE   CE1  C Y N 305 
PHE   CE2  C Y N 306 
PHE   CZ   C Y N 307 
PHE   OXT  O N N 308 
PHE   H    H N N 309 
PHE   H2   H N N 310 
PHE   HA   H N N 311 
PHE   HB2  H N N 312 
PHE   HB3  H N N 313 
PHE   HD1  H N N 314 
PHE   HD2  H N N 315 
PHE   HE1  H N N 316 
PHE   HE2  H N N 317 
PHE   HZ   H N N 318 
PHE   HXT  H N N 319 
PRO   N    N N N 320 
PRO   CA   C N S 321 
PRO   C    C N N 322 
PRO   O    O N N 323 
PRO   CB   C N N 324 
PRO   CG   C N N 325 
PRO   CD   C N N 326 
PRO   OXT  O N N 327 
PRO   H    H N N 328 
PRO   HA   H N N 329 
PRO   HB2  H N N 330 
PRO   HB3  H N N 331 
PRO   HG2  H N N 332 
PRO   HG3  H N N 333 
PRO   HD2  H N N 334 
PRO   HD3  H N N 335 
PRO   HXT  H N N 336 
SER   N    N N N 337 
SER   CA   C N S 338 
SER   C    C N N 339 
SER   O    O N N 340 
SER   CB   C N N 341 
SER   OG   O N N 342 
SER   OXT  O N N 343 
SER   H    H N N 344 
SER   H2   H N N 345 
SER   HA   H N N 346 
SER   HB2  H N N 347 
SER   HB3  H N N 348 
SER   HG   H N N 349 
SER   HXT  H N N 350 
SO4   S    S N N 351 
SO4   O1   O N N 352 
SO4   O2   O N N 353 
SO4   O3   O N N 354 
SO4   O4   O N N 355 
THR   N    N N N 356 
THR   CA   C N S 357 
THR   C    C N N 358 
THR   O    O N N 359 
THR   CB   C N R 360 
THR   OG1  O N N 361 
THR   CG2  C N N 362 
THR   OXT  O N N 363 
THR   H    H N N 364 
THR   H2   H N N 365 
THR   HA   H N N 366 
THR   HB   H N N 367 
THR   HG1  H N N 368 
THR   HG21 H N N 369 
THR   HG22 H N N 370 
THR   HG23 H N N 371 
THR   HXT  H N N 372 
TRP   N    N N N 373 
TRP   CA   C N S 374 
TRP   C    C N N 375 
TRP   O    O N N 376 
TRP   CB   C N N 377 
TRP   CG   C Y N 378 
TRP   CD1  C Y N 379 
TRP   CD2  C Y N 380 
TRP   NE1  N Y N 381 
TRP   CE2  C Y N 382 
TRP   CE3  C Y N 383 
TRP   CZ2  C Y N 384 
TRP   CZ3  C Y N 385 
TRP   CH2  C Y N 386 
TRP   OXT  O N N 387 
TRP   H    H N N 388 
TRP   H2   H N N 389 
TRP   HA   H N N 390 
TRP   HB2  H N N 391 
TRP   HB3  H N N 392 
TRP   HD1  H N N 393 
TRP   HE1  H N N 394 
TRP   HE3  H N N 395 
TRP   HZ2  H N N 396 
TRP   HZ3  H N N 397 
TRP   HH2  H N N 398 
TRP   HXT  H N N 399 
TYR   N    N N N 400 
TYR   CA   C N S 401 
TYR   C    C N N 402 
TYR   O    O N N 403 
TYR   CB   C N N 404 
TYR   CG   C Y N 405 
TYR   CD1  C Y N 406 
TYR   CD2  C Y N 407 
TYR   CE1  C Y N 408 
TYR   CE2  C Y N 409 
TYR   CZ   C Y N 410 
TYR   OH   O N N 411 
TYR   OXT  O N N 412 
TYR   H    H N N 413 
TYR   H2   H N N 414 
TYR   HA   H N N 415 
TYR   HB2  H N N 416 
TYR   HB3  H N N 417 
TYR   HD1  H N N 418 
TYR   HD2  H N N 419 
TYR   HE1  H N N 420 
TYR   HE2  H N N 421 
TYR   HH   H N N 422 
TYR   HXT  H N N 423 
VAL   N    N N N 424 
VAL   CA   C N S 425 
VAL   C    C N N 426 
VAL   O    O N N 427 
VAL   CB   C N N 428 
VAL   CG1  C N N 429 
VAL   CG2  C N N 430 
VAL   OXT  O N N 431 
VAL   H    H N N 432 
VAL   H2   H N N 433 
VAL   HA   H N N 434 
VAL   HB   H N N 435 
VAL   HG11 H N N 436 
VAL   HG12 H N N 437 
VAL   HG13 H N N 438 
VAL   HG21 H N N 439 
VAL   HG22 H N N 440 
VAL   HG23 H N N 441 
VAL   HXT  H N N 442 
# 
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 
A1BGO C1  C2   sing N N 1   
A1BGO C2  C3   sing N N 2   
A1BGO C3  O1   doub N N 3   
A1BGO C3  N1   sing N N 4   
A1BGO N1  C4   sing N N 5   
A1BGO C4  C5   doub Y N 6   
A1BGO C5  N2   sing Y N 7   
A1BGO N2  C6   doub Y N 8   
A1BGO C6  C7   sing Y N 9   
A1BGO C7  C8   sing N N 10  
A1BGO C8  O2   doub N N 11  
A1BGO C8  N3   sing N N 12  
A1BGO N3  C9   sing N N 13  
A1BGO C9  C10  doub Y N 14  
A1BGO C10 C11  sing Y N 15  
A1BGO C11 N4   doub Y N 16  
A1BGO N4  C12  sing Y N 17  
A1BGO C12 C13  doub Y N 18  
A1BGO C13 C14  sing N N 19  
A1BGO C7  C15  doub Y N 20  
A1BGO C4  C15  sing Y N 21  
A1BGO C9  C13  sing Y N 22  
A1BGO N1  H6   sing N N 23  
A1BGO N3  H9   sing N N 24  
A1BGO C5  H7   sing N N 25  
A1BGO C6  H8   sing N N 26  
A1BGO C10 H10  sing N N 27  
A1BGO C15 H16  sing N N 28  
A1BGO C1  H3   sing N N 29  
A1BGO C1  H1   sing N N 30  
A1BGO C1  H2   sing N N 31  
A1BGO C2  H4   sing N N 32  
A1BGO C2  H5   sing N N 33  
A1BGO C11 H11  sing N N 34  
A1BGO C12 H12  sing N N 35  
A1BGO C14 H13  sing N N 36  
A1BGO C14 H15  sing N N 37  
A1BGO C14 H14  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
DMS   S   O    doub N N 121 
DMS   S   C1   sing N N 122 
DMS   S   C2   sing N N 123 
DMS   C1  H11  sing N N 124 
DMS   C1  H12  sing N N 125 
DMS   C1  H13  sing N N 126 
DMS   C2  H21  sing N N 127 
DMS   C2  H22  sing N N 128 
DMS   C2  H23  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
SO4   S   O1   doub N N 337 
SO4   S   O2   doub N N 338 
SO4   S   O3   sing N N 339 
SO4   S   O4   sing N N 340 
THR   N   CA   sing N N 341 
THR   N   H    sing N N 342 
THR   N   H2   sing N N 343 
THR   CA  C    sing N N 344 
THR   CA  CB   sing N N 345 
THR   CA  HA   sing N N 346 
THR   C   O    doub N N 347 
THR   C   OXT  sing N N 348 
THR   CB  OG1  sing N N 349 
THR   CB  CG2  sing N N 350 
THR   CB  HB   sing N N 351 
THR   OG1 HG1  sing N N 352 
THR   CG2 HG21 sing N N 353 
THR   CG2 HG22 sing N N 354 
THR   CG2 HG23 sing N N 355 
THR   OXT HXT  sing N N 356 
TRP   N   CA   sing N N 357 
TRP   N   H    sing N N 358 
TRP   N   H2   sing N N 359 
TRP   CA  C    sing N N 360 
TRP   CA  CB   sing N N 361 
TRP   CA  HA   sing N N 362 
TRP   C   O    doub N N 363 
TRP   C   OXT  sing N N 364 
TRP   CB  CG   sing N N 365 
TRP   CB  HB2  sing N N 366 
TRP   CB  HB3  sing N N 367 
TRP   CG  CD1  doub Y N 368 
TRP   CG  CD2  sing Y N 369 
TRP   CD1 NE1  sing Y N 370 
TRP   CD1 HD1  sing N N 371 
TRP   CD2 CE2  doub Y N 372 
TRP   CD2 CE3  sing Y N 373 
TRP   NE1 CE2  sing Y N 374 
TRP   NE1 HE1  sing N N 375 
TRP   CE2 CZ2  sing Y N 376 
TRP   CE3 CZ3  doub Y N 377 
TRP   CE3 HE3  sing N N 378 
TRP   CZ2 CH2  doub Y N 379 
TRP   CZ2 HZ2  sing N N 380 
TRP   CZ3 CH2  sing Y N 381 
TRP   CZ3 HZ3  sing N N 382 
TRP   CH2 HH2  sing N N 383 
TRP   OXT HXT  sing N N 384 
TYR   N   CA   sing N N 385 
TYR   N   H    sing N N 386 
TYR   N   H2   sing N N 387 
TYR   CA  C    sing N N 388 
TYR   CA  CB   sing N N 389 
TYR   CA  HA   sing N N 390 
TYR   C   O    doub N N 391 
TYR   C   OXT  sing N N 392 
TYR   CB  CG   sing N N 393 
TYR   CB  HB2  sing N N 394 
TYR   CB  HB3  sing N N 395 
TYR   CG  CD1  doub Y N 396 
TYR   CG  CD2  sing Y N 397 
TYR   CD1 CE1  sing Y N 398 
TYR   CD1 HD1  sing N N 399 
TYR   CD2 CE2  doub Y N 400 
TYR   CD2 HD2  sing N N 401 
TYR   CE1 CZ   doub Y N 402 
TYR   CE1 HE1  sing N N 403 
TYR   CE2 CZ   sing Y N 404 
TYR   CE2 HE2  sing N N 405 
TYR   CZ  OH   sing N N 406 
TYR   OH  HH   sing N N 407 
TYR   OXT HXT  sing N N 408 
VAL   N   CA   sing N N 409 
VAL   N   H    sing N N 410 
VAL   N   H2   sing N N 411 
VAL   CA  C    sing N N 412 
VAL   CA  CB   sing N N 413 
VAL   CA  HA   sing N N 414 
VAL   C   O    doub N N 415 
VAL   C   OXT  sing N N 416 
VAL   CB  CG1  sing N N 417 
VAL   CB  CG2  sing N N 418 
VAL   CB  HB   sing N N 419 
VAL   CG1 HG11 sing N N 420 
VAL   CG1 HG12 sing N N 421 
VAL   CG1 HG13 sing N N 422 
VAL   CG2 HG21 sing N N 423 
VAL   CG2 HG22 sing N N 424 
VAL   CG2 HG23 sing N N 425 
VAL   OXT HXT  sing N N 426 
# 
_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                    7HP8 
_atom_sites.fract_transf_matrix[1][1]   0.023666 
_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]   0.023666 
_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]   0.004619 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 7   ? -21.413 19.010  -7.310  1.00 71.53  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.579 18.102  -7.459  1.00 70.37  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.468 17.493  -8.859  1.00 65.19  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.524 18.237  -9.856  1.00 68.77  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.925 18.804  -7.216  1.00 72.54  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.900 18.089  -6.278  1.00 77.36  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -25.641 18.807  -5.578  1.00 82.24  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -24.953 16.824  -6.260  1.00 81.47  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.220 16.197  -8.897  1.00 57.73  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.163 15.416  -10.135 1.00 54.47  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.596 15.203  -10.603 1.00 49.79  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.474 15.186  -9.757  1.00 49.65  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.466 14.076  -9.895  1.00 53.99  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.073 14.256  -9.409  1.00 55.14  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.286 12.677  -9.206  1.00 57.07  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.585 13.215  -9.045  1.00 56.30  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -23.789 15.045  -11.915 1.00 47.16  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.097 14.780  -12.564 1.00 44.69  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -24.871 13.857  -13.749 1.00 44.07  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -23.748 13.773  -14.258 1.00 43.01  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.788 16.076  -12.989 1.00 45.43  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.042 16.905  -13.993 1.00 45.36  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.039 17.762  -13.589 1.00 45.92  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.326 16.825  -15.357 1.00 46.79  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.315 18.510  -14.511 1.00 47.57  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.631 17.580  -16.292 1.00 46.91  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.613 18.421  -15.864 1.00 47.88  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -22.877 19.149  -16.759 1.00 50.29  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -25.936 13.178  -14.157 1.00 45.32  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -25.929 12.160  -15.248 1.00 44.44  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.732 12.669  -16.460 1.00 45.98  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.784 13.345  -16.248 1.00 46.15  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.419 10.787  -14.735 1.00 44.06  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -27.844 10.768  -14.200 1.00 44.41  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.462 10.220  -13.693 1.00 44.50  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.389 9.369   -14.105 1.00 44.57  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.228 12.385  -17.674 1.00 47.57  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -26.892 12.616  -19.005 1.00 48.23  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -26.891 11.288  -19.773 1.00 46.53  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -25.820 10.604  -19.832 1.00 42.46  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.159 13.637  -19.879 1.00 51.92  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -25.900 14.987  -19.245 1.00 55.94  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.125 15.973  -20.116 1.00 62.81  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.208 15.557  -20.881 1.00 66.11  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.427 17.183  -20.022 1.00 70.43  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.053 10.875  -20.279 1.00 47.16  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.152 9.639   -21.091 1.00 47.45  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.250 9.809   -22.303 1.00 47.53  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.184 10.966  -22.832 1.00 48.95  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.586 9.402   -21.531 1.00 49.04  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -29.834 8.005   -22.069 1.00 51.10  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.301 7.600   -21.931 1.00 54.08  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.484 6.185   -22.176 1.00 56.11  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.332 5.615   -23.379 1.00 58.56  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.035 6.349   -24.440 1.00 62.07  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.459 4.307   -23.528 1.00 57.16  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.533 8.737   -22.676 1.00 48.15  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.602 8.695   -23.828 1.00 47.62  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -25.912 7.525   -24.776 1.00 48.24  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.217 7.442   -25.824 1.00 49.79  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.157 8.680   -23.381 1.00 48.06  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -26.894 6.667   -24.502 1.00 45.91  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.337 5.709   -25.535 1.00 45.97  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.042 4.504   -24.957 1.00 47.36  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.161 4.460   -23.672 1.00 43.53  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.506 3.589   -25.838 1.00 47.28  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.040 2.251   -25.457 1.00 50.00  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -27.857 1.312   -25.246 1.00 53.12  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -26.739 1.608   -25.730 1.00 56.00  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -29.991 1.596   -26.463 1.00 49.85  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.287 2.347   -26.599 1.00 52.99  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.374 3.381   -25.957 1.00 51.70  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.161 1.950   -27.428 1.00 54.84  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.103 0.231   -24.516 1.00 54.90  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.094 -0.837  -24.316 1.00 56.21  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.527 -1.974  -25.246 1.00 56.00  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.476 -2.721  -24.937 1.00 55.24  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -26.946 -1.158  -22.827 1.00 57.74  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.284 0.022   -22.110 1.00 58.95  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.168 -2.436  -22.604 1.00 58.90  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.360 -0.049  -20.596 1.00 59.01  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -26.842 -2.058  -26.392 0.25 56.32  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -26.862 -2.085  -26.395 0.25 56.15  ? 60  THR   A N   1 
ATOM   84   N N   C THR   A 1 17  ? -26.842 -2.058  -26.392 0.25 56.32  ? 60  THR   A N   1 
ATOM   85   N N   D THR   A 1 17  ? -26.862 -2.085  -26.395 0.25 56.15  ? 60  THR   A N   1 
ATOM   86   C CA  A THR   A 1 17  ? -27.154 -2.958  -27.535 0.25 57.14  ? 60  THR   A CA  1 
ATOM   87   C CA  B THR   A 1 17  ? -27.213 -3.063  -27.456 0.25 56.77  ? 60  THR   A CA  1 
ATOM   88   C CA  C THR   A 1 17  ? -27.154 -2.958  -27.535 0.25 57.14  ? 60  THR   A CA  1 
ATOM   89   C CA  D THR   A 1 17  ? -27.213 -3.063  -27.456 0.25 56.77  ? 60  THR   A CA  1 
ATOM   90   C C   A THR   A 1 17  ? -25.855 -3.492  -28.155 0.25 56.96  ? 60  THR   A C   1 
ATOM   91   C C   B THR   A 1 17  ? -25.945 -3.477  -28.221 0.25 56.95  ? 60  THR   A C   1 
ATOM   92   C C   C THR   A 1 17  ? -25.855 -3.492  -28.155 0.25 56.96  ? 60  THR   A C   1 
ATOM   93   C C   D THR   A 1 17  ? -25.945 -3.477  -28.221 0.25 56.95  ? 60  THR   A C   1 
ATOM   94   O O   A THR   A 1 17  ? -24.881 -2.691  -28.332 0.25 56.40  ? 60  THR   A O   1 
ATOM   95   O O   B THR   A 1 17  ? -25.081 -2.581  -28.530 0.25 56.67  ? 60  THR   A O   1 
ATOM   96   O O   C THR   A 1 17  ? -24.881 -2.691  -28.332 0.25 56.40  ? 60  THR   A O   1 
ATOM   97   O O   D THR   A 1 17  ? -25.081 -2.581  -28.530 0.25 56.67  ? 60  THR   A O   1 
ATOM   98   C CB  A THR   A 1 17  ? -27.963 -2.225  -28.612 0.25 58.55  ? 60  THR   A CB  1 
ATOM   99   C CB  B THR   A 1 17  ? -28.318 -2.493  -28.356 0.25 57.89  ? 60  THR   A CB  1 
ATOM   100  C CB  C THR   A 1 17  ? -27.963 -2.225  -28.612 0.25 58.55  ? 60  THR   A CB  1 
ATOM   101  C CB  D THR   A 1 17  ? -28.318 -2.493  -28.356 0.25 57.89  ? 60  THR   A CB  1 
ATOM   102  O OG1 A THR   A 1 17  ? -27.119 -1.245  -29.216 0.25 58.21  ? 60  THR   A OG1 1 
ATOM   103  O OG1 B THR   A 1 17  ? -29.584 -2.799  -27.764 0.25 56.84  ? 60  THR   A OG1 1 
ATOM   104  O OG1 C THR   A 1 17  ? -27.119 -1.245  -29.216 0.25 58.21  ? 60  THR   A OG1 1 
ATOM   105  O OG1 D THR   A 1 17  ? -29.584 -2.799  -27.764 0.25 56.84  ? 60  THR   A OG1 1 
ATOM   106  C CG2 A THR   A 1 17  ? -29.208 -1.562  -28.067 0.25 58.25  ? 60  THR   A CG2 1 
ATOM   107  C CG2 B THR   A 1 17  ? -28.269 -3.029  -29.768 0.25 58.66  ? 60  THR   A CG2 1 
ATOM   108  C CG2 C THR   A 1 17  ? -29.208 -1.562  -28.067 0.25 58.25  ? 60  THR   A CG2 1 
ATOM   109  C CG2 D THR   A 1 17  ? -28.269 -3.029  -29.768 0.25 58.66  ? 60  THR   A CG2 1 
ATOM   110  N N   . TRP   A 1 18  ? -25.838 -4.789  -28.493 1.00 57.36  ? 61  TRP   A N   1 
ATOM   111  C CA  . TRP   A 1 18  ? -24.760 -5.342  -29.344 1.00 62.85  ? 61  TRP   A CA  1 
ATOM   112  C C   . TRP   A 1 18  ? -25.027 -4.797  -30.751 1.00 67.79  ? 61  TRP   A C   1 
ATOM   113  O O   . TRP   A 1 18  ? -26.179 -4.825  -31.178 1.00 66.92  ? 61  TRP   A O   1 
ATOM   114  C CB  . TRP   A 1 18  ? -24.800 -6.862  -29.284 1.00 63.24  ? 61  TRP   A CB  1 
ATOM   115  C CG  . TRP   A 1 18  ? -23.758 -7.523  -30.119 1.00 67.98  ? 61  TRP   A CG  1 
ATOM   116  C CD1 . TRP   A 1 18  ? -23.874 -7.835  -31.445 1.00 69.31  ? 61  TRP   A CD1 1 
ATOM   117  C CD2 . TRP   A 1 18  ? -22.468 -8.006  -29.691 1.00 68.89  ? 61  TRP   A CD2 1 
ATOM   118  N NE1 . TRP   A 1 18  ? -22.735 -8.451  -31.871 1.00 71.49  ? 61  TRP   A NE1 1 
ATOM   119  C CE2 . TRP   A 1 18  ? -21.861 -8.594  -30.826 1.00 70.12  ? 61  TRP   A CE2 1 
ATOM   120  C CE3 . TRP   A 1 18  ? -21.766 -8.014  -28.474 1.00 66.32  ? 61  TRP   A CE3 1 
ATOM   121  C CZ2 . TRP   A 1 18  ? -20.589 -9.172  -30.783 1.00 71.07  ? 61  TRP   A CZ2 1 
ATOM   122  C CZ3 . TRP   A 1 18  ? -20.506 -8.573  -28.434 1.00 66.35  ? 61  TRP   A CZ3 1 
ATOM   123  C CH2 . TRP   A 1 18  ? -19.927 -9.146  -29.569 1.00 69.73  ? 61  TRP   A CH2 1 
ATOM   124  N N   A GLU   A 1 19  ? -23.989 -4.303  -31.433 0.25 69.75  ? 62  GLU   A N   1 
ATOM   125  N N   B GLU   A 1 19  ? -23.989 -4.303  -31.433 0.25 69.75  ? 62  GLU   A N   1 
ATOM   126  N N   C GLU   A 1 19  ? -23.984 -4.292  -31.420 0.25 69.55  ? 62  GLU   A N   1 
ATOM   127  N N   D GLU   A 1 19  ? -23.984 -4.292  -31.420 0.25 69.55  ? 62  GLU   A N   1 
ATOM   128  C CA  A GLU   A 1 19  ? -24.091 -3.694  -32.788 0.25 73.76  ? 62  GLU   A CA  1 
ATOM   129  C CA  B GLU   A 1 19  ? -24.091 -3.694  -32.788 0.25 73.76  ? 62  GLU   A CA  1 
ATOM   130  C CA  C GLU   A 1 19  ? -24.050 -3.749  -32.806 0.25 73.51  ? 62  GLU   A CA  1 
ATOM   131  C CA  D GLU   A 1 19  ? -24.050 -3.749  -32.806 0.25 73.51  ? 62  GLU   A CA  1 
ATOM   132  C C   A GLU   A 1 19  ? -23.245 -4.501  -33.784 0.25 75.62  ? 62  GLU   A C   1 
ATOM   133  C C   B GLU   A 1 19  ? -23.245 -4.501  -33.784 0.25 75.62  ? 62  GLU   A C   1 
ATOM   134  C C   C GLU   A 1 19  ? -23.226 -4.634  -33.750 0.25 75.33  ? 62  GLU   A C   1 
ATOM   135  C C   D GLU   A 1 19  ? -23.226 -4.634  -33.750 0.25 75.33  ? 62  GLU   A C   1 
ATOM   136  O O   A GLU   A 1 19  ? -22.002 -4.450  -33.686 0.25 74.35  ? 62  GLU   A O   1 
ATOM   137  O O   B GLU   A 1 19  ? -22.002 -4.450  -33.686 0.25 74.35  ? 62  GLU   A O   1 
ATOM   138  O O   C GLU   A 1 19  ? -21.995 -4.444  -33.822 0.25 74.32  ? 62  GLU   A O   1 
ATOM   139  O O   D GLU   A 1 19  ? -21.995 -4.444  -33.822 0.25 74.32  ? 62  GLU   A O   1 
ATOM   140  C CB  A GLU   A 1 19  ? -23.657 -2.227  -32.738 0.25 75.20  ? 62  GLU   A CB  1 
ATOM   141  C CB  B GLU   A 1 19  ? -23.657 -2.227  -32.738 0.25 75.20  ? 62  GLU   A CB  1 
ATOM   142  C CB  C GLU   A 1 19  ? -23.556 -2.301  -32.850 0.25 74.82  ? 62  GLU   A CB  1 
ATOM   143  C CB  D GLU   A 1 19  ? -23.556 -2.301  -32.850 0.25 74.82  ? 62  GLU   A CB  1 
ATOM   144  C CG  A GLU   A 1 19  ? -24.328 -1.423  -31.628 0.25 75.50  ? 62  GLU   A CG  1 
ATOM   145  C CG  B GLU   A 1 19  ? -24.328 -1.423  -31.628 0.25 75.50  ? 62  GLU   A CG  1 
ATOM   146  C CG  C GLU   A 1 19  ? -24.586 -1.294  -32.357 0.25 76.21  ? 62  GLU   A CG  1 
ATOM   147  C CG  D GLU   A 1 19  ? -24.586 -1.294  -32.357 0.25 76.21  ? 62  GLU   A CG  1 
ATOM   148  C CD  A GLU   A 1 19  ? -25.732 -0.896  -31.902 0.25 77.57  ? 62  GLU   A CD  1 
ATOM   149  C CD  B GLU   A 1 19  ? -25.732 -0.896  -31.902 0.25 77.57  ? 62  GLU   A CD  1 
ATOM   150  C CD  C GLU   A 1 19  ? -25.845 -1.163  -33.207 0.25 78.59  ? 62  GLU   A CD  1 
ATOM   151  C CD  D GLU   A 1 19  ? -25.845 -1.163  -33.207 0.25 78.59  ? 62  GLU   A CD  1 
ATOM   152  O OE1 A GLU   A 1 19  ? -25.953 -0.338  -33.003 0.25 81.32  ? 62  GLU   A OE1 1 
ATOM   153  O OE1 B GLU   A 1 19  ? -25.953 -0.338  -33.003 0.25 81.32  ? 62  GLU   A OE1 1 
ATOM   154  O OE1 C GLU   A 1 19  ? -25.820 -0.397  -34.209 0.25 79.47  ? 62  GLU   A OE1 1 
ATOM   155  O OE1 D GLU   A 1 19  ? -25.820 -0.397  -34.209 0.25 79.47  ? 62  GLU   A OE1 1 
ATOM   156  O OE2 A GLU   A 1 19  ? -26.601 -1.020  -31.005 0.25 76.48  ? 62  GLU   A OE2 1 
ATOM   157  O OE2 B GLU   A 1 19  ? -26.601 -1.020  -31.005 0.25 76.48  ? 62  GLU   A OE2 1 
ATOM   158  O OE2 C GLU   A 1 19  ? -26.857 -1.821  -32.860 0.25 78.41  ? 62  GLU   A OE2 1 
ATOM   159  O OE2 D GLU   A 1 19  ? -26.857 -1.821  -32.860 0.25 78.41  ? 62  GLU   A OE2 1 
ATOM   160  N N   A LYS   A 1 20  ? -23.899 -5.209  -34.715 0.25 78.41  ? 63  LYS   A N   1 
ATOM   161  N N   B LYS   A 1 20  ? -23.899 -5.209  -34.715 0.25 78.41  ? 63  LYS   A N   1 
ATOM   162  N N   C LYS   A 1 20  ? -23.894 -5.559  -34.448 0.25 78.09  ? 63  LYS   A N   1 
ATOM   163  N N   D LYS   A 1 20  ? -23.894 -5.559  -34.448 0.25 78.09  ? 63  LYS   A N   1 
ATOM   164  C CA  A LYS   A 1 20  ? -23.237 -6.021  -35.775 0.25 80.01  ? 63  LYS   A CA  1 
ATOM   165  C CA  B LYS   A 1 20  ? -23.237 -6.021  -35.775 0.25 80.01  ? 63  LYS   A CA  1 
ATOM   166  C CA  C LYS   A 1 20  ? -23.308 -6.374  -35.547 0.25 79.84  ? 63  LYS   A CA  1 
ATOM   167  C CA  D LYS   A 1 20  ? -23.308 -6.374  -35.547 0.25 79.84  ? 63  LYS   A CA  1 
ATOM   168  C C   A LYS   A 1 20  ? -22.362 -5.100  -36.632 0.25 80.05  ? 63  LYS   A C   1 
ATOM   169  C C   B LYS   A 1 20  ? -22.362 -5.100  -36.632 0.25 80.05  ? 63  LYS   A C   1 
ATOM   170  C C   C LYS   A 1 20  ? -22.641 -5.424  -36.546 0.25 80.13  ? 63  LYS   A C   1 
ATOM   171  C C   D LYS   A 1 20  ? -22.641 -5.424  -36.546 0.25 80.13  ? 63  LYS   A C   1 
ATOM   172  O O   A LYS   A 1 20  ? -22.768 -3.945  -36.862 0.25 80.39  ? 63  LYS   A O   1 
ATOM   173  O O   B LYS   A 1 20  ? -22.768 -3.945  -36.862 0.25 80.39  ? 63  LYS   A O   1 
ATOM   174  O O   C LYS   A 1 20  ? -23.344 -4.540  -37.066 0.25 81.14  ? 63  LYS   A O   1 
ATOM   175  O O   D LYS   A 1 20  ? -23.344 -4.540  -37.066 0.25 81.14  ? 63  LYS   A O   1 
ATOM   176  C CB  A LYS   A 1 20  ? -24.272 -6.751  -36.637 0.25 82.42  ? 63  LYS   A CB  1 
ATOM   177  C CB  B LYS   A 1 20  ? -24.272 -6.751  -36.637 0.25 82.42  ? 63  LYS   A CB  1 
ATOM   178  C CB  C LYS   A 1 20  ? -24.400 -7.197  -36.237 0.25 81.95  ? 63  LYS   A CB  1 
ATOM   179  C CB  D LYS   A 1 20  ? -24.400 -7.197  -36.237 0.25 81.95  ? 63  LYS   A CB  1 
ATOM   180  C CG  A LYS   A 1 20  ? -24.739 -8.095  -36.093 0.25 83.12  ? 63  LYS   A CG  1 
ATOM   181  C CG  B LYS   A 1 20  ? -24.739 -8.095  -36.093 0.25 83.12  ? 63  LYS   A CG  1 
ATOM   182  C CG  C LYS   A 1 20  ? -25.629 -7.477  -35.381 0.25 82.18  ? 63  LYS   A CG  1 
ATOM   183  C CG  D LYS   A 1 20  ? -25.629 -7.477  -35.381 0.25 82.18  ? 63  LYS   A CG  1 
ATOM   184  C CD  A LYS   A 1 20  ? -25.835 -8.736  -36.922 0.25 85.89  ? 63  LYS   A CD  1 
ATOM   185  C CD  B LYS   A 1 20  ? -25.835 -8.736  -36.922 0.25 85.89  ? 63  LYS   A CD  1 
ATOM   186  C CD  C LYS   A 1 20  ? -26.938 -7.329  -36.133 0.25 84.29  ? 63  LYS   A CD  1 
ATOM   187  C CD  D LYS   A 1 20  ? -26.938 -7.329  -36.133 0.25 84.29  ? 63  LYS   A CD  1 
ATOM   188  C CE  A LYS   A 1 20  ? -26.190 -10.136 -36.464 0.25 86.30  ? 63  LYS   A CE  1 
ATOM   189  C CE  B LYS   A 1 20  ? -26.190 -10.136 -36.464 0.25 86.30  ? 63  LYS   A CE  1 
ATOM   190  C CE  C LYS   A 1 20  ? -27.296 -8.547  -36.956 0.25 86.57  ? 63  LYS   A CE  1 
ATOM   191  C CE  D LYS   A 1 20  ? -27.296 -8.547  -36.956 0.25 86.57  ? 63  LYS   A CE  1 
ATOM   192  N NZ  A LYS   A 1 20  ? -27.451 -10.610 -37.082 0.25 88.14  ? 63  LYS   A NZ  1 
ATOM   193  N NZ  B LYS   A 1 20  ? -27.451 -10.610 -37.082 0.25 88.14  ? 63  LYS   A NZ  1 
ATOM   194  N NZ  C LYS   A 1 20  ? -27.969 -9.577  -36.130 0.25 86.20  ? 63  LYS   A NZ  1 
ATOM   195  N NZ  D LYS   A 1 20  ? -27.969 -9.577  -36.130 0.25 86.20  ? 63  LYS   A NZ  1 
ATOM   196  N N   A ASP   A 1 21  ? -21.205 -5.596  -37.073 0.25 80.65  ? 64  ASP   A N   1 
ATOM   197  N N   B ASP   A 1 21  ? -21.205 -5.596  -37.073 0.25 80.65  ? 64  ASP   A N   1 
ATOM   198  N N   C ASP   A 1 21  ? -21.337 -5.584  -36.778 0.25 80.23  ? 64  ASP   A N   1 
ATOM   199  N N   D ASP   A 1 21  ? -21.337 -5.584  -36.778 0.25 80.23  ? 64  ASP   A N   1 
ATOM   200  C CA  A ASP   A 1 21  ? -20.218 -4.830  -37.882 0.25 82.46  ? 64  ASP   A CA  1 
ATOM   201  C CA  B ASP   A 1 21  ? -20.218 -4.830  -37.882 0.25 82.46  ? 64  ASP   A CA  1 
ATOM   202  C CA  C ASP   A 1 21  ? -20.558 -4.763  -37.744 0.25 82.37  ? 64  ASP   A CA  1 
ATOM   203  C CA  D ASP   A 1 21  ? -20.558 -4.763  -37.744 0.25 82.37  ? 64  ASP   A CA  1 
ATOM   204  C C   A ASP   A 1 21  ? -19.807 -3.567  -37.110 0.25 79.99  ? 64  ASP   A C   1 
ATOM   205  C C   B ASP   A 1 21  ? -19.807 -3.567  -37.110 0.25 79.99  ? 64  ASP   A C   1 
ATOM   206  C C   C ASP   A 1 21  ? -19.974 -3.533  -37.026 0.25 79.95  ? 64  ASP   A C   1 
ATOM   207  C C   D ASP   A 1 21  ? -19.974 -3.533  -37.026 0.25 79.95  ? 64  ASP   A C   1 
ATOM   208  O O   A ASP   A 1 21  ? -19.950 -2.460  -37.664 0.25 79.95  ? 64  ASP   A O   1 
ATOM   209  O O   B ASP   A 1 21  ? -19.950 -2.460  -37.664 0.25 79.95  ? 64  ASP   A O   1 
ATOM   210  O O   C ASP   A 1 21  ? -20.160 -2.412  -37.537 0.25 79.97  ? 64  ASP   A O   1 
ATOM   211  O O   D ASP   A 1 21  ? -20.160 -2.412  -37.537 0.25 79.97  ? 64  ASP   A O   1 
ATOM   212  C CB  A ASP   A 1 21  ? -20.771 -4.489  -39.273 0.25 86.50  ? 64  ASP   A CB  1 
ATOM   213  C CB  B ASP   A 1 21  ? -20.771 -4.489  -39.273 0.25 86.50  ? 64  ASP   A CB  1 
ATOM   214  C CB  C ASP   A 1 21  ? -21.431 -4.357  -38.941 0.25 86.35  ? 64  ASP   A CB  1 
ATOM   215  C CB  D ASP   A 1 21  ? -21.431 -4.357  -38.941 0.25 86.35  ? 64  ASP   A CB  1 
ATOM   216  C CG  A ASP   A 1 21  ? -20.621 -5.592  -40.312 0.25 88.86  ? 64  ASP   A CG  1 
ATOM   217  C CG  B ASP   A 1 21  ? -20.621 -5.592  -40.312 0.25 88.86  ? 64  ASP   A CG  1 
ATOM   218  C CG  C ASP   A 1 21  ? -22.005 -5.516  -39.751 0.25 88.09  ? 64  ASP   A CG  1 
ATOM   219  C CG  D ASP   A 1 21  ? -22.005 -5.516  -39.751 0.25 88.09  ? 64  ASP   A CG  1 
ATOM   220  O OD1 A ASP   A 1 21  ? -19.470 -6.019  -40.563 0.25 88.72  ? 64  ASP   A OD1 1 
ATOM   221  O OD1 B ASP   A 1 21  ? -19.470 -6.019  -40.563 0.25 88.72  ? 64  ASP   A OD1 1 
ATOM   222  O OD1 C ASP   A 1 21  ? -21.419 -6.624  -39.704 0.25 89.61  ? 64  ASP   A OD1 1 
ATOM   223  O OD1 D ASP   A 1 21  ? -21.419 -6.624  -39.704 0.25 89.61  ? 64  ASP   A OD1 1 
ATOM   224  O OD2 A ASP   A 1 21  ? -21.658 -6.011  -40.872 0.25 90.27  ? 64  ASP   A OD2 1 
ATOM   225  O OD2 B ASP   A 1 21  ? -21.658 -6.011  -40.872 0.25 90.27  ? 64  ASP   A OD2 1 
ATOM   226  O OD2 C ASP   A 1 21  ? -23.038 -5.300  -40.430 0.25 87.74  ? 64  ASP   A OD2 1 
ATOM   227  O OD2 D ASP   A 1 21  ? -23.038 -5.300  -40.430 0.25 87.74  ? 64  ASP   A OD2 1 
ATOM   228  N N   . ALA   A 1 22  ? -19.302 -3.735  -35.881 1.00 77.71  ? 65  ALA   A N   1 
ATOM   229  C CA  . ALA   A 1 22  ? -18.609 -2.657  -35.123 1.00 72.48  ? 65  ALA   A CA  1 
ATOM   230  C C   . ALA   A 1 22  ? -17.093 -2.797  -35.358 1.00 69.50  ? 65  ALA   A C   1 
ATOM   231  O O   . ALA   A 1 22  ? -16.631 -3.913  -35.716 1.00 69.33  ? 65  ALA   A O   1 
ATOM   232  C CB  . ALA   A 1 22  ? -18.947 -2.733  -33.661 1.00 72.23  ? 65  ALA   A CB  1 
ATOM   233  N N   A GLU   A 1 23  ? -16.385 -1.666  -35.155 0.25 70.79  ? 66  GLU   A N   1 
ATOM   234  N N   B GLU   A 1 23  ? -16.385 -1.666  -35.155 0.25 70.79  ? 66  GLU   A N   1 
ATOM   235  N N   C GLU   A 1 23  ? -16.332 -1.707  -35.156 0.25 68.13  ? 66  GLU   A N   1 
ATOM   236  N N   D GLU   A 1 23  ? -16.332 -1.707  -35.156 0.25 68.13  ? 66  GLU   A N   1 
ATOM   237  C CA  A GLU   A 1 23  ? -14.921 -1.464  -35.346 0.25 72.16  ? 66  GLU   A CA  1 
ATOM   238  C CA  B GLU   A 1 23  ? -14.921 -1.464  -35.346 0.25 72.16  ? 66  GLU   A CA  1 
ATOM   239  C CA  C GLU   A 1 23  ? -14.845 -1.722  -35.252 0.25 67.53  ? 66  GLU   A CA  1 
ATOM   240  C CA  D GLU   A 1 23  ? -14.845 -1.722  -35.252 0.25 67.53  ? 66  GLU   A CA  1 
ATOM   241  C C   A GLU   A 1 23  ? -14.159 -2.436  -34.435 0.25 71.16  ? 66  GLU   A C   1 
ATOM   242  C C   B GLU   A 1 23  ? -14.159 -2.436  -34.435 0.25 71.16  ? 66  GLU   A C   1 
ATOM   243  C C   C GLU   A 1 23  ? -14.309 -2.840  -34.347 0.25 66.17  ? 66  GLU   A C   1 
ATOM   244  C C   D GLU   A 1 23  ? -14.309 -2.840  -34.347 0.25 66.17  ? 66  GLU   A C   1 
ATOM   245  O O   A GLU   A 1 23  ? -13.949 -2.106  -33.244 0.25 69.64  ? 66  GLU   A O   1 
ATOM   246  O O   B GLU   A 1 23  ? -13.949 -2.106  -33.244 0.25 69.64  ? 66  GLU   A O   1 
ATOM   247  O O   C GLU   A 1 23  ? -14.613 -2.826  -33.132 0.25 61.11  ? 66  GLU   A O   1 
ATOM   248  O O   D GLU   A 1 23  ? -14.613 -2.826  -33.132 0.25 61.11  ? 66  GLU   A O   1 
ATOM   249  C CB  A GLU   A 1 23  ? -14.609 0.010   -35.055 0.25 73.66  ? 66  GLU   A CB  1 
ATOM   250  C CB  B GLU   A 1 23  ? -14.609 0.010   -35.055 0.25 73.66  ? 66  GLU   A CB  1 
ATOM   251  C CB  C GLU   A 1 23  ? -14.269 -0.359  -34.865 0.25 67.92  ? 66  GLU   A CB  1 
ATOM   252  C CB  D GLU   A 1 23  ? -14.269 -0.359  -34.865 0.25 67.92  ? 66  GLU   A CB  1 
ATOM   253  C CG  A GLU   A 1 23  ? -13.180 0.448   -35.339 0.25 75.62  ? 66  GLU   A CG  1 
ATOM   254  C CG  B GLU   A 1 23  ? -13.180 0.448   -35.339 0.25 75.62  ? 66  GLU   A CG  1 
ATOM   255  C CG  C GLU   A 1 23  ? -12.762 -0.360  -34.680 0.25 67.95  ? 66  GLU   A CG  1 
ATOM   256  C CG  D GLU   A 1 23  ? -12.762 -0.360  -34.680 0.25 67.95  ? 66  GLU   A CG  1 
ATOM   257  C CD  A GLU   A 1 23  ? -13.057 1.927   -35.688 0.25 77.25  ? 66  GLU   A CD  1 
ATOM   258  C CD  B GLU   A 1 23  ? -13.057 1.927   -35.688 0.25 77.25  ? 66  GLU   A CD  1 
ATOM   259  C CD  C GLU   A 1 23  ? -12.232 0.929   -34.078 0.25 68.46  ? 66  GLU   A CD  1 
ATOM   260  C CD  D GLU   A 1 23  ? -12.232 0.929   -34.078 0.25 68.46  ? 66  GLU   A CD  1 
ATOM   261  O OE1 A GLU   A 1 23  ? -13.310 2.285   -36.862 0.25 79.03  ? 66  GLU   A OE1 1 
ATOM   262  O OE1 B GLU   A 1 23  ? -13.310 2.285   -36.862 0.25 79.03  ? 66  GLU   A OE1 1 
ATOM   263  O OE1 C GLU   A 1 23  ? -13.065 1.931   -33.984 0.25 68.16  ? 66  GLU   A OE1 1 
ATOM   264  O OE1 D GLU   A 1 23  ? -13.065 1.931   -33.984 0.25 68.16  ? 66  GLU   A OE1 1 
ATOM   265  O OE2 A GLU   A 1 23  ? -12.735 2.725   -34.781 0.25 76.62  ? 66  GLU   A OE2 1 
ATOM   266  O OE2 B GLU   A 1 23  ? -12.735 2.725   -34.781 0.25 76.62  ? 66  GLU   A OE2 1 
ATOM   267  O OE2 C GLU   A 1 23  ? -10.993 0.934   -33.705 0.25 69.07  ? 66  GLU   A OE2 1 
ATOM   268  O OE2 D GLU   A 1 23  ? -10.993 0.934   -33.705 0.25 69.07  ? 66  GLU   A OE2 1 
ATOM   269  N N   A VAL   A 1 24  ? -13.798 -3.613  -34.962 0.25 70.80  ? 67  VAL   A N   1 
ATOM   270  N N   B VAL   A 1 24  ? -13.798 -3.613  -34.962 0.25 70.80  ? 67  VAL   A N   1 
ATOM   271  N N   C VAL   A 1 24  ? -13.579 -3.800  -34.925 0.25 66.53  ? 67  VAL   A N   1 
ATOM   272  N N   D VAL   A 1 24  ? -13.579 -3.800  -34.925 0.25 66.53  ? 67  VAL   A N   1 
ATOM   273  C CA  A VAL   A 1 24  ? -13.111 -4.699  -34.199 0.25 68.39  ? 67  VAL   A CA  1 
ATOM   274  C CA  B VAL   A 1 24  ? -13.111 -4.699  -34.199 0.25 68.39  ? 67  VAL   A CA  1 
ATOM   275  C CA  C VAL   A 1 24  ? -13.035 -4.987  -34.198 0.25 65.05  ? 67  VAL   A CA  1 
ATOM   276  C CA  D VAL   A 1 24  ? -13.035 -4.987  -34.198 0.25 65.05  ? 67  VAL   A CA  1 
ATOM   277  C C   A VAL   A 1 24  ? -11.632 -4.324  -34.046 0.25 67.67  ? 67  VAL   A C   1 
ATOM   278  C C   B VAL   A 1 24  ? -11.632 -4.324  -34.046 0.25 67.67  ? 67  VAL   A C   1 
ATOM   279  C C   C VAL   A 1 24  ? -11.526 -4.792  -34.014 0.25 65.09  ? 67  VAL   A C   1 
ATOM   280  C C   D VAL   A 1 24  ? -11.526 -4.792  -34.014 0.25 65.09  ? 67  VAL   A C   1 
ATOM   281  O O   A VAL   A 1 24  ? -11.024 -3.896  -35.038 0.25 67.11  ? 67  VAL   A O   1 
ATOM   282  O O   B VAL   A 1 24  ? -11.024 -3.896  -35.038 0.25 67.11  ? 67  VAL   A O   1 
ATOM   283  O O   C VAL   A 1 24  ? -10.779 -5.038  -34.968 0.25 65.01  ? 67  VAL   A O   1 
ATOM   284  O O   D VAL   A 1 24  ? -10.779 -5.038  -34.968 0.25 65.01  ? 67  VAL   A O   1 
ATOM   285  C CB  A VAL   A 1 24  ? -13.271 -6.076  -34.872 0.25 69.21  ? 67  VAL   A CB  1 
ATOM   286  C CB  B VAL   A 1 24  ? -13.271 -6.076  -34.872 0.25 69.21  ? 67  VAL   A CB  1 
ATOM   287  C CB  C VAL   A 1 24  ? -13.357 -6.305  -34.929 0.25 66.10  ? 67  VAL   A CB  1 
ATOM   288  C CB  D VAL   A 1 24  ? -13.357 -6.305  -34.929 0.25 66.10  ? 67  VAL   A CB  1 
ATOM   289  C CG1 A VAL   A 1 24  ? -12.633 -7.173  -34.038 0.25 68.14  ? 67  VAL   A CG1 1 
ATOM   290  C CG1 B VAL   A 1 24  ? -12.633 -7.173  -34.038 0.25 68.14  ? 67  VAL   A CG1 1 
ATOM   291  C CG1 C VAL   A 1 24  ? -12.869 -7.506  -34.140 0.25 65.12  ? 67  VAL   A CG1 1 
ATOM   292  C CG1 D VAL   A 1 24  ? -12.869 -7.506  -34.140 0.25 65.12  ? 67  VAL   A CG1 1 
ATOM   293  C CG2 A VAL   A 1 24  ? -14.727 -6.409  -35.165 0.25 69.53  ? 67  VAL   A CG2 1 
ATOM   294  C CG2 B VAL   A 1 24  ? -14.727 -6.409  -35.165 0.25 69.53  ? 67  VAL   A CG2 1 
ATOM   295  C CG2 C VAL   A 1 24  ? -14.840 -6.442  -35.237 0.25 66.40  ? 67  VAL   A CG2 1 
ATOM   296  C CG2 D VAL   A 1 24  ? -14.840 -6.442  -35.237 0.25 66.40  ? 67  VAL   A CG2 1 
ATOM   297  N N   A THR   A 1 25  ? -11.082 -4.471  -32.837 0.25 65.87  ? 68  THR   A N   1 
ATOM   298  N N   B THR   A 1 25  ? -11.082 -4.471  -32.837 0.25 65.87  ? 68  THR   A N   1 
ATOM   299  N N   C THR   A 1 25  ? -11.106 -4.358  -32.821 0.25 63.93  ? 68  THR   A N   1 
ATOM   300  N N   D THR   A 1 25  ? -11.106 -4.358  -32.821 0.25 63.93  ? 68  THR   A N   1 
ATOM   301  C CA  A THR   A 1 25  ? -9.700  -4.047  -32.492 0.25 65.61  ? 68  THR   A CA  1 
ATOM   302  C CA  B THR   A 1 25  ? -9.700  -4.047  -32.492 0.25 65.61  ? 68  THR   A CA  1 
ATOM   303  C CA  C THR   A 1 25  ? -9.697  -4.013  -32.491 0.25 64.20  ? 68  THR   A CA  1 
ATOM   304  C CA  D THR   A 1 25  ? -9.697  -4.013  -32.491 0.25 64.20  ? 68  THR   A CA  1 
ATOM   305  C C   A THR   A 1 25  ? -9.377  -4.488  -31.060 0.25 63.68  ? 68  THR   A C   1 
ATOM   306  C C   B THR   A 1 25  ? -9.377  -4.488  -31.060 0.25 63.68  ? 68  THR   A C   1 
ATOM   307  C C   C THR   A 1 25  ? -9.379  -4.477  -31.065 0.25 62.85  ? 68  THR   A C   1 
ATOM   308  C C   D THR   A 1 25  ? -9.379  -4.477  -31.065 0.25 62.85  ? 68  THR   A C   1 
ATOM   309  O O   A THR   A 1 25  ? -10.270 -5.071  -30.418 0.25 61.68  ? 68  THR   A O   1 
ATOM   310  O O   B THR   A 1 25  ? -10.270 -5.071  -30.418 0.25 61.68  ? 68  THR   A O   1 
ATOM   311  O O   C THR   A 1 25  ? -10.274 -5.066  -30.432 0.25 60.89  ? 68  THR   A O   1 
ATOM   312  O O   D THR   A 1 25  ? -10.274 -5.066  -30.432 0.25 60.89  ? 68  THR   A O   1 
ATOM   313  C CB  A THR   A 1 25  ? -9.550  -2.532  -32.672 0.25 66.76  ? 68  THR   A CB  1 
ATOM   314  C CB  B THR   A 1 25  ? -9.550  -2.532  -32.672 0.25 66.76  ? 68  THR   A CB  1 
ATOM   315  C CB  C THR   A 1 25  ? -9.456  -2.508  -32.669 0.25 65.33  ? 68  THR   A CB  1 
ATOM   316  C CB  D THR   A 1 25  ? -9.456  -2.508  -32.669 0.25 65.33  ? 68  THR   A CB  1 
ATOM   317  O OG1 A THR   A 1 25  ? -8.167  -2.198  -32.560 0.25 67.43  ? 68  THR   A OG1 1 
ATOM   318  O OG1 B THR   A 1 25  ? -8.167  -2.198  -32.560 0.25 67.43  ? 68  THR   A OG1 1 
ATOM   319  O OG1 C THR   A 1 25  ? -8.048  -2.279  -32.623 0.25 66.08  ? 68  THR   A OG1 1 
ATOM   320  O OG1 D THR   A 1 25  ? -8.048  -2.279  -32.623 0.25 66.08  ? 68  THR   A OG1 1 
ATOM   321  C CG2 A THR   A 1 25  ? -10.361 -1.741  -31.668 0.25 65.67  ? 68  THR   A CG2 1 
ATOM   322  C CG2 B THR   A 1 25  ? -10.361 -1.741  -31.668 0.25 65.67  ? 68  THR   A CG2 1 
ATOM   323  C CG2 C THR   A 1 25  ? -10.154 -1.670  -31.620 0.25 64.21  ? 68  THR   A CG2 1 
ATOM   324  C CG2 D THR   A 1 25  ? -10.154 -1.670  -31.620 0.25 64.21  ? 68  THR   A CG2 1 
ATOM   325  N N   . GLY   A 1 26  ? -8.154  -4.207  -30.594 1.00 63.22  ? 69  GLY   A N   1 
ATOM   326  C CA  . GLY   A 1 26  ? -7.644  -4.656  -29.284 1.00 62.05  ? 69  GLY   A CA  1 
ATOM   327  C C   . GLY   A 1 26  ? -6.975  -6.021  -29.384 1.00 62.49  ? 69  GLY   A C   1 
ATOM   328  O O   . GLY   A 1 26  ? -7.454  -6.836  -30.170 1.00 65.09  ? 69  GLY   A O   1 
ATOM   329  N N   . ASN   A 1 27  ? -5.918  -6.252  -28.606 1.00 63.05  ? 70  ASN   A N   1 
ATOM   330  C CA  . ASN   A 1 27  ? -5.282  -7.585  -28.354 1.00 65.87  ? 70  ASN   A CA  1 
ATOM   331  C C   . ASN   A 1 27  ? -5.919  -8.295  -27.121 1.00 60.25  ? 70  ASN   A C   1 
ATOM   332  O O   . ASN   A 1 27  ? -6.962  -7.796  -26.606 1.00 55.40  ? 70  ASN   A O   1 
ATOM   333  C CB  . ASN   A 1 27  ? -3.757  -7.414  -28.271 1.00 70.18  ? 70  ASN   A CB  1 
ATOM   334  C CG  . ASN   A 1 27  ? -3.328  -6.479  -27.156 1.00 74.38  ? 70  ASN   A CG  1 
ATOM   335  O OD1 . ASN   A 1 27  ? -3.824  -5.353  -27.048 1.00 81.95  ? 70  ASN   A OD1 1 
ATOM   336  N ND2 . ASN   A 1 27  ? -2.404  -6.922  -26.319 1.00 76.99  ? 70  ASN   A ND2 1 
ATOM   337  N N   . SER   A 1 28  ? -5.387  -9.468  -26.711 1.00 58.69  ? 71  SER   A N   1 
ATOM   338  C CA  . SER   A 1 28  ? -5.904  -10.348 -25.611 1.00 58.99  ? 71  SER   A CA  1 
ATOM   339  C C   . SER   A 1 28  ? -4.776  -10.763 -24.680 1.00 59.29  ? 71  SER   A C   1 
ATOM   340  O O   . SER   A 1 28  ? -4.493  -11.946 -24.592 1.00 64.30  ? 71  SER   A O   1 
ATOM   341  C CB  . SER   A 1 28  ? -6.545  -11.628 -26.111 1.00 60.10  ? 71  SER   A CB  1 
ATOM   342  O OG  . SER   A 1 28  ? -7.621  -11.391 -26.996 1.00 64.56  ? 71  SER   A OG  1 
ATOM   343  N N   . PRO   A 1 29  ? -4.095  -9.855  -23.956 1.00 59.76  ? 72  PRO   A N   1 
ATOM   344  C CA  . PRO   A 1 29  ? -2.923  -10.246 -23.175 1.00 61.57  ? 72  PRO   A CA  1 
ATOM   345  C C   . PRO   A 1 29  ? -3.297  -11.013 -21.895 1.00 60.98  ? 72  PRO   A C   1 
ATOM   346  O O   . PRO   A 1 29  ? -4.322  -10.661 -21.262 1.00 58.22  ? 72  PRO   A O   1 
ATOM   347  C CB  . PRO   A 1 29  ? -2.243  -8.890  -22.901 1.00 63.14  ? 72  PRO   A CB  1 
ATOM   348  C CG  . PRO   A 1 29  ? -3.405  -7.905  -22.814 1.00 62.21  ? 72  PRO   A CG  1 
ATOM   349  C CD  . PRO   A 1 29  ? -4.420  -8.428  -23.816 1.00 62.72  ? 72  PRO   A CD  1 
ATOM   350  N N   . ARG   A 1 30  ? -2.497  -12.035 -21.554 1.00 64.07  ? 73  ARG   A N   1 
ATOM   351  C CA  . ARG   A 1 30  ? -2.538  -12.750 -20.243 1.00 70.05  ? 73  ARG   A CA  1 
ATOM   352  C C   . ARG   A 1 30  ? -1.507  -12.103 -19.310 1.00 67.12  ? 73  ARG   A C   1 
ATOM   353  O O   . ARG   A 1 30  ? -0.327  -12.220 -19.614 1.00 66.18  ? 73  ARG   A O   1 
ATOM   354  C CB  . ARG   A 1 30  ? -2.285  -14.254 -20.397 1.00 78.40  ? 73  ARG   A CB  1 
ATOM   355  C CG  . ARG   A 1 30  ? -3.438  -15.003 -21.054 1.00 88.26  ? 73  ARG   A CG  1 
ATOM   356  C CD  . ARG   A 1 30  ? -3.078  -16.372 -21.634 1.00 100.44 ? 73  ARG   A CD  1 
ATOM   357  N NE  . ARG   A 1 30  ? -4.096  -16.876 -22.573 1.00 108.69 ? 73  ARG   A NE  1 
ATOM   358  C CZ  . ARG   A 1 30  ? -4.910  -17.926 -22.379 1.00 111.17 ? 73  ARG   A CZ  1 
ATOM   359  N NH1 . ARG   A 1 30  ? -4.847  -18.643 -21.267 1.00 116.37 ? 73  ARG   A NH1 1 
ATOM   360  N NH2 . ARG   A 1 30  ? -5.794  -18.260 -23.308 1.00 104.46 ? 73  ARG   A NH2 1 
ATOM   361  N N   . LEU   A 1 31  ? -1.958  -11.434 -18.236 1.00 64.24  ? 74  LEU   A N   1 
ATOM   362  C CA  . LEU   A 1 31  ? -1.120  -10.590 -17.346 1.00 62.99  ? 74  LEU   A CA  1 
ATOM   363  C C   . LEU   A 1 31  ? -1.261  -11.093 -15.899 1.00 62.38  ? 74  LEU   A C   1 
ATOM   364  O O   . LEU   A 1 31  ? -2.399  -11.346 -15.474 1.00 59.57  ? 74  LEU   A O   1 
ATOM   365  C CB  . LEU   A 1 31  ? -1.572  -9.129  -17.466 1.00 64.81  ? 74  LEU   A CB  1 
ATOM   366  C CG  . LEU   A 1 31  ? -1.310  -8.422  -18.801 1.00 65.63  ? 74  LEU   A CG  1 
ATOM   367  C CD1 . LEU   A 1 31  ? -1.983  -7.061  -18.802 1.00 64.67  ? 74  LEU   A CD1 1 
ATOM   368  C CD2 . LEU   A 1 31  ? 0.191   -8.274  -19.095 1.00 66.49  ? 74  LEU   A CD2 1 
ATOM   369  N N   . ASP   A 1 32  ? -0.136  -11.226 -15.190 1.00 59.33  ? 75  ASP   A N   1 
ATOM   370  C CA  . ASP   A 1 32  ? -0.079  -11.487 -13.734 1.00 59.95  ? 75  ASP   A CA  1 
ATOM   371  C C   . ASP   A 1 32  ? -0.265  -10.186 -12.960 1.00 55.25  ? 75  ASP   A C   1 
ATOM   372  O O   . ASP   A 1 32  ? 0.638   -9.298  -13.060 1.00 54.65  ? 75  ASP   A O   1 
ATOM   373  C CB  . ASP   A 1 32  ? 1.264   -12.094 -13.354 1.00 65.44  ? 75  ASP   A CB  1 
ATOM   374  C CG  . ASP   A 1 32  ? 1.386   -13.540 -13.779 1.00 68.62  ? 75  ASP   A CG  1 
ATOM   375  O OD1 . ASP   A 1 32  ? 0.346   -14.254 -13.780 1.00 68.52  ? 75  ASP   A OD1 1 
ATOM   376  O OD2 . ASP   A 1 32  ? 2.515   -13.926 -14.108 1.00 76.92  ? 75  ASP   A OD2 1 
ATOM   377  N N   . VAL   A 1 33  ? -1.380  -10.075 -12.226 1.00 52.76  ? 76  VAL   A N   1 
ATOM   378  C CA  . VAL   A 1 33  ? -1.768  -8.817  -11.514 1.00 53.50  ? 76  VAL   A CA  1 
ATOM   379  C C   . VAL   A 1 33  ? -2.035  -9.130  -10.023 1.00 53.65  ? 76  VAL   A C   1 
ATOM   380  O O   . VAL   A 1 33  ? -2.340  -10.304 -9.674  1.00 53.18  ? 76  VAL   A O   1 
ATOM   381  C CB  . VAL   A 1 33  ? -2.950  -8.098  -12.202 1.00 52.16  ? 76  VAL   A CB  1 
ATOM   382  C CG1 . VAL   A 1 33  ? -2.721  -7.913  -13.686 1.00 53.66  ? 76  VAL   A CG1 1 
ATOM   383  C CG2 . VAL   A 1 33  ? -4.270  -8.812  -11.975 1.00 52.10  ? 76  VAL   A CG2 1 
ATOM   384  N N   . ALA   A 1 34  ? -1.894  -8.113  -9.173  1.00 52.66  ? 77  ALA   A N   1 
ATOM   385  C CA  . ALA   A 1 34  ? -2.189  -8.134  -7.715  1.00 52.86  ? 77  ALA   A CA  1 
ATOM   386  C C   . ALA   A 1 34  ? -3.255  -7.074  -7.467  1.00 50.39  ? 77  ALA   A C   1 
ATOM   387  O O   . ALA   A 1 34  ? -3.190  -6.045  -8.131  1.00 51.09  ? 77  ALA   A O   1 
ATOM   388  C CB  . ALA   A 1 34  ? -0.942  -7.857  -6.921  1.00 52.91  ? 77  ALA   A CB  1 
ATOM   389  N N   . LEU   A 1 35  ? -4.252  -7.367  -6.653  1.00 48.40  ? 78  LEU   A N   1 
ATOM   390  C CA  . LEU   A 1 35  ? -5.283  -6.372  -6.281  1.00 49.27  ? 78  LEU   A CA  1 
ATOM   391  C C   . LEU   A 1 35  ? -5.053  -5.964  -4.821  1.00 50.59  ? 78  LEU   A C   1 
ATOM   392  O O   . LEU   A 1 35  ? -5.070  -6.849  -3.959  1.00 53.37  ? 78  LEU   A O   1 
ATOM   393  C CB  . LEU   A 1 35  ? -6.671  -6.976  -6.497  1.00 48.35  ? 78  LEU   A CB  1 
ATOM   394  C CG  . LEU   A 1 35  ? -7.840  -6.032  -6.205  1.00 47.61  ? 78  LEU   A CG  1 
ATOM   395  C CD1 . LEU   A 1 35  ? -7.657  -4.687  -6.886  1.00 47.43  ? 78  LEU   A CD1 1 
ATOM   396  C CD2 . LEU   A 1 35  ? -9.149  -6.675  -6.615  1.00 45.97  ? 78  LEU   A CD2 1 
ATOM   397  N N   . ASP   A 1 36  ? -4.804  -4.679  -4.577  1.00 51.82  ? 79  ASP   A N   1 
ATOM   398  C CA  . ASP   A 1 36  ? -4.544  -4.109  -3.234  1.00 51.86  ? 79  ASP   A CA  1 
ATOM   399  C C   . ASP   A 1 36  ? -5.885  -3.754  -2.555  1.00 51.61  ? 79  ASP   A C   1 
ATOM   400  O O   . ASP   A 1 36  ? -6.958  -3.764  -3.218  1.00 51.19  ? 79  ASP   A O   1 
ATOM   401  C CB  . ASP   A 1 36  ? -3.531  -2.957  -3.341  1.00 53.30  ? 79  ASP   A CB  1 
ATOM   402  C CG  . ASP   A 1 36  ? -4.087  -1.578  -3.670  1.00 55.62  ? 79  ASP   A CG  1 
ATOM   403  O OD1 . ASP   A 1 36  ? -5.307  -1.459  -3.942  1.00 54.42  ? 79  ASP   A OD1 1 
