data_7HOU
# 
_entry.id   7HOU 
# 
_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   7HOU         pdb_00007hou 10.2210/pdb7hou/pdb 
WWPDB D_1001407744 ?            ?                   
# 
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                        7HOU 
_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 '(2P)-2-(6-fluoro-5-methylpyridin-3-yl)-N-(1-methyl-1H-pyrazol-4-yl)benzamide' 310.326   1   ? ?    ? ? 
5 non-polymer syn 'SULFATE ION'                                                                  96.063    1   ? ?    ? ? 
6 water       nat water                                                                          18.015    101 ? ?    ? ? 
# 
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 '(2P)-2-(6-fluoro-5-methylpyridin-3-yl)-N-(1-methyl-1H-pyrazol-4-yl)benzamide' A1BG3 
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 
A1BG3 non-polymer         . '(2P)-2-(6-fluoro-5-methylpyridin-3-yl)-N-(1-methyl-1H-pyrazol-4-yl)benzamide' ? 'C17 H15 F N4 O' 
310.326 
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        A1BG3 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BG3 
_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 A1BG3 1  204 301 A1BG3 LIG B . 
G 5 SO4   1  205 302 SO4   SO4 B . 
H 6 HOH   1  101 105 HOH   HOH A . 
H 6 HOH   2  102 48  HOH   HOH A . 
H 6 HOH   3  103 98  HOH   HOH A . 
H 6 HOH   4  104 34  HOH   HOH A . 
H 6 HOH   5  105 20  HOH   HOH A . 
H 6 HOH   6  106 54  HOH   HOH A . 
H 6 HOH   7  107 135 HOH   HOH A . 
H 6 HOH   8  108 16  HOH   HOH A . 
H 6 HOH   9  109 49  HOH   HOH A . 
H 6 HOH   10 110 65  HOH   HOH A . 
H 6 HOH   11 111 118 HOH   HOH A . 
H 6 HOH   12 112 103 HOH   HOH A . 
H 6 HOH   13 113 110 HOH   HOH A . 
H 6 HOH   14 114 70  HOH   HOH A . 
H 6 HOH   15 115 120 HOH   HOH A . 
H 6 HOH   16 116 36  HOH   HOH A . 
H 6 HOH   17 117 50  HOH   HOH A . 
H 6 HOH   18 118 121 HOH   HOH A . 
H 6 HOH   19 119 29  HOH   HOH A . 
H 6 HOH   20 120 119 HOH   HOH A . 
H 6 HOH   21 121 129 HOH   HOH A . 
H 6 HOH   22 122 27  HOH   HOH A . 
I 6 HOH   1  301 92  HOH   HOH B . 
I 6 HOH   2  302 51  HOH   HOH B . 
I 6 HOH   3  303 58  HOH   HOH B . 
I 6 HOH   4  304 126 HOH   HOH B . 
I 6 HOH   5  305 11  HOH   HOH B . 
I 6 HOH   6  306 5   HOH   HOH B . 
I 6 HOH   7  307 90  HOH   HOH B . 
I 6 HOH   8  308 57  HOH   HOH B . 
I 6 HOH   9  309 117 HOH   HOH B . 
I 6 HOH   10 310 40  HOH   HOH B . 
I 6 HOH   11 311 1   HOH   HOH B . 
I 6 HOH   12 312 77  HOH   HOH B . 
I 6 HOH   13 313 14  HOH   HOH B . 
I 6 HOH   14 314 9   HOH   HOH B . 
I 6 HOH   15 315 31  HOH   HOH B . 
I 6 HOH   16 316 30  HOH   HOH B . 
I 6 HOH   17 317 4   HOH   HOH B . 
I 6 HOH   18 318 81  HOH   HOH B . 
I 6 HOH   19 319 67  HOH   HOH B . 
I 6 HOH   20 320 23  HOH   HOH B . 
I 6 HOH   21 321 66  HOH   HOH B . 
I 6 HOH   22 322 108 HOH   HOH B . 
I 6 HOH   23 323 60  HOH   HOH B . 
I 6 HOH   24 324 100 HOH   HOH B . 
I 6 HOH   25 325 63  HOH   HOH B . 
I 6 HOH   26 326 24  HOH   HOH B . 
I 6 HOH   27 327 32  HOH   HOH B . 
I 6 HOH   28 328 46  HOH   HOH B . 
I 6 HOH   29 329 89  HOH   HOH B . 
I 6 HOH   30 330 132 HOH   HOH B . 
I 6 HOH   31 331 106 HOH   HOH B . 
I 6 HOH   32 332 125 HOH   HOH B . 
I 6 HOH   33 333 42  HOH   HOH B . 
I 6 HOH   34 334 62  HOH   HOH B . 
I 6 HOH   35 335 107 HOH   HOH B . 
I 6 HOH   36 336 56  HOH   HOH B . 
I 6 HOH   37 337 35  HOH   HOH B . 
I 6 HOH   38 338 2   HOH   HOH B . 
I 6 HOH   39 339 123 HOH   HOH B . 
I 6 HOH   40 340 116 HOH   HOH B . 
I 6 HOH   41 341 124 HOH   HOH B . 
I 6 HOH   42 342 13  HOH   HOH B . 
I 6 HOH   43 343 94  HOH   HOH B . 
I 6 HOH   44 344 21  HOH   HOH B . 
I 6 HOH   45 345 28  HOH   HOH B . 
I 6 HOH   46 346 12  HOH   HOH B . 
I 6 HOH   47 347 69  HOH   HOH B . 
I 6 HOH   48 348 39  HOH   HOH B . 
I 6 HOH   49 349 68  HOH   HOH B . 
I 6 HOH   50 350 102 HOH   HOH B . 
I 6 HOH   51 351 10  HOH   HOH B . 
I 6 HOH   52 352 115 HOH   HOH B . 
I 6 HOH   53 353 3   HOH   HOH B . 
I 6 HOH   54 354 72  HOH   HOH B . 
I 6 HOH   55 355 82  HOH   HOH B . 
I 6 HOH   56 356 133 HOH   HOH B . 
I 6 HOH   57 357 64  HOH   HOH B . 
I 6 HOH   58 358 17  HOH   HOH B . 
I 6 HOH   59 359 43  HOH   HOH B . 
I 6 HOH   60 360 18  HOH   HOH B . 
I 6 HOH   61 361 73  HOH   HOH B . 
I 6 HOH   62 362 127 HOH   HOH B . 
I 6 HOH   63 363 112 HOH   HOH B . 
I 6 HOH   64 364 87  HOH   HOH B . 
I 6 HOH   65 365 131 HOH   HOH B . 
I 6 HOH   66 366 26  HOH   HOH B . 
I 6 HOH   67 367 122 HOH   HOH B . 
I 6 HOH   68 368 61  HOH   HOH B . 
I 6 HOH   69 369 128 HOH   HOH B . 
I 6 HOH   70 370 83  HOH   HOH B . 
I 6 HOH   71 371 79  HOH   HOH B . 
I 6 HOH   72 372 80  HOH   HOH B . 
I 6 HOH   73 373 59  HOH   HOH B . 
I 6 HOH   74 374 45  HOH   HOH B . 
I 6 HOH   75 375 85  HOH   HOH B . 
I 6 HOH   76 376 134 HOH   HOH B . 
I 6 HOH   77 377 44  HOH   HOH B . 
I 6 HOH   78 378 109 HOH   HOH B . 
I 6 HOH   79 379 75  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           7HOU 
_cell.length_a           42.503 
_cell.length_b           42.503 
_cell.length_c           216.415 
_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                         7HOU 
_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          7HOU 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.11 
_exptl_crystal.density_percent_sol   41.65 
_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   2023-09-19 
_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                     7HOU 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             216.48 
_reflns.d_resolution_high            1.48 
_reflns.number_obs                   34587 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.103 
_reflns.pdbx_netI_over_sigmaI        10.9 
_reflns.pdbx_redundancy              24.6 
_reflns.pdbx_Rrim_I_all              0.105 
_reflns.pdbx_Rpim_I_all              0.021 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     850293 
_reflns.pdbx_chi_squared             0.29 
_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                  1.48 
_reflns_shell.d_res_low                   1.51 
_reflns_shell.number_measured_all         32517 
_reflns_shell.number_unique_obs           1687 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_chi_squared            0.11 
_reflns_shell.pdbx_redundancy             19.3 
_reflns_shell.percent_possible_obs        99.7 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             11.905 
_reflns_shell.pdbx_Rpim_I_all             2.658 
_reflns_shell.pdbx_CC_half                0.182 
_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                                 7HOU 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     29154 
_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                             54.10 
_refine.ls_d_res_high                            1.48 
_refine.ls_percent_reflns_obs                    89.12 
_refine.ls_R_factor_obs                          0.24049 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.23826 
_refine.ls_R_factor_R_free                       0.28299 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  1550 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.950 
_refine.B_iso_mean                               47.451 
_refine.aniso_B[1][1]                            -0.20 
_refine.aniso_B[2][2]                            -0.20 
_refine.aniso_B[3][3]                            0.39 
_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                       0.113 
_refine.pdbx_overall_ESU_R_Free                  0.115 
_refine.overall_SU_ML                            0.209 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             14.904 
_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         40 
_refine_hist.number_atoms_solvent             101 
_refine_hist.number_atoms_total               1617 
_refine_hist.d_res_high                       1.48 
_refine_hist.d_res_low                        54.10 
# 
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             0.020  0.014  ? 2110 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.008  0.015  ? 1707 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.921  1.640  ? 2579 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.430  1.590  ? 3939 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.695  5.000  ? 250  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       33.041 22.674 ? 86   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.826 15.000 ? 286  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       20.757 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.088  0.200  ? 222  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.012  0.020  ? 2261 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.005  0.020  ? 443  '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                  1.395  2.107  ? 1051 'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.416  1.919  ? 1013 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 2.533  2.837  ? 1206 'X-RAY DIFFRACTION' ? 
r_mcangle_other              2.532  2.841  ? 1207 'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.662  2.691  ? 1059 'X-RAY DIFFRACTION' ? 
r_scbond_other               1.670  2.633  ? 1040 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              2.743  3.470  ? 1362 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       22.932 23.200 ? 2090 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         22.970 22.806 ? 2076 '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                       1.481 
_refine_ls_shell.d_res_low                        1.520 
_refine_ls_shell.number_reflns_R_work             303 
_refine_ls_shell.R_factor_R_work                  0.660 
_refine_ls_shell.percent_reflns_obs               12.75 
_refine_ls_shell.R_factor_R_free                  0.668 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             15 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HOU 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0014704-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HOU 
_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 7HOU A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HOU 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 7HOU SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HOU MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HOU MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HOU LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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 TRP B 41  ? LYS B 45  ? TRP B 50  LYS B 54  1 ? 5 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_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               2.579 
_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  ? MET B 40  ? VAL B 45  MET B 49  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 SER B 128 ? LEU B 131 ? SER B 137 LEU B 140 
AA2 5 VAL B 137 ? TYR B 141 ? VAL B 146 TYR B 150 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 4 5 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O 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 SER B 128 ? N SER B 137 O TYR B 141 ? O TYR B 150 
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                   7HOU 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD2 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    90 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OG 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   SER 
_pdbx_validate_close_contact.auth_seq_id_2    93 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.79 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1  1 C   A THR 60  ? A O   A THR 60  ? A 1.380 1.229 0.151 0.019 N 
2  1 C   A THR 60  ? B O   A THR 60  ? B 1.387 1.229 0.158 0.019 N 
3  1 C   A THR 60  ? C O   A THR 60  ? C 1.380 1.229 0.151 0.019 N 
4  1 C   A THR 60  ? D O   A THR 60  ? D 1.387 1.229 0.158 0.019 N 
5  1 C   B TRP 50  ? A O   B TRP 50  ? A 1.404 1.229 0.175 0.019 N 
6  1 C   B TRP 50  ? B O   B TRP 50  ? B 1.373 1.229 0.144 0.019 N 
7  1 C   B TRP 50  ? C O   B TRP 50  ? C 1.404 1.229 0.175 0.019 N 
8  1 C   B TRP 50  ? D O   B TRP 50  ? D 1.373 1.229 0.144 0.019 N 
9  1 CE1 B TYR 68  ? ? CZ  B TYR 68  ? ? 1.479 1.381 0.098 0.013 N 
10 1 CD  B GLU 104 ? ? OE2 B GLU 104 ? ? 1.334 1.252 0.082 0.011 N 
11 1 CB  B THR 111 ? ? OG1 B THR 111 ? ? 1.567 1.428 0.139 0.020 N 
12 1 C   B LEU 140 ? ? O   B LEU 140 ? ? 1.417 1.229 0.188 0.019 N 
13 1 C   B GLY 151 ? C O   B GLY 151 ? C 1.345 1.232 0.113 0.016 N 
14 1 C   B GLY 151 ? D O   B GLY 151 ? D 1.348 1.232 0.116 0.016 N 
15 1 C   B ASN 152 ? A O   B ASN 152 ? A 1.433 1.229 0.204 0.019 N 
16 1 C   B ASN 152 ? B O   B ASN 152 ? B 1.432 1.229 0.203 0.019 N 
17 1 C   B ASN 152 ? C O   B ASN 152 ? C 1.348 1.229 0.119 0.019 N 
18 1 C   B ASN 152 ? D O   B ASN 152 ? D 1.349 1.229 0.120 0.019 N 
19 1 C   B ASN 152 ? C N   B GLY 153 ? ? 1.520 1.336 0.184 0.023 Y 
20 1 C   B ASN 152 ? D N   B GLY 153 ? ? 1.521 1.336 0.185 0.023 Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ALA 65  ? ? CA A ALA 65  ? ? C   A ALA 65  ? ? 96.94  110.10 -13.16 1.50 N 
2 1 O  B GLU 94  ? ? C  B GLU 94  ? ? N   B VAL 95  ? ? 133.75 122.70 11.05  1.60 Y 
3 1 CG B GLN 96  ? ? CD B GLN 96  ? ? OE1 B GLN 96  ? ? 134.21 121.60 12.61  2.00 N 
4 1 CA B ASN 152 ? C C  B ASN 152 ? C N   B GLY 153 ? ? 103.20 116.20 -13.00 2.00 Y 
5 1 CA B ASN 152 ? D C  B ASN 152 ? D N   B GLY 153 ? ? 103.09 116.20 -13.11 2.00 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 GLU A 66 ? ? -35.21  123.69  
2 1 LEU B 30 ? ? -122.01 -166.09 
3 1 CYS B 80 ? ? 79.10   -3.01   
4 1 LEU B 92 ? ? -129.99 -51.85  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ALA 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    164 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   ILE 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    165 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            144.30 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 THR A 60 ? B 13.34 
2 1 THR A 60 ? D 13.34 
3 1 ALA A 65 ? ? 10.47 
# 
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 348 ? I HOH . 
3 1 B HOH 369 ? I HOH . 
4 1 B HOH 374 ? 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 -13.5352 -1.7479 -19.3335 0.3795 0.3838 0.0515 0.1542 0.0768 0.0740 2.0643 2.0817 1.2804 -1.1457 
0.0392 0.3585 0.3839 0.3252 0.3006 -0.3542 -0.3489 -0.2599 0.0233 0.1922 -0.0349 
'X-RAY DIFFRACTION' 2 ? refined -18.3017 0.9526  -15.8552 0.4201 0.4024 0.0668 0.1382 0.0467 0.0163 0.7093 0.5614 0.6249 -0.3233 
0.4614 0.0215 0.2599 0.1742 0.0915 -0.1433 -0.2794 0.0224  0.1240 0.1041 0.0194  
# 
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 302 ? ? ? ? 