ATOM   404  O OD2 . ASP   A 1 36  ? -3.281  -0.617  -3.653  1.00 60.07  ? 79  ASP   A OD2 1 
ATOM   405  N N   . GLU   A 1 37  ? -5.812  -3.420  -1.262  1.00 52.50  ? 80  GLU   A N   1 
ATOM   406  C CA  . GLU   A 1 37  ? -6.983  -3.136  -0.404  1.00 53.30  ? 80  GLU   A CA  1 
ATOM   407  C C   . GLU   A 1 37  ? -7.697  -1.878  -0.935  1.00 50.75  ? 80  GLU   A C   1 
ATOM   408  O O   . GLU   A 1 37  ? -8.940  -1.798  -0.783  1.00 47.90  ? 80  GLU   A O   1 
ATOM   409  C CB  . GLU   A 1 37  ? -6.528  -3.047  1.060   1.00 56.66  ? 80  GLU   A CB  1 
ATOM   410  C CG  . GLU   A 1 37  ? -7.687  -3.179  2.036   1.00 62.01  ? 80  GLU   A CG  1 
ATOM   411  C CD  . GLU   A 1 37  ? -7.397  -3.040  3.534   1.00 64.49  ? 80  GLU   A CD  1 
ATOM   412  O OE1 . GLU   A 1 37  ? -6.982  -1.943  3.993   1.00 65.22  ? 80  GLU   A OE1 1 
ATOM   413  O OE2 . GLU   A 1 37  ? -7.599  -4.035  4.247   1.00 70.67  ? 80  GLU   A OE2 1 
ATOM   414  N N   . SER   A 1 38  ? -6.970  -0.949  -1.567  1.00 49.56  ? 81  SER   A N   1 
ATOM   415  C CA  . SER   A 1 38  ? -7.532  0.291   -2.152  1.00 51.20  ? 81  SER   A CA  1 
ATOM   416  C C   . SER   A 1 38  ? -8.173  0.026   -3.517  1.00 50.11  ? 81  SER   A C   1 
ATOM   417  O O   . SER   A 1 38  ? -8.561  1.028   -4.152  1.00 51.73  ? 81  SER   A O   1 
ATOM   418  C CB  . SER   A 1 38  ? -6.485  1.344   -2.288  1.00 54.44  ? 81  SER   A CB  1 
ATOM   419  O OG  . SER   A 1 38  ? -5.863  1.556   -1.046  1.00 60.45  ? 81  SER   A OG  1 
ATOM   420  N N   . GLY   A 1 39  ? -8.289  -1.234  -3.965  1.00 47.87  ? 82  GLY   A N   1 
ATOM   421  C CA  . GLY   A 1 39  ? -8.919  -1.538  -5.270  1.00 49.41  ? 82  GLY   A CA  1 
ATOM   422  C C   . GLY   A 1 39  ? -8.054  -1.133  -6.472  1.00 48.42  ? 82  GLY   A C   1 
ATOM   423  O O   . GLY   A 1 39  ? -8.594  -1.072  -7.566  1.00 49.50  ? 82  GLY   A O   1 
ATOM   424  N N   . ASP   A 1 40  ? -6.740  -0.955  -6.286  1.00 49.83  ? 83  ASP   A N   1 
ATOM   425  C CA  . ASP   A 1 40  ? -5.734  -0.666  -7.339  1.00 51.51  ? 83  ASP   A CA  1 
ATOM   426  C C   . ASP   A 1 40  ? -5.055  -1.980  -7.753  1.00 50.23  ? 83  ASP   A C   1 
ATOM   427  O O   . ASP   A 1 40  ? -4.473  -2.666  -6.895  1.00 48.85  ? 83  ASP   A O   1 
ATOM   428  C CB  . ASP   A 1 40  ? -4.760  0.419   -6.857  1.00 55.23  ? 83  ASP   A CB  1 
ATOM   429  C CG  . ASP   A 1 40  ? -5.457  1.755   -6.619  1.00 60.41  ? 83  ASP   A CG  1 
ATOM   430  O OD1 . ASP   A 1 40  ? -6.546  1.977   -7.195  1.00 66.40  ? 83  ASP   A OD1 1 
ATOM   431  O OD2 . ASP   A 1 40  ? -4.926  2.567   -5.870  1.00 66.99  ? 83  ASP   A OD2 1 
ATOM   432  N N   . PHE   A 1 41  ? -5.102  -2.300  -9.049  1.00 49.36  ? 84  PHE   A N   1 
ATOM   433  C CA  . PHE   A 1 41  ? -4.361  -3.436  -9.652  1.00 47.76  ? 84  PHE   A CA  1 
ATOM   434  C C   . PHE   A 1 41  ? -2.911  -3.038  -9.888  1.00 52.04  ? 84  PHE   A C   1 
ATOM   435  O O   . PHE   A 1 41  ? -2.638  -1.847  -10.088 1.00 53.79  ? 84  PHE   A O   1 
ATOM   436  C CB  . PHE   A 1 41  ? -4.952  -3.849  -10.989 1.00 44.41  ? 84  PHE   A CB  1 
ATOM   437  C CG  . PHE   A 1 41  ? -6.239  -4.616  -10.921 1.00 42.64  ? 84  PHE   A CG  1 
ATOM   438  C CD1 . PHE   A 1 41  ? -6.241  -5.941  -10.560 1.00 42.39  ? 84  PHE   A CD1 1 
ATOM   439  C CD2 . PHE   A 1 41  ? -7.459  -4.009  -11.220 1.00 42.63  ? 84  PHE   A CD2 1 
ATOM   440  C CE1 . PHE   A 1 41  ? -7.437  -6.655  -10.539 1.00 43.35  ? 84  PHE   A CE1 1 
ATOM   441  C CE2 . PHE   A 1 41  ? -8.655  -4.716  -11.160 1.00 40.97  ? 84  PHE   A CE2 1 
ATOM   442  C CZ  . PHE   A 1 41  ? -8.643  -6.047  -10.845 1.00 40.10  ? 84  PHE   A CZ  1 
ATOM   443  N N   . SER   A 1 42  ? -2.014  -4.019  -9.915  1.00 52.75  ? 85  SER   A N   1 
ATOM   444  C CA  . SER   A 1 42  ? -0.597  -3.807  -10.269 1.00 56.13  ? 85  SER   A CA  1 
ATOM   445  C C   . SER   A 1 42  ? -0.044  -5.086  -10.896 1.00 58.73  ? 85  SER   A C   1 
ATOM   446  O O   . SER   A 1 42  ? -0.602  -6.167  -10.620 1.00 54.35  ? 85  SER   A O   1 
ATOM   447  C CB  . SER   A 1 42  ? 0.184   -3.397  -9.068  1.00 59.52  ? 85  SER   A CB  1 
ATOM   448  O OG  . SER   A 1 42  ? 0.029   -4.353  -8.027  1.00 59.74  ? 85  SER   A OG  1 
ATOM   449  N N   . LEU   A 1 43  ? 0.973   -4.952  -11.752 1.00 64.82  ? 86  LEU   A N   1 
ATOM   450  C CA  . LEU   A 1 43  ? 1.616   -6.109  -12.435 1.00 70.30  ? 86  LEU   A CA  1 
ATOM   451  C C   . LEU   A 1 43  ? 2.614   -6.748  -11.473 1.00 70.39  ? 86  LEU   A C   1 
ATOM   452  O O   . LEU   A 1 43  ? 3.573   -6.078  -11.085 1.00 68.63  ? 86  LEU   A O   1 
ATOM   453  C CB  . LEU   A 1 43  ? 2.285   -5.649  -13.731 1.00 73.12  ? 86  LEU   A CB  1 
ATOM   454  C CG  . LEU   A 1 43  ? 1.304   -5.252  -14.836 1.00 75.94  ? 86  LEU   A CG  1 
ATOM   455  C CD1 . LEU   A 1 43  ? 1.924   -4.250  -15.797 1.00 78.71  ? 86  LEU   A CD1 1 
ATOM   456  C CD2 . LEU   A 1 43  ? 0.807   -6.479  -15.595 1.00 77.93  ? 86  LEU   A CD2 1 
ATOM   457  N N   . VAL   A 1 44  ? 2.325   -7.975  -11.059 1.00 73.24  ? 87  VAL   A N   1 
ATOM   458  C CA  . VAL   A 1 44  ? 3.337   -8.967  -10.597 1.00 79.75  ? 87  VAL   A CA  1 
ATOM   459  C C   . VAL   A 1 44  ? 4.184   -9.294  -11.821 1.00 88.05  ? 87  VAL   A C   1 
ATOM   460  O O   . VAL   A 1 44  ? 3.659   -9.167  -12.953 1.00 97.64  ? 87  VAL   A O   1 
ATOM   461  C CB  . VAL   A 1 44  ? 2.656   -10.235 -10.052 1.00 77.68  ? 87  VAL   A CB  1 
ATOM   462  C CG1 . VAL   A 1 44  ? 3.664   -11.283 -9.584  1.00 77.87  ? 87  VAL   A CG1 1 
ATOM   463  C CG2 . VAL   A 1 44  ? 1.638   -9.894  -8.970  1.00 73.48  ? 87  VAL   A CG2 1 
ATOM   464  N N   . GLU   A 1 45  ? 5.420   -9.728  -11.633 1.00 98.12  ? 88  GLU   A N   1 
ATOM   465  C CA  . GLU   A 1 45  ? 6.325   -9.975  -12.785 1.00 105.55 ? 88  GLU   A CA  1 
ATOM   466  C C   . GLU   A 1 45  ? 7.229   -11.177 -12.489 1.00 107.61 ? 88  GLU   A C   1 
ATOM   467  O O   . GLU   A 1 45  ? 6.743   -12.289 -12.711 1.00 105.41 ? 88  GLU   A O   1 
ATOM   468  C CB  . GLU   A 1 45  ? 7.049   -8.663  -13.093 1.00 109.33 ? 88  GLU   A CB  1 
ATOM   469  C CG  . GLU   A 1 45  ? 6.242   -7.718  -13.976 1.00 109.19 ? 88  GLU   A CG  1 
ATOM   470  C CD  . GLU   A 1 45  ? 5.742   -8.312  -15.281 1.00 106.67 ? 88  GLU   A CD  1 
ATOM   471  O OE1 . GLU   A 1 45  ? 4.568   -8.755  -15.312 1.00 102.40 ? 88  GLU   A OE1 1 
ATOM   472  O OE2 . GLU   A 1 45  ? 6.525   -8.324  -16.259 1.00 107.48 ? 88  GLU   A OE2 1 
ATOM   473  N N   . GLY   B 2 7   ? -36.530 12.288  -11.761 1.00 88.21  ? 16  GLY   B N   1 
ATOM   474  C CA  . GLY   B 2 7   ? -35.299 12.149  -12.618 1.00 88.52  ? 16  GLY   B CA  1 
ATOM   475  C C   . GLY   B 2 7   ? -35.446 11.087  -13.708 1.00 88.08  ? 16  GLY   B C   1 
ATOM   476  O O   . GLY   B 2 7   ? -36.408 10.282  -13.620 1.00 90.58  ? 16  GLY   B O   1 
ATOM   477  N N   . GLU   B 2 8   ? -34.521 11.066  -14.689 1.00 82.29  ? 17  GLU   B N   1 
ATOM   478  C CA  . GLU   B 2 8   ? -34.517 10.115  -15.846 1.00 76.05  ? 17  GLU   B CA  1 
ATOM   479  C C   . GLU   B 2 8   ? -34.076 8.719   -15.377 1.00 70.09  ? 17  GLU   B C   1 
ATOM   480  O O   . GLU   B 2 8   ? -32.916 8.534   -14.984 1.00 68.88  ? 17  GLU   B O   1 
ATOM   481  C CB  . GLU   B 2 8   ? -33.608 10.581  -16.994 1.00 78.92  ? 17  GLU   B CB  1 
ATOM   482  C CG  . GLU   B 2 8   ? -33.719 9.699   -18.241 1.00 76.98  ? 17  GLU   B CG  1 
ATOM   483  C CD  . GLU   B 2 8   ? -33.011 10.188  -19.500 1.00 79.18  ? 17  GLU   B CD  1 
ATOM   484  O OE1 . GLU   B 2 8   ? -32.034 10.987  -19.386 1.00 71.78  ? 17  GLU   B OE1 1 
ATOM   485  O OE2 . GLU   B 2 8   ? -33.477 9.807   -20.616 1.00 83.16  ? 17  GLU   B OE2 1 
ATOM   486  N N   A THR   B 2 9   ? -34.987 7.745   -15.419 0.25 69.29  ? 18  THR   B N   1 
ATOM   487  N N   B THR   B 2 9   ? -35.010 7.768   -15.451 0.25 68.54  ? 18  THR   B N   1 
ATOM   488  N N   C THR   B 2 9   ? -34.987 7.745   -15.419 0.25 69.29  ? 18  THR   B N   1 
ATOM   489  N N   D THR   B 2 9   ? -35.010 7.768   -15.451 0.25 68.54  ? 18  THR   B N   1 
ATOM   490  C CA  A THR   B 2 9   ? -34.744 6.363   -14.926 0.25 68.99  ? 18  THR   B CA  1 
ATOM   491  C CA  B THR   B 2 9   ? -34.890 6.384   -14.929 0.25 67.80  ? 18  THR   B CA  1 
ATOM   492  C CA  C THR   B 2 9   ? -34.744 6.363   -14.926 0.25 68.99  ? 18  THR   B CA  1 
ATOM   493  C CA  D THR   B 2 9   ? -34.890 6.384   -14.929 0.25 67.80  ? 18  THR   B CA  1 
ATOM   494  C C   A THR   B 2 9   ? -34.723 5.372   -16.094 0.25 67.22  ? 18  THR   B C   1 
ATOM   495  C C   B THR   B 2 9   ? -34.694 5.395   -16.086 0.25 66.52  ? 18  THR   B C   1 
ATOM   496  C C   C THR   B 2 9   ? -34.723 5.372   -16.094 0.25 67.22  ? 18  THR   B C   1 
ATOM   497  C C   D THR   B 2 9   ? -34.694 5.395   -16.086 0.25 66.52  ? 18  THR   B C   1 
ATOM   498  O O   A THR   B 2 9   ? -34.610 4.160   -15.816 0.25 68.30  ? 18  THR   B O   1 
ATOM   499  O O   B THR   B 2 9   ? -34.407 4.215   -15.794 0.25 67.55  ? 18  THR   B O   1 
ATOM   500  O O   C THR   B 2 9   ? -34.610 4.160   -15.816 0.25 68.30  ? 18  THR   B O   1 
ATOM   501  O O   D THR   B 2 9   ? -34.407 4.215   -15.794 0.25 67.55  ? 18  THR   B O   1 
ATOM   502  C CB  A THR   B 2 9   ? -35.791 5.964   -13.881 0.25 70.13  ? 18  THR   B CB  1 
ATOM   503  C CB  B THR   B 2 9   ? -36.121 6.045   -14.078 0.25 68.05  ? 18  THR   B CB  1 
ATOM   504  C CB  C THR   B 2 9   ? -35.791 5.964   -13.881 0.25 70.13  ? 18  THR   B CB  1 
ATOM   505  C CB  D THR   B 2 9   ? -36.121 6.045   -14.078 0.25 68.05  ? 18  THR   B CB  1 
ATOM   506  O OG1 A THR   B 2 9   ? -36.051 7.113   -13.076 0.25 71.02  ? 18  THR   B OG1 1 
ATOM   507  O OG1 B THR   B 2 9   ? -37.283 6.497   -14.774 0.25 67.22  ? 18  THR   B OG1 1 
ATOM   508  O OG1 C THR   B 2 9   ? -36.051 7.113   -13.076 0.25 71.02  ? 18  THR   B OG1 1 
ATOM   509  O OG1 D THR   B 2 9   ? -37.283 6.497   -14.774 0.25 67.22  ? 18  THR   B OG1 1 
ATOM   510  C CG2 A THR   B 2 9   ? -35.344 4.801   -13.021 0.25 70.44  ? 18  THR   B CG2 1 
ATOM   511  C CG2 B THR   B 2 9   ? -36.086 6.685   -12.708 0.25 68.53  ? 18  THR   B CG2 1 
ATOM   512  C CG2 C THR   B 2 9   ? -35.344 4.801   -13.021 0.25 70.44  ? 18  THR   B CG2 1 
ATOM   513  C CG2 D THR   B 2 9   ? -36.086 6.685   -12.708 0.25 68.53  ? 18  THR   B CG2 1 
ATOM   514  N N   . THR   B 2 10  ? -34.821 5.858   -17.338 1.00 64.65  ? 19  THR   B N   1 
ATOM   515  C CA  . THR   B 2 10  ? -34.780 5.007   -18.556 1.00 61.35  ? 19  THR   B CA  1 
ATOM   516  C C   . THR   B 2 10  ? -33.491 4.163   -18.567 1.00 54.70  ? 19  THR   B C   1 
ATOM   517  O O   . THR   B 2 10  ? -32.379 4.745   -18.407 1.00 51.40  ? 19  THR   B O   1 
ATOM   518  C CB  . THR   B 2 10  ? -34.871 5.823   -19.864 1.00 62.66  ? 19  THR   B CB  1 
ATOM   519  O OG1 . THR   B 2 10  ? -35.859 6.858   -19.845 1.00 69.67  ? 19  THR   B OG1 1 
ATOM   520  C CG2 . THR   B 2 10  ? -35.218 4.960   -21.056 1.00 61.08  ? 19  THR   B CG2 1 
ATOM   521  N N   . ASP   B 2 11  ? -33.635 2.847   -18.759 1.00 49.79  ? 20  ASP   B N   1 
ATOM   522  C CA  . ASP   B 2 11  ? -32.483 1.930   -18.943 1.00 50.78  ? 20  ASP   B CA  1 
ATOM   523  C C   . ASP   B 2 11  ? -31.524 2.517   -19.978 1.00 50.33  ? 20  ASP   B C   1 
ATOM   524  O O   . ASP   B 2 11  ? -31.971 3.334   -20.835 1.00 52.17  ? 20  ASP   B O   1 
ATOM   525  C CB  . ASP   B 2 11  ? -32.921 0.526   -19.358 1.00 52.71  ? 20  ASP   B CB  1 
ATOM   526  C CG  . ASP   B 2 11  ? -33.446 -0.335  -18.220 1.00 55.91  ? 20  ASP   B CG  1 
ATOM   527  O OD1 . ASP   B 2 11  ? -33.560 0.175   -17.089 1.00 53.90  ? 20  ASP   B OD1 1 
ATOM   528  O OD2 . ASP   B 2 11  ? -33.734 -1.523  -18.483 1.00 59.95  ? 20  ASP   B OD2 1 
ATOM   529  N N   . GLY   B 2 12  ? -30.251 2.124   -19.932 1.00 47.86  ? 21  GLY   B N   1 
ATOM   530  C CA  . GLY   B 2 12  ? -29.263 2.599   -20.912 1.00 45.10  ? 21  GLY   B CA  1 
ATOM   531  C C   . GLY   B 2 12  ? -28.008 3.120   -20.261 1.00 42.39  ? 21  GLY   B C   1 
ATOM   532  O O   . GLY   B 2 12  ? -27.836 2.929   -19.068 1.00 40.04  ? 21  GLY   B O   1 
ATOM   533  N N   . VAL   B 2 13  ? -27.147 3.751   -21.049 1.00 41.84  ? 22  VAL   B N   1 
ATOM   534  C CA  . VAL   B 2 13  ? -25.794 4.185   -20.616 1.00 41.30  ? 22  VAL   B CA  1 
ATOM   535  C C   . VAL   B 2 13  ? -25.784 5.704   -20.490 1.00 41.34  ? 22  VAL   B C   1 
ATOM   536  O O   . VAL   B 2 13  ? -26.582 6.379   -21.173 1.00 41.73  ? 22  VAL   B O   1 
ATOM   537  C CB  . VAL   B 2 13  ? -24.683 3.608   -21.492 1.00 42.66  ? 22  VAL   B CB  1 
ATOM   538  C CG1 . VAL   B 2 13  ? -24.802 4.020   -22.992 1.00 44.91  ? 22  VAL   B CG1 1 
ATOM   539  C CG2 . VAL   B 2 13  ? -23.315 3.967   -20.932 1.00 42.40  ? 22  VAL   B CG2 1 
ATOM   540  N N   . TYR   B 2 14  ? -25.081 6.201   -19.473 1.00 41.27  ? 23  TYR   B N   1 
ATOM   541  C CA  . TYR   B 2 14  ? -25.155 7.615   -19.041 1.00 40.37  ? 23  TYR   B CA  1 
ATOM   542  C C   . TYR   B 2 14  ? -23.766 8.153   -18.819 1.00 40.91  ? 23  TYR   B C   1 
ATOM   543  O O   . TYR   B 2 14  ? -22.910 7.397   -18.364 1.00 43.84  ? 23  TYR   B O   1 
ATOM   544  C CB  . TYR   B 2 14  ? -25.923 7.766   -17.738 1.00 39.97  ? 23  TYR   B CB  1 
ATOM   545  C CG  . TYR   B 2 14  ? -27.397 7.614   -17.929 1.00 37.88  ? 23  TYR   B CG  1 
ATOM   546  C CD1 . TYR   B 2 14  ? -27.934 6.378   -18.218 1.00 37.50  ? 23  TYR   B CD1 1 
ATOM   547  C CD2 . TYR   B 2 14  ? -28.219 8.719   -17.854 1.00 37.55  ? 23  TYR   B CD2 1 
ATOM   548  C CE1 . TYR   B 2 14  ? -29.294 6.215   -18.370 1.00 37.95  ? 23  TYR   B CE1 1 
ATOM   549  C CE2 . TYR   B 2 14  ? -29.584 8.580   -18.043 1.00 38.94  ? 23  TYR   B CE2 1 
ATOM   550  C CZ  . TYR   B 2 14  ? -30.117 7.325   -18.277 1.00 39.50  ? 23  TYR   B CZ  1 
ATOM   551  O OH  . TYR   B 2 14  ? -31.461 7.203   -18.450 1.00 42.04  ? 23  TYR   B OH  1 
ATOM   552  N N   . ARG   B 2 15  ? -23.578 9.422   -19.134 1.00 41.30  ? 24  ARG   B N   1 
ATOM   553  C CA  . ARG   B 2 15  ? -22.359 10.156  -18.729 1.00 41.20  ? 24  ARG   B CA  1 
ATOM   554  C C   . ARG   B 2 15  ? -22.560 10.626  -17.287 1.00 40.93  ? 24  ARG   B C   1 
ATOM   555  O O   . ARG   B 2 15  ? -23.663 11.036  -16.970 1.00 37.65  ? 24  ARG   B O   1 
ATOM   556  C CB  . ARG   B 2 15  ? -22.093 11.335  -19.664 1.00 42.08  ? 24  ARG   B CB  1 
ATOM   557  C CG  . ARG   B 2 15  ? -22.066 10.980  -21.149 1.00 43.12  ? 24  ARG   B CG  1 
ATOM   558  C CD  . ARG   B 2 15  ? -21.946 12.261  -21.956 1.00 46.29  ? 24  ARG   B CD  1 
ATOM   559  N NE  . ARG   B 2 15  ? -21.961 12.054  -23.409 1.00 46.69  ? 24  ARG   B NE  1 
ATOM   560  C CZ  . ARG   B 2 15  ? -20.885 11.801  -24.160 1.00 47.49  ? 24  ARG   B CZ  1 
ATOM   561  N NH1 . ARG   B 2 15  ? -19.668 11.776  -23.643 1.00 48.76  ? 24  ARG   B NH1 1 
ATOM   562  N NH2 . ARG   B 2 15  ? -21.028 11.594  -25.448 1.00 48.77  ? 24  ARG   B NH2 1 
ATOM   563  N N   . VAL   B 2 16  ? -21.467 10.660  -16.533 1.00 41.96  ? 25  VAL   B N   1 
ATOM   564  C CA  . VAL   B 2 16  ? -21.331 11.268  -15.188 1.00 42.27  ? 25  VAL   B CA  1 
ATOM   565  C C   . VAL   B 2 16  ? -20.437 12.508  -15.295 1.00 42.61  ? 25  VAL   B C   1 
ATOM   566  O O   . VAL   B 2 16  ? -19.240 12.368  -15.563 1.00 42.27  ? 25  VAL   B O   1 
ATOM   567  C CB  . VAL   B 2 16  ? -20.750 10.234  -14.195 1.00 43.55  ? 25  VAL   B CB  1 
ATOM   568  C CG1 . VAL   B 2 16  ? -20.596 10.845  -12.798 1.00 44.06  ? 25  VAL   B CG1 1 
ATOM   569  C CG2 . VAL   B 2 16  ? -21.588 8.948   -14.156 1.00 42.47  ? 25  VAL   B CG2 1 
ATOM   570  N N   . MET   B 2 17  ? -21.017 13.670  -15.006 1.00 45.14  ? 26  MET   B N   1 
ATOM   571  C CA  . MET   B 2 17  ? -20.466 15.021  -15.253 1.00 47.12  ? 26  MET   B CA  1 
ATOM   572  C C   . MET   B 2 17  ? -20.272 15.739  -13.912 1.00 49.12  ? 26  MET   B C   1 
ATOM   573  O O   . MET   B 2 17  ? -21.063 15.496  -12.985 1.00 48.08  ? 26  MET   B O   1 
ATOM   574  C CB  . MET   B 2 17  ? -21.455 15.844  -16.083 1.00 48.77  ? 26  MET   B CB  1 
ATOM   575  C CG  . MET   B 2 17  ? -21.860 15.206  -17.438 1.00 49.21  ? 26  MET   B CG  1 
ATOM   576  S SD  . MET   B 2 17  ? -20.516 14.955  -18.641 1.00 51.28  ? 26  MET   B SD  1 
ATOM   577  C CE  . MET   B 2 17  ? -19.900 16.635  -18.778 1.00 53.17  ? 26  MET   B CE  1 
ATOM   578  N N   . THR   B 2 18  ? -19.323 16.667  -13.859 1.00 50.90  ? 27  THR   B N   1 
ATOM   579  C CA  . THR   B 2 18  ? -19.153 17.619  -12.746 1.00 54.87  ? 27  THR   B CA  1 
ATOM   580  C C   . THR   B 2 18  ? -18.958 19.049  -13.283 1.00 58.97  ? 27  THR   B C   1 
ATOM   581  O O   . THR   B 2 18  ? -18.327 19.202  -14.380 1.00 54.10  ? 27  THR   B O   1 
ATOM   582  C CB  . THR   B 2 18  ? -18.006 17.134  -11.854 1.00 56.46  ? 27  THR   B CB  1 
ATOM   583  O OG1 . THR   B 2 18  ? -17.986 18.069  -10.775 1.00 59.02  ? 27  THR   B OG1 1 
ATOM   584  C CG2 . THR   B 2 18  ? -16.669 17.028  -12.564 1.00 55.57  ? 27  THR   B CG2 1 
ATOM   585  N N   . ARG   B 2 19  ? -19.443 20.054  -12.525 1.00 63.07  ? 28  ARG   B N   1 
ATOM   586  C CA  . ARG   B 2 19  ? -19.159 21.504  -12.744 1.00 69.08  ? 28  ARG   B CA  1 
ATOM   587  C C   . ARG   B 2 19  ? -18.057 22.014  -11.787 1.00 67.76  ? 28  ARG   B C   1 
ATOM   588  O O   . ARG   B 2 19  ? -17.615 23.162  -11.940 1.00 68.96  ? 28  ARG   B O   1 
ATOM   589  C CB  . ARG   B 2 19  ? -20.470 22.290  -12.667 1.00 72.92  ? 28  ARG   B CB  1 
ATOM   590  C CG  . ARG   B 2 19  ? -21.545 21.750  -13.603 1.00 78.40  ? 28  ARG   B CG  1 
ATOM   591  C CD  . ARG   B 2 19  ? -22.304 22.818  -14.378 1.00 84.12  ? 28  ARG   B CD  1 
ATOM   592  N NE  . ARG   B 2 19  ? -23.526 22.333  -15.025 1.00 87.78  ? 28  ARG   B NE  1 
ATOM   593  C CZ  . ARG   B 2 19  ? -24.686 22.072  -14.407 1.00 94.44  ? 28  ARG   B CZ  1 
ATOM   594  N NH1 . ARG   B 2 19  ? -24.813 22.231  -13.095 1.00 92.63  ? 28  ARG   B NH1 1 
ATOM   595  N NH2 . ARG   B 2 19  ? -25.720 21.634  -15.114 1.00 96.56  ? 28  ARG   B NH2 1 
ATOM   596  N N   . ARG   B 2 20  ? -17.539 21.145  -10.925 1.00 73.02  ? 29  ARG   B N   1 
ATOM   597  C CA  . ARG   B 2 20  ? -16.575 21.439  -9.823  1.00 78.93  ? 29  ARG   B CA  1 
ATOM   598  C C   . ARG   B 2 20  ? -15.190 21.824  -10.383 1.00 79.12  ? 29  ARG   B C   1 
ATOM   599  O O   . ARG   B 2 20  ? -14.417 22.479  -9.660  1.00 78.48  ? 29  ARG   B O   1 
ATOM   600  C CB  . ARG   B 2 20  ? -16.509 20.195  -8.927  1.00 80.62  ? 29  ARG   B CB  1 
ATOM   601  C CG  . ARG   B 2 20  ? -15.956 20.406  -7.526  1.00 87.05  ? 29  ARG   B CG  1 
ATOM   602  C CD  . ARG   B 2 20  ? -15.487 19.082  -6.918  1.00 93.45  ? 29  ARG   B CD  1 
ATOM   603  N NE  . ARG   B 2 20  ? -14.320 18.463  -7.574  1.00 99.25  ? 29  ARG   B NE  1 
ATOM   604  C CZ  . ARG   B 2 20  ? -13.087 18.311  -7.047  1.00 104.63 ? 29  ARG   B CZ  1 
ATOM   605  N NH1 . ARG   B 2 20  ? -12.811 18.714  -5.813  1.00 106.99 ? 29  ARG   B NH1 1 
ATOM   606  N NH2 . ARG   B 2 20  ? -12.123 17.748  -7.765  1.00 100.76 ? 29  ARG   B NH2 1 
ATOM   607  N N   . LEU   B 2 21  ? -14.854 21.396  -11.601 1.00 76.86  ? 30  LEU   B N   1 
ATOM   608  C CA  . LEU   B 2 21  ? -13.639 21.849  -12.331 1.00 74.62  ? 30  LEU   B CA  1 
ATOM   609  C C   . LEU   B 2 21  ? -14.068 22.905  -13.371 1.00 72.51  ? 30  LEU   B C   1 
ATOM   610  O O   . LEU   B 2 21  ? -15.228 23.387  -13.272 1.00 71.93  ? 30  LEU   B O   1 
ATOM   611  C CB  . LEU   B 2 21  ? -12.966 20.622  -12.952 1.00 74.69  ? 30  LEU   B CB  1 
ATOM   612  C CG  . LEU   B 2 21  ? -11.951 19.901  -12.072 1.00 77.45  ? 30  LEU   B CG  1 
ATOM   613  C CD1 . LEU   B 2 21  ? -12.461 19.750  -10.654 1.00 77.13  ? 30  LEU   B CD1 1 
ATOM   614  C CD2 . LEU   B 2 21  ? -11.584 18.539  -12.658 1.00 77.92  ? 30  LEU   B CD2 1 
ATOM   615  N N   . LEU   B 2 22  ? -13.173 23.274  -14.305 1.00 71.52  ? 31  LEU   B N   1 
ATOM   616  C CA  . LEU   B 2 22  ? -13.439 24.222  -15.431 1.00 69.59  ? 31  LEU   B CA  1 
ATOM   617  C C   . LEU   B 2 22  ? -14.531 23.646  -16.331 1.00 67.58  ? 31  LEU   B C   1 
ATOM   618  O O   . LEU   B 2 22  ? -14.491 22.426  -16.575 1.00 69.25  ? 31  LEU   B O   1 
ATOM   619  C CB  . LEU   B 2 22  ? -12.155 24.426  -16.233 1.00 68.47  ? 31  LEU   B CB  1 
ATOM   620  C CG  . LEU   B 2 22  ? -12.245 25.463  -17.349 1.00 67.69  ? 31  LEU   B CG  1 
ATOM   621  C CD1 . LEU   B 2 22  ? -12.120 26.877  -16.796 1.00 66.59  ? 31  LEU   B CD1 1 
ATOM   622  C CD2 . LEU   B 2 22  ? -11.182 25.190  -18.406 1.00 67.55  ? 31  LEU   B CD2 1 
ATOM   623  N N   . GLY   B 2 23  ? -15.466 24.480  -16.799 1.00 65.90  ? 32  GLY   B N   1 
ATOM   624  C CA  . GLY   B 2 23  ? -16.616 24.048  -17.623 1.00 62.62  ? 32  GLY   B CA  1 
ATOM   625  C C   . GLY   B 2 23  ? -17.357 22.860  -17.020 1.00 59.42  ? 32  GLY   B C   1 
ATOM   626  O O   . GLY   B 2 23  ? -17.405 22.751  -15.779 1.00 60.46  ? 32  GLY   B O   1 
ATOM   627  N N   . SER   B 2 24  ? -17.971 22.035  -17.868 1.00 58.40  ? 33  SER   B N   1 
ATOM   628  C CA  . SER   B 2 24  ? -18.558 20.715  -17.527 1.00 57.84  ? 33  SER   B CA  1 
ATOM   629  C C   . SER   B 2 24  ? -17.535 19.625  -17.862 1.00 56.83  ? 33  SER   B C   1 
ATOM   630  O O   . SER   B 2 24  ? -17.135 19.581  -19.025 1.00 54.63  ? 33  SER   B O   1 
ATOM   631  C CB  . SER   B 2 24  ? -19.842 20.514  -18.260 1.00 58.28  ? 33  SER   B CB  1 
ATOM   632  O OG  . SER   B 2 24  ? -20.828 21.399  -17.741 1.00 60.93  ? 33  SER   B OG  1 
ATOM   633  N N   . THR   B 2 25  ? -17.101 18.815  -16.886 1.00 53.98  ? 34  THR   B N   1 
ATOM   634  C CA  . THR   B 2 25  ? -16.048 17.779  -17.077 1.00 54.23  ? 34  THR   B CA  1 
ATOM   635  C C   . THR   B 2 25  ? -16.688 16.402  -16.910 1.00 53.54  ? 34  THR   B C   1 
ATOM   636  O O   . THR   B 2 25  ? -17.401 16.216  -15.926 1.00 54.58  ? 34  THR   B O   1 
ATOM   637  C CB  . THR   B 2 25  ? -14.849 17.991  -16.142 1.00 55.98  ? 34  THR   B CB  1 
ATOM   638  O OG1 . THR   B 2 25  ? -14.235 19.246  -16.456 1.00 57.47  ? 34  THR   B OG1 1 
ATOM   639  C CG2 . THR   B 2 25  ? -13.801 16.901  -16.262 1.00 55.60  ? 34  THR   B CG2 1 
ATOM   640  N N   . GLN   B 2 26  ? -16.460 15.473  -17.839 1.00 52.68  ? 35  GLN   B N   1 
ATOM   641  C CA  . GLN   B 2 26  ? -17.024 14.102  -17.715 1.00 50.60  ? 35  GLN   B CA  1 
ATOM   642  C C   . GLN   B 2 26  ? -16.038 13.298  -16.860 1.00 51.97  ? 35  GLN   B C   1 
ATOM   643  O O   . GLN   B 2 26  ? -14.895 13.160  -17.301 1.00 52.80  ? 35  GLN   B O   1 
ATOM   644  C CB  . GLN   B 2 26  ? -17.256 13.459  -19.076 1.00 49.24  ? 35  GLN   B CB  1 
ATOM   645  C CG  . GLN   B 2 26  ? -17.833 12.055  -18.994 1.00 48.78  ? 35  GLN   B CG  1 
ATOM   646  C CD  . GLN   B 2 26  ? -18.109 11.422  -20.339 1.00 47.83  ? 35  GLN   B CD  1 
ATOM   647  O OE1 . GLN   B 2 26  ? -18.835 11.959  -21.170 1.00 51.07  ? 35  GLN   B OE1 1 
ATOM   648  N NE2 . GLN   B 2 26  ? -17.616 10.216  -20.528 1.00 45.84  ? 35  GLN   B NE2 1 
ATOM   649  N N   . VAL   B 2 27  ? -16.434 12.856  -15.659 1.00 49.29  ? 36  VAL   B N   1 
ATOM   650  C CA  . VAL   B 2 27  ? -15.523 12.092  -14.752 1.00 47.45  ? 36  VAL   B CA  1 
ATOM   651  C C   . VAL   B 2 27  ? -15.687 10.580  -15.010 1.00 44.58  ? 36  VAL   B C   1 
ATOM   652  O O   . VAL   B 2 27  ? -14.783 9.793   -14.660 1.00 43.62  ? 36  VAL   B O   1 
ATOM   653  C CB  . VAL   B 2 27  ? -15.761 12.487  -13.271 1.00 50.13  ? 36  VAL   B CB  1 
ATOM   654  C CG1 . VAL   B 2 27  ? -15.101 13.828  -12.938 1.00 51.52  ? 36  VAL   B CG1 1 
ATOM   655  C CG2 . VAL   B 2 27  ? -17.236 12.531  -12.880 1.00 48.22  ? 36  VAL   B CG2 1 
ATOM   656  N N   . GLY   B 2 28  ? -16.807 10.154  -15.592 1.00 41.25  ? 37  GLY   B N   1 
ATOM   657  C CA  . GLY   B 2 28  ? -16.982 8.739   -15.965 1.00 38.90  ? 37  GLY   B CA  1 
ATOM   658  C C   . GLY   B 2 28  ? -18.338 8.512   -16.578 1.00 37.78  ? 37  GLY   B C   1 
ATOM   659  O O   . GLY   B 2 28  ? -18.932 9.473   -16.998 1.00 39.76  ? 37  GLY   B O   1 
ATOM   660  N N   . VAL   B 2 29  ? -18.842 7.283   -16.492 1.00 36.91  ? 38  VAL   B N   1 
ATOM   661  C CA  . VAL   B 2 29  ? -19.990 6.698   -17.253 1.00 36.68  ? 38  VAL   B CA  1 
ATOM   662  C C   . VAL   B 2 29  ? -20.656 5.729   -16.297 1.00 37.02  ? 38  VAL   B C   1 
ATOM   663  O O   . VAL   B 2 29  ? -19.958 5.314   -15.367 1.00 39.16  ? 38  VAL   B O   1 
ATOM   664  C CB  . VAL   B 2 29  ? -19.490 5.912   -18.494 1.00 36.98  ? 38  VAL   B CB  1 
ATOM   665  C CG1 . VAL   B 2 29  ? -20.604 5.292   -19.312 1.00 37.60  ? 38  VAL   B CG1 1 
ATOM   666  C CG2 . VAL   B 2 29  ? -18.591 6.740   -19.369 1.00 36.83  ? 38  VAL   B CG2 1 
ATOM   667  N N   . GLY   B 2 30  ? -21.904 5.338   -16.541 1.00 36.98  ? 39  GLY   B N   1 
ATOM   668  C CA  . GLY   B 2 30  ? -22.549 4.243   -15.808 1.00 35.43  ? 39  GLY   B CA  1 
ATOM   669  C C   . GLY   B 2 30  ? -23.752 3.703   -16.523 1.00 35.93  ? 39  GLY   B C   1 
ATOM   670  O O   . GLY   B 2 30  ? -24.086 4.197   -17.626 1.00 38.03  ? 39  GLY   B O   1 
ATOM   671  N N   . VAL   B 2 31  ? -24.354 2.675   -15.953 1.00 35.99  ? 40  VAL   B N   1 
ATOM   672  C CA  . VAL   B 2 31  ? -25.481 1.889   -16.529 1.00 36.72  ? 40  VAL   B CA  1 
ATOM   673  C C   . VAL   B 2 31  ? -26.705 2.067   -15.655 1.00 37.61  ? 40  VAL   B C   1 
ATOM   674  O O   . VAL   B 2 31  ? -26.582 1.816   -14.393 1.00 37.39  ? 40  VAL   B O   1 
ATOM   675  C CB  . VAL   B 2 31  ? -25.171 0.397   -16.610 1.00 37.58  ? 40  VAL   B CB  1 
ATOM   676  C CG1 . VAL   B 2 31  ? -26.371 -0.379  -17.100 1.00 38.83  ? 40  VAL   B CG1 1 
ATOM   677  C CG2 . VAL   B 2 31  ? -23.971 0.156   -17.480 1.00 38.33  ? 40  VAL   B CG2 1 
ATOM   678  N N   . MET   B 2 32  ? -27.829 2.453   -16.265 1.00 37.66  ? 41  MET   B N   1 
ATOM   679  C CA  . MET   B 2 32  ? -29.138 2.462   -15.591 1.00 39.50  ? 41  MET   B CA  1 
ATOM   680  C C   . MET   B 2 32  ? -29.860 1.157   -15.963 1.00 40.68  ? 41  MET   B C   1 
ATOM   681  O O   . MET   B 2 32  ? -29.987 0.869   -17.162 1.00 39.90  ? 41  MET   B O   1 
ATOM   682  C CB  . MET   B 2 32  ? -29.903 3.726   -16.004 1.00 40.79  ? 41  MET   B CB  1 
ATOM   683  C CG  . MET   B 2 32  ? -31.191 3.978   -15.240 1.00 42.30  ? 41  MET   B CG  1 
ATOM   684  S SD  . MET   B 2 32  ? -30.919 4.424   -13.486 1.00 44.70  ? 41  MET   B SD  1 
ATOM   685  C CE  . MET   B 2 32  ? -30.108 6.018   -13.639 1.00 44.17  ? 41  MET   B CE  1 
ATOM   686  N N   . GLN   B 2 33  ? -30.228 0.317   -14.997 1.00 41.59  ? 42  GLN   B N   1 
ATOM   687  C CA  . GLN   B 2 33  ? -30.969 -0.932  -15.278 1.00 43.77  ? 42  GLN   B CA  1 
ATOM   688  C C   . GLN   B 2 33  ? -31.960 -1.200  -14.170 1.00 46.65  ? 42  GLN   B C   1 
ATOM   689  O O   . GLN   B 2 33  ? -31.614 -1.072  -12.997 1.00 45.10  ? 42  GLN   B O   1 
ATOM   690  C CB  . GLN   B 2 33  ? -30.042 -2.135  -15.403 1.00 45.73  ? 42  GLN   B CB  1 
ATOM   691  C CG  . GLN   B 2 33  ? -30.796 -3.351  -15.922 1.00 48.61  ? 42  GLN   B CG  1 
ATOM   692  C CD  . GLN   B 2 33  ? -29.891 -4.434  -16.466 1.00 52.68  ? 42  GLN   B CD  1 
ATOM   693  O OE1 . GLN   B 2 33  ? -29.963 -5.594  -16.041 1.00 57.21  ? 42  GLN   B OE1 1 
ATOM   694  N NE2 . GLN   B 2 33  ? -28.996 -4.068  -17.372 1.00 51.27  ? 42  GLN   B NE2 1 
ATOM   695  N N   . GLU   B 2 34  ? -33.160 -1.608  -14.516 1.00 51.06  ? 43  GLU   B N   1 
ATOM   696  C CA  . GLU   B 2 34  ? -34.181 -1.874  -13.473 1.00 52.23  ? 43  GLU   B CA  1 
ATOM   697  C C   . GLU   B 2 34  ? -34.159 -0.748  -12.416 1.00 50.84  ? 43  GLU   B C   1 
ATOM   698  O O   . GLU   B 2 34  ? -34.300 -1.076  -11.245 1.00 48.51  ? 43  GLU   B O   1 
ATOM   699  C CB  . GLU   B 2 34  ? -33.888 -3.243  -12.838 1.00 55.77  ? 43  GLU   B CB  1 
ATOM   700  C CG  . GLU   B 2 34  ? -34.092 -4.440  -13.763 1.00 59.28  ? 43  GLU   B CG  1 
ATOM   701  C CD  . GLU   B 2 34  ? -33.259 -5.691  -13.473 1.00 61.21  ? 43  GLU   B CD  1 
ATOM   702  O OE1 . GLU   B 2 34  ? -33.599 -6.396  -12.525 1.00 61.65  ? 43  GLU   B OE1 1 
ATOM   703  O OE2 . GLU   B 2 34  ? -32.296 -5.988  -14.238 1.00 63.66  ? 43  GLU   B OE2 1 
ATOM   704  N N   . GLY   B 2 35  ? -33.967 0.528   -12.776 1.00 47.60  ? 44  GLY   B N   1 
ATOM   705  C CA  . GLY   B 2 35  ? -34.124 1.660   -11.836 1.00 46.32  ? 44  GLY   B CA  1 
ATOM   706  C C   . GLY   B 2 35  ? -32.916 1.887   -10.937 1.00 45.82  ? 44  GLY   B C   1 
ATOM   707  O O   . GLY   B 2 35  ? -32.969 2.825   -10.125 1.00 45.37  ? 44  GLY   B O   1 
ATOM   708  N N   . VAL   B 2 36  ? -31.852 1.081   -11.087 1.00 44.20  ? 45  VAL   B N   1 
ATOM   709  C CA  . VAL   B 2 36  ? -30.567 1.195   -10.340 1.00 41.27  ? 45  VAL   B CA  1 
ATOM   710  C C   . VAL   B 2 36  ? -29.485 1.723   -11.282 1.00 39.59  ? 45  VAL   B C   1 
ATOM   711  O O   . VAL   B 2 36  ? -29.402 1.210   -12.446 1.00 40.51  ? 45  VAL   B O   1 
ATOM   712  C CB  . VAL   B 2 36  ? -30.181 -0.148  -9.678  1.00 42.16  ? 45  VAL   B CB  1 
ATOM   713  C CG1 . VAL   B 2 36  ? -28.765 -0.129  -9.124  1.00 42.65  ? 45  VAL   B CG1 1 
ATOM   714  C CG2 . VAL   B 2 36  ? -31.147 -0.487  -8.553  1.00 43.56  ? 45  VAL   B CG2 1 
ATOM   715  N N   . PHE   B 2 37  ? -28.708 2.699   -10.811 1.00 36.97  ? 46  PHE   B N   1 
ATOM   716  C CA  . PHE   B 2 37  ? -27.537 3.277   -11.513 1.00 36.72  ? 46  PHE   B CA  1 
ATOM   717  C C   . PHE   B 2 37  ? -26.267 2.608   -10.989 1.00 35.91  ? 46  PHE   B C   1 
ATOM   718  O O   . PHE   B 2 37  ? -26.025 2.587   -9.769  1.00 35.48  ? 46  PHE   B O   1 
ATOM   719  C CB  . PHE   B 2 37  ? -27.461 4.792   -11.350 1.00 35.84  ? 46  PHE   B CB  1 
ATOM   720  C CG  . PHE   B 2 37  ? -26.460 5.414   -12.288 1.00 36.14  ? 46  PHE   B CG  1 
ATOM   721  C CD1 . PHE   B 2 37  ? -26.614 5.320   -13.657 1.00 36.87  ? 46  PHE   B CD1 1 
ATOM   722  C CD2 . PHE   B 2 37  ? -25.327 6.028   -11.798 1.00 36.58  ? 46  PHE   B CD2 1 
ATOM   723  C CE1 . PHE   B 2 37  ? -25.703 5.918   -14.516 1.00 37.84  ? 46  PHE   B CE1 1 
ATOM   724  C CE2 . PHE   B 2 37  ? -24.375 6.562   -12.648 1.00 36.92  ? 46  PHE   B CE2 1 
ATOM   725  C CZ  . PHE   B 2 37  ? -24.571 6.524   -14.009 1.00 37.75  ? 46  PHE   B CZ  1 
ATOM   726  N N   . HIS   B 2 38  ? -25.464 2.086   -11.898 1.00 35.09  ? 47  HIS   B N   1 
ATOM   727  C CA  . HIS   B 2 38  ? -24.251 1.283   -11.627 1.00 34.70  ? 47  HIS   B CA  1 
ATOM   728  C C   . HIS   B 2 38  ? -23.060 2.037   -12.178 1.00 35.33  ? 47  HIS   B C   1 
ATOM   729  O O   . HIS   B 2 38  ? -23.077 2.328   -13.365 1.00 34.63  ? 47  HIS   B O   1 
ATOM   730  C CB  . HIS   B 2 38  ? -24.350 -0.067  -12.280 1.00 34.75  ? 47  HIS   B CB  1 
ATOM   731  C CG  . HIS   B 2 38  ? -25.579 -0.842  -11.994 1.00 35.41  ? 47  HIS   B CG  1 
ATOM   732  N ND1 . HIS   B 2 38  ? -26.789 -0.534  -12.546 1.00 36.45  ? 47  HIS   B ND1 1 
ATOM   733  C CD2 . HIS   B 2 38  ? -25.766 -1.975  -11.279 1.00 37.02  ? 47  HIS   B CD2 1 
ATOM   734  C CE1 . HIS   B 2 38  ? -27.690 -1.432  -12.184 1.00 37.09  ? 47  HIS   B CE1 1 
ATOM   735  N NE2 . HIS   B 2 38  ? -27.090 -2.315  -11.375 1.00 37.63  ? 47  HIS   B NE2 1 
ATOM   736  N N   . THR   B 2 39  ? -22.095 2.402   -11.340 1.00 35.93  ? 48  THR   B N   1 
ATOM   737  C CA  . THR   B 2 39  ? -20.828 2.956   -11.831 1.00 37.99  ? 48  THR   B CA  1 
ATOM   738  C C   . THR   B 2 39  ? -19.659 2.339   -11.058 1.00 39.62  ? 48  THR   B C   1 
ATOM   739  O O   . THR   B 2 39  ? -19.878 1.432   -10.221 1.00 39.20  ? 48  THR   B O   1 
ATOM   740  C CB  . THR   B 2 39  ? -20.908 4.481   -11.870 1.00 38.59  ? 48  THR   B CB  1 
ATOM   741  O OG1 . THR   B 2 39  ? -19.755 4.976   -12.558 1.00 40.38  ? 48  THR   B OG1 1 
ATOM   742  C CG2 . THR   B 2 39  ? -20.971 5.122   -10.502 1.00 38.70  ? 48  THR   B CG2 1 
ATOM   743  N N   . MET   B 2 40  ? -18.452 2.818   -11.363 1.00 41.49  ? 49  MET   B N   1 
ATOM   744  C CA  . MET   B 2 40  ? -17.220 2.469   -10.616 1.00 42.28  ? 49  MET   B CA  1 
ATOM   745  C C   . MET   B 2 40  ? -17.009 3.479   -9.468  1.00 42.21  ? 49  MET   B C   1 
ATOM   746  O O   . MET   B 2 40  ? -17.264 4.659   -9.652  1.00 41.96  ? 49  MET   B O   1 
ATOM   747  C CB  . MET   B 2 40  ? -16.021 2.460   -11.560 1.00 43.33  ? 49  MET   B CB  1 
ATOM   748  C CG  . MET   B 2 40  ? -16.290 1.731   -12.892 1.00 45.51  ? 49  MET   B CG  1 
ATOM   749  S SD  . MET   B 2 40  ? -14.816 0.806   -13.360 1.00 50.39  ? 49  MET   B SD  1 
ATOM   750  C CE  . MET   B 2 40  ? -15.071 -0.735  -12.481 1.00 49.18  ? 49  MET   B CE  1 
ATOM   751  N N   A TRP   B 2 41  ? -16.545 2.999   -8.306  0.25 42.46  ? 50  TRP   B N   1 
ATOM   752  N N   B TRP   B 2 41  ? -16.537 3.003   -8.314  0.25 41.86  ? 50  TRP   B N   1 
ATOM   753  N N   C TRP   B 2 41  ? -16.545 2.999   -8.306  0.25 42.46  ? 50  TRP   B N   1 
ATOM   754  N N   D TRP   B 2 41  ? -16.537 3.003   -8.314  0.25 41.86  ? 50  TRP   B N   1 
ATOM   755  C CA  A TRP   B 2 41  ? -16.385 3.795   -7.057  0.25 42.43  ? 50  TRP   B CA  1 
ATOM   756  C CA  B TRP   B 2 41  ? -16.422 3.821   -7.079  0.25 41.45  ? 50  TRP   B CA  1 
ATOM   757  C CA  C TRP   B 2 41  ? -16.385 3.795   -7.057  0.25 42.43  ? 50  TRP   B CA  1 
ATOM   758  C CA  D TRP   B 2 41  ? -16.422 3.821   -7.079  0.25 41.45  ? 50  TRP   B CA  1 
ATOM   759  C C   A TRP   B 2 41  ? -15.468 4.999   -7.303  0.25 42.26  ? 50  TRP   B C   1 
ATOM   760  C C   B TRP   B 2 41  ? -15.465 5.002   -7.298  0.25 41.69  ? 50  TRP   B C   1 
ATOM   761  C C   C TRP   B 2 41  ? -15.468 4.999   -7.303  0.25 42.26  ? 50  TRP   B C   1 
ATOM   762  C C   D TRP   B 2 41  ? -15.465 5.002   -7.298  0.25 41.69  ? 50  TRP   B C   1 
ATOM   763  O O   A TRP   B 2 41  ? -15.780 6.088   -6.794  0.25 41.54  ? 50  TRP   B O   1 
ATOM   764  O O   B TRP   B 2 41  ? -15.748 6.087   -6.765  0.25 40.97  ? 50  TRP   B O   1 
ATOM   765  O O   C TRP   B 2 41  ? -15.780 6.088   -6.794  0.25 41.54  ? 50  TRP   B O   1 
ATOM   766  O O   D TRP   B 2 41  ? -15.748 6.087   -6.765  0.25 40.97  ? 50  TRP   B O   1 
ATOM   767  C CB  A TRP   B 2 41  ? -15.852 2.934   -5.898  0.25 43.04  ? 50  TRP   B CB  1 
ATOM   768  C CB  B TRP   B 2 41  ? -15.988 2.980   -5.872  0.25 41.35  ? 50  TRP   B CB  1 
ATOM   769  C CB  C TRP   B 2 41  ? -15.852 2.934   -5.898  0.25 43.04  ? 50  TRP   B CB  1 
ATOM   770  C CB  D TRP   B 2 41  ? -15.988 2.980   -5.872  0.25 41.35  ? 50  TRP   B CB  1 
ATOM   771  C CG  A TRP   B 2 41  ? -15.875 3.634   -4.569  0.25 43.66  ? 50  TRP   B CG  1 
ATOM   772  C CG  B TRP   B 2 41  ? -15.840 3.836   -4.652  0.25 41.22  ? 50  TRP   B CG  1 
ATOM   773  C CG  C TRP   B 2 41  ? -15.875 3.634   -4.569  0.25 43.66  ? 50  TRP   B CG  1 
ATOM   774  C CG  D TRP   B 2 41  ? -15.840 3.836   -4.652  0.25 41.22  ? 50  TRP   B CG  1 
ATOM   775  C CD1 A TRP   B 2 41  ? -16.839 3.526   -3.611  0.25 43.98  ? 50  TRP   B CD1 1 
ATOM   776  C CD1 B TRP   B 2 41  ? -14.818 4.698   -4.380  0.25 41.07  ? 50  TRP   B CD1 1 
ATOM   777  C CD1 C TRP   B 2 41  ? -16.839 3.526   -3.611  0.25 43.98  ? 50  TRP   B CD1 1 
ATOM   778  C CD1 D TRP   B 2 41  ? -14.818 4.698   -4.380  0.25 41.07  ? 50  TRP   B CD1 1 
ATOM   779  C CD2 A TRP   B 2 41  ? -14.901 4.563   -4.047  0.25 44.03  ? 50  TRP   B CD2 1 
ATOM   780  C CD2 B TRP   B 2 41  ? -16.782 3.983   -3.577  0.25 41.32  ? 50  TRP   B CD2 1 
ATOM   781  C CD2 C TRP   B 2 41  ? -14.901 4.563   -4.047  0.25 44.03  ? 50  TRP   B CD2 1 
ATOM   782  C CD2 D TRP   B 2 41  ? -16.782 3.983   -3.577  0.25 41.32  ? 50  TRP   B CD2 1 
ATOM   783  N NE1 A TRP   B 2 41  ? -16.533 4.312   -2.532  0.25 44.46  ? 50  TRP   B NE1 1 
ATOM   784  N NE1 B TRP   B 2 41  ? -15.046 5.356   -3.207  0.25 41.20  ? 50  TRP   B NE1 1 
ATOM   785  N NE1 C TRP   B 2 41  ? -16.533 4.312   -2.532  0.25 44.46  ? 50  TRP   B NE1 1 
ATOM   786  N NE1 D TRP   B 2 41  ? -15.046 5.356   -3.207  0.25 41.20  ? 50  TRP   B NE1 1 
ATOM   787  C CE2 A TRP   B 2 41  ? -15.356 4.970   -2.775  0.25 44.64  ? 50  TRP   B CE2 1 
ATOM   788  C CE2 B TRP   B 2 41  ? -16.239 4.933   -2.684  0.25 41.34  ? 50  TRP   B CE2 1 
ATOM   789  C CE2 C TRP   B 2 41  ? -15.356 4.970   -2.775  0.25 44.64  ? 50  TRP   B CE2 1 
ATOM   790  C CE2 D TRP   B 2 41  ? -16.239 4.933   -2.684  0.25 41.34  ? 50  TRP   B CE2 1 
ATOM   791  C CE3 A TRP   B 2 41  ? -13.695 5.093   -4.522  0.25 44.91  ? 50  TRP   B CE3 1 
ATOM   792  C CE3 B TRP   B 2 41  ? -18.013 3.398   -3.268  0.25 41.49  ? 50  TRP   B CE3 1 
ATOM   793  C CE3 C TRP   B 2 41  ? -13.695 5.093   -4.522  0.25 44.91  ? 50  TRP   B CE3 1 
ATOM   794  C CE3 D TRP   B 2 41  ? -18.013 3.398   -3.268  0.25 41.49  ? 50  TRP   B CE3 1 
ATOM   795  C CZ2 A TRP   B 2 41  ? -14.644 5.869   -1.979  0.25 45.19  ? 50  TRP   B CZ2 1 
ATOM   796  C CZ2 B TRP   B 2 41  ? -16.886 5.307   -1.510  0.25 41.13  ? 50  TRP   B CZ2 1 
ATOM   797  C CZ2 C TRP   B 2 41  ? -14.644 5.869   -1.979  0.25 45.19  ? 50  TRP   B CZ2 1 
ATOM   798  C CZ2 D TRP   B 2 41  ? -16.886 5.307   -1.510  0.25 41.13  ? 50  TRP   B CZ2 1 
ATOM   799  C CZ3 A TRP   B 2 41  ? -12.995 5.986   -3.740  0.25 44.98  ? 50  TRP   B CZ3 1 
ATOM   800  C CZ3 B TRP   B 2 41  ? -18.646 3.760   -2.099  0.25 41.28  ? 50  TRP   B CZ3 1 
ATOM   801  C CZ3 C TRP   B 2 41  ? -12.995 5.986   -3.740  0.25 44.98  ? 50  TRP   B CZ3 1 
ATOM   802  C CZ3 D TRP   B 2 41  ? -18.646 3.760   -2.099  0.25 41.28  ? 50  TRP   B CZ3 1 
ATOM   803  C CH2 A TRP   B 2 41  ? -13.464 6.367   -2.483  0.25 45.22  ? 50  TRP   B CH2 1 
ATOM   804  C CH2 B TRP   B 2 41  ? -18.095 4.710   -1.239  0.25 41.15  ? 50  TRP   B CH2 1 
ATOM   805  C CH2 C TRP   B 2 41  ? -13.464 6.367   -2.483  0.25 45.22  ? 50  TRP   B CH2 1 
ATOM   806  C CH2 D TRP   B 2 41  ? -18.095 4.710   -1.239  0.25 41.15  ? 50  TRP   B CH2 1 
ATOM   807  N N   . HIS   B 2 42  ? -14.377 4.819   -8.052  1.00 42.38  ? 51  HIS   B N   1 
ATOM   808  C CA  . HIS   B 2 42  ? -13.391 5.923   -8.288  1.00 43.82  ? 51  HIS   B CA  1 
ATOM   809  C C   . HIS   B 2 42  ? -14.004 7.095   -9.098  1.00 45.13  ? 51  HIS   B C   1 
ATOM   810  O O   . HIS   B 2 42  ? -13.415 8.171   -9.071  1.00 46.32  ? 51  HIS   B O   1 
ATOM   811  C CB  . HIS   B 2 42  ? -12.064 5.421   -8.851  1.00 42.89  ? 51  HIS   B CB  1 
ATOM   812  C CG  . HIS   B 2 42  ? -12.104 5.132   -10.306 1.00 43.56  ? 51  HIS   B CG  1 
ATOM   813  N ND1 . HIS   B 2 42  ? -12.302 3.849   -10.797 1.00 43.15  ? 51  HIS   B ND1 1 
ATOM   814  C CD2 . HIS   B 2 42  ? -11.984 5.944   -11.383 1.00 44.75  ? 51  HIS   B CD2 1 
ATOM   815  C CE1 . HIS   B 2 42  ? -12.317 3.892   -12.114 1.00 43.11  ? 51  HIS   B CE1 1 
ATOM   816  N NE2 . HIS   B 2 42  ? -12.151 5.175   -12.499 1.00 42.90  ? 51  HIS   B NE2 1 
ATOM   817  N N   . VAL   B 2 43  ? -15.158 6.917   -9.738  1.00 45.52  ? 52  VAL   B N   1 
ATOM   818  C CA  . VAL   B 2 43  ? -15.859 7.964   -10.539 1.00 46.46  ? 52  VAL   B CA  1 
ATOM   819  C C   . VAL   B 2 43  ? -16.568 8.945   -9.586  1.00 45.66  ? 52  VAL   B C   1 
ATOM   820  O O   . VAL   B 2 43  ? -16.322 10.159  -9.724  1.00 46.46  ? 52  VAL   B O   1 
ATOM   821  C CB  . VAL   B 2 43  ? -16.818 7.299   -11.555 1.00 46.83  ? 52  VAL   B CB  1 
ATOM   822  C CG1 . VAL   B 2 43  ? -17.736 8.273   -12.286 1.00 48.58  ? 52  VAL   B CG1 1 
ATOM   823  C CG2 . VAL   B 2 43  ? -16.069 6.456   -12.569 1.00 47.65  ? 52  VAL   B CG2 1 
ATOM   824  N N   . THR   B 2 44  ? -17.423 8.447   -8.672  1.00 45.18  ? 53  THR   B N   1 
ATOM   825  C CA  . THR   B 2 44  ? -18.315 9.277   -7.798  1.00 44.73  ? 53  THR   B CA  1 
ATOM   826  C C   . THR   B 2 44  ? -17.682 9.474   -6.420  1.00 45.66  ? 53  THR   B C   1 
ATOM   827  O O   . THR   B 2 44  ? -18.012 10.497  -5.748  1.00 45.79  ? 53  THR   B O   1 
ATOM   828  C CB  . THR   B 2 44  ? -19.722 8.673   -7.719  1.00 42.71  ? 53  THR   B CB  1 
ATOM   829  O OG1 . THR   B 2 44  ? -19.665 7.448   -6.987  1.00 40.54  ? 53  THR   B OG1 1 
ATOM   830  C CG2 . THR   B 2 44  ? -20.280 8.399   -9.102  1.00 41.54  ? 53  THR   B CG2 1 
ATOM   831  N N   . LYS   B 2 45  ? -16.791 8.562   -6.024  1.00 46.71  ? 54  LYS   B N   1 
ATOM   832  C CA  . LYS   B 2 45  ? -16.315 8.416   -4.620  1.00 51.91  ? 54  LYS   B CA  1 
ATOM   833  C C   . LYS   B 2 45  ? -17.498 8.180   -3.668  1.00 49.41  ? 54  LYS   B C   1 
ATOM   834  O O   . LYS   B 2 45  ? -17.357 8.527   -2.507  1.00 52.10  ? 54  LYS   B O   1 
ATOM   835  C CB  . LYS   B 2 45  ? -15.571 9.659   -4.121  1.00 56.21  ? 54  LYS   B CB  1 
ATOM   836  C CG  . LYS   B 2 45  ? -14.494 10.197  -5.040  1.00 61.18  ? 54  LYS   B CG  1 
ATOM   837  C CD  . LYS   B 2 45  ? -13.323 9.292   -5.124  1.00 66.46  ? 54  LYS   B CD  1 
ATOM   838  C CE  . LYS   B 2 45  ? -12.286 9.861   -6.068  1.00 75.50  ? 54  LYS   B CE  1 
ATOM   839  N NZ  . LYS   B 2 45  ? -11.414 8.795   -6.621  1.00 83.01  ? 54  LYS   B NZ  1 
ATOM   840  N N   . GLY   B 2 46  ? -18.616 7.624   -4.130  1.00 48.07  ? 55  GLY   B N   1 
ATOM   841  C CA  . GLY   B 2 46  ? -19.785 7.355   -3.276  1.00 47.56  ? 55  GLY   B CA  1 
ATOM   842  C C   . GLY   B 2 46  ? -20.648 8.585   -3.046  1.00 47.83  ? 55  GLY   B C   1 
ATOM   843  O O   . GLY   B 2 46  ? -21.648 8.454   -2.380  1.00 48.35  ? 55  GLY   B O   1 
ATOM   844  N N   . ALA   B 2 47  ? -20.360 9.715   -3.686  1.00 49.97  ? 56  ALA   B N   1 
ATOM   845  C CA  . ALA   B 2 47  ? -21.198 10.940  -3.640  1.00 48.34  ? 56  ALA   B CA  1 
ATOM   846  C C   . ALA   B 2 47  ? -22.551 10.709  -4.318  1.00 48.19  ? 56  ALA   B C   1 
ATOM   847  O O   . ALA   B 2 47  ? -22.648 9.885   -5.235  1.00 46.59  ? 56  ALA   B O   1 
ATOM   848  C CB  . ALA   B 2 47  ? -20.477 12.103  -4.287  1.00 47.93  ? 56  ALA   B CB  1 
ATOM   849  N N   . ALA   B 2 48  ? -23.558 11.466  -3.883  1.00 46.74  ? 57  ALA   B N   1 
ATOM   850  C CA  . ALA   B 2 48  ? -24.879 11.592  -4.525  1.00 46.33  ? 57  ALA   B CA  1 
ATOM   851  C C   . ALA   B 2 48  ? -24.744 12.253  -5.906  1.00 47.43  ? 57  ALA   B C   1 
ATOM   852  O O   . ALA   B 2 48  ? -23.714 12.940  -6.181  1.00 49.57  ? 57  ALA   B O   1 
ATOM   853  C CB  . ALA   B 2 48  ? -25.803 12.378  -3.635  1.00 48.33  ? 57  ALA   B CB  1 
ATOM   854  N N   . LEU   B 2 49  ? -25.755 12.031  -6.745  1.00 45.45  ? 58  LEU   B N   1 
ATOM   855  C CA  . LEU   B 2 49  ? -25.811 12.459  -8.171  1.00 48.24  ? 58  LEU   B CA  1 
ATOM   856  C C   . LEU   B 2 49  ? -27.161 13.109  -8.478  1.00 49.87  ? 58  LEU   B C   1 
ATOM   857  O O   . LEU   B 2 49  ? -28.190 12.677  -7.923  1.00 54.15  ? 58  LEU   B O   1 
ATOM   858  C CB  . LEU   B 2 49  ? -25.664 11.246  -9.088  1.00 45.95  ? 58  LEU   B CB  1 
ATOM   859  C CG  . LEU   B 2 49  ? -24.423 10.371  -8.906  1.00 44.68  ? 58  LEU   B CG  1 
ATOM   860  C CD1 . LEU   B 2 49  ? -24.602 9.100   -9.700  1.00 44.10  ? 58  LEU   B CD1 1 
ATOM   861  C CD2 . LEU   B 2 49  ? -23.146 11.096  -9.306  1.00 44.36  ? 58  LEU   B CD2 1 
ATOM   862  N N   . ARG   B 2 50  ? -27.164 14.072  -9.381  1.00 50.73  ? 59  ARG   B N   1 
ATOM   863  C CA  . ARG   B 2 50  ? -28.407 14.678  -9.896  1.00 52.96  ? 59  ARG   B CA  1 
ATOM   864  C C   . ARG   B 2 50  ? -28.792 13.988  -11.216 1.00 53.10  ? 59  ARG   B C   1 
ATOM   865  O O   . ARG   B 2 50  ? -27.898 13.536  -11.966 1.00 51.40  ? 59  ARG   B O   1 
ATOM   866  C CB  . ARG   B 2 50  ? -28.132 16.176  -9.963  1.00 59.71  ? 59  ARG   B CB  1 
ATOM   867  C CG  . ARG   B 2 50  ? -29.324 17.027  -10.379 1.00 66.95  ? 59  ARG   B CG  1 
ATOM   868  C CD  . ARG   B 2 50  ? -29.051 18.498  -10.117 1.00 69.89  ? 59  ARG   B CD  1 
ATOM   869  N NE  . ARG   B 2 50  ? -27.667 18.878  -10.429 1.00 71.68  ? 59  ARG   B NE  1 
ATOM   870  C CZ  . ARG   B 2 50  ? -27.212 19.210  -11.638 1.00 74.35  ? 59  ARG   B CZ  1 
ATOM   871  N NH1 . ARG   B 2 50  ? -28.010 19.168  -12.697 1.00 73.47  ? 59  ARG   B NH1 1 
ATOM   872  N NH2 . ARG   B 2 50  ? -25.947 19.574  -11.782 1.00 76.80  ? 59  ARG   B NH2 1 
ATOM   873  N N   . SER   B 2 51  ? -30.086 13.782  -11.419 1.00 53.93  ? 60  SER   B N   1 
ATOM   874  C CA  . SER   B 2 51  ? -30.729 13.430  -12.711 1.00 58.17  ? 60  SER   B CA  1 
ATOM   875  C C   . SER   B 2 51  ? -31.968 14.323  -12.893 1.00 59.82  ? 60  SER   B C   1 
ATOM   876  O O   . SER   B 2 51  ? -32.999 14.071  -12.259 1.00 62.12  ? 60  SER   B O   1 
ATOM   877  C CB  . SER   B 2 51  ? -31.091 11.971  -12.754 1.00 56.89  ? 60  SER   B CB  1 
ATOM   878  O OG  . SER   B 2 51  ? -31.803 11.680  -13.943 1.00 56.13  ? 60  SER   B OG  1 
ATOM   879  N N   . GLY   B 2 52  ? -31.866 15.375  -13.686 1.00 64.72  ? 61  GLY   B N   1 
ATOM   880  C CA  . GLY   B 2 52  ? -32.930 16.390  -13.760 1.00 69.68  ? 61  GLY   B CA  1 
ATOM   881  C C   . GLY   B 2 52  ? -32.947 17.196  -12.482 1.00 72.64  ? 61  GLY   B C   1 
ATOM   882  O O   . GLY   B 2 52  ? -31.865 17.603  -12.024 1.00 76.91  ? 61  GLY   B O   1 
ATOM   883  N N   . GLU   B 2 53  ? -34.116 17.394  -11.888 1.00 76.99  ? 62  GLU   B N   1 
ATOM   884  C CA  . GLU   B 2 53  ? -34.164 17.918  -10.504 1.00 80.83  ? 62  GLU   B CA  1 
ATOM   885  C C   . GLU   B 2 53  ? -34.260 16.734  -9.538  1.00 76.87  ? 62  GLU   B C   1 
ATOM   886  O O   . GLU   B 2 53  ? -34.142 16.992  -8.348  1.00 81.12  ? 62  GLU   B O   1 
ATOM   887  C CB  . GLU   B 2 53  ? -35.220 19.019  -10.388 1.00 85.10  ? 62  GLU   B CB  1 
ATOM   888  C CG  . GLU   B 2 53  ? -34.642 20.366  -10.814 1.00 93.39  ? 62  GLU   B CG  1 
ATOM   889  C CD  . GLU   B 2 53  ? -35.349 21.616  -10.311 1.00 101.34 ? 62  GLU   B CD  1 
ATOM   890  O OE1 . GLU   B 2 53  ? -36.560 21.541  -10.028 1.00 107.46 ? 62  GLU   B OE1 1 
ATOM   891  O OE2 . GLU   B 2 53  ? -34.679 22.669  -10.197 1.00 106.67 ? 62  GLU   B OE2 1 
ATOM   892  N N   . GLY   B 2 54  ? -34.345 15.492  -10.046 1.00 74.35  ? 63  GLY   B N   1 
ATOM   893  C CA  . GLY   B 2 54  ? -34.260 14.240  -9.260  1.00 71.72  ? 63  GLY   B CA  1 
ATOM   894  C C   . GLY   B 2 54  ? -32.887 14.039  -8.623  1.00 68.27  ? 63  GLY   B C   1 
ATOM   895  O O   . GLY   B 2 54  ? -31.914 14.651  -9.128  1.00 65.31  ? 63  GLY   B O   1 
ATOM   896  N N   . ARG   B 2 55  ? -32.807 13.235  -7.546  1.00 63.38  ? 64  ARG   B N   1 
ATOM   897  C CA  . ARG   B 2 55  ? -31.553 12.930  -6.784  1.00 62.69  ? 64  ARG   B CA  1 
ATOM   898  C C   . ARG   B 2 55  ? -31.327 11.412  -6.674  1.00 58.27  ? 64  ARG   B C   1 
ATOM   899  O O   . ARG   B 2 55  ? -32.294 10.671  -6.495  1.00 57.57  ? 64  ARG   B O   1 
ATOM   900  C CB  . ARG   B 2 55  ? -31.577 13.511  -5.367  1.00 66.73  ? 64  ARG   B CB  1 
ATOM   901  C CG  . ARG   B 2 55  ? -30.230 13.457  -4.657  1.00 70.01  ? 64  ARG   B CG  1 
ATOM   902  C CD  . ARG   B 2 55  ? -30.412 13.633  -3.167  1.00 75.52  ? 64  ARG   B CD  1 
ATOM   903  N NE  . ARG   B 2 55  ? -29.219 13.428  -2.355  1.00 76.24  ? 64  ARG   B NE  1 
ATOM   904  C CZ  . ARG   B 2 55  ? -28.596 14.361  -1.633  1.00 78.29  ? 64  ARG   B CZ  1 
ATOM   905  N NH1 . ARG   B 2 55  ? -29.036 15.608  -1.624  1.00 77.78  ? 64  ARG   B NH1 1 
ATOM   906  N NH2 . ARG   B 2 55  ? -27.536 14.036  -0.900  1.00 79.53  ? 64  ARG   B NH2 1 
ATOM   907  N N   . LEU   B 2 56  ? -30.078 10.967  -6.779  1.00 53.97  ? 65  LEU   B N   1 
ATOM   908  C CA  . LEU   B 2 56  ? -29.720 9.530   -6.753  1.00 52.90  ? 65  LEU   B CA  1 
ATOM   909  C C   . LEU   B 2 56  ? -28.809 9.348   -5.542  1.00 50.45  ? 65  LEU   B C   1 
ATOM   910  O O   . LEU   B 2 56  ? -27.711 9.963   -5.564  1.00 50.88  ? 65  LEU   B O   1 
ATOM   911  C CB  . LEU   B 2 56  ? -28.988 9.131   -8.046  1.00 52.35  ? 65  LEU   B CB  1 
ATOM   912  C CG  . LEU   B 2 56  ? -29.693 9.284   -9.396  1.00 55.36  ? 65  LEU   B CG  1 
ATOM   913  C CD1 . LEU   B 2 56  ? -29.073 8.320   -10.398 1.00 54.61  ? 65  LEU   B CD1 1 
ATOM   914  C CD2 . LEU   B 2 56  ? -31.189 9.020   -9.318  1.00 56.72  ? 65  LEU   B CD2 1 
ATOM   915  N N   . ASP   B 2 57  ? -29.233 8.570   -4.536  1.00 48.53  ? 66  ASP   B N   1 
ATOM   916  C CA  . ASP   B 2 57  ? -28.403 8.308   -3.328  1.00 47.00  ? 66  ASP   B CA  1 
ATOM   917  C C   . ASP   B 2 57  ? -27.725 6.945   -3.429  1.00 42.75  ? 66  ASP   B C   1 
ATOM   918  O O   . ASP   B 2 57  ? -28.368 5.955   -3.817  1.00 41.49  ? 66  ASP   B O   1 
ATOM   919  C CB  . ASP   B 2 57  ? -29.235 8.364   -2.051  1.00 52.07  ? 66  ASP   B CB  1 
ATOM   920  C CG  . ASP   B 2 57  ? -29.817 9.743   -1.795  1.00 55.78  ? 66  ASP   B CG  1 
ATOM   921  O OD1 . ASP   B 2 57  ? -29.039 10.708  -1.797  1.00 60.18  ? 66  ASP   B OD1 1 
ATOM   922  O OD2 . ASP   B 2 57  ? -31.050 9.844   -1.649  1.00 60.52  ? 66  ASP   B OD2 1 
ATOM   923  N N   . PRO   B 2 58  ? -26.444 6.834   -3.015  1.00 39.69  ? 67  PRO   B N   1 
ATOM   924  C CA  . PRO   B 2 58  ? -25.740 5.553   -3.050  1.00 39.84  ? 67  PRO   B CA  1 
ATOM   925  C C   . PRO   B 2 58  ? -26.512 4.536   -2.192  1.00 40.94  ? 67  PRO   B C   1 
ATOM   926  O O   . PRO   B 2 58  ? -27.215 4.906   -1.231  1.00 43.30  ? 67  PRO   B O   1 
ATOM   927  C CB  . PRO   B 2 58  ? -24.349 5.851   -2.467  1.00 39.74  ? 67  PRO   B CB  1 
ATOM   928  C CG  . PRO   B 2 58  ? -24.574 7.100   -1.640  1.00 40.00  ? 67  PRO   B CG  1 
ATOM   929  C CD  . PRO   B 2 58  ? -25.622 7.889   -2.396  1.00 39.93  ? 67  PRO   B CD  1 
ATOM   930  N N   . TYR   B 2 59  ? -26.416 3.266   -2.551  1.00 38.57  ? 68  TYR   B N   1 
ATOM   931  C CA  . TYR   B 2 59  ? -27.133 2.184   -1.852  1.00 38.40  ? 68  TYR   B CA  1 
ATOM   932  C C   . TYR   B 2 59  ? -26.137 1.122   -1.429  1.00 37.05  ? 68  TYR   B C   1 
ATOM   933  O O   . TYR   B 2 59  ? -26.282 0.562   -0.349  1.00 38.38  ? 68  TYR   B O   1 
ATOM   934  C CB  . TYR   B 2 59  ? -28.237 1.641   -2.752  1.00 38.96  ? 68  TYR   B CB  1 
ATOM   935  C CG  . TYR   B 2 59  ? -29.069 0.535   -2.167  1.00 38.68  ? 68  TYR   B CG  1 
ATOM   936  C CD1 . TYR   B 2 59  ? -28.585 -0.759  -2.127  1.00 38.76  ? 68  TYR   B CD1 1 
ATOM   937  C CD2 . TYR   B 2 59  ? -30.380 0.766   -1.780  1.00 39.53  ? 68  TYR   B CD2 1 
ATOM   938  C CE1 . TYR   B 2 59  ? -29.376 -1.803  -1.666  1.00 40.16  ? 68  TYR   B CE1 1 
ATOM   939  C CE2 . TYR   B 2 59  ? -31.185 -0.263  -1.311  1.00 40.42  ? 68  TYR   B CE2 1 
ATOM   940  C CZ  . TYR   B 2 59  ? -30.671 -1.549  -1.235  1.00 41.31  ? 68  TYR   B CZ  1 
ATOM   941  O OH  . TYR   B 2 59  ? -31.423 -2.575  -0.732  1.00 43.49  ? 68  TYR   B OH  1 
ATOM   942  N N   . TRP   B 2 60  ? -25.181 0.841   -2.282  1.00 35.05  ? 69  TRP   B N   1 
ATOM   943  C CA  . TRP   B 2 60  ? -24.165 -0.233  -2.109  1.00 34.55  ? 69  TRP   B CA  1 
ATOM   944  C C   . TRP   B 2 60  ? -22.862 0.246   -2.725  1.00 35.08  ? 69  TRP   B C   1 
ATOM   945  O O   . TRP   B 2 60  ? -22.883 0.843   -3.857  1.00 37.06  ? 69  TRP   B O   1 
ATOM   946  C CB  . TRP   B 2 60  ? -24.615 -1.604  -2.629  1.00 33.91  ? 69  TRP   B CB  1 
ATOM   947  C CG  . TRP   B 2 60  ? -23.493 -2.597  -2.561  1.00 34.95  ? 69  TRP   B CG  1 
ATOM   948  C CD1 . TRP   B 2 60  ? -23.097 -3.323  -1.469  1.00 35.29  ? 69  TRP   B CD1 1 
ATOM   949  C CD2 . TRP   B 2 60  ? -22.567 -2.939  -3.619  1.00 35.57  ? 69  TRP   B CD2 1 
ATOM   950  N NE1 . TRP   B 2 60  ? -21.971 -4.054  -1.771  1.00 36.03  ? 69  TRP   B NE1 1 
ATOM   951  C CE2 . TRP   B 2 60  ? -21.622 -3.841  -3.085  1.00 35.86  ? 69  TRP   B CE2 1 
ATOM   952  C CE3 . TRP   B 2 60  ? -22.399 -2.509  -4.943  1.00 36.24  ? 69  TRP   B CE3 1 
ATOM   953  C CZ2 . TRP   B 2 60  ? -20.576 -4.368  -3.844  1.00 35.80  ? 69  TRP   B CZ2 1 
ATOM   954  C CZ3 . TRP   B 2 60  ? -21.370 -3.037  -5.699  1.00 36.28  ? 69  TRP   B CZ3 1 
ATOM   955  C CH2 . TRP   B 2 60  ? -20.460 -3.935  -5.150  1.00 36.56  ? 69  TRP   B CH2 1 
ATOM   956  N N   . GLY   B 2 61  ? -21.751 -0.062  -2.087  1.00 36.41  ? 70  GLY   B N   1 
ATOM   957  C CA  . GLY   B 2 61  ? -20.427 0.157   -2.695  1.00 37.69  ? 70  GLY   B CA  1 
ATOM   958  C C   . GLY   B 2 61  ? -19.355 -0.626  -2.003  1.00 38.02  ? 70  GLY   B C   1 
ATOM   959  O O   . GLY   B 2 61  ? -19.563 -1.022  -0.821  1.00 38.81  ? 70  GLY   B O   1 
ATOM   960  N N   . ASP   B 2 62  ? -18.212 -0.717  -2.653  1.00 38.26  ? 71  ASP   B N   1 
ATOM   961  C CA  . ASP   B 2 62  ? -17.036 -1.499  -2.203  1.00 39.50  ? 71  ASP   B CA  1 
ATOM   962  C C   . ASP   B 2 62  ? -15.850 -0.956  -2.974  1.00 39.19  ? 71  ASP   B C   1 
ATOM   963  O O   . ASP   B 2 62  ? -15.819 -1.133  -4.227  1.00 41.18  ? 71  ASP   B O   1 
ATOM   964  C CB  . ASP   B 2 62  ? -17.255 -2.987  -2.385  1.00 42.10  ? 71  ASP   B CB  1 
ATOM   965  C CG  . ASP   B 2 62  ? -16.158 -3.859  -1.799  1.00 47.42  ? 71  ASP   B CG  1 
ATOM   966  O OD1 . ASP   B 2 62  ? -14.979 -3.500  -1.881  1.00 52.49  ? 71  ASP   B OD1 1 
ATOM   967  O OD2 . ASP   B 2 62  ? -16.499 -4.936  -1.306  1.00 56.88  ? 71  ASP   B OD2 1 
ATOM   968  N N   . VAL   B 2 63  ? -14.979 -0.228  -2.281  1.00 38.83  ? 72  VAL   B N   1 
ATOM   969  C CA  . VAL   B 2 63  ? -13.743 0.398   -2.833  1.00 39.40  ? 72  VAL   B CA  1 
ATOM   970  C C   . VAL   B 2 63  ? -12.849 -0.715  -3.394  1.00 42.08  ? 72  VAL   B C   1 
ATOM   971  O O   . VAL   B 2 63  ? -12.117 -0.452  -4.398  1.00 44.51  ? 72  VAL   B O   1 
ATOM   972  C CB  . VAL   B 2 63  ? -13.005 1.220   -1.757  1.00 38.86  ? 72  VAL   B CB  1 
ATOM   973  C CG1 . VAL   B 2 63  ? -11.528 1.322   -1.997  1.00 38.75  ? 72  VAL   B CG1 1 
ATOM   974  C CG2 . VAL   B 2 63  ? -13.569 2.622   -1.560  1.00 39.47  ? 72  VAL   B CG2 1 
ATOM   975  N N   . LYS   B 2 64  ? -12.872 -1.915  -2.808  1.00 43.49  ? 73  LYS   B N   1 
ATOM   976  C CA  . LYS   B 2 64  ? -11.944 -2.974  -3.284  1.00 44.94  ? 73  LYS   B CA  1 
ATOM   977  C C   . LYS   B 2 64  ? -12.394 -3.500  -4.657  1.00 45.10  ? 73  LYS   B C   1 
ATOM   978  O O   . LYS   B 2 64  ? -11.518 -3.666  -5.495  1.00 47.28  ? 73  LYS   B O   1 
ATOM   979  C CB  . LYS   B 2 64  ? -11.813 -4.166  -2.340  1.00 45.00  ? 73  LYS   B CB  1 
ATOM   980  C CG  . LYS   B 2 64  ? -10.667 -5.046  -2.809  1.00 45.94  ? 73  LYS   B CG  1 
ATOM   981  C CD  . LYS   B 2 64  ? -10.380 -6.192  -1.968  1.00 47.25  ? 73  LYS   B CD  1 
ATOM   982  C CE  . LYS   B 2 64  ? -9.091  -6.853  -2.401  1.00 50.07  ? 73  LYS   B CE  1 
ATOM   983  N NZ  . LYS   B 2 64  ? -8.826  -8.027  -1.545  1.00 50.82  ? 73  LYS   B NZ  1 
ATOM   984  N N   . GLN   B 2 65  ? -13.687 -3.825  -4.828  1.00 45.18  ? 74  GLN   B N   1 
ATOM   985  C CA  . GLN   B 2 65  ? -14.332 -4.175  -6.122  1.00 45.11  ? 74  GLN   B CA  1 
ATOM   986  C C   . GLN   B 2 65  ? -14.335 -2.966  -7.080  1.00 43.96  ? 74  GLN   B C   1 
ATOM   987  O O   . GLN   B 2 65  ? -14.480 -3.187  -8.317  1.00 42.88  ? 74  GLN   B O   1 
ATOM   988  C CB  . GLN   B 2 65  ? -15.774 -4.634  -5.929  1.00 46.56  ? 74  GLN   B CB  1 
ATOM   989  C CG  . GLN   B 2 65  ? -15.897 -5.969  -5.214  1.00 49.04  ? 74  GLN   B CG  1 
ATOM   990  C CD  . GLN   B 2 65  ? -17.349 -6.390  -5.083  1.00 51.97  ? 74  GLN   B CD  1 
ATOM   991  O OE1 . GLN   B 2 65  ? -18.091 -6.568  -6.065  1.00 53.92  ? 74  GLN   B OE1 1 
ATOM   992  N NE2 . GLN   B 2 65  ? -17.799 -6.501  -3.848  1.00 51.58  ? 74  GLN   B NE2 1 
ATOM   993  N N   . ASP   B 2 66  ? -14.158 -1.768  -6.522  1.00 41.80  ? 75  ASP   B N   1 
ATOM   994  C CA  . ASP   B 2 66  ? -14.220 -0.419  -7.142  1.00 41.46  ? 75  ASP   B CA  1 
ATOM   995  C C   . ASP   B 2 66  ? -15.562 -0.273  -7.839  1.00 40.09  ? 75  ASP   B C   1 
ATOM   996  O O   . ASP   B 2 66  ? -15.500 0.181   -8.987  1.00 40.26  ? 75  ASP   B O   1 
ATOM   997  C CB  . ASP   B 2 66  ? -13.087 -0.192  -8.159  1.00 41.96  ? 75  ASP   B CB  1 
ATOM   998  C CG  . ASP   B 2 66  ? -13.055 1.198   -8.799  1.00 40.80  ? 75  ASP   B CG  1 
ATOM   999  O OD1 . ASP   B 2 66  ? -13.393 2.203   -8.119  1.00 39.04  ? 75  ASP   B OD1 1 
ATOM   1000 O OD2 . ASP   B 2 66  ? -12.694 1.266   -10.013 1.00 41.56  ? 75  ASP   B OD2 1 
ATOM   1001 N N   . LEU   B 2 67  ? -16.674 -0.706  -7.212  1.00 37.94  ? 76  LEU   B N   1 
ATOM   1002 C CA  . LEU   B 2 67  ? -18.063 -0.597  -7.740  1.00 37.93  ? 76  LEU   B CA  1 
ATOM   1003 C C   . LEU   B 2 67  ? -18.975 0.182   -6.792  1.00 39.52  ? 76  LEU   B C   1 
ATOM   1004 O O   . LEU   B 2 67  ? -18.746 0.145   -5.550  1.00 39.80  ? 76  LEU   B O   1 
ATOM   1005 C CB  . LEU   B 2 67  ? -18.592 -2.011  -7.976  1.00 38.67  ? 76  LEU   B CB  1 
ATOM   1006 C CG  . LEU   B 2 67  ? -17.888 -2.821  -9.086  1.00 39.29  ? 76  LEU   B CG  1 
ATOM   1007 C CD1 . LEU   B 2 67  ? -18.556 -4.176  -9.292  1.00 39.40  ? 76  LEU   B CD1 1 
ATOM   1008 C CD2 . LEU   B 2 67  ? -17.927 -2.051  -10.418 1.00 41.44  ? 76  LEU   B CD2 1 
ATOM   1009 N N   . VAL   B 2 68  ? -20.039 0.795   -7.325  1.00 40.78  ? 77  VAL   B N   1 
ATOM   1010 C CA  . VAL   B 2 68  ? -21.127 1.444   -6.523  1.00 38.75  ? 77  VAL   B CA  1 
ATOM   1011 C C   . VAL   B 2 68  ? -22.474 1.388   -7.268  1.00 38.10  ? 77  VAL   B C   1 
ATOM   1012 O O   . VAL   B 2 68  ? -22.481 1.617   -8.519  1.00 39.29  ? 77  VAL   B O   1 
ATOM   1013 C CB  . VAL   B 2 68  ? -20.742 2.887   -6.152  1.00 38.86  ? 77  VAL   B CB  1 
ATOM   1014 C CG1 . VAL   B 2 68  ? -20.491 3.740   -7.377  1.00 38.85  ? 77  VAL   B CG1 1 
ATOM   1015 C CG2 . VAL   B 2 68  ? -21.777 3.545   -5.232  1.00 38.40  ? 77  VAL   B CG2 1 
ATOM   1016 N N   . SER   B 2 69  ? -23.577 1.171   -6.542  1.00 35.90  ? 78  SER   B N   1 
ATOM   1017 C CA  . SER   B 2 69  ? -24.964 1.187   -7.071  1.00 36.09  ? 78  SER   B CA  1 
ATOM   1018 C C   . SER   B 2 69  ? -25.762 2.337   -6.439  1.00 36.41  ? 78  SER   B C   1 
ATOM   1019 O O   . SER   B 2 69  ? -25.551 2.663   -5.219  1.00 36.11  ? 78  SER   B O   1 
ATOM   1020 C CB  . SER   B 2 69  ? -25.653 -0.172  -6.935  1.00 36.12  ? 78  SER   B CB  1 
ATOM   1021 O OG  . SER   B 2 69  ? -26.080 -0.430  -5.588  1.00 37.89  ? 78  SER   B OG  1 
ATOM   1022 N N   . TYR   B 2 70  ? -26.736 2.886   -7.170  1.00 36.38  ? 79  TYR   B N   1 
ATOM   1023 C CA  . TYR   B 2 70  ? -27.597 4.005   -6.688  1.00 35.88  ? 79  TYR   B CA  1 
ATOM   1024 C C   . TYR   B 2 70  ? -29.074 3.599   -6.812  1.00 36.70  ? 79  TYR   B C   1 
ATOM   1025 O O   . TYR   B 2 70  ? -29.465 3.050   -7.845  1.00 36.41  ? 79  TYR   B O   1 
ATOM   1026 C CB  . TYR   B 2 70  ? -27.305 5.302   -7.450  1.00 35.41  ? 79  TYR   B CB  1 
ATOM   1027 C CG  . TYR   B 2 70  ? -25.971 5.935   -7.158  1.00 35.58  ? 79  TYR   B CG  1 
ATOM   1028 C CD1 . TYR   B 2 70  ? -24.805 5.419   -7.671  1.00 36.34  ? 79  TYR   B CD1 1 
ATOM   1029 C CD2 . TYR   B 2 70  ? -25.858 7.042   -6.330  1.00 38.04  ? 79  TYR   B CD2 1 
ATOM   1030 C CE1 . TYR   B 2 70  ? -23.567 5.976   -7.393  1.00 36.71  ? 79  TYR   B CE1 1 
ATOM   1031 C CE2 . TYR   B 2 70  ? -24.627 7.631   -6.042  1.00 37.97  ? 79  TYR   B CE2 1 
ATOM   1032 C CZ  . TYR   B 2 70  ? -23.473 7.085   -6.571  1.00 37.22  ? 79  TYR   B CZ  1 
ATOM   1033 O OH  . TYR   B 2 70  ? -22.241 7.634   -6.331  1.00 39.27  ? 79  TYR   B OH  1 
ATOM   1034 N N   A CYS   B 2 71  ? -29.839 3.865   -5.744  0.25 36.93  ? 80  CYS   B N   1 
ATOM   1035 N N   B CYS   B 2 71  ? -29.839 3.865   -5.744  0.25 36.93  ? 80  CYS   B N   1 
ATOM   1036 N N   C CYS   B 2 71  ? -29.859 3.844   -5.756  0.25 36.82  ? 80  CYS   B N   1 
ATOM   1037 N N   D CYS   B 2 71  ? -29.859 3.844   -5.756  0.25 36.82  ? 80  CYS   B N   1 
ATOM   1038 C CA  A CYS   B 2 71  ? -31.315 3.703   -5.593  0.25 37.75  ? 80  CYS   B CA  1 
ATOM   1039 C CA  B CYS   B 2 71  ? -31.315 3.703   -5.593  0.25 37.75  ? 80  CYS   B CA  1 
ATOM   1040 C CA  C CYS   B 2 71  ? -31.339 3.675   -5.693  0.25 37.58  ? 80  CYS   B CA  1 
ATOM   1041 C CA  D CYS   B 2 71  ? -31.339 3.675   -5.693  0.25 37.58  ? 80  CYS   B CA  1 
ATOM   1042 C C   A CYS   B 2 71  ? -31.683 2.251   -5.252  0.25 37.59  ? 80  CYS   B C   1 
ATOM   1043 C C   B CYS   B 2 71  ? -31.683 2.251   -5.252  0.25 37.59  ? 80  CYS   B C   1 
ATOM   1044 C C   C CYS   B 2 71  ? -31.725 2.206   -5.497  0.25 37.66  ? 80  CYS   B C   1 
ATOM   1045 C C   D CYS   B 2 71  ? -31.725 2.206   -5.497  0.25 37.66  ? 80  CYS   B C   1 
ATOM   1046 O O   A CYS   B 2 71  ? -32.826 2.030   -4.797  0.25 37.69  ? 80  CYS   B O   1 
ATOM   1047 O O   B CYS   B 2 71  ? -32.826 2.030   -4.797  0.25 37.69  ? 80  CYS   B O   1 
ATOM   1048 O O   C CYS   B 2 71  ? -32.943 1.910   -5.490  0.25 38.24  ? 80  CYS   B O   1 
ATOM   1049 O O   D CYS   B 2 71  ? -32.943 1.910   -5.490  0.25 38.24  ? 80  CYS   B O   1 
ATOM   1050 C CB  A CYS   B 2 71  ? -32.078 4.201   -6.817  0.25 39.00  ? 80  CYS   B CB  1 
ATOM   1051 C CB  B CYS   B 2 71  ? -32.078 4.201   -6.817  0.25 39.00  ? 80  CYS   B CB  1 
ATOM   1052 C CB  C CYS   B 2 71  ? -32.011 4.191   -6.958  0.25 38.55  ? 80  CYS   B CB  1 
ATOM   1053 C CB  D CYS   B 2 71  ? -32.011 4.191   -6.958  0.25 38.55  ? 80  CYS   B CB  1 
ATOM   1054 S SG  A CYS   B 2 71  ? -32.088 6.024   -6.956  0.25 40.29  ? 80  CYS   B SG  1 
ATOM   1055 S SG  B CYS   B 2 71  ? -32.088 6.024   -6.956  0.25 40.29  ? 80  CYS   B SG  1 
ATOM   1056 S SG  C CYS   B 2 71  ? -31.154 5.635   -7.659  0.25 39.07  ? 80  CYS   B SG  1 
ATOM   1057 S SG  D CYS   B 2 71  ? -31.154 5.635   -7.659  0.25 39.07  ? 80  CYS   B SG  1 
ATOM   1058 N N   . GLY   B 2 72  ? -30.747 1.306   -5.384  1.00 36.77  ? 81  GLY   B N   1 
ATOM   1059 C CA  . GLY   B 2 72  ? -31.081 -0.114  -5.211  1.00 36.62  ? 81  GLY   B CA  1 
ATOM   1060 C C   . GLY   B 2 72  ? -29.824 -0.951  -5.246  1.00 35.53  ? 81  GLY   B C   1 
ATOM   1061 O O   . GLY   B 2 72  ? -28.717 -0.435  -5.420  1.00 35.78  ? 81  GLY   B O   1 
ATOM   1062 N N   . PRO   B 2 73  ? -29.970 -2.257  -5.019  1.00 36.04  ? 82  PRO   B N   1 
ATOM   1063 C CA  . PRO   B 2 73  ? -28.818 -3.163  -5.035  1.00 37.88  ? 82  PRO   B CA  1 
ATOM   1064 C C   . PRO   B 2 73  ? -28.287 -3.392  -6.464  1.00 40.07  ? 82  PRO   B C   1 
ATOM   1065 O O   . PRO   B 2 73  ? -29.089 -3.303  -7.377  1.00 40.96  ? 82  PRO   B O   1 
ATOM   1066 C CB  . PRO   B 2 73  ? -29.397 -4.465  -4.427  1.00 37.16  ? 82  PRO   B CB  1 
ATOM   1067 C CG  . PRO   B 2 73  ? -30.903 -4.403  -4.686  1.00 37.22  ? 82  PRO   B CG  1 
ATOM   1068 C CD  . PRO   B 2 73  ? -31.259 -2.933  -4.803  1.00 36.79  ? 82  PRO   B CD  1 
ATOM   1069 N N   . TRP   B 2 74  ? -26.996 -3.740  -6.606  1.00 41.12  ? 83  TRP   B N   1 
ATOM   1070 C CA  . TRP   B 2 74  ? -26.352 -4.217  -7.848  1.00 41.64  ? 83  TRP   B CA  1 
ATOM   1071 C C   . TRP   B 2 74  ? -27.261 -5.213  -8.576  1.00 44.51  ? 83  TRP   B C   1 
ATOM   1072 O O   . TRP   B 2 74  ? -27.617 -6.220  -7.974  1.00 45.60  ? 83  TRP   B O   1 
ATOM   1073 C CB  . TRP   B 2 74  ? -24.984 -4.831  -7.561  1.00 41.31  ? 83  TRP   B CB  1 
ATOM   1074 C CG  . TRP   B 2 74  ? -24.198 -5.003  -8.822  1.00 40.48  ? 83  TRP   B CG  1 
ATOM   1075 C CD1 . TRP   B 2 74  ? -24.184 -6.096  -9.637  1.00 39.91  ? 83  TRP   B CD1 1 
ATOM   1076 C CD2 . TRP   B 2 74  ? -23.360 -4.015  -9.451  1.00 39.46  ? 83  TRP   B CD2 1 
ATOM   1077 N NE1 . TRP   B 2 74  ? -23.356 -5.875  -10.704 1.00 39.81  ? 83  TRP   B NE1 1 
ATOM   1078 C CE2 . TRP   B 2 74  ? -22.858 -4.597  -10.637 1.00 39.27  ? 83  TRP   B CE2 1 
ATOM   1079 C CE3 . TRP   B 2 74  ? -23.024 -2.685  -9.159  1.00 39.16  ? 83  TRP   B CE3 1 
ATOM   1080 C CZ2 . TRP   B 2 74  ? -22.020 -3.903  -11.512 1.00 38.22  ? 83  TRP   B CZ2 1 
ATOM   1081 C CZ3 . TRP   B 2 74  ? -22.187 -2.006  -10.019 1.00 39.33  ? 83  TRP   B CZ3 1 
ATOM   1082 C CH2 . TRP   B 2 74  ? -21.699 -2.608  -11.191 1.00 38.63  ? 83  TRP   B CH2 1 
ATOM   1083 N N   . LYS   B 2 75  ? -27.555 -4.950  -9.858  1.00 45.53  ? 84  LYS   B N   1 
ATOM   1084 C CA  . LYS   B 2 75  ? -28.518 -5.711  -10.695 1.00 47.34  ? 84  LYS   B CA  1 
ATOM   1085 C C   . LYS   B 2 75  ? -27.836 -6.545  -11.796 1.00 47.65  ? 84  LYS   B C   1 
ATOM   1086 O O   . LYS   B 2 75  ? -28.516 -7.433  -12.305 1.00 49.08  ? 84  LYS   B O   1 
ATOM   1087 C CB  . LYS   B 2 75  ? -29.430 -4.747  -11.439 1.00 49.68  ? 84  LYS   B CB  1 
ATOM   1088 C CG  . LYS   B 2 75  ? -30.352 -3.936  -10.570 1.00 51.34  ? 84  LYS   B CG  1 
ATOM   1089 C CD  . LYS   B 2 75  ? -31.392 -4.763  -9.909  1.00 53.74  ? 84  LYS   B CD  1 
ATOM   1090 C CE  . LYS   B 2 75  ? -32.168 -3.909  -8.932  1.00 55.49  ? 84  LYS   B CE  1 
ATOM   1091 N NZ  . LYS   B 2 75  ? -32.957 -4.753  -8.021  1.00 59.07  ? 84  LYS   B NZ  1 
ATOM   1092 N N   . LEU   B 2 76  ? -26.583 -6.267  -12.167 1.00 47.44  ? 85  LEU   B N   1 
ATOM   1093 C CA  . LEU   B 2 76  ? -25.905 -6.826  -13.373 1.00 48.27  ? 85  LEU   B CA  1 
ATOM   1094 C C   . LEU   B 2 76  ? -25.190 -8.130  -12.994 1.00 50.90  ? 85  LEU   B C   1 
ATOM   1095 O O   . LEU   B 2 76  ? -24.150 -8.067  -12.272 1.00 48.96  ? 85  LEU   B O   1 
ATOM   1096 C CB  . LEU   B 2 76  ? -24.927 -5.780  -13.927 1.00 46.71  ? 85  LEU   B CB  1 
ATOM   1097 C CG  . LEU   B 2 76  ? -25.496 -4.359  -14.095 1.00 44.76  ? 85  LEU   B CG  1 
ATOM   1098 C CD1 . LEU   B 2 76  ? -24.467 -3.411  -14.686 1.00 44.75  ? 85  LEU   B CD1 1 
ATOM   1099 C CD2 . LEU   B 2 76  ? -26.759 -4.315  -14.933 1.00 44.85  ? 85  LEU   B CD2 1 
ATOM   1100 N N   . ASP   B 2 77  ? -25.752 -9.264  -13.427 1.00 53.39  ? 86  ASP   B N   1 
ATOM   1101 C CA  . ASP   B 2 77  ? -25.286 -10.618 -13.020 1.00 59.31  ? 86  ASP   B CA  1 
ATOM   1102 C C   . ASP   B 2 77  ? -24.630 -11.376 -14.192 1.00 57.11  ? 86  ASP   B C   1 
ATOM   1103 O O   . ASP   B 2 77  ? -24.106 -12.437 -13.937 1.00 58.32  ? 86  ASP   B O   1 
ATOM   1104 C CB  . ASP   B 2 77  ? -26.395 -11.438 -12.344 1.00 64.73  ? 86  ASP   B CB  1 
ATOM   1105 C CG  . ASP   B 2 77  ? -27.751 -11.350 -13.016 1.00 72.08  ? 86  ASP   B CG  1 
ATOM   1106 O OD1 . ASP   B 2 77  ? -27.920 -10.443 -13.868 1.00 78.35  ? 86  ASP   B OD1 1 
ATOM   1107 O OD2 . ASP   B 2 77  ? -28.639 -12.184 -12.682 1.00 79.64  ? 86  ASP   B OD2 1 
ATOM   1108 N N   . ALA   B 2 78  ? -24.575 -10.859 -15.419 1.00 56.05  ? 87  ALA   B N   1 
ATOM   1109 C CA  . ALA   B 2 78  ? -24.012 -11.615 -16.558 1.00 53.53  ? 87  ALA   B CA  1 
ATOM   1110 C C   . ALA   B 2 78  ? -22.485 -11.679 -16.410 1.00 52.85  ? 87  ALA   B C   1 
ATOM   1111 O O   . ALA   B 2 78  ? -21.864 -10.717 -15.858 1.00 50.42  ? 87  ALA   B O   1 
ATOM   1112 C CB  . ALA   B 2 78  ? -24.429 -10.995 -17.870 1.00 53.87  ? 87  ALA   B CB  1 
ATOM   1113 N N   . ALA   B 2 79  ? -21.895 -12.764 -16.921 1.00 53.00  ? 88  ALA   B N   1 
ATOM   1114 C CA  . ALA   B 2 79  ? -20.439 -13.022 -16.907 1.00 51.84  ? 88  ALA   B CA  1 
ATOM   1115 C C   . ALA   B 2 79  ? -19.900 -13.296 -18.320 1.00 50.69  ? 88  ALA   B C   1 
ATOM   1116 O O   . ALA   B 2 79  ? -20.599 -13.968 -19.084 1.00 47.67  ? 88  ALA   B O   1 
ATOM   1117 C CB  . ALA   B 2 79  ? -20.220 -14.211 -16.026 1.00 53.69  ? 88  ALA   B CB  1 
ATOM   1118 N N   . TRP   B 2 80  ? -18.661 -12.875 -18.608 1.00 51.45  ? 89  TRP   B N   1 
ATOM   1119 C CA  . TRP   B 2 80  ? -17.849 -13.380 -19.756 1.00 53.87  ? 89  TRP   B CA  1 
ATOM   1120 C C   . TRP   B 2 80  ? -17.861 -14.908 -19.716 1.00 54.13  ? 89  TRP   B C   1 
ATOM   1121 O O   . TRP   B 2 80  ? -17.823 -15.471 -18.625 1.00 51.81  ? 89  TRP   B O   1 
ATOM   1122 C CB  . TRP   B 2 80  ? -16.413 -12.832 -19.753 1.00 53.70  ? 89  TRP   B CB  1 
ATOM   1123 C CG  . TRP   B 2 80  ? -15.630 -13.183 -20.979 1.00 54.27  ? 89  TRP   B CG  1 
ATOM   1124 C CD1 . TRP   B 2 80  ? -16.099 -13.247 -22.263 1.00 54.80  ? 89  TRP   B CD1 1 
ATOM   1125 C CD2 . TRP   B 2 80  ? -14.220 -13.468 -21.060 1.00 54.69  ? 89  TRP   B CD2 1 
ATOM   1126 N NE1 . TRP   B 2 80  ? -15.088 -13.560 -23.130 1.00 53.68  ? 89  TRP   B NE1 1 
ATOM   1127 C CE2 . TRP   B 2 80  ? -13.926 -13.717 -22.421 1.00 54.07  ? 89  TRP   B CE2 1 
ATOM   1128 C CE3 . TRP   B 2 80  ? -13.188 -13.583 -20.123 1.00 54.62  ? 89  TRP   B CE3 1 
ATOM   1129 C CZ2 . TRP   B 2 80  ? -12.651 -14.063 -22.863 1.00 53.90  ? 89  TRP   B CZ2 1 
ATOM   1130 C CZ3 . TRP   B 2 80  ? -11.923 -13.921 -20.564 1.00 54.41  ? 89  TRP   B CZ3 1 
ATOM   1131 C CH2 . TRP   B 2 80  ? -11.659 -14.129 -21.924 1.00 53.94  ? 89  TRP   B CH2 1 
ATOM   1132 N N   . ASP   B 2 81  ? -18.000 -15.554 -20.870 1.00 56.59  ? 90  ASP   B N   1 
ATOM   1133 C CA  . ASP   B 2 81  ? -18.173 -17.026 -20.923 1.00 57.55  ? 90  ASP   B CA  1 
ATOM   1134 C C   . ASP   B 2 81  ? -16.777 -17.637 -20.990 1.00 58.81  ? 90  ASP   B C   1 
ATOM   1135 O O   . ASP   B 2 81  ? -16.697 -18.870 -20.839 1.00 62.80  ? 90  ASP   B O   1 
ATOM   1136 C CB  . ASP   B 2 81  ? -19.100 -17.430 -22.069 1.00 58.50  ? 90  ASP   B CB  1 
ATOM   1137 C CG  . ASP   B 2 81  ? -18.560 -17.155 -23.459 1.00 57.78  ? 90  ASP   B CG  1 
ATOM   1138 O OD1 . ASP   B 2 81  ? -17.541 -16.423 -23.589 1.00 57.96  ? 90  ASP   B OD1 1 
ATOM   1139 O OD2 . ASP   B 2 81  ? -19.165 -17.683 -24.416 1.00 58.47  ? 90  ASP   B OD2 1 
ATOM   1140 N N   . GLY   B 2 82  ? -15.760 -16.780 -21.188 1.00 58.12  ? 91  GLY   B N   1 
ATOM   1141 C CA  . GLY   B 2 82  ? -14.324 -17.112 -21.240 1.00 59.22  ? 91  GLY   B CA  1 
ATOM   1142 C C   . GLY   B 2 82  ? -13.831 -17.378 -22.654 1.00 61.58  ? 91  GLY   B C   1 
ATOM   1143 O O   . GLY   B 2 82  ? -12.616 -17.578 -22.826 1.00 61.51  ? 91  GLY   B O   1 
ATOM   1144 N N   . LEU   B 2 83  ? -14.740 -17.408 -23.631 1.00 63.93  ? 92  LEU   B N   1 
ATOM   1145 C CA  . LEU   B 2 83  ? -14.461 -17.807 -25.033 1.00 65.98  ? 92  LEU   B CA  1 
ATOM   1146 C C   . LEU   B 2 83  ? -14.768 -16.646 -25.985 1.00 67.29  ? 92  LEU   B C   1 
ATOM   1147 O O   . LEU   B 2 83  ? -13.901 -16.270 -26.799 1.00 68.06  ? 92  LEU   B O   1 
ATOM   1148 C CB  . LEU   B 2 83  ? -15.376 -18.978 -25.394 1.00 69.49  ? 92  LEU   B CB  1 
ATOM   1149 C CG  . LEU   B 2 83  ? -14.924 -20.386 -25.019 1.00 73.07  ? 92  LEU   B CG  1 
ATOM   1150 C CD1 . LEU   B 2 83  ? -15.769 -21.403 -25.789 1.00 75.30  ? 92  LEU   B CD1 1 
ATOM   1151 C CD2 . LEU   B 2 83  ? -13.442 -20.607 -25.310 1.00 73.03  ? 92  LEU   B CD2 1 
ATOM   1152 N N   . SER   B 2 84  ? -16.013 -16.172 -25.968 1.00 67.62  ? 93  SER   B N   1 
ATOM   1153 C CA  . SER   B 2 84  ? -16.605 -15.310 -27.030 1.00 64.03  ? 93  SER   B CA  1 
ATOM   1154 C C   . SER   B 2 84  ? -15.984 -13.909 -27.009 1.00 61.74  ? 93  SER   B C   1 
ATOM   1155 O O   . SER   B 2 84  ? -15.474 -13.460 -25.975 1.00 64.33  ? 93  SER   B O   1 
ATOM   1156 C CB  . SER   B 2 84  ? -18.089 -15.212 -26.866 1.00 64.31  ? 93  SER   B CB  1 
ATOM   1157 O OG  . SER   B 2 84  ? -18.564 -16.221 -25.988 1.00 64.75  ? 93  SER   B OG  1 
ATOM   1158 N N   . GLU   B 2 85  ? -16.048 -13.223 -28.131 1.00 60.17  ? 94  GLU   B N   1 
ATOM   1159 C CA  . GLU   B 2 85  ? -15.730 -11.778 -28.233 1.00 58.46  ? 94  GLU   B CA  1 
ATOM   1160 C C   . GLU   B 2 85  ? -16.891 -11.031 -27.542 1.00 52.80  ? 94  GLU   B C   1 
ATOM   1161 O O   . GLU   B 2 85  ? -18.045 -11.613 -27.403 1.00 52.20  ? 94  GLU   B O   1 
ATOM   1162 C CB  . GLU   B 2 85  ? -15.575 -11.343 -29.708 1.00 61.82  ? 94  GLU   B CB  1 
ATOM   1163 C CG  . GLU   B 2 85  ? -14.247 -11.772 -30.350 1.00 62.25  ? 94  GLU   B CG  1 
ATOM   1164 C CD  . GLU   B 2 85  ? -13.828 -11.164 -31.694 1.00 65.66  ? 94  GLU   B CD  1 
ATOM   1165 O OE1 . GLU   B 2 85  ? -14.545 -10.283 -32.236 1.00 63.53  ? 94  GLU   B OE1 1 
ATOM   1166 O OE2 . GLU   B 2 85  ? -12.758 -11.580 -32.206 1.00 65.85  ? 94  GLU   B OE2 1 
ATOM   1167 N N   . VAL   B 2 86  ? -16.577 -9.774  -27.210 1.00 50.20  ? 95  VAL   B N   1 
ATOM   1168 C CA  . VAL   B 2 86  ? -17.455 -8.843  -26.438 1.00 49.04  ? 95  VAL   B CA  1 
ATOM   1169 C C   . VAL   B 2 86  ? -17.392 -7.466  -27.081 1.00 48.03  ? 95  VAL   B C   1 
ATOM   1170 O O   . VAL   B 2 86  ? -16.467 -7.261  -27.882 1.00 50.98  ? 95  VAL   B O   1 
ATOM   1171 C CB  . VAL   B 2 86  ? -17.015 -8.755  -24.956 1.00 45.76  ? 95  VAL   B CB  1 
ATOM   1172 C CG1 . VAL   B 2 86  ? -16.905 -10.138 -24.370 1.00 46.67  ? 95  VAL   B CG1 1 
ATOM   1173 C CG2 . VAL   B 2 86  ? -15.706 -7.986  -24.792 1.00 45.33  ? 95  VAL   B CG2 1 
ATOM   1174 N N   . GLN   B 2 87  ? -18.269 -6.542  -26.658 1.00 49.08  ? 96  GLN   B N   1 
ATOM   1175 C CA  . GLN   B 2 87  ? -18.219 -5.114  -27.086 1.00 50.15  ? 96  GLN   B CA  1 
ATOM   1176 C C   . GLN   B 2 87  ? -18.111 -4.191  -25.860 1.00 47.33  ? 96  GLN   B C   1 
ATOM   1177 O O   . GLN   B 2 87  ? -18.975 -4.263  -25.006 1.00 49.94  ? 96  GLN   B O   1 
ATOM   1178 C CB  . GLN   B 2 87  ? -19.419 -4.752  -27.977 1.00 50.28  ? 96  GLN   B CB  1 
ATOM   1179 C CG  . GLN   B 2 87  ? -19.271 -5.290  -29.395 1.00 53.81  ? 96  GLN   B CG  1 
ATOM   1180 C CD  . GLN   B 2 87  ? -20.394 -4.938  -30.354 1.00 53.65  ? 96  GLN   B CD  1 
ATOM   1181 O OE1 . GLN   B 2 87  ? -21.213 -4.038  -30.129 1.00 51.57  ? 96  GLN   B OE1 1 
ATOM   1182 N NE2 . GLN   B 2 87  ? -20.430 -5.664  -31.462 1.00 53.92  ? 96  GLN   B NE2 1 
ATOM   1183 N N   . LEU   B 2 88  ? -17.068 -3.369  -25.820 1.00 45.78  ? 97  LEU   B N   1 
ATOM   1184 C CA  . LEU   B 2 88  ? -16.999 -2.121  -25.027 1.00 45.97  ? 97  LEU   B CA  1 
ATOM   1185 C C   . LEU   B 2 88  ? -17.914 -1.073  -25.669 1.00 45.66  ? 97  LEU   B C   1 
ATOM   1186 O O   . LEU   B 2 88  ? -17.556 -0.580  -26.776 1.00 45.70  ? 97  LEU   B O   1 
ATOM   1187 C CB  . LEU   B 2 88  ? -15.548 -1.612  -24.945 1.00 45.73  ? 97  LEU   B CB  1 
ATOM   1188 C CG  . LEU   B 2 88  ? -15.378 -0.297  -24.182 1.00 46.01  ? 97  LEU   B CG  1 
ATOM   1189 C CD1 . LEU   B 2 88  ? -15.807 -0.454  -22.734 1.00 45.45  ? 97  LEU   B CD1 1 
ATOM   1190 C CD2 . LEU   B 2 88  ? -13.947 0.206   -24.248 1.00 47.04  ? 97  LEU   B CD2 1 
ATOM   1191 N N   . LEU   B 2 89  ? -19.054 -0.778  -25.045 1.00 42.78  ? 98  LEU   B N   1 
ATOM   1192 C CA  . LEU   B 2 89  ? -19.845 0.412   -25.387 1.00 42.16  ? 98  LEU   B CA  1 
ATOM   1193 C C   . LEU   B 2 89  ? -19.125 1.592   -24.766 1.00 42.92  ? 98  LEU   B C   1 
ATOM   1194 O O   . LEU   B 2 89  ? -19.539 2.074   -23.645 1.00 46.49  ? 98  LEU   B O   1 
ATOM   1195 C CB  . LEU   B 2 89  ? -21.282 0.184   -24.950 1.00 41.63  ? 98  LEU   B CB  1 
ATOM   1196 C CG  . LEU   B 2 89  ? -22.277 1.348   -25.108 1.00 43.59  ? 98  LEU   B CG  1 
ATOM   1197 C CD1 . LEU   B 2 89  ? -21.842 2.391   -26.120 1.00 44.64  ? 98  LEU   B CD1 1 
ATOM   1198 C CD2 . LEU   B 2 89  ? -23.666 0.843   -25.480 1.00 44.17  ? 98  LEU   B CD2 1 
ATOM   1199 N N   . ALA   B 2 90  ? -18.055 2.041   -25.429 1.00 43.28  ? 99  ALA   B N   1 
ATOM   1200 C CA  . ALA   B 2 90  ? -17.257 3.192   -24.954 1.00 43.61  ? 99  ALA   B CA  1 
ATOM   1201 C C   . ALA   B 2 90  ? -18.086 4.466   -25.035 1.00 44.87  ? 99  ALA   B C   1 
ATOM   1202 O O   . ALA   B 2 90  ? -18.631 4.743   -26.131 1.00 45.46  ? 99  ALA   B O   1 
ATOM   1203 C CB  . ALA   B 2 90  ? -15.997 3.401   -25.738 1.00 43.84  ? 99  ALA   B CB  1 
ATOM   1204 N N   . VAL   B 2 91  ? -18.086 5.254   -23.953 1.00 44.25  ? 100 VAL   B N   1 
ATOM   1205 C CA  . VAL   B 2 91  ? -18.636 6.637   -23.946 1.00 42.67  ? 100 VAL   B CA  1 
ATOM   1206 C C   . VAL   B 2 91  ? -17.553 7.635   -23.538 1.00 42.40  ? 100 VAL   B C   1 
ATOM   1207 O O   . VAL   B 2 91  ? -17.483 8.089   -22.412 1.00 41.21  ? 100 VAL   B O   1 
ATOM   1208 C CB  . VAL   B 2 91  ? -19.892 6.671   -23.082 1.00 41.55  ? 100 VAL   B CB  1 
ATOM   1209 C CG1 . VAL   B 2 91  ? -20.557 8.035   -23.080 1.00 42.81  ? 100 VAL   B CG1 1 
ATOM   1210 C CG2 . VAL   B 2 91  ? -20.862 5.596   -23.543 1.00 42.23  ? 100 VAL   B CG2 1 
ATOM   1211 N N   . PRO   B 2 92  ? -16.667 8.053   -24.463 1.00 42.82  ? 101 PRO   B N   1 
ATOM   1212 C CA  . PRO   B 2 92  ? -15.564 8.948   -24.119 1.00 43.53  ? 101 PRO   B CA  1 
ATOM   1213 C C   . PRO   B 2 92  ? -15.995 10.397  -23.971 1.00 44.65  ? 101 PRO   B C   1 
ATOM   1214 O O   . PRO   B 2 92  ? -17.077 10.794  -24.399 1.00 45.88  ? 101 PRO   B O   1 
ATOM   1215 C CB  . PRO   B 2 92  ? -14.528 8.752   -25.243 1.00 44.30  ? 101 PRO   B CB  1 
ATOM   1216 C CG  . PRO   B 2 92  ? -15.236 7.992   -26.337 1.00 44.18  ? 101 PRO   B CG  1 
ATOM   1217 C CD  . PRO   B 2 92  ? -16.629 7.626   -25.864 1.00 44.10  ? 101 PRO   B CD  1 
ATOM   1218 N N   . PRO   B 2 93  ? -15.187 11.240  -23.303 1.00 46.78  ? 102 PRO   B N   1 
ATOM   1219 C CA  . PRO   B 2 93  ? -15.621 12.605  -23.024 1.00 48.22  ? 102 PRO   B CA  1 
ATOM   1220 C C   . PRO   B 2 93  ? -15.812 13.351  -24.349 1.00 49.46  ? 102 PRO   B C   1 
ATOM   1221 O O   . PRO   B 2 93  ? -15.010 13.132  -25.246 1.00 50.16  ? 102 PRO   B O   1 
ATOM   1222 C CB  . PRO   B 2 93  ? -14.521 13.163  -22.106 1.00 47.52  ? 102 PRO   B CB  1 
ATOM   1223 C CG  . PRO   B 2 93  ? -13.930 11.908  -21.474 1.00 47.48  ? 102 PRO   B CG  1 
ATOM   1224 C CD  . PRO   B 2 93  ? -13.927 10.905  -22.616 1.00 48.27  ? 102 PRO   B CD  1 
ATOM   1225 N N   . GLY   B 2 94  ? -16.911 14.112  -24.450 1.00 49.33  ? 103 GLY   B N   1 
ATOM   1226 C CA  . GLY   B 2 94  ? -17.273 14.941  -25.611 1.00 51.52  ? 103 GLY   B CA  1 
ATOM   1227 C C   . GLY   B 2 94  ? -17.585 14.175  -26.909 1.00 51.70  ? 103 GLY   B C   1 
ATOM   1228 O O   . GLY   B 2 94  ? -17.904 14.838  -27.888 1.00 53.96  ? 103 GLY   B O   1 
ATOM   1229 N N   . GLU   B 2 95  ? -17.552 12.843  -26.938 1.00 50.77  ? 104 GLU   B N   1 
ATOM   1230 C CA  . GLU   B 2 95  ? -17.658 12.037  -28.184 1.00 51.17  ? 104 GLU   B CA  1 
ATOM   1231 C C   . GLU   B 2 95  ? -18.845 11.088  -28.047 1.00 51.92  ? 104 GLU   B C   1 
ATOM   1232 O O   . GLU   B 2 95  ? -19.204 10.754  -26.896 1.00 51.35  ? 104 GLU   B O   1 
ATOM   1233 C CB  . GLU   B 2 95  ? -16.353 11.273  -28.408 1.00 51.34  ? 104 GLU   B CB  1 
ATOM   1234 C CG  . GLU   B 2 95  ? -15.133 12.187  -28.472 1.00 53.77  ? 104 GLU   B CG  1 
ATOM   1235 C CD  . GLU   B 2 95  ? -13.787 11.470  -28.627 1.00 58.17  ? 104 GLU   B CD  1 
ATOM   1236 O OE1 . GLU   B 2 95  ? -13.767 10.214  -28.524 1.00 59.01  ? 104 GLU   B OE1 1 
ATOM   1237 O OE2 . GLU   B 2 95  ? -12.752 12.164  -28.878 1.00 61.56  ? 104 GLU   B OE2 1 
ATOM   1238 N N   . ARG   B 2 96  ? -19.475 10.710  -29.146 1.00 52.05  ? 105 ARG   B N   1 
ATOM   1239 C CA  . ARG   B 2 96  ? -20.682 9.846   -29.141 1.00 55.63  ? 105 ARG   B CA  1 
ATOM   1240 C C   . ARG   B 2 96  ? -20.309 8.452   -28.632 1.00 53.90  ? 105 ARG   B C   1 
ATOM   1241 O O   . ARG   B 2 96  ? -19.162 8.007   -28.863 1.00 51.22  ? 105 ARG   B O   1 
ATOM   1242 C CB  . ARG   B 2 96  ? -21.291 9.759   -30.552 1.00 62.11  ? 105 ARG   B CB  1 
ATOM   1243 C CG  . ARG   B 2 96  ? -22.660 9.080   -30.596 1.00 67.61  ? 105 ARG   B CG  1 
ATOM   1244 C CD  . ARG   B 2 96  ? -23.523 9.377   -31.821 1.00 72.41  ? 105 ARG   B CD  1 
ATOM   1245 N NE  . ARG   B 2 96  ? -22.761 9.205   -33.047 1.00 76.51  ? 105 ARG   B NE  1 
ATOM   1246 C CZ  . ARG   B 2 96  ? -22.146 10.175  -33.722 1.00 80.96  ? 105 ARG   B CZ  1 
ATOM   1247 N NH1 . ARG   B 2 96  ? -22.220 11.448  -33.347 1.00 80.14  ? 105 ARG   B NH1 1 
ATOM   1248 N NH2 . ARG   B 2 96  ? -21.466 9.852   -34.808 1.00 85.95  ? 105 ARG   B NH2 1 
ATOM   1249 N N   . ALA   B 2 97  ? -21.266 7.803   -27.963 1.00 53.03  ? 106 ALA   B N   1 
ATOM   1250 C CA  . ALA   B 2 97  ? -21.248 6.363   -27.646 1.00 53.61  ? 106 ALA   B CA  1 
ATOM   1251 C C   . ALA   B 2 97  ? -20.781 5.589   -28.879 1.00 54.25  ? 106 ALA   B C   1 
ATOM   1252 O O   . ALA   B 2 97  ? -21.416 5.722   -29.922 1.00 55.00  ? 106 ALA   B O   1 
ATOM   1253 C CB  . ALA   B 2 97  ? -22.622 5.927   -27.206 1.00 52.61  ? 106 ALA   B CB  1 
ATOM   1254 N N   . LYS   B 2 98  ? -19.735 4.771   -28.748 1.00 56.51  ? 107 LYS   B N   1 
ATOM   1255 C CA  . LYS   B 2 98  ? -19.190 3.950   -29.858 1.00 57.80  ? 107 LYS   B CA  1 
ATOM   1256 C C   . LYS   B 2 98  ? -18.858 2.545   -29.350 1.00 57.25  ? 107 LYS   B C   1 
ATOM   1257 O O   . LYS   B 2 98  ? -18.030 2.478   -28.410 1.00 56.03  ? 107 LYS   B O   1 
ATOM   1258 C CB  . LYS   B 2 98  ? -17.934 4.650   -30.377 1.00 64.31  ? 107 LYS   B CB  1 
ATOM   1259 C CG  . LYS   B 2 98  ? -17.257 4.023   -31.597 1.00 69.33  ? 107 LYS   B CG  1 
ATOM   1260 C CD  . LYS   B 2 98  ? -15.831 4.539   -31.832 1.00 74.68  ? 107 LYS   B CD  1 
ATOM   1261 C CE  . LYS   B 2 98  ? -15.084 4.888   -30.548 1.00 77.12  ? 107 LYS   B CE  1 
ATOM   1262 N NZ  . LYS   B 2 98  ? -13.636 5.109   -30.787 1.00 80.58  ? 107 LYS   B NZ  1 
ATOM   1263 N N   . ASN   B 2 99  ? -19.491 1.502   -29.922 1.00 52.74  ? 108 ASN   B N   1 
ATOM   1264 C CA  . ASN   B 2 99  ? -19.181 0.069   -29.667 1.00 51.30  ? 108 ASN   B CA  1 
ATOM   1265 C C   . ASN   B 2 99  ? -17.831 -0.280  -30.297 1.00 52.66  ? 108 ASN   B C   1 
ATOM   1266 O O   . ASN   B 2 99  ? -17.595 0.104   -31.441 1.00 54.75  ? 108 ASN   B O   1 
ATOM   1267 C CB  . ASN   B 2 99  ? -20.180 -0.947  -30.240 1.00 50.50  ? 108 ASN   B CB  1 
ATOM   1268 C CG  . ASN   B 2 99  ? -21.581 -0.816  -29.695 1.00 51.82  ? 108 ASN   B CG  1 
ATOM   1269 O OD1 . ASN   B 2 99  ? -22.193 0.243   -29.825 1.00 54.50  ? 108 ASN   B OD1 1 
ATOM   1270 N ND2 . ASN   B 2 99  ? -22.126 -1.864  -29.096 1.00 52.07  ? 108 ASN   B ND2 1 
ATOM   1271 N N   . ILE   B 2 100 ? -17.037 -1.104  -29.629 1.00 49.41  ? 109 ILE   B N   1 
ATOM   1272 C CA  . ILE   B 2 100 ? -15.684 -1.533  -30.063 1.00 49.79  ? 109 ILE   B CA  1 
ATOM   1273 C C   . ILE   B 2 100 ? -15.577 -2.993  -29.682 1.00 48.95  ? 109 ILE   B C   1 
ATOM   1274 O O   . ILE   B 2 100 ? -15.693 -3.297  -28.460 1.00 51.86  ? 109 ILE   B O   1 
ATOM   1275 C CB  . ILE   B 2 100 ? -14.613 -0.707  -29.342 1.00 51.03  ? 109 ILE   B CB  1 
ATOM   1276 C CG1 . ILE   B 2 100 ? -14.860 0.801   -29.444 1.00 51.53  ? 109 ILE   B CG1 1 
ATOM   1277 C CG2 . ILE   B 2 100 ? -13.230 -1.131  -29.794 1.00 51.13  ? 109 ILE   B CG2 1 
ATOM   1278 C CD1 . ILE   B 2 100 ? -14.495 1.405   -30.789 1.00 52.69  ? 109 ILE   B CD1 1 
ATOM   1279 N N   . GLN   B 2 101 ? -15.436 -3.872  -30.646 1.00 49.79  ? 110 GLN   B N   1 
ATOM   1280 C CA  . GLN   B 2 101 ? -15.535 -5.327  -30.433 1.00 51.72  ? 110 GLN   B CA  1 
ATOM   1281 C C   . GLN   B 2 101 ? -14.116 -5.830  -30.238 1.00 53.94  ? 110 GLN   B C   1 
ATOM   1282 O O   . GLN   B 2 101 ? -13.232 -5.218  -30.872 1.00 52.91  ? 110 GLN   B O   1 
ATOM   1283 C CB  . GLN   B 2 101 ? -16.234 -6.014  -31.587 1.00 54.43  ? 110 GLN   B CB  1 
ATOM   1284 C CG  . GLN   B 2 101 ? -16.217 -7.525  -31.481 1.00 54.27  ? 110 GLN   B CG  1 
ATOM   1285 C CD  . GLN   B 2 101 ? -17.327 -8.100  -32.327 1.00 55.53  ? 110 GLN   B CD  1 
ATOM   1286 O OE1 . GLN   B 2 101 ? -18.345 -7.449  -32.584 1.00 54.18  ? 110 GLN   B OE1 1 
ATOM   1287 N NE2 . GLN   B 2 101 ? -17.135 -9.329  -32.770 1.00 55.68  ? 110 GLN   B NE2 1 
ATOM   1288 N N   . THR   B 2 102 ? -13.923 -6.767  -29.277 1.00 54.01  ? 111 THR   B N   1 
ATOM   1289 C CA  . THR   B 2 102 ? -12.593 -7.263  -28.822 1.00 53.59  ? 111 THR   B CA  1 
ATOM   1290 C C   . THR   B 2 102 ? -12.749 -8.654  -28.180 1.00 52.85  ? 111 THR   B C   1 
ATOM   1291 O O   . THR   B 2 102 ? -13.901 -9.021  -27.804 1.00 54.35  ? 111 THR   B O   1 
ATOM   1292 C CB  . THR   B 2 102 ? -11.908 -6.183  -27.969 1.00 53.88  ? 111 THR   B CB  1 
ATOM   1293 O OG1 . THR   B 2 102 ? -10.509 -6.478  -27.933 1.00 53.43  ? 111 THR   B OG1 1 
ATOM   1294 C CG2 . THR   B 2 102 ? -12.455 -6.046  -26.566 1.00 54.36  ? 111 THR   B CG2 1 
ATOM   1295 N N   . LEU   B 2 103 ? -11.671 -9.455  -28.222 1.00 51.31  ? 112 LEU   B N   1 
ATOM   1296 C CA  . LEU   B 2 103 ? -11.516 -10.719 -27.454 1.00 51.38  ? 112 LEU   B CA  1 
ATOM   1297 C C   . LEU   B 2 103 ? -10.722 -10.394 -26.184 1.00 51.85  ? 112 LEU   B C   1 
ATOM   1298 O O   . LEU   B 2 103 ? -9.540  -9.994  -26.210 1.00 51.69  ? 112 LEU   B O   1 
ATOM   1299 C CB  . LEU   B 2 103 ? -10.819 -11.835 -28.238 1.00 51.59  ? 112 LEU   B CB  1 
ATOM   1300 C CG  . LEU   B 2 103 ? -10.736 -13.160 -27.475 1.00 51.21  ? 112 LEU   B CG  1 
ATOM   1301 C CD1 . LEU   B 2 103 ? -12.036 -13.938 -27.589 1.00 50.45  ? 112 LEU   B CD1 1 
ATOM   1302 C CD2 . LEU   B 2 103 ? -9.573  -13.986 -27.969 1.00 53.37  ? 112 LEU   B CD2 1 
ATOM   1303 N N   . PRO   B 2 104 ? -11.378 -10.512 -25.011 1.00 50.69  ? 113 PRO   B N   1 
ATOM   1304 C CA  . PRO   B 2 104 ? -10.716 -10.168 -23.767 1.00 49.81  ? 113 PRO   B CA  1 
ATOM   1305 C C   . PRO   B 2 104 ? -9.494  -11.079 -23.534 1.00 50.98  ? 113 PRO   B C   1 
ATOM   1306 O O   . PRO   B 2 104 ? -9.545  -12.288 -23.804 1.00 52.32  ? 113 PRO   B O   1 
ATOM   1307 C CB  . PRO   B 2 104 ? -11.775 -10.397 -22.681 1.00 49.10  ? 113 PRO   B CB  1 
ATOM   1308 C CG  . PRO   B 2 104 ? -13.087 -10.543 -23.404 1.00 49.57  ? 113 PRO   B CG  1 
ATOM   1309 C CD  . PRO   B 2 104 ? -12.772 -10.943 -24.836 1.00 50.96  ? 113 PRO   B CD  1 
ATOM   1310 N N   . GLY   B 2 105 ? -8.419  -10.467 -23.040 1.00 51.14  ? 114 GLY   B N   1 
ATOM   1311 C CA  . GLY   B 2 105 ? -7.356  -11.184 -22.332 1.00 52.63  ? 114 GLY   B CA  1 
ATOM   1312 C C   . GLY   B 2 105 ? -7.816  -11.575 -20.933 1.00 54.17  ? 114 GLY   B C   1 
ATOM   1313 O O   . GLY   B 2 105 ? -9.053  -11.602 -20.677 1.00 51.33  ? 114 GLY   B O   1 
ATOM   1314 N N   . ILE   B 2 106 ? -6.840  -11.872 -20.079 1.00 54.50  ? 115 ILE   B N   1 
ATOM   1315 C CA  . ILE   B 2 106 ? -6.987  -12.477 -18.723 1.00 55.68  ? 115 ILE   B CA  1 
ATOM   1316 C C   . ILE   B 2 106 ? -6.066  -11.737 -17.739 1.00 53.58  ? 115 ILE   B C   1 
ATOM   1317 O O   . ILE   B 2 106 ? -4.870  -11.673 -17.987 1.00 56.78  ? 115 ILE   B O   1 
ATOM   1318 C CB  . ILE   B 2 106 ? -6.597  -13.964 -18.806 1.00 58.18  ? 115 ILE   B CB  1 
ATOM   1319 C CG1 . ILE   B 2 106 ? -7.457  -14.751 -19.788 1.00 64.02  ? 115 ILE   B CG1 1 
ATOM   1320 C CG2 . ILE   B 2 106 ? -6.644  -14.610 -17.456 1.00 61.10  ? 115 ILE   B CG2 1 
ATOM   1321 C CD1 . ILE   B 2 106 ? -8.837  -15.031 -19.281 1.00 63.44  ? 115 ILE   B CD1 1 
ATOM   1322 N N   . PHE   B 2 107 ? -6.599  -11.228 -16.638 1.00 52.91  ? 116 PHE   B N   1 
ATOM   1323 C CA  . PHE   B 2 107 ? -5.852  -10.908 -15.396 1.00 52.41  ? 116 PHE   B CA  1 
ATOM   1324 C C   . PHE   B 2 107 ? -5.784  -12.185 -14.567 1.00 53.18  ? 116 PHE   B C   1 
ATOM   1325 O O   . PHE   B 2 107 ? -6.869  -12.672 -14.194 1.00 53.99  ? 116 PHE   B O   1 
ATOM   1326 C CB  . PHE   B 2 107 ? -6.585  -9.847  -14.591 1.00 51.14  ? 116 PHE   B CB  1 
ATOM   1327 C CG  . PHE   B 2 107 ? -6.373  -8.421  -15.006 1.00 50.94  ? 116 PHE   B CG  1 
ATOM   1328 C CD1 . PHE   B 2 107 ? -5.676  -8.092  -16.156 1.00 52.42  ? 116 PHE   B CD1 1 
ATOM   1329 C CD2 . PHE   B 2 107 ? -6.944  -7.400  -14.255 1.00 50.31  ? 116 PHE   B CD2 1 
ATOM   1330 C CE1 . PHE   B 2 107 ? -5.520  -6.769  -16.532 1.00 51.63  ? 116 PHE   B CE1 1 
ATOM   1331 C CE2 . PHE   B 2 107 ? -6.772  -6.073  -14.622 1.00 50.43  ? 116 PHE   B CE2 1 
ATOM   1332 C CZ  . PHE   B 2 107 ? -6.077  -5.762  -15.768 1.00 51.65  ? 116 PHE   B CZ  1 
ATOM   1333 N N   . LYS   B 2 108 ? -4.581  -12.715 -14.348 1.00 53.53  ? 117 LYS   B N   1 
ATOM   1334 C CA  . LYS   B 2 108 ? -4.284  -13.832 -13.408 1.00 56.53  ? 117 LYS   B CA  1 
ATOM   1335 C C   . LYS   B 2 108 ? -3.980  -13.229 -12.026 1.00 53.46  ? 117 LYS   B C   1 
ATOM   1336 O O   . LYS   B 2 108 ? -3.030  -12.437 -11.924 1.00 49.50  ? 117 LYS   B O   1 
ATOM   1337 C CB  . LYS   B 2 108 ? -3.102  -14.683 -13.897 1.00 61.39  ? 117 LYS   B CB  1 
ATOM   1338 C CG  . LYS   B 2 108 ? -3.462  -15.860 -14.798 1.00 69.14  ? 117 LYS   B CG  1 
ATOM   1339 C CD  . LYS   B 2 108 ? -2.334  -16.340 -15.729 1.00 73.70  ? 117 LYS   B CD  1 
ATOM   1340 C CE  . LYS   B 2 108 ? -2.730  -17.495 -16.653 1.00 80.53  ? 117 LYS   B CE  1 
ATOM   1341 N NZ  . LYS   B 2 108 ? -1.959  -17.585 -17.940 1.00 79.97  ? 117 LYS   B NZ  1 
ATOM   1342 N N   . THR   B 2 109 ? -4.793  -13.559 -11.023 1.00 54.59  ? 118 THR   B N   1 
ATOM   1343 C CA  . THR   B 2 109 ? -4.613  -13.132 -9.598  1.00 55.52  ? 118 THR   B CA  1 
ATOM   1344 C C   . THR   B 2 109 ? -4.612  -14.361 -8.680  1.00 58.45  ? 118 THR   B C   1 
ATOM   1345 O O   . THR   B 2 109 ? -5.225  -15.396 -9.037  1.00 55.34  ? 118 THR   B O   1 
ATOM   1346 C CB  . THR   B 2 109 ? -5.691  -12.142 -9.133  1.00 55.40  ? 118 THR   B CB  1 
ATOM   1347 O OG1 . THR   B 2 109 ? -6.906  -12.830 -8.821  1.00 54.06  ? 118 THR   B OG1 1 
ATOM   1348 C CG2 . THR   B 2 109 ? -5.969  -11.056 -10.153 1.00 56.16  ? 118 THR   B CG2 1 
ATOM   1349 N N   . LYS   B 2 110 ? -3.996  -14.223 -7.501  1.00 63.24  ? 119 LYS   B N   1 
ATOM   1350 C CA  . LYS   B 2 110 ? -3.997  -15.236 -6.408  1.00 65.03  ? 119 LYS   B CA  1 
ATOM   1351 C C   . LYS   B 2 110 ? -5.437  -15.693 -6.141  1.00 66.81  ? 119 LYS   B C   1 
ATOM   1352 O O   . LYS   B 2 110 ? -5.605  -16.897 -5.860  1.00 70.43  ? 119 LYS   B O   1 
ATOM   1353 C CB  . LYS   B 2 110 ? -3.330  -14.680 -5.143  1.00 66.33  ? 119 LYS   B CB  1 
ATOM   1354 C CG  . LYS   B 2 110 ? -4.017  -13.479 -4.512  1.00 69.15  ? 119 LYS   B CG  1 
ATOM   1355 C CD  . LYS   B 2 110 ? -3.244  -12.867 -3.343  1.00 73.29  ? 119 LYS   B CD  1 
ATOM   1356 C CE  . LYS   B 2 110 ? -3.958  -12.985 -2.013  1.00 75.82  ? 119 LYS   B CE  1 
ATOM   1357 N NZ  . LYS   B 2 110 ? -5.177  -12.140 -1.954  1.00 76.00  ? 119 LYS   B NZ  1 
ATOM   1358 N N   . ASP   B 2 111 ? -6.434  -14.800 -6.255  1.00 66.43  ? 120 ASP   B N   1 
ATOM   1359 C CA  . ASP   B 2 111 ? -7.855  -15.100 -5.916  1.00 68.44  ? 120 ASP   B CA  1 