# 
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 
A1BG3 N1   N N N 1   
A1BG3 N3   N Y N 2   
A1BG3 C4   C Y N 3   
A1BG3 C5   C Y N 4   
A1BG3 C6   C Y N 5   
A1BG3 C7   C Y N 6   
A1BG3 C8   C Y N 7   
A1BG3 C10  C Y N 8   
A1BG3 C13  C Y N 9   
A1BG3 C15  C Y N 10  
A1BG3 C17  C Y N 11  
A1BG3 C1   C N N 12  
A1BG3 C2   C Y N 13  
A1BG3 C3   C Y N 14  
A1BG3 C9   C Y N 15  
A1BG3 C11  C N N 16  
A1BG3 O1   O N N 17  
A1BG3 C12  C Y N 18  
A1BG3 N2   N Y N 19  
A1BG3 C14  C N N 20  
A1BG3 C16  C Y N 21  
A1BG3 N4   N Y N 22  
A1BG3 F1   F N N 23  
A1BG3 H9   H N N 24  
A1BG3 H5   H N N 25  
A1BG3 H6   H N N 26  
A1BG3 H7   H N N 27  
A1BG3 H10  H N N 28  
A1BG3 H14  H N N 29  
A1BG3 H3   H N N 30  
A1BG3 H2   H N N 31  
A1BG3 H1   H N N 32  
A1BG3 H4   H N N 33  
A1BG3 H8   H N N 34  
A1BG3 H11  H N N 35  
A1BG3 H13  H N N 36  
A1BG3 H12  H N N 37  
A1BG3 H15  H N N 38  
ALA   N    N N N 39  
ALA   CA   C N S 40  
ALA   C    C N N 41  
ALA   O    O N N 42  
ALA   CB   C N N 43  
ALA   OXT  O N N 44  
ALA   H    H N N 45  
ALA   H2   H N N 46  
ALA   HA   H N N 47  
ALA   HB1  H N N 48  
ALA   HB2  H N N 49  
ALA   HB3  H N N 50  
ALA   HXT  H N N 51  
ARG   N    N N N 52  
ARG   CA   C N S 53  
ARG   C    C N N 54  
ARG   O    O N N 55  
ARG   CB   C N N 56  
ARG   CG   C N N 57  
ARG   CD   C N N 58  
ARG   NE   N N N 59  
ARG   CZ   C N N 60  
ARG   NH1  N N N 61  
ARG   NH2  N N N 62  
ARG   OXT  O N N 63  
ARG   H    H N N 64  
ARG   H2   H N N 65  
ARG   HA   H N N 66  
ARG   HB2  H N N 67  
ARG   HB3  H N N 68  
ARG   HG2  H N N 69  
ARG   HG3  H N N 70  
ARG   HD2  H N N 71  
ARG   HD3  H N N 72  
ARG   HE   H N N 73  
ARG   HH11 H N N 74  
ARG   HH12 H N N 75  
ARG   HH21 H N N 76  
ARG   HH22 H N N 77  
ARG   HXT  H N N 78  
ASN   N    N N N 79  
ASN   CA   C N S 80  
ASN   C    C N N 81  
ASN   O    O N N 82  
ASN   CB   C N N 83  
ASN   CG   C N N 84  
ASN   OD1  O N N 85  
ASN   ND2  N N N 86  
ASN   OXT  O N N 87  
ASN   H    H N N 88  
ASN   H2   H N N 89  
ASN   HA   H N N 90  
ASN   HB2  H N N 91  
ASN   HB3  H N N 92  
ASN   HD21 H N N 93  
ASN   HD22 H N N 94  
ASN   HXT  H N N 95  
ASP   N    N N N 96  
ASP   CA   C N S 97  
ASP   C    C N N 98  
ASP   O    O N N 99  
ASP   CB   C N N 100 
ASP   CG   C N N 101 
ASP   OD1  O N N 102 
ASP   OD2  O N N 103 
ASP   OXT  O N N 104 
ASP   H    H N N 105 
ASP   H2   H N N 106 
ASP   HA   H N N 107 
ASP   HB2  H N N 108 
ASP   HB3  H N N 109 
ASP   HD2  H N N 110 
ASP   HXT  H N N 111 
CYS   N    N N N 112 
CYS   CA   C N R 113 
CYS   C    C N N 114 
CYS   O    O N N 115 
CYS   CB   C N N 116 
CYS   SG   S N N 117 
CYS   OXT  O N N 118 
CYS   H    H N N 119 
CYS   H2   H N N 120 
CYS   HA   H N N 121 
CYS   HB2  H N N 122 
CYS   HB3  H N N 123 
CYS   HG   H N N 124 
CYS   HXT  H N N 125 
DMS   S    S N N 126 
DMS   O    O N N 127 
DMS   C1   C N N 128 
DMS   C2   C N N 129 
DMS   H11  H N N 130 
DMS   H12  H N N 131 
DMS   H13  H N N 132 
DMS   H21  H N N 133 
DMS   H22  H N N 134 
DMS   H23  H N N 135 
GLN   N    N N N 136 
GLN   CA   C N S 137 
GLN   C    C N N 138 
GLN   O    O N N 139 
GLN   CB   C N N 140 
GLN   CG   C N N 141 
GLN   CD   C N N 142 
GLN   OE1  O N N 143 
GLN   NE2  N N N 144 
GLN   OXT  O N N 145 
GLN   H    H N N 146 
GLN   H2   H N N 147 
GLN   HA   H N N 148 
GLN   HB2  H N N 149 
GLN   HB3  H N N 150 
GLN   HG2  H N N 151 
GLN   HG3  H N N 152 
GLN   HE21 H N N 153 
GLN   HE22 H N N 154 
GLN   HXT  H N N 155 
GLU   N    N N N 156 
GLU   CA   C N S 157 
GLU   C    C N N 158 
GLU   O    O N N 159 
GLU   CB   C N N 160 
GLU   CG   C N N 161 
GLU   CD   C N N 162 
GLU   OE1  O N N 163 
GLU   OE2  O N N 164 
GLU   OXT  O N N 165 
GLU   H    H N N 166 
GLU   H2   H N N 167 
GLU   HA   H N N 168 
GLU   HB2  H N N 169 
GLU   HB3  H N N 170 
GLU   HG2  H N N 171 
GLU   HG3  H N N 172 
GLU   HE2  H N N 173 
GLU   HXT  H N N 174 
GLY   N    N N N 175 
GLY   CA   C N N 176 
GLY   C    C N N 177 
GLY   O    O N N 178 
GLY   OXT  O N N 179 
GLY   H    H N N 180 
GLY   H2   H N N 181 
GLY   HA2  H N N 182 
GLY   HA3  H N N 183 
GLY   HXT  H N N 184 
HIS   N    N N N 185 
HIS   CA   C N S 186 
HIS   C    C N N 187 
HIS   O    O N N 188 
HIS   CB   C N N 189 
HIS   CG   C Y N 190 
HIS   ND1  N Y N 191 
HIS   CD2  C Y N 192 
HIS   CE1  C Y N 193 
HIS   NE2  N Y N 194 
HIS   OXT  O N N 195 
HIS   H    H N N 196 
HIS   H2   H N N 197 
HIS   HA   H N N 198 
HIS   HB2  H N N 199 
HIS   HB3  H N N 200 
HIS   HD1  H N N 201 
HIS   HD2  H N N 202 
HIS   HE1  H N N 203 
HIS   HE2  H N N 204 
HIS   HXT  H N N 205 
HOH   O    O N N 206 
HOH   H1   H N N 207 
HOH   H2   H N N 208 
ILE   N    N N N 209 
ILE   CA   C N S 210 
ILE   C    C N N 211 
ILE   O    O N N 212 
ILE   CB   C N S 213 
ILE   CG1  C N N 214 
ILE   CG2  C N N 215 
ILE   CD1  C N N 216 
ILE   OXT  O N N 217 
ILE   H    H N N 218 
ILE   H2   H N N 219 
ILE   HA   H N N 220 
ILE   HB   H N N 221 
ILE   HG12 H N N 222 
ILE   HG13 H N N 223 
ILE   HG21 H N N 224 
ILE   HG22 H N N 225 
ILE   HG23 H N N 226 
ILE   HD11 H N N 227 
ILE   HD12 H N N 228 
ILE   HD13 H N N 229 
ILE   HXT  H N N 230 
LEU   N    N N N 231 
LEU   CA   C N S 232 
LEU   C    C N N 233 
LEU   O    O N N 234 
LEU   CB   C N N 235 
LEU   CG   C N N 236 
LEU   CD1  C N N 237 
LEU   CD2  C N N 238 
LEU   OXT  O N N 239 
LEU   H    H N N 240 
LEU   H2   H N N 241 
LEU   HA   H N N 242 
LEU   HB2  H N N 243 
LEU   HB3  H N N 244 
LEU   HG   H N N 245 
LEU   HD11 H N N 246 
LEU   HD12 H N N 247 
LEU   HD13 H N N 248 
LEU   HD21 H N N 249 
LEU   HD22 H N N 250 
LEU   HD23 H N N 251 
LEU   HXT  H N N 252 
LYS   N    N N N 253 
LYS   CA   C N S 254 
LYS   C    C N N 255 
LYS   O    O N N 256 
LYS   CB   C N N 257 
LYS   CG   C N N 258 
LYS   CD   C N N 259 
LYS   CE   C N N 260 
LYS   NZ   N N N 261 
LYS   OXT  O N N 262 
LYS   H    H N N 263 
LYS   H2   H N N 264 
LYS   HA   H N N 265 
LYS   HB2  H N N 266 
LYS   HB3  H N N 267 
LYS   HG2  H N N 268 
LYS   HG3  H N N 269 
LYS   HD2  H N N 270 
LYS   HD3  H N N 271 
LYS   HE2  H N N 272 
LYS   HE3  H N N 273 
LYS   HZ1  H N N 274 
LYS   HZ2  H N N 275 
LYS   HZ3  H N N 276 
LYS   HXT  H N N 277 
MET   N    N N N 278 
MET   CA   C N S 279 
MET   C    C N N 280 
MET   O    O N N 281 
MET   CB   C N N 282 
MET   CG   C N N 283 
MET   SD   S N N 284 
MET   CE   C N N 285 
MET   OXT  O N N 286 
MET   H    H N N 287 
MET   H2   H N N 288 
MET   HA   H N N 289 
MET   HB2  H N N 290 
MET   HB3  H N N 291 
MET   HG2  H N N 292 
MET   HG3  H N N 293 
MET   HE1  H N N 294 
MET   HE2  H N N 295 
MET   HE3  H N N 296 
MET   HXT  H N N 297 
PHE   N    N N N 298 
PHE   CA   C N S 299 
PHE   C    C N N 300 
PHE   O    O N N 301 
PHE   CB   C N N 302 
PHE   CG   C Y N 303 
PHE   CD1  C Y N 304 
PHE   CD2  C Y N 305 
PHE   CE1  C Y N 306 
PHE   CE2  C Y N 307 
PHE   CZ   C Y N 308 
PHE   OXT  O N N 309 
PHE   H    H N N 310 
PHE   H2   H N N 311 
PHE   HA   H N N 312 
PHE   HB2  H N N 313 
PHE   HB3  H N N 314 
PHE   HD1  H N N 315 
PHE   HD2  H N N 316 
PHE   HE1  H N N 317 
PHE   HE2  H N N 318 
PHE   HZ   H N N 319 
PHE   HXT  H N N 320 
PRO   N    N N N 321 
PRO   CA   C N S 322 
PRO   C    C N N 323 
PRO   O    O N N 324 
PRO   CB   C N N 325 
PRO   CG   C N N 326 
PRO   CD   C N N 327 
PRO   OXT  O N N 328 
PRO   H    H N N 329 
PRO   HA   H N N 330 
PRO   HB2  H N N 331 
PRO   HB3  H N N 332 
PRO   HG2  H N N 333 
PRO   HG3  H N N 334 
PRO   HD2  H N N 335 
PRO   HD3  H N N 336 
PRO   HXT  H N N 337 
SER   N    N N N 338 
SER   CA   C N S 339 
SER   C    C N N 340 
SER   O    O N N 341 
SER   CB   C N N 342 
SER   OG   O N N 343 
SER   OXT  O N N 344 
SER   H    H N N 345 
SER   H2   H N N 346 
SER   HA   H N N 347 
SER   HB2  H N N 348 
SER   HB3  H N N 349 
SER   HG   H N N 350 
SER   HXT  H N N 351 
SO4   S    S N N 352 
SO4   O1   O N N 353 
SO4   O2   O N N 354 
SO4   O3   O N N 355 
SO4   O4   O N N 356 
THR   N    N N N 357 
THR   CA   C N S 358 
THR   C    C N N 359 
THR   O    O N N 360 
THR   CB   C N R 361 
THR   OG1  O N N 362 
THR   CG2  C N N 363 
THR   OXT  O N N 364 
THR   H    H N N 365 
THR   H2   H N N 366 
THR   HA   H N N 367 
THR   HB   H N N 368 
THR   HG1  H N N 369 
THR   HG21 H N N 370 
THR   HG22 H N N 371 
THR   HG23 H N N 372 
THR   HXT  H N N 373 
TRP   N    N N N 374 
TRP   CA   C N S 375 
TRP   C    C N N 376 
TRP   O    O N N 377 
TRP   CB   C N N 378 
TRP   CG   C Y N 379 
TRP   CD1  C Y N 380 
TRP   CD2  C Y N 381 
TRP   NE1  N Y N 382 
TRP   CE2  C Y N 383 
TRP   CE3  C Y N 384 
TRP   CZ2  C Y N 385 
TRP   CZ3  C Y N 386 
TRP   CH2  C Y N 387 
TRP   OXT  O N N 388 
TRP   H    H N N 389 
TRP   H2   H N N 390 
TRP   HA   H N N 391 
TRP   HB2  H N N 392 
TRP   HB3  H N N 393 
TRP   HD1  H N N 394 
TRP   HE1  H N N 395 
TRP   HE3  H N N 396 
TRP   HZ2  H N N 397 
TRP   HZ3  H N N 398 
TRP   HH2  H N N 399 
TRP   HXT  H N N 400 
TYR   N    N N N 401 
TYR   CA   C N S 402 
TYR   C    C N N 403 
TYR   O    O N N 404 
TYR   CB   C N N 405 
TYR   CG   C Y N 406 
TYR   CD1  C Y N 407 
TYR   CD2  C Y N 408 
TYR   CE1  C Y N 409 
TYR   CE2  C Y N 410 
TYR   CZ   C Y N 411 
TYR   OH   O N N 412 
TYR   OXT  O N N 413 
TYR   H    H N N 414 
TYR   H2   H N N 415 
TYR   HA   H N N 416 
TYR   HB2  H N N 417 
TYR   HB3  H N N 418 
TYR   HD1  H N N 419 
TYR   HD2  H N N 420 
TYR   HE1  H N N 421 
TYR   HE2  H N N 422 
TYR   HH   H N N 423 
TYR   HXT  H N N 424 
VAL   N    N N N 425 
VAL   CA   C N S 426 
VAL   C    C N N 427 
VAL   O    O N N 428 
VAL   CB   C N N 429 
VAL   CG1  C N N 430 
VAL   CG2  C N N 431 
VAL   OXT  O N N 432 
VAL   H    H N N 433 
VAL   H2   H N N 434 
VAL   HA   H N N 435 
VAL   HB   H N N 436 
VAL   HG11 H N N 437 
VAL   HG12 H N N 438 
VAL   HG13 H N N 439 
VAL   HG21 H N N 440 
VAL   HG22 H N N 441 
VAL   HG23 H N N 442 
VAL   HXT  H N N 443 
# 
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 
A1BG3 C1  C2   sing N N 1   
A1BG3 C2  C3   doub Y N 2   
A1BG3 C3  C4   sing Y N 3   
A1BG3 C4  C5   sing N N 4   
A1BG3 C5  C6   doub Y N 5   
A1BG3 C6  C7   sing Y N 6   
A1BG3 C7  C8   doub Y N 7   
A1BG3 C8  C9   sing Y N 8   
A1BG3 C9  C10  doub Y N 9   
A1BG3 C10 C11  sing N N 10  
A1BG3 C11 O1   doub N N 11  
A1BG3 C11 N1   sing N N 12  
A1BG3 N1  C12  sing N N 13  
A1BG3 C12 C13  sing Y N 14  
A1BG3 C13 N2   doub Y N 15  
A1BG3 N2  N3   sing Y N 16  
A1BG3 N3  C14  sing N N 17  
A1BG3 N3  C15  sing Y N 18  
A1BG3 C4  C16  doub Y N 19  
A1BG3 C16 N4   sing Y N 20  
A1BG3 N4  C17  doub Y N 21  
A1BG3 C17 F1   sing N N 22  
A1BG3 C2  C17  sing Y N 23  
A1BG3 C5  C10  sing Y N 24  
A1BG3 C12 C15  doub Y N 25  
A1BG3 N1  H9   sing N N 26  
A1BG3 C6  H5   sing N N 27  
A1BG3 C7  H6   sing N N 28  
A1BG3 C8  H7   sing N N 29  
A1BG3 C13 H10  sing N N 30  
A1BG3 C15 H14  sing N N 31  
A1BG3 C1  H3   sing N N 32  
A1BG3 C1  H2   sing N N 33  
A1BG3 C1  H1   sing N N 34  
A1BG3 C3  H4   sing N N 35  
A1BG3 C9  H8   sing N N 36  
A1BG3 C14 H11  sing N N 37  
A1BG3 C14 H13  sing N N 38  
A1BG3 C14 H12  sing N N 39  
A1BG3 C16 H15  sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
DMS   S   O    doub N N 123 
DMS   S   C1   sing N N 124 
DMS   S   C2   sing N N 125 
DMS   C1  H11  sing N N 126 
DMS   C1  H12  sing N N 127 
DMS   C1  H13  sing N N 128 
DMS   C2  H21  sing N N 129 
DMS   C2  H22  sing N N 130 
DMS   C2  H23  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
SO4   S   O1   doub N N 339 
SO4   S   O2   doub N N 340 
SO4   S   O3   sing N N 341 
SO4   S   O4   sing N N 342 
THR   N   CA   sing N N 343 
THR   N   H    sing N N 344 
THR   N   H2   sing N N 345 
THR   CA  C    sing N N 346 
THR   CA  CB   sing N N 347 
THR   CA  HA   sing N N 348 
THR   C   O    doub N N 349 
THR   C   OXT  sing N N 350 
THR   CB  OG1  sing N N 351 
THR   CB  CG2  sing N N 352 
THR   CB  HB   sing N N 353 
THR   OG1 HG1  sing N N 354 
THR   CG2 HG21 sing N N 355 
THR   CG2 HG22 sing N N 356 
THR   CG2 HG23 sing N N 357 
THR   OXT HXT  sing N N 358 
TRP   N   CA   sing N N 359 
TRP   N   H    sing N N 360 
TRP   N   H2   sing N N 361 
TRP   CA  C    sing N N 362 
TRP   CA  CB   sing N N 363 
TRP   CA  HA   sing N N 364 
TRP   C   O    doub N N 365 
TRP   C   OXT  sing N N 366 
TRP   CB  CG   sing N N 367 
TRP   CB  HB2  sing N N 368 
TRP   CB  HB3  sing N N 369 
TRP   CG  CD1  doub Y N 370 
TRP   CG  CD2  sing Y N 371 
TRP   CD1 NE1  sing Y N 372 
TRP   CD1 HD1  sing N N 373 
TRP   CD2 CE2  doub Y N 374 
TRP   CD2 CE3  sing Y N 375 
TRP   NE1 CE2  sing Y N 376 
TRP   NE1 HE1  sing N N 377 
TRP   CE2 CZ2  sing Y N 378 
TRP   CE3 CZ3  doub Y N 379 
TRP   CE3 HE3  sing N N 380 
TRP   CZ2 CH2  doub Y N 381 
TRP   CZ2 HZ2  sing N N 382 
TRP   CZ3 CH2  sing Y N 383 
TRP   CZ3 HZ3  sing N N 384 
TRP   CH2 HH2  sing N N 385 
TRP   OXT HXT  sing N N 386 
TYR   N   CA   sing N N 387 
TYR   N   H    sing N N 388 
TYR   N   H2   sing N N 389 
TYR   CA  C    sing N N 390 
TYR   CA  CB   sing N N 391 
TYR   CA  HA   sing N N 392 
TYR   C   O    doub N N 393 
TYR   C   OXT  sing N N 394 
TYR   CB  CG   sing N N 395 
TYR   CB  HB2  sing N N 396 
TYR   CB  HB3  sing N N 397 
TYR   CG  CD1  doub Y N 398 
TYR   CG  CD2  sing Y N 399 
TYR   CD1 CE1  sing Y N 400 
TYR   CD1 HD1  sing N N 401 
TYR   CD2 CE2  doub Y N 402 
TYR   CD2 HD2  sing N N 403 
TYR   CE1 CZ   doub Y N 404 
TYR   CE1 HE1  sing N N 405 
TYR   CE2 CZ   sing Y N 406 
TYR   CE2 HE2  sing N N 407 
TYR   CZ  OH   sing N N 408 
TYR   OH  HH   sing N N 409 
TYR   OXT HXT  sing N N 410 
VAL   N   CA   sing N N 411 
VAL   N   H    sing N N 412 
VAL   N   H2   sing N N 413 
VAL   CA  C    sing N N 414 
VAL   CA  CB   sing N N 415 
VAL   CA  HA   sing N N 416 
VAL   C   O    doub N N 417 
VAL   C   OXT  sing N N 418 
VAL   CB  CG1  sing N N 419 
VAL   CB  CG2  sing N N 420 
VAL   CB  HB   sing N N 421 
VAL   CG1 HG11 sing N N 422 
VAL   CG1 HG12 sing N N 423 
VAL   CG1 HG13 sing N N 424 
VAL   CG2 HG21 sing N N 425 
VAL   CG2 HG22 sing N N 426 
VAL   CG2 HG23 sing N N 427 
VAL   OXT HXT  sing N N 428 
# 
_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                    7HOU 
_atom_sites.fract_transf_matrix[1][1]   0.023528 
_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]   0.023528 
_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]   0.004621 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
F 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 7   ? -20.743 19.159  -7.772  1.00 59.79  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.042 18.464  -7.603  1.00 57.38  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.406 17.758  -8.921  1.00 54.45  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.534 18.418  -9.988  1.00 55.89  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.129 19.421  -7.123  1.00 59.88  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.490 18.769  -6.946  1.00 60.35  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.716 18.140  -5.885  1.00 62.84  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.323 18.898  -7.869  1.00 61.45  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.580 16.451  -8.846  1.00 48.71  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.488 15.574  -10.030 1.00 45.60  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.894 15.315  -10.546 1.00 42.89  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.839 15.214  -9.735  1.00 41.87  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.800 14.254  -9.688  1.00 44.90  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.365 14.427  -9.358  1.00 46.21  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.538 12.832  -9.250  1.00 45.81  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.860 13.420  -9.057  1.00 46.61  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -24.036 15.274  -11.866 1.00 39.67  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.331 15.038  -12.531 1.00 38.41  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.111 14.059  -13.680 1.00 36.96  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -23.972 13.892  -14.129 1.00 35.30  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.969 16.355  -12.970 1.00 39.55  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.195 17.130  -14.003 1.00 41.12  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.170 17.976  -13.618 1.00 42.27  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.485 17.023  -15.365 1.00 42.02  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.448 18.712  -14.545 1.00 44.42  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.763 17.751  -16.311 1.00 43.36  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.738 18.596  -15.898 1.00 44.56  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -22.968 19.295  -16.794 1.00 47.19  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.181 13.367  -14.057 1.00 36.79  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.147 12.350  -15.150 1.00 36.51  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.950 12.840  -16.379 1.00 37.55  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.899 13.629  -16.232 1.00 36.75  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.613 10.974  -14.652 1.00 36.00  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.071 10.913  -14.215 1.00 36.55  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.722 10.476  -13.526 1.00 35.35  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.503 9.481   -14.013 1.00 36.57  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.539 12.375  -17.574 1.00 38.48  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.147 12.746  -18.894 1.00 40.66  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.196 11.480  -19.759 1.00 39.06  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.127 10.785  -19.873 1.00 37.73  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.279 13.736  -19.677 1.00 43.90  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.430 15.195  -19.302 1.00 46.84  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.460 16.096  -20.068 1.00 50.07  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.618 15.578  -20.860 1.00 53.09  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.509 17.314  -19.864 1.00 53.60  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.377 11.116  -20.271 1.00 39.50  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.490 9.846   -21.030 1.00 39.80  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.584 9.975   -22.256 1.00 39.45  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.465 11.122  -22.748 1.00 41.28  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.925 9.563   -21.457 1.00 41.84  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.155 8.129   -21.914 1.00 42.93  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.594 7.680   -21.668 1.00 45.01  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.823 6.285   -22.006 1.00 45.68  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.810 5.824   -23.274 1.00 46.62  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.580 6.657   -24.272 1.00 50.57  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.989 4.540   -23.538 1.00 44.22  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.898 8.897   -22.647 1.00 38.45  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.989 8.868   -23.836 1.00 39.73  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.360 7.785   -24.846 1.00 40.43  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.721 7.799   -25.915 1.00 41.41  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.534 8.700   -23.471 1.00 39.42  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.283 6.874   -24.572 1.00 39.78  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.606 5.825   -25.550 1.00 40.84  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.353 4.687   -24.928 1.00 41.08  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.402 4.616   -23.608 1.00 38.41  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.848 3.798   -25.794 1.00 42.30  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.355 2.447   -25.452 1.00 43.35  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.142 1.524   -25.310 1.00 44.10  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -27.065 1.789   -25.920 1.00 45.27  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.310 1.862   -26.502 1.00 45.50  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.648 2.569   -26.646 1.00 47.24  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.857 3.596   -25.960 1.00 45.67  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.481 2.109   -27.503 1.00 48.98  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.291 0.464   -24.525 1.00 44.12  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.260 -0.593  -24.448 1.00 43.55  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.683 -1.712  -25.404 1.00 44.96  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.665 -2.453  -25.107 1.00 43.45  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.080 -1.011  -22.996 1.00 43.58  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.531 0.182   -22.204 1.00 42.56  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.192 -2.225  -22.931 1.00 43.75  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.598 0.032   -20.695 1.00 42.28  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -26.966 -1.792  -26.538 0.25 45.73  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -26.960 -1.846  -26.519 0.25 45.87  ? 60  THR   A N   1 