ATOM   1360 C C   . ASP   B 2 111 ? -8.607  -15.648 -7.126  1.00 71.63  ? 120 ASP   B C   1 
ATOM   1361 O O   . ASP   B 2 111 ? -9.687  -16.220 -6.907  1.00 77.15  ? 120 ASP   B O   1 
ATOM   1362 C CB  . ASP   B 2 111 ? -8.587  -13.887 -5.337  1.00 69.04  ? 120 ASP   B CB  1 
ATOM   1363 C CG  . ASP   B 2 111 ? -8.260  -13.696 -3.868  1.00 70.14  ? 120 ASP   B CG  1 
ATOM   1364 O OD1 . ASP   B 2 111 ? -7.412  -14.467 -3.384  1.00 69.38  ? 120 ASP   B OD1 1 
ATOM   1365 O OD2 . ASP   B 2 111 ? -8.862  -12.799 -3.222  1.00 73.79  ? 120 ASP   B OD2 1 
ATOM   1366 N N   . GLY   B 2 112 ? -8.085  -15.460 -8.341  1.00 70.77  ? 121 GLY   B N   1 
ATOM   1367 C CA  . GLY   B 2 112 ? -8.672  -16.047 -9.557  1.00 69.70  ? 121 GLY   B CA  1 
ATOM   1368 C C   . GLY   B 2 112 ? -8.325  -15.267 -10.809 1.00 65.67  ? 121 GLY   B C   1 
ATOM   1369 O O   . GLY   B 2 112 ? -7.640  -14.254 -10.695 1.00 64.72  ? 121 GLY   B O   1 
ATOM   1370 N N   . ASP   B 2 113 ? -8.784  -15.757 -11.958 1.00 66.15  ? 122 ASP   B N   1 
ATOM   1371 C CA  . ASP   B 2 113 ? -8.606  -15.120 -13.292 1.00 64.73  ? 122 ASP   B CA  1 
ATOM   1372 C C   . ASP   B 2 113 ? -9.836  -14.263 -13.600 1.00 61.02  ? 122 ASP   B C   1 
ATOM   1373 O O   . ASP   B 2 113 ? -10.960 -14.667 -13.248 1.00 56.31  ? 122 ASP   B O   1 
ATOM   1374 C CB  . ASP   B 2 113 ? -8.288  -16.170 -14.356 1.00 66.98  ? 122 ASP   B CB  1 
ATOM   1375 C CG  . ASP   B 2 113 ? -6.903  -16.781 -14.175 1.00 71.26  ? 122 ASP   B CG  1 
ATOM   1376 O OD1 . ASP   B 2 113 ? -6.240  -16.460 -13.167 1.00 76.86  ? 122 ASP   B OD1 1 
ATOM   1377 O OD2 . ASP   B 2 113 ? -6.487  -17.556 -15.044 1.00 74.64  ? 122 ASP   B OD2 1 
ATOM   1378 N N   . ILE   B 2 114 ? -9.607  -13.085 -14.178 1.00 58.13  ? 123 ILE   B N   1 
ATOM   1379 C CA  . ILE   B 2 114 ? -10.671 -12.115 -14.552 1.00 56.48  ? 123 ILE   B CA  1 
ATOM   1380 C C   . ILE   B 2 114 ? -10.443 -11.804 -16.028 1.00 54.97  ? 123 ILE   B C   1 
ATOM   1381 O O   . ILE   B 2 114 ? -9.293  -11.613 -16.385 1.00 53.81  ? 123 ILE   B O   1 
ATOM   1382 C CB  . ILE   B 2 114 ? -10.588 -10.812 -13.732 1.00 55.21  ? 123 ILE   B CB  1 
ATOM   1383 C CG1 . ILE   B 2 114 ? -10.152 -11.042 -12.289 1.00 60.11  ? 123 ILE   B CG1 1 
ATOM   1384 C CG2 . ILE   B 2 114 ? -11.880 -10.031 -13.799 1.00 55.29  ? 123 ILE   B CG2 1 
ATOM   1385 C CD1 . ILE   B 2 114 ? -9.373  -9.869  -11.710 1.00 61.74  ? 123 ILE   B CD1 1 
ATOM   1386 N N   . GLY   B 2 115 ? -11.503 -11.661 -16.811 1.00 54.35  ? 124 GLY   B N   1 
ATOM   1387 C CA  . GLY   B 2 115 ? -11.408 -11.043 -18.149 1.00 52.82  ? 124 GLY   B CA  1 
ATOM   1388 C C   . GLY   B 2 115 ? -10.758 -9.673  -18.048 1.00 51.51  ? 124 GLY   B C   1 
ATOM   1389 O O   . GLY   B 2 115 ? -10.833 -9.001  -16.966 1.00 48.33  ? 124 GLY   B O   1 
ATOM   1390 N N   . ALA   B 2 116 ? -10.075 -9.301  -19.110 1.00 50.63  ? 125 ALA   B N   1 
ATOM   1391 C CA  . ALA   B 2 116 ? -9.456  -7.977  -19.285 1.00 52.08  ? 125 ALA   B CA  1 
ATOM   1392 C C   . ALA   B 2 116 ? -9.632  -7.573  -20.753 1.00 51.58  ? 125 ALA   B C   1 
ATOM   1393 O O   . ALA   B 2 116 ? -9.579  -8.436  -21.619 1.00 52.18  ? 125 ALA   B O   1 
ATOM   1394 C CB  . ALA   B 2 116 ? -8.009  -8.021  -18.889 1.00 52.82  ? 125 ALA   B CB  1 
ATOM   1395 N N   A VAL   B 2 117 ? -9.869  -6.281  -21.004 0.25 51.47  ? 126 VAL   B N   1 
ATOM   1396 N N   B VAL   B 2 117 ? -9.824  -6.271  -20.986 0.25 51.45  ? 126 VAL   B N   1 
ATOM   1397 N N   C VAL   B 2 117 ? -9.869  -6.281  -21.004 0.25 51.47  ? 126 VAL   B N   1 
ATOM   1398 N N   D VAL   B 2 117 ? -9.824  -6.271  -20.986 0.25 51.45  ? 126 VAL   B N   1 
ATOM   1399 C CA  A VAL   B 2 117 ? -10.022 -5.698  -22.370 0.25 52.67  ? 126 VAL   B CA  1 
ATOM   1400 C CA  B VAL   B 2 117 ? -10.034 -5.641  -22.322 0.25 52.57  ? 126 VAL   B CA  1 
ATOM   1401 C CA  C VAL   B 2 117 ? -10.022 -5.698  -22.370 0.25 52.67  ? 126 VAL   B CA  1 
ATOM   1402 C CA  D VAL   B 2 117 ? -10.034 -5.641  -22.322 0.25 52.57  ? 126 VAL   B CA  1 
ATOM   1403 C C   A VAL   B 2 117 ? -8.895  -4.683  -22.601 0.25 52.83  ? 126 VAL   B C   1 
ATOM   1404 C C   B VAL   B 2 117 ? -8.880  -4.665  -22.589 0.25 52.77  ? 126 VAL   B C   1 
ATOM   1405 C C   C VAL   B 2 117 ? -8.895  -4.683  -22.601 0.25 52.83  ? 126 VAL   B C   1 
ATOM   1406 C C   D VAL   B 2 117 ? -8.880  -4.665  -22.589 0.25 52.77  ? 126 VAL   B C   1 
ATOM   1407 O O   A VAL   B 2 117 ? -8.741  -3.774  -21.772 0.25 52.32  ? 126 VAL   B O   1 
ATOM   1408 O O   B VAL   B 2 117 ? -8.685  -3.757  -21.767 0.25 52.25  ? 126 VAL   B O   1 
ATOM   1409 O O   C VAL   B 2 117 ? -8.741  -3.774  -21.772 0.25 52.32  ? 126 VAL   B O   1 
ATOM   1410 O O   D VAL   B 2 117 ? -8.685  -3.757  -21.767 0.25 52.25  ? 126 VAL   B O   1 
ATOM   1411 C CB  A VAL   B 2 117 ? -11.414 -5.065  -22.553 0.25 52.54  ? 126 VAL   B CB  1 
ATOM   1412 C CB  B VAL   B 2 117 ? -11.403 -4.938  -22.363 0.25 52.35  ? 126 VAL   B CB  1 
ATOM   1413 C CB  C VAL   B 2 117 ? -11.414 -5.065  -22.553 0.25 52.54  ? 126 VAL   B CB  1 
ATOM   1414 C CB  D VAL   B 2 117 ? -11.403 -4.938  -22.363 0.25 52.35  ? 126 VAL   B CB  1 
ATOM   1415 C CG1 A VAL   B 2 117 ? -12.520 -6.038  -22.173 0.25 52.61  ? 126 VAL   B CG1 1 
ATOM   1416 C CG1 B VAL   B 2 117 ? -11.399 -3.743  -23.299 0.25 52.56  ? 126 VAL   B CG1 1 
ATOM   1417 C CG1 C VAL   B 2 117 ? -12.520 -6.038  -22.173 0.25 52.61  ? 126 VAL   B CG1 1 
ATOM   1418 C CG1 D VAL   B 2 117 ? -11.399 -3.743  -23.299 0.25 52.56  ? 126 VAL   B CG1 1 
ATOM   1419 C CG2 A VAL   B 2 117 ? -11.550 -3.767  -21.778 0.25 52.02  ? 126 VAL   B CG2 1 
ATOM   1420 C CG2 B VAL   B 2 117 ? -12.520 -5.908  -22.721 0.25 52.84  ? 126 VAL   B CG2 1 
ATOM   1421 C CG2 C VAL   B 2 117 ? -11.550 -3.767  -21.778 0.25 52.02  ? 126 VAL   B CG2 1 
ATOM   1422 C CG2 D VAL   B 2 117 ? -12.520 -5.908  -22.721 0.25 52.84  ? 126 VAL   B CG2 1 
ATOM   1423 N N   . ALA   B 2 118 ? -8.123  -4.851  -23.679 1.00 53.64  ? 127 ALA   B N   1 
ATOM   1424 C CA  . ALA   B 2 118 ? -6.980  -3.953  -24.001 1.00 55.40  ? 127 ALA   B CA  1 
ATOM   1425 C C   . ALA   B 2 118 ? -7.457  -2.877  -24.977 1.00 58.65  ? 127 ALA   B C   1 
ATOM   1426 O O   . ALA   B 2 118 ? -7.290  -3.101  -26.179 1.00 58.72  ? 127 ALA   B O   1 
ATOM   1427 C CB  . ALA   B 2 118 ? -5.809  -4.734  -24.546 1.00 56.71  ? 127 ALA   B CB  1 
ATOM   1428 N N   . LEU   B 2 119 ? -8.122  -1.818  -24.492 1.00 56.89  ? 128 LEU   B N   1 
ATOM   1429 C CA  . LEU   B 2 119 ? -8.549  -0.670  -25.331 1.00 57.29  ? 128 LEU   B CA  1 
ATOM   1430 C C   . LEU   B 2 119 ? -8.131  0.609   -24.608 1.00 58.88  ? 128 LEU   B C   1 
ATOM   1431 O O   . LEU   B 2 119 ? -8.142  0.627   -23.393 1.00 61.33  ? 128 LEU   B O   1 
ATOM   1432 C CB  . LEU   B 2 119 ? -10.051 -0.764  -25.606 1.00 56.40  ? 128 LEU   B CB  1 
ATOM   1433 C CG  . LEU   B 2 119 ? -10.518 -2.041  -26.305 1.00 55.38  ? 128 LEU   B CG  1 
ATOM   1434 C CD1 . LEU   B 2 119 ? -12.029 -2.173  -26.260 1.00 53.78  ? 128 LEU   B CD1 1 
ATOM   1435 C CD2 . LEU   B 2 119 ? -10.046 -2.069  -27.754 1.00 58.03  ? 128 LEU   B CD2 1 
ATOM   1436 N N   . ASP   B 2 120 ? -7.674  1.608   -25.343 1.00 62.51  ? 129 ASP   B N   1 
ATOM   1437 C CA  . ASP   B 2 120 ? -6.935  2.753   -24.770 1.00 66.88  ? 129 ASP   B CA  1 
ATOM   1438 C C   . ASP   B 2 120 ? -7.861  3.972   -24.881 1.00 66.63  ? 129 ASP   B C   1 
ATOM   1439 O O   . ASP   B 2 120 ? -7.947  4.557   -25.975 1.00 73.90  ? 129 ASP   B O   1 
ATOM   1440 C CB  . ASP   B 2 120 ? -5.575  2.840   -25.477 1.00 73.51  ? 129 ASP   B CB  1 
ATOM   1441 C CG  . ASP   B 2 120 ? -4.500  3.675   -24.793 1.00 79.49  ? 129 ASP   B CG  1 
ATOM   1442 O OD1 . ASP   B 2 120 ? -4.599  3.893   -23.551 1.00 82.47  ? 129 ASP   B OD1 1 
ATOM   1443 O OD2 . ASP   B 2 120 ? -3.564  4.106   -25.508 1.00 83.53  ? 129 ASP   B OD2 1 
ATOM   1444 N N   . TYR   B 2 121 ? -8.563  4.337   -23.811 1.00 61.49  ? 130 TYR   B N   1 
ATOM   1445 C CA  . TYR   B 2 121 ? -9.476  5.511   -23.792 1.00 61.04  ? 130 TYR   B CA  1 
ATOM   1446 C C   . TYR   B 2 121 ? -9.144  6.388   -22.598 1.00 57.81  ? 130 TYR   B C   1 
ATOM   1447 O O   . TYR   B 2 121 ? -8.483  5.942   -21.679 1.00 61.06  ? 130 TYR   B O   1 
ATOM   1448 C CB  . TYR   B 2 121 ? -10.939 5.083   -23.747 1.00 61.08  ? 130 TYR   B CB  1 
ATOM   1449 C CG  . TYR   B 2 121 ? -11.472 4.503   -25.032 1.00 64.51  ? 130 TYR   B CG  1 
ATOM   1450 C CD1 . TYR   B 2 121 ? -11.906 5.318   -26.063 1.00 64.32  ? 130 TYR   B CD1 1 
ATOM   1451 C CD2 . TYR   B 2 121 ? -11.550 3.128   -25.222 1.00 68.93  ? 130 TYR   B CD2 1 
ATOM   1452 C CE1 . TYR   B 2 121 ? -12.392 4.782   -27.245 1.00 67.84  ? 130 TYR   B CE1 1 
ATOM   1453 C CE2 . TYR   B 2 121 ? -12.038 2.577   -26.402 1.00 68.72  ? 130 TYR   B CE2 1 
ATOM   1454 C CZ  . TYR   B 2 121 ? -12.467 3.410   -27.416 1.00 68.52  ? 130 TYR   B CZ  1 
ATOM   1455 O OH  . TYR   B 2 121 ? -12.948 2.891   -28.584 1.00 74.54  ? 130 TYR   B OH  1 
ATOM   1456 N N   . PRO   B 2 122 ? -9.577  7.665   -22.571 1.00 57.15  ? 131 PRO   B N   1 
ATOM   1457 C CA  . PRO   B 2 122 ? -9.291  8.539   -21.440 1.00 56.55  ? 131 PRO   B CA  1 
ATOM   1458 C C   . PRO   B 2 122 ? -9.978  8.045   -20.162 1.00 51.95  ? 131 PRO   B C   1 
ATOM   1459 O O   . PRO   B 2 122 ? -10.926 7.259   -20.225 1.00 48.36  ? 131 PRO   B O   1 
ATOM   1460 C CB  . PRO   B 2 122 ? -9.835  9.915   -21.848 1.00 58.11  ? 131 PRO   B CB  1 
ATOM   1461 C CG  . PRO   B 2 122 ? -10.124 9.819   -23.331 1.00 59.06  ? 131 PRO   B CG  1 
ATOM   1462 C CD  . PRO   B 2 122 ? -10.355 8.348   -23.613 1.00 59.67  ? 131 PRO   B CD  1 
ATOM   1463 N N   . ALA   B 2 123 ? -9.488  8.535   -19.037 1.00 52.44  ? 132 ALA   B N   1 
ATOM   1464 C CA  . ALA   B 2 123 ? -9.944  8.119   -17.689 1.00 52.32  ? 132 ALA   B CA  1 
ATOM   1465 C C   . ALA   B 2 123 ? -11.440 8.430   -17.509 1.00 51.01  ? 132 ALA   B C   1 
ATOM   1466 O O   . ALA   B 2 123 ? -12.148 7.583   -16.876 1.00 49.36  ? 132 ALA   B O   1 
ATOM   1467 C CB  . ALA   B 2 123 ? -9.070  8.771   -16.653 1.00 53.74  ? 132 ALA   B CB  1 
ATOM   1468 N N   . GLY   B 2 124 ? -11.932 9.528   -18.107 1.00 47.93  ? 133 GLY   B N   1 
ATOM   1469 C CA  . GLY   B 2 124 ? -13.361 9.896   -18.053 1.00 44.57  ? 133 GLY   B CA  1 
ATOM   1470 C C   . GLY   B 2 124 ? -14.278 8.856   -18.697 1.00 43.20  ? 133 GLY   B C   1 
ATOM   1471 O O   . GLY   B 2 124 ? -15.512 9.008   -18.522 1.00 42.00  ? 133 GLY   B O   1 
ATOM   1472 N N   . THR   B 2 125 ? -13.742 7.853   -19.420 1.00 41.97  ? 134 THR   B N   1 
ATOM   1473 C CA  . THR   B 2 125 ? -14.514 6.711   -20.004 1.00 43.26  ? 134 THR   B CA  1 
ATOM   1474 C C   . THR   B 2 125 ? -14.801 5.623   -18.956 1.00 43.94  ? 134 THR   B C   1 
ATOM   1475 O O   . THR   B 2 125 ? -15.605 4.689   -19.275 1.00 45.10  ? 134 THR   B O   1 
ATOM   1476 C CB  . THR   B 2 125 ? -13.801 6.081   -21.219 1.00 44.42  ? 134 THR   B CB  1 
ATOM   1477 O OG1 . THR   B 2 125 ? -13.334 7.126   -22.066 1.00 45.53  ? 134 THR   B OG1 1 
ATOM   1478 C CG2 . THR   B 2 125 ? -14.680 5.180   -22.063 1.00 43.84  ? 134 THR   B CG2 1 
ATOM   1479 N N   . SER   B 2 126 ? -14.196 5.732   -17.758 1.00 43.13  ? 135 SER   B N   1 
ATOM   1480 C CA  . SER   B 2 126 ? -14.359 4.804   -16.610 1.00 41.93  ? 135 SER   B CA  1 
ATOM   1481 C C   . SER   B 2 126 ? -15.858 4.548   -16.354 1.00 40.41  ? 135 SER   B C   1 
ATOM   1482 O O   . SER   B 2 126 ? -16.627 5.541   -16.224 1.00 39.36  ? 135 SER   B O   1 
ATOM   1483 C CB  . SER   B 2 126 ? -13.644 5.353   -15.406 1.00 41.81  ? 135 SER   B CB  1 
ATOM   1484 O OG  . SER   B 2 126 ? -12.236 5.138   -15.466 1.00 41.70  ? 135 SER   B OG  1 
ATOM   1485 N N   . GLY   B 2 127 ? -16.287 3.278   -16.375 1.00 39.40  ? 136 GLY   B N   1 
ATOM   1486 C CA  . GLY   B 2 127 ? -17.695 2.916   -16.122 1.00 40.03  ? 136 GLY   B CA  1 
ATOM   1487 C C   . GLY   B 2 127 ? -18.459 2.531   -17.357 1.00 40.64  ? 136 GLY   B C   1 
ATOM   1488 O O   . GLY   B 2 127 ? -19.583 2.014   -17.181 1.00 42.85  ? 136 GLY   B O   1 
ATOM   1489 N N   . SER   B 2 128 ? -17.884 2.738   -18.560 1.00 40.84  ? 137 SER   B N   1 
ATOM   1490 C CA  . SER   B 2 128 ? -18.466 2.271   -19.824 1.00 39.41  ? 137 SER   B CA  1 
ATOM   1491 C C   . SER   B 2 128 ? -18.708 0.778   -19.704 1.00 38.57  ? 137 SER   B C   1 
ATOM   1492 O O   . SER   B 2 128 ? -17.800 0.030   -19.390 1.00 40.19  ? 137 SER   B O   1 
ATOM   1493 C CB  . SER   B 2 128 ? -17.565 2.615   -20.994 1.00 40.59  ? 137 SER   B CB  1 
ATOM   1494 O OG  . SER   B 2 128 ? -17.540 4.023   -21.186 1.00 40.20  ? 137 SER   B OG  1 
ATOM   1495 N N   . PRO   B 2 129 ? -19.909 0.284   -20.042 1.00 37.74  ? 138 PRO   B N   1 
ATOM   1496 C CA  . PRO   B 2 129 ? -20.177 -1.148  -20.011 1.00 38.35  ? 138 PRO   B CA  1 
ATOM   1497 C C   . PRO   B 2 129 ? -19.603 -2.035  -21.109 1.00 40.41  ? 138 PRO   B C   1 
ATOM   1498 O O   . PRO   B 2 129 ? -19.486 -1.638  -22.322 1.00 42.00  ? 138 PRO   B O   1 
ATOM   1499 C CB  . PRO   B 2 129 ? -21.703 -1.228  -20.178 1.00 38.26  ? 138 PRO   B CB  1 
ATOM   1500 C CG  . PRO   B 2 129 ? -22.061 0.023   -20.959 1.00 37.57  ? 138 PRO   B CG  1 
ATOM   1501 C CD  . PRO   B 2 129 ? -21.083 1.065   -20.463 1.00 37.18  ? 138 PRO   B CD  1 
ATOM   1502 N N   . ILE   B 2 130 ? -19.447 -3.292  -20.734 1.00 39.97  ? 139 ILE   B N   1 
ATOM   1503 C CA  . ILE   B 2 130 ? -18.945 -4.359  -21.613 1.00 42.21  ? 139 ILE   B CA  1 
ATOM   1504 C C   . ILE   B 2 130 ? -20.096 -5.329  -21.797 1.00 43.54  ? 139 ILE   B C   1 
ATOM   1505 O O   . ILE   B 2 130 ? -20.697 -5.636  -20.793 1.00 41.73  ? 139 ILE   B O   1 
ATOM   1506 C CB  . ILE   B 2 130 ? -17.719 -5.008  -20.992 1.00 42.46  ? 139 ILE   B CB  1 
ATOM   1507 C CG1 . ILE   B 2 130 ? -16.543 -4.028  -20.896 1.00 42.75  ? 139 ILE   B CG1 1 
ATOM   1508 C CG2 . ILE   B 2 130 ? -17.376 -6.267  -21.771 1.00 43.53  ? 139 ILE   B CG2 1 
ATOM   1509 C CD1 . ILE   B 2 130 ? -15.579 -4.414  -19.820 1.00 43.85  ? 139 ILE   B CD1 1 
ATOM   1510 N N   . LEU   B 2 131 ? -20.409 -5.710  -23.049 1.00 45.22  ? 140 LEU   B N   1 
ATOM   1511 C CA  . LEU   B 2 131 ? -21.611 -6.505  -23.405 1.00 48.11  ? 140 LEU   B CA  1 
ATOM   1512 C C   . LEU   B 2 131 ? -21.226 -7.867  -23.971 1.00 49.99  ? 140 LEU   B C   1 
ATOM   1513 O O   . LEU   B 2 131 ? -20.214 -7.949  -24.677 1.00 50.19  ? 140 LEU   B O   1 
ATOM   1514 C CB  . LEU   B 2 131 ? -22.398 -5.779  -24.497 1.00 50.89  ? 140 LEU   B CB  1 
ATOM   1515 C CG  . LEU   B 2 131 ? -22.452 -4.270  -24.371 1.00 52.29  ? 140 LEU   B CG  1 
ATOM   1516 C CD1 . LEU   B 2 131 ? -23.314 -3.678  -25.481 1.00 52.79  ? 140 LEU   B CD1 1 
ATOM   1517 C CD2 . LEU   B 2 131 ? -22.976 -3.899  -22.989 1.00 51.20  ? 140 LEU   B CD2 1 
ATOM   1518 N N   . ASP   B 2 132 ? -22.098 -8.854  -23.756 1.00 51.41  ? 141 ASP   B N   1 
ATOM   1519 C CA  . ASP   B 2 132 ? -22.094 -10.133 -24.498 1.00 53.95  ? 141 ASP   B CA  1 
ATOM   1520 C C   . ASP   B 2 132 ? -22.990 -10.000 -25.743 1.00 57.04  ? 141 ASP   B C   1 
ATOM   1521 O O   . ASP   B 2 132 ? -23.698 -8.959  -25.886 1.00 55.84  ? 141 ASP   B O   1 
ATOM   1522 C CB  . ASP   B 2 132 ? -22.516 -11.313 -23.619 1.00 53.22  ? 141 ASP   B CB  1 
ATOM   1523 C CG  . ASP   B 2 132 ? -23.956 -11.307 -23.151 1.00 53.72  ? 141 ASP   B CG  1 
ATOM   1524 O OD1 . ASP   B 2 132 ? -24.728 -10.464 -23.590 1.00 50.07  ? 141 ASP   B OD1 1 
ATOM   1525 O OD2 . ASP   B 2 132 ? -24.257 -12.115 -22.246 1.00 59.11  ? 141 ASP   B OD2 1 
ATOM   1526 N N   . LYS   B 2 133 ? -22.996 -11.062 -26.550 1.00 61.47  ? 142 LYS   B N   1 
ATOM   1527 C CA  . LYS   B 2 133 ? -23.629 -11.147 -27.894 1.00 66.13  ? 142 LYS   B CA  1 
ATOM   1528 C C   . LYS   B 2 133 ? -25.126 -10.873 -27.721 1.00 63.86  ? 142 LYS   B C   1 
ATOM   1529 O O   . LYS   B 2 133 ? -25.730 -10.364 -28.664 1.00 61.40  ? 142 LYS   B O   1 
ATOM   1530 C CB  . LYS   B 2 133 ? -23.285 -12.501 -28.552 1.00 69.96  ? 142 LYS   B CB  1 
ATOM   1531 C CG  . LYS   B 2 133 ? -21.917 -12.546 -29.247 1.00 74.62  ? 142 LYS   B CG  1 
ATOM   1532 C CD  . LYS   B 2 133 ? -21.135 -13.886 -29.218 1.00 77.74  ? 142 LYS   B CD  1 
ATOM   1533 C CE  . LYS   B 2 133 ? -19.718 -13.752 -29.770 1.00 78.94  ? 142 LYS   B CE  1 
ATOM   1534 N NZ  . LYS   B 2 133 ? -19.126 -15.027 -30.266 1.00 79.19  ? 142 LYS   B NZ  1 
ATOM   1535 N N   . CYS   B 2 134 ? -25.684 -11.150 -26.539 1.00 61.11  ? 143 CYS   B N   1 
ATOM   1536 C CA  . CYS   B 2 134 ? -27.133 -10.971 -26.282 1.00 61.00  ? 143 CYS   B CA  1 
ATOM   1537 C C   . CYS   B 2 134 ? -27.428 -9.570  -25.742 1.00 56.41  ? 143 CYS   B C   1 
ATOM   1538 O O   . CYS   B 2 134 ? -28.564 -9.348  -25.342 1.00 56.68  ? 143 CYS   B O   1 
ATOM   1539 C CB  . CYS   B 2 134 ? -27.649 -12.004 -25.301 1.00 64.66  ? 143 CYS   B CB  1 
ATOM   1540 S SG  . CYS   B 2 134 ? -27.744 -13.646 -26.040 1.00 67.31  ? 143 CYS   B SG  1 
ATOM   1541 N N   . GLY   B 2 135 ? -26.461 -8.650  -25.767 1.00 55.09  ? 144 GLY   B N   1 
ATOM   1542 C CA  . GLY   B 2 135 ? -26.638 -7.276  -25.245 1.00 54.73  ? 144 GLY   B CA  1 
ATOM   1543 C C   . GLY   B 2 135 ? -26.663 -7.174  -23.713 1.00 52.50  ? 144 GLY   B C   1 
ATOM   1544 O O   . GLY   B 2 135 ? -26.999 -6.084  -23.210 1.00 50.55  ? 144 GLY   B O   1 
ATOM   1545 N N   . ARG   B 2 136 ? -26.293 -8.219  -22.962 1.00 52.81  ? 145 ARG   B N   1 
ATOM   1546 C CA  . ARG   B 2 136 ? -26.293 -8.161  -21.461 1.00 53.24  ? 145 ARG   B CA  1 
ATOM   1547 C C   . ARG   B 2 136 ? -24.967 -7.604  -20.937 1.00 49.51  ? 145 ARG   B C   1 
ATOM   1548 O O   . ARG   B 2 136 ? -23.918 -8.003  -21.484 1.00 47.80  ? 145 ARG   B O   1 
ATOM   1549 C CB  . ARG   B 2 136 ? -26.603 -9.541  -20.896 1.00 55.56  ? 145 ARG   B CB  1 
ATOM   1550 C CG  . ARG   B 2 136 ? -28.082 -9.884  -21.006 1.00 58.16  ? 145 ARG   B CG  1 
ATOM   1551 C CD  . ARG   B 2 136 ? -28.317 -11.329 -20.668 1.00 61.66  ? 145 ARG   B CD  1 
ATOM   1552 N NE  . ARG   B 2 136 ? -27.289 -12.118 -21.327 1.00 67.12  ? 145 ARG   B NE  1 
ATOM   1553 C CZ  . ARG   B 2 136 ? -26.773 -13.264 -20.887 1.00 70.85  ? 145 ARG   B CZ  1 
ATOM   1554 N NH1 . ARG   B 2 136 ? -27.153 -13.802 -19.734 1.00 75.26  ? 145 ARG   B NH1 1 
ATOM   1555 N NH2 . ARG   B 2 136 ? -25.844 -13.861 -21.613 1.00 72.81  ? 145 ARG   B NH2 1 
ATOM   1556 N N   . VAL   B 2 137 ? -24.997 -6.729  -19.913 1.00 47.85  ? 146 VAL   B N   1 
ATOM   1557 C CA  . VAL   B 2 137 ? -23.743 -6.113  -19.377 1.00 46.22  ? 146 VAL   B CA  1 
ATOM   1558 C C   . VAL   B 2 137 ? -23.005 -7.172  -18.527 1.00 47.59  ? 146 VAL   B C   1 
ATOM   1559 O O   . VAL   B 2 137 ? -23.589 -7.703  -17.522 1.00 47.22  ? 146 VAL   B O   1 
ATOM   1560 C CB  . VAL   B 2 137 ? -23.988 -4.821  -18.589 1.00 45.78  ? 146 VAL   B CB  1 
ATOM   1561 C CG1 . VAL   B 2 137 ? -22.675 -4.183  -18.192 1.00 45.56  ? 146 VAL   B CG1 1 
ATOM   1562 C CG2 . VAL   B 2 137 ? -24.836 -3.822  -19.353 1.00 47.72  ? 146 VAL   B CG2 1 
ATOM   1563 N N   . ILE   B 2 138 ? -21.773 -7.498  -18.905 1.00 45.54  ? 147 ILE   B N   1 
ATOM   1564 C CA  . ILE   B 2 138 ? -20.955 -8.525  -18.201 1.00 45.18  ? 147 ILE   B CA  1 
ATOM   1565 C C   . ILE   B 2 138 ? -19.944 -7.823  -17.279 1.00 44.07  ? 147 ILE   B C   1 
ATOM   1566 O O   . ILE   B 2 138 ? -19.164 -8.544  -16.566 1.00 42.67  ? 147 ILE   B O   1 
ATOM   1567 C CB  . ILE   B 2 138 ? -20.270 -9.466  -19.218 1.00 45.16  ? 147 ILE   B CB  1 
ATOM   1568 C CG1 . ILE   B 2 138 ? -19.423 -8.702  -20.229 1.00 45.65  ? 147 ILE   B CG1 1 
ATOM   1569 C CG2 . ILE   B 2 138 ? -21.286 -10.356 -19.901 1.00 44.82  ? 147 ILE   B CG2 1 
ATOM   1570 C CD1 . ILE   B 2 138 ? -18.356 -9.551  -20.891 1.00 48.05  ? 147 ILE   B CD1 1 
ATOM   1571 N N   . GLY   B 2 139 ? -19.913 -6.484  -17.286 1.00 41.13  ? 148 GLY   B N   1 
ATOM   1572 C CA  . GLY   B 2 139 ? -19.015 -5.779  -16.351 1.00 40.08  ? 148 GLY   B CA  1 
ATOM   1573 C C   . GLY   B 2 139 ? -18.707 -4.398  -16.835 1.00 39.71  ? 148 GLY   B C   1 
ATOM   1574 O O   . GLY   B 2 139 ? -19.217 -4.031  -17.930 1.00 38.24  ? 148 GLY   B O   1 
ATOM   1575 N N   . LEU   B 2 140 ? -17.869 -3.676  -16.111 1.00 39.27  ? 149 LEU   B N   1 
ATOM   1576 C CA  . LEU   B 2 140 ? -17.549 -2.270  -16.421 1.00 39.88  ? 149 LEU   B CA  1 
ATOM   1577 C C   . LEU   B 2 140 ? -16.055 -2.127  -16.632 1.00 40.67  ? 149 LEU   B C   1 
ATOM   1578 O O   . LEU   B 2 140 ? -15.260 -2.880  -16.024 1.00 40.68  ? 149 LEU   B O   1 
ATOM   1579 C CB  . LEU   B 2 140 ? -17.996 -1.329  -15.310 1.00 39.89  ? 149 LEU   B CB  1 
ATOM   1580 C CG  . LEU   B 2 140 ? -19.472 -1.330  -14.923 1.00 40.06  ? 149 LEU   B CG  1 
ATOM   1581 C CD1 . LEU   B 2 140 ? -19.723 -0.218  -13.917 1.00 41.23  ? 149 LEU   B CD1 1 
ATOM   1582 C CD2 . LEU   B 2 140 ? -20.400 -1.190  -16.107 1.00 40.67  ? 149 LEU   B CD2 1 
ATOM   1583 N N   . TYR   B 2 141 ? -15.745 -1.183  -17.511 1.00 40.52  ? 150 TYR   B N   1 
ATOM   1584 C CA  . TYR   B 2 141 ? -14.406 -0.836  -18.011 1.00 41.67  ? 150 TYR   B CA  1 
ATOM   1585 C C   . TYR   B 2 141 ? -13.905 0.348   -17.219 1.00 41.13  ? 150 TYR   B C   1 
ATOM   1586 O O   . TYR   B 2 141 ? -14.699 1.274   -17.001 1.00 44.75  ? 150 TYR   B O   1 
ATOM   1587 C CB  . TYR   B 2 141 ? -14.485 -0.455  -19.512 1.00 43.65  ? 150 TYR   B CB  1 
ATOM   1588 C CG  . TYR   B 2 141 ? -13.256 0.239   -20.054 1.00 44.11  ? 150 TYR   B CG  1 
ATOM   1589 C CD1 . TYR   B 2 141 ? -13.079 1.609   -19.944 1.00 44.60  ? 150 TYR   B CD1 1 
ATOM   1590 C CD2 . TYR   B 2 141 ? -12.241 -0.488  -20.668 1.00 45.91  ? 150 TYR   B CD2 1 
ATOM   1591 C CE1 . TYR   B 2 141 ? -11.932 2.234   -20.424 1.00 47.48  ? 150 TYR   B CE1 1 
ATOM   1592 C CE2 . TYR   B 2 141 ? -11.108 0.123   -21.187 1.00 46.25  ? 150 TYR   B CE2 1 
ATOM   1593 C CZ  . TYR   B 2 141 ? -10.949 1.497   -21.092 1.00 48.19  ? 150 TYR   B CZ  1 
ATOM   1594 O OH  . TYR   B 2 141 ? -9.826  2.108   -21.635 1.00 49.18  ? 150 TYR   B OH  1 
ATOM   1595 N N   . GLY   B 2 142 ? -12.633 0.354   -16.849 1.00 42.40  ? 151 GLY   B N   1 
ATOM   1596 C CA  . GLY   B 2 142 ? -12.029 1.551   -16.217 1.00 43.49  ? 151 GLY   B CA  1 
ATOM   1597 C C   . GLY   B 2 142 ? -11.204 1.255   -14.967 1.00 44.55  ? 151 GLY   B C   1 
ATOM   1598 O O   . GLY   B 2 142 ? -10.622 2.244   -14.409 1.00 45.82  ? 151 GLY   B O   1 
ATOM   1599 N N   . ASN   B 2 143 ? -11.112 -0.013  -14.523 1.00 42.66  ? 152 ASN   B N   1 
ATOM   1600 C CA  . ASN   B 2 143 ? -10.142 -0.359  -13.458 1.00 43.24  ? 152 ASN   B CA  1 
ATOM   1601 C C   . ASN   B 2 143 ? -9.174  -1.441  -13.937 1.00 42.71  ? 152 ASN   B C   1 
ATOM   1602 O O   . ASN   B 2 143 ? -9.572  -2.592  -14.065 1.00 42.85  ? 152 ASN   B O   1 
ATOM   1603 C CB  . ASN   B 2 143 ? -10.815 -0.861  -12.180 1.00 43.67  ? 152 ASN   B CB  1 
ATOM   1604 C CG  . ASN   B 2 143 ? -9.896  -0.824  -10.970 1.00 45.48  ? 152 ASN   B CG  1 
ATOM   1605 O OD1 . ASN   B 2 143 ? -8.958  0.000   -10.891 1.00 46.35  ? 152 ASN   B OD1 1 
ATOM   1606 N ND2 . ASN   B 2 143 ? -10.179 -1.708  -10.012 1.00 44.67  ? 152 ASN   B ND2 1 
ATOM   1607 N N   . GLY   B 2 144 ? -7.917  -1.079  -14.067 1.00 43.28  ? 153 GLY   B N   1 
ATOM   1608 C CA  . GLY   B 2 144 ? -6.902  -2.070  -14.445 1.00 46.95  ? 153 GLY   B CA  1 
ATOM   1609 C C   . GLY   B 2 144 ? -5.523  -1.485  -14.306 1.00 50.57  ? 153 GLY   B C   1 
ATOM   1610 O O   . GLY   B 2 144 ? -5.238  -0.880  -13.251 1.00 49.75  ? 153 GLY   B O   1 
ATOM   1611 N N   . VAL   B 2 145 ? -4.702  -1.635  -15.343 1.00 55.39  ? 154 VAL   B N   1 
ATOM   1612 C CA  . VAL   B 2 145 ? -3.229  -1.525  -15.216 1.00 59.54  ? 154 VAL   B CA  1 
ATOM   1613 C C   . VAL   B 2 145 ? -2.632  -0.876  -16.475 1.00 65.19  ? 154 VAL   B C   1 
ATOM   1614 O O   . VAL   B 2 145 ? -3.288  -0.867  -17.541 1.00 62.00  ? 154 VAL   B O   1 
ATOM   1615 C CB  . VAL   B 2 145 ? -2.689  -2.930  -14.897 1.00 61.57  ? 154 VAL   B CB  1 
ATOM   1616 C CG1 . VAL   B 2 145 ? -2.377  -3.760  -16.133 1.00 60.78  ? 154 VAL   B CG1 1 
ATOM   1617 C CG2 . VAL   B 2 145 ? -1.507  -2.828  -13.966 1.00 65.09  ? 154 VAL   B CG2 1 
ATOM   1618 N N   . VAL   B 2 146 ? -1.442  -0.298  -16.330 1.00 69.73  ? 155 VAL   B N   1 
ATOM   1619 C CA  . VAL   B 2 146 ? -0.694  0.371   -17.428 1.00 73.04  ? 155 VAL   B CA  1 
ATOM   1620 C C   . VAL   B 2 146 ? 0.488   -0.536  -17.780 1.00 76.16  ? 155 VAL   B C   1 
ATOM   1621 O O   . VAL   B 2 146 ? 1.238   -0.871  -16.858 1.00 76.63  ? 155 VAL   B O   1 
ATOM   1622 C CB  . VAL   B 2 146 ? -0.284  1.781   -16.980 1.00 74.13  ? 155 VAL   B CB  1 
ATOM   1623 C CG1 . VAL   B 2 146 ? 0.495   2.498   -18.053 1.00 77.47  ? 155 VAL   B CG1 1 
ATOM   1624 C CG2 . VAL   B 2 146 ? -1.501  2.602   -16.592 1.00 75.49  ? 155 VAL   B CG2 1 
ATOM   1625 N N   . ILE   B 2 147 ? 0.601   -0.982  -19.038 1.00 78.90  ? 156 ILE   B N   1 
ATOM   1626 C CA  . ILE   B 2 147 ? 1.412   -2.189  -19.384 1.00 84.23  ? 156 ILE   B CA  1 
ATOM   1627 C C   . ILE   B 2 147 ? 2.775   -1.770  -19.936 1.00 88.61  ? 156 ILE   B C   1 
ATOM   1628 O O   . ILE   B 2 147 ? 3.003   -0.566  -20.129 1.00 83.19  ? 156 ILE   B O   1 
ATOM   1629 C CB  . ILE   B 2 147 ? 0.667   -3.143  -20.343 1.00 86.25  ? 156 ILE   B CB  1 
ATOM   1630 C CG1 . ILE   B 2 147 ? -0.010  -2.428  -21.520 1.00 87.60  ? 156 ILE   B CG1 1 
ATOM   1631 C CG2 . ILE   B 2 147 ? -0.308  -4.016  -19.572 1.00 85.79  ? 156 ILE   B CG2 1 
ATOM   1632 C CD1 . ILE   B 2 147 ? -0.178  -3.326  -22.733 1.00 87.16  ? 156 ILE   B CD1 1 
ATOM   1633 N N   A LYS   B 2 148 ? 3.657   -2.756  -20.155 0.25 92.10  ? 157 LYS   B N   1 
ATOM   1634 N N   B LYS   B 2 148 ? 3.657   -2.756  -20.155 0.25 92.10  ? 157 LYS   B N   1 
ATOM   1635 N N   C LYS   B 2 148 ? 3.650   -2.759  -20.164 0.25 91.40  ? 157 LYS   B N   1 
ATOM   1636 N N   D LYS   B 2 148 ? 3.650   -2.759  -20.164 0.25 91.40  ? 157 LYS   B N   1 
ATOM   1637 C CA  A LYS   B 2 148 ? 5.000   -2.598  -20.781 0.25 96.33  ? 157 LYS   B CA  1 
ATOM   1638 C CA  B LYS   B 2 148 ? 5.000   -2.598  -20.781 0.25 96.33  ? 157 LYS   B CA  1 
ATOM   1639 C CA  C LYS   B 2 148 ? 4.996   -2.608  -20.783 0.25 95.13  ? 157 LYS   B CA  1 
ATOM   1640 C CA  D LYS   B 2 148 ? 4.996   -2.608  -20.783 0.25 95.13  ? 157 LYS   B CA  1 
ATOM   1641 C C   A LYS   B 2 148 ? 4.942   -1.527  -21.880 0.25 98.90  ? 157 LYS   B C   1 
ATOM   1642 C C   B LYS   B 2 148 ? 4.942   -1.527  -21.880 0.25 98.90  ? 157 LYS   B C   1 
ATOM   1643 C C   C LYS   B 2 148 ? 4.951   -1.544  -21.890 0.25 98.19  ? 157 LYS   B C   1 
ATOM   1644 C C   D LYS   B 2 148 ? 4.951   -1.544  -21.890 0.25 98.19  ? 157 LYS   B C   1 
ATOM   1645 O O   A LYS   B 2 148 ? 5.838   -0.659  -21.901 0.25 101.01 ? 157 LYS   B O   1 
ATOM   1646 O O   B LYS   B 2 148 ? 5.838   -0.659  -21.901 0.25 101.01 ? 157 LYS   B O   1 
ATOM   1647 O O   C LYS   B 2 148 ? 5.868   -0.699  -21.929 0.25 100.39 ? 157 LYS   B O   1 
ATOM   1648 O O   D LYS   B 2 148 ? 5.868   -0.699  -21.929 0.25 100.39 ? 157 LYS   B O   1 
ATOM   1649 C CB  A LYS   B 2 148 ? 5.473   -3.934  -21.369 0.25 97.42  ? 157 LYS   B CB  1 
ATOM   1650 C CB  B LYS   B 2 148 ? 5.473   -3.934  -21.369 0.25 97.42  ? 157 LYS   B CB  1 
ATOM   1651 C CB  C LYS   B 2 148 ? 5.463   -3.957  -21.343 0.25 95.25  ? 157 LYS   B CB  1 
ATOM   1652 C CB  D LYS   B 2 148 ? 5.463   -3.957  -21.343 0.25 95.25  ? 157 LYS   B CB  1 
ATOM   1653 C CG  A LYS   B 2 148 ? 5.321   -5.147  -20.456 0.25 97.30  ? 157 LYS   B CG  1 
ATOM   1654 C CG  B LYS   B 2 148 ? 5.321   -5.147  -20.456 0.25 97.30  ? 157 LYS   B CG  1 
ATOM   1655 C CG  C LYS   B 2 148 ? 4.706   -5.176  -20.822 0.25 94.23  ? 157 LYS   B CG  1 
ATOM   1656 C CG  D LYS   B 2 148 ? 4.706   -5.176  -20.822 0.25 94.23  ? 157 LYS   B CG  1 
ATOM   1657 C CD  A LYS   B 2 148 ? 5.268   -6.472  -21.199 0.25 97.63  ? 157 LYS   B CD  1 
ATOM   1658 C CD  B LYS   B 2 148 ? 5.268   -6.472  -21.199 0.25 97.63  ? 157 LYS   B CD  1 
ATOM   1659 C CD  C LYS   B 2 148 ? 3.539   -5.600  -21.699 0.25 93.11  ? 157 LYS   B CD  1 
ATOM   1660 C CD  D LYS   B 2 148 ? 3.539   -5.600  -21.699 0.25 93.11  ? 157 LYS   B CD  1 
ATOM   1661 C CE  A LYS   B 2 148 ? 6.498   -6.740  -22.042 0.25 98.52  ? 157 LYS   B CE  1 
ATOM   1662 C CE  B LYS   B 2 148 ? 6.498   -6.740  -22.042 0.25 98.52  ? 157 LYS   B CE  1 
ATOM   1663 C CE  C LYS   B 2 148 ? 3.904   -6.654  -22.725 0.25 93.01  ? 157 LYS   B CE  1 
ATOM   1664 C CE  D LYS   B 2 148 ? 3.904   -6.654  -22.725 0.25 93.01  ? 157 LYS   B CE  1 
ATOM   1665 N NZ  A LYS   B 2 148 ? 7.684   -7.021  -21.201 0.25 98.33  ? 157 LYS   B NZ  1 
ATOM   1666 N NZ  B LYS   B 2 148 ? 7.684   -7.021  -21.201 0.25 98.33  ? 157 LYS   B NZ  1 
ATOM   1667 N NZ  C LYS   B 2 148 ? 5.048   -6.237  -23.571 0.25 93.28  ? 157 LYS   B NZ  1 
ATOM   1668 N NZ  D LYS   B 2 148 ? 5.048   -6.237  -23.571 0.25 93.28  ? 157 LYS   B NZ  1 
ATOM   1669 N N   . ASN   B 2 149 ? 3.908   -1.583  -22.732 1.00 100.22 ? 158 ASN   B N   1 
ATOM   1670 C CA  . ASN   B 2 149 ? 3.749   -0.722  -23.946 1.00 100.14 ? 158 ASN   B CA  1 
ATOM   1671 C C   . ASN   B 2 149 ? 3.391   0.745   -23.632 1.00 95.71  ? 158 ASN   B C   1 
ATOM   1672 O O   . ASN   B 2 149 ? 3.600   1.604   -24.513 1.00 94.67  ? 158 ASN   B O   1 
ATOM   1673 C CB  . ASN   B 2 149 ? 2.650   -1.272  -24.876 1.00 105.96 ? 158 ASN   B CB  1 
ATOM   1674 C CG  . ASN   B 2 149 ? 2.684   -2.774  -25.132 1.00 108.25 ? 158 ASN   B CG  1 
ATOM   1675 O OD1 . ASN   B 2 149 ? 3.645   -3.472  -24.800 1.00 115.48 ? 158 ASN   B OD1 1 
ATOM   1676 N ND2 . ASN   B 2 149 ? 1.624   -3.294  -25.733 1.00 106.66 ? 158 ASN   B ND2 1 
ATOM   1677 N N   . GLY   B 2 150 ? 2.787   1.026   -22.479 1.00 93.15  ? 159 GLY   B N   1 
ATOM   1678 C CA  . GLY   B 2 150 ? 2.263   2.367   -22.138 1.00 87.84  ? 159 GLY   B CA  1 
ATOM   1679 C C   . GLY   B 2 150 ? 0.742   2.457   -22.217 1.00 85.49  ? 159 GLY   B C   1 
ATOM   1680 O O   . GLY   B 2 150 ? 0.165   3.402   -21.632 1.00 83.77  ? 159 GLY   B O   1 
ATOM   1681 N N   A SER   B 2 151 ? 0.105   1.502   -22.913 0.25 84.14  ? 160 SER   B N   1 
ATOM   1682 N N   B SER   B 2 151 ? 0.109   1.502   -22.910 0.25 84.29  ? 160 SER   B N   1 
ATOM   1683 N N   C SER   B 2 151 ? 0.105   1.502   -22.913 0.25 84.14  ? 160 SER   B N   1 
ATOM   1684 N N   D SER   B 2 151 ? 0.109   1.502   -22.910 0.25 84.29  ? 160 SER   B N   1 
ATOM   1685 C CA  A SER   B 2 151 ? -1.369  1.408   -23.108 0.25 81.15  ? 160 SER   B CA  1 
ATOM   1686 C CA  B SER   B 2 151 ? -1.363  1.402   -23.110 0.25 81.37  ? 160 SER   B CA  1 
ATOM   1687 C CA  C SER   B 2 151 ? -1.369  1.408   -23.108 0.25 81.15  ? 160 SER   B CA  1 
ATOM   1688 C CA  D SER   B 2 151 ? -1.363  1.402   -23.110 0.25 81.37  ? 160 SER   B CA  1 
ATOM   1689 C C   A SER   B 2 151 ? -2.054  0.978   -21.801 0.25 78.25  ? 160 SER   B C   1 
ATOM   1690 C C   B SER   B 2 151 ? -2.055  0.964   -21.808 0.25 78.39  ? 160 SER   B C   1 
ATOM   1691 C C   C SER   B 2 151 ? -2.054  0.978   -21.801 0.25 78.25  ? 160 SER   B C   1 
ATOM   1692 C C   D SER   B 2 151 ? -2.055  0.964   -21.808 0.25 78.39  ? 160 SER   B C   1 
ATOM   1693 O O   A SER   B 2 151 ? -1.347  0.503   -20.882 0.25 77.51  ? 160 SER   B O   1 
ATOM   1694 O O   B SER   B 2 151 ? -1.352  0.473   -20.895 0.25 77.68  ? 160 SER   B O   1 
ATOM   1695 O O   C SER   B 2 151 ? -1.347  0.503   -20.882 0.25 77.51  ? 160 SER   B O   1 
ATOM   1696 O O   D SER   B 2 151 ? -1.352  0.473   -20.895 0.25 77.68  ? 160 SER   B O   1 
ATOM   1697 C CB  A SER   B 2 151 ? -1.710  0.463   -24.238 0.25 81.58  ? 160 SER   B CB  1 
ATOM   1698 C CB  B SER   B 2 151 ? -1.671  0.460   -24.246 0.25 81.96  ? 160 SER   B CB  1 
ATOM   1699 C CB  C SER   B 2 151 ? -1.710  0.463   -24.238 0.25 81.58  ? 160 SER   B CB  1 
ATOM   1700 C CB  D SER   B 2 151 ? -1.671  0.460   -24.246 0.25 81.96  ? 160 SER   B CB  1 
ATOM   1701 O OG  A SER   B 2 151 ? -3.098  0.516   -24.542 0.25 81.21  ? 160 SER   B OG  1 
ATOM   1702 O OG  B SER   B 2 151 ? -0.866  -0.708  -24.163 0.25 82.51  ? 160 SER   B OG  1 
ATOM   1703 O OG  C SER   B 2 151 ? -3.098  0.516   -24.542 0.25 81.21  ? 160 SER   B OG  1 
ATOM   1704 O OG  D SER   B 2 151 ? -0.866  -0.708  -24.163 0.25 82.51  ? 160 SER   B OG  1 
ATOM   1705 N N   . TYR   B 2 152 ? -3.381  1.144   -21.731 1.00 74.92  ? 161 TYR   B N   1 
ATOM   1706 C CA  . TYR   B 2 152 ? -4.225  0.710   -20.579 1.00 72.03  ? 161 TYR   B CA  1 
ATOM   1707 C C   . TYR   B 2 152 ? -4.855  -0.656  -20.882 1.00 64.93  ? 161 TYR   B C   1 
ATOM   1708 O O   . TYR   B 2 152 ? -5.380  -0.839  -21.952 1.00 60.74  ? 161 TYR   B O   1 
ATOM   1709 C CB  . TYR   B 2 152 ? -5.360  1.702   -20.281 1.00 71.90  ? 161 TYR   B CB  1 
ATOM   1710 C CG  . TYR   B 2 152 ? -5.916  1.614   -18.878 1.00 72.43  ? 161 TYR   B CG  1 
ATOM   1711 C CD1 . TYR   B 2 152 ? -5.178  2.090   -17.806 1.00 72.69  ? 161 TYR   B CD1 1 
ATOM   1712 C CD2 . TYR   B 2 152 ? -7.170  1.080   -18.600 1.00 72.53  ? 161 TYR   B CD2 1 
ATOM   1713 C CE1 . TYR   B 2 152 ? -5.646  2.009   -16.504 1.00 71.57  ? 161 TYR   B CE1 1 
ATOM   1714 C CE2 . TYR   B 2 152 ? -7.655  1.003   -17.296 1.00 70.77  ? 161 TYR   B CE2 1 
ATOM   1715 C CZ  . TYR   B 2 152 ? -6.890  1.464   -16.234 1.00 71.12  ? 161 TYR   B CZ  1 
ATOM   1716 O OH  . TYR   B 2 152 ? -7.323  1.424   -14.920 1.00 75.03  ? 161 TYR   B OH  1 
ATOM   1717 N N   . VAL   B 2 153 ? -4.863  -1.556  -19.905 1.00 60.22  ? 162 VAL   B N   1 
ATOM   1718 C CA  . VAL   B 2 153 ? -5.647  -2.828  -19.896 1.00 57.19  ? 162 VAL   B CA  1 
ATOM   1719 C C   . VAL   B 2 153 ? -6.608  -2.796  -18.690 1.00 53.40  ? 162 VAL   B C   1 
ATOM   1720 O O   . VAL   B 2 153 ? -6.102  -2.790  -17.595 1.00 51.44  ? 162 VAL   B O   1 
ATOM   1721 C CB  . VAL   B 2 153 ? -4.682  -4.030  -19.794 1.00 56.73  ? 162 VAL   B CB  1 
ATOM   1722 C CG1 . VAL   B 2 153 ? -5.377  -5.354  -20.082 1.00 55.55  ? 162 VAL   B CG1 1 
ATOM   1723 C CG2 . VAL   B 2 153 ? -3.472  -3.844  -20.691 1.00 61.14  ? 162 VAL   B CG2 1 
ATOM   1724 N N   . SER   B 2 154 ? -7.924  -2.832  -18.904 1.00 50.91  ? 163 SER   B N   1 
ATOM   1725 C CA  . SER   B 2 154 ? -8.989  -2.815  -17.879 1.00 47.68  ? 163 SER   B CA  1 
ATOM   1726 C C   . SER   B 2 154 ? -9.509  -4.234  -17.605 1.00 46.86  ? 163 SER   B C   1 
ATOM   1727 O O   . SER   B 2 154 ? -9.775  -4.981  -18.552 1.00 46.17  ? 163 SER   B O   1 
ATOM   1728 C CB  . SER   B 2 154 ? -10.127 -1.917  -18.293 1.00 47.05  ? 163 SER   B CB  1 
ATOM   1729 O OG  . SER   B 2 154 ? -11.269 -2.077  -17.436 1.00 45.61  ? 163 SER   B OG  1 
ATOM   1730 N N   . ALA   B 2 155 ? -9.739  -4.551  -16.331 1.00 42.72  ? 164 ALA   B N   1 
ATOM   1731 C CA  . ALA   B 2 155 ? -10.545 -5.706  -15.916 1.00 41.93  ? 164 ALA   B CA  1 
ATOM   1732 C C   . ALA   B 2 155 ? -11.926 -5.535  -16.533 1.00 42.77  ? 164 ALA   B C   1 
ATOM   1733 O O   . ALA   B 2 155 ? -12.387 -4.384  -16.702 1.00 43.78  ? 164 ALA   B O   1 
ATOM   1734 C CB  . ALA   B 2 155 ? -10.644 -5.745  -14.398 1.00 41.62  ? 164 ALA   B CB  1 
ATOM   1735 N N   . ILE   B 2 156 ? -12.584 -6.649  -16.819 1.00 43.37  ? 165 ILE   B N   1 
ATOM   1736 C CA  . ILE   B 2 156 ? -14.062 -6.736  -16.824 1.00 42.88  ? 165 ILE   B CA  1 
ATOM   1737 C C   . ILE   B 2 156 ? -14.524 -6.848  -15.351 1.00 42.97  ? 165 ILE   B C   1 
ATOM   1738 O O   . ILE   B 2 156 ? -14.601 -7.995  -14.830 1.00 42.17  ? 165 ILE   B O   1 
ATOM   1739 C CB  . ILE   B 2 156 ? -14.521 -7.929  -17.673 1.00 44.16  ? 165 ILE   B CB  1 
ATOM   1740 C CG1 . ILE   B 2 156 ? -13.832 -7.899  -19.049 1.00 46.70  ? 165 ILE   B CG1 1 
ATOM   1741 C CG2 . ILE   B 2 156 ? -16.054 -7.916  -17.752 1.00 43.67  ? 165 ILE   B CG2 1 
ATOM   1742 C CD1 . ILE   B 2 156 ? -14.123 -9.083  -19.946 1.00 48.28  ? 165 ILE   B CD1 1 
ATOM   1743 N N   . THR   B 2 157 ? -14.811 -5.701  -14.715 1.00 42.73  ? 166 THR   B N   1 
ATOM   1744 C CA  . THR   B 2 157 ? -15.271 -5.565  -13.293 1.00 40.86  ? 166 THR   B CA  1 
ATOM   1745 C C   . THR   B 2 157 ? -16.798 -5.738  -13.235 1.00 41.86  ? 166 THR   B C   1 
ATOM   1746 O O   . THR   B 2 157 ? -17.526 -4.828  -13.738 1.00 41.42  ? 166 THR   B O   1 
ATOM   1747 C CB  . THR   B 2 157 ? -14.865 -4.212  -12.706 1.00 40.44  ? 166 THR   B CB  1 
ATOM   1748 O OG1 . THR   B 2 157 ? -13.437 -4.112  -12.827 1.00 38.76  ? 166 THR   B OG1 1 
ATOM   1749 C CG2 . THR   B 2 157 ? -15.312 -4.065  -11.260 1.00 40.31  ? 166 THR   B CG2 1 
ATOM   1750 N N   . GLN   B 2 158 ? -17.262 -6.869  -12.684 1.00 41.95  ? 167 GLN   B N   1 
ATOM   1751 C CA  . GLN   B 2 158 ? -18.686 -7.185  -12.429 1.00 42.43  ? 167 GLN   B CA  1 
ATOM   1752 C C   . GLN   B 2 158 ? -18.892 -7.316  -10.905 1.00 46.43  ? 167 GLN   B C   1 
ATOM   1753 O O   . GLN   B 2 158 ? -17.975 -7.764  -10.202 1.00 43.64  ? 167 GLN   B O   1 
ATOM   1754 C CB  . GLN   B 2 158 ? -19.028 -8.467  -13.169 1.00 42.19  ? 167 GLN   B CB  1 
ATOM   1755 C CG  . GLN   B 2 158 ? -20.477 -8.906  -13.091 1.00 42.15  ? 167 GLN   B CG  1 
ATOM   1756 C CD  . GLN   B 2 158 ? -21.412 -7.820  -13.566 1.00 43.06  ? 167 GLN   B CD  1 
ATOM   1757 O OE1 . GLN   B 2 158 ? -21.507 -6.756  -12.959 1.00 41.79  ? 167 GLN   B OE1 1 
ATOM   1758 N NE2 . GLN   B 2 158 ? -22.081 -8.067  -14.687 1.00 43.18  ? 167 GLN   B NE2 1 
ATOM   1759 N N   . GLY   B 2 159 ? -20.050 -6.901  -10.420 1.00 51.03  ? 168 GLY   B N   1 
ATOM   1760 C CA  . GLY   B 2 159 ? -20.471 -7.116  -9.030  1.00 57.56  ? 168 GLY   B CA  1 
ATOM   1761 C C   . GLY   B 2 159 ? -21.242 -8.412  -8.891  1.00 64.54  ? 168 GLY   B C   1 
ATOM   1762 O O   . GLY   B 2 159 ? -21.491 -9.085  -9.870  1.00 63.24  ? 168 GLY   B O   1 
ATOM   1763 N N   A LYS   B 2 160 ? -21.604 -8.744  -7.651  0.17 68.33  ? 169 LYS   B N   1 
ATOM   1764 N N   B LYS   B 2 160 ? -21.604 -8.744  -7.651  0.17 68.33  ? 169 LYS   B N   1 
ATOM   1765 N N   C LYS   B 2 160 ? -21.580 -8.758  -7.646  0.33 69.99  ? 169 LYS   B N   1 
ATOM   1766 N N   D LYS   B 2 160 ? -21.580 -8.758  -7.646  0.33 69.99  ? 169 LYS   B N   1 
ATOM   1767 C CA  A LYS   B 2 160 ? -22.465 -9.902  -7.292  0.17 71.52  ? 169 LYS   B CA  1 
ATOM   1768 C CA  B LYS   B 2 160 ? -22.465 -9.902  -7.292  0.17 71.52  ? 169 LYS   B CA  1 
ATOM   1769 C CA  C LYS   B 2 160 ? -22.455 -9.903  -7.266  0.33 72.99  ? 169 LYS   B CA  1 
ATOM   1770 C CA  D LYS   B 2 160 ? -22.455 -9.903  -7.266  0.33 72.99  ? 169 LYS   B CA  1 
ATOM   1771 C C   A LYS   B 2 160 ? -23.909 -9.402  -7.148  0.17 75.16  ? 169 LYS   B C   1 
ATOM   1772 C C   B LYS   B 2 160 ? -23.909 -9.402  -7.148  0.17 75.16  ? 169 LYS   B C   1 
ATOM   1773 C C   C LYS   B 2 160 ? -23.904 -9.388  -7.188  0.33 76.17  ? 169 LYS   B C   1 
ATOM   1774 C C   D LYS   B 2 160 ? -23.904 -9.388  -7.188  0.33 76.17  ? 169 LYS   B C   1 
ATOM   1775 O O   A LYS   B 2 160 ? -24.089 -8.237  -6.737  0.17 75.17  ? 169 LYS   B O   1 
ATOM   1776 O O   B LYS   B 2 160 ? -24.089 -8.237  -6.737  0.17 75.17  ? 169 LYS   B O   1 
ATOM   1777 O O   C LYS   B 2 160 ? -24.086 -8.190  -6.879  0.33 75.69  ? 169 LYS   B O   1 
ATOM   1778 O O   D LYS   B 2 160 ? -24.086 -8.190  -6.879  0.33 75.69  ? 169 LYS   B O   1 
ATOM   1779 C CB  A LYS   B 2 160 ? -21.953 -10.552 -6.001  0.17 70.93  ? 169 LYS   B CB  1 
ATOM   1780 C CB  B LYS   B 2 160 ? -21.953 -10.552 -6.001  0.17 70.93  ? 169 LYS   B CB  1 
ATOM   1781 C CB  C LYS   B 2 160 ? -21.980 -10.510 -5.936  0.33 72.76  ? 169 LYS   B CB  1 
ATOM   1782 C CB  D LYS   B 2 160 ? -21.980 -10.510 -5.936  0.33 72.76  ? 169 LYS   B CB  1 
ATOM   1783 C CG  A LYS   B 2 160 ? -22.624 -11.863 -5.618  0.17 70.23  ? 169 LYS   B CG  1 
ATOM   1784 C CG  B LYS   B 2 160 ? -22.624 -11.863 -5.618  0.17 70.23  ? 169 LYS   B CG  1 
ATOM   1785 C CG  C LYS   B 2 160 ? -20.467 -10.543 -5.725  0.33 71.16  ? 169 LYS   B CG  1 
ATOM   1786 C CG  D LYS   B 2 160 ? -20.467 -10.543 -5.725  0.33 71.16  ? 169 LYS   B CG  1 
ATOM   1787 C CD  A LYS   B 2 160 ? -22.162 -12.392 -4.286  0.17 69.19  ? 169 LYS   B CD  1 
ATOM   1788 C CD  B LYS   B 2 160 ? -22.162 -12.392 -4.286  0.17 69.19  ? 169 LYS   B CD  1 
ATOM   1789 C CD  C LYS   B 2 160 ? -19.744 -11.497 -6.655  0.33 69.98  ? 169 LYS   B CD  1 
ATOM   1790 C CD  D LYS   B 2 160 ? -19.744 -11.497 -6.655  0.33 69.98  ? 169 LYS   B CD  1 
ATOM   1791 C CE  A LYS   B 2 160 ? -22.938 -13.608 -3.838  0.17 68.97  ? 169 LYS   B CE  1 
ATOM   1792 C CE  B LYS   B 2 160 ? -22.938 -13.608 -3.838  0.17 68.97  ? 169 LYS   B CE  1 
ATOM   1793 C CE  C LYS   B 2 160 ? -18.237 -11.349 -6.615  0.33 69.43  ? 169 LYS   B CE  1 
ATOM   1794 C CE  D LYS   B 2 160 ? -18.237 -11.349 -6.615  0.33 69.43  ? 169 LYS   B CE  1 
ATOM   1795 N NZ  A LYS   B 2 160 ? -22.793 -13.821 -2.379  0.17 68.92  ? 169 LYS   B NZ  1 
ATOM   1796 N NZ  B LYS   B 2 160 ? -22.793 -13.821 -2.379  0.17 68.92  ? 169 LYS   B NZ  1 
ATOM   1797 N NZ  C LYS   B 2 160 ? -17.776 -10.149 -7.351  0.33 68.38  ? 169 LYS   B NZ  1 
ATOM   1798 N NZ  D LYS   B 2 160 ? -17.776 -10.149 -7.351  0.33 68.38  ? 169 LYS   B NZ  1 
ATOM   1799 N N   . ARG   B 2 161 ? -24.888 -10.245 -7.491  1.00 79.47  ? 170 ARG   B N   1 
ATOM   1800 C CA  . ARG   B 2 161 ? -26.348 -9.940  -7.319  1.00 85.40  ? 170 ARG   B CA  1 
ATOM   1801 C C   . ARG   B 2 161 ? -26.898 -10.935 -6.280  1.00 90.65  ? 170 ARG   B C   1 
ATOM   1802 O O   . ARG   B 2 161 ? -26.749 -12.144 -6.520  1.00 95.99  ? 170 ARG   B O   1 
ATOM   1803 C CB  . ARG   B 2 161 ? -27.073 -10.021 -8.674  1.00 90.36  ? 170 ARG   B CB  1 
ATOM   1804 C CG  . ARG   B 2 161 ? -28.571 -9.715  -8.648  1.00 91.88  ? 170 ARG   B CG  1 
ATOM   1805 C CD  . ARG   B 2 161 ? -29.294 -10.099 -9.943  1.00 95.45  ? 170 ARG   B CD  1 
ATOM   1806 N NE  . ARG   B 2 161 ? -30.765 -10.041 -9.878  1.00 97.79  ? 170 ARG   B NE  1 
ATOM   1807 C CZ  . ARG   B 2 161 ? -31.579 -9.319  -10.674 1.00 96.81  ? 170 ARG   B CZ  1 
ATOM   1808 N NH1 . ARG   B 2 161 ? -31.101 -8.547  -11.641 1.00 91.12  ? 170 ARG   B NH1 1 
ATOM   1809 N NH2 . ARG   B 2 161 ? -32.891 -9.372  -10.490 1.00 96.35  ? 170 ARG   B NH2 1 
ATOM   1810 N N   . GLU   B 2 162 ? -27.474 -10.460 -5.164  1.00 97.07  ? 171 GLU   B N   1 
ATOM   1811 C CA  . GLU   B 2 162 ? -27.902 -11.302 -4.001  1.00 99.20  ? 171 GLU   B CA  1 
ATOM   1812 C C   . GLU   B 2 162 ? -29.423 -11.521 -4.056  1.00 92.89  ? 171 GLU   B C   1 
ATOM   1813 O O   . GLU   B 2 162 ? -29.970 -12.206 -4.930  1.00 84.60  ? 171 GLU   B O   1 
ATOM   1814 C CB  . GLU   B 2 162 ? -27.463 -10.659 -2.675  1.00 104.52 ? 171 GLU   B CB  1 
ATOM   1815 C CG  . GLU   B 2 162 ? -25.946 -10.564 -2.479  1.00 107.79 ? 171 GLU   B CG  1 
ATOM   1816 C CD  . GLU   B 2 162 ? -25.321 -11.539 -1.485  1.00 109.04 ? 171 GLU   B CD  1 
ATOM   1817 O OE1 . GLU   B 2 162 ? -25.451 -11.310 -0.260  1.00 105.73 ? 171 GLU   B OE1 1 
ATOM   1818 O OE2 . GLU   B 2 162 ? -24.693 -12.517 -1.932  1.00 112.00 ? 171 GLU   B OE2 1 
HETATM 1819 S S   A DMS   C 3 .   ? -7.922  5.301   -18.411 0.07 113.70 ? 201 DMS   B S   1 
HETATM 1820 S S   B DMS   C 3 .   ? -7.922  5.301   -18.411 0.07 113.70 ? 201 DMS   B S   1 
HETATM 1821 S S   C DMS   C 3 .   ? -5.240  8.056   -24.574 0.43 109.22 ? 201 DMS   B S   1 
HETATM 1822 S S   D DMS   C 3 .   ? -5.240  8.056   -24.574 0.43 109.22 ? 201 DMS   B S   1 
HETATM 1823 O O   A DMS   C 3 .   ? -6.614  4.705   -18.848 0.07 113.70 ? 201 DMS   B O   1 
HETATM 1824 O O   B DMS   C 3 .   ? -6.614  4.705   -18.848 0.07 113.70 ? 201 DMS   B O   1 
HETATM 1825 O O   C DMS   C 3 .   ? -4.774  9.088   -25.558 0.43 109.18 ? 201 DMS   B O   1 
HETATM 1826 O O   D DMS   C 3 .   ? -4.774  9.088   -25.558 0.43 109.18 ? 201 DMS   B O   1 
HETATM 1827 C C1  A DMS   C 3 .   ? -8.009  5.071   -16.654 0.07 113.38 ? 201 DMS   B C1  1 
HETATM 1828 C C1  B DMS   C 3 .   ? -8.009  5.071   -16.654 0.07 113.38 ? 201 DMS   B C1  1 
HETATM 1829 C C1  C DMS   C 3 .   ? -6.476  7.111   -25.414 0.43 107.81 ? 201 DMS   B C1  1 
HETATM 1830 C C1  D DMS   C 3 .   ? -6.476  7.111   -25.414 0.43 107.81 ? 201 DMS   B C1  1 
HETATM 1831 C C2  A DMS   C 3 .   ? -9.177  4.133   -18.868 0.07 113.47 ? 201 DMS   B C2  1 
HETATM 1832 C C2  B DMS   C 3 .   ? -9.177  4.133   -18.868 0.07 113.47 ? 201 DMS   B C2  1 
HETATM 1833 C C2  C DMS   C 3 .   ? -6.310  8.907   -23.445 0.43 106.52 ? 201 DMS   B C2  1 
HETATM 1834 C C2  D DMS   C 3 .   ? -6.310  8.907   -23.445 0.43 106.52 ? 201 DMS   B C2  1 
HETATM 1835 S S   A DMS   D 3 .   ? -17.772 11.813  -0.277  0.25 382.19 ? 202 DMS   B S   1 
HETATM 1836 S S   B DMS   D 3 .   ? -17.772 11.813  -0.277  0.25 382.19 ? 202 DMS   B S   1 
HETATM 1837 S S   C DMS   D 3 .   ? -21.119 15.846  -23.515 0.25 64.52  ? 202 DMS   B S   1 