ATOM   84   N N   C THR   A 1 17  ? -26.966 -1.792  -26.538 0.25 45.73  ? 60  THR   A N   1 
ATOM   85   N N   D THR   A 1 17  ? -26.960 -1.846  -26.519 0.25 45.87  ? 60  THR   A N   1 
ATOM   86   C CA  A THR   A 1 17  ? -27.246 -2.656  -27.720 0.25 47.38  ? 60  THR   A CA  1 
ATOM   87   C CA  B THR   A 1 17  ? -27.306 -2.755  -27.642 0.25 47.57  ? 60  THR   A CA  1 
ATOM   88   C CA  C THR   A 1 17  ? -27.246 -2.656  -27.720 0.25 47.38  ? 60  THR   A CA  1 
ATOM   89   C CA  D THR   A 1 17  ? -27.306 -2.755  -27.642 0.25 47.57  ? 60  THR   A CA  1 
ATOM   90   C C   A THR   A 1 17  ? -25.879 -3.173  -28.285 0.25 47.94  ? 60  THR   A C   1 
ATOM   91   C C   B THR   A 1 17  ? -25.986 -3.160  -28.373 0.25 48.32  ? 60  THR   A C   1 
ATOM   92   C C   C THR   A 1 17  ? -25.879 -3.173  -28.285 0.25 47.94  ? 60  THR   A C   1 
ATOM   93   C C   D THR   A 1 17  ? -25.986 -3.160  -28.373 0.25 48.32  ? 60  THR   A C   1 
ATOM   94   O O   A THR   A 1 17  ? -24.767 -2.386  -28.063 0.25 48.43  ? 60  THR   A O   1 
ATOM   95   O O   B THR   A 1 17  ? -24.940 -2.264  -28.211 0.25 49.03  ? 60  THR   A O   1 
ATOM   96   O O   C THR   A 1 17  ? -24.767 -2.386  -28.063 0.25 48.43  ? 60  THR   A O   1 
ATOM   97   O O   D THR   A 1 17  ? -24.940 -2.264  -28.211 0.25 49.03  ? 60  THR   A O   1 
ATOM   98   C CB  A THR   A 1 17  ? -28.084 -1.914  -28.784 0.25 48.51  ? 60  THR   A CB  1 
ATOM   99   C CB  B THR   A 1 17  ? -28.374 -2.109  -28.548 0.25 48.80  ? 60  THR   A CB  1 
ATOM   100  C CB  C THR   A 1 17  ? -28.084 -1.914  -28.784 0.25 48.51  ? 60  THR   A CB  1 
ATOM   101  C CB  D THR   A 1 17  ? -28.374 -2.109  -28.548 0.25 48.80  ? 60  THR   A CB  1 
ATOM   102  O OG1 A THR   A 1 17  ? -27.199 -1.125  -29.581 0.25 49.13  ? 60  THR   A OG1 1 
ATOM   103  O OG1 B THR   A 1 17  ? -29.624 -2.122  -27.844 0.25 48.18  ? 60  THR   A OG1 1 
ATOM   104  O OG1 C THR   A 1 17  ? -27.199 -1.125  -29.581 0.25 49.13  ? 60  THR   A OG1 1 
ATOM   105  O OG1 D THR   A 1 17  ? -29.624 -2.122  -27.844 0.25 48.18  ? 60  THR   A OG1 1 
ATOM   106  C CG2 A THR   A 1 17  ? -29.160 -1.030  -28.181 0.25 48.16  ? 60  THR   A CG2 1 
ATOM   107  C CG2 B THR   A 1 17  ? -28.516 -2.799  -29.885 0.25 50.57  ? 60  THR   A CG2 1 
ATOM   108  C CG2 C THR   A 1 17  ? -29.160 -1.030  -28.181 0.25 48.16  ? 60  THR   A CG2 1 
ATOM   109  C CG2 D THR   A 1 17  ? -28.516 -2.799  -29.885 0.25 50.57  ? 60  THR   A CG2 1 
ATOM   110  N N   . TRP   A 1 18  ? -25.935 -4.549  -28.595 1.00 48.45  ? 61  TRP   A N   1 
ATOM   111  C CA  . TRP   A 1 18  ? -24.885 -5.123  -29.467 1.00 50.78  ? 61  TRP   A CA  1 
ATOM   112  C C   . TRP   A 1 18  ? -25.098 -4.489  -30.847 1.00 54.08  ? 61  TRP   A C   1 
ATOM   113  O O   . TRP   A 1 18  ? -26.255 -4.355  -31.244 1.00 55.66  ? 61  TRP   A O   1 
ATOM   114  C CB  . TRP   A 1 18  ? -25.009 -6.644  -29.477 1.00 49.17  ? 61  TRP   A CB  1 
ATOM   115  C CG  . TRP   A 1 18  ? -23.894 -7.246  -30.240 1.00 49.12  ? 61  TRP   A CG  1 
ATOM   116  C CD1 . TRP   A 1 18  ? -23.877 -7.444  -31.591 1.00 50.92  ? 61  TRP   A CD1 1 
ATOM   117  C CD2 . TRP   A 1 18  ? -22.629 -7.702  -29.750 1.00 48.20  ? 61  TRP   A CD2 1 
ATOM   118  N NE1 . TRP   A 1 18  ? -22.679 -7.979  -31.959 1.00 51.48  ? 61  TRP   A NE1 1 
ATOM   119  C CE2 . TRP   A 1 18  ? -21.898 -8.179  -30.857 1.00 49.88  ? 61  TRP   A CE2 1 
ATOM   120  C CE3 . TRP   A 1 18  ? -22.034 -7.774  -28.493 1.00 46.10  ? 61  TRP   A CE3 1 
ATOM   121  C CZ2 . TRP   A 1 18  ? -20.607 -8.692  -30.745 1.00 49.70  ? 61  TRP   A CZ2 1 
ATOM   122  C CZ3 . TRP   A 1 18  ? -20.770 -8.291  -28.389 1.00 46.07  ? 61  TRP   A CZ3 1 
ATOM   123  C CH2 . TRP   A 1 18  ? -20.067 -8.766  -29.477 1.00 48.71  ? 61  TRP   A CH2 1 
ATOM   124  N N   A GLU   A 1 19  ? -24.018 -4.115  -31.536 0.25 55.68  ? 62  GLU   A N   1 
ATOM   125  N N   B GLU   A 1 19  ? -24.018 -4.115  -31.536 0.25 55.68  ? 62  GLU   A N   1 
ATOM   126  N N   C GLU   A 1 19  ? -24.011 -4.037  -31.496 0.25 55.14  ? 62  GLU   A N   1 
ATOM   127  N N   D GLU   A 1 19  ? -24.011 -4.037  -31.496 0.25 55.14  ? 62  GLU   A N   1 
ATOM   128  C CA  A GLU   A 1 19  ? -24.079 -3.486  -32.883 0.25 58.97  ? 62  GLU   A CA  1 
ATOM   129  C CA  B GLU   A 1 19  ? -24.079 -3.486  -32.883 0.25 58.97  ? 62  GLU   A CA  1 
ATOM   130  C CA  C GLU   A 1 19  ? -24.004 -3.483  -32.885 0.25 58.23  ? 62  GLU   A CA  1 
ATOM   131  C CA  D GLU   A 1 19  ? -24.004 -3.483  -32.885 0.25 58.23  ? 62  GLU   A CA  1 
ATOM   132  C C   A GLU   A 1 19  ? -23.281 -4.358  -33.860 0.25 61.13  ? 62  GLU   A C   1 
ATOM   133  C C   B GLU   A 1 19  ? -23.281 -4.358  -33.860 0.25 61.13  ? 62  GLU   A C   1 
ATOM   134  C C   C GLU   A 1 19  ? -23.274 -4.472  -33.799 0.25 60.43  ? 62  GLU   A C   1 
ATOM   135  C C   D GLU   A 1 19  ? -23.274 -4.472  -33.799 0.25 60.43  ? 62  GLU   A C   1 
ATOM   136  O O   A GLU   A 1 19  ? -22.017 -4.406  -33.716 0.25 60.30  ? 62  GLU   A O   1 
ATOM   137  O O   B GLU   A 1 19  ? -22.017 -4.406  -33.716 0.25 60.30  ? 62  GLU   A O   1 
ATOM   138  O O   C GLU   A 1 19  ? -22.038 -4.724  -33.552 0.25 59.48  ? 62  GLU   A O   1 
ATOM   139  O O   D GLU   A 1 19  ? -22.038 -4.724  -33.552 0.25 59.48  ? 62  GLU   A O   1 
ATOM   140  C CB  A GLU   A 1 19  ? -23.551 -2.051  -32.811 0.25 59.33  ? 62  GLU   A CB  1 
ATOM   141  C CB  B GLU   A 1 19  ? -23.551 -2.051  -32.811 0.25 59.33  ? 62  GLU   A CB  1 
ATOM   142  C CB  C GLU   A 1 19  ? -23.298 -2.123  -32.986 0.25 58.33  ? 62  GLU   A CB  1 
ATOM   143  C CB  D GLU   A 1 19  ? -23.298 -2.123  -32.986 0.25 58.33  ? 62  GLU   A CB  1 
ATOM   144  C CG  A GLU   A 1 19  ? -24.379 -1.144  -31.913 0.25 58.53  ? 62  GLU   A CG  1 
ATOM   145  C CG  B GLU   A 1 19  ? -24.379 -1.144  -31.913 0.25 58.53  ? 62  GLU   A CG  1 
ATOM   146  C CG  C GLU   A 1 19  ? -23.073 -1.667  -34.432 0.25 60.76  ? 62  GLU   A CG  1 
ATOM   147  C CG  D GLU   A 1 19  ? -23.073 -1.667  -34.432 0.25 60.76  ? 62  GLU   A CG  1 
ATOM   148  C CD  A GLU   A 1 19  ? -25.743 -0.750  -32.464 0.25 60.40  ? 62  GLU   A CD  1 
ATOM   149  C CD  B GLU   A 1 19  ? -25.743 -0.750  -32.464 0.25 60.40  ? 62  GLU   A CD  1 
ATOM   150  C CD  C GLU   A 1 19  ? -22.315 -0.363  -34.650 0.25 61.23  ? 62  GLU   A CD  1 
ATOM   151  C CD  D GLU   A 1 19  ? -22.315 -0.363  -34.650 0.25 61.23  ? 62  GLU   A CD  1 
ATOM   152  O OE1 A GLU   A 1 19  ? -25.809 -0.373  -33.664 0.25 63.32  ? 62  GLU   A OE1 1 
ATOM   153  O OE1 B GLU   A 1 19  ? -25.809 -0.373  -33.664 0.25 63.32  ? 62  GLU   A OE1 1 
ATOM   154  O OE1 C GLU   A 1 19  ? -21.975 0.306   -33.641 0.25 61.80  ? 62  GLU   A OE1 1 
ATOM   155  O OE1 D GLU   A 1 19  ? -21.975 0.306   -33.641 0.25 61.80  ? 62  GLU   A OE1 1 
ATOM   156  O OE2 A GLU   A 1 19  ? -26.737 -0.819  -31.701 0.25 59.94  ? 62  GLU   A OE2 1 
ATOM   157  O OE2 B GLU   A 1 19  ? -26.737 -0.819  -31.701 0.25 59.94  ? 62  GLU   A OE2 1 
ATOM   158  O OE2 C GLU   A 1 19  ? -22.066 -0.018  -35.842 0.25 63.86  ? 62  GLU   A OE2 1 
ATOM   159  O OE2 D GLU   A 1 19  ? -22.066 -0.018  -35.842 0.25 63.86  ? 62  GLU   A OE2 1 
ATOM   160  N N   . LYS   A 1 20  ? -23.994 -5.007  -34.808 1.00 64.28  ? 63  LYS   A N   1 
ATOM   161  C CA  . LYS   A 1 20  ? -23.374 -5.884  -35.846 1.00 68.05  ? 63  LYS   A CA  1 
ATOM   162  C C   . LYS   A 1 20  ? -22.429 -5.018  -36.679 1.00 68.96  ? 63  LYS   A C   1 
ATOM   163  O O   . LYS   A 1 20  ? -22.784 -3.851  -36.953 1.00 67.96  ? 63  LYS   A O   1 
ATOM   164  C CB  . LYS   A 1 20  ? -24.437 -6.552  -36.723 1.00 73.78  ? 63  LYS   A CB  1 
ATOM   165  C CG  . LYS   A 1 20  ? -25.091 -7.791  -36.118 1.00 76.86  ? 63  LYS   A CG  1 
ATOM   166  C CD  . LYS   A 1 20  ? -26.416 -8.140  -36.781 1.00 81.25  ? 63  LYS   A CD  1 
ATOM   167  C CE  . LYS   A 1 20  ? -27.084 -9.371  -36.201 1.00 82.98  ? 63  LYS   A CE  1 
ATOM   168  N NZ  . LYS   A 1 20  ? -28.546 -9.343  -36.449 1.00 85.98  ? 63  LYS   A NZ  1 
ATOM   169  N N   . ASP   A 1 21  ? -21.234 -5.524  -36.979 1.00 70.26  ? 64  ASP   A N   1 
ATOM   170  C CA  . ASP   A 1 21  ? -20.249 -4.794  -37.833 1.00 75.19  ? 64  ASP   A CA  1 
ATOM   171  C C   . ASP   A 1 21  ? -19.840 -3.480  -37.083 1.00 70.85  ? 64  ASP   A C   1 
ATOM   172  O O   . ASP   A 1 21  ? -19.840 -2.427  -37.679 1.00 73.47  ? 64  ASP   A O   1 
ATOM   173  C CB  . ASP   A 1 21  ? -20.796 -4.570  -39.265 1.00 81.63  ? 64  ASP   A CB  1 
ATOM   174  C CG  . ASP   A 1 21  ? -21.122 -5.822  -40.076 1.00 87.02  ? 64  ASP   A CG  1 
ATOM   175  O OD1 . ASP   A 1 21  ? -20.202 -6.338  -40.785 1.00 90.56  ? 64  ASP   A OD1 1 
ATOM   176  O OD2 . ASP   A 1 21  ? -22.310 -6.259  -40.026 1.00 89.17  ? 64  ASP   A OD2 1 
ATOM   177  N N   . ALA   A 1 22  ? -19.491 -3.507  -35.767 1.00 66.93  ? 65  ALA   A N   1 
ATOM   178  C CA  . ALA   A 1 22  ? -18.688 -2.380  -35.115 1.00 62.60  ? 65  ALA   A CA  1 
ATOM   179  C C   . ALA   A 1 22  ? -17.117 -2.553  -35.148 1.00 62.24  ? 65  ALA   A C   1 
ATOM   180  O O   . ALA   A 1 22  ? -16.725 -3.579  -35.450 1.00 63.39  ? 65  ALA   A O   1 
ATOM   181  C CB  . ALA   A 1 22  ? -18.842 -2.385  -33.598 1.00 61.40  ? 65  ALA   A CB  1 
ATOM   182  N N   . GLU   A 1 23  ? -16.394 -1.376  -35.231 1.00 62.89  ? 66  GLU   A N   1 
ATOM   183  C CA  . GLU   A 1 23  ? -14.895 -1.339  -35.287 1.00 63.60  ? 66  GLU   A CA  1 
ATOM   184  C C   . GLU   A 1 23  ? -14.404 -2.468  -34.415 1.00 62.63  ? 66  GLU   A C   1 
ATOM   185  O O   . GLU   A 1 23  ? -14.875 -2.566  -33.198 1.00 55.56  ? 66  GLU   A O   1 
ATOM   186  C CB  . GLU   A 1 23  ? -14.376 0.043   -34.863 1.00 66.97  ? 66  GLU   A CB  1 
ATOM   187  C CG  . GLU   A 1 23  ? -12.851 0.171   -34.979 1.00 71.47  ? 66  GLU   A CG  1 
ATOM   188  C CD  . GLU   A 1 23  ? -12.377 1.621   -34.905 1.00 76.41  ? 66  GLU   A CD  1 
ATOM   189  O OE1 . GLU   A 1 23  ? -12.257 2.310   -35.996 1.00 81.75  ? 66  GLU   A OE1 1 
ATOM   190  O OE2 . GLU   A 1 23  ? -12.133 2.070   -33.745 1.00 75.89  ? 66  GLU   A OE2 1 
ATOM   191  N N   . VAL   A 1 24  ? -13.567 -3.391  -35.024 1.00 62.52  ? 67  VAL   A N   1 
ATOM   192  C CA  . VAL   A 1 24  ? -13.048 -4.534  -34.200 1.00 61.36  ? 67  VAL   A CA  1 
ATOM   193  C C   . VAL   A 1 24  ? -11.568 -4.256  -33.946 1.00 61.47  ? 67  VAL   A C   1 
ATOM   194  O O   . VAL   A 1 24  ? -10.840 -4.064  -34.928 1.00 63.65  ? 67  VAL   A O   1 
ATOM   195  C CB  . VAL   A 1 24  ? -13.272 -5.905  -34.866 1.00 63.41  ? 67  VAL   A CB  1 
ATOM   196  C CG1 . VAL   A 1 24  ? -12.776 -7.020  -33.979 1.00 61.44  ? 67  VAL   A CG1 1 
ATOM   197  C CG2 . VAL   A 1 24  ? -14.734 -6.122  -35.244 1.00 64.56  ? 67  VAL   A CG2 1 
ATOM   198  N N   . THR   A 1 25  ? -11.136 -4.203  -32.675 1.00 57.62  ? 68  THR   A N   1 
ATOM   199  C CA  . THR   A 1 25  ? -9.757  -3.752  -32.350 1.00 57.58  ? 68  THR   A CA  1 
ATOM   200  C C   . THR   A 1 25  ? -9.383  -4.289  -30.962 1.00 55.32  ? 68  THR   A C   1 
ATOM   201  O O   . THR   A 1 25  ? -10.229 -4.963  -30.357 1.00 53.59  ? 68  THR   A O   1 
ATOM   202  C CB  . THR   A 1 25  ? -9.685  -2.228  -32.552 1.00 59.02  ? 68  THR   A CB  1 
ATOM   203  O OG1 . THR   A 1 25  ? -8.283  -1.813  -32.672 1.00 61.53  ? 68  THR   A OG1 1 
ATOM   204  C CG2 . THR   A 1 25  ? -10.410 -1.447  -31.467 1.00 58.33  ? 68  THR   A CG2 1 
ATOM   205  N N   . GLY   A 1 26  ? -8.160  -4.021  -30.510 1.00 55.51  ? 69  GLY   A N   1 
ATOM   206  C CA  . GLY   A 1 26  ? -7.654  -4.462  -29.198 1.00 55.25  ? 69  GLY   A CA  1 
ATOM   207  C C   . GLY   A 1 26  ? -7.072  -5.857  -29.255 1.00 56.46  ? 69  GLY   A C   1 
ATOM   208  O O   . GLY   A 1 26  ? -7.590  -6.687  -30.010 1.00 58.70  ? 69  GLY   A O   1 
ATOM   209  N N   . ASN   A 1 27  ? -6.018  -6.096  -28.475 1.00 55.29  ? 70  ASN   A N   1 
ATOM   210  C CA  . ASN   A 1 27  ? -5.401  -7.433  -28.313 1.00 55.51  ? 70  ASN   A CA  1 
ATOM   211  C C   . ASN   A 1 27  ? -5.982  -8.078  -27.031 1.00 52.86  ? 70  ASN   A C   1 
ATOM   212  O O   . ASN   A 1 27  ? -6.940  -7.473  -26.435 1.00 48.77  ? 70  ASN   A O   1 
ATOM   213  C CB  . ASN   A 1 27  ? -3.887  -7.256  -28.447 1.00 58.39  ? 70  ASN   A CB  1 
ATOM   214  C CG  . ASN   A 1 27  ? -3.281  -6.620  -27.214 1.00 59.68  ? 70  ASN   A CG  1 
ATOM   215  O OD1 . ASN   A 1 27  ? -3.686  -5.532  -26.800 1.00 61.19  ? 70  ASN   A OD1 1 
ATOM   216  N ND2 . ASN   A 1 27  ? -2.323  -7.304  -26.611 1.00 61.23  ? 70  ASN   A ND2 1 
ATOM   217  N N   . SER   A 1 28  ? -5.476  -9.260  -26.641 1.00 52.44  ? 71  SER   A N   1 
ATOM   218  C CA  . SER   A 1 28  ? -6.043  -10.179 -25.620 1.00 52.16  ? 71  SER   A CA  1 
ATOM   219  C C   . SER   A 1 28  ? -4.928  -10.625 -24.683 1.00 52.62  ? 71  SER   A C   1 
ATOM   220  O O   . SER   A 1 28  ? -4.641  -11.810 -24.596 1.00 54.19  ? 71  SER   A O   1 
ATOM   221  C CB  . SER   A 1 28  ? -6.766  -11.367 -26.228 1.00 52.30  ? 71  SER   A CB  1 
ATOM   222  O OG  . SER   A 1 28  ? -7.545  -10.942 -27.363 1.00 56.89  ? 71  SER   A OG  1 
ATOM   223  N N   . PRO   A 1 29  ? -4.264  -9.696  -23.962 1.00 52.36  ? 72  PRO   A N   1 
ATOM   224  C CA  . PRO   A 1 29  ? -3.095  -10.042 -23.155 1.00 53.05  ? 72  PRO   A CA  1 
ATOM   225  C C   . PRO   A 1 29  ? -3.468  -10.822 -21.884 1.00 52.05  ? 72  PRO   A C   1 
ATOM   226  O O   . PRO   A 1 29  ? -4.469  -10.467 -21.230 1.00 48.69  ? 72  PRO   A O   1 
ATOM   227  C CB  . PRO   A 1 29  ? -2.473  -8.665  -22.836 1.00 53.26  ? 72  PRO   A CB  1 
ATOM   228  C CG  . PRO   A 1 29  ? -3.675  -7.725  -22.783 1.00 52.25  ? 72  PRO   A CG  1 
ATOM   229  C CD  . PRO   A 1 29  ? -4.631  -8.271  -23.838 1.00 52.67  ? 72  PRO   A CD  1 
ATOM   230  N N   . ARG   A 1 30  ? -2.679  -11.851 -21.571 1.00 53.65  ? 73  ARG   A N   1 
ATOM   231  C CA  . ARG   A 1 30  ? -2.748  -12.606 -20.286 1.00 56.66  ? 73  ARG   A CA  1 
ATOM   232  C C   . ARG   A 1 30  ? -1.743  -11.986 -19.302 1.00 53.85  ? 73  ARG   A C   1 
ATOM   233  O O   . ARG   A 1 30  ? -0.562  -12.101 -19.554 1.00 52.25  ? 73  ARG   A O   1 
ATOM   234  C CB  . ARG   A 1 30  ? -2.493  -14.103 -20.511 1.00 62.42  ? 73  ARG   A CB  1 
ATOM   235  C CG  . ARG   A 1 30  ? -3.631  -14.822 -21.236 1.00 68.12  ? 73  ARG   A CG  1 
ATOM   236  C CD  . ARG   A 1 30  ? -3.248  -16.156 -21.876 1.00 75.96  ? 73  ARG   A CD  1 
ATOM   237  N NE  . ARG   A 1 30  ? -4.322  -16.769 -22.678 1.00 80.50  ? 73  ARG   A NE  1 
ATOM   238  C CZ  . ARG   A 1 30  ? -5.083  -17.811 -22.312 1.00 83.40  ? 73  ARG   A CZ  1 
ATOM   239  N NH1 . ARG   A 1 30  ? -4.910  -18.393 -21.131 1.00 86.12  ? 73  ARG   A NH1 1 
ATOM   240  N NH2 . ARG   A 1 30  ? -6.021  -18.266 -23.136 1.00 79.64  ? 73  ARG   A NH2 1 
ATOM   241  N N   . LEU   A 1 31  ? -2.207  -11.379 -18.200 1.00 51.77  ? 74  LEU   A N   1 
ATOM   242  C CA  . LEU   A 1 31  ? -1.353  -10.598 -17.268 1.00 51.01  ? 74  LEU   A CA  1 
ATOM   243  C C   . LEU   A 1 31  ? -1.510  -11.128 -15.827 1.00 48.84  ? 74  LEU   A C   1 
ATOM   244  O O   . LEU   A 1 31  ? -2.651  -11.324 -15.401 1.00 46.69  ? 74  LEU   A O   1 
ATOM   245  C CB  . LEU   A 1 31  ? -1.765  -9.125  -17.362 1.00 51.36  ? 74  LEU   A CB  1 
ATOM   246  C CG  . LEU   A 1 31  ? -1.547  -8.461  -18.724 1.00 53.22  ? 74  LEU   A CG  1 
ATOM   247  C CD1 . LEU   A 1 31  ? -2.172  -7.073  -18.750 1.00 52.85  ? 74  LEU   A CD1 1 
ATOM   248  C CD2 . LEU   A 1 31  ? -0.062  -8.384  -19.067 1.00 55.11  ? 74  LEU   A CD2 1 
ATOM   249  N N   . ASP   A 1 32  ? -0.404  -11.344 -15.113 1.00 48.67  ? 75  ASP   A N   1 
ATOM   250  C CA  . ASP   A 1 32  ? -0.394  -11.598 -13.647 1.00 48.79  ? 75  ASP   A CA  1 
ATOM   251  C C   . ASP   A 1 32  ? -0.585  -10.291 -12.903 1.00 44.97  ? 75  ASP   A C   1 
ATOM   252  O O   . ASP   A 1 32  ? 0.298   -9.396  -13.023 1.00 44.91  ? 75  ASP   A O   1 
ATOM   253  C CB  . ASP   A 1 32  ? 0.919   -12.214 -13.179 1.00 52.55  ? 75  ASP   A CB  1 
ATOM   254  C CG  . ASP   A 1 32  ? 1.149   -13.542 -13.857 1.00 56.42  ? 75  ASP   A CG  1 
ATOM   255  O OD1 . ASP   A 1 32  ? 0.127   -14.171 -14.253 1.00 59.39  ? 75  ASP   A OD1 1 
ATOM   256  O OD2 . ASP   A 1 32  ? 2.335   -13.907 -14.028 1.00 61.30  ? 75  ASP   A OD2 1 
ATOM   257  N N   . VAL   A 1 33  ? -1.676  -10.195 -12.157 1.00 43.24  ? 76  VAL   A N   1 
ATOM   258  C CA  . VAL   A 1 33  ? -2.015  -8.930  -11.443 1.00 42.49  ? 76  VAL   A CA  1 
ATOM   259  C C   . VAL   A 1 33  ? -2.353  -9.237  -9.963  1.00 41.98  ? 76  VAL   A C   1 
ATOM   260  O O   . VAL   A 1 33  ? -2.820  -10.367 -9.611  1.00 40.62  ? 76  VAL   A O   1 
ATOM   261  C CB  . VAL   A 1 33  ? -3.118  -8.120  -12.180 1.00 41.57  ? 76  VAL   A CB  1 
ATOM   262  C CG1 . VAL   A 1 33  ? -2.843  -7.956  -13.673 1.00 42.80  ? 76  VAL   A CG1 1 
ATOM   263  C CG2 . VAL   A 1 33  ? -4.499  -8.716  -12.008 1.00 40.79  ? 76  VAL   A CG2 1 
ATOM   264  N N   . ALA   A 1 34  ? -2.139  -8.228  -9.125  1.00 41.31  ? 77  ALA   A N   1 
ATOM   265  C CA  . ALA   A 1 34  ? -2.544  -8.199  -7.700  1.00 40.77  ? 77  ALA   A CA  1 
ATOM   266  C C   . ALA   A 1 34  ? -3.534  -7.054  -7.525  1.00 39.46  ? 77  ALA   A C   1 
ATOM   267  O O   . ALA   A 1 34  ? -3.425  -6.066  -8.251  1.00 40.57  ? 77  ALA   A O   1 
ATOM   268  C CB  . ALA   A 1 34  ? -1.321  -8.047  -6.839  1.00 41.65  ? 77  ALA   A CB  1 
ATOM   269  N N   . LEU   A 1 35  ? -4.521  -7.252  -6.662  1.00 37.98  ? 78  LEU   A N   1 
ATOM   270  C CA  . LEU   A 1 35  ? -5.544  -6.262  -6.306  1.00 37.28  ? 78  LEU   A CA  1 
ATOM   271  C C   . LEU   A 1 35  ? -5.364  -5.914  -4.817  1.00 38.34  ? 78  LEU   A C   1 
ATOM   272  O O   . LEU   A 1 35  ? -5.386  -6.875  -3.968  1.00 39.20  ? 78  LEU   A O   1 
ATOM   273  C CB  . LEU   A 1 35  ? -6.909  -6.882  -6.625  1.00 36.05  ? 78  LEU   A CB  1 
ATOM   274  C CG  . LEU   A 1 35  ? -8.104  -6.009  -6.266  1.00 35.27  ? 78  LEU   A CG  1 
ATOM   275  C CD1 . LEU   A 1 35  ? -8.109  -4.713  -7.021  1.00 35.32  ? 78  LEU   A CD1 1 
ATOM   276  C CD2 . LEU   A 1 35  ? -9.393  -6.768  -6.470  1.00 34.65  ? 78  LEU   A CD2 1 
ATOM   277  N N   . ASP   A 1 36  ? -5.110  -4.638  -4.529  1.00 37.86  ? 79  ASP   A N   1 
ATOM   278  C CA  . ASP   A 1 36  ? -4.823  -4.184  -3.143  1.00 39.00  ? 79  ASP   A CA  1 
ATOM   279  C C   . ASP   A 1 36  ? -6.131  -3.741  -2.477  1.00 38.15  ? 79  ASP   A C   1 
ATOM   280  O O   . ASP   A 1 36  ? -7.200  -3.684  -3.125  1.00 36.52  ? 79  ASP   A O   1 
ATOM   281  C CB  . ASP   A 1 36  ? -3.711  -3.136  -3.133  1.00 40.43  ? 79  ASP   A CB  1 
ATOM   282  C CG  . ASP   A 1 36  ? -4.064  -1.719  -3.558  1.00 40.53  ? 79  ASP   A CG  1 
ATOM   283  O OD1 . ASP   A 1 36  ? -5.236  -1.421  -3.809  1.00 39.69  ? 79  ASP   A OD1 1 
ATOM   284  O OD2 . ASP   A 1 36  ? -3.124  -0.898  -3.602  1.00 43.36  ? 79  ASP   A OD2 1 
ATOM   285  N N   . GLU   A 1 37  ? -6.053  -3.438  -1.179  1.00 39.45  ? 80  GLU   A N   1 
ATOM   286  C CA  . GLU   A 1 37  ? -7.266  -3.125  -0.410  1.00 39.85  ? 80  GLU   A CA  1 
ATOM   287  C C   . GLU   A 1 37  ? -7.903  -1.825  -0.923  1.00 38.40  ? 80  GLU   A C   1 
ATOM   288  O O   . GLU   A 1 37  ? -9.117  -1.704  -0.784  1.00 38.51  ? 80  GLU   A O   1 
ATOM   289  C CB  . GLU   A 1 37  ? -6.868  -3.111  1.065   1.00 42.29  ? 80  GLU   A CB  1 
ATOM   290  C CG  . GLU   A 1 37  ? -8.067  -3.069  1.972   1.00 44.51  ? 80  GLU   A CG  1 
ATOM   291  C CD  . GLU   A 1 37  ? -7.679  -2.968  3.448   1.00 47.30  ? 80  GLU   A CD  1 
ATOM   292  O OE1 . GLU   A 1 37  ? -7.485  -1.832  3.964   1.00 49.03  ? 80  GLU   A OE1 1 
ATOM   293  O OE2 . GLU   A 1 37  ? -7.497  -4.026  4.064   1.00 50.47  ? 80  GLU   A OE2 1 
ATOM   294  N N   . SER   A 1 38  ? -7.136  -0.909  -1.536  1.00 39.40  ? 81  SER   A N   1 
ATOM   295  C CA  . SER   A 1 38  ? -7.651  0.346   -2.142  1.00 39.65  ? 81  SER   A CA  1 
ATOM   296  C C   . SER   A 1 38  ? -8.266  0.092   -3.531  1.00 38.41  ? 81  SER   A C   1 
ATOM   297  O O   . SER   A 1 38  ? -8.683  1.064   -4.137  1.00 37.83  ? 81  SER   A O   1 
ATOM   298  C CB  . SER   A 1 38  ? -6.575  1.370   -2.282  1.00 42.15  ? 81  SER   A CB  1 
ATOM   299  O OG  . SER   A 1 38  ? -5.990  1.654   -1.033  1.00 46.05  ? 81  SER   A OG  1 
ATOM   300  N N   . GLY   A 1 39  ? -8.353  -1.148  -4.010  1.00 37.56  ? 82  GLY   A N   1 
ATOM   301  C CA  . GLY   A 1 39  ? -8.994  -1.447  -5.313  1.00 37.27  ? 82  GLY   A CA  1 
ATOM   302  C C   . GLY   A 1 39  ? -8.117  -1.067  -6.511  1.00 37.34  ? 82  GLY   A C   1 
ATOM   303  O O   . GLY   A 1 39  ? -8.693  -0.942  -7.589  1.00 36.39  ? 82  GLY   A O   1 