HETATM 1838 S S   D DMS   D 3 .   ? -21.119 15.846  -23.515 0.25 64.52  ? 202 DMS   B S   1 
HETATM 1839 O O   A DMS   D 3 .   ? -18.043 10.335  -0.234  0.25 380.72 ? 202 DMS   B O   1 
HETATM 1840 O O   B DMS   D 3 .   ? -18.043 10.335  -0.234  0.25 380.72 ? 202 DMS   B O   1 
HETATM 1841 O O   C DMS   D 3 .   ? -22.434 15.412  -24.104 0.25 64.65  ? 202 DMS   B O   1 
HETATM 1842 O O   D DMS   D 3 .   ? -22.434 15.412  -24.104 0.25 64.65  ? 202 DMS   B O   1 
HETATM 1843 C C1  A DMS   D 3 .   ? -19.330 12.590  -0.623  0.25 380.84 ? 202 DMS   B C1  1 
HETATM 1844 C C1  B DMS   D 3 .   ? -19.330 12.590  -0.623  0.25 380.84 ? 202 DMS   B C1  1 
HETATM 1845 C C1  C DMS   D 3 .   ? -21.523 16.910  -22.156 0.25 62.87  ? 202 DMS   B C1  1 
HETATM 1846 C C1  D DMS   D 3 .   ? -21.523 16.910  -22.156 0.25 62.87  ? 202 DMS   B C1  1 
HETATM 1847 C C2  A DMS   D 3 .   ? -16.996 12.127  -1.841  0.25 380.02 ? 202 DMS   B C2  1 
HETATM 1848 C C2  B DMS   D 3 .   ? -16.996 12.127  -1.841  0.25 380.02 ? 202 DMS   B C2  1 
HETATM 1849 C C2  C DMS   D 3 .   ? -20.497 17.089  -24.623 0.25 64.88  ? 202 DMS   B C2  1 
HETATM 1850 C C2  D DMS   D 3 .   ? -20.497 17.089  -24.623 0.25 64.88  ? 202 DMS   B C2  1 
HETATM 1851 S S   A DMS   E 3 .   ? -5.585  3.412   -13.440 0.07 58.76  ? 203 DMS   B S   1 
HETATM 1852 S S   B DMS   E 3 .   ? -5.585  3.412   -13.440 0.07 58.76  ? 203 DMS   B S   1 
HETATM 1853 O O   A DMS   E 3 .   ? -4.896  2.319   -12.683 0.07 58.67  ? 203 DMS   B O   1 
HETATM 1854 O O   B DMS   E 3 .   ? -4.896  2.319   -12.683 0.07 58.67  ? 203 DMS   B O   1 
HETATM 1855 C C1  A DMS   E 3 .   ? -7.231  3.510   -12.776 0.07 58.77  ? 203 DMS   B C1  1 
HETATM 1856 C C1  B DMS   E 3 .   ? -7.231  3.510   -12.776 0.07 58.77  ? 203 DMS   B C1  1 
HETATM 1857 C C2  A DMS   E 3 .   ? -4.970  4.935   -12.774 0.07 58.80  ? 203 DMS   B C2  1 
HETATM 1858 C C2  B DMS   E 3 .   ? -4.970  4.935   -12.774 0.07 58.80  ? 203 DMS   B C2  1 
HETATM 1859 N N1  C A1BGO F 4 .   ? -6.659  5.509   -19.371 0.43 66.64  ? 204 A1BGO B N1  1 
HETATM 1860 N N1  D A1BGO F 4 .   ? -6.659  5.509   -19.371 0.43 66.64  ? 204 A1BGO B N1  1 
HETATM 1861 N N3  C A1BGO F 4 .   ? -8.909  4.683   -13.755 0.43 69.11  ? 204 A1BGO B N3  1 
HETATM 1862 N N3  D A1BGO F 4 .   ? -8.909  4.683   -13.755 0.43 69.11  ? 204 A1BGO B N3  1 
HETATM 1863 C C4  C A1BGO F 4 .   ? -7.580  5.059   -18.400 0.43 63.93  ? 204 A1BGO B C4  1 
HETATM 1864 C C4  D A1BGO F 4 .   ? -7.580  5.059   -18.400 0.43 63.93  ? 204 A1BGO B C4  1 
HETATM 1865 C C5  C A1BGO F 4 .   ? -8.722  4.354   -18.766 0.43 62.25  ? 204 A1BGO B C5  1 
HETATM 1866 C C5  D A1BGO F 4 .   ? -8.722  4.354   -18.766 0.43 62.25  ? 204 A1BGO B C5  1 
HETATM 1867 C C6  C A1BGO F 4 .   ? -9.406  4.176   -16.588 0.43 60.38  ? 204 A1BGO B C6  1 
HETATM 1868 C C6  D A1BGO F 4 .   ? -9.406  4.176   -16.588 0.43 60.38  ? 204 A1BGO B C6  1 
HETATM 1869 C C7  C A1BGO F 4 .   ? -8.304  4.876   -16.114 0.43 64.44  ? 204 A1BGO B C7  1 
HETATM 1870 C C7  D A1BGO F 4 .   ? -8.304  4.876   -16.114 0.43 64.44  ? 204 A1BGO B C7  1 
HETATM 1871 C C8  C A1BGO F 4 .   ? -8.037  5.174   -14.667 0.43 68.05  ? 204 A1BGO B C8  1 
HETATM 1872 C C8  D A1BGO F 4 .   ? -8.037  5.174   -14.667 0.43 68.05  ? 204 A1BGO B C8  1 
HETATM 1873 C C10 C A1BGO F 4 .   ? -8.579  3.338   -11.737 0.43 70.88  ? 204 A1BGO B C10 1 
HETATM 1874 C C10 D A1BGO F 4 .   ? -8.579  3.338   -11.737 0.43 70.88  ? 204 A1BGO B C10 1 
HETATM 1875 C C13 C A1BGO F 4 .   ? -8.586  5.729   -11.562 0.43 74.01  ? 204 A1BGO B C13 1 
HETATM 1876 C C13 D A1BGO F 4 .   ? -8.586  5.729   -11.562 0.43 74.01  ? 204 A1BGO B C13 1 
HETATM 1877 C C15 C A1BGO F 4 .   ? -7.380  5.330   -17.047 0.43 63.69  ? 204 A1BGO B C15 1 
HETATM 1878 C C15 D A1BGO F 4 .   ? -7.380  5.330   -17.047 0.43 63.69  ? 204 A1BGO B C15 1 
HETATM 1879 C C1  C A1BGO F 4 .   ? -4.708  6.688   -21.421 0.43 69.74  ? 204 A1BGO B C1  1 
HETATM 1880 C C1  D A1BGO F 4 .   ? -4.708  6.688   -21.421 0.43 69.74  ? 204 A1BGO B C1  1 
HETATM 1881 C C2  C A1BGO F 4 .   ? -4.587  5.446   -20.595 0.43 69.96  ? 204 A1BGO B C2  1 
HETATM 1882 C C2  D A1BGO F 4 .   ? -4.587  5.446   -20.595 0.43 69.96  ? 204 A1BGO B C2  1 
HETATM 1883 C C3  C A1BGO F 4 .   ? -5.310  5.535   -19.270 0.43 69.68  ? 204 A1BGO B C3  1 
HETATM 1884 C C3  D A1BGO F 4 .   ? -5.310  5.535   -19.270 0.43 69.68  ? 204 A1BGO B C3  1 
HETATM 1885 O O1  C A1BGO F 4 .   ? -4.717  5.632   -18.202 0.43 71.52  ? 204 A1BGO B O1  1 
HETATM 1886 O O1  D A1BGO F 4 .   ? -4.717  5.632   -18.202 0.43 71.52  ? 204 A1BGO B O1  1 
HETATM 1887 N N2  C A1BGO F 4 .   ? -9.626  3.916   -17.882 0.43 60.52  ? 204 A1BGO B N2  1 
HETATM 1888 N N2  D A1BGO F 4 .   ? -9.626  3.916   -17.882 0.43 60.52  ? 204 A1BGO B N2  1 
HETATM 1889 O O2  C A1BGO F 4 .   ? -7.052  5.833   -14.349 0.43 68.95  ? 204 A1BGO B O2  1 
HETATM 1890 O O2  D A1BGO F 4 .   ? -7.052  5.833   -14.349 0.43 68.95  ? 204 A1BGO B O2  1 
HETATM 1891 C C9  C A1BGO F 4 .   ? -8.691  4.577   -12.351 0.43 72.17  ? 204 A1BGO B C9  1 
HETATM 1892 C C9  D A1BGO F 4 .   ? -8.691  4.577   -12.351 0.43 72.17  ? 204 A1BGO B C9  1 
HETATM 1893 C C11 C A1BGO F 4 .   ? -8.372  3.292   -10.384 0.43 71.46  ? 204 A1BGO B C11 1 
HETATM 1894 C C11 D A1BGO F 4 .   ? -8.372  3.292   -10.384 0.43 71.46  ? 204 A1BGO B C11 1 
HETATM 1895 N N4  C A1BGO F 4 .   ? -8.270  4.373   -9.606  0.43 71.16  ? 204 A1BGO B N4  1 
HETATM 1896 N N4  D A1BGO F 4 .   ? -8.270  4.373   -9.606  0.43 71.16  ? 204 A1BGO B N4  1 
HETATM 1897 C C12 C A1BGO F 4 .   ? -8.375  5.573   -10.200 0.43 72.87  ? 204 A1BGO B C12 1 
HETATM 1898 C C12 D A1BGO F 4 .   ? -8.375  5.573   -10.200 0.43 72.87  ? 204 A1BGO B C12 1 
HETATM 1899 C C14 C A1BGO F 4 .   ? -8.701  7.114   -12.153 0.43 74.40  ? 204 A1BGO B C14 1 
HETATM 1900 C C14 D A1BGO F 4 .   ? -8.701  7.114   -12.153 0.43 74.40  ? 204 A1BGO B C14 1 
HETATM 1901 S S   C SO4   G 5 .   ? -18.585 11.606  -0.316  0.50 101.48 ? 205 SO4   B S   1 
HETATM 1902 S S   D SO4   G 5 .   ? -18.585 11.606  -0.316  0.50 101.48 ? 205 SO4   B S   1 
HETATM 1903 O O1  C SO4   G 5 .   ? -18.376 12.421  -1.483  0.50 101.64 ? 205 SO4   B O1  1 
HETATM 1904 O O1  D SO4   G 5 .   ? -18.376 12.421  -1.483  0.50 101.64 ? 205 SO4   B O1  1 
HETATM 1905 O O2  C SO4   G 5 .   ? -19.476 10.522  -0.634  0.50 100.93 ? 205 SO4   B O2  1 
HETATM 1906 O O2  D SO4   G 5 .   ? -19.476 10.522  -0.634  0.50 100.93 ? 205 SO4   B O2  1 
HETATM 1907 O O3  C SO4   G 5 .   ? -17.322 11.070  0.123   0.50 101.90 ? 205 SO4   B O3  1 
HETATM 1908 O O3  D SO4   G 5 .   ? -17.322 11.070  0.123   0.50 101.90 ? 205 SO4   B O3  1 
HETATM 1909 O O4  C SO4   G 5 .   ? -19.164 12.408  0.730   0.50 98.79  ? 205 SO4   B O4  1 
HETATM 1910 O O4  D SO4   G 5 .   ? -19.164 12.408  0.730   0.50 98.79  ? 205 SO4   B O4  1 
HETATM 1911 O O   A HOH   H 6 .   ? -26.176 0.130   -28.983 0.50 96.85  ? 101 HOH   A O   1 
HETATM 1912 O O   B HOH   H 6 .   ? -26.176 0.130   -28.983 0.50 96.85  ? 101 HOH   A O   1 
HETATM 1913 O O   . HOH   H 6 .   ? -27.947 -6.025  -28.040 1.00 49.33  ? 102 HOH   A O   1 
HETATM 1914 O O   A HOH   H 6 .   ? -2.155  -3.820  -6.512  0.50 61.79  ? 103 HOH   A O   1 
HETATM 1915 O O   B HOH   H 6 .   ? -2.155  -3.820  -6.512  0.50 61.79  ? 103 HOH   A O   1 
HETATM 1916 O O   . HOH   H 6 .   ? -23.937 8.936   -27.598 1.00 42.72  ? 104 HOH   A O   1 
HETATM 1917 O O   . HOH   H 6 .   ? 6.039   -5.927  -17.312 1.00 82.37  ? 105 HOH   A O   1 
HETATM 1918 O O   A HOH   H 6 .   ? -10.054 1.158   -7.888  0.07 30.69  ? 106 HOH   A O   1 
HETATM 1919 O O   B HOH   H 6 .   ? -10.054 1.158   -7.888  0.07 30.69  ? 106 HOH   A O   1 
HETATM 1920 O O   C HOH   H 6 .   ? -9.390  2.237   -7.662  0.43 62.12  ? 106 HOH   A O   1 
HETATM 1921 O O   D HOH   H 6 .   ? -9.390  2.237   -7.662  0.43 62.12  ? 106 HOH   A O   1 
HETATM 1922 O O   . HOH   H 6 .   ? -23.566 19.056  -19.442 1.00 56.19  ? 107 HOH   A O   1 
HETATM 1923 O O   C HOH   H 6 .   ? 8.499   -9.993  -15.413 0.50 67.42  ? 108 HOH   A O   1 
HETATM 1924 O O   D HOH   H 6 .   ? 8.499   -9.993  -15.413 0.50 67.42  ? 108 HOH   A O   1 
HETATM 1925 O O   A HOH   H 6 .   ? -28.789 15.565  -14.962 0.50 57.32  ? 109 HOH   A O   1 
HETATM 1926 O O   B HOH   H 6 .   ? -28.789 15.565  -14.962 0.50 57.32  ? 109 HOH   A O   1 
HETATM 1927 O O   C HOH   H 6 .   ? -24.958 12.349  -23.727 0.50 57.82  ? 110 HOH   A O   1 
HETATM 1928 O O   D HOH   H 6 .   ? -24.958 12.349  -23.727 0.50 57.82  ? 110 HOH   A O   1 
HETATM 1929 O O   . HOH   H 6 .   ? -30.534 0.360   -23.012 1.00 51.49  ? 111 HOH   A O   1 
HETATM 1930 O O   A HOH   H 6 .   ? -26.226 -3.640  -35.334 0.50 64.64  ? 112 HOH   A O   1 
HETATM 1931 O O   B HOH   H 6 .   ? -26.226 -3.640  -35.334 0.50 64.64  ? 112 HOH   A O   1 
HETATM 1932 O O   . HOH   H 6 .   ? -4.278  -14.710 -25.369 1.00 54.37  ? 113 HOH   A O   1 
HETATM 1933 O O   A HOH   H 6 .   ? -30.857 -0.317  -28.799 0.50 73.86  ? 114 HOH   A O   1 
HETATM 1934 O O   B HOH   H 6 .   ? -30.857 -0.317  -28.799 0.50 73.86  ? 114 HOH   A O   1 
HETATM 1935 O O   A HOH   H 6 .   ? -3.152  -3.641  0.034   0.50 76.87  ? 115 HOH   A O   1 
HETATM 1936 O O   B HOH   H 6 .   ? -3.152  -3.641  0.034   0.50 76.87  ? 115 HOH   A O   1 
HETATM 1937 O O   A HOH   H 6 .   ? -4.493  -10.129 -5.579  0.50 60.16  ? 116 HOH   A O   1 
HETATM 1938 O O   B HOH   H 6 .   ? -4.493  -10.129 -5.579  0.50 60.16  ? 116 HOH   A O   1 
HETATM 1939 O O   . HOH   H 6 .   ? -30.644 12.593  -16.601 1.00 57.12  ? 117 HOH   A O   1 
HETATM 1940 O O   A HOH   H 6 .   ? -22.328 -9.064  -34.892 0.50 84.06  ? 118 HOH   A O   1 
HETATM 1941 O O   B HOH   H 6 .   ? -22.328 -9.064  -34.892 0.50 84.06  ? 118 HOH   A O   1 
HETATM 1942 O O   C HOH   H 6 .   ? -26.384 1.919   -28.826 0.50 68.60  ? 119 HOH   A O   1 
HETATM 1943 O O   D HOH   H 6 .   ? -26.384 1.919   -28.826 0.50 68.60  ? 119 HOH   A O   1 
HETATM 1944 O O   . HOH   H 6 .   ? -2.675  -8.801  -3.378  1.00 61.48  ? 120 HOH   A O   1 
HETATM 1945 O O   A HOH   H 6 .   ? -8.819  2.934   -9.181  0.07 15.37  ? 121 HOH   A O   1 
HETATM 1946 O O   B HOH   H 6 .   ? -8.819  2.934   -9.181  0.07 15.37  ? 121 HOH   A O   1 
HETATM 1947 O O   . HOH   H 6 .   ? -3.532  -0.886  -0.299  1.00 62.70  ? 122 HOH   A O   1 
HETATM 1948 O O   C HOH   H 6 .   ? -22.016 -0.778  -34.805 0.50 65.38  ? 123 HOH   A O   1 
HETATM 1949 O O   D HOH   H 6 .   ? -22.016 -0.778  -34.805 0.50 65.38  ? 123 HOH   A O   1 
HETATM 1950 O O   A HOH   H 6 .   ? 5.021   -5.090  -15.132 0.50 111.10 ? 124 HOH   A O   1 
HETATM 1951 O O   B HOH   H 6 .   ? 5.021   -5.090  -15.132 0.50 111.10 ? 124 HOH   A O   1 
HETATM 1952 O O   . HOH   I 6 .   ? -33.922 1.607   -15.424 1.00 52.90  ? 301 HOH   B O   1 
HETATM 1953 O O   A HOH   I 6 .   ? -22.727 10.211  -25.984 0.50 81.03  ? 302 HOH   B O   1 
HETATM 1954 O O   B HOH   I 6 .   ? -22.727 10.211  -25.984 0.50 81.03  ? 302 HOH   B O   1 
HETATM 1955 O O   . HOH   I 6 .   ? -30.454 12.615  -19.369 1.00 48.81  ? 303 HOH   B O   1 
HETATM 1956 O O   . HOH   I 6 .   ? -17.081 12.633  -5.516  1.00 50.12  ? 304 HOH   B O   1 
HETATM 1957 O O   A HOH   I 6 .   ? -15.577 -10.099 -15.179 0.50 67.18  ? 305 HOH   B O   1 
HETATM 1958 O O   B HOH   I 6 .   ? -15.577 -10.099 -15.179 0.50 67.18  ? 305 HOH   B O   1 
HETATM 1959 O O   A HOH   I 6 .   ? -34.093 0.328   -3.770  0.50 58.87  ? 306 HOH   B O   1 
HETATM 1960 O O   B HOH   I 6 .   ? -34.093 0.328   -3.770  0.50 58.87  ? 306 HOH   B O   1 
HETATM 1961 O O   . HOH   I 6 .   ? -25.895 -8.142  -16.799 1.00 44.10  ? 307 HOH   B O   1 
HETATM 1962 O O   C HOH   I 6 .   ? -20.612 14.190  1.624   0.50 69.06  ? 308 HOH   B O   1 
HETATM 1963 O O   D HOH   I 6 .   ? -20.612 14.190  1.624   0.50 69.06  ? 308 HOH   B O   1 
HETATM 1964 O O   . HOH   I 6 .   ? -15.856 25.772  -13.116 1.00 72.95  ? 309 HOH   B O   1 
HETATM 1965 O O   A HOH   I 6 .   ? -4.864  2.650   -10.115 0.07 17.87  ? 310 HOH   B O   1 
HETATM 1966 O O   B HOH   I 6 .   ? -4.864  2.650   -10.115 0.07 17.87  ? 310 HOH   B O   1 
HETATM 1967 O O   . HOH   I 6 .   ? -6.294  -0.373  -10.933 1.00 52.29  ? 311 HOH   B O   1 
HETATM 1968 O O   A HOH   I 6 .   ? -16.058 20.464  -14.206 0.50 57.46  ? 312 HOH   B O   1 
HETATM 1969 O O   B HOH   I 6 .   ? -16.058 20.464  -14.206 0.50 57.46  ? 312 HOH   B O   1 
HETATM 1970 O O   . HOH   I 6 .   ? -14.596 -6.711  -1.355  1.00 58.14  ? 313 HOH   B O   1 
HETATM 1971 O O   . HOH   I 6 .   ? -15.504 9.340   -0.636  1.00 56.17  ? 314 HOH   B O   1 
HETATM 1972 O O   . HOH   I 6 .   ? -17.773 -10.768 -16.553 1.00 47.40  ? 315 HOH   B O   1 
HETATM 1973 O O   A HOH   I 6 .   ? -28.392 -7.699  -5.948  0.50 60.21  ? 316 HOH   B O   1 
HETATM 1974 O O   B HOH   I 6 .   ? -28.392 -7.699  -5.948  0.50 60.21  ? 316 HOH   B O   1 
HETATM 1975 O O   . HOH   I 6 .   ? -16.286 -7.439  -8.208  1.00 58.04  ? 317 HOH   B O   1 
HETATM 1976 O O   . HOH   I 6 .   ? -23.629 -6.853  -4.542  1.00 51.89  ? 318 HOH   B O   1 
HETATM 1977 O O   . HOH   I 6 .   ? -10.521 11.559  -19.070 1.00 55.34  ? 319 HOH   B O   1 
HETATM 1978 O O   A HOH   I 6 .   ? -18.207 -20.791 -21.876 0.50 76.41  ? 320 HOH   B O   1 
HETATM 1979 O O   B HOH   I 6 .   ? -18.207 -20.791 -21.876 0.50 76.41  ? 320 HOH   B O   1 
HETATM 1980 O O   . HOH   I 6 .   ? -12.939 -2.355  -14.805 1.00 46.61  ? 321 HOH   B O   1 
HETATM 1981 O O   C HOH   I 6 .   ? -21.853 14.881  -6.180  0.50 56.96  ? 322 HOH   B O   1 
HETATM 1982 O O   D HOH   I 6 .   ? -21.853 14.881  -6.180  0.50 56.96  ? 322 HOH   B O   1 
HETATM 1983 O O   . HOH   I 6 .   ? -9.333  -6.914  -25.545 1.00 58.31  ? 323 HOH   B O   1 
HETATM 1984 O O   . HOH   I 6 .   ? -6.918  -9.103  -3.138  1.00 51.38  ? 324 HOH   B O   1 
HETATM 1985 O O   . HOH   I 6 .   ? -12.220 -3.508  -10.178 1.00 45.12  ? 325 HOH   B O   1 
HETATM 1986 O O   . HOH   I 6 .   ? -31.534 7.083   -4.482  1.00 69.52  ? 326 HOH   B O   1 
HETATM 1987 O O   A HOH   I 6 .   ? -28.683 -4.031  -22.488 0.50 62.29  ? 327 HOH   B O   1 
HETATM 1988 O O   B HOH   I 6 .   ? -28.683 -4.031  -22.488 0.50 62.29  ? 327 HOH   B O   1 
HETATM 1989 O O   A HOH   I 6 .   ? -20.522 -8.021  -5.224  0.50 73.75  ? 328 HOH   B O   1 
HETATM 1990 O O   B HOH   I 6 .   ? -20.522 -8.021  -5.224  0.50 73.75  ? 328 HOH   B O   1 
HETATM 1991 O O   . HOH   I 6 .   ? -30.519 4.673   -2.602  1.00 60.73  ? 329 HOH   B O   1 
HETATM 1992 O O   A HOH   I 6 .   ? -21.578 -14.198 -21.681 0.50 65.20  ? 330 HOH   B O   1 
HETATM 1993 O O   B HOH   I 6 .   ? -21.578 -14.198 -21.681 0.50 65.20  ? 330 HOH   B O   1 
HETATM 1994 O O   . HOH   I 6 .   ? -8.523  -10.972 -7.514  1.00 64.54  ? 331 HOH   B O   1 
HETATM 1995 O O   . HOH   I 6 .   ? -11.960 2.075   -5.730  1.00 51.23  ? 332 HOH   B O   1 
HETATM 1996 O O   A HOH   I 6 .   ? -19.846 -12.504 -25.452 0.50 56.75  ? 333 HOH   B O   1 
HETATM 1997 O O   B HOH   I 6 .   ? -19.846 -12.504 -25.452 0.50 56.75  ? 333 HOH   B O   1 
HETATM 1998 O O   . HOH   I 6 .   ? -14.244 -12.174 -16.538 1.00 48.80  ? 334 HOH   B O   1 
HETATM 1999 O O   A HOH   I 6 .   ? -0.661  0.564   -13.776 0.07 22.05  ? 335 HOH   B O   1 
HETATM 2000 O O   B HOH   I 6 .   ? -0.661  0.564   -13.776 0.07 22.05  ? 335 HOH   B O   1 
HETATM 2001 O O   A HOH   I 6 .   ? -35.315 3.476   -8.679  0.50 71.07  ? 336 HOH   B O   1 
HETATM 2002 O O   B HOH   I 6 .   ? -35.315 3.476   -8.679  0.50 71.07  ? 336 HOH   B O   1 
HETATM 2003 O O   A HOH   I 6 .   ? -10.858 7.322   -14.277 0.07 11.39  ? 337 HOH   B O   1 
HETATM 2004 O O   B HOH   I 6 .   ? -10.858 7.322   -14.277 0.07 11.39  ? 337 HOH   B O   1 
HETATM 2005 O O   A HOH   I 6 .   ? -21.387 -12.076 -13.081 0.50 71.50  ? 338 HOH   B O   1 
HETATM 2006 O O   B HOH   I 6 .   ? -21.387 -12.076 -13.081 0.50 71.50  ? 338 HOH   B O   1 
HETATM 2007 O O   A HOH   I 6 .   ? -21.127 6.923   0.000   0.50 108.29 ? 339 HOH   B O   1 
HETATM 2008 O O   B HOH   I 6 .   ? -21.127 6.923   0.000   0.50 108.29 ? 339 HOH   B O   1 
HETATM 2009 O O   . HOH   I 6 .   ? -35.053 1.221   -7.329  1.00 60.69  ? 340 HOH   B O   1 
HETATM 2010 O O   A HOH   I 6 .   ? -16.270 -14.346 -30.789 0.50 71.47  ? 341 HOH   B O   1 
HETATM 2011 O O   B HOH   I 6 .   ? -16.270 -14.346 -30.789 0.50 71.47  ? 341 HOH   B O   1 
HETATM 2012 O O   . HOH   I 6 .   ? -29.535 -1.330  -19.005 1.00 54.93  ? 342 HOH   B O   1 
HETATM 2013 O O   C HOH   I 6 .   ? -20.767 13.963  -33.371 0.50 58.80  ? 343 HOH   B O   1 
HETATM 2014 O O   D HOH   I 6 .   ? -20.767 13.963  -33.371 0.50 58.80  ? 343 HOH   B O   1 
HETATM 2015 O O   . HOH   I 6 .   ? -27.762 -6.457  -18.541 1.00 53.35  ? 344 HOH   B O   1 
HETATM 2016 O O   . HOH   I 6 .   ? -2.659  -11.657 -7.026  1.00 50.67  ? 345 HOH   B O   1 
HETATM 2017 O O   A HOH   I 6 .   ? -20.530 6.604   -32.577 0.50 77.25  ? 346 HOH   B O   1 
HETATM 2018 O O   B HOH   I 6 .   ? -20.530 6.604   -32.577 0.50 77.25  ? 346 HOH   B O   1 
HETATM 2019 O O   A HOH   I 6 .   ? -14.644 16.436  -19.948 0.50 62.13  ? 347 HOH   B O   1 
HETATM 2020 O O   B HOH   I 6 .   ? -14.644 16.436  -19.948 0.50 62.13  ? 347 HOH   B O   1 
HETATM 2021 O O   A HOH   I 6 .   ? -18.142 25.148  -14.188 0.50 68.65  ? 348 HOH   B O   1 
HETATM 2022 O O   B HOH   I 6 .   ? -18.142 25.148  -14.188 0.50 68.65  ? 348 HOH   B O   1 
HETATM 2023 O O   C HOH   I 6 .   ? -6.977  10.080  -19.409 0.43 55.33  ? 349 HOH   B O   1 
HETATM 2024 O O   D HOH   I 6 .   ? -6.977  10.080  -19.409 0.43 55.33  ? 349 HOH   B O   1 
HETATM 2025 O O   . HOH   I 6 .   ? -18.572 14.874  -22.089 1.00 45.64  ? 350 HOH   B O   1 
HETATM 2026 O O   A HOH   I 6 .   ? -6.939  -6.261  -0.004  0.50 92.62  ? 351 HOH   B O   1 
HETATM 2027 O O   B HOH   I 6 .   ? -6.939  -6.261  -0.004  0.50 92.62  ? 351 HOH   B O   1 
HETATM 2028 O O   . HOH   I 6 .   ? -19.310 -5.910  -0.742  1.00 48.07  ? 352 HOH   B O   1 
HETATM 2029 O O   . HOH   I 6 .   ? -9.353  6.572   -6.585  1.00 66.16  ? 353 HOH   B O   1 
HETATM 2030 O O   A HOH   I 6 .   ? -15.688 -14.635 -16.630 0.50 67.22  ? 354 HOH   B O   1 
HETATM 2031 O O   B HOH   I 6 .   ? -15.688 -14.635 -16.630 0.50 67.22  ? 354 HOH   B O   1 
HETATM 2032 O O   . HOH   I 6 .   ? -14.989 -4.888  1.370   1.00 43.58  ? 355 HOH   B O   1 
HETATM 2033 O O   A HOH   I 6 .   ? -20.198 24.313  -16.937 0.50 74.09  ? 356 HOH   B O   1 
HETATM 2034 O O   B HOH   I 6 .   ? -20.198 24.313  -16.937 0.50 74.09  ? 356 HOH   B O   1 
HETATM 2035 O O   C HOH   I 6 .   ? -14.864 -8.759  -11.817 0.50 65.67  ? 357 HOH   B O   1 
HETATM 2036 O O   D HOH   I 6 .   ? -14.864 -8.759  -11.817 0.50 65.67  ? 357 HOH   B O   1 
HETATM 2037 O O   C HOH   I 6 .   ? -0.839  5.690   -26.126 0.50 64.96  ? 358 HOH   B O   1 
HETATM 2038 O O   D HOH   I 6 .   ? -0.839  5.690   -26.126 0.50 64.96  ? 358 HOH   B O   1 
HETATM 2039 O O   . HOH   I 6 .   ? -17.158 14.297  -30.966 1.00 52.92  ? 359 HOH   B O   1 
HETATM 2040 O O   . HOH   I 6 .   ? -25.572 -5.072  -4.033  1.00 48.61  ? 360 HOH   B O   1 
HETATM 2041 O O   A HOH   I 6 .   ? -19.410 -13.430 -22.883 0.50 46.51  ? 361 HOH   B O   1 
HETATM 2042 O O   B HOH   I 6 .   ? -19.410 -13.430 -22.883 0.50 46.51  ? 361 HOH   B O   1 
HETATM 2043 O O   . HOH   I 6 .   ? -11.404 -5.297  -8.326  1.00 52.12  ? 362 HOH   B O   1 
HETATM 2044 O O   C HOH   I 6 .   ? -21.735 -14.049 -25.712 0.50 53.20  ? 363 HOH   B O   1 
HETATM 2045 O O   D HOH   I 6 .   ? -21.735 -14.049 -25.712 0.50 53.20  ? 363 HOH   B O   1 
HETATM 2046 O O   . HOH   I 6 .   ? -16.684 16.115  -21.737 1.00 55.61  ? 364 HOH   B O   1 
HETATM 2047 O O   C HOH   I 6 .   ? -32.396 13.049  -1.108  0.50 67.71  ? 365 HOH   B O   1 
HETATM 2048 O O   D HOH   I 6 .   ? -32.396 13.049  -1.108  0.50 67.71  ? 365 HOH   B O   1 
HETATM 2049 O O   A HOH   I 6 .   ? -30.390 -8.737  -4.197  0.50 92.24  ? 366 HOH   B O   1 
HETATM 2050 O O   B HOH   I 6 .   ? -30.390 -8.737  -4.197  0.50 92.24  ? 366 HOH   B O   1 
HETATM 2051 O O   . HOH   I 6 .   ? -6.627  -11.098 -5.377  1.00 51.44  ? 367 HOH   B O   1 
HETATM 2052 O O   C HOH   I 6 .   ? -9.718  -16.016 -24.154 0.50 55.22  ? 368 HOH   B O   1 
HETATM 2053 O O   D HOH   I 6 .   ? -9.718  -16.016 -24.154 0.50 55.22  ? 368 HOH   B O   1 
HETATM 2054 O O   A HOH   I 6 .   ? -24.441 -15.241 -17.378 0.50 73.18  ? 369 HOH   B O   1 
HETATM 2055 O O   B HOH   I 6 .   ? -24.441 -15.241 -17.378 0.50 73.18  ? 369 HOH   B O   1 
HETATM 2056 O O   . HOH   I 6 .   ? -1.267  -14.978 -10.088 1.00 64.12  ? 370 HOH   B O   1 
HETATM 2057 O O   A HOH   I 6 .   ? -31.341 -10.913 -27.064 0.25 80.40  ? 371 HOH   B O   1 
HETATM 2058 O O   B HOH   I 6 .   ? -31.341 -10.913 -27.064 0.25 80.40  ? 371 HOH   B O   1 
HETATM 2059 O O   A HOH   I 6 .   ? -9.976  21.492  -14.477 0.50 71.27  ? 372 HOH   B O   1 
HETATM 2060 O O   B HOH   I 6 .   ? -9.976  21.492  -14.477 0.50 71.27  ? 372 HOH   B O   1 
HETATM 2061 O O   A HOH   I 6 .   ? -30.826 -7.505  -6.652  0.50 64.90  ? 373 HOH   B O   1 
HETATM 2062 O O   B HOH   I 6 .   ? -30.826 -7.505  -6.652  0.50 64.90  ? 373 HOH   B O   1 
HETATM 2063 O O   . HOH   I 6 .   ? -11.788 12.655  -14.620 1.00 69.82  ? 374 HOH   B O   1 
HETATM 2064 O O   . HOH   I 6 .   ? -29.279 -6.154  -1.005  1.00 55.27  ? 375 HOH   B O   1 
HETATM 2065 O O   A HOH   I 6 .   ? -12.458 -9.356  0.080   0.50 74.73  ? 376 HOH   B O   1 
HETATM 2066 O O   B HOH   I 6 .   ? -12.458 -9.356  0.080   0.50 74.73  ? 376 HOH   B O   1 
HETATM 2067 O O   A HOH   I 6 .   ? -19.060 -11.769 -12.873 0.50 77.49  ? 377 HOH   B O   1 
HETATM 2068 O O   B HOH   I 6 .   ? -19.060 -11.769 -12.873 0.50 77.49  ? 377 HOH   B O   1 
HETATM 2069 O O   A HOH   I 6 .   ? -20.135 3.953   0.010   0.50 65.81  ? 378 HOH   B O   1 
HETATM 2070 O O   B HOH   I 6 .   ? -20.135 3.953   0.010   0.50 65.81  ? 378 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   ? 0.9364 0.8257 0.9556 0.0671 0.0847  -0.0545 50  ASP A N   
2    C CA  . ASP A 7   ? 0.9228 0.8246 0.9260 0.0735 0.0854  -0.0550 50  ASP A CA  
3    C C   . ASP A 7   ? 0.8568 0.7647 0.8551 0.0802 0.0849  -0.0356 50  ASP A C   
4    O O   . ASP A 7   ? 0.9008 0.8004 0.9116 0.0875 0.0871  -0.0236 50  ASP A O   
5    C CB  . ASP A 7   ? 0.9486 0.8465 0.9609 0.0806 0.0893  -0.0646 50  ASP A CB  
6    C CG  . ASP A 7   ? 1.0105 0.9199 1.0089 0.0797 0.0909  -0.0787 50  ASP A CG  
7    O OD1 . ASP A 7   ? 1.0713 0.9758 1.0777 0.0817 0.0949  -0.0923 50  ASP A OD1 
8    O OD2 . ASP A 7   ? 1.0641 0.9868 1.0445 0.0773 0.0891  -0.0758 50  ASP A OD2 
9    N N   . MET A 8   ? 0.7643 0.6848 0.7441 0.0778 0.0819  -0.0327 51  MET A N   
10   C CA  . MET A 8   ? 0.7238 0.6514 0.6943 0.0844 0.0806  -0.0172 51  MET A CA  
11   C C   . MET A 8   ? 0.6636 0.5967 0.6315 0.0938 0.0803  -0.0177 51  MET A C   
12   O O   . MET A 8   ? 0.6604 0.5968 0.6291 0.0923 0.0812  -0.0308 51  MET A O   
13   C CB  . MET A 8   ? 0.7201 0.6584 0.6728 0.0785 0.0770  -0.0165 51  MET A CB  
14   C CG  . MET A 8   ? 0.7340 0.6692 0.6917 0.0697 0.0759  -0.0168 51  MET A CG  
15   S SD  . MET A 8   ? 0.7608 0.7083 0.6989 0.0650 0.0710  -0.0148 51  MET A SD  
16   C CE  . MET A 8   ? 0.7471 0.6911 0.7007 0.0575 0.0701  -0.0112 51  MET A CE  
17   N N   . TYR A 9   ? 0.6308 0.5652 0.5957 0.1034 0.0790  -0.0038 52  TYR A N   
18   C CA  . TYR A 9   ? 0.5979 0.5388 0.5610 0.1136 0.0762  -0.0028 52  TYR A CA  
19   C C   . TYR A 9   ? 0.5934 0.5405 0.5406 0.1198 0.0721  0.0096  52  TYR A C   
20   O O   . TYR A 9   ? 0.5830 0.5266 0.5243 0.1187 0.0737  0.0201  52  TYR A O   
21   C CB  . TYR A 9   ? 0.6049 0.5358 0.5855 0.1228 0.0780  -0.0001 52  TYR A CB  
22   C CG  . TYR A 9   ? 0.6066 0.5248 0.5919 0.1282 0.0802  0.0163  52  TYR A CG  
23   C CD1 . TYR A 9   ? 0.6139 0.5197 0.6110 0.1211 0.0851  0.0175  52  TYR A CD1 
24   C CD2 . TYR A 9   ? 0.6273 0.5455 0.6049 0.1404 0.0774  0.0310  52  TYR A CD2 
25   C CE1 . TYR A 9   ? 0.6367 0.5306 0.6400 0.1251 0.0888  0.0341  52  TYR A CE1 
26   C CE2 . TYR A 9   ? 0.6322 0.5380 0.6118 0.1457 0.0811  0.0479  52  TYR A CE2 
27   C CZ  . TYR A 9   ? 0.6439 0.5376 0.6374 0.1376 0.0877  0.0501  52  TYR A CZ  
28   O OH  . TYR A 9   ? 0.6773 0.5586 0.6748 0.1415 0.0931  0.0680  52  TYR A OH  
29   N N   . ILE A 10  ? 0.6077 0.5646 0.5495 0.1260 0.0671  0.0074  53  ILE A N   
30   C CA  . ILE A 10  ? 0.5999 0.5636 0.5248 0.1326 0.0613  0.0158  53  ILE A CA  
31   C C   . ILE A 10  ? 0.6194 0.5813 0.5462 0.1471 0.0570  0.0242  53  ILE A C   
32   O O   . ILE A 10  ? 0.6163 0.5783 0.5586 0.1514 0.0561  0.0185  53  ILE A O   
33   C CB  . ILE A 10  ? 0.5939 0.5701 0.5098 0.1270 0.0571  0.0058  53  ILE A CB  
34   C CG1 . ILE A 10  ? 0.5916 0.5758 0.5199 0.1273 0.0556  -0.0058 53  ILE A CG1 
35   C CG2 . ILE A 10  ? 0.6017 0.5781 0.5110 0.1144 0.0603  0.0008  53  ILE A CG2 
36   C CD1 . ILE A 10  ? 0.5924 0.5884 0.5127 0.1241 0.0507  -0.0116 53  ILE A CD1 
37   N N   . GLU A 11  ? 0.6454 0.6054 0.5565 0.1552 0.0547  0.0373  54  GLU A N   
38   C CA  . GLU A 11  ? 0.6564 0.6152 0.5606 0.1707 0.0484  0.0469  54  GLU A CA  
39   C C   . GLU A 11  ? 0.6393 0.6070 0.5216 0.1749 0.0409  0.0477  54  GLU A C   
40   O O   . GLU A 11  ? 0.5922 0.5600 0.4608 0.1701 0.0443  0.0511  54  GLU A O   
41   C CB  . GLU A 11  ? 0.7088 0.6537 0.6101 0.1783 0.0540  0.0643  54  GLU A CB  
42   C CG  . GLU A 11  ? 0.7567 0.6891 0.6794 0.1739 0.0620  0.0656  54  GLU A CG  
43   C CD  . GLU A 11  ? 0.8491 0.7664 0.7708 0.1802 0.0688  0.0845  54  GLU A CD  
44   O OE1 . GLU A 11  ? 0.8968 0.8136 0.8014 0.1822 0.0722  0.0964  54  GLU A OE1 
45   O OE2 . GLU A 11  ? 0.9438 0.8492 0.8827 0.1832 0.0716  0.0876  54  GLU A OE2 
46   N N   . ARG A 12  ? 0.6450 0.6208 0.5260 0.1830 0.0306  0.0430  55  ARG A N   
47   C CA  . ARG A 12  ? 0.6530 0.6360 0.5136 0.1881 0.0216  0.0422  55  ARG A CA  
48   C C   . ARG A 12  ? 0.6644 0.6389 0.5023 0.1982 0.0236  0.0580  55  ARG A C   
49   O O   . ARG A 12  ? 0.6850 0.6498 0.5250 0.2065 0.0272  0.0700  55  ARG A O   
50   C CB  . ARG A 12  ? 0.6680 0.6604 0.5347 0.1965 0.0089  0.0351  55  ARG A CB  
51   C CG  . ARG A 12  ? 0.6963 0.6973 0.5477 0.1983 -0.0016 0.0290  55  ARG A CG  
52   C CD  . ARG A 12  ? 0.7239 0.7380 0.5927 0.1992 -0.0128 0.0162  55  ARG A CD  
53   N NE  . ARG A 12  ? 0.7504 0.7720 0.6095 0.1968 -0.0217 0.0079  55  ARG A NE  
54   C CZ  . ARG A 12  ? 0.7897 0.8097 0.6253 0.2075 -0.0315 0.0112  55  ARG A CZ  
55   N NH1 . ARG A 12  ? 0.8426 0.8547 0.6609 0.2216 -0.0331 0.0236  55  ARG A NH1 
56   N NH2 . ARG A 12  ? 0.7727 0.7979 0.6009 0.2043 -0.0395 0.0021  55  ARG A NH2 
57   N N   . ALA A 13  ? 0.6781 0.6551 0.4961 0.1974 0.0229  0.0585  56  ALA A N   
58   C CA  . ALA A 13  ? 0.6817 0.6523 0.4752 0.2070 0.0265  0.0725  56  ALA A CA  
59   C C   . ALA A 13  ? 0.6958 0.6719 0.4652 0.2162 0.0153  0.0686  56  ALA A C   
60   O O   . ALA A 13  ? 0.7250 0.6963 0.4703 0.2262 0.0181  0.0795  56  ALA A O   
61   C CB  . ALA A 13  ? 0.6884 0.6553 0.4821 0.1977 0.0392  0.0781  56  ALA A CB  
62   N N   . GLY A 14  ? 0.6613 0.6467 0.4360 0.2137 0.0036  0.0540  57  GLY A N   
63   C CA  . GLY A 14  ? 0.6680 0.6572 0.4213 0.2243 -0.0093 0.0497  57  GLY A CA  
64   C C   . GLY A 14  ? 0.6792 0.6780 0.4420 0.2158 -0.0189 0.0326  57  GLY A C   
65   O O   . GLY A 14  ? 0.6219 0.6245 0.4074 0.2013 -0.0135 0.0256  57  GLY A O   
66   N N   . ASP A 15  ? 0.6826 0.6847 0.4291 0.2243 -0.0323 0.0261  58  ASP A N   
67   C CA  . ASP A 15  ? 0.7124 0.7217 0.4655 0.2164 -0.0418 0.0104  58  ASP A CA  
68   C C   . ASP A 15  ? 0.7583 0.7628 0.4971 0.2104 -0.0347 0.0103  58  ASP A C   
69   O O   . ASP A 15  ? 0.8033 0.8009 0.5234 0.2160 -0.0255 0.0215  58  ASP A O   
70   C CB  . ASP A 15  ? 0.7120 0.7260 0.4558 0.2272 -0.0605 0.0015  58  ASP A CB  
71   C CG  . ASP A 15  ? 0.7430 0.7645 0.5057 0.2327 -0.0703 -0.0008 58  ASP A CG  
72   O OD1 . ASP A 15  ? 0.7207 0.7422 0.5013 0.2289 -0.0611 0.0049  58  ASP A OD1 
73   O OD2 . ASP A 15  ? 0.7662 0.7930 0.5245 0.2423 -0.0876 -0.0084 58  ASP A OD2 
74   N N   . ILE A 16  ? 0.7761 0.7843 0.5256 0.1991 -0.0381 -0.0013 59  ILE A N   
75   C CA  . ILE A 16  ? 0.7983 0.8018 0.5355 0.1940 -0.0340 -0.0031 59  ILE A CA  
76   C C   . ILE A 16  ? 0.8008 0.8040 0.5229 0.2019 -0.0486 -0.0131 59  ILE A C   
77   O O   . ILE A 16  ? 0.7846 0.7926 0.5215 0.1956 -0.0588 -0.0253 59  ILE A O   
78   C CB  . ILE A 16  ? 0.8105 0.8156 0.5678 0.1767 -0.0265 -0.0071 59  ILE A CB  
79   C CG1 . ILE A 16  ? 0.8234 0.8268 0.5894 0.1717 -0.0127 0.0028  59  ILE A CG1 
80   C CG2 . ILE A 16  ? 0.8300 0.8305 0.5775 0.1718 -0.0260 -0.0109 59  ILE A CG2 
81   C CD1 . ILE A 16  ? 0.8170 0.8225 0.6024 0.1558 -0.0064 -0.0017 59  ILE A CD1 
82   N N   A THR A 17  ? 0.8163 0.8139 0.5096 0.2156 -0.0492 -0.0079 60  THR A N   
83   N N   B THR A 17  ? 0.8140 0.8117 0.5075 0.2156 -0.0496 -0.0082 60  THR A N   
84   N N   C THR A 17  ? 0.8163 0.8139 0.5096 0.2156 -0.0492 -0.0079 60  THR A N   
85   N N   D THR A 17  ? 0.8140 0.8117 0.5075 0.2156 -0.0496 -0.0082 60  THR A N   
86   C CA  A THR A 17  ? 0.8346 0.8302 0.5061 0.2274 -0.0636 -0.0168 60  THR A CA  
87   C CA  B THR A 17  ? 0.8292 0.8251 0.5028 0.2261 -0.0643 -0.0182 60  THR A CA  
88   C CA  C THR A 17  ? 0.8346 0.8302 0.5061 0.2274 -0.0636 -0.0168 60  THR A CA  
89   C CA  D THR A 17  ? 0.8292 0.8251 0.5028 0.2261 -0.0643 -0.0182 60  THR A CA  
90   C C   A THR A 17  ? 0.8443 0.8321 0.4876 0.2350 -0.0565 -0.0125 60  THR A C   
91   C C   B THR A 17  ? 0.8443 0.8323 0.4872 0.2358 -0.0577 -0.0129 60  THR A C   
92   C C   C THR A 17  ? 0.8443 0.8321 0.4876 0.2350 -0.0565 -0.0125 60  THR A C   
93   C C   D THR A 17  ? 0.8443 0.8323 0.4872 0.2358 -0.0577 -0.0129 60  THR A C   
94   O O   A THR A 17  ? 0.8415 0.8267 0.4748 0.2394 -0.0423 0.0018  60  THR A O   
95   O O   B THR A 17  ? 0.8455 0.8310 0.4766 0.2420 -0.0446 0.0018  60  THR A O   
96   O O   C THR A 17  ? 0.8415 0.8267 0.4748 0.2394 -0.0423 0.0018  60  THR A O   
97   O O   D THR A 17  ? 0.8455 0.8310 0.4766 0.2420 -0.0446 0.0018  60  THR A O   
98   C CB  A THR A 17  ? 0.8554 0.8533 0.5158 0.2424 -0.0743 -0.0147 60  THR A CB  
99   C CB  B THR A 17  ? 0.8432 0.8434 0.5129 0.2382 -0.0781 -0.0200 60  THR A CB  
100  C CB  C THR A 17  ? 0.8554 0.8533 0.5158 0.2424 -0.0743 -0.0147 60  THR A CB  
101  C CB  D THR A 17  ? 0.8432 0.8434 0.5129 0.2382 -0.0781 -0.0200 60  THR A CB  
102  O OG1 A THR A 17  ? 0.8595 0.8522 0.4998 0.2528 -0.0628 0.0016  60  THR A OG1 
103  O OG1 B THR A 17  ? 0.8173 0.8261 0.5161 0.2291 -0.0891 -0.0322 60  THR A OG1 
104  O OG1 C THR A 17  ? 0.8595 0.8522 0.4998 0.2528 -0.0628 0.0016  60  THR A OG1 
105  O OG1 D THR A 17  ? 0.8173 0.8261 0.5161 0.2291 -0.0891 -0.0322 60  THR A OG1 
106  C CG2 A THR A 17  ? 0.8387 0.8455 0.5288 0.2369 -0.0805 -0.0178 60  THR A CG2 
107  C CG2 B THR A 17  ? 0.8656 0.8613 0.5019 0.2551 -0.0897 -0.0241 60  THR A CG2 
108  C CG2 C THR A 17  ? 0.8387 0.8455 0.5288 0.2369 -0.0805 -0.0178 60  THR A CG2 
109  C CG2 D THR A 17  ? 0.8656 0.8613 0.5019 0.2551 -0.0897 -0.0241 60  THR A CG2 
110  N N   . TRP A 18  ? 0.8542 0.8384 0.4868 0.2369 -0.0656 -0.0247 61  TRP A N   
111  C CA  . TRP A 18  ? 0.9362 0.9133 0.5383 0.2483 -0.0612 -0.0229 61  TRP A CA  
112  C C   . TRP A 18  ? 1.0089 0.9849 0.5818 0.2674 -0.0674 -0.0192 61  TRP A C   
113  O O   . TRP A 18  ? 0.9966 0.9755 0.5705 0.2718 -0.0839 -0.0279 61  TRP A O   
114  C CB  . TRP A 18  ? 0.9432 0.9155 0.5441 0.2451 -0.0707 -0.0385 61  TRP A CB  
115  C CG  . TRP A 18  ? 1.0155 0.9804 0.5868 0.2573 -0.0667 -0.0392 61  TRP A CG  
116  C CD1 . TRP A 18  ? 1.0442 1.0051 0.5841 0.2745 -0.0758 -0.0452 61  TRP A CD1 
117  C CD2 . TRP A 18  ? 1.0286 0.9899 0.5990 0.2541 -0.0532 -0.0349 61  TRP A CD2 
118  N NE1 . TRP A 18  ? 1.0807 1.0355 0.5998 0.2823 -0.0672 -0.0449 61  TRP A NE1 
119  C CE2 . TRP A 18  ? 1.0566 1.0119 0.5953 0.2701 -0.0537 -0.0388 61  TRP A CE2 
120  C CE3 . TRP A 18  ? 0.9883 0.9508 0.5808 0.2401 -0.0417 -0.0288 61  TRP A CE3 
121  C CZ2 . TRP A 18  ? 1.0724 1.0240 0.6040 0.2726 -0.0421 -0.0365 61  TRP A CZ2 
122  C CZ3 . TRP A 18  ? 0.9921 0.9512 0.5775 0.2425 -0.0317 -0.0261 61  TRP A CZ3 
123  C CH2 . TRP A 18  ? 1.0461 1.0002 0.6030 0.2584 -0.0315 -0.0298 61  TRP A CH2 
124  N N   A GLU A 19  ? 1.0430 1.0154 0.5915 0.2784 -0.0542 -0.0062 62  GLU A N   
125  N N   B GLU A 19  ? 1.0430 1.0154 0.5915 0.2784 -0.0542 -0.0062 62  GLU A N   
126  N N   C GLU A 19  ? 1.0405 1.0129 0.5893 0.2783 -0.0541 -0.0060 62  GLU A N   
127  N N   D GLU A 19  ? 1.0405 1.0129 0.5893 0.2783 -0.0541 -0.0060 62  GLU A N   
128  C CA  A GLU A 19  ? 1.1058 1.0755 0.6213 0.2978 -0.0568 0.0009  62  GLU A CA  
129  C CA  B GLU A 19  ? 1.1058 1.0755 0.6213 0.2978 -0.0568 0.0009  62  GLU A CA  
130  C CA  C GLU A 19  ? 1.1029 1.0725 0.6175 0.2980 -0.0567 0.0006  62  GLU A CA  
131  C CA  D GLU A 19  ? 1.1029 1.0725 0.6175 0.2980 -0.0567 0.0006  62  GLU A CA  
132  C C   A GLU A 19  ? 1.1434 1.1069 0.6228 0.3117 -0.0542 -0.0020 62  GLU A C   
133  C C   B GLU A 19  ? 1.1434 1.1069 0.6228 0.3117 -0.0542 -0.0020 62  GLU A C   
134  C C   C GLU A 19  ? 1.1396 1.1030 0.6196 0.3111 -0.0547 -0.0036 62  GLU A C   
135  C C   D GLU A 19  ? 1.1396 1.1030 0.6196 0.3111 -0.0547 -0.0036 62  GLU A C   
136  O O   A GLU A 19  ? 1.1292 1.0913 0.6042 0.3115 -0.0359 0.0077  62  GLU A O   
137  O O   B GLU A 19  ? 1.1292 1.0913 0.6042 0.3115 -0.0359 0.0077  62  GLU A O   
138  O O   C GLU A 19  ? 1.1303 1.0920 0.6013 0.3135 -0.0362 0.0079  62  GLU A O   
139  O O   D GLU A 19  ? 1.1303 1.0920 0.6013 0.3135 -0.0362 0.0079  62  GLU A O   
140  C CB  A GLU A 19  ? 1.1227 1.0930 0.6414 0.2990 -0.0411 0.0217  62  GLU A CB  
141  C CB  B GLU A 19  ? 1.1227 1.0930 0.6414 0.2990 -0.0411 0.0217  62  GLU A CB  
142  C CB  C GLU A 19  ? 1.1194 1.0891 0.6341 0.3005 -0.0406 0.0217  62  GLU A CB  
143  C CB  D GLU A 19  ? 1.1194 1.0891 0.6341 0.3005 -0.0406 0.0217  62  GLU A CB  
144  C CG  A GLU A 19  ? 1.1124 1.0880 0.6683 0.2846 -0.0409 0.0242  62  GLU A CG  
145  C CG  B GLU A 19  ? 1.1124 1.0880 0.6683 0.2846 -0.0409 0.0242  62  GLU A CG  
146  C CG  C GLU A 19  ? 1.1274 1.1015 0.6666 0.2948 -0.0462 0.0253  62  GLU A CG  
147  C CG  D GLU A 19  ? 1.1274 1.1015 0.6666 0.2948 -0.0462 0.0253  62  GLU A CG  
148  C CD  A GLU A 19  ? 1.1353 1.1144 0.6975 0.2893 -0.0570 0.0204  62  GLU A CD  
149  C CD  B GLU A 19  ? 1.1353 1.1144 0.6975 0.2893 -0.0570 0.0204  62  GLU A CD  
150  C CD  C GLU A 19  ? 1.1612 1.1365 0.6882 0.3071 -0.0661 0.0190  62  GLU A CD  
151  C CD  D GLU A 19  ? 1.1612 1.1365 0.6882 0.3071 -0.0661 0.0190  62  GLU A CD  
152  O OE1 A GLU A 19  ? 1.1923 1.1683 0.7289 0.3057 -0.0613 0.0278  62  GLU A OE1 
153  O OE1 B GLU A 19  ? 1.1923 1.1683 0.7289 0.3057 -0.0613 0.0278  62  GLU A OE1 
154  O OE1 C GLU A 19  ? 1.1824 1.1537 0.6833 0.3228 -0.0652 0.0308  62  GLU A OE1 
155  O OE1 D GLU A 19  ? 1.1824 1.1537 0.6833 0.3228 -0.0652 0.0308  62  GLU A OE1 
156  O OE2 A GLU A 19  ? 1.1091 1.0944 0.7021 0.2770 -0.0646 0.0109  62  GLU A OE2 
157  O OE2 B GLU A 19  ? 1.1091 1.0944 0.7021 0.2770 -0.0646 0.0109  62  GLU A OE2 
158  O OE2 C GLU A 19  ? 1.1514 1.1319 0.6958 0.3009 -0.0826 0.0027  62  GLU A OE2 
159  O OE2 D GLU A 19  ? 1.1514 1.1319 0.6958 0.3009 -0.0826 0.0027  62  GLU A OE2 
160  N N   A LYS A 20  ? 1.1876 1.1481 0.6433 0.3238 -0.0719 -0.0159 63  LYS A N   
161  N N   B LYS A 20  ? 1.1876 1.1481 0.6433 0.3238 -0.0719 -0.0159 63  LYS A N   
162  N N   C LYS A 20  ? 1.1813 1.1417 0.6440 0.3195 -0.0732 -0.0204 63  LYS A N   
163  N N   D LYS A 20  ? 1.1813 1.1417 0.6440 0.3195 -0.0732 -0.0204 63  LYS A N   
164  C CA  A LYS A 20  ? 1.2232 1.1767 0.6401 0.3395 -0.0717 -0.0219 63  LYS A CA  
165  C CA  B LYS A 20  ? 1.2232 1.1767 0.6401 0.3395 -0.0717 -0.0219 63  LYS A CA  
166  C CA  C LYS A 20  ? 1.2187 1.1721 0.6425 0.3356 -0.0745 -0.0272 63  LYS A CA  
167  C CA  D LYS A 20  ? 1.2187 1.1721 0.6425 0.3356 -0.0745 -0.0272 63  LYS A CA  
168  C C   A LYS A 20  ? 1.2345 1.1859 0.6209 0.3541 -0.0542 -0.0023 63  LYS A C   
169  C C   B LYS A 20  ? 1.2345 1.1859 0.6209 0.3541 -0.0542 -0.0023 63  LYS A C   
170  C C   C LYS A 20  ? 1.2343 1.1858 0.6244 0.3523 -0.0607 -0.0091 63  LYS A C   
171  C C   D LYS A 20  ? 1.2343 1.1858 0.6244 0.3523 -0.0607 -0.0091 63  LYS A C   
172  O O   A LYS A 20  ? 1.2389 1.1920 0.6235 0.3581 -0.0529 0.0110  63  LYS A O   
173  O O   B LYS A 20  ? 1.2389 1.1920 0.6235 0.3581 -0.0529 0.0110  63  LYS A O   
174  O O   C LYS A 20  ? 1.2501 1.2025 0.6302 0.3603 -0.0673 -0.0019 63  LYS A O   
175  O O   D LYS A 20  ? 1.2501 1.2025 0.6302 0.3603 -0.0673 -0.0019 63  LYS A O   
176  C CB  A LYS A 20  ? 1.2613 1.2119 0.6585 0.3502 -0.0967 -0.0408 63  LYS A CB  
177  C CB  B LYS A 20  ? 1.2613 1.2119 0.6585 0.3502 -0.0967 -0.0408 63  LYS A CB  
178  C CB  C LYS A 20  ? 1.2507 1.2016 0.6612 0.3433 -0.1002 -0.0477 63  LYS A CB  
179  C CB  D LYS A 20  ? 1.2507 1.2016 0.6612 0.3433 -0.1002 -0.0477 63  LYS A CB  
180  C CG  A LYS A 20  ? 1.2639 1.2127 0.6814 0.3393 -0.1113 -0.0626 63  LYS A CG  
181  C CG  B LYS A 20  ? 1.2639 1.2127 0.6814 0.3393 -0.1113 -0.0626 63  LYS A CG  
182  C CG  C LYS A 20  ? 1.2390 1.1954 0.6879 0.3278 -0.1168 -0.0600 63  LYS A CG  
183  C CG  D LYS A 20  ? 1.2390 1.1954 0.6879 0.3278 -0.1168 -0.0600 63  LYS A CG  
184  C CD  A LYS A 20  ? 1.3045 1.2512 0.7074 0.3487 -0.1377 -0.0821 63  LYS A CD  
185  C CD  B LYS A 20  ? 1.3045 1.2512 0.7074 0.3487 -0.1377 -0.0821 63  LYS A CD  
186  C CD  C LYS A 20  ? 1.2673 1.2266 0.7084 0.3370 -0.1402 -0.0697 63  LYS A CD  
187  C CD  D LYS A 20  ? 1.2673 1.2266 0.7084 0.3370 -0.1402 -0.0697 63  LYS A CD  
188  C CE  A LYS A 20  ? 1.3046 1.2472 0.7270 0.3382 -0.1509 -0.1035 63  LYS A CE  
189  C CE  B LYS A 20  ? 1.3046 1.2472 0.7270 0.3382 -0.1509 -0.1035 63  LYS A CE  
190  C CE  C LYS A 20  ? 1.3053 1.2585 0.7253 0.3464 -0.1600 -0.0914 63  LYS A CE  
191  C CE  D LYS A 20  ? 1.3053 1.2585 0.7253 0.3464 -0.1600 -0.0914 63  LYS A CE  
192  N NZ  A LYS A 20  ? 1.3284 1.2716 0.7487 0.3433 -0.1785 -0.1226 63  LYS A NZ  
193  N NZ  B LYS A 20  ? 1.3284 1.2716 0.7487 0.3433 -0.1785 -0.1226 63  LYS A NZ  
194  N NZ  C LYS A 20  ? 1.2881 1.2425 0.7444 0.3296 -0.1723 -0.1091 63  LYS A NZ  
195  N NZ  D LYS A 20  ? 1.2881 1.2425 0.7444 0.3296 -0.1723 -0.1091 63  LYS A NZ  
196  N N   A ASP A 21  ? 1.2504 1.1983 0.6153 0.3619 -0.0403 -0.0003 64  ASP A N   
197  N N   B ASP A 21  ? 1.2504 1.1983 0.6153 0.3619 -0.0403 -0.0003 64  ASP A N   
198  N N   C ASP A 21  ? 1.2415 1.1905 0.6165 0.3573 -0.0417 -0.0012 64  ASP A N   
199  N N   D ASP A 21  ? 1.2415 1.1905 0.6165 0.3573 -0.0417 -0.0012 64  ASP A N   
200  C CA  A ASP A 21  ? 1.2832 1.2297 0.6199 0.3754 -0.0198 0.0189  64  ASP A CA  
201  C CA  B ASP A 21  ? 1.2832 1.2297 0.6199 0.3754 -0.0198 0.0189  64  ASP A CA  
202  C CA  C ASP A 21  ? 1.2800 1.2270 0.6226 0.3730 -0.0247 0.0172  64  ASP A CA  
203  C CA  D ASP A 21  ? 1.2800 1.2270 0.6226 0.3730 -0.0247 0.0172  64  ASP A CA  
204  C C   A ASP A 21  ? 1.2407 1.1919 0.6064 0.3636 -0.0024 0.0399  64  ASP A C   
205  C C   B ASP A 21  ? 1.2407 1.1919 0.6064 0.3636 -0.0024 0.0399  64  ASP A C   
206  C C   C ASP A 21  ? 1.2390 1.1905 0.6080 0.3622 -0.0048 0.0389  64  ASP A C   
207  C C   D ASP A 21  ? 1.2390 1.1905 0.6080 0.3622 -0.0048 0.0389  64  ASP A C   
208  O O   A ASP A 21  ? 1.2452 1.1949 0.5976 0.3717 0.0028  0.0560  64  ASP A O   
209  O O   B ASP A 21  ? 1.2452 1.1949 0.5976 0.3717 0.0028  0.0560  64  ASP A O   
210  O O   C ASP A 21  ? 1.2437 1.1938 0.6009 0.3698 -0.0001 0.0548  64  ASP A O   
211  O O   D ASP A 21  ? 1.2437 1.1938 0.6009 0.3698 -0.0001 0.0548  64  ASP A O   
212  C CB  A ASP A 21  ? 1.3512 1.2926 0.6428 0.3968 -0.0290 0.0208  64  ASP A CB  
213  C CB  B ASP A 21  ? 1.3512 1.2926 0.6428 0.3968 -0.0290 0.0208  64  ASP A CB  
214  C CB  C ASP A 21  ? 1.3437 1.2869 0.6500 0.3911 -0.0389 0.0173  64  ASP A CB  
215  C CB  D ASP A 21  ? 1.3437 1.2869 0.6500 0.3911 -0.0389 0.0173  64  ASP A CB  
216  C CG  A ASP A 21  ? 1.3968 1.3321 0.6473 0.4137 -0.0369 0.0050  64  ASP A CG  
217  C CG  B ASP A 21  ? 1.3968 1.3321 0.6473 0.4137 -0.0369 0.0050  64  ASP A CG  
218  C CG  C ASP A 21  ? 1.3770 1.3152 0.6544 0.4032 -0.0602 -0.0052 64  ASP A CG  
219  C CG  D ASP A 21  ? 1.3770 1.3152 0.6544 0.4032 -0.0602 -0.0052 64  ASP A CG  
220  O OD1 A ASP A 21  ? 1.4001 1.3340 0.6366 0.4191 -0.0196 0.0076  64  ASP A OD1 
221  O OD1 B ASP A 21  ? 1.4001 1.3340 0.6366 0.4191 -0.0196 0.0076  64  ASP A OD1 
222  O OD1 C ASP A 21  ? 1.3985 1.3338 0.6722 0.4028 -0.0583 -0.0180 64  ASP A OD1 
223  O OD1 D ASP A 21  ? 1.3985 1.3338 0.6722 0.4028 -0.0583 -0.0180 64  ASP A OD1 
224  O OD2 A ASP A 21  ? 1.4213 1.3535 0.6547 0.4217 -0.0608 -0.0104 64  ASP A OD2 
225  O OD2 B ASP A 21  ? 1.4213 1.3535 0.6547 0.4217 -0.0608 -0.0104 64  ASP A OD2 
226  O OD2 C ASP A 21  ? 1.3789 1.3160 0.6385 0.4133 -0.0794 -0.0103 64  ASP A OD2 
227  O OD2 D ASP A 21  ? 1.3789 1.3160 0.6385 0.4133 -0.0794 -0.0103 64  ASP A OD2 
228  N N   . ALA A 22  ? 1.1978 1.1536 0.6012 0.3455 0.0054  0.0395  65  ALA A N   
229  C CA  . ALA A 22  ? 1.1209 1.0809 0.5519 0.3342 0.0242  0.0579  65  ALA A CA  
230  C C   . ALA A 22  ? 1.0848 1.0467 0.5090 0.3381 0.0462  0.0675  65  ALA A C   
231  O O   . ALA A 22  ? 1.0884 1.0490 0.4967 0.3449 0.0454  0.0563  65  ALA A O   
232  C CB  . ALA A 22  ? 1.1021 1.0664 0.5757 0.3132 0.0190  0.0513  65  ALA A CB  
233  N N   A GLU A 23  ? 1.0955 1.0601 0.5340 0.3339 0.0650  0.0874  66  GLU A N   
234  N N   B GLU A 23  ? 1.0955 1.0601 0.5340 0.3339 0.0650  0.0874  66  GLU A N   
235  N N   C GLU A 23  ? 1.0618 1.0265 0.5002 0.3340 0.0655  0.0872  66  GLU A N   
236  N N   D GLU A 23  ? 1.0618 1.0265 0.5002 0.3340 0.0655  0.0872  66  GLU A N   
237  C CA  A GLU A 23  ? 1.1111 1.0797 0.5507 0.3362 0.0891  0.1011  66  GLU A CA  
238  C CA  B GLU A 23  ? 1.1111 1.0797 0.5507 0.3362 0.0891  0.1011  66  GLU A CA  
239  C CA  C GLU A 23  ? 1.0518 1.0210 0.4930 0.3353 0.0882  0.0978  66  GLU A CA  
240  C CA  D GLU A 23  ? 1.0518 1.0210 0.4930 0.3353 0.0882  0.0978  66  GLU A CA  
241  C C   A GLU A 23  ? 1.0881 1.0626 0.5527 0.3252 0.0911  0.0905  66  GLU A C   
242  C C   B GLU A 23  ? 1.0881 1.0626 0.5527 0.3252 0.0911  0.0905  66  GLU A C   
243  C C   C GLU A 23  ? 1.0254 0.9993 0.4892 0.3247 0.0857  0.0839  66  GLU A C   
244  C C   D GLU A 23  ? 1.0254 0.9993 0.4892 0.3247 0.0857  0.0839  66  GLU A C   
245  O O   A GLU A 23  ? 1.0549 1.0339 0.5569 0.3080 0.0930  0.0924  66  GLU A O   
246  O O   B GLU A 23  ? 1.0549 1.0339 0.5569 0.3080 0.0930  0.0924  66  GLU A O   
247  O O   C GLU A 23  ? 0.9496 0.9258 0.4464 0.3077 0.0784  0.0787  66  GLU A O   
248  O O   D GLU A 23  ? 0.9496 0.9258 0.4464 0.3077 0.0784  0.0787  66  GLU A O   
249  C CB  A GLU A 23  ? 1.1227 1.0925 0.5833 0.3291 0.1039  0.1222  66  GLU A CB  
250  C CB  B GLU A 23  ? 1.1227 1.0925 0.5833 0.3291 0.1039  0.1222  66  GLU A CB  
251  C CB  C GLU A 23  ? 1.0475 1.0197 0.5131 0.3269 0.1058  0.1188  66  GLU A CB  
252  C CB  D GLU A 23  ? 1.0475 1.0197 0.5131 0.3269 0.1058  0.1188  66  GLU A CB  
253  C CG  A GLU A 23  ? 1.1446 1.1191 0.6095 0.3312 0.1299  0.1393  66  GLU A CG  
254  C CG  B GLU A 23  ? 1.1446 1.1191 0.6095 0.3312 0.1299  0.1393  66  GLU A CG  
255  C CG  C GLU A 23  ? 1.0400 1.0198 0.5218 0.3236 0.1277  0.1283  66  GLU A CG  
256  C CG  D GLU A 23  ? 1.0400 1.0198 0.5218 0.3236 0.1277  0.1283  66  GLU A CG  
257  C CD  A GLU A 23  ? 1.1656 1.1364 0.6330 0.3324 0.1440  0.1623  66  GLU A CD  
258  C CD  B GLU A 23  ? 1.1656 1.1364 0.6330 0.3324 0.1440  0.1623  66  GLU A CD  
259  C CD  C GLU A 23  ? 1.0344 1.0173 0.5492 0.3114 0.1422  0.1459  66  GLU A CD  
260  C CD  D GLU A 23  ? 1.0344 1.0173 0.5492 0.3114 0.1422  0.1459  66  GLU A CD  
261  O OE1 A GLU A 23  ? 1.2026 1.1668 0.6333 0.3489 0.1475  0.1723  66  GLU A OE1 
262  O OE1 B GLU A 23  ? 1.2026 1.1668 0.6333 0.3489 0.1475  0.1723  66  GLU A OE1 
263  O OE1 C GLU A 23  ? 1.0313 1.0080 0.5502 0.3084 0.1368  0.1528  66  GLU A OE1 
264  O OE1 D GLU A 23  ? 1.0313 1.0080 0.5502 0.3084 0.1368  0.1528  66  GLU A OE1 
265  O OE2 A GLU A 23  ? 1.1441 1.1176 0.6494 0.3170 0.1508  0.1701  66  GLU A OE2 
266  O OE2 B GLU A 23  ? 1.1441 1.1176 0.6494 0.3170 0.1508  0.1701  66  GLU A OE2 
267  O OE2 C GLU A 23  ? 1.0317 1.0230 0.5695 0.3052 0.1583  0.1522  66  GLU A OE2 
268  O OE2 D GLU A 23  ? 1.0317 1.0230 0.5695 0.3052 0.1583  0.1522  66  GLU A OE2 
269  N N   A VAL A 24  ? 1.0909 1.0644 0.5345 0.3354 0.0893  0.0787  67  VAL A N   
270  N N   B VAL A 24  ? 1.0909 1.0644 0.5345 0.3354 0.0893  0.0787  67  VAL A N   
271  N N   C VAL A 24  ? 1.0362 1.0105 0.4810 0.3354 0.0911  0.0776  67  VAL A N   