ATOM   304  N N   . ASP   A 1 40  ? -6.804  -0.931  -6.323  1.00 39.10  ? 83  ASP   A N   1 
ATOM   305  C CA  . ASP   A 1 40  ? -5.786  -0.698  -7.379  1.00 41.76  ? 83  ASP   A CA  1 
ATOM   306  C C   . ASP   A 1 40  ? -5.204  -2.050  -7.788  1.00 41.36  ? 83  ASP   A C   1 
ATOM   307  O O   . ASP   A 1 40  ? -4.645  -2.780  -6.930  1.00 40.49  ? 83  ASP   A O   1 
ATOM   308  C CB  . ASP   A 1 40  ? -4.728  0.320   -6.940  1.00 44.88  ? 83  ASP   A CB  1 
ATOM   309  C CG  . ASP   A 1 40  ? -5.309  1.698   -6.669  1.00 47.41  ? 83  ASP   A CG  1 
ATOM   310  O OD1 . ASP   A 1 40  ? -6.412  1.963   -7.148  1.00 51.12  ? 83  ASP   A OD1 1 
ATOM   311  O OD2 . ASP   A 1 40  ? -4.685  2.488   -5.951  1.00 52.73  ? 83  ASP   A OD2 1 
ATOM   312  N N   . PHE   A 1 41  ? -5.300  -2.351  -9.083  1.00 40.78  ? 84  PHE   A N   1 
ATOM   313  C CA  . PHE   A 1 41  ? -4.602  -3.493  -9.722  1.00 41.26  ? 84  PHE   A CA  1 
ATOM   314  C C   . PHE   A 1 41  ? -3.139  -3.129  -9.900  1.00 43.53  ? 84  PHE   A C   1 
ATOM   315  O O   . PHE   A 1 41  ? -2.865  -1.949  -10.108 1.00 45.54  ? 84  PHE   A O   1 
ATOM   316  C CB  . PHE   A 1 41  ? -5.256  -3.822  -11.057 1.00 39.19  ? 84  PHE   A CB  1 
ATOM   317  C CG  . PHE   A 1 41  ? -6.567  -4.575  -10.946 1.00 37.81  ? 84  PHE   A CG  1 
ATOM   318  C CD1 . PHE   A 1 41  ? -6.580  -5.906  -10.560 1.00 37.09  ? 84  PHE   A CD1 1 
ATOM   319  C CD2 . PHE   A 1 41  ? -7.795  -3.979  -11.277 1.00 36.91  ? 84  PHE   A CD2 1 
ATOM   320  C CE1 . PHE   A 1 41  ? -7.779  -6.620  -10.507 1.00 36.81  ? 84  PHE   A CE1 1 
ATOM   321  C CE2 . PHE   A 1 41  ? -8.990  -4.709  -11.210 1.00 36.61  ? 84  PHE   A CE2 1 
ATOM   322  C CZ  . PHE   A 1 41  ? -8.975  -6.029  -10.870 1.00 36.66  ? 84  PHE   A CZ  1 
ATOM   323  N N   . SER   A 1 42  ? -2.229  -4.093  -9.827  1.00 45.61  ? 85  SER   A N   1 
ATOM   324  C CA  . SER   A 1 42  ? -0.793  -3.860  -10.112 1.00 47.84  ? 85  SER   A CA  1 
ATOM   325  C C   . SER   A 1 42  ? -0.234  -5.094  -10.812 1.00 49.58  ? 85  SER   A C   1 
ATOM   326  O O   . SER   A 1 42  ? -0.800  -6.196  -10.621 1.00 48.10  ? 85  SER   A O   1 
ATOM   327  C CB  . SER   A 1 42  ? -0.038  -3.517  -8.856  1.00 50.55  ? 85  SER   A CB  1 
ATOM   328  O OG  . SER   A 1 42  ? -0.052  -4.593  -7.908  1.00 49.26  ? 85  SER   A OG  1 
ATOM   329  N N   . LEU   A 1 43  ? 0.781   -4.912  -11.659 1.00 53.31  ? 86  LEU   A N   1 
ATOM   330  C CA  . LEU   A 1 43  ? 1.430   -6.051  -12.358 1.00 55.78  ? 86  LEU   A CA  1 
ATOM   331  C C   . LEU   A 1 43  ? 2.356   -6.777  -11.386 1.00 57.59  ? 86  LEU   A C   1 
ATOM   332  O O   . LEU   A 1 43  ? 3.233   -6.125  -10.813 1.00 57.22  ? 86  LEU   A O   1 
ATOM   333  C CB  . LEU   A 1 43  ? 2.193   -5.528  -13.572 1.00 58.28  ? 86  LEU   A CB  1 
ATOM   334  C CG  . LEU   A 1 43  ? 1.279   -5.165  -14.731 1.00 58.73  ? 86  LEU   A CG  1 
ATOM   335  C CD1 . LEU   A 1 43  ? 1.984   -4.222  -15.684 1.00 61.49  ? 86  LEU   A CD1 1 
ATOM   336  C CD2 . LEU   A 1 43  ? 0.813   -6.427  -15.444 1.00 59.76  ? 86  LEU   A CD2 1 
ATOM   337  N N   . VAL   A 1 44  ? 2.139   -8.076  -11.212 1.00 59.89  ? 87  VAL   A N   1 
ATOM   338  C CA  . VAL   A 1 44  ? 3.126   -9.045  -10.641 1.00 63.93  ? 87  VAL   A CA  1 
ATOM   339  C C   . VAL   A 1 44  ? 4.070   -9.451  -11.781 1.00 68.95  ? 87  VAL   A C   1 
ATOM   340  O O   . VAL   A 1 44  ? 3.659   -9.351  -12.969 1.00 72.47  ? 87  VAL   A O   1 
ATOM   341  C CB  . VAL   A 1 44  ? 2.388   -10.269 -10.070 1.00 62.13  ? 87  VAL   A CB  1 
ATOM   342  C CG1 . VAL   A 1 44  ? 3.341   -11.322 -9.521  1.00 63.17  ? 87  VAL   A CG1 1 
ATOM   343  C CG2 . VAL   A 1 44  ? 1.350   -9.851  -9.039  1.00 60.30  ? 87  VAL   A CG2 1 
ATOM   344  N N   . GLU   A 1 45  ? 5.275   -9.908  -11.467 1.00 75.55  ? 88  GLU   A N   1 
ATOM   345  C CA  . GLU   A 1 45  ? 6.257   -10.319 -12.510 1.00 80.20  ? 88  GLU   A CA  1 
ATOM   346  C C   . GLU   A 1 45  ? 7.082   -11.528 -12.042 1.00 81.68  ? 88  GLU   A C   1 
ATOM   347  O O   . GLU   A 1 45  ? 6.875   -12.081 -10.941 1.00 79.77  ? 88  GLU   A O   1 
ATOM   348  C CB  . GLU   A 1 45  ? 7.109   -9.098  -12.852 1.00 84.25  ? 88  GLU   A CB  1 
ATOM   349  C CG  . GLU   A 1 45  ? 6.394   -8.109  -13.756 1.00 85.38  ? 88  GLU   A CG  1 
ATOM   350  C CD  . GLU   A 1 45  ? 6.473   -8.470  -15.225 1.00 85.34  ? 88  GLU   A CD  1 
ATOM   351  O OE1 . GLU   A 1 45  ? 6.634   -9.674  -15.528 1.00 85.00  ? 88  GLU   A OE1 1 
ATOM   352  O OE2 . GLU   A 1 45  ? 6.419   -7.543  -16.049 1.00 85.82  ? 88  GLU   A OE2 1 
ATOM   353  N N   . GLY   B 2 7   ? -36.462 12.317  -11.742 1.00 60.83  ? 16  GLY   B N   1 
ATOM   354  C CA  . GLY   B 2 7   ? -35.335 12.202  -12.739 1.00 61.79  ? 16  GLY   B CA  1 
ATOM   355  C C   . GLY   B 2 7   ? -35.597 11.173  -13.843 1.00 60.19  ? 16  GLY   B C   1 
ATOM   356  O O   . GLY   B 2 7   ? -36.524 10.331  -13.700 1.00 62.30  ? 16  GLY   B O   1 
ATOM   357  N N   . GLU   B 2 8   ? -34.800 11.221  -14.915 1.00 57.01  ? 17  GLU   B N   1 
ATOM   358  C CA  . GLU   B 2 8   ? -34.799 10.211  -16.010 1.00 53.68  ? 17  GLU   B CA  1 
ATOM   359  C C   . GLU   B 2 8   ? -34.379 8.832   -15.478 1.00 50.73  ? 17  GLU   B C   1 
ATOM   360  O O   . GLU   B 2 8   ? -33.274 8.688   -14.946 1.00 50.03  ? 17  GLU   B O   1 
ATOM   361  C CB  . GLU   B 2 8   ? -33.824 10.627  -17.103 1.00 55.47  ? 17  GLU   B CB  1 
ATOM   362  C CG  . GLU   B 2 8   ? -33.994 9.826   -18.365 1.00 55.82  ? 17  GLU   B CG  1 
ATOM   363  C CD  . GLU   B 2 8   ? -33.269 10.446  -19.547 1.00 58.46  ? 17  GLU   B CD  1 
ATOM   364  O OE1 . GLU   B 2 8   ? -32.290 11.235  -19.314 1.00 57.87  ? 17  GLU   B OE1 1 
ATOM   365  O OE2 . GLU   B 2 8   ? -33.721 10.181  -20.701 1.00 61.35  ? 17  GLU   B OE2 1 
ATOM   366  N N   A THR   B 2 9   ? -35.243 7.828   -15.644 0.25 50.33  ? 18  THR   B N   1 
ATOM   367  N N   B THR   B 2 9   ? -35.269 7.847   -15.635 0.25 49.68  ? 18  THR   B N   1 
ATOM   368  N N   C THR   B 2 9   ? -35.243 7.828   -15.644 0.25 50.33  ? 18  THR   B N   1 
ATOM   369  N N   D THR   B 2 9   ? -35.269 7.847   -15.635 0.25 49.68  ? 18  THR   B N   1 
ATOM   370  C CA  A THR   B 2 9   ? -35.052 6.461   -15.091 0.25 49.78  ? 18  THR   B CA  1 
ATOM   371  C CA  B THR   B 2 9   ? -35.140 6.475   -15.079 0.25 48.73  ? 18  THR   B CA  1 
ATOM   372  C CA  C THR   B 2 9   ? -35.052 6.461   -15.091 0.25 49.78  ? 18  THR   B CA  1 
ATOM   373  C CA  D THR   B 2 9   ? -35.140 6.475   -15.079 0.25 48.73  ? 18  THR   B CA  1 
ATOM   374  C C   A THR   B 2 9   ? -35.110 5.415   -16.206 0.25 48.59  ? 18  THR   B C   1 
ATOM   375  C C   B THR   B 2 9   ? -34.943 5.457   -16.209 0.25 47.95  ? 18  THR   B C   1 
ATOM   376  C C   C THR   B 2 9   ? -35.110 5.415   -16.206 0.25 48.59  ? 18  THR   B C   1 
ATOM   377  C C   D THR   B 2 9   ? -34.943 5.457   -16.209 0.25 47.95  ? 18  THR   B C   1 
ATOM   378  O O   A THR   B 2 9   ? -35.092 4.216   -15.870 0.25 48.92  ? 18  THR   B O   1 
ATOM   379  O O   B THR   B 2 9   ? -34.514 4.330   -15.892 0.25 48.08  ? 18  THR   B O   1 
ATOM   380  O O   C THR   B 2 9   ? -35.092 4.216   -15.870 0.25 48.92  ? 18  THR   B O   1 
ATOM   381  O O   D THR   B 2 9   ? -34.514 4.330   -15.892 0.25 48.08  ? 18  THR   B O   1 
ATOM   382  C CB  A THR   B 2 9   ? -36.101 6.175   -14.011 0.25 50.47  ? 18  THR   B CB  1 
ATOM   383  C CB  B THR   B 2 9   ? -36.352 6.132   -14.198 0.25 48.69  ? 18  THR   B CB  1 
ATOM   384  C CB  C THR   B 2 9   ? -36.101 6.175   -14.011 0.25 50.47  ? 18  THR   B CB  1 
ATOM   385  C CB  D THR   B 2 9   ? -36.352 6.132   -14.198 0.25 48.69  ? 18  THR   B CB  1 
ATOM   386  O OG1 A THR   B 2 9   ? -36.274 7.402   -13.304 0.25 51.34  ? 18  THR   B OG1 1 
ATOM   387  O OG1 B THR   B 2 9   ? -37.544 6.513   -14.883 0.25 48.57  ? 18  THR   B OG1 1 
ATOM   388  O OG1 C THR   B 2 9   ? -36.274 7.402   -13.304 0.25 51.34  ? 18  THR   B OG1 1 
ATOM   389  O OG1 D THR   B 2 9   ? -37.544 6.513   -14.883 0.25 48.57  ? 18  THR   B OG1 1 
ATOM   390  C CG2 A THR   B 2 9   ? -35.705 5.056   -13.071 0.25 50.95  ? 18  THR   B CG2 1 
ATOM   391  C CG2 B THR   B 2 9   ? -36.315 6.820   -12.850 0.25 49.02  ? 18  THR   B CG2 1 
ATOM   392  C CG2 C THR   B 2 9   ? -35.705 5.056   -13.071 0.25 50.95  ? 18  THR   B CG2 1 
ATOM   393  C CG2 D THR   B 2 9   ? -36.315 6.820   -12.850 0.25 49.02  ? 18  THR   B CG2 1 
ATOM   394  N N   . THR   B 2 10  ? -35.194 5.845   -17.469 1.00 47.51  ? 19  THR   B N   1 
ATOM   395  C CA  . THR   B 2 10  ? -35.151 4.929   -18.630 1.00 45.62  ? 19  THR   B CA  1 
ATOM   396  C C   . THR   B 2 10  ? -33.838 4.134   -18.577 1.00 42.30  ? 19  THR   B C   1 
ATOM   397  O O   . THR   B 2 10  ? -32.779 4.759   -18.399 1.00 42.30  ? 19  THR   B O   1 
ATOM   398  C CB  . THR   B 2 10  ? -35.289 5.690   -19.963 1.00 45.43  ? 19  THR   B CB  1 
ATOM   399  O OG1 . THR   B 2 10  ? -36.301 6.700   -19.905 1.00 47.27  ? 19  THR   B OG1 1 
ATOM   400  C CG2 . THR   B 2 10  ? -35.649 4.757   -21.092 1.00 46.38  ? 19  THR   B CG2 1 
ATOM   401  N N   . ASP   B 2 11  ? -33.915 2.810   -18.715 1.00 41.36  ? 20  ASP   B N   1 
ATOM   402  C CA  . ASP   B 2 11  ? -32.694 1.992   -18.979 1.00 41.35  ? 20  ASP   B CA  1 
ATOM   403  C C   . ASP   B 2 11  ? -31.802 2.699   -20.016 1.00 41.66  ? 20  ASP   B C   1 
ATOM   404  O O   . ASP   B 2 11  ? -32.358 3.397   -20.962 1.00 41.58  ? 20  ASP   B O   1 
ATOM   405  C CB  . ASP   B 2 11  ? -33.048 0.573   -19.427 1.00 42.64  ? 20  ASP   B CB  1 
ATOM   406  C CG  . ASP   B 2 11  ? -33.690 -0.298  -18.350 1.00 44.23  ? 20  ASP   B CG  1 
ATOM   407  O OD1 . ASP   B 2 11  ? -33.914 0.211   -17.218 1.00 41.99  ? 20  ASP   B OD1 1 
ATOM   408  O OD2 . ASP   B 2 11  ? -33.942 -1.510  -18.655 1.00 45.74  ? 20  ASP   B OD2 1 
ATOM   409  N N   . GLY   B 2 12  ? -30.483 2.557   -19.849 1.00 39.03  ? 21  GLY   B N   1 
ATOM   410  C CA  . GLY   B 2 12  ? -29.479 2.889   -20.874 1.00 38.48  ? 21  GLY   B CA  1 
ATOM   411  C C   . GLY   B 2 12  ? -28.184 3.304   -20.235 1.00 37.21  ? 21  GLY   B C   1 
ATOM   412  O O   . GLY   B 2 12  ? -27.987 3.036   -19.004 1.00 35.99  ? 21  GLY   B O   1 
ATOM   413  N N   . VAL   B 2 13  ? -27.321 3.911   -21.037 1.00 35.44  ? 22  VAL   B N   1 
ATOM   414  C CA  . VAL   B 2 13  ? -25.976 4.384   -20.625 1.00 34.40  ? 22  VAL   B CA  1 
ATOM   415  C C   . VAL   B 2 13  ? -26.038 5.898   -20.472 1.00 34.28  ? 22  VAL   B C   1 
ATOM   416  O O   . VAL   B 2 13  ? -26.793 6.610   -21.241 1.00 34.60  ? 22  VAL   B O   1 