272  N N   D VAL A 24  ? 1.0362 1.0105 0.4810 0.3354 0.0911  0.0776  67  VAL A N   
273  C CA  A VAL A 24  ? 1.0525 1.0297 0.5161 0.3277 0.0891  0.0674  67  VAL A CA  
274  C CA  B VAL A 24  ? 1.0525 1.0297 0.5161 0.3277 0.0891  0.0674  67  VAL A CA  
275  C CA  C VAL A 24  ? 1.0107 0.9876 0.4731 0.3284 0.0881  0.0641  67  VAL A CA  
276  C CA  D VAL A 24  ? 1.0107 0.9876 0.4731 0.3284 0.0881  0.0641  67  VAL A CA  
277  C C   A VAL A 24  ? 1.0346 1.0208 0.5156 0.3259 0.1126  0.0816  67  VAL A C   
278  C C   B VAL A 24  ? 1.0346 1.0208 0.5156 0.3259 0.1126  0.0816  67  VAL A C   
279  C C   C VAL A 24  ? 1.0023 0.9884 0.4822 0.3270 0.1105  0.0762  67  VAL A C   
280  C C   D VAL A 24  ? 1.0023 0.9884 0.4822 0.3270 0.1105  0.0762  67  VAL A C   
281  O O   A VAL A 24  ? 1.0339 1.0217 0.4940 0.3390 0.1290  0.0938  67  VAL A O   
282  O O   B VAL A 24  ? 1.0339 1.0217 0.4940 0.3390 0.1290  0.0938  67  VAL A O   
283  O O   C VAL A 24  ? 1.0085 0.9961 0.4654 0.3419 0.1237  0.0798  67  VAL A O   
284  O O   D VAL A 24  ? 1.0085 0.9961 0.4654 0.3419 0.1237  0.0798  67  VAL A O   
285  C CB  A VAL A 24  ? 1.0744 1.0455 0.5098 0.3403 0.0785  0.0491  67  VAL A CB  
286  C CB  B VAL A 24  ? 1.0744 1.0455 0.5098 0.3403 0.0785  0.0491  67  VAL A CB  
287  C CB  C VAL A 24  ? 1.0365 1.0064 0.4686 0.3415 0.0757  0.0455  67  VAL A CB  
288  C CB  D VAL A 24  ? 1.0365 1.0064 0.4686 0.3415 0.0757  0.0455  67  VAL A CB  
289  C CG1 A VAL A 24  ? 1.0527 1.0257 0.5104 0.3323 0.0772  0.0382  67  VAL A CG1 
290  C CG1 B VAL A 24  ? 1.0527 1.0257 0.5104 0.3323 0.0772  0.0382  67  VAL A CG1 
291  C CG1 C VAL A 24  ? 1.0174 0.9876 0.4692 0.3342 0.0716  0.0324  67  VAL A CG1 
292  C CG1 D VAL A 24  ? 1.0174 0.9876 0.4692 0.3342 0.0716  0.0324  67  VAL A CG1 
293  C CG2 A VAL A 24  ? 1.0867 1.0497 0.5051 0.3431 0.0550  0.0350  67  VAL A CG2 
294  C CG2 B VAL A 24  ? 1.0867 1.0497 0.5051 0.3431 0.0550  0.0350  67  VAL A CG2 
295  C CG2 C VAL A 24  ? 1.0482 1.0105 0.4639 0.3440 0.0532  0.0338  67  VAL A CG2 
296  C CG2 D VAL A 24  ? 1.0482 1.0105 0.4639 0.3440 0.0532  0.0338  67  VAL A CG2 
297  N N   A THR A 25  ? 0.9973 0.9897 0.5158 0.3103 0.1140  0.0804  68  THR A N   
298  N N   B THR A 25  ? 0.9973 0.9897 0.5158 0.3103 0.1140  0.0804  68  THR A N   
299  N N   C THR A 25  ? 0.9722 0.9648 0.4917 0.3098 0.1144  0.0816  68  THR A N   
300  N N   D THR A 25  ? 0.9722 0.9648 0.4917 0.3098 0.1144  0.0816  68  THR A N   
301  C CA  A THR A 25  ? 0.9816 0.9849 0.5261 0.3056 0.1339  0.0932  68  THR A CA  
302  C CA  B THR A 25  ? 0.9816 0.9849 0.5261 0.3056 0.1339  0.0932  68  THR A CA  
303  C CA  C THR A 25  ? 0.9636 0.9670 0.5084 0.3055 0.1342  0.0936  68  THR A CA  
304  C CA  D THR A 25  ? 0.9636 0.9670 0.5084 0.3055 0.1342  0.0936  68  THR A CA  
305  C C   A THR A 25  ? 0.9433 0.9513 0.5249 0.2888 0.1271  0.0860  68  THR A C   
306  C C   B THR A 25  ? 0.9433 0.9513 0.5249 0.2888 0.1271  0.0860  68  THR A C   
307  C C   C THR A 25  ? 0.9328 0.9407 0.5143 0.2888 0.1272  0.0862  68  THR A C   
308  C C   D THR A 25  ? 0.9328 0.9407 0.5143 0.2888 0.1272  0.0862  68  THR A C   
309  O O   A THR A 25  ? 0.9194 0.9210 0.5031 0.2816 0.1088  0.0728  68  THR A O   
310  O O   B THR A 25  ? 0.9194 0.9210 0.5031 0.2816 0.1088  0.0728  68  THR A O   
311  O O   C THR A 25  ? 0.9094 0.9111 0.4928 0.2817 0.1088  0.0728  68  THR A O   
312  O O   D THR A 25  ? 0.9094 0.9111 0.4928 0.2817 0.1088  0.0728  68  THR A O   
313  C CB  A THR A 25  ? 0.9926 0.9983 0.5456 0.3026 0.1478  0.1132  68  THR A CB  
314  C CB  B THR A 25  ? 0.9926 0.9983 0.5456 0.3026 0.1478  0.1132  68  THR A CB  
315  C CB  C THR A 25  ? 0.9737 0.9802 0.5281 0.3026 0.1493  0.1140  68  THR A CB  
316  C CB  D THR A 25  ? 0.9737 0.9802 0.5281 0.3026 0.1493  0.1140  68  THR A CB  
317  O OG1 A THR A 25  ? 0.9896 1.0064 0.5657 0.3003 0.1682  0.1252  68  THR A OG1 
318  O OG1 B THR A 25  ? 0.9896 1.0064 0.5657 0.3003 0.1682  0.1252  68  THR A OG1 
319  O OG1 C THR A 25  ? 0.9726 0.9902 0.5479 0.3015 0.1697  0.1252  68  THR A OG1 
320  O OG1 D THR A 25  ? 0.9726 0.9902 0.5479 0.3015 0.1697  0.1252  68  THR A OG1 
321  C CG2 A THR A 25  ? 0.9716 0.9746 0.5486 0.2865 0.1371  0.1138  68  THR A CG2 
322  C CG2 B THR A 25  ? 0.9716 0.9746 0.5486 0.2865 0.1371  0.1138  68  THR A CG2 
323  C CG2 C THR A 25  ? 0.9513 0.9558 0.5324 0.2857 0.1400  0.1157  68  THR A CG2 
324  C CG2 D THR A 25  ? 0.9513 0.9558 0.5324 0.2857 0.1400  0.1157  68  THR A CG2 
325  N N   . GLY A 26  ? 0.9244 0.9433 0.5343 0.2830 0.1412  0.0949  69  GLY A N   
326  C CA  . GLY A 26  ? 0.8965 0.9210 0.5400 0.2692 0.1355  0.0891  69  GLY A CA  
327  C C   . GLY A 26  ? 0.9028 0.9289 0.5423 0.2772 0.1344  0.0787  69  GLY A C   
328  O O   . GLY A 26  ? 0.9487 0.9665 0.5578 0.2896 0.1284  0.0689  69  GLY A O   
329  N N   . ASN A 27  ? 0.8964 0.9326 0.5665 0.2707 0.1388  0.0801  70  ASN A N   
330  C CA  . ASN A 27  ? 0.9302 0.9675 0.6050 0.2754 0.1345  0.0695  70  ASN A CA  
331  C C   . ASN A 27  ? 0.8584 0.8874 0.5433 0.2629 0.1141  0.0579  70  ASN A C   
332  O O   . ASN A 27  ? 0.7995 0.8219 0.4834 0.2522 0.1039  0.0568  70  ASN A O   
333  C CB  . ASN A 27  ? 0.9698 1.0239 0.6728 0.2769 0.1510  0.0785  70  ASN A CB  
334  C CG  . ASN A 27  ? 1.0071 1.0708 0.7482 0.2597 0.1517  0.0871  70  ASN A CG  
335  O OD1 . ASN A 27  ? 1.1023 1.1645 0.8466 0.2514 0.1534  0.0949  70  ASN A OD1 
336  N ND2 . ASN A 27  ? 1.0271 1.1003 0.7977 0.2546 0.1497  0.0852  70  ASN A ND2 
337  N N   . SER A 28  ? 0.8365 0.8646 0.5286 0.2653 0.1083  0.0494  71  SER A N   
338  C CA  . SER A 28  ? 0.8413 0.8596 0.5401 0.2556 0.0900  0.0391  71  SER A CA  
339  C C   . SER A 28  ? 0.8327 0.8594 0.5604 0.2512 0.0900  0.0407  71  SER A C   
340  O O   . SER A 28  ? 0.8987 0.9197 0.6244 0.2573 0.0839  0.0326  71  SER A O   
341  C CB  . SER A 28  ? 0.8688 0.8721 0.5426 0.2648 0.0793  0.0249  71  SER A CB  
342  O OG  . SER A 28  ? 0.9371 0.9324 0.5832 0.2700 0.0763  0.0211  71  SER A OG  
343  N N   . PRO A 29  ? 0.8248 0.8647 0.5809 0.2411 0.0954  0.0505  72  PRO A N   
344  C CA  . PRO A 29  ? 0.8349 0.8850 0.6194 0.2390 0.0949  0.0519  72  PRO A CA  
345  C C   . PRO A 29  ? 0.8292 0.8694 0.6184 0.2292 0.0766  0.0450  72  PRO A C   
346  O O   . PRO A 29  ? 0.7993 0.8308 0.5818 0.2174 0.0674  0.0434  72  PRO A O   
347  C CB  . PRO A 29  ? 0.8403 0.9066 0.6519 0.2305 0.1055  0.0639  72  PRO A CB  
348  C CG  . PRO A 29  ? 0.8351 0.8935 0.6349 0.2209 0.1027  0.0661  72  PRO A CG  
349  C CD  . PRO A 29  ? 0.8580 0.9029 0.6218 0.2312 0.1007  0.0597  72  PRO A CD  
350  N N   . ARG A 30  ? 0.8644 0.9056 0.6642 0.2346 0.0723  0.0416  73  ARG A N   
351  C CA  . ARG A 30  ? 0.9398 0.9735 0.7481 0.2262 0.0563  0.0380  73  ARG A CA  
352  C C   . ARG A 30  ? 0.8864 0.9367 0.7270 0.2182 0.0565  0.0453  73  ARG A C   
353  O O   . ARG A 30  ? 0.8633 0.9277 0.7234 0.2265 0.0642  0.0484  73  ARG A O   
354  C CB  . ARG A 30  ? 1.0515 1.0746 0.8527 0.2374 0.0499  0.0304  73  ARG A CB  
355  C CG  . ARG A 30  ? 1.1929 1.1964 0.9639 0.2422 0.0447  0.0208  73  ARG A CG  
356  C CD  . ARG A 30  ? 1.3532 1.3469 1.1160 0.2572 0.0428  0.0122  73  ARG A CD  
357  N NE  . ARG A 30  ? 1.4726 1.4505 1.2065 0.2637 0.0404  0.0022  73  ARG A NE  
358  C CZ  . ARG A 30  ? 1.5151 1.4725 1.2363 0.2624 0.0274  -0.0071 73  ARG A CZ  
359  N NH1 . ARG A 30  ? 1.5803 1.5284 1.3126 0.2553 0.0162  -0.0067 73  ARG A NH1 
360  N NH2 . ARG A 30  ? 1.4420 1.3876 1.1393 0.2684 0.0251  -0.0168 73  ARG A NH2 
361  N N   . LEU A 31  ? 0.8485 0.8976 0.6947 0.2030 0.0484  0.0473  74  LEU A N   
362  C CA  . LEU A 31  ? 0.8177 0.8821 0.6932 0.1936 0.0474  0.0530  74  LEU A CA  
363  C C   . LEU A 31  ? 0.8123 0.8689 0.6887 0.1845 0.0301  0.0502  74  LEU A C   
364  O O   . LEU A 31  ? 0.7893 0.8298 0.6442 0.1782 0.0223  0.0464  74  LEU A O   
365  C CB  . LEU A 31  ? 0.8382 0.9074 0.7168 0.1842 0.0550  0.0576  74  LEU A CB  
366  C CG  . LEU A 31  ? 0.8451 0.9232 0.7252 0.1921 0.0732  0.0636  74  LEU A CG  
367  C CD1 . LEU A 31  ? 0.8334 0.9108 0.7129 0.1821 0.0778  0.0679  74  LEU A CD1 
368  C CD2 . LEU A 31  ? 0.8390 0.9373 0.7499 0.1980 0.0838  0.0695  74  LEU A CD2 
369  N N   . ASP A 32  ? 0.7616 0.8299 0.6626 0.1844 0.0245  0.0524  75  ASP A N   
370  C CA  . ASP A 32  ? 0.7699 0.8339 0.6737 0.1757 0.0080  0.0515  75  ASP A CA  
371  C C   . ASP A 32  ? 0.7053 0.7756 0.6181 0.1612 0.0060  0.0529  75  ASP A C   
372  O O   . ASP A 32  ? 0.6823 0.7709 0.6233 0.1594 0.0118  0.0563  75  ASP A O   
373  C CB  . ASP A 32  ? 0.8274 0.9032 0.7556 0.1827 0.0019  0.0530  75  ASP A CB  
374  C CG  . ASP A 32  ? 0.8747 0.9399 0.7924 0.1962 -0.0005 0.0504  75  ASP A CG  
375  O OD1 . ASP A 32  ? 0.8899 0.9340 0.7796 0.1959 -0.0049 0.0469  75  ASP A OD1 
376  O OD2 . ASP A 32  ? 0.9681 1.0463 0.9078 0.2069 0.0023  0.0516  75  ASP A OD2 
377  N N   . VAL A 33  ? 0.6858 0.7415 0.5771 0.1514 -0.0011 0.0501  76  VAL A N   
378  C CA  . VAL A 33  ? 0.6930 0.7514 0.5881 0.1380 -0.0023 0.0496  76  VAL A CA  
379  C C   . VAL A 33  ? 0.7015 0.7511 0.5857 0.1297 -0.0179 0.0470  76  VAL A C   
380  O O   . VAL A 33  ? 0.7059 0.7423 0.5724 0.1331 -0.0255 0.0464  76  VAL A O   
381  C CB  . VAL A 33  ? 0.6834 0.7347 0.5634 0.1346 0.0075  0.0488  76  VAL A CB  
382  C CG1 . VAL A 33  ? 0.6988 0.7566 0.5832 0.1445 0.0222  0.0522  76  VAL A CG1 
383  C CG2 . VAL A 33  ? 0.6989 0.7313 0.5493 0.1326 0.0025  0.0448  76  VAL A CG2 
384  N N   . ALA A 34  ? 0.6836 0.7394 0.5777 0.1194 -0.0222 0.0456  77  ALA A N   
385  C CA  . ALA A 34  ? 0.6930 0.7411 0.5740 0.1106 -0.0358 0.0425  77  ALA A CA  
386  C C   . ALA A 34  ? 0.6672 0.7097 0.5377 0.1002 -0.0310 0.0389  77  ALA A C   
387  O O   . ALA A 34  ? 0.6680 0.7188 0.5541 0.0985 -0.0213 0.0392  77  ALA A O   
388  C CB  . ALA A 34  ? 0.6813 0.7433 0.5854 0.1091 -0.0466 0.0422  77  ALA A CB  
389  N N   . LEU A 35  ? 0.6554 0.6836 0.5000 0.0946 -0.0360 0.0363  78  LEU A N   
390  C CA  . LEU A 35  ? 0.6712 0.6944 0.5062 0.0851 -0.0319 0.0318  78  LEU A CA  
391  C C   . LEU A 35  ? 0.6894 0.7124 0.5200 0.0771 -0.0432 0.0276  78  LEU A C   
392  O O   . LEU A 35  ? 0.7333 0.7483 0.5460 0.0774 -0.0528 0.0285  78  LEU A O   
393  C CB  . LEU A 35  ? 0.6727 0.6812 0.4829 0.0848 -0.0272 0.0314  78  LEU A CB  
394  C CG  . LEU A 35  ? 0.6679 0.6717 0.4693 0.0763 -0.0217 0.0267  78  LEU A CG  
395  C CD1 . LEU A 35  ? 0.6556 0.6692 0.4772 0.0752 -0.0136 0.0258  78  LEU A CD1 
396  C CD2 . LEU A 35  ? 0.6569 0.6493 0.4402 0.0770 -0.0166 0.0265  78  LEU A CD2 
397  N N   . ASP A 36  ? 0.6972 0.7281 0.5435 0.0707 -0.0425 0.0232  79  ASP A N   
398  C CA  . ASP A 36  ? 0.6985 0.7301 0.5418 0.0632 -0.0538 0.0169  79  ASP A CA  
399  C C   . ASP A 36  ? 0.7084 0.7270 0.5254 0.0562 -0.0507 0.0116  79  ASP A C   
400  O O   . ASP A 36  ? 0.7081 0.7202 0.5165 0.0565 -0.0394 0.0127  79  ASP A O   
401  C CB  . ASP A 36  ? 0.7006 0.7470 0.5775 0.0599 -0.0552 0.0138  79  ASP A CB  
402  C CG  . ASP A 36  ? 0.7266 0.7727 0.6137 0.0534 -0.0452 0.0096  79  ASP A CG  
403  O OD1 . ASP A 36  ? 0.7208 0.7566 0.5901 0.0524 -0.0361 0.0091  79  ASP A OD1 
404  O OD2 . ASP A 36  ? 0.7703 0.8266 0.6855 0.0495 -0.0469 0.0069  79  ASP A OD2 
405  N N   . GLU A 37  ? 0.7244 0.7404 0.5298 0.0505 -0.0606 0.0053  80  GLU A N   
406  C CA  . GLU A 37  ? 0.7474 0.7519 0.5259 0.0443 -0.0582 -0.0003 80  GLU A CA  
407  C C   . GLU A 37  ? 0.7108 0.7162 0.5012 0.0400 -0.0465 -0.0056 80  GLU A C   
408  O O   . GLU A 37  ? 0.6836 0.6802 0.4562 0.0374 -0.0386 -0.0079 80  GLU A O   
409  C CB  . GLU A 37  ? 0.7956 0.7983 0.5589 0.0408 -0.0726 -0.0061 80  GLU A CB  
410  C CG  . GLU A 37  ? 0.8796 0.8690 0.6075 0.0366 -0.0699 -0.0095 80  GLU A CG  
411  C CD  . GLU A 37  ? 0.9197 0.9053 0.6250 0.0337 -0.0828 -0.0160 80  GLU A CD  
412  O OE1 . GLU A 37  ? 0.9239 0.9147 0.6392 0.0296 -0.0887 -0.0264 80  GLU A OE1 
413  O OE2 . GLU A 37  ? 1.0107 0.9870 0.6872 0.0356 -0.0872 -0.0106 80  GLU A OE2 
414  N N   . SER A 38  ? 0.6822 0.6977 0.5030 0.0395 -0.0446 -0.0066 81  SER A N   
415  C CA  . SER A 38  ? 0.6982 0.7137 0.5334 0.0363 -0.0337 -0.0100 81  SER A CA  
416  C C   . SER A 38  ? 0.6837 0.6982 0.5218 0.0419 -0.0208 -0.0023 81  SER A C   
417  O O   . SER A 38  ? 0.6998 0.7144 0.5510 0.0408 -0.0118 -0.0030 81  SER A O   
418  C CB  . SER A 38  ? 0.7253 0.7505 0.5924 0.0332 -0.0365 -0.0127 81  SER A CB  
419  O OG  . SER A 38  ? 0.8018 0.8284 0.6666 0.0285 -0.0507 -0.0211 81  SER A OG  
420  N N   . GLY A 39  ? 0.6600 0.6726 0.4861 0.0480 -0.0204 0.0043  82  GLY A N   
421  C CA  . GLY A 39  ? 0.6799 0.6909 0.5062 0.0541 -0.0098 0.0101  82  GLY A CA  
422  C C   . GLY A 39  ? 0.6557 0.6767 0.5072 0.0594 -0.0039 0.0161  82  GLY A C   
423  O O   . GLY A 39  ? 0.6698 0.6896 0.5213 0.0642 0.0053  0.0201  82  GLY A O   
424  N N   . ASP A 40  ? 0.6635 0.6945 0.5353 0.0591 -0.0092 0.0172  83  ASP A N   
425  C CA  . ASP A 40  ? 0.6721 0.7146 0.5704 0.0640 -0.0028 0.0239  83  ASP A CA  
426  C C   . ASP A 40  ? 0.6550 0.7018 0.5514 0.0728 -0.0055 0.0293  83  ASP A C   
427  O O   . ASP A 40  ? 0.6379 0.6863 0.5315 0.0724 -0.0171 0.0275  83  ASP A O   
428  C CB  . ASP A 40  ? 0.7066 0.7583 0.6333 0.0572 -0.0065 0.0209  83  ASP A CB  
429  C CG  . ASP A 40  ? 0.7732 0.8187 0.7034 0.0497 -0.0023 0.0155  83  ASP A CG  
430  O OD1 . ASP A 40  ? 0.8559 0.8932 0.7734 0.0516 0.0065  0.0170  83  ASP A OD1 
431  O OD2 . ASP A 40  ? 0.8501 0.8986 0.7963 0.0425 -0.0087 0.0093  83  ASP A OD2 
432  N N   . PHE A 41  ? 0.6431 0.6915 0.5405 0.0812 0.0047  0.0355  84  PHE A N   
433  C CA  . PHE A 41  ? 0.6206 0.6741 0.5200 0.0912 0.0046  0.0402  84  PHE A CA  
434  C C   . PHE A 41  ? 0.6582 0.7284 0.5904 0.0928 0.0064  0.0440  84  PHE A C   
435  O O   . PHE A 41  ? 0.6714 0.7481 0.6241 0.0879 0.0128  0.0453  84  PHE A O   
436  C CB  . PHE A 41  ? 0.5837 0.6327 0.4708 0.1003 0.0153  0.0441  84  PHE A CB  
437  C CG  . PHE A 41  ? 0.5757 0.6101 0.4340 0.1010 0.0125  0.0406  84  PHE A CG  
438  C CD1 . PHE A 41  ? 0.5794 0.6072 0.4240 0.1044 0.0045  0.0394  84  PHE A CD1 
439  C CD2 . PHE A 41  ? 0.5818 0.6090 0.4288 0.0981 0.0177  0.0388  84  PHE A CD2 
440  C CE1 . PHE A 41  ? 0.6037 0.6180 0.4252 0.1042 0.0027  0.0365  84  PHE A CE1 
441  C CE2 . PHE A 41  ? 0.5721 0.5876 0.3969 0.0981 0.0151  0.0352  84  PHE A CE2 
442  C CZ  . PHE A 41  ? 0.5673 0.5764 0.3799 0.1007 0.0080  0.0342  84  PHE A CZ  
443  N N   . SER A 42  ? 0.6627 0.7396 0.6016 0.0999 0.0017  0.0460  85  SER A N   
444  C CA  . SER A 42  ? 0.6881 0.7834 0.6612 0.1033 0.0048  0.0501  85  SER A CA  
445  C C   . SER A 42  ? 0.7205 0.8191 0.6918 0.1161 0.0062  0.0534  85  SER A C   
446  O O   . SER A 42  ? 0.6777 0.7636 0.6235 0.1200 -0.0010 0.0510  85  SER A O   
447  C CB  . SER A 42  ? 0.7215 0.8253 0.7145 0.0952 -0.0086 0.0457  85  SER A CB  
448  O OG  . SER A 42  ? 0.7337 0.8294 0.7065 0.0955 -0.0242 0.0417  85  SER A OG  
449  N N   . LEU A 43  ? 0.7836 0.8979 0.7813 0.1227 0.0165  0.0587  86  LEU A N   
450  C CA  . LEU A 43  ? 0.8506 0.9699 0.8502 0.1364 0.0197  0.0612  86  LEU A CA  
451  C C   . LEU A 43  ? 0.8429 0.9711 0.8602 0.1374 0.0045  0.0590  86  LEU A C   
452  O O   . LEU A 43  ? 0.8039 0.9489 0.8546 0.1325 0.0019  0.0596  86  LEU A O   
453  C CB  . LEU A 43  ? 0.8748 1.0082 0.8951 0.1434 0.0388  0.0680  86  LEU A CB  
454  C CG  . LEU A 43  ? 0.9218 1.0448 0.9187 0.1463 0.0532  0.0711  86  LEU A CG  
455  C CD1 . LEU A 43  ? 0.9443 1.0810 0.9649 0.1475 0.0717  0.0795  86  LEU A CD1 
456  C CD2 . LEU A 43  ? 0.9605 1.0724 0.9281 0.1592 0.0552  0.0691  86  LEU A CD2 
457  N N   . VAL A 44  ? 0.8904 1.0064 0.8856 0.1429 -0.0060 0.0566  87  VAL A N   
458  C CA  . VAL A 44  ? 0.9659 1.0890 0.9750 0.1507 -0.0173 0.0566  87  VAL A CA  
459  C C   . VAL A 44  ? 1.0595 1.1965 1.0892 0.1636 -0.0030 0.0603  87  VAL A C   
460  O O   . VAL A 44  ? 1.1869 1.3193 1.2036 0.1681 0.0126  0.0620  87  VAL A O   
461  C CB  . VAL A 44  ? 0.9575 1.0597 0.9340 0.1544 -0.0291 0.0545  87  VAL A CB  
462  C CG1 . VAL A 44  ? 0.9539 1.0611 0.9435 0.1637 -0.0413 0.0554  87  VAL A CG1 
463  C CG2 . VAL A 44  ? 0.9177 1.0049 0.8691 0.1420 -0.0389 0.0515  87  VAL A CG2 
464  N N   . GLU A 45  ? 1.1719 1.3251 1.2310 0.1704 -0.0082 0.0612  88  GLU A N   
465  C CA  . GLU A 45  ? 1.2527 1.4222 1.3355 0.1830 0.0073  0.0646  88  GLU A CA  
466  C C   . GLU A 45  ? 1.2724 1.4475 1.3687 0.1951 -0.0029 0.0636  88  GLU A C   
467  O O   . GLU A 45  ? 1.2593 1.4169 1.3287 0.2042 -0.0053 0.0616  88  GLU A O   
468  C CB  . GLU A 45  ? 1.2807 1.4725 1.4008 0.1762 0.0189  0.0686  88  GLU A CB  
469  C CG  . GLU A 45  ? 1.2859 1.4715 1.3914 0.1714 0.0365  0.0720  88  GLU A CG  
470  C CD  . GLU A 45  ? 1.2658 1.4420 1.3450 0.1842 0.0522  0.0736  88  GLU A CD  
471  O OE1 . GLU A 45  ? 1.2320 1.3862 1.2722 0.1844 0.0479  0.0701  88  GLU A OE1 
472  O OE2 . GLU A 45  ? 1.2648 1.4559 1.3627 0.1938 0.0686  0.0781  88  GLU A OE2 
473  N N   . GLY B 7   ? 1.1234 1.2031 1.0248 0.0854 0.0304  -0.0534 16  GLY B N   
474  C CA  . GLY B 7   ? 1.1328 1.2027 1.0277 0.0895 0.0314  -0.0478 16  GLY B CA  
475  C C   . GLY B 7   ? 1.1309 1.1961 1.0194 0.0925 0.0286  -0.0473 16  GLY B C   
476  O O   . GLY B 7   ? 1.1610 1.2300 1.0506 0.0896 0.0258  -0.0510 16  GLY B O   
477  N N   . GLU B 8   ? 1.0623 1.1199 0.9443 0.0982 0.0291  -0.0428 17  GLU B N   
478  C CA  . GLU B 8   ? 0.9877 1.0396 0.8620 0.1029 0.0262  -0.0422 17  GLU B CA  
479  C C   . GLU B 8   ? 0.9141 0.9636 0.7851 0.0981 0.0254  -0.0412 17  GLU B C   
480  O O   . GLU B 8   ? 0.9005 0.9472 0.7694 0.0968 0.0281  -0.0369 17  GLU B O   
481  C CB  . GLU B 8   ? 1.0282 1.0739 0.8964 0.1110 0.0276  -0.0373 17  GLU B CB  
482  C CG  . GLU B 8   ? 1.0082 1.0487 0.8679 0.1173 0.0242  -0.0375 17  GLU B CG  
483  C CD  . GLU B 8   ? 1.0397 1.0756 0.8929 0.1265 0.0253  -0.0329 17  GLU B CD  
484  O OE1 . GLU B 8   ? 0.9458 0.9813 0.8001 0.1273 0.0294  -0.0275 17  GLU B OE1 
485  O OE2 . GLU B 8   ? 1.0932 1.1261 0.9403 0.1331 0.0219  -0.0346 17  GLU B OE2 
486  N N   A THR B 9   ? 0.9038 0.9543 0.7745 0.0955 0.0214  -0.0450 18  THR B N   
487  N N   B THR B 9   ? 0.8943 0.9448 0.7650 0.0957 0.0213  -0.0451 18  THR B N   
488  N N   C THR B 9   ? 0.9038 0.9543 0.7745 0.0955 0.0214  -0.0450 18  THR B N   
489  N N   D THR B 9   ? 0.8943 0.9448 0.7650 0.0957 0.0213  -0.0451 18  THR B N   
490  C CA  A THR B 9   ? 0.9018 0.9495 0.7697 0.0903 0.0196  -0.0445 18  THR B CA  
491  C CA  B THR B 9   ? 0.8864 0.9347 0.7548 0.0901 0.0193  -0.0450 18  THR B CA  
492  C CA  C THR B 9   ? 0.9018 0.9495 0.7697 0.0903 0.0196  -0.0445 18  THR B CA  
493  C CA  D THR B 9   ? 0.8864 0.9347 0.7548 0.0901 0.0193  -0.0450 18  THR B CA  
494  C C   A THR B 9   ? 0.8849 0.9247 0.7443 0.0957 0.0150  -0.0448 18  THR B C   
495  C C   B THR B 9   ? 0.8760 0.9158 0.7354 0.0957 0.0151  -0.0447 18  THR B C   
496  C C   C THR B 9   ? 0.8849 0.9247 0.7443 0.0957 0.0150  -0.0448 18  THR B C   
497  C C   D THR B 9   ? 0.8760 0.9158 0.7354 0.0957 0.0151  -0.0447 18  THR B C   
498  O O   A THR B 9   ? 0.9009 0.9369 0.7572 0.0919 0.0123  -0.0448 18  THR B O   
499  O O   B THR B 9   ? 0.8917 0.9272 0.7474 0.0923 0.0130  -0.0441 18  THR B O   
500  O O   C THR B 9   ? 0.9009 0.9369 0.7572 0.0919 0.0123  -0.0448 18  THR B O   
501  O O   D THR B 9   ? 0.8917 0.9272 0.7474 0.0923 0.0130  -0.0441 18  THR B O   
502  C CB  A THR B 9   ? 0.9114 0.9666 0.7864 0.0816 0.0183  -0.0482 18  THR B CB  
503  C CB  B THR B 9   ? 0.8846 0.9407 0.7603 0.0824 0.0174  -0.0493 18  THR B CB  
504  C CB  C THR B 9   ? 0.9114 0.9666 0.7864 0.0816 0.0183  -0.0482 18  THR B CB  
505  C CB  D THR B 9   ? 0.8846 0.9407 0.7603 0.0824 0.0174  -0.0493 18  THR B CB  
506  O OG1 A THR B 9   ? 0.9176 0.9808 0.8000 0.0794 0.0219  -0.0492 18  THR B OG1 
507  O OG1 B THR B 9   ? 0.8718 0.9317 0.7503 0.0858 0.0147  -0.0535 18  THR B OG1 
508  O OG1 C THR B 9   ? 0.9176 0.9808 0.8000 0.0794 0.0219  -0.0492 18  THR B OG1 
509  O OG1 D THR B 9   ? 0.8718 0.9317 0.7503 0.0858 0.0147  -0.0535 18  THR B OG1 
510  C CG2 A THR B 9   ? 0.9167 0.9697 0.7900 0.0748 0.0180  -0.0464 18  THR B CG2 
511  C CG2 B THR B 9   ? 0.8857 0.9495 0.7685 0.0763 0.0216  -0.0492 18  THR B CG2 
512  C CG2 C THR B 9   ? 0.9167 0.9697 0.7900 0.0748 0.0180  -0.0464 18  THR B CG2 
513  C CG2 D THR B 9   ? 0.8857 0.9495 0.7685 0.0763 0.0216  -0.0492 18  THR B CG2 
514  N N   . THR B 10  ? 0.8546 0.8917 0.7099 0.1043 0.0138  -0.0450 19  THR B N   
515  C CA  . THR B 10  ? 0.8184 0.8479 0.6646 0.1112 0.0092  -0.0456 19  THR B CA  
516  C C   . THR B 10  ? 0.7391 0.7616 0.5774 0.1126 0.0099  -0.0415 19  THR B C   
517  O O   . THR B 10  ? 0.6975 0.7203 0.5350 0.1144 0.0149  -0.0367 19  THR B O   
518  C CB  . THR B 10  ? 0.8368 0.8648 0.6791 0.1213 0.0090  -0.0454 19  THR B CB  
519  O OG1 . THR B 10  ? 0.9211 0.9555 0.7704 0.1211 0.0094  -0.0484 19  THR B OG1 
520  C CG2 . THR B 10  ? 0.8217 0.8433 0.6557 0.1281 0.0031  -0.0479 19  THR B CG2 
521  N N   . ASP B 11  ? 0.6807 0.6973 0.5137 0.1120 0.0046  -0.0433 20  ASP B N   
522  C CA  . ASP B 11  ? 0.6987 0.7077 0.5227 0.1150 0.0040  -0.0403 20  ASP B CA  
523  C C   . ASP B 11  ? 0.6960 0.7031 0.5132 0.1256 0.0069  -0.0364 20  ASP B C   
524  O O   . ASP B 11  ? 0.7186 0.7277 0.5358 0.1315 0.0072  -0.0371 20  ASP B O   
525  C CB  . ASP B 11  ? 0.7279 0.7290 0.5456 0.1155 -0.0035 -0.0436 20  ASP B CB  
526  C CG  . ASP B 11  ? 0.7667 0.7681 0.5895 0.1045 -0.0061 -0.0453 20  ASP B CG  
527  O OD1 . ASP B 11  ? 0.7360 0.7447 0.5672 0.0966 -0.0018 -0.0443 20  ASP B OD1 
528  O OD2 . ASP B 11  ? 0.8220 0.8160 0.6399 0.1040 -0.0128 -0.0475 20  ASP B OD2 
529  N N   . GLY B 12  ? 0.6678 0.6716 0.4790 0.1281 0.0091  -0.0322 21  GLY B N   
530  C CA  . GLY B 12  ? 0.6352 0.6385 0.4399 0.1381 0.0122  -0.0277 21  GLY B CA  
531  C C   . GLY B 12  ? 0.5987 0.6056 0.4060 0.1361 0.0186  -0.0218 21  GLY B C   
532  O O   . GLY B 12  ? 0.5668 0.5751 0.3793 0.1276 0.0200  -0.0216 21  GLY B O   
533  N N   . VAL B 13  ? 0.5924 0.6009 0.3961 0.1439 0.0223  -0.0168 22  VAL B N   
534  C CA  . VAL B 13  ? 0.5838 0.5959 0.3893 0.1433 0.0281  -0.0103 22  VAL B CA  
535  C C   . VAL B 13  ? 0.5795 0.5976 0.3935 0.1416 0.0330  -0.0071 22  VAL B C   
536  O O   . VAL B 13  ? 0.5839 0.6026 0.3988 0.1449 0.0321  -0.0086 22  VAL B O   
537  C CB  . VAL B 13  ? 0.6052 0.6153 0.4003 0.1527 0.0285  -0.0064 22  VAL B CB  
538  C CG1 . VAL B 13  ? 0.6357 0.6460 0.4243 0.1640 0.0282  -0.0050 22  VAL B CG1 
539  C CG2 . VAL B 13  ? 0.5993 0.6140 0.3974 0.1510 0.0342  0.0000  22  VAL B CG2 
540  N N   . TYR B 14  ? 0.5750 0.5968 0.3961 0.1352 0.0371  -0.0038 23  TYR B N   
541  C CA  . TYR B 14  ? 0.5589 0.5853 0.3896 0.1314 0.0407  -0.0017 23  TYR B CA  
542  C C   . TYR B 14  ? 0.5638 0.5935 0.3970 0.1313 0.0456  0.0054  23  TYR B C   
543  O O   . TYR B 14  ? 0.6018 0.6312 0.4327 0.1299 0.0463  0.0070  23  TYR B O   
544  C CB  . TYR B 14  ? 0.5504 0.5786 0.3894 0.1216 0.0399  -0.0064 23  TYR B CB  
545  C CG  . TYR B 14  ? 0.5241 0.5515 0.3637 0.1209 0.0358  -0.0129 23  TYR B CG  
546  C CD1 . TYR B 14  ? 0.5226 0.5460 0.3561 0.1218 0.0312  -0.0168 23  TYR B CD1 
547  C CD2 . TYR B 14  ? 0.5166 0.5471 0.3628 0.1196 0.0362  -0.0149 23  TYR B CD2 
548  C CE1 . TYR B 14  ? 0.5278 0.5512 0.3627 0.1206 0.0271  -0.0226 23  TYR B CE1 
549  C CE2 . TYR B 14  ? 0.5337 0.5647 0.3809 0.1192 0.0324  -0.0209 23  TYR B CE2 
550  C CZ  . TYR B 14  ? 0.5436 0.5715 0.3856 0.1194 0.0280  -0.0246 23  TYR B CZ  
551  O OH  . TYR B 14  ? 0.5747 0.6038 0.4187 0.1185 0.0240  -0.0303 23  TYR B OH  
552  N N   . ARG B 15  ? 0.5661 0.5986 0.4043 0.1327 0.0486  0.0095  24  ARG B N   
553  C CA  . ARG B 15  ? 0.5618 0.5981 0.4055 0.1305 0.0530  0.0163  24  ARG B CA  
554  C C   . ARG B 15  ? 0.5547 0.5922 0.4080 0.1207 0.0533  0.0136  24  ARG B C   
555  O O   . ARG B 15  ? 0.5122 0.5491 0.3692 0.1178 0.0513  0.0085  24  ARG B O   
556  C CB  . ARG B 15  ? 0.5717 0.6099 0.4171 0.1356 0.0555  0.0223  24  ARG B CB  
557  C CG  . ARG B 15  ? 0.5884 0.6259 0.4238 0.1461 0.0552  0.0246  24  ARG B CG  
558  C CD  . ARG B 15  ? 0.6271 0.6664 0.4651 0.1500 0.0576  0.0305  24  ARG B CD  
559  N NE  . ARG B 15  ? 0.6354 0.6747 0.4638 0.1606 0.0575  0.0330  24  ARG B NE  
560  C CZ  . ARG B 15  ? 0.6461 0.6890 0.4690 0.1672 0.0605  0.0399  24  ARG B CZ  
561  N NH1 . ARG B 15  ? 0.6595 0.7069 0.4862 0.1642 0.0640  0.0456  24  ARG B NH1 
562  N NH2 . ARG B 15  ? 0.6655 0.7083 0.4790 0.1773 0.0600  0.0413  24  ARG B NH2 
563  N N   . VAL B 16  ? 0.5658 0.6056 0.4229 0.1168 0.0558  0.0175  25  VAL B N   
564  C CA  . VAL B 16  ? 0.5661 0.6076 0.4324 0.1085 0.0567  0.0165  25  VAL B CA  
565  C C   . VAL B 16  ? 0.5672 0.6113 0.4402 0.1084 0.0596  0.0234  25  VAL B C   
566  O O   . VAL B 16  ? 0.5624 0.6089 0.4346 0.1104 0.0622  0.0297  25  VAL B O   
567  C CB  . VAL B 16  ? 0.5827 0.6244 0.4476 0.1039 0.0566  0.0153  25  VAL B CB  
568  C CG1 . VAL B 16  ? 0.5856 0.6291 0.4594 0.0959 0.0573  0.0141  25  VAL B CG1 
569  C CG2 . VAL B 16  ? 0.5724 0.6108 0.4304 0.1039 0.0532  0.0093  25  VAL B CG2 
570  N N   . MET B 17  ? 0.5972 0.6408 0.4771 0.1056 0.0590  0.0220  26  MET B N   
571  C CA  . MET B 17  ? 0.6198 0.6640 0.5064 0.1058 0.0606  0.0280  26  MET B CA  
572  C C   . MET B 17  ? 0.6419 0.6865 0.5378 0.0981 0.0601  0.0265  26  MET B C   
573  O O   . MET B 17  ? 0.6285 0.6725 0.5255 0.0940 0.0580  0.0194  26  MET B O   
574  C CB  . MET B 17  ? 0.6416 0.6834 0.5277 0.1097 0.0591  0.0268  26  MET B CB  
575  C CG  . MET B 17  ? 0.6507 0.6917 0.5272 0.1179 0.0589  0.0271  26  MET B CG  
576  S SD  . MET B 17  ? 0.6777 0.7217 0.5487 0.1251 0.0626  0.0372  26  MET B SD  
577  C CE  . MET B 17  ? 0.6982 0.7431 0.5786 0.1234 0.0646  0.0453  26  MET B CE  
578  N N   . THR B 18  ? 0.6620 0.7074 0.5645 0.0966 0.0615  0.0330  27  THR B N   
579  C CA  . THR B 18  ? 0.7095 0.7540 0.6212 0.0903 0.0602  0.0319  27  THR B CA  
580  C C   . THR B 18  ? 0.7601 0.8024 0.6778 0.0912 0.0598  0.0373  27  THR B C   
581  O O   . THR B 18  ? 0.6985 0.7422 0.6146 0.0954 0.0621  0.0452  27  THR B O   
582  C CB  . THR B 18  ? 0.7277 0.7752 0.6423 0.0859 0.0615  0.0341  27  THR B CB  
583  O OG1 . THR B 18  ? 0.7577 0.8037 0.6808 0.0803 0.0595  0.0320  27  THR B OG1 
584  C CG2 . THR B 18  ? 0.7151 0.7661 0.6298 0.0883 0.0647  0.0435  27  THR B CG2 
585  N N   . ARG B 19  ? 0.8110 0.8501 0.7352 0.0875 0.0569  0.0336  28  ARG B N   
586  C CA  . ARG B 19  ? 0.8859 0.9215 0.8173 0.0867 0.0555  0.0384  28  ARG B CA  
587  C C   . ARG B 19  ? 0.8661 0.9020 0.8063 0.0806 0.0549  0.0417  28  ARG B C   
588  O O   . ARG B 19  ? 0.8801 0.9129 0.8271 0.0792 0.0535  0.0470  28  ARG B O   
589  C CB  . ARG B 19  ? 0.9359 0.9669 0.8677 0.0879 0.0518  0.0318  28  ARG B CB  
590  C CG  . ARG B 19  ? 1.0080 1.0392 0.9315 0.0938 0.0521  0.0283  28  ARG B CG  
591  C CD  . ARG B 19  ? 1.0819 1.1084 1.0055 0.0978 0.0499  0.0285  28  ARG B CD  
592  N NE  . ARG B 19  ? 1.1306 1.1575 1.0472 0.1029 0.0492  0.0229  28  ARG B NE  
593  C CZ  . ARG B 19  ? 1.2149 1.2428 1.1305 0.1022 0.0469  0.0135  28  ARG B CZ  
594  N NH1 . ARG B 19  ? 1.1900 1.2188 1.1105 0.0970 0.0453  0.0083  28  ARG B NH1 
595  N NH2 . ARG B 19  ? 1.2434 1.2720 1.1531 0.1069 0.0462  0.0094  28  ARG B NH2 
596  N N   . ARG B 20  ? 0.9316 0.9711 0.8715 0.0773 0.0559  0.0397  29  ARG B N   
597  C CA  . ARG B 20  ? 1.0037 1.0439 0.9513 0.0714 0.0549  0.0410  29  ARG B CA  
598  C C   . ARG B 20  ? 1.0034 1.0462 0.9565 0.0707 0.0570  0.0520  29  ARG B C   
599  O O   . ARG B 20  ? 0.9926 1.0348 0.9543 0.0658 0.0552  0.0543  29  ARG B O   
600  C CB  . ARG B 20  ? 1.0252 1.0690 0.9688 0.0694 0.0559  0.0359  29  ARG B CB  
601  C CG  . ARG B 20  ? 1.1046 1.1485 1.0543 0.0636 0.0539  0.0334  29  ARG B CG  
602  C CD  . ARG B 20  ? 1.1857 1.2339 1.1311 0.0622 0.0559  0.0318  29  ARG B CD  
603  N NE  . ARG B 20  ? 1.2582 1.3106 1.2023 0.0639 0.0593  0.0395  29  ARG B NE  
604  C CZ  . ARG B 20  ? 1.3237 1.3794 1.2721 0.0609 0.0600  0.0435  29  ARG B CZ  
605  N NH1 . ARG B 20  ? 1.3519 1.4066 1.3064 0.0559 0.0574  0.0404  29  ARG B NH1 
606  N NH2 . ARG B 20  ? 1.2737 1.3342 1.2205 0.0635 0.0632  0.0505  29  ARG B NH2 
607  N N   . LEU B 21  ? 0.9752 1.0215 0.9236 0.0756 0.0606  0.0585  30  LEU B N   
608  C CA  . LEU B 21  ? 0.9439 0.9939 0.8973 0.0758 0.0630  0.0699  30  LEU B CA  
609  C C   . LEU B 21  ? 0.9181 0.9643 0.8727 0.0787 0.0624  0.0746  30  LEU B C   
610  O O   . LEU B 21  ? 0.9133 0.9532 0.8662 0.0796 0.0592  0.0680  30  LEU B O   
611  C CB  . LEU B 21  ? 0.9445 1.0018 0.8912 0.0800 0.0675  0.0739  30  LEU B CB  
612  C CG  . LEU B 21  ? 0.9770 1.0393 0.9261 0.0764 0.0685  0.0742  30  LEU B CG  
613  C CD1 . LEU B 21  ? 0.9739 1.0323 0.9243 0.0714 0.0652  0.0647  30  LEU B CD1 
614  C CD2 . LEU B 21  ? 0.9842 1.0522 0.9239 0.0818 0.0721  0.0755  30  LEU B CD2 
615  N N   . LEU B 22  ? 0.9033 0.9534 0.8607 0.0803 0.0652  0.0856  31  LEU B N   
616  C CA  . LEU B 22  ? 0.8797 0.9269 0.8374 0.0836 0.0652  0.0920  31  LEU B CA  
617  C C   . LEU B 22  ? 0.8586 0.9045 0.8046 0.0911 0.0663  0.0876  31  LEU B C   
618  O O   . LEU B 22  ? 0.8807 0.9315 0.8188 0.0950 0.0690  0.0856  31  LEU B O   
619  C CB  . LEU B 22  ? 0.8617 0.9162 0.8236 0.0841 0.0691  0.1053  31  LEU B CB  
620  C CG  . LEU B 22  ? 0.8521 0.9041 0.8154 0.0866 0.0694  0.1138  31  LEU B CG  
621  C CD1 . LEU B 22  ? 0.8368 0.8816 0.8117 0.0798 0.0647  0.1162  31  LEU B CD1 
622  C CD2 . LEU B 22  ? 0.8471 0.9094 0.8098 0.0902 0.0750  0.1260  31  LEU B CD2 
623  N N   . GLY B 23  ? 0.8399 0.8791 0.7849 0.0933 0.0637  0.0860  32  GLY B N   
624  C CA  . GLY B 23  ? 0.8023 0.8398 0.7370 0.1004 0.0639  0.0810  32  GLY B CA  
625  C C   . GLY B 23  ? 0.7637 0.8020 0.6917 0.1011 0.0633  0.0703  32  GLY B C   
626  O O   . GLY B 23  ? 0.7758 0.8131 0.7081 0.0955 0.0612  0.0642  32  GLY B O   
627  N N   . SER B 24  ? 0.7537 0.7934 0.6717 0.1078 0.0646  0.0678  33  SER B N   
628  C CA  . SER B 24  ? 0.7485 0.7896 0.6593 0.1091 0.0643  0.0593  33  SER B CA  
629  C C   . SER B 24  ? 0.7351 0.7826 0.6414 0.1115 0.0680  0.0641  33  SER B C   
630  O O   . SER B 24  ? 0.7078 0.7581 0.6096 0.1176 0.0706  0.0709  33  SER B O   
631  C CB  . SER B 24  ? 0.7576 0.7959 0.6608 0.1148 0.0626  0.0537  33  SER B CB  
632  O OG  . SER B 24  ? 0.7915 0.8246 0.6989 0.1123 0.0589  0.0477  33  SER B OG  
633  N N   . THR B 25  ? 0.6980 0.7478 0.6051 0.1073 0.0682  0.0608  34  THR B N   
634  C CA  . THR B 25  ? 0.7005 0.7562 0.6036 0.1095 0.0713  0.0650  34  THR B CA  
635  C C   . THR B 25  ? 0.6951 0.7497 0.5892 0.1116 0.0701  0.0570  34  THR B C   
636  O O   . THR B 25  ? 0.7088 0.7604 0.6044 0.1069 0.0675  0.0492  34  THR B O   
637  C CB  . THR B 25  ? 0.7185 0.7778 0.6304 0.1031 0.0724  0.0692  34  THR B CB  
638  O OG1 . THR B 25  ? 0.7342 0.7945 0.6545 0.1014 0.0733  0.0776  34  THR B OG1 
639  C CG2 . THR B 25  ? 0.7129 0.7787 0.6207 0.1056 0.0753  0.0727  34  THR B CG2 
640  N N   . GLN B 26  ? 0.6865 0.7435 0.5713 0.1187 0.0716  0.0589  35  GLN B N   
641  C CA  . GLN B 26  ? 0.6638 0.7188 0.5397 0.1208 0.0697  0.0515  35  GLN B CA  
642  C C   . GLN B 26  ? 0.6799 0.7379 0.5566 0.1173 0.0708  0.0521  35  GLN B C   
643  O O   . GLN B 26  ? 0.6889 0.7522 0.5650 0.1205 0.0737  0.0593  35  GLN B O   
644  C CB  . GLN B 26  ? 0.6503 0.7054 0.5153 0.1304 0.0699  0.0524  35  GLN B CB  
645  C CG  . GLN B 26  ? 0.6484 0.7003 0.5044 0.1324 0.0671  0.0450  35  GLN B CG  
646  C CD  . GLN B 26  ? 0.6404 0.6914 0.4852 0.1425 0.0663  0.0451  35  GLN B CD  
647  O OE1 . GLN B 26  ? 0.6827 0.7321 0.5256 0.1467 0.0656  0.0448  35  GLN B OE1 
648  N NE2 . GLN B 26  ? 0.6178 0.6692 0.4544 0.1466 0.0659  0.0445  35  GLN B NE2 
649  N N   . VAL B 27  ? 0.6463 0.7016 0.5247 0.1111 0.0686  0.0454  36  VAL B N   
650  C CA  . VAL B 27  ? 0.6220 0.6795 0.5010 0.1075 0.0692  0.0456  36  VAL B CA  
651  C C   . VAL B 27  ? 0.5901 0.6456 0.4580 0.1118 0.0678  0.0418  36  VAL B C   
652  O O   . VAL B 27  ? 0.5780 0.6356 0.4435 0.1119 0.0686  0.0433  36  VAL B O   
653  C CB  . VAL B 27  ? 0.6539 0.7098 0.5408 0.0986 0.0677  0.0411  36  VAL B CB  
654  C CG1 . VAL B 27  ? 0.6670 0.7253 0.5649 0.0946 0.0689  0.0463  36  VAL B CG1 
655  C CG2 . VAL B 27  ? 0.6314 0.6829 0.5176 0.0961 0.0646  0.0329  36  VAL B CG2 
656  N N   . GLY B 28  ? 0.5515 0.6028 0.4128 0.1152 0.0653  0.0367  37  GLY B N   
657  C CA  . GLY B 28  ? 0.5264 0.5746 0.3769 0.1198 0.0631  0.0333  37  GLY B CA  
658  C C   . GLY B 28  ? 0.5155 0.5589 0.3608 0.1226 0.0598  0.0277  37  GLY B C   
659  O O   . GLY B 28  ? 0.5392 0.5830 0.3882 0.1232 0.0601  0.0280  37  GLY B O   
660  N N   . VAL B 29  ? 0.5084 0.5473 0.3464 0.1232 0.0563  0.0223  38  VAL B N   
661  C CA  . VAL B 29  ? 0.5095 0.5436 0.3404 0.1274 0.0523  0.0170  38  VAL B CA  
662  C C   . VAL B 29  ? 0.5156 0.5454 0.3455 0.1210 0.0487  0.0106  38  VAL B C   
663  O O   . VAL B 29  ? 0.5421 0.5724 0.3734 0.1166 0.0495  0.0115  38  VAL B O   
664  C CB  . VAL B 29  ? 0.5174 0.5502 0.3371 0.1378 0.0515  0.0192  38  VAL B CB  
665  C CG1 . VAL B 29  ? 0.5297 0.5570 0.3418 0.1426 0.0467  0.0137  38  VAL B CG1 
666  C CG2 . VAL B 29  ? 0.5134 0.5520 0.3336 0.1441 0.0558  0.0269  38  VAL B CG2 
667  N N   . GLY B 30  ? 0.5171 0.5431 0.3445 0.1209 0.0446  0.0049  39  GLY B N   
668  C CA  . GLY B 30  ? 0.4997 0.5214 0.3250 0.1156 0.0406  -0.0004 39  GLY B CA  
669  C C   . GLY B 30  ? 0.5089 0.5264 0.3296 0.1183 0.0357  -0.0055 39  GLY B C   
670  O O   . GLY B 30  ? 0.5362 0.5540 0.3547 0.1250 0.0355  -0.0051 39  GLY B O   
671  N N   . VAL B 31  ? 0.5117 0.5251 0.3306 0.1134 0.0316  -0.0098 40  VAL B N   
672  C CA  . VAL B 31  ? 0.5241 0.5325 0.3384 0.1149 0.0257  -0.0150 40  VAL B CA  
673  C C   . VAL B 31  ? 0.5318 0.5429 0.3543 0.1059 0.0245  -0.0192 40  VAL B C   
674  O O   . VAL B 31  ? 0.5271 0.5398 0.3538 0.0977 0.0256  -0.0192 40  VAL B O   
675  C CB  . VAL B 31  ? 0.5407 0.5412 0.3458 0.1165 0.0210  -0.0162 40  VAL B CB  
676  C CG1 . VAL B 31  ? 0.5594 0.5545 0.3612 0.1167 0.0143  -0.0216 40  VAL B CG1 
677  C CG2 . VAL B 31  ? 0.5538 0.5524 0.3501 0.1263 0.0221  -0.0124 40  VAL B CG2 
678  N N   . MET B 32  ? 0.5313 0.5436 0.3558 0.1076 0.0222  -0.0226 41  MET B N   
679  C CA  . MET B 32  ? 0.5511 0.5667 0.3827 0.1000 0.0201  -0.0272 41  MET B CA  
680  C C   . MET B 32  ? 0.5700 0.5793 0.3963 0.0997 0.0133  -0.0309 41  MET B C   
681  O O   . MET B 32  ? 0.5639 0.5685 0.3835 0.1076 0.0098  -0.0321 41  MET B O   
682  C CB  . MET B 32  ? 0.5637 0.5848 0.4012 0.1020 0.0217  -0.0286 41  MET B CB  
683  C CG  . MET B 32  ? 0.5779 0.6050 0.4240 0.0947 0.0206  -0.0330 41  MET B CG  
684  S SD  . MET B 32  ? 0.6033 0.6371 0.4579 0.0849 0.0252  -0.0319 41  MET B SD  
685  C CE  . MET B 32  ? 0.5944 0.6312 0.4525 0.0892 0.0306  -0.0283 41  MET B CE  
686  N N   . GLN B 33  ? 0.5810 0.5895 0.4095 0.0913 0.0111  -0.0324 42  GLN B N   
687  C CA  . GLN B 33  ? 0.6121 0.6141 0.4366 0.0898 0.0039  -0.0357 42  GLN B CA  
688  C C   . GLN B 33  ? 0.6443 0.6512 0.4770 0.0789 0.0029  -0.0378 42  GLN B C   
689  O O   . GLN B 33  ? 0.6219 0.6329 0.4588 0.0723 0.0067  -0.0358 42  GLN B O   
690  C CB  . GLN B 33  ? 0.6435 0.6357 0.4581 0.0923 0.0008  -0.0341 42  GLN B CB  
691  C CG  . GLN B 33  ? 0.6844 0.6683 0.4940 0.0924 -0.0076 -0.0377 42  GLN B CG  
692  C CD  . GLN B 33  ? 0.7437 0.7165 0.5413 0.0987 -0.0118 -0.0370 42  GLN B CD  
693  O OE1 . GLN B 33  ? 0.8046 0.7700 0.5989 0.0942 -0.0169 -0.0377 42  GLN B OE1 
694  N NE2 . GLN B 33  ? 0.7285 0.7002 0.5192 0.1093 -0.0096 -0.0351 42  GLN B NE2 
695  N N   . GLU B 34  ? 0.6994 0.7062 0.5342 0.0769 -0.0022 -0.0415 43  GLU B N   
696  C CA  . GLU B 34  ? 0.7092 0.7225 0.5527 0.0662 -0.0031 -0.0430 43  GLU B CA  
697  C C   . GLU B 34  ? 0.6850 0.7095 0.5371 0.0617 0.0039  -0.0418 43  GLU B C   
698  O O   . GLU B 34  ? 0.6527 0.6812 0.5090 0.0532 0.0052  -0.0408 43  GLU B O   
699  C CB  . GLU B 34  ? 0.7578 0.7637 0.5973 0.0601 -0.0068 -0.0415 43  GLU B CB  
700  C CG  . GLU B 34  ? 0.8087 0.8030 0.6405 0.0634 -0.0152 -0.0434 43  GLU B CG  
701  C CD  . GLU B 34  ? 0.8397 0.8227 0.6630 0.0622 -0.0187 -0.0413 43  GLU B CD  
702  O OE1 . GLU B 34  ? 0.8443 0.8272 0.6709 0.0528 -0.0204 -0.0402 43  GLU B OE1 
703  O OE2 . GLU B 34  ? 0.8770 0.8513 0.6902 0.0710 -0.0201 -0.0406 43  GLU B OE2 
704  N N   . GLY B 35  ? 0.6416 0.6708 0.4960 0.0671 0.0082  -0.0417 44  GLY B N   
705  C CA  . GLY B 35  ? 0.6191 0.6587 0.4819 0.0633 0.0137  -0.0416 44  GLY B CA  
706  C C   . GLY B 35  ? 0.6132 0.6525 0.4752 0.0614 0.0186  -0.0378 44  GLY B C   
707  O O   . GLY B 35  ? 0.6026 0.6498 0.4712 0.0586 0.0228  -0.0379 44  GLY B O   
708  N N   . VAL B 36  ? 0.5981 0.6289 0.4524 0.0633 0.0178  -0.0349 45  VAL B N   
709  C CA  . VAL B 36  ? 0.5618 0.5916 0.4145 0.0623 0.0219  -0.0310 45  VAL B CA  
710  C C   . VAL B 36  ? 0.5436 0.5694 0.3912 0.0712 0.0239  -0.0282 45  VAL B C   
711  O O   . VAL B 36  ? 0.5596 0.5790 0.4002 0.0778 0.0205  -0.0284 45  VAL B O   
712  C CB  . VAL B 36  ? 0.5766 0.6007 0.4246 0.0572 0.0195  -0.0296 45  VAL B CB  
713  C CG1 . VAL B 36  ? 0.5846 0.6064 0.4294 0.0578 0.0230  -0.0258 45  VAL B CG1 
714  C CG2 . VAL B 36  ? 0.5902 0.6203 0.4444 0.0475 0.0189  -0.0311 45  VAL B CG2 
715  N N   . PHE B 37  ? 0.5078 0.5376 0.3591 0.0714 0.0289  -0.0256 46  PHE B N   
716  C CA  . PHE B 37  ? 0.5064 0.5341 0.3545 0.0786 0.0316  -0.0217 46  PHE B CA  
717  C C   . PHE B 37  ? 0.4987 0.5230 0.3424 0.0776 0.0329  -0.0182 46  PHE B C   
718  O O   . PHE B 37  ? 0.4912 0.5181 0.3385 0.0712 0.0347  -0.0178 46  PHE B O   
719  C CB  . PHE B 37  ? 0.4909 0.5247 0.3463 0.0791 0.0357  -0.0207 46  PHE B CB  
720  C CG  . PHE B 37  ? 0.4961 0.5281 0.3487 0.0866 0.0380  -0.0163 46  PHE B CG  
721  C CD1 . PHE B 37  ? 0.5084 0.5371 0.3554 0.0944 0.0362  -0.0161 46  PHE B CD1 
722  C CD2 . PHE B 37  ? 0.5001 0.5340 0.3556 0.0860 0.0419  -0.0122 46  PHE B CD2 
723  C CE1 . PHE B 37  ? 0.5215 0.5499 0.3661 0.1013 0.0387  -0.0113 46  PHE B CE1 
724  C CE2 . PHE B 37  ? 0.5053 0.5385 0.3588 0.0923 0.0441  -0.0073 46  PHE B CE2 
725  C CZ  . PHE B 37  ? 0.5184 0.5493 0.3666 0.1001 0.0428  -0.0066 46  PHE B CZ  
726  N N   . HIS B 38  ? 0.4929 0.5117 0.3286 0.0846 0.0318  -0.0158 47  HIS B N   
727  C CA  . HIS B 38  ? 0.4912 0.5059 0.3210 0.0855 0.0321  -0.0127 47  HIS B CA  
728  C C   . HIS B 38  ? 0.4985 0.5156 0.3279 0.0918 0.0361  -0.0079 47  HIS B C   
729  O O   . HIS B 38  ? 0.4910 0.5075 0.3172 0.0992 0.0359  -0.0070 47  HIS B O   
730  C CB  . HIS B 38  ? 0.4979 0.5043 0.3180 0.0891 0.0268  -0.0142 47  HIS B CB  
731  C CG  . HIS B 38  ? 0.5071 0.5105 0.3275 0.0836 0.0219  -0.0185 47  HIS B CG  
732  N ND1 . HIS B 38  ? 0.5187 0.5239 0.3421 0.0838 0.0197  -0.0219 47  HIS B ND1 
733  C CD2 . HIS B 38  ? 0.5299 0.5286 0.3477 0.0778 0.0184  -0.0196 47  HIS B CD2 
734  C CE1 . HIS B 38  ? 0.5279 0.5301 0.3513 0.0782 0.0151  -0.0248 47  HIS B CE1 
735  N NE2 . HIS B 38  ? 0.5372 0.5353 0.3573 0.0740 0.0143  -0.0233 47  HIS B NE2 
736  N N   . THR B 39  ? 0.5039 0.5242 0.3370 0.0889 0.0397  -0.0048 48  THR B N   
737  C CA  . THR B 39  ? 0.5293 0.5522 0.3620 0.0944 0.0433  0.0004  48  THR B CA  
738  C C   . THR B 39  ? 0.5508 0.5731 0.3813 0.0926 0.0443  0.0029  48  THR B C   
739  O O   . THR B 39  ? 0.5474 0.5661 0.3756 0.0876 0.0419  0.0004  48  THR B O   
740  C CB  . THR B 39  ? 0.5319 0.5606 0.3734 0.0938 0.0469  0.0022  48  THR B CB  
741  O OG1 . THR B 39  ? 0.5539 0.5852 0.3949 0.0996 0.0499  0.0081  48  THR B OG1 
742  C CG2 . THR B 39  ? 0.5291 0.5617 0.3794 0.0856 0.0487  0.0012  48  THR B CG2 
743  N N   . MET B 40  ? 0.5729 0.5989 0.4043 0.0967 0.0477  0.0081  49  MET B N   
744  C CA  . MET B 40  ? 0.5826 0.6098 0.4137 0.0953 0.0493  0.0110  49  MET B CA  
745  C C   . MET B 40  ? 0.5765 0.6090 0.4182 0.0880 0.0523  0.0118  49  MET B C   
746  O O   . MET B 40  ? 0.5697 0.6060 0.4185 0.0875 0.0543  0.0128  49  MET B O   
747  C CB  . MET B 40  ? 0.5963 0.6262 0.4235 0.1037 0.0513  0.0163  49  MET B CB  
748  C CG  . MET B 40  ? 0.6288 0.6544 0.4457 0.1126 0.0486  0.0154  49  MET B CG  
749  S SD  . MET B 40  ? 0.6936 0.7196 0.5013 0.1209 0.0488  0.0193  49  MET B SD  
750  C CE  . MET B 40  ? 0.6839 0.7005 0.4842 0.1170 0.0434  0.0141  49  MET B CE  
751  N N   A TRP B 41  ? 0.5797 0.6117 0.4218 0.0830 0.0521  0.0112  50  TRP B N   
752  N N   B TRP B 41  ? 0.5721 0.6041 0.4142 0.0830 0.0521  0.0113  50  TRP B N   
753  N N   C TRP B 41  ? 0.5797 0.6117 0.4218 0.0830 0.0521  0.0112  50  TRP B N   
754  N N   D TRP B 41  ? 0.5721 0.6041 0.4142 0.0830 0.0521  0.0113  50  TRP B N   
755  C CA  A TRP B 41  ? 0.5749 0.6111 0.4260 0.0759 0.0540  0.0110  50  TRP B CA  
756  C CA  B TRP B 41  ? 0.5625 0.5987 0.4137 0.0760 0.0540  0.0110  50  TRP B CA  
757  C CA  C TRP B 41  ? 0.5749 0.6111 0.4260 0.0759 0.0540  0.0110  50  TRP B CA  
758  C CA  D TRP B 41  ? 0.5625 0.5987 0.4137 0.0760 0.0540  0.0110  50  TRP B CA  
759  C C   A TRP B 41  ? 0.5685 0.6103 0.4269 0.0777 0.0574  0.0159  50  TRP B C   
760  C C   B TRP B 41  ? 0.5612 0.6031 0.4197 0.0777 0.0574  0.0159  50  TRP B C   
761  C C   C TRP B 41  ? 0.5685 0.6103 0.4269 0.0777 0.0574  0.0159  50  TRP B C   
762  C C   D TRP B 41  ? 0.5612 0.6031 0.4197 0.0777 0.0574  0.0159  50  TRP B C   
763  O O   A TRP B 41  ? 0.5555 0.6003 0.4224 0.0737 0.0584  0.0152  50  TRP B O   
764  O O   B TRP B 41  ? 0.5482 0.5931 0.4152 0.0736 0.0585  0.0153  50  TRP B O   
765  O O   C TRP B 41  ? 0.5555 0.6003 0.4224 0.0737 0.0584  0.0152  50  TRP B O   
766  O O   D TRP B 41  ? 0.5482 0.5931 0.4152 0.0736 0.0585  0.0153  50  TRP B O   
767  C CB  A TRP B 41  ? 0.5841 0.6184 0.4325 0.0718 0.0532  0.0103  50  TRP B CB  
768  C CB  B TRP B 41  ? 0.5626 0.5969 0.4114 0.0713 0.0531  0.0099  50  TRP B CB  
769  C CB  C TRP B 41  ? 0.5841 0.6184 0.4325 0.0718 0.0532  0.0103  50  TRP B CB  
770  C CB  D TRP B 41  ? 0.5626 0.5969 0.4114 0.0713 0.0531  0.0099  50  TRP B CB  
771  C CG  A TRP B 41  ? 0.5881 0.6261 0.4444 0.0648 0.0544  0.0090  50  TRP B CG  
772  C CG  B TRP B 41  ? 0.5567 0.5954 0.4141 0.0651 0.0548  0.0093  50  TRP B CG  
773  C CG  C TRP B 41  ? 0.5881 0.6261 0.4444 0.0648 0.0544  0.0090  50  TRP B CG  
774  C CG  D TRP B 41  ? 0.5567 0.5954 0.4141 0.0651 0.0548  0.0093  50  TRP B CG  
775  C CD1 A TRP B 41  ? 0.5918 0.6294 0.4496 0.0586 0.0532  0.0047  50  TRP B CD1 
776  C CD1 B TRP B 41  ? 0.5511 0.5943 0.4151 0.0650 0.0572  0.0128  50  TRP B CD1 
777  C CD1 C TRP B 41  ? 0.5918 0.6294 0.4496 0.0586 0.0532  0.0047  50  TRP B CD1 
778  C CD1 D TRP B 41  ? 0.5511 0.5943 0.4151 0.0650 0.0572  0.0128  50  TRP B CD1 
779  C CD2 A TRP B 41  ? 0.5887 0.6316 0.4525 0.0634 0.0568  0.0119  50  TRP B CD2 
780  C CD2 B TRP B 41  ? 0.5566 0.5959 0.4173 0.0584 0.0540  0.0051  50  TRP B CD2 
781  C CD2 C TRP B 41  ? 0.5887 0.6316 0.4525 0.0634 0.0568  0.0119  50  TRP B CD2 
782  C CD2 D TRP B 41  ? 0.5566 0.5959 0.4173 0.0584 0.0540  0.0051  50  TRP B CD2 
783  N NE1 A TRP B 41  ? 0.5942 0.6359 0.4590 0.0543 0.0547  0.0044  50  TRP B NE1 
784  N NE1 B TRP B 41  ? 0.5497 0.5953 0.4203 0.0590 0.0575  0.0105  50  TRP B NE1 
785  N NE1 C TRP B 41  ? 0.5942 0.6359 0.4590 0.0543 0.0547  0.0044  50  TRP B NE1 
786  N NE1 D TRP B 41  ? 0.5497 0.5953 0.4203 0.0590 0.0575  0.0105  50  TRP B NE1 
787  C CE2 A TRP B 41  ? 0.5943 0.6387 0.4631 0.0569 0.0566  0.0086  50  TRP B CE2 
788  C CE2 B TRP B 41  ? 0.5528 0.5965 0.4212 0.0552 0.0558  0.0057  50  TRP B CE2 
789  C CE2 C TRP B 41  ? 0.5943 0.6387 0.4631 0.0569 0.0566  0.0086  50  TRP B CE2 
790  C CE2 D TRP B 41  ? 0.5528 0.5965 0.4212 0.0552 0.0558  0.0057  50  TRP B CE2 
791  C CE3 A TRP B 41  ? 0.5975 0.6441 0.4646 0.0670 0.0590  0.0171  50  TRP B CE3 
792  C CE3 B TRP B 41  ? 0.5603 0.5975 0.4184 0.0550 0.0519  0.0009  50  TRP B CE3 
793  C CE3 C TRP B 41  ? 0.5975 0.6441 0.4646 0.0670 0.0590  0.0171  50  TRP B CE3 
794  C CE3 D TRP B 41  ? 0.5603 0.5975 0.4184 0.0550 0.0519  0.0009  50  TRP B CE3 
795  C CZ2 A TRP B 41  ? 0.5974 0.6458 0.4738 0.0542 0.0579  0.0098  50  TRP B CZ2 
796  C CZ2 B TRP B 41  ? 0.5480 0.5939 0.4206 0.0494 0.0555  0.0020  50  TRP B CZ2 
797  C CZ2 C TRP B 41  ? 0.5974 0.6458 0.4738 0.0542 0.0579  0.0098  50  TRP B CZ2 
798  C CZ2 D TRP B 41  ? 0.5480 0.5939 0.4206 0.0494 0.0555  0.0020  50  TRP B CZ2 
799  C CZ3 A TRP B 41  ? 0.5942 0.6449 0.4697 0.0636 0.0603  0.0187  50  TRP B CZ3 
800  C CZ3 B TRP B 41  ? 0.5551 0.5955 0.4179 0.0488 0.0522  -0.0021 50  TRP B CZ3 