ATOM   417  C CB  . VAL   B 2 13  ? -24.885 3.854   -21.561 1.00 34.33  ? 22  VAL   B CB  1 
ATOM   418  C CG1 . VAL   B 2 13  ? -25.025 4.370   -23.029 1.00 34.70  ? 22  VAL   B CG1 1 
ATOM   419  C CG2 . VAL   B 2 13  ? -23.486 4.138   -21.064 1.00 34.13  ? 22  VAL   B CG2 1 
ATOM   420  N N   . TYR   B 2 14  ? -25.339 6.405   -19.439 1.00 33.54  ? 23  TYR   B N   1 
ATOM   421  C CA  . TYR   B 2 14  ? -25.399 7.823   -19.053 1.00 33.86  ? 23  TYR   B CA  1 
ATOM   422  C C   . TYR   B 2 14  ? -23.996 8.320   -18.809 1.00 33.97  ? 23  TYR   B C   1 
ATOM   423  O O   . TYR   B 2 14  ? -23.127 7.572   -18.261 1.00 34.38  ? 23  TYR   B O   1 
ATOM   424  C CB  . TYR   B 2 14  ? -26.224 8.030   -17.775 1.00 33.91  ? 23  TYR   B CB  1 
ATOM   425  C CG  . TYR   B 2 14  ? -27.697 7.813   -17.959 1.00 34.57  ? 23  TYR   B CG  1 
ATOM   426  C CD1 . TYR   B 2 14  ? -28.191 6.554   -18.318 1.00 35.19  ? 23  TYR   B CD1 1 
ATOM   427  C CD2 . TYR   B 2 14  ? -28.569 8.886   -17.759 1.00 35.41  ? 23  TYR   B CD2 1 
ATOM   428  C CE1 . TYR   B 2 14  ? -29.547 6.342   -18.441 1.00 36.11  ? 23  TYR   B CE1 1 
ATOM   429  C CE2 . TYR   B 2 14  ? -29.936 8.698   -17.878 1.00 36.27  ? 23  TYR   B CE2 1 
ATOM   430  C CZ  . TYR   B 2 14  ? -30.418 7.429   -18.230 1.00 37.13  ? 23  TYR   B CZ  1 
ATOM   431  O OH  . TYR   B 2 14  ? -31.768 7.241   -18.344 1.00 39.96  ? 23  TYR   B OH  1 
ATOM   432  N N   . ARG   B 2 15  ? -23.815 9.600   -19.072 1.00 34.14  ? 24  ARG   B N   1 
ATOM   433  C CA  . ARG   B 2 15  ? -22.583 10.316  -18.684 1.00 34.66  ? 24  ARG   B CA  1 
ATOM   434  C C   . ARG   B 2 15  ? -22.723 10.785  -17.226 1.00 34.38  ? 24  ARG   B C   1 
ATOM   435  O O   . ARG   B 2 15  ? -23.820 11.182  -16.845 1.00 33.24  ? 24  ARG   B O   1 
ATOM   436  C CB  . ARG   B 2 15  ? -22.330 11.508  -19.607 1.00 35.78  ? 24  ARG   B CB  1 
ATOM   437  C CG  . ARG   B 2 15  ? -22.244 11.147  -21.089 1.00 36.89  ? 24  ARG   B CG  1 
ATOM   438  C CD  . ARG   B 2 15  ? -22.284 12.439  -21.881 1.00 38.44  ? 24  ARG   B CD  1 
ATOM   439  N NE  . ARG   B 2 15  ? -22.420 12.170  -23.321 1.00 39.18  ? 24  ARG   B NE  1 
ATOM   440  C CZ  . ARG   B 2 15  ? -21.411 11.914  -24.157 1.00 39.83  ? 24  ARG   B CZ  1 
ATOM   441  N NH1 . ARG   B 2 15  ? -20.155 11.965  -23.747 1.00 39.18  ? 24  ARG   B NH1 1 
ATOM   442  N NH2 . ARG   B 2 15  ? -21.683 11.632  -25.427 1.00 41.33  ? 24  ARG   B NH2 1 
ATOM   443  N N   . VAL   B 2 16  ? -21.606 10.806  -16.510 1.00 34.88  ? 25  VAL   B N   1 
ATOM   444  C CA  . VAL   B 2 16  ? -21.500 11.422  -15.173 1.00 35.29  ? 25  VAL   B CA  1 
ATOM   445  C C   . VAL   B 2 16  ? -20.636 12.672  -15.271 1.00 35.83  ? 25  VAL   B C   1 
ATOM   446  O O   . VAL   B 2 16  ? -19.463 12.562  -15.605 1.00 36.76  ? 25  VAL   B O   1 
ATOM   447  C CB  . VAL   B 2 16  ? -20.936 10.412  -14.152 1.00 35.53  ? 25  VAL   B CB  1 
ATOM   448  C CG1 . VAL   B 2 16  ? -20.943 11.063  -12.778 1.00 35.16  ? 25  VAL   B CG1 1 
ATOM   449  C CG2 . VAL   B 2 16  ? -21.737 9.104   -14.162 1.00 35.41  ? 25  VAL   B CG2 1 
ATOM   450  N N   . MET   B 2 17  ? -21.240 13.819  -14.976 1.00 37.70  ? 26  MET   B N   1 
ATOM   451  C CA  . MET   B 2 17  ? -20.688 15.172  -15.208 1.00 39.59  ? 26  MET   B CA  1 
ATOM   452  C C   . MET   B 2 17  ? -20.487 15.901  -13.876 1.00 41.70  ? 26  MET   B C   1 
ATOM   453  O O   . MET   B 2 17  ? -21.251 15.606  -12.901 1.00 40.47  ? 26  MET   B O   1 
ATOM   454  C CB  . MET   B 2 17  ? -21.685 15.995  -16.034 1.00 39.85  ? 26  MET   B CB  1 
ATOM   455  C CG  . MET   B 2 17  ? -22.164 15.337  -17.320 1.00 40.95  ? 26  MET   B CG  1 
ATOM   456  S SD  . MET   B 2 17  ? -20.829 15.065  -18.517 1.00 41.02  ? 26  MET   B SD  1 
ATOM   457  C CE  . MET   B 2 17  ? -20.204 16.743  -18.662 1.00 42.61  ? 26  MET   B CE  1 
ATOM   458  N N   . THR   B 2 18  ? -19.590 16.886  -13.853 1.00 43.74  ? 27  THR   B N   1 
ATOM   459  C CA  . THR   B 2 18  ? -19.469 17.854  -12.731 1.00 47.89  ? 27  THR   B CA  1 
ATOM   460  C C   . THR   B 2 18  ? -19.282 19.280  -13.281 1.00 51.06  ? 27  THR   B C   1 
ATOM   461  O O   . THR   B 2 18  ? -18.697 19.421  -14.385 1.00 48.84  ? 27  THR   B O   1 
ATOM   462  C CB  . THR   B 2 18  ? -18.341 17.419  -11.782 1.00 47.86  ? 27  THR   B CB  1 
ATOM   463  O OG1 . THR   B 2 18  ? -18.354 18.340  -10.679 1.00 48.41  ? 27  THR   B OG1 1 
ATOM   464  C CG2 . THR   B 2 18  ? -16.983 17.362  -12.453 1.00 48.12  ? 27  THR   B CG2 1 
ATOM   465  N N   . ARG   B 2 19  ? -19.702 20.294  -12.503 1.00 55.70  ? 28  ARG   B N   1 
ATOM   466  C CA  . ARG   B 2 19  ? -19.408 21.729  -12.777 1.00 60.38  ? 28  ARG   B CA  1 
ATOM   467  C C   . ARG   B 2 19  ? -18.410 22.321  -11.762 1.00 60.34  ? 28  ARG   B C   1 
ATOM   468  O O   . ARG   B 2 19  ? -18.176 23.543  -11.821 1.00 59.63  ? 28  ARG   B O   1 
ATOM   469  C CB  . ARG   B 2 19  ? -20.718 22.509  -12.820 1.00 62.88  ? 28  ARG   B CB  1 
ATOM   470  C CG  . ARG   B 2 19  ? -21.634 22.019  -13.927 1.00 66.67  ? 28  ARG   B CG  1 
ATOM   471  C CD  . ARG   B 2 19  ? -22.114 23.137  -14.829 1.00 68.41  ? 28  ARG   B CD  1 
ATOM   472  N NE  . ARG   B 2 19  ? -23.182 22.688  -15.705 1.00 70.60  ? 28  ARG   B NE  1 
ATOM   473  C CZ  . ARG   B 2 19  ? -24.424 22.405  -15.318 1.00 73.76  ? 28  ARG   B CZ  1 
ATOM   474  N NH1 . ARG   B 2 19  ? -24.780 22.515  -14.045 1.00 78.53  ? 28  ARG   B NH1 1 
ATOM   475  N NH2 . ARG   B 2 19  ? -25.315 22.004  -16.210 1.00 74.38  ? 28  ARG   B NH2 1 
ATOM   476  N N   . ARG   B 2 20  ? -17.775 21.491  -10.935 1.00 63.01  ? 29  ARG   B N   1 
ATOM   477  C CA  . ARG   B 2 20  ? -16.897 21.935  -9.811  1.00 68.67  ? 29  ARG   B CA  1 
ATOM   478  C C   . ARG   B 2 20  ? -15.506 22.271  -10.368 1.00 68.42  ? 29  ARG   B C   1 
ATOM   479  O O   . ARG   B 2 20  ? -14.604 22.650  -9.584  1.00 69.53  ? 29  ARG   B O   1 
ATOM   480  C CB  . ARG   B 2 20  ? -16.840 20.829  -8.751  1.00 72.26  ? 29  ARG   B CB  1 
ATOM   481  C CG  . ARG   B 2 20  ? -16.476 21.283  -7.344  1.00 79.19  ? 29  ARG   B CG  1 
ATOM   482  C CD  . ARG   B 2 20  ? -16.166 20.071  -6.478  1.00 85.93  ? 29  ARG   B CD  1 
ATOM   483  N NE  . ARG   B 2 20  ? -15.251 19.142  -7.155  1.00 91.44  ? 29  ARG   B NE  1 
ATOM   484  C CZ  . ARG   B 2 20  ? -13.927 19.070  -6.974  1.00 96.40  ? 29  ARG   B CZ  1 
ATOM   485  N NH1 . ARG   B 2 20  ? -13.315 19.861  -6.105  1.00 100.61 ? 29  ARG   B NH1 1 
ATOM   486  N NH2 . ARG   B 2 20  ? -13.212 18.195  -7.665  1.00 96.02  ? 29  ARG   B NH2 1 
ATOM   487  N N   . LEU   B 2 21  ? -15.325 22.080  -11.675 1.00 65.43  ? 30  LEU   B N   1 
ATOM   488  C CA  . LEU   B 2 21  ? -14.071 22.366  -12.415 1.00 62.77  ? 30  LEU   B CA  1 
ATOM   489  C C   . LEU   B 2 21  ? -14.404 23.371  -13.531 1.00 60.68  ? 30  LEU   B C   1 
ATOM   490  O O   . LEU   B 2 21  ? -15.503 23.999  -13.459 1.00 59.15  ? 30  LEU   B O   1 
ATOM   491  C CB  . LEU   B 2 21  ? -13.539 21.022  -12.916 1.00 62.32  ? 30  LEU   B CB  1 
ATOM   492  C CG  . LEU   B 2 21  ? -12.424 20.364  -12.108 1.00 63.13  ? 30  LEU   B CG  1 
ATOM   493  C CD1 . LEU   B 2 21  ? -12.528 20.629  -10.611 1.00 63.36  ? 30  LEU   B CD1 1 
ATOM   494  C CD2 . LEU   B 2 21  ? -12.408 18.868  -12.375 1.00 62.67  ? 30  LEU   B CD2 1 
ATOM   495  N N   . LEU   B 2 22  ? -13.502 23.565  -14.504 1.00 59.65  ? 31  LEU   B N   1 
ATOM   496  C CA  . LEU   B 2 22  ? -13.731 24.495  -15.641 1.00 58.21  ? 31  LEU   B CA  1 
ATOM   497  C C   . LEU   B 2 22  ? -14.849 23.932  -16.515 1.00 57.41  ? 31  LEU   B C   1 
ATOM   498  O O   . LEU   B 2 22  ? -14.822 22.723  -16.740 1.00 59.26  ? 31  LEU   B O   1 
ATOM   499  C CB  . LEU   B 2 22  ? -12.435 24.632  -16.430 1.00 57.76  ? 31  LEU   B CB  1 
ATOM   500  C CG  . LEU   B 2 22  ? -12.446 25.731  -17.478 1.00 57.45  ? 31  LEU   B CG  1 
ATOM   501  C CD1 . LEU   B 2 22  ? -12.244 27.109  -16.852 1.00 56.53  ? 31  LEU   B CD1 1 
ATOM   502  C CD2 . LEU   B 2 22  ? -11.390 25.426  -18.534 1.00 57.87  ? 31  LEU   B CD2 1 
ATOM   503  N N   . GLY   B 2 23  ? -15.798 24.761  -16.965 1.00 56.42  ? 32  GLY   B N   1 
ATOM   504  C CA  . GLY   B 2 23  ? -16.993 24.301  -17.702 1.00 54.65  ? 32  GLY   B CA  1 
ATOM   505  C C   . GLY   B 2 23  ? -17.676 23.101  -17.034 1.00 53.65  ? 32  GLY   B C   1 
ATOM   506  O O   . GLY   B 2 23  ? -17.681 22.995  -15.773 1.00 53.64  ? 32  GLY   B O   1 
ATOM   507  N N   . SER   B 2 24  ? -18.288 22.250  -17.858 1.00 51.09  ? 33  SER   B N   1 
ATOM   508  C CA  . SER   B 2 24  ? -18.899 20.950  -17.496 1.00 48.65  ? 33  SER   B CA  1 
ATOM   509  C C   . SER   B 2 24  ? -17.915 19.865  -17.901 1.00 47.20  ? 33  SER   B C   1 
ATOM   510  O O   . SER   B 2 24  ? -17.575 19.831  -19.074 1.00 46.27  ? 33  SER   B O   1 
ATOM   511  C CB  . SER   B 2 24  ? -20.205 20.764  -18.191 1.00 48.54  ? 33  SER   B CB  1 
ATOM   512  O OG  . SER   B 2 24  ? -21.149 21.707  -17.706 1.00 49.32  ? 33  SER   B OG  1 
ATOM   513  N N   . THR   B 2 25  ? -17.437 19.062  -16.954 1.00 44.31  ? 34  THR   B N   1 
ATOM   514  C CA  . THR   B 2 25  ? -16.373 18.055  -17.158 1.00 43.94  ? 34  THR   B CA  1 
ATOM   515  C C   . THR   B 2 25  ? -16.958 16.660  -16.942 1.00 42.87  ? 34  THR   B C   1 
ATOM   516  O O   . THR   B 2 25  ? -17.676 16.480  -15.942 1.00 40.39  ? 34  THR   B O   1 
ATOM   517  C CB  . THR   B 2 25  ? -15.179 18.300  -16.225 1.00 44.61  ? 34  THR   B CB  1 
ATOM   518  O OG1 . THR   B 2 25  ? -14.732 19.654  -16.369 1.00 46.01  ? 34  THR   B OG1 1 
ATOM   519  C CG2 . THR   B 2 25  ? -14.034 17.348  -16.502 1.00 44.55  ? 34  THR   B CG2 1 
ATOM   520  N N   . GLN   B 2 26  ? -16.687 15.723  -17.851 1.00 41.52  ? 35  GLN   B N   1 
ATOM   521  C CA  . GLN   B 2 26  ? -17.208 14.334  -17.734 1.00 40.33  ? 35  GLN   B CA  1 
ATOM   522  C C   . GLN   B 2 26  ? -16.189 13.559  -16.895 1.00 40.22  ? 35  GLN   B C   1 
ATOM   523  O O   . GLN   B 2 26  ? -15.011 13.390  -17.356 1.00 40.41  ? 35  GLN   B O   1 
ATOM   524  C CB  . GLN   B 2 26  ? -17.447 13.644  -19.089 1.00 39.45  ? 35  GLN   B CB  1 
ATOM   525  C CG  . GLN   B 2 26  ? -17.881 12.173  -18.986 1.00 38.23  ? 35  GLN   B CG  1 
ATOM   526  C CD  . GLN   B 2 26  ? -18.253 11.523  -20.306 1.00 37.99  ? 35  GLN   B CD  1 
ATOM   527  O OE1 . GLN   B 2 26  ? -18.961 12.125  -21.119 1.00 38.40  ? 35  GLN   B OE1 1 
ATOM   528  N NE2 . GLN   B 2 26  ? -17.839 10.277  -20.520 1.00 36.76  ? 35  GLN   B NE2 1 
ATOM   529  N N   . VAL   B 2 27  ? -16.622 13.120  -15.716 1.00 39.92  ? 36  VAL   B N   1 