801  C CZ3 C TRP B 41  ? 0.5942 0.6449 0.4697 0.0636 0.0603  0.0187  50  TRP B CZ3 
802  C CZ3 D TRP B 41  ? 0.5551 0.5955 0.4179 0.0488 0.0522  -0.0021 50  TRP B CZ3 
803  C CH2 A TRP B 41  ? 0.5956 0.6467 0.4756 0.0574 0.0595  0.0148  50  TRP B CH2 
804  C CH2 B TRP B 41  ? 0.5498 0.5945 0.4193 0.0465 0.0540  -0.0017 50  TRP B CH2 
805  C CH2 C TRP B 41  ? 0.5956 0.6467 0.4756 0.0574 0.0595  0.0148  50  TRP B CH2 
806  C CH2 D TRP B 41  ? 0.5498 0.5945 0.4193 0.0465 0.0540  -0.0017 50  TRP B CH2 
807  N N   . HIS B 42  ? 0.5703 0.6140 0.4259 0.0836 0.0589  0.0208  51  HIS B N   
808  C CA  . HIS B 42  ? 0.5838 0.6338 0.4471 0.0848 0.0621  0.0266  51  HIS B CA  
809  C C   . HIS B 42  ? 0.5982 0.6497 0.4665 0.0864 0.0632  0.0279  51  HIS B C   
810  O O   . HIS B 42  ? 0.6092 0.6650 0.4858 0.0852 0.0653  0.0321  51  HIS B O   
811  C CB  . HIS B 42  ? 0.5723 0.6256 0.4318 0.0907 0.0637  0.0320  51  HIS B CB  
812  C CG  . HIS B 42  ? 0.5830 0.6363 0.4356 0.0992 0.0640  0.0343  51  HIS B CG  
813  N ND1 . HIS B 42  ? 0.5834 0.6316 0.4245 0.1044 0.0614  0.0317  51  HIS B ND1 
814  C CD2 . HIS B 42  ? 0.5959 0.6532 0.4508 0.1039 0.0663  0.0388  51  HIS B CD2 
815  C CE1 . HIS B 42  ? 0.5840 0.6334 0.4205 0.1122 0.0620  0.0341  51  HIS B CE1 
816  N NE2 . HIS B 42  ? 0.5766 0.6318 0.4214 0.1121 0.0652  0.0387  51  HIS B NE2 
817  N N   . VAL B 43  ? 0.6058 0.6537 0.4698 0.0886 0.0614  0.0244  52  VAL B N   
818  C CA  . VAL B 43  ? 0.6163 0.6650 0.4840 0.0906 0.0620  0.0250  52  VAL B CA  
819  C C   . VAL B 43  ? 0.6031 0.6521 0.4795 0.0838 0.0614  0.0216  52  VAL B C   
820  O O   . VAL B 43  ? 0.6099 0.6613 0.4937 0.0833 0.0628  0.0248  52  VAL B O   
821  C CB  . VAL B 43  ? 0.6251 0.6697 0.4842 0.0959 0.0598  0.0220  52  VAL B CB  
822  C CG1 . VAL B 43  ? 0.6463 0.6909 0.5084 0.0977 0.0597  0.0213  52  VAL B CG1 
823  C CG2 . VAL B 43  ? 0.6385 0.6830 0.4888 0.1039 0.0601  0.0254  52  VAL B CG2 
824  N N   . THR B 44  ? 0.5981 0.6449 0.4736 0.0789 0.0593  0.0155  53  THR B N   
825  C CA  . THR B 44  ? 0.5899 0.6375 0.4721 0.0734 0.0585  0.0111  53  THR B CA  
826  C C   . THR B 44  ? 0.5992 0.6488 0.4867 0.0677 0.0589  0.0108  53  THR B C   
827  O O   . THR B 44  ? 0.5980 0.6491 0.4926 0.0642 0.0586  0.0087  53  THR B O   
828  C CB  . THR B 44  ? 0.5662 0.6118 0.4447 0.0721 0.0561  0.0050  53  THR B CB  
829  O OG1 . THR B 44  ? 0.5408 0.5849 0.4145 0.0690 0.0550  0.0030  53  THR B OG1 
830  C CG2 . THR B 44  ? 0.5539 0.5973 0.4269 0.0782 0.0551  0.0051  53  THR B CG2 
831  N N   . LYS B 45  ? 0.6139 0.6632 0.4975 0.0671 0.0593  0.0125  54  LYS B N   
832  C CA  . LYS B 45  ? 0.6785 0.7290 0.5648 0.0617 0.0592  0.0111  54  LYS B CA  
833  C C   . LYS B 45  ? 0.6471 0.6972 0.5330 0.0568 0.0576  0.0048  54  LYS B C   
834  O O   . LYS B 45  ? 0.6792 0.7311 0.5692 0.0525 0.0575  0.0030  54  LYS B O   
835  C CB  . LYS B 45  ? 0.7287 0.7823 0.6244 0.0595 0.0601  0.0135  54  LYS B CB  
836  C CG  . LYS B 45  ? 0.7900 0.8455 0.6887 0.0634 0.0620  0.0204  54  LYS B CG  
837  C CD  . LYS B 45  ? 0.8578 0.9147 0.7524 0.0654 0.0631  0.0242  54  LYS B CD  
838  C CE  . LYS B 45  ? 0.9699 1.0306 0.8681 0.0694 0.0653  0.0316  54  LYS B CE  
839  N NZ  . LYS B 45  ? 1.0668 1.1291 0.9580 0.0742 0.0664  0.0351  54  LYS B NZ  
840  N N   . GLY B 46  ? 0.6322 0.6804 0.5136 0.0577 0.0562  0.0017  55  GLY B N   
841  C CA  . GLY B 46  ? 0.6254 0.6747 0.5069 0.0530 0.0549  -0.0036 55  GLY B CA  
842  C C   . GLY B 46  ? 0.6253 0.6780 0.5137 0.0518 0.0548  -0.0067 55  GLY B C   
843  O O   . GLY B 46  ? 0.6310 0.6861 0.5200 0.0484 0.0540  -0.0111 55  GLY B O   
844  N N   . ALA B 47  ? 0.6508 0.7038 0.5440 0.0549 0.0555  -0.0045 56  ALA B N   
845  C CA  . ALA B 47  ? 0.6275 0.6825 0.5267 0.0549 0.0548  -0.0076 56  ALA B CA  
846  C C   . ALA B 47  ? 0.6263 0.6816 0.5230 0.0566 0.0536  -0.0110 56  ALA B C   
847  O O   . ALA B 47  ? 0.6088 0.6615 0.4997 0.0595 0.0533  -0.0097 56  ALA B O   
848  C CB  . ALA B 47  ? 0.6210 0.6749 0.5252 0.0579 0.0555  -0.0034 56  ALA B CB  
849  N N   . ALA B 48  ? 0.6053 0.6639 0.5064 0.0554 0.0527  -0.0156 57  ALA B N   
850  C CA  . ALA B 48  ? 0.5999 0.6598 0.5005 0.0574 0.0514  -0.0191 57  ALA B CA  
851  C C   . ALA B 48  ? 0.6150 0.6715 0.5155 0.0632 0.0513  -0.0161 57  ALA B C   
852  O O   . ALA B 48  ? 0.6421 0.6963 0.5450 0.0650 0.0524  -0.0116 57  ALA B O   
853  C CB  . ALA B 48  ? 0.6217 0.6868 0.5276 0.0553 0.0506  -0.0244 57  ALA B CB  
854  N N   . LEU B 49  ? 0.5907 0.6472 0.4887 0.0660 0.0500  -0.0184 58  LEU B N   
855  C CA  . LEU B 49  ? 0.6277 0.6811 0.5240 0.0722 0.0497  -0.0159 58  LEU B CA  
856  C C   . LEU B 49  ? 0.6468 0.7024 0.5454 0.0741 0.0479  -0.0207 58  LEU B C   
857  O O   . LEU B 49  ? 0.6994 0.7592 0.5987 0.0712 0.0467  -0.0258 58  LEU B O   
858  C CB  . LEU B 49  ? 0.6022 0.6526 0.4908 0.0752 0.0493  -0.0140 58  LEU B CB  
859  C CG  . LEU B 49  ? 0.5883 0.6364 0.4728 0.0744 0.0506  -0.0098 58  LEU B CG  
860  C CD1 . LEU B 49  ? 0.5847 0.6296 0.4611 0.0773 0.0490  -0.0099 58  LEU B CD1 
861  C CD2 . LEU B 49  ? 0.5840 0.6310 0.4704 0.0772 0.0529  -0.0036 58  LEU B CD2 
862  N N   . ARG B 50  ? 0.6582 0.7114 0.5579 0.0789 0.0476  -0.0189 59  ARG B N   
863  C CA  . ARG B 50  ? 0.6855 0.7402 0.5865 0.0820 0.0456  -0.0231 59  ARG B CA  
864  C C   . ARG B 50  ? 0.6901 0.7424 0.5849 0.0869 0.0446  -0.0224 59  ARG B C   
865  O O   . ARG B 50  ? 0.6714 0.7199 0.5613 0.0899 0.0458  -0.0172 59  ARG B O   
866  C CB  . ARG B 50  ? 0.7700 0.8226 0.6759 0.0840 0.0455  -0.0215 59  ARG B CB  
867  C CG  . ARG B 50  ? 0.8607 0.9143 0.7685 0.0875 0.0433  -0.0258 59  ARG B CG  
868  C CD  . ARG B 50  ? 0.8971 0.9481 0.8102 0.0883 0.0425  -0.0250 59  ARG B CD  
869  N NE  . ARG B 50  ? 0.9212 0.9673 0.8350 0.0885 0.0441  -0.0174 59  ARG B NE  
870  C CZ  . ARG B 50  ? 0.9571 0.9990 0.8686 0.0930 0.0447  -0.0116 59  ARG B CZ  
871  N NH1 . ARG B 50  ? 0.9476 0.9888 0.8551 0.0982 0.0438  -0.0128 59  ARG B NH1 
872  N NH2 . ARG B 50  ? 0.9885 1.0276 0.9019 0.0924 0.0464  -0.0045 59  ARG B NH2 
873  N N   . SER B 51  ? 0.6997 0.7548 0.5942 0.0876 0.0424  -0.0277 60  SER B N   
874  C CA  . SER B 51  ? 0.7558 0.8089 0.6455 0.0932 0.0404  -0.0284 60  SER B CA  
875  C C   . SER B 51  ? 0.7743 0.8306 0.6677 0.0954 0.0384  -0.0334 60  SER B C   
876  O O   . SER B 51  ? 0.8005 0.8626 0.6970 0.0921 0.0369  -0.0389 60  SER B O   
877  C CB  . SER B 51  ? 0.7410 0.7944 0.6262 0.0912 0.0388  -0.0304 60  SER B CB  
878  O OG  . SER B 51  ? 0.7333 0.7848 0.6143 0.0966 0.0361  -0.0320 60  SER B OG  
879  N N   . GLY B 52  ? 0.8375 0.8905 0.7309 0.1008 0.0383  -0.0313 61  GLY B N   
880  C CA  . GLY B 52  ? 0.8983 0.9537 0.7955 0.1032 0.0363  -0.0358 61  GLY B CA  
881  C C   . GLY B 52  ? 0.9325 0.9911 0.8363 0.0990 0.0367  -0.0382 61  GLY B C   
882  O O   . GLY B 52  ? 0.9869 1.0426 0.8925 0.0970 0.0386  -0.0340 61  GLY B O   
883  N N   . GLU B 53  ? 0.9841 1.0493 0.8917 0.0977 0.0350  -0.0448 62  GLU B N   
884  C CA  . GLU B 53  ? 1.0294 1.0991 0.9425 0.0934 0.0355  -0.0478 62  GLU B CA  
885  C C   . GLU B 53  ? 0.9771 1.0529 0.8906 0.0870 0.0367  -0.0494 62  GLU B C   
886  O O   . GLU B 53  ? 1.0285 1.1081 0.9455 0.0833 0.0375  -0.0512 62  GLU B O   
887  C CB  . GLU B 53  ? 1.0811 1.1543 0.9980 0.0968 0.0330  -0.0535 62  GLU B CB  
888  C CG  . GLU B 53  ? 1.1884 1.2537 1.1060 0.1009 0.0322  -0.0505 62  GLU B CG  
889  C CD  . GLU B 53  ? 1.2872 1.3543 1.2089 0.1033 0.0296  -0.0558 62  GLU B CD  
890  O OE1 . GLU B 53  ? 1.3615 1.4366 1.2848 0.1042 0.0281  -0.0623 62  GLU B OE1 
891  O OE2 . GLU B 53  ? 1.3563 1.4169 1.2798 0.1045 0.0287  -0.0533 62  GLU B OE2 
892  N N   . GLY B 54  ? 0.9467 1.0222 0.8560 0.0860 0.0367  -0.0483 63  GLY B N   
893  C CA  . GLY B 54  ? 0.9124 0.9914 0.8210 0.0798 0.0376  -0.0483 63  GLY B CA  
894  C C   . GLY B 54  ? 0.8705 0.9454 0.7779 0.0766 0.0400  -0.0437 63  GLY B C   
895  O O   . GLY B 54  ? 0.8355 0.9041 0.7418 0.0797 0.0410  -0.0393 63  GLY B O   
896  N N   . ARG B 55  ? 0.8070 0.8860 0.7150 0.0705 0.0410  -0.0443 64  ARG B N   
897  C CA  . ARG B 55  ? 0.7995 0.8756 0.7065 0.0670 0.0432  -0.0405 64  ARG B CA  
898  C C   . ARG B 55  ? 0.7455 0.8204 0.6478 0.0632 0.0433  -0.0387 64  ARG B C   
899  O O   . ARG B 55  ? 0.7351 0.8147 0.6375 0.0604 0.0420  -0.0416 64  ARG B O   
900  C CB  . ARG B 55  ? 0.8473 0.9290 0.7590 0.0633 0.0441  -0.0431 64  ARG B CB  
901  C CG  . ARG B 55  ? 0.8902 0.9683 0.8014 0.0607 0.0459  -0.0393 64  ARG B CG  
902  C CD  . ARG B 55  ? 0.9567 1.0413 0.8712 0.0565 0.0466  -0.0425 64  ARG B CD  
903  N NE  . ARG B 55  ? 0.9669 1.0490 0.8807 0.0535 0.0480  -0.0396 64  ARG B NE  
904  C CZ  . ARG B 55  ? 0.9920 1.0734 0.9092 0.0535 0.0480  -0.0398 64  ARG B CZ  
905  N NH1 . ARG B 55  ? 0.9839 1.0662 0.9051 0.0565 0.0464  -0.0429 64  ARG B NH1 
906  N NH2 . ARG B 55  ? 1.0086 1.0881 0.9249 0.0505 0.0490  -0.0372 64  ARG B NH2 
907  N N   . LEU B 56  ? 0.6943 0.7633 0.5929 0.0632 0.0445  -0.0339 65  LEU B N   
908  C CA  . LEU B 56  ? 0.6836 0.7496 0.5766 0.0605 0.0441  -0.0319 65  LEU B CA  
909  C C   . LEU B 56  ? 0.6522 0.7188 0.5459 0.0559 0.0461  -0.0301 65  LEU B C   
910  O O   . LEU B 56  ? 0.6584 0.7219 0.5527 0.0578 0.0477  -0.0267 65  LEU B O   
911  C CB  . LEU B 56  ? 0.6811 0.7396 0.5680 0.0659 0.0436  -0.0279 65  LEU B CB  
912  C CG  . LEU B 56  ? 0.7207 0.7773 0.6054 0.0717 0.0415  -0.0291 65  LEU B CG  
913  C CD1 . LEU B 56  ? 0.7160 0.7659 0.5928 0.0758 0.0404  -0.0259 65  LEU B CD1 
914  C CD2 . LEU B 56  ? 0.7354 0.7971 0.6226 0.0697 0.0390  -0.0344 65  LEU B CD2 
915  N N   . ASP B 57  ? 0.6265 0.6971 0.5203 0.0502 0.0460  -0.0319 66  ASP B N   
916  C CA  . ASP B 57  ? 0.6069 0.6782 0.5006 0.0458 0.0477  -0.0303 66  ASP B CA  
917  C C   . ASP B 57  ? 0.5572 0.6227 0.4443 0.0442 0.0470  -0.0271 66  ASP B C   
918  O O   . ASP B 57  ? 0.5428 0.6068 0.4265 0.0430 0.0449  -0.0278 66  ASP B O   
919  C CB  . ASP B 57  ? 0.6670 0.7468 0.5645 0.0408 0.0482  -0.0340 66  ASP B CB  
920  C CG  . ASP B 57  ? 0.7100 0.7955 0.6136 0.0428 0.0486  -0.0376 66  ASP B CG  
921  O OD1 . ASP B 57  ? 0.7661 0.8488 0.6716 0.0455 0.0492  -0.0365 66  ASP B OD1 
922  O OD2 . ASP B 57  ? 0.7667 0.8595 0.6732 0.0420 0.0479  -0.0415 66  ASP B OD2 
923  N N   . PRO B 58  ? 0.5202 0.5822 0.4053 0.0440 0.0485  -0.0238 67  PRO B N   
924  C CA  . PRO B 58  ? 0.5263 0.5827 0.4047 0.0430 0.0477  -0.0209 67  PRO B CA  
925  C C   . PRO B 58  ? 0.5399 0.5985 0.4168 0.0367 0.0464  -0.0227 67  PRO B C   
926  O O   . PRO B 58  ? 0.5658 0.6318 0.4474 0.0327 0.0474  -0.0253 67  PRO B O   
927  C CB  . PRO B 58  ? 0.5255 0.5804 0.4041 0.0430 0.0497  -0.0178 67  PRO B CB  
928  C CG  . PRO B 58  ? 0.5242 0.5852 0.4101 0.0415 0.0512  -0.0201 67  PRO B CG  
929  C CD  . PRO B 58  ? 0.5213 0.5849 0.4108 0.0443 0.0505  -0.0228 67  PRO B CD  
930  N N   . TYR B 59  ? 0.5140 0.5666 0.3845 0.0361 0.0441  -0.0212 68  TYR B N   
931  C CA  . TYR B 59  ? 0.5121 0.5656 0.3809 0.0298 0.0423  -0.0220 68  TYR B CA  
932  C C   . TYR B 59  ? 0.4996 0.5463 0.3617 0.0283 0.0416  -0.0189 68  TYR B C   
933  O O   . TYR B 59  ? 0.5160 0.5646 0.3776 0.0225 0.0417  -0.0186 68  TYR B O   
934  C CB  . TYR B 59  ? 0.5200 0.5722 0.3879 0.0302 0.0389  -0.0238 68  TYR B CB  
935  C CG  . TYR B 59  ? 0.5165 0.5695 0.3836 0.0233 0.0365  -0.0242 68  TYR B CG  
936  C CD1 . TYR B 59  ? 0.5226 0.5671 0.3827 0.0215 0.0337  -0.0218 68  TYR B CD1 
937  C CD2 . TYR B 59  ? 0.5221 0.5844 0.3955 0.0191 0.0365  -0.0268 68  TYR B CD2 
938  C CE1 . TYR B 59  ? 0.5406 0.5850 0.4000 0.0148 0.0309  -0.0215 68  TYR B CE1 
939  C CE2 . TYR B 59  ? 0.5328 0.5966 0.4062 0.0124 0.0342  -0.0264 68  TYR B CE2 
940  C CZ  . TYR B 59  ? 0.5496 0.6040 0.4161 0.0099 0.0313  -0.0235 68  TYR B CZ  
941  O OH  . TYR B 59  ? 0.5768 0.6320 0.4434 0.0026 0.0287  -0.0225 68  TYR B OH  
942  N N   . TRP B 60  ? 0.4786 0.5178 0.3353 0.0336 0.0407  -0.0167 69  TRP B N   
943  C CA  . TRP B 60  ? 0.4773 0.5090 0.3264 0.0338 0.0393  -0.0139 69  TRP B CA  
944  C C   . TRP B 60  ? 0.4854 0.5146 0.3328 0.0405 0.0411  -0.0113 69  TRP B C   
945  O O   . TRP B 60  ? 0.5102 0.5393 0.3584 0.0463 0.0413  -0.0113 69  TRP B O   
946  C CB  . TRP B 60  ? 0.4741 0.4979 0.3163 0.0332 0.0345  -0.0140 69  TRP B CB  
947  C CG  . TRP B 60  ? 0.4928 0.5082 0.3267 0.0349 0.0328  -0.0114 69  TRP B CG  
948  C CD1 . TRP B 60  ? 0.4988 0.5121 0.3298 0.0301 0.0325  -0.0100 69  TRP B CD1 
949  C CD2 . TRP B 60  ? 0.5052 0.5137 0.3323 0.0427 0.0313  -0.0099 69  TRP B CD2 
950  N NE1 . TRP B 60  ? 0.5135 0.5188 0.3365 0.0344 0.0309  -0.0079 69  TRP B NE1 
951  C CE2 . TRP B 60  ? 0.5131 0.5157 0.3337 0.0423 0.0301  -0.0078 69  TRP B CE2 
952  C CE3 . TRP B 60  ? 0.5146 0.5220 0.3404 0.0505 0.0312  -0.0099 69  TRP B CE3 
953  C CZ2 . TRP B 60  ? 0.5171 0.5132 0.3299 0.0495 0.0286  -0.0062 69  TRP B CZ2 
954  C CZ3 . TRP B 60  ? 0.5197 0.5210 0.3378 0.0576 0.0299  -0.0080 69  TRP B CZ3 
955  C CH2 . TRP B 60  ? 0.5270 0.5230 0.3388 0.0572 0.0286  -0.0062 69  TRP B CH2 
956  N N   . GLY B 61  ? 0.5037 0.5310 0.3484 0.0401 0.0421  -0.0090 70  GLY B N   
957  C CA  . GLY B 61  ? 0.5214 0.5466 0.3638 0.0463 0.0433  -0.0059 70  GLY B CA  
958  C C   . GLY B 61  ? 0.5285 0.5502 0.3658 0.0455 0.0430  -0.0038 70  GLY B C   
959  O O   . GLY B 61  ? 0.5382 0.5605 0.3756 0.0394 0.0428  -0.0046 70  GLY B O   
960  N N   . ASP B 62  ? 0.5334 0.5529 0.3672 0.0516 0.0435  -0.0010 71  ASP B N   
961  C CA  . ASP B 62  ? 0.5521 0.5681 0.3803 0.0527 0.0429  0.0011  71  ASP B CA  
962  C C   . ASP B 62  ? 0.5471 0.5656 0.3761 0.0595 0.0451  0.0045  71  ASP B C   
963  O O   . ASP B 62  ? 0.5744 0.5907 0.3994 0.0660 0.0441  0.0053  71  ASP B O   
964  C CB  . ASP B 62  ? 0.5915 0.5983 0.4097 0.0530 0.0383  0.0004  71  ASP B CB  
965  C CG  . ASP B 62  ? 0.6625 0.6650 0.4743 0.0537 0.0372  0.0022  71  ASP B CG  
966  O OD1 . ASP B 62  ? 0.7254 0.7309 0.5380 0.0578 0.0395  0.0046  71  ASP B OD1 
967  O OD2 . ASP B 62  ? 0.7865 0.7823 0.5923 0.0503 0.0338  0.0013  71  ASP B OD2 
968  N N   . VAL B 63  ? 0.5388 0.5627 0.3736 0.0582 0.0480  0.0063  72  VAL B N   
969  C CA  . VAL B 63  ? 0.5436 0.5719 0.3813 0.0635 0.0506  0.0104  72  VAL B CA  
970  C C   . VAL B 63  ? 0.5821 0.6061 0.4104 0.0696 0.0489  0.0123  72  VAL B C   
971  O O   . VAL B 63  ? 0.6120 0.6390 0.4399 0.0763 0.0503  0.0156  72  VAL B O   
972  C CB  . VAL B 63  ? 0.5322 0.5662 0.3778 0.0595 0.0529  0.0115  72  VAL B CB  
973  C CG1 . VAL B 63  ? 0.5295 0.5669 0.3760 0.0638 0.0545  0.0158  72  VAL B CG1 
974  C CG2 . VAL B 63  ? 0.5349 0.5741 0.3907 0.0564 0.0548  0.0105  72  VAL B CG2 
975  N N   . LYS B 64  ? 0.6047 0.6223 0.4253 0.0678 0.0458  0.0107  73  LYS B N   
976  C CA  . LYS B 64  ? 0.6277 0.6408 0.4388 0.0742 0.0437  0.0123  73  LYS B CA  
977  C C   . LYS B 64  ? 0.6338 0.6420 0.4377 0.0810 0.0412  0.0116  73  LYS B C   
978  O O   . LYS B 64  ? 0.6623 0.6718 0.4621 0.0889 0.0416  0.0140  73  LYS B O   
979  C CB  . LYS B 64  ? 0.6333 0.6392 0.4371 0.0711 0.0404  0.0108  73  LYS B CB  
980  C CG  . LYS B 64  ? 0.6492 0.6519 0.4442 0.0787 0.0387  0.0126  73  LYS B CG  
981  C CD  . LYS B 64  ? 0.6708 0.6662 0.4581 0.0768 0.0352  0.0116  73  LYS B CD  
982  C CE  . LYS B 64  ? 0.7093 0.7036 0.4893 0.0851 0.0341  0.0135  73  LYS B CE  
983  N NZ  . LYS B 64  ? 0.7246 0.7103 0.4961 0.0833 0.0301  0.0123  73  LYS B NZ  
984  N N   . GLN B 65  ? 0.6372 0.6401 0.4392 0.0780 0.0383  0.0083  74  GLN B N   
985  C CA  . GLN B 65  ? 0.6396 0.6380 0.4361 0.0837 0.0355  0.0069  74  GLN B CA  
986  C C   . GLN B 65  ? 0.6205 0.6264 0.4231 0.0881 0.0393  0.0089  74  GLN B C   
987  O O   . GLN B 65  ? 0.6094 0.6131 0.4065 0.0954 0.0376  0.0088  74  GLN B O   
988  C CB  . GLN B 65  ? 0.6602 0.6528 0.4557 0.0780 0.0319  0.0031  74  GLN B CB  
989  C CG  . GLN B 65  ? 0.6971 0.6806 0.4853 0.0743 0.0272  0.0016  74  GLN B CG  
990  C CD  . GLN B 65  ? 0.7357 0.7146 0.5241 0.0682 0.0236  -0.0013 74  GLN B CD  
991  O OE1 . GLN B 65  ? 0.7623 0.7379 0.5484 0.0714 0.0206  -0.0032 74  GLN B OE1 
992  N NE2 . GLN B 65  ? 0.7293 0.7091 0.5213 0.0594 0.0240  -0.0018 74  GLN B NE2 
993  N N   . ASP B 66  ? 0.5870 0.6010 0.4001 0.0839 0.0436  0.0105  75  ASP B N   
994  C CA  . ASP B 66  ? 0.5775 0.5988 0.3987 0.0856 0.0473  0.0127  75  ASP B CA  
995  C C   . ASP B 66  ? 0.5612 0.5799 0.3820 0.0859 0.0455  0.0096  75  ASP B C   
996  O O   . ASP B 66  ? 0.5629 0.5837 0.3831 0.0923 0.0465  0.0114  75  ASP B O   
997  C CB  . ASP B 66  ? 0.5830 0.6086 0.4024 0.0943 0.0496  0.0174  75  ASP B CB  
998  C CG  . ASP B 66  ? 0.5632 0.5961 0.3909 0.0959 0.0534  0.0207  75  ASP B CG  
999  O OD1 . ASP B 66  ? 0.5366 0.5729 0.3738 0.0896 0.0552  0.0203  75  ASP B OD1 
1000 O OD2 . ASP B 66  ? 0.5733 0.6082 0.3974 0.1039 0.0543  0.0236  75  ASP B OD2 
1001 N N   . LEU B 67  ? 0.5353 0.5500 0.3559 0.0796 0.0428  0.0054  76  LEU B N   
1002 C CA  . LEU B 67  ? 0.5355 0.5486 0.3568 0.0787 0.0407  0.0020  76  LEU B CA  
1003 C C   . LEU B 67  ? 0.5512 0.5688 0.3815 0.0707 0.0421  -0.0002 76  LEU B C   
1004 O O   . LEU B 67  ? 0.5531 0.5725 0.3864 0.0647 0.0432  -0.0004 76  LEU B O   
1005 C CB  . LEU B 67  ? 0.5510 0.5551 0.3631 0.0793 0.0352  -0.0006 76  LEU B CB  
1006 C CG  . LEU B 67  ? 0.5641 0.5627 0.3658 0.0888 0.0326  0.0005  76  LEU B CG  
1007 C CD1 . LEU B 67  ? 0.5719 0.5602 0.3648 0.0888 0.0261  -0.0028 76  LEU B CD1 
1008 C CD2 . LEU B 67  ? 0.5901 0.5922 0.3922 0.0965 0.0343  0.0018  76  LEU B CD2 
1009 N N   . VAL B 68  ? 0.5652 0.5848 0.3993 0.0708 0.0419  -0.0024 77  VAL B N   
1010 C CA  . VAL B 68  ? 0.5355 0.5596 0.3773 0.0640 0.0426  -0.0055 77  VAL B CA  
1011 C C   . VAL B 68  ? 0.5275 0.5507 0.3692 0.0647 0.0399  -0.0089 77  VAL B C   
1012 O O   . VAL B 68  ? 0.5439 0.5656 0.3830 0.0716 0.0393  -0.0082 77  VAL B O   
1013 C CB  . VAL B 68  ? 0.5316 0.5625 0.3822 0.0632 0.0466  -0.0041 77  VAL B CB  
1014 C CG1 . VAL B 68  ? 0.5307 0.5629 0.3825 0.0699 0.0480  -0.0017 77  VAL B CG1 
1015 C CG2 . VAL B 68  ? 0.5217 0.5577 0.3796 0.0569 0.0472  -0.0076 77  VAL B CG2 
1016 N N   . SER B 69  ? 0.4980 0.5231 0.3427 0.0582 0.0384  -0.0122 78  SER B N   
1017 C CA  . SER B 69  ? 0.4996 0.5256 0.3461 0.0577 0.0359  -0.0157 78  SER B CA  
1018 C C   . SER B 69  ? 0.4977 0.5323 0.3535 0.0538 0.0384  -0.0180 78  SER B C   
1019 O O   . SER B 69  ? 0.4909 0.5299 0.3509 0.0487 0.0408  -0.0178 78  SER B O   
1020 C CB  . SER B 69  ? 0.5032 0.5240 0.3449 0.0539 0.0313  -0.0175 78  SER B CB  
1021 O OG  . SER B 69  ? 0.5232 0.5478 0.3686 0.0454 0.0319  -0.0182 78  SER B OG  
1022 N N   . TYR B 70  ? 0.4955 0.5325 0.3542 0.0561 0.0374  -0.0205 79  TYR B N   
1023 C CA  . TYR B 70  ? 0.4837 0.5289 0.3508 0.0536 0.0393  -0.0232 79  TYR B CA  
1024 C C   . TYR B 70  ? 0.4924 0.5404 0.3613 0.0508 0.0362  -0.0271 79  TYR B C   
1025 O O   . TYR B 70  ? 0.4917 0.5352 0.3565 0.0542 0.0329  -0.0279 79  TYR B O   
1026 C CB  . TYR B 70  ? 0.4763 0.5227 0.3463 0.0596 0.0412  -0.0223 79  TYR B CB  
1027 C CG  . TYR B 70  ? 0.4783 0.5242 0.3493 0.0610 0.0444  -0.0184 79  TYR B CG  
1028 C CD1 . TYR B 70  ? 0.4915 0.5322 0.3567 0.0647 0.0448  -0.0143 79  TYR B CD1 
1029 C CD2 . TYR B 70  ? 0.5055 0.5563 0.3835 0.0586 0.0468  -0.0189 79  TYR B CD2 
1030 C CE1 . TYR B 70  ? 0.4954 0.5367 0.3625 0.0656 0.0476  -0.0105 79  TYR B CE1 
1031 C CE2 . TYR B 70  ? 0.5041 0.5544 0.3839 0.0593 0.0492  -0.0153 79  TYR B CE2 
1032 C CZ  . TYR B 70  ? 0.4978 0.5437 0.3725 0.0625 0.0497  -0.0108 79  TYR B CZ  
1033 O OH  . TYR B 70  ? 0.5228 0.5692 0.4000 0.0632 0.0520  -0.0069 79  TYR B OH  
1034 N N   A CYS B 71  ? 0.4908 0.5467 0.3658 0.0448 0.0373  -0.0294 80  CYS B N   
1035 N N   B CYS B 71  ? 0.4908 0.5467 0.3658 0.0448 0.0373  -0.0294 80  CYS B N   
1036 N N   C CYS B 71  ? 0.4893 0.5452 0.3642 0.0448 0.0372  -0.0295 80  CYS B N   
1037 N N   D CYS B 71  ? 0.4893 0.5452 0.3642 0.0448 0.0372  -0.0295 80  CYS B N   
1038 C CA  A CYS B 71  ? 0.4975 0.5599 0.3768 0.0411 0.0354  -0.0331 80  CYS B CA  
1039 C CA  B CYS B 71  ? 0.4975 0.5599 0.3768 0.0411 0.0354  -0.0331 80  CYS B CA  
1040 C CA  C CYS B 71  ? 0.4956 0.5576 0.3747 0.0414 0.0351  -0.0331 80  CYS B CA  
1041 C CA  D CYS B 71  ? 0.4956 0.5576 0.3747 0.0414 0.0351  -0.0331 80  CYS B CA  
1042 C C   A CYS B 71  ? 0.4974 0.5573 0.3736 0.0353 0.0323  -0.0325 80  CYS B C   
1043 C C   B CYS B 71  ? 0.4974 0.5573 0.3736 0.0353 0.0323  -0.0325 80  CYS B C   
1044 C C   C CYS B 71  ? 0.4988 0.5576 0.3744 0.0362 0.0317  -0.0327 80  CYS B C   
1045 C C   D CYS B 71  ? 0.4988 0.5576 0.3744 0.0362 0.0317  -0.0327 80  CYS B C   
1046 O O   A CYS B 71  ? 0.4947 0.5616 0.3756 0.0302 0.0312  -0.0347 80  CYS B O   
1047 O O   B CYS B 71  ? 0.4947 0.5616 0.3756 0.0302 0.0312  -0.0347 80  CYS B O   
1048 O O   C CYS B 71  ? 0.5033 0.5671 0.3826 0.0328 0.0294  -0.0351 80  CYS B O   
1049 O O   D CYS B 71  ? 0.5033 0.5671 0.3826 0.0328 0.0294  -0.0351 80  CYS B O   
1050 C CB  A CYS B 71  ? 0.5129 0.5754 0.3933 0.0465 0.0334  -0.0355 80  CYS B CB  
1051 C CB  B CYS B 71  ? 0.5129 0.5754 0.3933 0.0465 0.0334  -0.0355 80  CYS B CB  
1052 C CB  C CYS B 71  ? 0.5077 0.5693 0.3875 0.0473 0.0332  -0.0354 80  CYS B CB  
1053 C CB  D CYS B 71  ? 0.5077 0.5693 0.3875 0.0473 0.0332  -0.0354 80  CYS B CB  
1054 S SG  A CYS B 71  ? 0.5256 0.5934 0.4119 0.0514 0.0365  -0.0370 80  CYS B SG  
1055 S SG  B CYS B 71  ? 0.5256 0.5934 0.4119 0.0514 0.0365  -0.0370 80  CYS B SG  
1056 S SG  C CYS B 71  ? 0.5148 0.5745 0.3951 0.0552 0.0361  -0.0338 80  CYS B SG  
1057 S SG  D CYS B 71  ? 0.5148 0.5745 0.3951 0.0552 0.0361  -0.0338 80  CYS B SG  
1058 N N   . GLY B 72  ? 0.4924 0.5431 0.3614 0.0358 0.0309  -0.0296 81  GLY B N   
1059 C CA  . GLY B 72  ? 0.4934 0.5394 0.3586 0.0308 0.0269  -0.0290 81  GLY B CA  
1060 C C   . GLY B 72  ? 0.4858 0.5215 0.3426 0.0325 0.0260  -0.0257 81  GLY B C   
1061 O O   . GLY B 72  ? 0.4904 0.5239 0.3448 0.0374 0.0286  -0.0239 81  GLY B O   
1062 N N   . PRO B 73  ? 0.4956 0.5254 0.3480 0.0282 0.0220  -0.0248 82  PRO B N   
1063 C CA  . PRO B 73  ? 0.5253 0.5447 0.3689 0.0300 0.0204  -0.0221 82  PRO B CA  
1064 C C   . PRO B 73  ? 0.5584 0.5689 0.3948 0.0392 0.0174  -0.0223 82  PRO B C   
1065 O O   . PRO B 73  ? 0.5695 0.5798 0.4068 0.0419 0.0146  -0.0247 82  PRO B O   
1066 C CB  . PRO B 73  ? 0.5181 0.5337 0.3599 0.0223 0.0161  -0.0214 82  PRO B CB  
1067 C CG  . PRO B 73  ? 0.5147 0.5363 0.3630 0.0186 0.0138  -0.0240 82  PRO B CG  
1068 C CD  . PRO B 73  ? 0.5032 0.5356 0.3590 0.0216 0.0185  -0.0262 82  PRO B CD  
1069 N N   . TRP B 74  ? 0.5764 0.5801 0.4056 0.0437 0.0177  -0.0199 83  TRP B N   
1070 C CA  . TRP B 74  ? 0.5889 0.5837 0.4093 0.0526 0.0145  -0.0196 83  TRP B CA  
1071 C C   . TRP B 74  ? 0.6291 0.6165 0.4454 0.0527 0.0074  -0.0222 83  TRP B C   
1072 O O   . TRP B 74  ? 0.6450 0.6277 0.4597 0.0463 0.0036  -0.0221 83  TRP B O   
1073 C CB  . TRP B 74  ? 0.5892 0.5779 0.4022 0.0551 0.0148  -0.0167 83  TRP B CB  
1074 C CG  . TRP B 74  ? 0.5833 0.5662 0.3883 0.0657 0.0132  -0.0162 83  TRP B CG  
1075 C CD1 . TRP B 74  ? 0.5827 0.5552 0.3783 0.0705 0.0070  -0.0174 83  TRP B CD1 
1076 C CD2 . TRP B 74  ? 0.5686 0.5562 0.3744 0.0731 0.0178  -0.0142 83  TRP B CD2 
1077 N NE1 . TRP B 74  ? 0.5838 0.5549 0.3736 0.0809 0.0077  -0.0164 83  TRP B NE1 
1078 C CE2 . TRP B 74  ? 0.5717 0.5524 0.3679 0.0825 0.0145  -0.0141 83  TRP B CE2 
1079 C CE3 . TRP B 74  ? 0.5590 0.5560 0.3726 0.0728 0.0240  -0.0124 83  TRP B CE3 
1080 C CZ2 . TRP B 74  ? 0.5578 0.5419 0.3524 0.0913 0.0178  -0.0117 83  TRP B CZ2 
1081 C CZ3 . TRP B 74  ? 0.5608 0.5600 0.3732 0.0808 0.0269  -0.0099 83  TRP B CZ3 
1082 C CH2 . TRP B 74  ? 0.5570 0.5505 0.3601 0.0900 0.0241  -0.0093 83  TRP B CH2 
1083 N N   . LYS B 75  ? 0.6432 0.6289 0.4575 0.0601 0.0053  -0.0241 84  LYS B N   
1084 C CA  . LYS B 75  ? 0.6693 0.6487 0.4806 0.0611 -0.0017 -0.0273 84  LYS B CA  
1085 C C   . LYS B 75  ? 0.6811 0.6489 0.4805 0.0705 -0.0068 -0.0277 84  LYS B C   
1086 O O   . LYS B 75  ? 0.7030 0.6631 0.4987 0.0705 -0.0140 -0.0302 84  LYS B O   
1087 C CB  . LYS B 75  ? 0.6947 0.6810 0.5119 0.0639 -0.0008 -0.0299 84  LYS B CB  
1088 C CG  . LYS B 75  ? 0.7079 0.7058 0.5366 0.0561 0.0029  -0.0307 84  LYS B CG  
1089 C CD  . LYS B 75  ? 0.7370 0.7352 0.5694 0.0467 -0.0011 -0.0318 84  LYS B CD  
1090 C CE  . LYS B 75  ? 0.7511 0.7626 0.5945 0.0396 0.0035  -0.0322 84  LYS B CE  
1091 N NZ  . LYS B 75  ? 0.7945 0.8078 0.6417 0.0294 0.0009  -0.0318 84  LYS B NZ  
1092 N N   . LEU B 76  ? 0.6805 0.6474 0.4743 0.0784 -0.0036 -0.0253 85  LEU B N   
1093 C CA  . LEU B 76  ? 0.6977 0.6561 0.4801 0.0896 -0.0074 -0.0257 85  LEU B CA  
1094 C C   . LEU B 76  ? 0.7375 0.6854 0.5110 0.0894 -0.0119 -0.0250 85  LEU B C   
1095 O O   . LEU B 76  ? 0.7125 0.6623 0.4853 0.0885 -0.0077 -0.0218 85  LEU B O   
1096 C CB  . LEU B 76  ? 0.6759 0.6409 0.4580 0.0978 -0.0010 -0.0229 85  LEU B CB  
1097 C CG  . LEU B 76  ? 0.6445 0.6200 0.4362 0.0971 0.0041  -0.0228 85  LEU B CG  
1098 C CD1 . LEU B 76  ? 0.6428 0.6236 0.4337 0.1052 0.0098  -0.0192 85  LEU B CD1 
1099 C CD2 . LEU B 76  ? 0.6457 0.6201 0.4383 0.0987 -0.0001 -0.0268 85  LEU B CD2 
1100 N N   . ASP B 77  ? 0.7747 0.7117 0.5420 0.0898 -0.0205 -0.0280 86  ASP B N   
1101 C CA  . ASP B 77  ? 0.8566 0.7815 0.6153 0.0885 -0.0264 -0.0278 86  ASP B CA  
1102 C C   . ASP B 77  ? 0.8368 0.7511 0.5820 0.1010 -0.0322 -0.0295 86  ASP B C   
1103 O O   . ASP B 77  ? 0.8581 0.7622 0.5952 0.1016 -0.0371 -0.0295 86  ASP B O   
1104 C CB  . ASP B 77  ? 0.9257 0.8455 0.6881 0.0774 -0.0322 -0.0291 86  ASP B CB  
1105 C CG  . ASP B 77  ? 1.0171 0.9375 0.7842 0.0759 -0.0366 -0.0326 86  ASP B CG  
1106 O OD1 . ASP B 77  ? 1.0936 1.0204 0.8627 0.0825 -0.0337 -0.0340 86  ASP B OD1 
1107 O OD2 . ASP B 77  ? 1.1142 1.0287 0.8830 0.0681 -0.0430 -0.0338 86  ASP B OD2 
1108 N N   . ALA B 78  ? 0.8236 0.7403 0.5656 0.1113 -0.0317 -0.0309 87  ALA B N   
1109 C CA  . ALA B 78  ? 0.7994 0.7063 0.5278 0.1240 -0.0378 -0.0330 87  ALA B CA  
1110 C C   . ALA B 78  ? 0.7926 0.7008 0.5144 0.1306 -0.0337 -0.0296 87  ALA B C   
1111 O O   . ALA B 78  ? 0.7557 0.6753 0.4845 0.1283 -0.0247 -0.0256 87  ALA B O   
1112 C CB  . ALA B 78  ? 0.8032 0.7134 0.5302 0.1330 -0.0379 -0.0351 87  ALA B CB  
1113 N N   . ALA B 79  ? 0.8027 0.6995 0.5114 0.1390 -0.0404 -0.0314 88  ALA B N   
1114 C CA  . ALA B 79  ? 0.7906 0.6876 0.4912 0.1470 -0.0380 -0.0289 88  ALA B CA  
1115 C C   . ALA B 79  ? 0.7813 0.6752 0.4694 0.1631 -0.0413 -0.0307 88  ALA B C   
1116 O O   . ALA B 79  ? 0.7486 0.6323 0.4301 0.1673 -0.0499 -0.0353 88  ALA B O   
1117 C CB  . ALA B 79  ? 0.8196 0.7051 0.5153 0.1416 -0.0438 -0.0294 88  ALA B CB  
1118 N N   . TRP B 80  ? 0.7892 0.6914 0.4740 0.1719 -0.0353 -0.0272 89  TRP B N   
1119 C CA  . TRP B 80  ? 0.8256 0.7247 0.4963 0.1881 -0.0385 -0.0284 89  TRP B CA  
1120 C C   . TRP B 80  ? 0.8388 0.7204 0.4974 0.1907 -0.0497 -0.0329 89  TRP B C   
1121 O O   . TRP B 80  ? 0.8108 0.6864 0.4713 0.1814 -0.0516 -0.0325 89  TRP B O   
1122 C CB  . TRP B 80  ? 0.8196 0.7308 0.4898 0.1948 -0.0302 -0.0232 89  TRP B CB  
1123 C CG  . TRP B 80  ? 0.8312 0.7426 0.4881 0.2119 -0.0322 -0.0238 89  TRP B CG  
1124 C CD1 . TRP B 80  ? 0.8413 0.7500 0.4906 0.2222 -0.0363 -0.0269 89  TRP B CD1 
1125 C CD2 . TRP B 80  ? 0.8375 0.7534 0.4870 0.2213 -0.0297 -0.0211 89  TRP B CD2 
1126 N NE1 . TRP B 80  ? 0.8303 0.7416 0.4677 0.2376 -0.0365 -0.0263 89  TRP B NE1 
1127 C CE2 . TRP B 80  ? 0.8337 0.7497 0.4711 0.2374 -0.0326 -0.0228 89  TRP B CE2 
1128 C CE3 . TRP B 80  ? 0.8346 0.7546 0.4861 0.2181 -0.0259 -0.0177 89  TRP B CE3 
1129 C CZ2 . TRP B 80  ? 0.8332 0.7539 0.4607 0.2503 -0.0314 -0.0210 89  TRP B CZ2 
1130 C CZ3 . TRP B 80  ? 0.8335 0.7580 0.4758 0.2306 -0.0249 -0.0160 89  TRP B CZ3 
1131 C CH2 . TRP B 80  ? 0.8311 0.7567 0.4618 0.2466 -0.0273 -0.0174 89  TRP B CH2 
1132 N N   . ASP B 81  ? 0.8769 0.7499 0.5233 0.2026 -0.0574 -0.0373 90  ASP B N   
1133 C CA  . ASP B 81  ? 0.8992 0.7534 0.5338 0.2052 -0.0698 -0.0424 90  ASP B CA  
1134 C C   . ASP B 81  ? 0.9197 0.7723 0.5425 0.2161 -0.0703 -0.0415 90  ASP B C   
1135 O O   . ASP B 81  ? 0.9789 0.8157 0.5915 0.2179 -0.0800 -0.0451 90  ASP B O   
1136 C CB  . ASP B 81  ? 0.9167 0.7614 0.5444 0.2120 -0.0789 -0.0481 90  ASP B CB  
1137 C CG  . ASP B 81  ? 0.9092 0.7593 0.5269 0.2296 -0.0780 -0.0491 90  ASP B CG  
1138 O OD1 . ASP B 81  ? 0.9065 0.7707 0.5250 0.2357 -0.0685 -0.0443 90  ASP B OD1 
1139 O OD2 . ASP B 81  ? 0.9240 0.7643 0.5332 0.2373 -0.0869 -0.0545 90  ASP B OD2 
1140 N N   . GLY B 82  ? 0.9050 0.7734 0.5297 0.2225 -0.0603 -0.0368 91  GLY B N   
1141 C CA  . GLY B 82  ? 0.9206 0.7927 0.5365 0.2329 -0.0583 -0.0347 91  GLY B CA  
1142 C C   . GLY B 82  ? 0.9550 0.8276 0.5569 0.2518 -0.0614 -0.0371 91  GLY B C   
1143 O O   . GLY B 82  ? 0.9547 0.8328 0.5493 0.2621 -0.0590 -0.0352 91  GLY B O   
1144 N N   . LEU B 83  ? 0.9878 0.8551 0.5859 0.2566 -0.0667 -0.0412 92  LEU B N   
1145 C CA  . LEU B 83  ? 1.0196 0.8846 0.6026 0.2752 -0.0717 -0.0447 92  LEU B CA  
1146 C C   . LEU B 83  ? 1.0300 0.9088 0.6176 0.2801 -0.0648 -0.0423 92  LEU B C   
1147 O O   . LEU B 83  ? 1.0379 0.9283 0.6196 0.2934 -0.0597 -0.0394 92  LEU B O   
1148 C CB  . LEU B 83  ? 1.0744 0.9182 0.6475 0.2769 -0.0862 -0.0526 92  LEU B CB  
1149 C CG  . LEU B 83  ? 1.1295 0.9564 0.6903 0.2802 -0.0965 -0.0566 92  LEU B CG  
1150 C CD1 . LEU B 83  ? 1.1680 0.9755 0.7173 0.2863 -0.1111 -0.0646 92  LEU B CD1 
1151 C CD2 . LEU B 83  ? 1.1302 0.9642 0.6803 0.2948 -0.0935 -0.0548 92  LEU B CD2 
1152 N N   . SER B 84  ? 1.0319 0.9086 0.6286 0.2705 -0.0656 -0.0437 93  SER B N   
1153 C CA  . SER B 84  ? 0.9833 0.8676 0.5816 0.2761 -0.0627 -0.0436 93  SER B CA  
1154 C C   . SER B 84  ? 0.9441 0.8489 0.5527 0.2752 -0.0489 -0.0356 93  SER B C   
1155 O O   . SER B 84  ? 0.9710 0.8833 0.5898 0.2653 -0.0417 -0.0307 93  SER B O   
1156 C CB  . SER B 84  ? 0.9867 0.8634 0.5931 0.2650 -0.0674 -0.0473 93  SER B CB  
1157 O OG  . SER B 84  ? 0.9973 0.8589 0.6040 0.2550 -0.0758 -0.0510 93  SER B OG  
1158 N N   . GLU B 85  ? 0.9222 0.8356 0.5282 0.2851 -0.0456 -0.0343 94  GLU B N   
1159 C CA  . GLU B 85  ? 0.8908 0.8225 0.5076 0.2832 -0.0333 -0.0267 94  GLU B CA  
1160 C C   . GLU B 85  ? 0.8142 0.7456 0.4464 0.2670 -0.0313 -0.0268 94  GLU B C   
1161 O O   . GLU B 85  ? 0.8109 0.7292 0.4430 0.2611 -0.0399 -0.0331 94  GLU B O   
1162 C CB  . GLU B 85  ? 0.9338 0.8731 0.5419 0.2990 -0.0315 -0.0256 94  GLU B CB  
1163 C CG  . GLU B 85  ? 0.9414 0.8871 0.5367 0.3151 -0.0301 -0.0233 94  GLU B CG  
1164 C CD  . GLU B 85  ? 0.9827 0.9409 0.5710 0.3306 -0.0253 -0.0195 94  GLU B CD  
1165 O OE1 . GLU B 85  ? 0.9526 0.9152 0.5459 0.3295 -0.0224 -0.0182 94  GLU B OE1 
1166 O OE2 . GLU B 85  ? 0.9869 0.9509 0.5643 0.3442 -0.0245 -0.0178 94  GLU B OE2 
1167 N N   . VAL B 86  ? 0.7723 0.7182 0.4167 0.2611 -0.0206 -0.0199 95  VAL B N   
1168 C CA  . VAL B 86  ? 0.7512 0.7003 0.4115 0.2459 -0.0165 -0.0187 95  VAL B CA  
1169 C C   . VAL B 86  ? 0.7319 0.6947 0.3984 0.2489 -0.0080 -0.0131 95  VAL B C   
1170 O O   . VAL B 86  ? 0.7687 0.7398 0.4285 0.2608 -0.0041 -0.0089 95  VAL B O   
1171 C CB  . VAL B 86  ? 0.7055 0.6569 0.3762 0.2326 -0.0123 -0.0157 95  VAL B CB  
1172 C CG1 . VAL B 86  ? 0.7238 0.6621 0.3871 0.2310 -0.0203 -0.0202 95  VAL B CG1 
1173 C CG2 . VAL B 86  ? 0.6937 0.6597 0.3687 0.2348 -0.0025 -0.0078 95  VAL B CG2 
1174 N N   . GLN B 87  ? 0.7400 0.7057 0.4191 0.2380 -0.0049 -0.0125 96  GLN B N   
1175 C CA  . GLN B 87  ? 0.7468 0.7250 0.4337 0.2387 0.0034  -0.0066 96  GLN B CA  
1176 C C   . GLN B 87  ? 0.7035 0.6887 0.4061 0.2245 0.0104  -0.0024 96  GLN B C   
1177 O O   . GLN B 87  ? 0.7359 0.7157 0.4458 0.2131 0.0078  -0.0060 96  GLN B O   
1178 C CB  . GLN B 87  ? 0.7499 0.7251 0.4355 0.2418 0.0000  -0.0104 96  GLN B CB  
1179 C CG  . GLN B 87  ? 0.8006 0.7731 0.4707 0.2586 -0.0043 -0.0124 96  GLN B CG  
1180 C CD  . GLN B 87  ? 0.8002 0.7700 0.4680 0.2631 -0.0079 -0.0161 96  GLN B CD  
1181 O OE1 . GLN B 87  ? 0.7695 0.7421 0.4479 0.2551 -0.0054 -0.0157 96  GLN B OE1 
1182 N NE2 . GLN B 87  ? 0.8103 0.7745 0.4636 0.2769 -0.0142 -0.0200 96  GLN B NE2 
1183 N N   . LEU B 88  ? 0.6783 0.6754 0.3857 0.2257 0.0186  0.0052  97  LEU B N   
1184 C CA  . LEU B 88  ? 0.6728 0.6784 0.3952 0.2149 0.0260  0.0102  97  LEU B CA  
1185 C C   . LEU B 88  ? 0.6665 0.6746 0.3935 0.2150 0.0275  0.0106  97  LEU B C   
1186 O O   . LEU B 88  ? 0.6665 0.6808 0.3889 0.2252 0.0305  0.0148  97  LEU B O   
1187 C CB  . LEU B 88  ? 0.6649 0.6822 0.3901 0.2176 0.0335  0.0185  97  LEU B CB  
1188 C CG  . LEU B 88  ? 0.6605 0.6863 0.4011 0.2072 0.0405  0.0240  97  LEU B CG  
1189 C CD1 . LEU B 88  ? 0.6523 0.6730 0.4014 0.1935 0.0389  0.0203  97  LEU B CD1 
1190 C CD2 . LEU B 88  ? 0.6686 0.7065 0.4121 0.2104 0.0475  0.0327  97  LEU B CD2 
1191 N N   . LEU B 89  ? 0.6288 0.6326 0.3639 0.2049 0.0254  0.0063  98  LEU B N   
1192 C CA  . LEU B 89  ? 0.6173 0.6248 0.3596 0.2029 0.0280  0.0073  98  LEU B CA  
1193 C C   . LEU B 89  ? 0.6199 0.6370 0.3737 0.1966 0.0359  0.0145  98  LEU B C   
1194 O O   . LEU B 89  ? 0.6614 0.6787 0.4262 0.1848 0.0371  0.0134  98  LEU B O   
1195 C CB  . LEU B 89  ? 0.6118 0.6119 0.3579 0.1952 0.0224  0.0000  98  LEU B CB  
1196 C CG  . LEU B 89  ? 0.6328 0.6359 0.3872 0.1917 0.0240  -0.0004 98  LEU B CG  
1197 C CD1 . LEU B 89  ? 0.6442 0.6543 0.3975 0.1998 0.0291  0.0056  98  LEU B CD1 
1198 C CD2 . LEU B 89  ? 0.6437 0.6394 0.3952 0.1919 0.0167  -0.0082 98  LEU B CD2 
1199 N N   . ALA B 90  ? 0.6225 0.6477 0.3739 0.2042 0.0411  0.0218  99  ALA B N   
1200 C CA  . ALA B 90  ? 0.6199 0.6547 0.3824 0.1989 0.0484  0.0296  99  ALA B CA  
1201 C C   . ALA B 90  ? 0.6326 0.6687 0.4037 0.1944 0.0503  0.0305  99  ALA B C   
1202 O O   . ALA B 90  ? 0.6419 0.6774 0.4077 0.2020 0.0492  0.0302  99  ALA B O   
1203 C CB  . ALA B 90  ? 0.6211 0.6650 0.3795 0.2082 0.0534  0.0378  99  ALA B CB  
1204 N N   . VAL B 91  ? 0.6197 0.6580 0.4033 0.1834 0.0530  0.0319  100 VAL B N   
1205 C CA  . VAL B 91  ? 0.5958 0.6364 0.3887 0.1791 0.0555  0.0340  100 VAL B CA  
1206 C C   . VAL B 91  ? 0.5866 0.6351 0.3890 0.1751 0.0616  0.0425  100 VAL B C   
1207 O O   . VAL B 91  ? 0.5682 0.6172 0.3804 0.1653 0.0626  0.0423  100 VAL B O   
1208 C CB  . VAL B 91  ? 0.5817 0.6165 0.3804 0.1701 0.0517  0.0263  100 VAL B CB  
1209 C CG1 . VAL B 91  ? 0.5943 0.6306 0.4015 0.1664 0.0534  0.0273  100 VAL B CG1 
1210 C CG2 . VAL B 91  ? 0.5958 0.6233 0.3853 0.1741 0.0454  0.0187  100 VAL B CG2 
1211 N N   . PRO B 92  ? 0.5905 0.6460 0.3904 0.1826 0.0657  0.0507  101 PRO B N   
1212 C CA  . PRO B 92  ? 0.5936 0.6572 0.4029 0.1787 0.0712  0.0595  101 PRO B CA  
1213 C C   . PRO B 92  ? 0.6043 0.6682 0.4240 0.1729 0.0728  0.0624  101 PRO B C   
1214 O O   . PRO B 92  ? 0.6218 0.6810 0.4402 0.1741 0.0705  0.0587  101 PRO B O   
1215 C CB  . PRO B 92  ? 0.6031 0.6747 0.4051 0.1896 0.0747  0.0672  101 PRO B CB  
1216 C CG  . PRO B 92  ? 0.6077 0.6747 0.3961 0.2002 0.0710  0.0624  101 PRO B CG  
1217 C CD  . PRO B 92  ? 0.6103 0.6668 0.3982 0.1953 0.0651  0.0520  101 PRO B CD  
1218 N N   . PRO B 93  ? 0.6259 0.6948 0.4567 0.1660 0.0763  0.0685  102 PRO B N   
1219 C CA  . PRO B 93  ? 0.6412 0.7086 0.4821 0.1598 0.0769  0.0704  102 PRO B CA  
1220 C C   . PRO B 93  ? 0.6575 0.7267 0.4951 0.1673 0.0785  0.0760  102 PRO B C   
1221 O O   . PRO B 93  ? 0.6659 0.7416 0.4981 0.1750 0.0816  0.0828  102 PRO B O   
1222 C CB  . PRO B 93  ? 0.6269 0.6995 0.4791 0.1521 0.0798  0.0762  102 PRO B CB  
1223 C CG  . PRO B 93  ? 0.6272 0.7010 0.4755 0.1516 0.0793  0.0731  102 PRO B CG  
1224 C CD  . PRO B 93  ? 0.6415 0.7162 0.4763 0.1629 0.0789  0.0726  102 PRO B CD  
1225 N N   . GLY B 94  ? 0.6569 0.7204 0.4968 0.1656 0.0762  0.0725  103 GLY B N   
1226 C CA  . GLY B 94  ? 0.6855 0.7491 0.5228 0.1718 0.0771  0.0771  103 GLY B CA  
1227 C C   . GLY B 94  ? 0.6923 0.7560 0.5158 0.1839 0.0763  0.0759  103 GLY B C   
1228 O O   . GLY B 94  ? 0.7219 0.7857 0.5425 0.1895 0.0770  0.0796  103 GLY B O   
1229 N N   . GLU B 95  ? 0.6836 0.7467 0.4984 0.1879 0.0744  0.0707  104 GLU B N   
1230 C CA  . GLU B 95  ? 0.6932 0.7567 0.4940 0.2004 0.0734  0.0699  104 GLU B CA  
1231 C C   . GLU B 95  ? 0.7077 0.7628 0.5022 0.2011 0.0671  0.0582  104 GLU B C   
1232 O O   . GLU B 95  ? 0.6999 0.7510 0.4999 0.1922 0.0647  0.0521  104 GLU B O   
1233 C CB  . GLU B 95  ? 0.6945 0.7656 0.4904 0.2056 0.0765  0.0753  104 GLU B CB  
1234 C CG  . GLU B 95  ? 0.7194 0.8003 0.5232 0.2039 0.0828  0.0874  104 GLU B CG  
1235 C CD  . GLU B 95  ? 0.7732 0.8635 0.5734 0.2088 0.0862  0.0930  104 GLU B CD  
1236 O OE1 . GLU B 95  ? 0.7875 0.8754 0.5791 0.2128 0.0834  0.0868  104 GLU B OE1 
1237 O OE2 . GLU B 95  ? 0.8110 0.9111 0.6168 0.2089 0.0916  0.1039  104 GLU B OE2 
1238 N N   . ARG B 96  ? 0.7137 0.7661 0.4975 0.2108 0.0644  0.0553  105 ARG B N   
1239 C CA  . ARG B 96  ? 0.7639 0.8081 0.5417 0.2118 0.0578  0.0444  105 ARG B CA  
1240 C C   . ARG B 96  ? 0.7442 0.7863 0.5171 0.2114 0.0552  0.0398  105 ARG B C   
1241 O O   . ARG B 96  ? 0.7101 0.7573 0.4786 0.2163 0.0580  0.0450  105 ARG B O   
1242 C CB  . ARG B 96  ? 0.8502 0.8925 0.6170 0.2238 0.0554  0.0431  105 ARG B CB  
1243 C CG  . ARG B 96  ? 0.9241 0.9581 0.6867 0.2241 0.0481  0.0321  105 ARG B CG  
1244 C CD  . ARG B 96  ? 0.9881 1.0197 0.7433 0.2335 0.0454  0.0301  105 ARG B CD  
1245 N NE  . ARG B 96  ? 1.0423 1.0781 0.7863 0.2463 0.0477  0.0360  105 ARG B NE  
1246 C CZ  . ARG B 96  ? 1.0965 1.1387 0.8407 0.2508 0.0532  0.0456  105 ARG B CZ  
1247 N NH1 . ARG B 96  ? 1.0820 1.1259 0.8369 0.2438 0.0566  0.0503  105 ARG B NH1 
1248 N NH2 . ARG B 96  ? 1.1620 1.2087 0.8950 0.2630 0.0550  0.0505  105 ARG B NH2 
1249 N N   . ALA B 97  ? 0.7353 0.7704 0.5091 0.2058 0.0498  0.0307  106 ALA B N   
1250 C CA  . ALA B 97  ? 0.7465 0.7767 0.5136 0.2063 0.0453  0.0248  106 ALA B CA  
1251 C C   . ALA B 97  ? 0.7592 0.7896 0.5122 0.2200 0.0439  0.0258  106 ALA B C   
1252 O O   . ALA B 97  ? 0.7715 0.8001 0.5179 0.2280 0.0417  0.0242  106 ALA B O   
1253 C CB  . ALA B 97  ? 0.7358 0.7586 0.5044 0.2009 0.0392  0.0153  106 ALA B CB  
1254 N N   . LYS B 98  ? 0.7889 0.8212 0.5367 0.2231 0.0448  0.0279  107 LYS B N   
1255 C CA  . LYS B 98  ? 0.8098 0.8427 0.5433 0.2369 0.0433  0.0287  107 LYS B CA  
1256 C C   . LYS B 98  ? 0.8068 0.8342 0.5342 0.2370 0.0387  0.0237  107 LYS B C   
1257 O O   . LYS B 98  ? 0.7882 0.8190 0.5215 0.2304 0.0419  0.0267  107 LYS B O   
1258 C CB  . LYS B 98  ? 0.8883 0.9328 0.6222 0.2425 0.0508  0.0394  107 LYS B CB  
1259 C CG  . LYS B 98  ? 0.9555 1.0037 0.6750 0.2580 0.0508  0.0419  107 LYS B CG  
1260 C CD  . LYS B 98  ? 1.0181 1.0796 0.7396 0.2617 0.0587  0.0530  107 LYS B CD  
1261 C CE  . LYS B 98  ? 1.0431 1.1090 0.7778 0.2495 0.0629  0.0570  107 LYS B CE  
1262 N NZ  . LYS B 98  ? 1.0825 1.1613 0.8179 0.2540 0.0694  0.0670  107 LYS B NZ  
1263 N N   . ASN B 99  ? 0.7563 0.7751 0.4725 0.2438 0.0313  0.0163  108 ASN B N   
1264 C CA  . ASN B 99  ? 0.7432 0.7551 0.4507 0.2463 0.0257  0.0114  108 ASN B CA  
1265 C C   . ASN B 99  ? 0.7612 0.7799 0.4594 0.2579 0.0289  0.0169  108 ASN B C   
1266 O O   . ASN B 99  ? 0.7880 0.8124 0.4797 0.2691 0.0312  0.0207  108 ASN B O   
1267 C CB  . ASN B 99  ? 0.7403 0.7406 0.4376 0.2518 0.0161  0.0023  108 ASN B CB  
1268 C CG  . ASN B 99  ? 0.7567 0.7503 0.4619 0.2414 0.0118  -0.0039 108 ASN B CG  
1269 O OD1 . ASN B 99  ? 0.7869 0.7843 0.4994 0.2382 0.0147  -0.0024 108 ASN B OD1 
1270 N ND2 . ASN B 99  ? 0.7634 0.7473 0.4674 0.2360 0.0047  -0.0107 108 ASN B ND2 
1271 N N   . ILE B 100 ? 0.7210 0.7387 0.4174 0.2564 0.0282  0.0166  109 ILE B N   
1272 C CA  . ILE B 100 ? 0.7263 0.7511 0.4144 0.2669 0.0310  0.0214  109 ILE B CA  
1273 C C   . ILE B 100 ? 0.7220 0.7366 0.4012 0.2686 0.0236  0.0147  109 ILE B C   
1274 O O   . ILE B 100 ? 0.7581 0.7676 0.4445 0.2567 0.0222  0.0122  109 ILE B O   
1275 C CB  . ILE B 100 ? 0.7340 0.7709 0.4337 0.2601 0.0398  0.0303  109 ILE B CB  
1276 C CG1 . ILE B 100 ? 0.7340 0.7785 0.4452 0.2547 0.0462  0.0365  109 ILE B CG1 
1277 C CG2 . ILE B 100 ? 0.7349 0.7808 0.4269 0.2708 0.0429  0.0355  109 ILE B CG2 
1278 C CD1 . ILE B 100 ? 0.7476 0.8012 0.4529 0.2668 0.0503  0.0429  109 ILE B CD1 
1279 N N   . GLN B 101 ? 0.7389 0.7497 0.4029 0.2825 0.0185  0.0113  110 GLN B N   
1280 C CA  . GLN B 101 ? 0.7711 0.7690 0.4248 0.2852 0.0094  0.0036  110 GLN B CA  
1281 C C   . GLN B 101 ? 0.7987 0.8029 0.4476 0.2910 0.0122  0.0075  110 GLN B C   
1282 O O   . GLN B 101 ? 0.7814 0.7994 0.4293 0.2991 0.0192  0.0148  110 GLN B O   
1283 C CB  . GLN B 101 ? 0.8132 0.8020 0.4528 0.2974 0.0010  -0.0030 110 GLN B CB  
1284 C CG  . GLN B 101 ? 0.8195 0.7948 0.4474 0.3019 -0.0088 -0.0105 110 GLN B CG  
1285 C CD  . GLN B 101 ? 0.8428 0.8059 0.4612 0.3084 -0.0187 -0.0186 110 GLN B CD  
1286 O OE1 . GLN B 101 ? 0.8240 0.7864 0.4481 0.3043 -0.0188 -0.0200 110 GLN B OE1 
1287 N NE2 . GLN B 101 ? 0.8529 0.8060 0.4566 0.3189 -0.0274 -0.0244 110 GLN B NE2 
1288 N N   . THR B 102 ? 0.8027 0.7984 0.4509 0.2852 0.0077  0.0036  111 THR B N   
1289 C CA  . THR B 102 ? 0.7965 0.7975 0.4419 0.2882 0.0101  0.0068  111 THR B CA  
1290 C C   . THR B 102 ? 0.7948 0.7802 0.4329 0.2862 0.0008  -0.0006 111 THR B C   
1291 O O   . THR B 102 ? 0.8176 0.7899 0.4575 0.2780 -0.0057 -0.0068 111 THR B O   
1292 C CB  . THR B 102 ? 0.7907 0.8049 0.4517 0.2777 0.0201  0.0151  111 THR B CB  
1293 O OG1 . THR B 102 ? 0.7831 0.8066 0.4404 0.2846 0.0237  0.0197  111 THR B OG1 
1294 C CG2 . THR B 102 ? 0.7946 0.8026 0.4680 0.2603 0.0197  0.0131  111 THR B CG2 
1295 N N   . LEU B 103 ? 0.7781 0.7647 0.4067 0.2952 -0.0004 -0.0002 112 LEU B N   
1296 C CA  . LEU B 103 ? 0.7853 0.7588 0.4078 0.2928 -0.0080 -0.0057 112 LEU B CA  
1297 C C   . LEU B 103 ? 0.7851 0.7657 0.4190 0.2819 -0.0016 -0.0006 112 LEU B C   
1298 O O   . LEU B 103 ? 0.7776 0.7725 0.4135 0.2864 0.0055  0.0057  112 LEU B O   
1299 C CB  . LEU B 103 ? 0.7955 0.7648 0.3998 0.3100 -0.0141 -0.0091 112 LEU B CB  
1300 C CG  . LEU B 103 ? 0.7983 0.7519 0.3956 0.3076 -0.0231 -0.0150 112 LEU B CG  
1301 C CD1 . LEU B 103 ? 0.7969 0.7310 0.3889 0.3047 -0.0344 -0.0235 112 LEU B CD1 
1302 C CD2 . LEU B 103 ? 0.8298 0.7854 0.4125 0.3236 -0.0254 -0.0156 112 LEU B CD2 
1303 N N   . PRO B 104 ? 0.7705 0.7422 0.4130 0.2667 -0.0038 -0.0031 113 PRO B N   
1304 C CA  . PRO B 104 ? 0.7536 0.7316 0.4071 0.2559 0.0018  0.0011  113 PRO B CA  
1305 C C   . PRO B 104 ? 0.7714 0.7494 0.4160 0.2633 0.0001  0.0013  113 PRO B C   
1306 O O   . PRO B 104 ? 0.7971 0.7625 0.4281 0.2708 -0.0086 -0.0044 113 PRO B O   
1307 C CB  . PRO B 104 ? 0.7463 0.7123 0.4069 0.2405 -0.0023 -0.0031 113 PRO B CB  
1308 C CG  . PRO B 104 ? 0.7565 0.7130 0.4135 0.2416 -0.0085 -0.0084 113 PRO B CG  
1309 C CD  . PRO B 104 ? 0.7790 0.7356 0.4215 0.2593 -0.0117 -0.0099 113 PRO B CD  
1310 N N   . GLY B 105 ? 0.7660 0.7582 0.4186 0.2612 0.0082  0.0079  114 GLY B N   
1311 C CA  . GLY B 105 ? 0.7860 0.7783 0.4351 0.2626 0.0074  0.0084  114 GLY B CA  
1312 C C   . GLY B 105 ? 0.8074 0.7884 0.4623 0.2480 0.0041  0.0054  114 GLY B C   
1313 O O   . GLY B 105 ? 0.7740 0.7443 0.4319 0.2391 0.0002  0.0014  114 GLY B O   
1314 N N   . ILE B 106 ? 0.8101 0.7942 0.4662 0.2460 0.0057  0.0073  115 ILE B N   
1315 C CA  . ILE B 106 ? 0.8279 0.8012 0.4864 0.2346 0.0021  0.0047  115 ILE B CA  
1316 C C   . ILE B 106 ? 0.7928 0.7793 0.4636 0.2272 0.0100  0.0105  115 ILE B C   
1317 O O   . ILE B 106 ? 0.8301 0.8279 0.4992 0.2354 0.0138  0.0144  115 ILE B O   
1318 C CB  . ILE B 106 ? 0.8692 0.8296 0.5115 0.2436 -0.0068 -0.0003 115 ILE B CB  
1319 C CG1 . ILE B 106 ? 0.9521 0.8986 0.5817 0.2516 -0.0158 -0.0065 115 ILE B CG1 
1320 C CG2 . ILE B 106 ? 0.9092 0.8590 0.5530 0.2330 -0.0105 -0.0022 115 ILE B CG2 
1321 C CD1 . ILE B 106 ? 0.9487 0.8802 0.5812 0.2396 -0.0217 -0.0109 115 ILE B CD1 
1322 N N   . PHE B 107 ? 0.7808 0.7658 0.4634 0.2124 0.0122  0.0111  116 PHE B N   
1323 C CA  . PHE B 107 ? 0.7694 0.7608 0.4612 0.2040 0.0166  0.0144  116 PHE B CA  
1324 C C   . PHE B 107 ? 0.7867 0.7639 0.4699 0.2020 0.0094  0.0100  116 PHE B C   
1325 O O   . PHE B 107 ? 0.8022 0.7656 0.4835 0.1948 0.0039  0.0056  116 PHE B O   
1326 C CB  . PHE B 107 ? 0.7471 0.7416 0.4541 0.1895 0.0211  0.0160  116 PHE B CB  
1327 C CG  . PHE B 107 ? 0.7355 0.7455 0.4542 0.1887 0.0293  0.0217  116 PHE B CG  
1328 C CD1 . PHE B 107 ? 0.7515 0.7724 0.4675 0.2003 0.0327  0.0257  116 PHE B CD1 
1329 C CD2 . PHE B 107 ? 0.7219 0.7352 0.4543 0.1764 0.0332  0.0231  116 PHE B CD2 
1330 C CE1 . PHE B 107 ? 0.7333 0.7677 0.4604 0.1988 0.0399  0.0315  116 PHE B CE1 
1331 C CE2 . PHE B 107 ? 0.7156 0.7417 0.4588 0.1753 0.0400  0.0284  116 PHE B CE2 
1332 C CZ  . PHE B 107 ? 0.7284 0.7647 0.4691 0.1862 0.0433  0.0328  116 PHE B CZ  
1333 N N   . LYS B 108 ? 0.7918 0.7724 0.4697 0.2084 0.0093  0.0112  117 LYS B N   
1334 C CA  . LYS B 108 ? 0.8361 0.8049 0.5067 0.2063 0.0034  0.0081  117 LYS B CA  
1335 C C   . LYS B 108 ? 0.7910 0.7657 0.4742 0.1938 0.0084  0.0111  117 LYS B C   
1336 O O   . LYS B 108 ? 0.7329 0.7233 0.4245 0.1948 0.0153  0.0160  117 LYS B O   
1337 C CB  . LYS B 108 ? 0.9014 0.8715 0.5595 0.2207 0.0006  0.0076  117 LYS B CB  
1338 C CG  . LYS B 108 ? 1.0101 0.9656 0.6511 0.2318 -0.0086 0.0020  117 LYS B CG  
1339 C CD  . LYS B 108 ? 1.0694 1.0316 0.6989 0.2494 -0.0094 0.0022  117 LYS B CD  
1340 C CE  . LYS B 108 ? 1.1670 1.1139 0.7789 0.2612 -0.0195 -0.0040 117 LYS B CE  
1341 N NZ  . LYS B 108 ? 1.1597 1.1165 0.7621 0.2792 -0.0186 -0.0034 117 LYS B NZ  
1342 N N   . THR B 109 ? 0.8087 0.7719 0.4936 0.1823 0.0050  0.0084  118 THR B N   
1343 C CA  . THR B 109 ? 0.8159 0.7824 0.5111 0.1704 0.0086  0.0104  118 THR B CA  
1344 C C   . THR B 109 ? 0.8608 0.8126 0.5471 0.1673 0.0017  0.0072  118 THR B C   
1345 O O   . THR B 109 ? 0.8303 0.7669 0.5052 0.1701 -0.0060 0.0031  118 THR B O   
1346 C CB  . THR B 109 ? 0.8093 0.7782 0.5172 0.1579 0.0123  0.0110  118 THR B CB  
1347 O OG1 . THR B 109 ? 0.7987 0.7528 0.5024 0.1514 0.0062  0.0068  118 THR B OG1 
1348 C CG2 . THR B 109 ? 0.8132 0.7927 0.5280 0.1609 0.0173  0.0133  118 THR B CG2 
1349 N N   . LYS B 110 ? 0.9186 0.8741 0.6100 0.1612 0.0043  0.0090  119 LYS B N   
1350 C CA  . LYS B 110 ? 0.9477 0.8903 0.6325 0.1562 -0.0011 0.0068  119 LYS B CA  
1351 C C   . LYS B 110 ? 0.9756 0.9040 0.6586 0.1474 -0.0061 0.0038  119 LYS B C   
1352 O O   . LYS B 110 ? 1.0302 0.9434 0.7022 0.1477 -0.0137 0.0012  119 LYS B O   
1353 C CB  . LYS B 110 ? 0.9582 0.9094 0.6524 0.1488 0.0038  0.0096  119 LYS B CB  
1354 C CG  . LYS B 110 ? 0.9864 0.9454 0.6954 0.1370 0.0097  0.0114  119 LYS B CG  
1355 C CD  . LYS B 110 ? 1.0327 1.0011 0.7508 0.1313 0.0144  0.0139  119 LYS B CD  
1356 C CE  . LYS B 110 ? 1.0661 1.0276 0.7868 0.1193 0.0132  0.0127  119 LYS B CE  
1357 N NZ  . LYS B 110 ? 1.0646 1.0283 0.7946 0.1106 0.0160  0.0125  119 LYS B NZ  
1358 N N   . ASP B 111 ? 0.9660 0.8990 0.6590 0.1402 -0.0025 0.0043  120 ASP B N   
1359 C CA  . ASP B 111 ? 0.9947 0.9170 0.6884 0.1305 -0.0064 0.0020  120 ASP B CA  
1360 C C   . ASP B 111 ? 1.0409 0.9539 0.7266 0.1366 -0.0123 -0.0011 120 ASP B C   
1361 O O   . ASP B 111 ? 1.1154 1.0169 0.7990 0.1299 -0.0176 -0.0033 120 ASP B O   
1362 C CB  . ASP B 111 ? 0.9942 0.9262 0.7026 0.1196 0.0000  0.0036  120 ASP B CB  
1363 C CG  . ASP B 111 ? 1.0053 0.9404 0.7193 0.1108 0.0027  0.0053  120 ASP B CG  
1364 O OD1 . ASP B 111 ? 0.9997 0.9299 0.7064 0.1137 0.0001  0.0055  120 ASP B OD1 
1365 O OD2 . ASP B 111 ? 1.0455 0.9874 0.7706 0.1017 0.0073  0.0062  120 ASP B OD2 
1366 N N   . GLY B 112 ? 1.0295 0.9479 0.7114 0.1485 -0.0114 -0.0010 121 GLY B N   
1367 C CA  . GLY B 112 ? 1.0221 0.9314 0.6947 0.1563 -0.0177 -0.0044 121 GLY B CA  
1368 C C   . GLY B 112 ? 0.9666 0.8878 0.6407 0.1664 -0.0132 -0.0031 121 GLY B C   
1369 O O   . GLY B 112 ? 0.9464 0.8829 0.6295 0.1664 -0.0051 0.0008  121 GLY B O   
1370 N N   . ASP B 113 ? 0.9781 0.8921 0.6432 0.1748 -0.0187 -0.0063 122 ASP B N   
1371 C CA  . ASP B 113 ? 0.9570 0.8807 0.6215 0.1855 -0.0154 -0.0054 122 ASP B CA  
1372 C C   . ASP B 113 ? 0.9060 0.8324 0.5798 0.1786 -0.0131 -0.0056 122 ASP B C   
1373 O O   . ASP B 113 ? 0.8498 0.7653 0.5242 0.1704 -0.0181 -0.0087 122 ASP B O   
1374 C CB  . ASP B 113 ? 0.9940 0.9086 0.6421 0.2001 -0.0230 -0.0090 122 ASP B CB  
1375 C CG  . ASP B 113 ? 1.0503 0.9667 0.6902 0.2089 -0.0236 -0.0081 122 ASP B CG  
1376 O OD1 . ASP B 113 ? 1.1166 1.0400 0.7637 0.2027 -0.0187 -0.0048 122 ASP B OD1 
1377 O OD2 . ASP B 113 ? 1.0994 1.0106 0.7259 0.2224 -0.0290 -0.0108 122 ASP B OD2 
1378 N N   . ILE B 114 ? 0.8619 0.8032 0.5436 0.1815 -0.0055 -0.0021 123 ILE B N   
1379 C CA  . ILE B 114 ? 0.8365 0.7822 0.5273 0.1763 -0.0024 -0.0019 123 ILE B CA  
1380 C C   . ILE B 114 ? 0.8171 0.7688 0.5027 0.1894 -0.0013 -0.0012 123 ILE B C   
1381 O O   . ILE B 114 ? 0.7998 0.7611 0.4833 0.1979 0.0026  0.0022  123 ILE B O   
1382 C CB  . ILE B 114 ? 0.8108 0.7693 0.5174 0.1661 0.0062  0.0024  123 ILE B CB  
1383 C CG1 . ILE B 114 ? 0.8719 0.8294 0.5825 0.1571 0.0071  0.0034  123 ILE B CG1 
1384 C CG2 . ILE B 114 ? 0.8086 0.7680 0.5240 0.1584 0.0075  0.0013  123 ILE B CG2 
1385 C CD1 . ILE B 114 ? 0.8835 0.8559 0.6062 0.1531 0.0157  0.0085  123 ILE B CD1 
1386 N N   . GLY B 115 ? 0.8109 0.7585 0.4955 0.1905 -0.0040 -0.0039 124 GLY B N   
1387 C CA  . GLY B 115 ? 0.7895 0.7454 0.4720 0.2012 -0.0012 -0.0023 124 GLY B CA  
1388 C C   . GLY B 115 ? 0.7631 0.7364 0.4575 0.1992 0.0091  0.0043  124 GLY B C   
1389 O O   . GLY B 115 ? 0.7173 0.6950 0.4240 0.1872 0.0136  0.0066  124 GLY B O   
1390 N N   . ALA B 116 ? 0.7500 0.7329 0.4408 0.2108 0.0126  0.0076  125 ALA B N   
1391 C CA  . ALA B 116 ? 0.7592 0.7590 0.4606 0.2106 0.0220  0.0147  125 ALA B CA  
1392 C C   . ALA B 116 ? 0.7528 0.7576 0.4492 0.2218 0.0232  0.0161  125 ALA B C   
1393 O O   . ALA B 116 ? 0.7669 0.7660 0.4496 0.2334 0.0179  0.0128  125 ALA B O   
1394 C CB  . ALA B 116 ? 0.7650 0.7744 0.4672 0.2136 0.0262  0.0194  125 ALA B CB  
1395 N N   A VAL B 117 ? 0.7446 0.7592 0.4515 0.2182 0.0296  0.0206  126 VAL B N   
1396 N N   B VAL B 117 ? 0.7442 0.7592 0.4512 0.2182 0.0298  0.0208  126 VAL B N   
1397 N N   C VAL B 117 ? 0.7446 0.7592 0.4515 0.2182 0.0296  0.0206  126 VAL B N   
1398 N N   D VAL B 117 ? 0.7442 0.7592 0.4512 0.2182 0.0298  0.0208  126 VAL B N   
1399 C CA  A VAL B 117 ? 0.7588 0.7799 0.4625 0.2281 0.0319  0.0231  126 VAL B CA  
1400 C CA  B VAL B 117 ? 0.7572 0.7785 0.4616 0.2273 0.0321  0.0232  126 VAL B CA  
1401 C CA  C VAL B 117 ? 0.7588 0.7799 0.4625 0.2281 0.0319  0.0231  126 VAL B CA  
1402 C CA  D VAL B 117 ? 0.7572 0.7785 0.4616 0.2273 0.0321  0.0232  126 VAL B CA  
1403 C C   A VAL B 117 ? 0.7525 0.7911 0.4636 0.2306 0.0409  0.0322  126 VAL B C   
1404 C C   B VAL B 117 ? 0.7515 0.7904 0.4629 0.2305 0.0410  0.0323  126 VAL B C   
1405 C C   C VAL B 117 ? 0.7525 0.7911 0.4636 0.2306 0.0409  0.0322  126 VAL B C   
1406 C C   D VAL B 117 ? 0.7515 0.7904 0.4629 0.2305 0.0410  0.0323  126 VAL B C   
1407 O O   A VAL B 117 ? 0.7395 0.7842 0.4643 0.2199 0.0460  0.0361  126 VAL B O   
1408 O O   B VAL B 117 ? 0.7383 0.7835 0.4633 0.2200 0.0462  0.0364  126 VAL B O   
1409 O O   C VAL B 117 ? 0.7395 0.7842 0.4643 0.2199 0.0460  0.0361  126 VAL B O   
1410 O O   D VAL B 117 ? 0.7383 0.7835 0.4633 0.2200 0.0462  0.0364  126 VAL B O   
1411 C CB  A VAL B 117 ? 0.7570 0.7731 0.4660 0.2218 0.0307  0.0203  126 VAL B CB  
1412 C CB  B VAL B 117 ? 0.7536 0.7704 0.4649 0.2197 0.0315  0.0208  126 VAL B CB  
1413 C CB  C VAL B 117 ? 0.7570 0.7731 0.4660 0.2218 0.0307  0.0203  126 VAL B CB  
1414 C CB  D VAL B 117 ? 0.7536 0.7704 0.4649 0.2197 0.0315  0.0208  126 VAL B CB  
1415 C CG1 A VAL B 117 ? 0.7650 0.7649 0.4690 0.2172 0.0220  0.0120  126 VAL B CG1 
1416 C CG1 B VAL B 117 ? 0.7511 0.7789 0.4669 0.2240 0.0374  0.0264  126 VAL B CG1 
1417 C CG1 C VAL B 117 ? 0.7650 0.7649 0.4690 0.2172 0.0220  0.0120  126 VAL B CG1 
1418 C CG1 D VAL B 117 ? 0.7511 0.7789 0.4669 0.2240 0.0374  0.0264  126 VAL B CG1 
1419 C CG2 A VAL B 117 ? 0.7424 0.7660 0.4678 0.2096 0.0372  0.0247  126 VAL B CG2 
1420 C CG2 B VAL B 117 ? 0.7680 0.7699 0.4696 0.2219 0.0224  0.0126  126 VAL B CG2 
1421 C CG2 C VAL B 117 ? 0.7424 0.7660 0.4678 0.2096 0.0372  0.0247  126 VAL B CG2 
1422 C CG2 D VAL B 117 ? 0.7680 0.7699 0.4696 0.2219 0.0224  0.0126  126 VAL B CG2 
1423 N N   . ALA B 118 ? 0.7629 0.8096 0.4653 0.2446 0.0425  0.0355  127 ALA B N   
1424 C CA  . ALA B 118 ? 0.7770 0.8418 0.4861 0.2480 0.0511  0.0451  127 ALA B CA  
1425 C C   . ALA B 118 ? 0.8149 0.8862 0.5274 0.2506 0.0552  0.0494  127 ALA B C   
1426 O O   . ALA B 118 ? 0.8179 0.8930 0.5199 0.2639 0.0550  0.0505  127 ALA B O   
1427 C CB  . ALA B 118 ? 0.7948 0.8666 0.4931 0.2615 0.0512  0.0469  127 ALA B CB  
1428 N N   . LEU B 119 ? 0.7883 0.8593 0.5137 0.2388 0.0579  0.0510  128 LEU B N   
1429 C CA  . LEU B 119 ? 0.7898 0.8669 0.5198 0.2402 0.0620  0.0557  128 LEU B CA  
1430 C C   . LEU B 119 ? 0.8012 0.8875 0.5482 0.2290 0.0686  0.0629  128 LEU B C   
1431 O O   . LEU B 119 ? 0.8307 0.9134 0.5859 0.2179 0.0680  0.0609  128 LEU B O   
1432 C CB  . LEU B 119 ? 0.7841 0.8483 0.5105 0.2384 0.0564  0.0484  128 LEU B CB  
1433 C CG  . LEU B 119 ? 0.7801 0.8338 0.4900 0.2490 0.0488  0.0408  128 LEU B CG  
1434 C CD1 . LEU B 119 ? 0.7645 0.8049 0.4738 0.2439 0.0427  0.0330  128 LEU B CD1 
1435 C CD2 . LEU B 119 ? 0.8147 0.8763 0.5139 0.2650 0.0504  0.0444  128 LEU B CD2 
1436 N N   . ASP B 120 ? 0.8416 0.9400 0.5934 0.2324 0.0747  0.0715  129 ASP B N   
1437 C CA  . ASP B 120 ? 0.8882 0.9974 0.6555 0.2237 0.0811  0.0800  129 ASP B CA  
1438 C C   . ASP B 120 ? 0.8829 0.9896 0.6589 0.2168 0.0824  0.0814  129 ASP B C   
1439 O O   . ASP B 120 ? 0.9739 1.0860 0.7477 0.2236 0.0851  0.0864  129 ASP B O   
1440 C CB  . ASP B 120 ? 0.9671 1.0928 0.7331 0.2329 0.0866  0.0893  129 ASP B CB  
1441 C CG  . ASP B 120 ? 1.0337 1.1717 0.8147 0.2250 0.0924  0.0980  129 ASP B CG  
1442 O OD1 . ASP B 120 ? 1.0698 1.2028 0.8607 0.2128 0.0913  0.0954  129 ASP B OD1 
1443 O OD2 . ASP B 120 ? 1.0792 1.2322 0.8621 0.2311 0.0979  0.1074  129 ASP B OD2 
1444 N N   . TYR B 121 ? 0.8176 0.9162 0.6025 0.2045 0.0804  0.0770  130 TYR B N   
1445 C CA  . TYR B 121 ? 0.8100 0.9055 0.6036 0.1975 0.0811  0.0775  130 TYR B CA  
1446 C C   . TYR B 121 ? 0.7632 0.8611 0.5721 0.1847 0.0834  0.0804  130 TYR B C   
1447 O O   . TYR B 121 ? 0.8029 0.9020 0.6149 0.1804 0.0833  0.0796  130 TYR B O   
1448 C CB  . TYR B 121 ? 0.8168 0.8989 0.6048 0.1961 0.0751  0.0677  130 TYR B CB  
1449 C CG  . TYR B 121 ? 0.8659 0.9448 0.6402 0.2082 0.0723  0.0649  130 TYR B CG  
1450 C CD1 . TYR B 121 ? 0.8629 0.9443 0.6364 0.2131 0.0742  0.0684  130 TYR B CD1 
1451 C CD2 . TYR B 121 ? 0.9282 1.0008 0.6897 0.2150 0.0673  0.0586  130 TYR B CD2 
1452 C CE1 . TYR B 121 ? 0.9130 0.9913 0.6733 0.2247 0.0713  0.0656  130 TYR B CE1 
1453 C CE2 . TYR B 121 ? 0.9312 1.0001 0.6797 0.2266 0.0640  0.0555  130 TYR B CE2 
1454 C CZ  . TYR B 121 ? 0.9278 0.9999 0.6757 0.2316 0.0661  0.0589  130 TYR B CZ  
1455 O OH  . TYR B 121 ? 1.0096 1.0782 0.7444 0.2434 0.0626  0.0557  130 TYR B OH  
1456 N N   . PRO B 122 ? 0.7514 0.8497 0.5702 0.1787 0.0852  0.0836  131 PRO B N   
1457 C CA  . PRO B 122 ? 0.7385 0.8382 0.5718 0.1670 0.0867  0.0858  131 PRO B CA  
1458 C C   . PRO B 122 ? 0.6830 0.7729 0.5178 0.1585 0.0823  0.0764  131 PRO B C   
1459 O O   . PRO B 122 ? 0.6432 0.7245 0.4696 0.1604 0.0781  0.0685  131 PRO B O   
1460 C CB  . PRO B 122 ? 0.7559 0.8555 0.5965 0.1641 0.0882  0.0897  131 PRO B CB  
1461 C CG  . PRO B 122 ? 0.7706 0.8719 0.6011 0.1755 0.0890  0.0921  131 PRO B CG  
1462 C CD  . PRO B 122 ? 0.7845 0.8814 0.6009 0.1832 0.0856  0.0850  131 PRO B CD  
1463 N N   . ALA B 123 ? 0.6848 0.7767 0.5306 0.1492 0.0833  0.0778  132 ALA B N   
1464 C CA  . ALA B 123 ? 0.6849 0.7695 0.5332 0.1407 0.0799  0.0701  132 ALA B CA  
1465 C C   . ALA B 123 ? 0.6714 0.7469 0.5199 0.1367 0.0766  0.0631  132 ALA B C   
1466 O O   . ALA B 123 ? 0.6545 0.7226 0.4983 0.1340 0.0728  0.0553  132 ALA B O   
1467 C CB  . ALA B 123 ? 0.6972 0.7868 0.5576 0.1326 0.0818  0.0740  132 ALA B CB  
1468 N N   . GLY B 124 ? 0.6308 0.7067 0.4836 0.1369 0.0777  0.0659  133 GLY B N   
1469 C CA  . GLY B 124 ? 0.5906 0.6590 0.4436 0.1342 0.0747  0.0596  133 GLY B CA  
1470 C C   . GLY B 124 ? 0.5793 0.6417 0.4203 0.1404 0.0712  0.0532  133 GLY B C   
1471 O O   . GLY B 124 ? 0.5659 0.6224 0.4073 0.1375 0.0683  0.0470  133 GLY B O   
1472 N N   . THR B 125 ? 0.5666 0.6306 0.3974 0.1488 0.0712  0.0543  134 THR B N   
1473 C CA  . THR B 125 ? 0.5893 0.6466 0.4078 0.1551 0.0669  0.0478  134 THR B CA  
1474 C C   . THR B 125 ? 0.6008 0.6518 0.4169 0.1497 0.0630  0.0408  134 THR B C   
1475 O O   . THR B 125 ? 0.6208 0.6647 0.4281 0.1529 0.0584  0.0346  134 THR B O   
1476 C CB  . THR B 125 ? 0.6063 0.6674 0.4141 0.1671 0.0679  0.0516  134 THR B CB  
1477 O OG1 . THR B 125 ? 0.6166 0.6854 0.4278 0.1712 0.0724  0.0598  134 THR B OG1 
1478 C CG2 . THR B 125 ? 0.6053 0.6593 0.4008 0.1748 0.0631  0.0455  134 THR B CG2 
1479 N N   . SER B 126 ? 0.5873 0.6403 0.4108 0.1419 0.0644  0.0417  135 SER B N   
1480 C CA  . SER B 126 ? 0.5743 0.6221 0.3966 0.1358 0.0613  0.0361  135 SER B CA  
1481 C C   . SER B 126 ? 0.5581 0.5982 0.3791 0.1318 0.0571  0.0284  135 SER B C   
1482 O O   . SER B 126 ? 0.5421 0.5828 0.3704 0.1276 0.0577  0.0274  135 SER B O   
1483 C CB  . SER B 126 ? 0.5681 0.6199 0.4004 0.1277 0.0639  0.0385  135 SER B CB  
1484 O OG  . SER B 126 ? 0.5648 0.6229 0.3967 0.1311 0.0666  0.0442  135 SER B OG  
1485 N N   . GLY B 127 ? 0.5505 0.5838 0.3626 0.1335 0.0526  0.0233  136 GLY B N   
1486 C CA  . GLY B 127 ? 0.5609 0.5876 0.3722 0.1293 0.0482  0.0163  136 GLY B CA  
1487 C C   . GLY B 127 ? 0.5728 0.5953 0.3758 0.1370 0.0447  0.0136  136 GLY B C   
1488 O O   . GLY B 127 ? 0.6032 0.6200 0.4048 0.1338 0.0403  0.0077  136 GLY B O   
1489 N N   . SER B 128 ? 0.5760 0.6016 0.3739 0.1468 0.0465  0.0178  137 SER B N   
1490 C CA  . SER B 128 ? 0.5626 0.5840 0.3508 0.1560 0.0429  0.0153  137 SER B CA  
1491 C C   . SER B 128 ? 0.5579 0.5707 0.3367 0.1572 0.0367  0.0099  137 SER B C   
1492 O O   . SER B 128 ? 0.5801 0.5922 0.3546 0.1586 0.0365  0.0112  137 SER B O   
1493 C CB  . SER B 128 ? 0.5772 0.6044 0.3604 0.1666 0.0462  0.0215  137 SER B CB  
1494 O OG  . SER B 128 ? 0.5672 0.6010 0.3591 0.1651 0.0510  0.0264  137 SER B OG  
1495 N N   . PRO B 129 ? 0.5509 0.5568 0.3261 0.1574 0.0312  0.0039  138 PRO B N   
1496 C CA  . PRO B 129 ? 0.5647 0.5613 0.3310 0.1586 0.0244  -0.0010 138 PRO B CA  
1497 C C   . PRO B 129 ? 0.5967 0.5893 0.3494 0.1711 0.0211  -0.0011 138 PRO B C   
1498 O O   . PRO B 129 ? 0.6174 0.6130 0.3651 0.1811 0.0222  0.0007  138 PRO B O   
1499 C CB  . PRO B 129 ? 0.5647 0.5564 0.3325 0.1553 0.0195  -0.0070 138 PRO B CB  
1500 C CG  . PRO B 129 ? 0.5526 0.5504 0.3245 0.1590 0.0230  -0.0049 138 PRO B CG  
1501 C CD  . PRO B 129 ? 0.5421 0.5487 0.3218 0.1563 0.0305  0.0015  138 PRO B CD  
1502 N N   . ILE B 130 ? 0.5961 0.5807 0.3419 0.1707 0.0159  -0.0043 139 ILE B N   
1503 C CA  . ILE B 130 ? 0.6312 0.6098 0.3628 0.1822 0.0111  -0.0058 139 ILE B CA  
1504 C C   . ILE B 130 ? 0.6537 0.6204 0.3800 0.1812 0.0020  -0.0129 139 ILE B C   
1505 O O   . ILE B 130 ? 0.6302 0.5928 0.3622 0.1703 -0.0001 -0.0154 139 ILE B O   
1506 C CB  . ILE B 130 ? 0.6355 0.6142 0.3636 0.1827 0.0121  -0.0033 139 ILE B CB  
1507 C CG1 . ILE B 130 ? 0.6329 0.6243 0.3669 0.1841 0.0209  0.0040  139 ILE B CG1 
1508 C CG2 . ILE B 130 ? 0.6570 0.6272 0.3698 0.1940 0.0055  -0.0064 139 ILE B CG2 
1509 C CD1 . ILE B 130 ? 0.6459 0.6384 0.3818 0.1793 0.0227  0.0061  139 ILE B CD1 
1510 N N   . LEU B 131 ? 0.6799 0.6420 0.3962 0.1921 -0.0027 -0.0158 140 LEU B N   
1511 C CA  . LEU B 131 ? 0.7216 0.6727 0.4335 0.1918 -0.0119 -0.0227 140 LEU B CA  
1512 C C   . LEU B 131 ? 0.7540 0.6942 0.4511 0.2013 -0.0199 -0.0262 140 LEU B C   
1513 O O   . LEU B 131 ? 0.7585 0.7018 0.4467 0.2130 -0.0180 -0.0237 140 LEU B O   
1514 C CB  . LEU B 131 ? 0.7558 0.7098 0.4678 0.1977 -0.0120 -0.0240 140 LEU B CB  
1515 C CG  . LEU B 131 ? 0.7658 0.7318 0.4890 0.1938 -0.0034 -0.0194 140 LEU B CG  
1516 C CD1 . LEU B 131 ? 0.7722 0.7392 0.4941 0.2000 -0.0047 -0.0213 140 LEU B CD1 
1517 C CD2 . LEU B 131 ? 0.7470 0.7150 0.4834 0.1786 -0.0010 -0.0195 140 LEU B CD2 
1518 N N   . ASP B 132 ? 0.7768 0.7050 0.4714 0.1969 -0.0289 -0.0320 141 ASP B N   
1519 C CA  . ASP B 132 ? 0.8181 0.7334 0.4984 0.2064 -0.0390 -0.0370 141 ASP B CA  
1520 C C   . ASP B 132 ? 0.8595 0.7723 0.5354 0.2143 -0.0438 -0.0412 141 ASP B C   
1521 O O   . ASP B 132 ? 0.8387 0.7592 0.5237 0.2106 -0.0395 -0.0403 141 ASP B O   
1522 C CB  . ASP B 132 ? 0.8132 0.7158 0.4929 0.1973 -0.0469 -0.0407 141 ASP B CB  
1523 C CG  . ASP B 132 ? 0.8174 0.7167 0.5068 0.1851 -0.0508 -0.0439 141 ASP B CG  
1524 O OD1 . ASP B 132 ? 0.7670 0.6726 0.4627 0.1846 -0.0486 -0.0445 141 ASP B OD1 
1525 O OD2 . ASP B 132 ? 0.8876 0.7790 0.5791 0.1755 -0.0555 -0.0453 141 ASP B OD2 
1526 N N   . LYS B 133 ? 0.9240 0.8253 0.5862 0.2245 -0.0532 -0.0461 142 LYS B N   
1527 C CA  . LYS B 133 ? 0.9870 0.8843 0.6411 0.2357 -0.0593 -0.0506 142 LYS B CA  
1528 C C   . LYS B 133 ? 0.9556 0.8509 0.6198 0.2255 -0.0627 -0.0542 142 LYS B C   
1529 O O   . LYS B 133 ? 0.9240 0.8218 0.5871 0.2318 -0.0636 -0.0561 142 LYS B O   
1530 C CB  . LYS B 133 ? 1.0457 0.9292 0.6831 0.2473 -0.0699 -0.0557 142 LYS B CB  
1531 C CG  . LYS B 133 ? 1.1072 0.9957 0.7323 0.2627 -0.0663 -0.0527 142 LYS B CG  
1532 C CD  . LYS B 133 ? 1.1551 1.0320 0.7666 0.2700 -0.0738 -0.0555 142 LYS B CD  
1533 C CE  . LYS B 133 ? 1.1705 1.0565 0.7723 0.2843 -0.0680 -0.0514 142 LYS B CE  
1534 N NZ  . LYS B 133 ? 1.1833 1.0577 0.7678 0.2973 -0.0773 -0.0560 142 LYS B NZ  
1535 N N   . CYS B 134 ? 0.9184 0.8108 0.5927 0.2104 -0.0641 -0.0547 143 CYS B N   
1536 C CA  . CYS B 134 ? 0.9137 0.8053 0.5985 0.2000 -0.0676 -0.0580 143 CYS B CA  
1537 C C   . CYS B 134 ? 0.8459 0.7521 0.5451 0.1918 -0.0572 -0.0538 143 CYS B C   
1538 O O   . CYS B 134 ? 0.8456 0.7531 0.5548 0.1821 -0.0587 -0.0560 143 CYS B O   
1539 C CB  . CYS B 134 ? 0.9623 0.8438 0.6506 0.1879 -0.0746 -0.0603 143 CYS B CB  
1540 S SG  . CYS B 134 ? 1.0076 0.8693 0.6805 0.1964 -0.0899 -0.0669 143 CYS B SG  
1541 N N   . GLY B 135 ? 0.8254 0.7421 0.5254 0.1959 -0.0473 -0.0482 144 GLY B N   
1542 C CA  . GLY B 135 ? 0.8122 0.7419 0.5253 0.1886 -0.0377 -0.0441 144 GLY B CA  
1543 C C   . GLY B 135 ? 0.7790 0.7120 0.5036 0.1737 -0.0337 -0.0418 144 GLY B C   
1544 O O   . GLY B 135 ? 0.7473 0.6901 0.4833 0.1669 -0.0271 -0.0395 144 GLY B O   
1545 N N   . ARG B 136 ? 0.7864 0.7119 0.5080 0.1690 -0.0374 -0.0422 145 ARG B N   
1546 C CA  . ARG B 136 ? 0.7875 0.7161 0.5193 0.1550 -0.0337 -0.0398 145 ARG B CA  
1547 C C   . ARG B 136 ? 0.7373 0.6735 0.4701 0.1558 -0.0249 -0.0340 145 ARG B C   
1548 O O   . ARG B 136 ? 0.7199 0.6535 0.4425 0.1658 -0.0252 -0.0325 145 ARG B O   
1549 C CB  . ARG B 136 ? 0.8220 0.7386 0.5504 0.1490 -0.0422 -0.0428 145 ARG B CB  
1550 C CG  . ARG B 136 ? 0.8548 0.7671 0.5879 0.1429 -0.0494 -0.0476 145 ARG B CG  
1551 C CD  . ARG B 136 ? 0.9054 0.8040 0.6333 0.1387 -0.0591 -0.0502 145 ARG B CD  
1552 N NE  . ARG B 136 ? 0.9825 0.8716 0.6958 0.1504 -0.0632 -0.0508 145 ARG B NE  
1553 C CZ  . ARG B 136 ? 1.0359 0.9139 0.7419 0.1494 -0.0687 -0.0511 145 ARG B CZ  
1554 N NH1 . ARG B 136 ? 1.0909 0.9654 0.8030 0.1364 -0.0706 -0.0502 145 ARG B NH1 
1555 N NH2 . ARG B 136 ? 1.0678 0.9384 0.7600 0.1620 -0.0721 -0.0520 145 ARG B NH2 
1556 N N   . VAL B 137 ? 0.7093 0.6547 0.4541 0.1461 -0.0178 -0.0309 146 VAL B N   
1557 C CA  . VAL B 137 ? 0.6853 0.6384 0.4324 0.1462 -0.0096 -0.0253 146 VAL B CA  
1558 C C   . VAL B 137 ? 0.7063 0.6529 0.4488 0.1429 -0.0118 -0.0246 146 VAL B C   
1559 O O   . VAL B 137 ? 0.7015 0.6442 0.4484 0.1323 -0.0146 -0.0262 146 VAL B O   
1560 C CB  . VAL B 137 ? 0.6715 0.6356 0.4321 0.1377 -0.0020 -0.0226 146 VAL B CB  
1561 C CG1 . VAL B 137 ? 0.6656 0.6370 0.4282 0.1389 0.0054  -0.0169 146 VAL B CG1 
1562 C CG2 . VAL B 137 ? 0.6929 0.6622 0.4580 0.1403 -0.0006 -0.0237 146 VAL B CG2 
1563 N N   . ILE B 138 ? 0.6836 0.6293 0.4174 0.1518 -0.0108 -0.0222 147 ILE B N   
1564 C CA  . ILE B 138 ? 0.6832 0.6223 0.4111 0.1505 -0.0133 -0.0216 147 ILE B CA  
1565 C C   . ILE B 138 ? 0.6636 0.6123 0.3983 0.1463 -0.0049 -0.0164 147 ILE B C   
1566 O O   . ILE B 138 ? 0.6484 0.5934 0.3794 0.1447 -0.0058 -0.0153 147 ILE B O   
1567 C CB  . ILE B 138 ? 0.6905 0.6219 0.4034 0.1639 -0.0188 -0.0232 147 ILE B CB  
1568 C CG1 . ILE B 138 ? 0.6947 0.6353 0.4043 0.1758 -0.0131 -0.0197 147 ILE B CG1 
1569 C CG2 . ILE B 138 ? 0.6925 0.6118 0.3985 0.1664 -0.0288 -0.0291 147 ILE B CG2 
1570 C CD1 . ILE B 138 ? 0.7312 0.6676 0.4268 0.1886 -0.0162 -0.0196 147 ILE B CD1 
1571 N N   . GLY B 139 ? 0.6194 0.5796 0.3635 0.1448 0.0025  -0.0132 148 GLY B N   
1572 C CA  . GLY B 139 ? 0.6007 0.5697 0.3524 0.1398 0.0097  -0.0084 148 GLY B CA  
1573 C C   . GLY B 139 ? 0.5901 0.5703 0.3484 0.1429 0.0168  -0.0044 148 GLY B C   
1574 O O   . GLY B 139 ? 0.5719 0.5527 0.3281 0.1493 0.0160  -0.0053 148 GLY B O   
1575 N N   . LEU B 140 ? 0.5793 0.5675 0.3449 0.1392 0.0230  0.0000  149 LEU B N   
1576 C CA  . LEU B 140 ? 0.5809 0.5797 0.3545 0.1404 0.0297  0.0045  149 LEU B CA  
1577 C C   . LEU B 140 ? 0.5894 0.5945 0.3610 0.1466 0.0340  0.0101  149 LEU B C   
1578 O O   . LEU B 140 ? 0.5914 0.5946 0.3595 0.1460 0.0331  0.0106  149 LEU B O   
1579 C CB  . LEU B 140 ? 0.5752 0.5788 0.3616 0.1292 0.0332  0.0047  149 LEU B CB  
1580 C CG  . LEU B 140 ? 0.5772 0.5771 0.3676 0.1219 0.0300  -0.0003 149 LEU B CG  
1581 C CD1 . LEU B 140 ? 0.5857 0.5924 0.3884 0.1129 0.0344  0.0005  149 LEU B CD1 
1582 C CD2 . LEU B 140 ? 0.5866 0.5845 0.3739 0.1275 0.0273  -0.0028 149 LEU B CD2 
1583 N N   . TYR B 141 ? 0.5843 0.5970 0.3581 0.1524 0.0382  0.0144  150 TYR B N   
1584 C CA  . TYR B 141 ? 0.5964 0.6176 0.3692 0.1596 0.0429  0.0209  150 TYR B CA  
1585 C C   . TYR B 141 ? 0.5823 0.6121 0.3682 0.1520 0.0489  0.0257  150 TYR B C   
1586 O O   . TYR B 141 ? 0.6250 0.6559 0.4193 0.1460 0.0501  0.0250  150 TYR B O   
1587 C CB  . TYR B 141 ? 0.6221 0.6467 0.3897 0.1704 0.0439  0.0231  150 TYR B CB  
1588 C CG  . TYR B 141 ? 0.6234 0.6594 0.3930 0.1764 0.0501  0.0312  150 TYR B CG  
1589 C CD1 . TYR B 141 ? 0.6230 0.6673 0.4041 0.1720 0.0557  0.0367  150 TYR B CD1 
1590 C CD2 . TYR B 141 ? 0.6484 0.6874 0.4085 0.1867 0.0501  0.0336  150 TYR B CD2 
1591 C CE1 . TYR B 141 ? 0.6549 0.7103 0.4387 0.1767 0.0612  0.0449  150 TYR B CE1 
1592 C CE2 . TYR B 141 ? 0.6479 0.6990 0.4102 0.1923 0.0560  0.0415  150 TYR B CE2 
1593 C CZ  . TYR B 141 ? 0.6655 0.7251 0.4400 0.1872 0.0617  0.0476  150 TYR B CZ  
1594 O OH  . TYR B 141 ? 0.6730 0.7451 0.4504 0.1923 0.0674  0.0563  150 TYR B OH  
1595 N N   . GLY B 142 ? 0.5956 0.6317 0.3834 0.1527 0.0522  0.0304  151 GLY B N   
1596 C CA  . GLY B 142 ? 0.6022 0.6471 0.4028 0.1463 0.0576  0.0357  151 GLY B CA  
1597 C C   . GLY B 142 ? 0.6140 0.6602 0.4185 0.1402 0.0583  0.0362  151 GLY B C   
1598 O O   . GLY B 142 ? 0.6239 0.6775 0.4394 0.1350 0.0624  0.0406  151 GLY B O   
1599 N N   . ASN B 143 ? 0.5950 0.6345 0.3913 0.1408 0.0543  0.0322  152 ASN B N   
1600 C CA  . ASN B 143 ? 0.6009 0.6424 0.3995 0.1369 0.0551  0.0334  152 ASN B CA  
1601 C C   . ASN B 143 ? 0.5978 0.6393 0.3855 0.1463 0.0536  0.0344  152 ASN B C   
1602 O O   . ASN B 143 ? 0.6063 0.6384 0.3834 0.1495 0.0484  0.0297  152 ASN B O   
1603 C CB  . ASN B 143 ? 0.6087 0.6422 0.4082 0.1275 0.0518  0.0280  152 ASN B CB  
1604 C CG  . ASN B 143 ? 0.6286 0.6656 0.4336 0.1219 0.0535  0.0298  152 ASN B CG  
1605 O OD1 . ASN B 143 ? 0.6339 0.6804 0.4467 0.1219 0.0578  0.0350  152 ASN B OD1 
1606 N ND2 . ASN B 143 ? 0.6221 0.6516 0.4233 0.1170 0.0499  0.0256  152 ASN B ND2 
1607 N N   . GLY B 144 ? 0.6004 0.6523 0.3916 0.1499 0.0577  0.0404  153 GLY B N   
1608 C CA  . GLY B 144 ? 0.6496 0.7031 0.4309 0.1592 0.0566  0.0414  153 GLY B CA  
1609 C C   . GLY B 144 ? 0.6885 0.7555 0.4773 0.1603 0.0619  0.0484  153 GLY B C   
1610 O O   . GLY B 144 ? 0.6735 0.7436 0.4731 0.1512 0.0639  0.0498  153 GLY B O   
1611 N N   . VAL B 145 ? 0.7485 0.8238 0.5322 0.1713 0.0639  0.0528  154 VAL B N   
1612 C CA  . VAL B 145 ? 0.7955 0.8836 0.5831 0.1744 0.0677  0.0588  154 VAL B CA  
1613 C C   . VAL B 145 ? 0.8622 0.9636 0.6511 0.1830 0.0727  0.0664  154 VAL B C   
1614 O O   . VAL B 145 ? 0.8247 0.9238 0.6071 0.1894 0.0721  0.0657  154 VAL B O   
1615 C CB  . VAL B 145 ? 0.8269 0.9096 0.6029 0.1799 0.0635  0.0549  154 VAL B CB  
1616 C CG1 . VAL B 145 ? 0.8211 0.9050 0.5832 0.1945 0.0618  0.0547  154 VAL B CG1 
1617 C CG2 . VAL B 145 ? 0.8662 0.9572 0.6496 0.1762 0.0658  0.0581  154 VAL B CG2 
1618 N N   . VAL B 146 ? 0.9118 1.0274 0.7099 0.1826 0.0776  0.0736  155 VAL B N   
1619 C CA  . VAL B 146 ? 0.9475 1.0787 0.7488 0.1900 0.0831  0.0825  155 VAL B CA  
1620 C C   . VAL B 146 ? 0.9869 1.1268 0.7800 0.2009 0.0835  0.0844  155 VAL B C   
1621 O O   . VAL B 146 ? 0.9910 1.1330 0.7874 0.1976 0.0830  0.0840  155 VAL B O   
1622 C CB  . VAL B 146 ? 0.9521 1.0930 0.7713 0.1803 0.0879  0.0897  155 VAL B CB  
1623 C CG1 . VAL B 146 ? 0.9875 1.1447 0.8111 0.1866 0.0937  0.0997  155 VAL B CG1 
1624 C CG2 . VAL B 146 ? 0.9705 1.1015 0.7963 0.1703 0.0867  0.0866  155 VAL B CG2 
1625 N N   . ILE B 147 ? 1.0240 1.1680 0.8059 0.2141 0.0839  0.0857  156 ILE B N   
1626 C CA  . ILE B 147 ? 1.0948 1.2418 0.8637 0.2265 0.0818  0.0840  156 ILE B CA  
1627 C C   . ILE B 147 ? 1.1413 1.3100 0.9155 0.2332 0.0882  0.0937  156 ILE B C   
1628 O O   . ILE B 147 ? 1.0645 1.2444 0.8518 0.2282 0.0939  0.1019  156 ILE B O   
1629 C CB  . ILE B 147 ? 1.1298 1.2661 0.8809 0.2378 0.0768  0.0777  156 ILE B CB  
1630 C CG1 . ILE B 147 ? 1.1465 1.2852 0.8967 0.2419 0.0792  0.0807  156 ILE B CG1 
1631 C CG2 . ILE B 147 ? 1.1332 1.2490 0.8774 0.2324 0.0692  0.0675  156 ILE B CG2 
1632 C CD1 . ILE B 147 ? 1.1477 1.2837 0.8801 0.2577 0.0759  0.0774  156 ILE B CD1 
1633 N N   A LYS B 148 ? 1.1869 1.3611 0.9513 0.2442 0.0870  0.0930  157 LYS B N   
1634 N N   B LYS B 148 ? 1.1869 1.3611 0.9513 0.2442 0.0870  0.0930  157 LYS B N   
1635 N N   C LYS B 148 ? 1.1781 1.3522 0.9423 0.2443 0.0870  0.0929  157 LYS B N   
1636 N N   D LYS B 148 ? 1.1781 1.3522 0.9423 0.2443 0.0870  0.0929  157 LYS B N   
1637 C CA  A LYS B 148 ? 1.2325 1.4285 0.9991 0.2534 0.0927  0.1017  157 LYS B CA  
1638 C CA  B LYS B 148 ? 1.2325 1.4285 0.9991 0.2534 0.0927  0.1017  157 LYS B CA  
1639 C CA  C LYS B 148 ? 1.2173 1.4132 0.9838 0.2535 0.0926  0.1016  157 LYS B CA  
1640 C CA  D LYS B 148 ? 1.2173 1.4132 0.9838 0.2535 0.0926  0.1016  157 LYS B CA  
1641 C C   A LYS B 148 ? 1.2589 1.4675 1.0312 0.2560 0.0989  0.1105  157 LYS B C   
1642 C C   B LYS B 148 ? 1.2589 1.4675 1.0312 0.2560 0.0989  0.1105  157 LYS B C   
1643 C C   C LYS B 148 ? 1.2500 1.4586 1.0221 0.2562 0.0988  0.1105  157 LYS B C   
1644 C C   D LYS B 148 ? 1.2500 1.4586 1.0221 0.2562 0.0988  0.1105  157 LYS B C   
1645 O O   A LYS B 148 ? 1.2751 1.5016 1.0609 0.2530 0.1051  0.1203  157 LYS B O   
1646 O O   B LYS B 148 ? 1.2751 1.5016 1.0609 0.2530 0.1051  0.1203  157 LYS B O   
1647 O O   C LYS B 148 ? 1.2674 1.4942 1.0526 0.2536 0.1051  0.1203  157 LYS B O   
1648 O O   D LYS B 148 ? 1.2674 1.4942 1.0526 0.2536 0.1051  0.1203  157 LYS B O   
1649 C CB  A LYS B 148 ? 1.2521 1.4484 1.0009 0.2695 0.0892  0.0974  157 LYS B CB  
1650 C CB  B LYS B 148 ? 1.2521 1.4484 1.0009 0.2695 0.0892  0.0974  157 LYS B CB  
1651 C CB  C LYS B 148 ? 1.2249 1.4207 0.9735 0.2693 0.0890  0.0972  157 LYS B CB  
1652 C CB  D LYS B 148 ? 1.2249 1.4207 0.9735 0.2693 0.0890  0.0972  157 LYS B CB  
1653 C CG  A LYS B 148 ? 1.2593 1.4391 0.9986 0.2686 0.0816  0.0876  157 LYS B CG  
1654 C CG  B LYS B 148 ? 1.2593 1.4391 0.9986 0.2686 0.0816  0.0876  157 LYS B CG  
1655 C CG  C LYS B 148 ? 1.2239 1.3973 0.9589 0.2698 0.0801  0.0855  157 LYS B CG  
1656 C CG  D LYS B 148 ? 1.2239 1.3973 0.9589 0.2698 0.0801  0.0855  157 LYS B CG  
1657 C CD  A LYS B 148 ? 1.2727 1.4452 0.9913 0.2843 0.0758  0.0811  157 LYS B CD  
1658 C CD  B LYS B 148 ? 1.2727 1.4452 0.9913 0.2843 0.0758  0.0811  157 LYS B CD  
1659 C CD  C LYS B 148 ? 1.2189 1.3784 0.9405 0.2762 0.0755  0.0795  157 LYS B CD  
1660 C CD  D LYS B 148 ? 1.2189 1.3784 0.9405 0.2762 0.0755  0.0795  157 LYS B CD  
1661 C CE  A LYS B 148 ? 1.2792 1.4713 0.9925 0.2995 0.0795  0.0865  157 LYS B CE  
1662 C CE  B LYS B 148 ? 1.2792 1.4713 0.9925 0.2995 0.0795  0.0865  157 LYS B CE  
1663 C CE  C LYS B 148 ? 1.2232 1.3842 0.9265 0.2945 0.0724  0.0768  157 LYS B CE  
1664 C CE  D LYS B 148 ? 1.2232 1.3842 0.9265 0.2945 0.0724  0.0768  157 LYS B CE  
1665 N NZ  A LYS B 148 ? 1.2719 1.4735 0.9904 0.2984 0.0806  0.0884  157 LYS B NZ  
1666 N NZ  B LYS B 148 ? 1.2719 1.4735 0.9904 0.2984 0.0806  0.0884  157 LYS B NZ  
1667 N NZ  C LYS B 148 ? 1.2179 1.4027 0.9234 0.3049 0.0794  0.0860  157 LYS B NZ  
1668 N NZ  D LYS B 148 ? 1.2179 1.4027 0.9234 0.3049 0.0794  0.0860  157 LYS B NZ  
1669 N N   . ASN B 149 ? 1.2819 1.4811 1.0448 0.2608 0.0968  0.1072  158 ASN B N   
1670 C CA  . ASN B 149 ? 1.2770 1.4864 1.0414 0.2658 0.1019  0.1147  158 ASN B CA  
1671 C C   . ASN B 149 ? 1.2144 1.4258 0.9963 0.2520 0.1060  0.1209  158 ASN B C   
1672 O O   . ASN B 149 ? 1.1954 1.4195 0.9820 0.2549 0.1115  0.1300  158 ASN B O   
1673 C CB  . ASN B 149 ? 1.3605 1.5568 1.1087 0.2749 0.0974  0.1080  158 ASN B CB  
1674 C CG  . ASN B 149 ? 1.3985 1.5865 1.1279 0.2875 0.0910  0.0994  158 ASN B CG  
1675 O OD1 . ASN B 149 ? 1.4890 1.6832 1.2153 0.2924 0.0905  0.0991  158 ASN B OD1 
1676 N ND2 . ASN B 149 ? 1.3874 1.5609 1.1039 0.2931 0.0855  0.0921  158 ASN B ND2 
1677 N N   . GLY B 150 ? 1.1833 1.3821 0.9736 0.2381 0.1031  0.1161  159 GLY B N   
1678 C CA  . GLY B 150 ? 1.1116 1.3088 0.9168 0.2252 0.1055  0.1201  159 GLY B CA  
1679 C C   . GLY B 150 ? 1.0895 1.2689 0.8899 0.2216 0.1013  0.1127  159 GLY B C   
1680 O O   . GLY B 150 ? 1.0655 1.2397 0.8774 0.2097 0.1015  0.1131  159 GLY B O   
1681 N N   A SER B 151 ? 1.0808 1.2513 0.8647 0.2318 0.0971  0.1060  160 SER B N   
1682 N N   B SER B 151 ? 1.0826 1.2531 0.8666 0.2318 0.0971  0.1060  160 SER B N   
1683 N N   C SER B 151 ? 1.0808 1.2513 0.8647 0.2318 0.0971  0.1060  160 SER B N   
1684 N N   D SER B 151 ? 1.0826 1.2531 0.8666 0.2318 0.0971  0.1060  160 SER B N   
1685 C CA  A SER B 151 ? 1.0507 1.2044 0.8281 0.2301 0.0924  0.0982  160 SER B CA  
1686 C CA  B SER B 151 ? 1.0534 1.2072 0.8308 0.2302 0.0924  0.0982  160 SER B CA  
1687 C CA  C SER B 151 ? 1.0507 1.2044 0.8281 0.2301 0.0924  0.0982  160 SER B CA  
1688 C CA  D SER B 151 ? 1.0534 1.2072 0.8308 0.2302 0.0924  0.0982  160 SER B CA  
1689 C C   A SER B 151 ? 1.0185 1.1566 0.7979 0.2192 0.0870  0.0893  160 SER B C   
1690 C C   B SER B 151 ? 1.0203 1.1584 0.7995 0.2193 0.0869  0.0892  160 SER B C   
1691 C C   C SER B 151 ? 1.0185 1.1566 0.7979 0.2192 0.0870  0.0893  160 SER B C   
1692 C C   D SER B 151 ? 1.0203 1.1584 0.7995 0.2193 0.0869  0.0892  160 SER B C   
1693 O O   A SER B 151 ? 1.0080 1.1472 0.7898 0.2158 0.0862  0.0882  160 SER B O   
1694 O O   B SER B 151 ? 1.0102 1.1494 0.7917 0.2161 0.0861  0.0881  160 SER B O   
1695 O O   C SER B 151 ? 1.0080 1.1472 0.7898 0.2158 0.0862  0.0882  160 SER B O   
1696 O O   D SER B 151 ? 1.0102 1.1494 0.7917 0.2161 0.0861  0.0881  160 SER B O   
1697 C CB  A SER B 151 ? 1.0635 1.2132 0.8229 0.2448 0.0891  0.0940  160 SER B CB  
1698 C CB  B SER B 151 ? 1.0680 1.2182 0.8275 0.2450 0.0892  0.0942  160 SER B CB  
1699 C CB  C SER B 151 ? 1.0635 1.2132 0.8229 0.2448 0.0891  0.0940  160 SER B CB  
1700 C CB  D SER B 151 ? 1.0680 1.2182 0.8275 0.2450 0.0892  0.0942  160 SER B CB  
1701 O OG  A SER B 151 ? 1.0650 1.2008 0.8198 0.2433 0.0850  0.0878  160 SER B OG  
1702 O OG  B SER B 151 ? 1.0777 1.2299 0.8274 0.2534 0.0870  0.0916  160 SER B OG  
1703 O OG  C SER B 151 ? 1.0650 1.2008 0.8198 0.2433 0.0850  0.0878  160 SER B OG  
1704 O OG  D SER B 151 ? 1.0777 1.2299 0.8274 0.2534 0.0870  0.0916  160 SER B OG  
1705 N N   . TYR B 152 ? 0.9811 1.1060 0.7595 0.2141 0.0835  0.0834  161 TYR B N   
1706 C CA  . TYR B 152 ? 0.9493 1.0591 0.7285 0.2042 0.0782  0.0747  161 TYR B CA  
1707 C C   . TYR B 152 ? 0.8690 0.9660 0.6320 0.2115 0.0714  0.0660  161 TYR B C   
1708 O O   . TYR B 152 ? 0.8197 0.9143 0.5737 0.2200 0.0698  0.0646  161 TYR B O   
1709 C CB  . TYR B 152 ? 0.9467 1.0502 0.7349 0.1941 0.0781  0.0732  161 TYR B CB  
1710 C CG  . TYR B 152 ? 0.9546 1.0484 0.7488 0.1817 0.0750  0.0673  161 TYR B CG  
1711 C CD1 . TYR B 152 ? 0.9523 1.0515 0.7580 0.1732 0.0774  0.0703  161 TYR B CD1 
1712 C CD2 . TYR B 152 ? 0.9624 1.0422 0.7512 0.1785 0.0696  0.0588  161 TYR B CD2 
1713 C CE1 . TYR B 152 ? 0.9392 1.0302 0.7498 0.1626 0.0747  0.0650  161 TYR B CE1 
1714 C CE2 . TYR B 152 ? 0.9407 1.0131 0.7351 0.1674 0.0672  0.0540  161 TYR B CE2 
1715 C CZ  . TYR B 152 ? 0.9398 1.0177 0.7446 0.1596 0.0698  0.0570  161 TYR B CZ  
1716 O OH  . TYR B 152 ? 0.9897 1.0611 0.7998 0.1491 0.0677  0.0525  161 TYR B OH  
1717 N N   . VAL B 153 ? 0.8133 0.9014 0.5733 0.2072 0.0670  0.0601  162 VAL B N   
1718 C CA  . VAL B 153 ? 0.7845 0.8571 0.5313 0.2103 0.0592  0.0510  162 VAL B CA  
1719 C C   . VAL B 153 ? 0.7382 0.7994 0.4914 0.1966 0.0561  0.0456  162 VAL B C   
1720 O O   . VAL B 153 ? 0.7107 0.7732 0.4703 0.1892 0.0571  0.0462  162 VAL B O   
1721 C CB  . VAL B 153 ? 0.7822 0.8546 0.5187 0.2183 0.0565  0.0495  162 VAL B CB  
1722 C CG1 . VAL B 153 ? 0.7775 0.8343 0.4987 0.2242 0.0481  0.0411  162 VAL B CG1 
1723 C CG2 . VAL B 153 ? 0.8334 0.9218 0.5678 0.2298 0.0615  0.0567  162 VAL B CG2 
1724 N N   . SER B 154 ? 0.7108 0.7618 0.4616 0.1940 0.0523  0.0404  163 SER B N   
1725 C CA  . SER B 154 ? 0.6715 0.7124 0.4277 0.1818 0.0493  0.0351  163 SER B CA  
1726 C C   . SER B 154 ? 0.6695 0.6963 0.4145 0.1827 0.0416  0.0277  163 SER B C   
1727 O O   . SER B 154 ? 0.6667 0.6877 0.3998 0.1922 0.0372  0.0247  163 SER B O   
1728 C CB  . SER B 154 ? 0.6620 0.7019 0.4237 0.1784 0.0501  0.0344  163 SER B CB  
1729 O OG  . SER B 154 ? 0.6460 0.6761 0.4108 0.1683 0.0463  0.0285  163 SER B OG  
1730 N N   . ALA B 155 ? 0.6178 0.6385 0.3667 0.1725 0.0396  0.0248  164 ALA B N   
1731 C CA  . ALA B 155 ? 0.6152 0.6215 0.3564 0.1696 0.0322  0.0181  164 ALA B CA  
1732 C C   . ALA B 155 ? 0.6279 0.6283 0.3685 0.1687 0.0292  0.0143  164 ALA B C   
1733 O O   . ALA B 155 ? 0.6355 0.6423 0.3854 0.1651 0.0334  0.0164  164 ALA B O   
1734 C CB  . ALA B 155 ? 0.6098 0.6134 0.3582 0.1572 0.0323  0.0170  164 ALA B CB  
1735 N N   . ILE B 156 ? 0.6430 0.6311 0.3734 0.1715 0.0218  0.0088  165 ILE B N   
1736 C CA  . ILE B 156 ? 0.6392 0.6190 0.3709 0.1656 0.0174  0.0039  165 ILE B CA  
1737 C C   . ILE B 156 ? 0.6390 0.6152 0.3782 0.1519 0.0168  0.0023  165 ILE B C   
1738 O O   . ILE B 156 ? 0.6345 0.6005 0.3672 0.1498 0.0111  -0.0007 165 ILE B O   
1739 C CB  . ILE B 156 ? 0.6640 0.6318 0.3821 0.1737 0.0089  -0.0011 165 ILE B CB  
1740 C CG1 . ILE B 156 ? 0.6975 0.6700 0.4067 0.1887 0.0098  0.0006  165 ILE B CG1 
1741 C CG2 . ILE B 156 ? 0.6591 0.6201 0.3801 0.1676 0.0046  -0.0057 165 ILE B CG2 
1742 C CD1 . ILE B 156 ? 0.7263 0.6871 0.4207 0.1988 0.0010  -0.0045 165 ILE B CD1 
1743 N N   . THR B 157 ? 0.6291 0.6132 0.3810 0.1433 0.0223  0.0044  166 THR B N   
1744 C CA  . THR B 157 ? 0.6029 0.5863 0.3633 0.1304 0.0230  0.0034  166 THR B CA  
1745 C C   . THR B 157 ? 0.6170 0.5941 0.3791 0.1244 0.0188  -0.0012 166 THR B C   
1746 O O   . THR B 157 ? 0.6079 0.5897 0.3759 0.1241 0.0209  -0.0014 166 THR B O   
1747 C CB  . THR B 157 ? 0.5895 0.5843 0.3624 0.1252 0.0304  0.0074  166 THR B CB  
1748 O OG1 . THR B 157 ? 0.5666 0.5677 0.3382 0.1310 0.0338  0.0120  166 THR B OG1 
1749 C CG2 . THR B 157 ? 0.5854 0.5800 0.3661 0.1132 0.0310  0.0061  166 THR B CG2 
1750 N N   . GLN B 158 ? 0.6231 0.5902 0.3803 0.1199 0.0129  -0.0045 167 GLN B N   
1751 C CA  . GLN B 158 ? 0.6302 0.5918 0.3899 0.1125 0.0085  -0.0085 167 GLN B CA  
1752 C C   . GLN B 158 ? 0.6788 0.6407 0.4446 0.1007 0.0095  -0.0082 167 GLN B C   
1753 O O   . GLN B 158 ? 0.6449 0.6053 0.4078 0.0999 0.0101  -0.0064 167 GLN B O   
1754 C CB  . GLN B 158 ? 0.6353 0.5844 0.3833 0.1179 0.0000  -0.0120 167 GLN B CB  
1755 C CG  . GLN B 158 ? 0.6362 0.5791 0.3862 0.1112 -0.0055 -0.0160 167 GLN B CG  
1756 C CD  . GLN B 158 ? 0.6423 0.5928 0.4007 0.1100 -0.0026 -0.0169 167 GLN B CD  
1757 O OE1 . GLN B 158 ? 0.6195 0.5799 0.3881 0.1045 0.0036  -0.0150 167 GLN B OE1 
1758 N NE2 . GLN B 158 ? 0.6470 0.5928 0.4006 0.1160 -0.0075 -0.0200 167 GLN B NE2 
1759 N N   . GLY B 159 ? 0.7334 0.6980 0.5073 0.0922 0.0099  -0.0100 168 GLY B N   
1760 C CA  . GLY B 159 ? 0.8143 0.7792 0.5933 0.0811 0.0101  -0.0101 168 GLY B CA  
1761 C C   . GLY B 159 ? 0.9083 0.8623 0.6817 0.0771 0.0027  -0.0126 168 GLY B C   
1762 O O   . GLY B 159 ? 0.8969 0.8429 0.6630 0.0828 -0.0029 -0.0147 168 GLY B O   
1763 N N   A LYS B 160 ? 0.9551 0.9090 0.7321 0.0671 0.0026  -0.0121 169 LYS B N   
1764 N N   B LYS B 160 ? 0.9551 0.9090 0.7321 0.0671 0.0026  -0.0121 169 LYS B N   
1765 N N   C LYS B 160 ? 0.9761 0.9299 0.7529 0.0672 0.0026  -0.0121 169 LYS B N   
1766 N N   D LYS B 160 ? 0.9761 0.9299 0.7529 0.0672 0.0026  -0.0121 169 LYS B N   
1767 C CA  A LYS B 160 ? 0.9994 0.9443 0.7734 0.0606 -0.0040 -0.0136 169 LYS B CA  
1768 C CA  B LYS B 160 ? 0.9994 0.9443 0.7734 0.0606 -0.0040 -0.0136 169 LYS B CA  
1769 C CA  C LYS B 160 ? 1.0181 0.9630 0.7921 0.0604 -0.0040 -0.0135 169 LYS B CA  
1770 C CA  D LYS B 160 ? 1.0181 0.9630 0.7921 0.0604 -0.0040 -0.0135 169 LYS B CA  
1771 C C   A LYS B 160 ? 1.0402 0.9916 0.8238 0.0533 -0.0036 -0.0153 169 LYS B C   
1772 C C   B LYS B 160 ? 1.0402 0.9916 0.8238 0.0533 -0.0036 -0.0153 169 LYS B C   
1773 C C   C LYS B 160 ? 1.0530 1.0043 0.8365 0.0536 -0.0036 -0.0154 169 LYS B C   
1774 C C   D LYS B 160 ? 1.0530 1.0043 0.8365 0.0536 -0.0036 -0.0154 169 LYS B C   
1775 O O   A LYS B 160 ? 1.0334 0.9964 0.8261 0.0507 0.0027  -0.0148 169 LYS B O   
1776 O O   B LYS B 160 ? 1.0334 0.9964 0.8261 0.0507 0.0027  -0.0148 169 LYS B O   
1777 O O   C LYS B 160 ? 1.0401 1.0030 0.8326 0.0517 0.0026  -0.0150 169 LYS B O   
1778 O O   D LYS B 160 ? 1.0401 1.0030 0.8326 0.0517 0.0026  -0.0150 169 LYS B O   
1779 C CB  A LYS B 160 ? 0.9937 0.9355 0.7657 0.0542 -0.0040 -0.0113 169 LYS B CB  
1780 C CB  B LYS B 160 ? 0.9937 0.9355 0.7657 0.0542 -0.0040 -0.0113 169 LYS B CB  
1781 C CB  C LYS B 160 ? 1.0165 0.9588 0.7890 0.0536 -0.0037 -0.0112 169 LYS B CB  
1782 C CB  D LYS B 160 ? 1.0165 0.9588 0.7890 0.0536 -0.0037 -0.0112 169 LYS B CB  
1783 C CG  A LYS B 160 ? 0.9899 0.9208 0.7575 0.0478 -0.0112 -0.0117 169 LYS B CG  
1784 C CG  B LYS B 160 ? 0.9899 0.9208 0.7575 0.0478 -0.0112 -0.0117 169 LYS B CG  
1785 C CG  C LYS B 160 ? 0.9983 0.9399 0.7654 0.0594 -0.0010 -0.0090 169 LYS B CG  
1786 C CG  D LYS B 160 ? 0.9983 0.9399 0.7654 0.0594 -0.0010 -0.0090 169 LYS B CG  
1787 C CD  A LYS B 160 ? 0.9779 0.9068 0.7439 0.0411 -0.0105 -0.0090 169 LYS B CD  
1788 C CD  B LYS B 160 ? 0.9779 0.9068 0.7439 0.0411 -0.0105 -0.0090 169 LYS B CD  
1789 C CD  C LYS B 160 ? 0.9911 0.9215 0.7460 0.0689 -0.0067 -0.0098 169 LYS B CD  
1790 C CD  D LYS B 160 ? 0.9911 0.9215 0.7460 0.0689 -0.0067 -0.0098 169 LYS B CD  
1791 C CE  A LYS B 160 ? 0.9794 0.8984 0.7425 0.0333 -0.0174 -0.0086 169 LYS B CE  
1792 C CE  B LYS B 160 ? 0.9794 0.8984 0.7425 0.0333 -0.0174 -0.0086 169 LYS B CE  
1793 C CE  C LYS B 160 ? 0.9849 0.9175 0.7355 0.0760 -0.0033 -0.0076 169 LYS B CE  
1794 C CE  D LYS B 160 ? 0.9849 0.9175 0.7355 0.0760 -0.0033 -0.0076 169 LYS B CE  
1795 N NZ  A LYS B 160 ? 0.9775 0.8987 0.7424 0.0247 -0.0149 -0.0055 169 LYS B NZ  
1796 N NZ  B LYS B 160 ? 0.9775 0.8987 0.7424 0.0247 -0.0149 -0.0055 169 LYS B NZ  
1797 N NZ  C LYS B 160 ? 0.9664 0.9097 0.7218 0.0826 0.0025  -0.0066 169 LYS B NZ  
1798 N NZ  D LYS B 160 ? 0.9664 0.9097 0.7218 0.0826 0.0025  -0.0066 169 LYS B NZ  
1799 N N   . ARG B 161 ? 1.0979 1.0420 0.8795 0.0505 -0.0104 -0.0174 170 ARG B N   
1800 C CA  . ARG B 161 ? 1.1678 1.1182 0.9587 0.0429 -0.0109 -0.0190 170 ARG B CA  
1801 C C   . ARG B 161 ? 1.2355 1.1817 1.0271 0.0322 -0.0146 -0.0175 170 ARG B C   
1802 O O   . ARG B 161 ? 1.3102 1.2433 1.0934 0.0329 -0.0217 -0.0176 170 ARG B O   
1803 C CB  . ARG B 161 ? 1.2324 1.1790 1.0217 0.0485 -0.0160 -0.0224 170 ARG B CB  
1804 C CG  . ARG B 161 ? 1.2462 1.1996 1.0450 0.0419 -0.0171 -0.0244 170 ARG B CG  
1805 C CD  . ARG B 161 ? 1.2947 1.2415 1.0904 0.0469 -0.0241 -0.0280 170 ARG B CD  
1806 N NE  . ARG B 161 ? 1.3195 1.2718 1.1242 0.0397 -0.0265 -0.0299 170 ARG B NE  
1807 C CZ  . ARG B 161 ? 1.3034 1.2618 1.1130 0.0428 -0.0264 -0.0328 170 ARG B CZ  
1808 N NH1 . ARG B 161 ? 1.2320 1.1916 1.0385 0.0531 -0.0239 -0.0341 170 ARG B NH1 
1809 N NH2 . ARG B 161 ? 1.2930 1.2568 1.1111 0.0354 -0.0288 -0.0343 170 ARG B NH2 
1810 N N   . GLU B 162 ? 1.3102 1.2670 1.1109 0.0231 -0.0100 -0.0161 171 GLU B N   
1811 C CA  . GLU B 162 ? 1.3373 1.2924 1.1391 0.0125 -0.0120 -0.0135 171 GLU B CA  
1812 C C   . GLU B 162 ? 1.2537 1.2126 1.0629 0.0051 -0.0154 -0.0145 171 GLU B C   
1813 O O   . GLU B 162 ? 1.1525 1.1028 0.9589 0.0063 -0.0226 -0.0164 171 GLU B O   
1814 C CB  . GLU B 162 ? 1.3999 1.3651 1.2062 0.0079 -0.0045 -0.0110 171 GLU B CB  
1815 C CG  . GLU B 162 ? 1.4447 1.4062 1.2443 0.0140 -0.0017 -0.0096 171 GLU B CG  
1816 C CD  . GLU B 162 ? 1.4651 1.4192 1.2584 0.0097 -0.0034 -0.0065 171 GLU B CD  
1817 O OE1 . GLU B 162 ? 1.4192 1.3809 1.2171 0.0027 0.0005  -0.0045 171 GLU B OE1 
1818 O OE2 . GLU B 162 ? 1.5103 1.4513 1.2938 0.0139 -0.0089 -0.0063 171 GLU B OE2 
1819 S S   A DMS C .   ? 1.4674 1.5596 1.2930 0.1589 0.0798  0.0716  201 DMS B S   
1820 S S   B DMS C .   ? 1.4674 1.5596 1.2930 0.1589 0.0798  0.0716  201 DMS B S   
1821 S S   C DMS C .   ? 1.3943 1.5398 1.2158 0.1992 0.1022  0.1162  201 DMS B S   
1822 S S   D DMS C .   ? 1.3943 1.5398 1.2158 0.1992 0.1022  0.1162  201 DMS B S   
1823 O O   A DMS C .   ? 1.4658 1.5674 1.2868 0.1670 0.0822  0.0768  201 DMS B O   
1824 O O   B DMS C .   ? 1.4658 1.5674 1.2868 0.1670 0.0822  0.0768  201 DMS B O   
1825 O O   C DMS C .   ? 1.3884 1.5455 1.2145 0.2027 0.1077  0.1278  201 DMS B O   
1826 O O   D DMS C .   ? 1.3884 1.5455 1.2145 0.2027 0.1077  0.1278  201 DMS B O   
1827 C C1  A DMS C .   ? 1.4630 1.5493 1.2953 0.1470 0.0773  0.0660  201 DMS B C1  
1828 C C1  B DMS C .   ? 1.4630 1.5493 1.2953 0.1470 0.0773  0.0660  201 DMS B C1  
1829 C C1  C DMS C .   ? 1.3863 1.5198 1.1900 0.2092 0.0971  0.1065  201 DMS B C1  
1830 C C1  D DMS C .   ? 1.3863 1.5198 1.1900 0.2092 0.0971  0.1065  201 DMS B C1  
1831 C C2  A DMS C .   ? 1.4735 1.5531 1.2846 0.1643 0.0739  0.0621  201 DMS B C2  
1832 C C2  B DMS C .   ? 1.4735 1.5531 1.2846 0.1643 0.0739  0.0621  201 DMS B C2  
1833 C C2  C DMS C .   ? 1.3606 1.4933 1.1933 0.1845 0.0990  0.1106  201 DMS B C2  
1834 C C2  D DMS C .   ? 1.3606 1.4933 1.1933 0.1845 0.0990  0.1106  201 DMS B C2  
1835 S S   A DMS D .   ? 4.8508 4.9087 4.7618 0.0453 0.0557  -0.0033 202 DMS B S   
1836 S S   B DMS D .   ? 4.8508 4.9087 4.7618 0.0453 0.0557  -0.0033 202 DMS B S   
1837 S S   C DMS D .   ? 0.8529 0.8964 0.7021 0.1551 0.0646  0.0501  202 DMS B S   
1838 S S   D DMS D .   ? 0.8529 0.8964 0.7021 0.1551 0.0646  0.0501  202 DMS B S   
1839 O O   A DMS D .   ? 4.8351 4.8924 4.7378 0.0447 0.0562  -0.0041 202 DMS B O   
1840 O O   B DMS D .   ? 4.8351 4.8924 4.7378 0.0447 0.0562  -0.0041 202 DMS B O   
1841 O O   C DMS D .   ? 0.8583 0.8977 0.7002 0.1601 0.0606  0.0423  202 DMS B O   
1842 O O   D DMS D .   ? 0.8583 0.8977 0.7002 0.1601 0.0606  0.0423  202 DMS B O   
1843 C C1  A DMS D .   ? 4.8328 4.8915 4.7458 0.0465 0.0545  -0.0081 202 DMS B C1  
1844 C C1  B DMS D .   ? 4.8328 4.8915 4.7458 0.0465 0.0545  -0.0081 202 DMS B C1  
1845 C C1  C DMS D .   ? 0.8286 0.8695 0.6906 0.1444 0.0631  0.0468  202 DMS B C1  
1846 C C1  D DMS D .   ? 0.8286 0.8695 0.6906 0.1444 0.0631  0.0468  202 DMS B C1  
1847 C C2  A DMS D .   ? 4.8236 4.8796 4.7355 0.0501 0.0569  0.0035  202 DMS B C2  
1848 C C2  B DMS D .   ? 4.8236 4.8796 4.7355 0.0501 0.0569  0.0035  202 DMS B C2  
1849 C C2  C DMS D .   ? 0.8562 0.9021 0.7065 0.1602 0.0680  0.0614  202 DMS B C2  
1850 C C2  D DMS D .   ? 0.8562 0.9021 0.7065 0.1602 0.0680  0.0614  202 DMS B C2  
1851 S S   A DMS E .   ? 0.7686 0.8580 0.6059 0.1357 0.0755  0.0634  203 DMS B S   
1852 S S   B DMS E .   ? 0.7686 0.8580 0.6059 0.1357 0.0755  0.0634  203 DMS B S   
1853 O O   A DMS E .   ? 0.7697 0.8575 0.6017 0.1362 0.0734  0.0608  203 DMS B O   
1854 O O   B DMS E .   ? 0.7697 0.8575 0.6017 0.1362 0.0734  0.0608  203 DMS B O   
1855 C C1  A DMS E .   ? 0.7729 0.8497 0.6105 0.1276 0.0717  0.0551  203 DMS B C1  
1856 C C1  B DMS E .   ? 0.7729 0.8497 0.6105 0.1276 0.0717  0.0551  203 DMS B C1  
1857 C C2  A DMS E .   ? 0.7603 0.8584 0.6154 0.1269 0.0792  0.0695  203 DMS B C2  
1858 C C2  B DMS E .   ? 0.7603 0.8584 0.6154 0.1269 0.0792  0.0695  203 DMS B C2  
# 