ATOM   530  C CA  . VAL   B 2 27  ? -15.763 12.362  -14.760 1.00 38.84  ? 36  VAL   B CA  1 
ATOM   531  C C   . VAL   B 2 27  ? -15.937 10.859  -15.001 1.00 37.27  ? 36  VAL   B C   1 
ATOM   532  O O   . VAL   B 2 27  ? -15.045 10.109  -14.629 1.00 37.12  ? 36  VAL   B O   1 
ATOM   533  C CB  . VAL   B 2 27  ? -16.099 12.780  -13.322 1.00 39.47  ? 36  VAL   B CB  1 
ATOM   534  C CG1 . VAL   B 2 27  ? -15.614 14.193  -13.074 1.00 40.93  ? 36  VAL   B CG1 1 
ATOM   535  C CG2 . VAL   B 2 27  ? -17.579 12.660  -13.027 1.00 38.76  ? 36  VAL   B CG2 1 
ATOM   536  N N   . GLY   B 2 28  ? -17.053 10.419  -15.600 1.00 35.67  ? 37  GLY   B N   1 
ATOM   537  C CA  . GLY   B 2 28  ? -17.201 9.012   -16.026 1.00 33.91  ? 37  GLY   B CA  1 
ATOM   538  C C   . GLY   B 2 28  ? -18.608 8.736   -16.563 1.00 33.06  ? 37  GLY   B C   1 
ATOM   539  O O   . GLY   B 2 28  ? -19.243 9.657   -17.090 1.00 34.30  ? 37  GLY   B O   1 
ATOM   540  N N   . VAL   B 2 29  ? -19.042 7.486   -16.501 1.00 32.29  ? 38  VAL   B N   1 
ATOM   541  C CA  . VAL   B 2 29  ? -20.194 6.878   -17.234 1.00 32.16  ? 38  VAL   B CA  1 
ATOM   542  C C   . VAL   B 2 29  ? -20.877 5.889   -16.286 1.00 31.91  ? 38  VAL   B C   1 
ATOM   543  O O   . VAL   B 2 29  ? -20.167 5.369   -15.379 1.00 31.15  ? 38  VAL   B O   1 
ATOM   544  C CB  . VAL   B 2 29  ? -19.692 6.148   -18.510 1.00 33.14  ? 38  VAL   B CB  1 
ATOM   545  C CG1 . VAL   B 2 29  ? -20.803 5.468   -19.297 1.00 32.99  ? 38  VAL   B CG1 1 
ATOM   546  C CG2 . VAL   B 2 29  ? -18.910 7.077   -19.394 1.00 33.52  ? 38  VAL   B CG2 1 
ATOM   547  N N   . GLY   B 2 30  ? -22.138 5.542   -16.536 1.00 31.83  ? 39  GLY   B N   1 
ATOM   548  C CA  . GLY   B 2 30  ? -22.777 4.429   -15.826 1.00 31.23  ? 39  GLY   B CA  1 
ATOM   549  C C   . GLY   B 2 30  ? -23.981 3.885   -16.522 1.00 31.78  ? 39  GLY   B C   1 
ATOM   550  O O   . GLY   B 2 30  ? -24.352 4.388   -17.672 1.00 32.11  ? 39  GLY   B O   1 
ATOM   551  N N   . VAL   B 2 31  ? -24.541 2.852   -15.922 1.00 31.05  ? 40  VAL   B N   1 
ATOM   552  C CA  . VAL   B 2 31  ? -25.644 2.034   -16.464 1.00 31.79  ? 40  VAL   B CA  1 
ATOM   553  C C   . VAL   B 2 31  ? -26.894 2.184   -15.624 1.00 32.45  ? 40  VAL   B C   1 
ATOM   554  O O   . VAL   B 2 31  ? -26.837 1.856   -14.397 1.00 31.18  ? 40  VAL   B O   1 
ATOM   555  C CB  . VAL   B 2 31  ? -25.271 0.558   -16.570 1.00 32.29  ? 40  VAL   B CB  1 
ATOM   556  C CG1 . VAL   B 2 31  ? -26.487 -0.260  -16.975 1.00 32.88  ? 40  VAL   B CG1 1 
ATOM   557  C CG2 . VAL   B 2 31  ? -24.108 0.369   -17.518 1.00 32.63  ? 40  VAL   B CG2 1 
ATOM   558  N N   . MET   B 2 32  ? -27.993 2.594   -16.249 1.00 32.71  ? 41  MET   B N   1 
ATOM   559  C CA  . MET   B 2 32  ? -29.321 2.575   -15.620 1.00 33.40  ? 41  MET   B CA  1 
ATOM   560  C C   . MET   B 2 32  ? -30.055 1.285   -16.043 1.00 34.41  ? 41  MET   B C   1 
ATOM   561  O O   . MET   B 2 32  ? -30.236 0.990   -17.264 1.00 33.83  ? 41  MET   B O   1 
ATOM   562  C CB  . MET   B 2 32  ? -30.079 3.851   -15.981 1.00 33.89  ? 41  MET   B CB  1 
ATOM   563  C CG  . MET   B 2 32  ? -31.359 4.063   -15.200 1.00 34.12  ? 41  MET   B CG  1 
ATOM   564  S SD  . MET   B 2 32  ? -31.015 4.654   -13.482 1.00 34.41  ? 41  MET   B SD  1 
ATOM   565  C CE  . MET   B 2 32  ? -30.520 6.337   -13.833 1.00 35.59  ? 41  MET   B CE  1 
ATOM   566  N N   . GLN   B 2 33  ? -30.420 0.466   -15.065 1.00 34.75  ? 42  GLN   B N   1 
ATOM   567  C CA  . GLN   B 2 33  ? -31.096 -0.818  -15.286 1.00 36.94  ? 42  GLN   B CA  1 
ATOM   568  C C   . GLN   B 2 33  ? -32.010 -1.104  -14.125 1.00 37.92  ? 42  GLN   B C   1 
ATOM   569  O O   . GLN   B 2 33  ? -31.526 -1.018  -12.930 1.00 37.31  ? 42  GLN   B O   1 
ATOM   570  C CB  . GLN   B 2 33  ? -30.135 -1.988  -15.527 1.00 37.92  ? 42  GLN   B CB  1 
ATOM   571  C CG  . GLN   B 2 33  ? -30.930 -3.273  -15.750 1.00 40.44  ? 42  GLN   B CG  1 
ATOM   572  C CD  . GLN   B 2 33  ? -30.167 -4.396  -16.417 1.00 42.81  ? 42  GLN   B CD  1 
ATOM   573  O OE1 . GLN   B 2 33  ? -30.242 -5.555  -15.979 1.00 48.50  ? 42  GLN   B OE1 1 
ATOM   574  N NE2 . GLN   B 2 33  ? -29.297 -4.043  -17.348 1.00 41.30  ? 42  GLN   B NE2 1 
ATOM   575  N N   . GLU   B 2 34  ? -33.256 -1.438  -14.420 1.00 39.37  ? 43  GLU   B N   1 
ATOM   576  C CA  . GLU   B 2 34  ? -34.315 -1.699  -13.407 1.00 41.05  ? 43  GLU   B CA  1 
ATOM   577  C C   . GLU   B 2 34  ? -34.359 -0.583  -12.361 1.00 40.41  ? 43  GLU   B C   1 
ATOM   578  O O   . GLU   B 2 34  ? -34.549 -0.900  -11.176 1.00 40.70  ? 43  GLU   B O   1 
ATOM   579  C CB  . GLU   B 2 34  ? -34.044 -3.050  -12.747 1.00 43.51  ? 43  GLU   B CB  1 
ATOM   580  C CG  . GLU   B 2 34  ? -34.204 -4.229  -13.690 1.00 45.89  ? 43  GLU   B CG  1 
ATOM   581  C CD  . GLU   B 2 34  ? -33.505 -5.523  -13.309 1.00 47.84  ? 43  GLU   B CD  1 
ATOM   582  O OE1 . GLU   B 2 34  ? -33.907 -6.113  -12.325 1.00 50.28  ? 43  GLU   B OE1 1 
ATOM   583  O OE2 . GLU   B 2 34  ? -32.595 -5.964  -14.054 1.00 52.62  ? 43  GLU   B OE2 1 
ATOM   584  N N   . GLY   B 2 35  ? -34.192 0.692   -12.729 1.00 38.47  ? 44  GLY   B N   1 
ATOM   585  C CA  . GLY   B 2 35  ? -34.333 1.816   -11.780 1.00 37.10  ? 44  GLY   B CA  1 
ATOM   586  C C   . GLY   B 2 35  ? -33.133 1.985   -10.842 1.00 35.22  ? 44  GLY   B C   1 
ATOM   587  O O   . GLY   B 2 35  ? -33.214 2.844   -9.954  1.00 35.10  ? 44  GLY   B O   1 
ATOM   588  N N   . VAL   B 2 36  ? -32.049 1.254   -11.068 1.00 33.48  ? 45  VAL   B N   1 
ATOM   589  C CA  . VAL   B 2 36  ? -30.758 1.372   -10.335 1.00 32.25  ? 45  VAL   B CA  1 
ATOM   590  C C   . VAL   B 2 36  ? -29.664 1.901   -11.268 1.00 31.46  ? 45  VAL   B C   1 
ATOM   591  O O   . VAL   B 2 36  ? -29.549 1.409   -12.434 1.00 31.32  ? 45  VAL   B O   1 
ATOM   592  C CB  . VAL   B 2 36  ? -30.393 0.023   -9.679  1.00 32.04  ? 45  VAL   B CB  1 
ATOM   593  C CG1 . VAL   B 2 36  ? -28.973 0.035   -9.136  1.00 31.67  ? 45  VAL   B CG1 1 
ATOM   594  C CG2 . VAL   B 2 36  ? -31.411 -0.324  -8.596  1.00 32.61  ? 45  VAL   B CG2 1 
ATOM   595  N N   . PHE   B 2 37  ? -28.916 2.897   -10.797 1.00 30.61  ? 46  PHE   B N   1 
ATOM   596  C CA  . PHE   B 2 37  ? -27.748 3.467   -11.476 1.00 30.70  ? 46  PHE   B CA  1 
ATOM   597  C C   . PHE   B 2 37  ? -26.483 2.794   -10.956 1.00 30.13  ? 46  PHE   B C   1 
ATOM   598  O O   . PHE   B 2 37  ? -26.225 2.784   -9.762  1.00 29.31  ? 46  PHE   B O   1 
ATOM   599  C CB  . PHE   B 2 37  ? -27.699 4.980   -11.394 1.00 30.98  ? 46  PHE   B CB  1 
ATOM   600  C CG  . PHE   B 2 37  ? -26.696 5.570   -12.337 1.00 31.50  ? 46  PHE   B CG  1 
ATOM   601  C CD1 . PHE   B 2 37  ? -26.838 5.418   -13.718 1.00 32.07  ? 46  PHE   B CD1 1 
ATOM   602  C CD2 . PHE   B 2 37  ? -25.597 6.248   -11.848 1.00 31.72  ? 46  PHE   B CD2 1 
ATOM   603  C CE1 . PHE   B 2 37  ? -25.898 5.948   -14.589 1.00 32.45  ? 46  PHE   B CE1 1 
ATOM   604  C CE2 . PHE   B 2 37  ? -24.657 6.785   -12.715 1.00 32.28  ? 46  PHE   B CE2 1 
ATOM   605  C CZ  . PHE   B 2 37  ? -24.828 6.659   -14.090 1.00 32.62  ? 46  PHE   B CZ  1 
ATOM   606  N N   . HIS   B 2 38  ? -25.707 2.275   -11.904 1.00 29.26  ? 47  HIS   B N   1 
ATOM   607  C CA  . HIS   B 2 38  ? -24.469 1.467   -11.702 1.00 29.24  ? 47  HIS   B CA  1 
ATOM   608  C C   . HIS   B 2 38  ? -23.257 2.213   -12.254 1.00 29.62  ? 47  HIS   B C   1 
ATOM   609  O O   . HIS   B 2 38  ? -23.259 2.560   -13.481 1.00 29.56  ? 47  HIS   B O   1 
ATOM   610  C CB  . HIS   B 2 38  ? -24.562 0.109   -12.376 1.00 29.20  ? 47  HIS   B CB  1 
ATOM   611  C CG  . HIS   B 2 38  ? -25.756 -0.710  -12.060 1.00 29.27  ? 47  HIS   B CG  1 
ATOM   612  N ND1 . HIS   B 2 38  ? -26.999 -0.354  -12.499 1.00 29.41  ? 47  HIS   B ND1 1 
ATOM   613  C CD2 . HIS   B 2 38  ? -25.899 -1.803  -11.224 1.00 29.41  ? 47  HIS   B CD2 1 
ATOM   614  C CE1 . HIS   B 2 38  ? -27.876 -1.248  -12.054 1.00 29.75  ? 47  HIS   B CE1 1 
ATOM   615  N NE2 . HIS   B 2 38  ? -27.221 -2.147  -11.237 1.00 29.69  ? 47  HIS   B NE2 1 
ATOM   616  N N   . THR   B 2 39  ? -22.235 2.446   -11.443 1.00 29.86  ? 48  THR   B N   1 
ATOM   617  C CA  . THR   B 2 39  ? -20.973 3.062   -11.903 1.00 30.20  ? 48  THR   B CA  1 
ATOM   618  C C   . THR   B 2 39  ? -19.797 2.525   -11.087 1.00 30.90  ? 48  THR   B C   1 
ATOM   619  O O   . THR   B 2 39  ? -19.980 1.594   -10.204 1.00 30.23  ? 48  THR   B O   1 
ATOM   620  C CB  . THR   B 2 39  ? -21.114 4.586   -12.025 1.00 30.31  ? 48  THR   B CB  1 
ATOM   621  O OG1 . THR   B 2 39  ? -19.977 5.183   -12.672 1.00 30.37  ? 48  THR   B OG1 1 
ATOM   622  C CG2 . THR   B 2 39  ? -21.279 5.283   -10.692 1.00 30.46  ? 48  THR   B CG2 1 
ATOM   623  N N   . MET   B 2 40  ? -18.616 3.082   -11.359 1.00 31.80  ? 49  MET   B N   1 
ATOM   624  C CA  . MET   B 2 40  ? -17.390 2.713   -10.605 1.00 32.24  ? 49  MET   B CA  1 
ATOM   625  C C   . MET   B 2 40  ? -17.195 3.696   -9.444  1.00 31.76  ? 49  MET   B C   1 
ATOM   626  O O   . MET   B 2 40  ? -17.517 4.924   -9.520  1.00 31.03  ? 49  MET   B O   1 
ATOM   627  C CB  . MET   B 2 40  ? -16.142 2.614   -11.483 1.00 34.03  ? 49  MET   B CB  1 
ATOM   628  C CG  . MET   B 2 40  ? -16.394 1.880   -12.804 1.00 35.20  ? 49  MET   B CG  1 
ATOM   629  S SD  . MET   B 2 40  ? -14.936 1.054   -13.435 1.00 37.84  ? 49  MET   B SD  1 
ATOM   630  C CE  . MET   B 2 40  ? -14.886 -0.419  -12.393 1.00 38.08  ? 49  MET   B CE  1 
ATOM   631  N N   A TRP   B 2 41  ? -16.693 3.152   -8.322  0.25 31.67  ? 50  TRP   B N   1 
ATOM   632  N N   B TRP   B 2 41  ? -16.691 3.169   -8.317  0.25 31.42  ? 50  TRP   B N   1 
ATOM   633  N N   C TRP   B 2 41  ? -16.693 3.152   -8.322  0.25 31.67  ? 50  TRP   B N   1 
ATOM   634  N N   D TRP   B 2 41  ? -16.691 3.169   -8.317  0.25 31.42  ? 50  TRP   B N   1 
ATOM   635  C CA  A TRP   B 2 41  ? -16.527 3.946   -7.077  0.25 31.82  ? 50  TRP   B CA  1 
ATOM   636  C CA  B TRP   B 2 41  ? -16.554 3.975   -7.075  0.25 31.41  ? 50  TRP   B CA  1 
ATOM   637  C CA  C TRP   B 2 41  ? -16.527 3.946   -7.077  0.25 31.82  ? 50  TRP   B CA  1 
ATOM   638  C CA  D TRP   B 2 41  ? -16.554 3.975   -7.075  0.25 31.41  ? 50  TRP   B CA  1 
ATOM   639  C C   A TRP   B 2 41  ? -15.654 5.196   -7.347  0.25 32.03  ? 50  TRP   B C   1 
ATOM   640  C C   B TRP   B 2 41  ? -15.619 5.189   -7.307  0.25 31.78  ? 50  TRP   B C   1 
ATOM   641  C C   C TRP   B 2 41  ? -15.654 5.196   -7.347  0.25 32.03  ? 50  TRP   B C   1 
ATOM   642  C C   D TRP   B 2 41  ? -15.619 5.189   -7.307  0.25 31.78  ? 50  TRP   B C   1 
ATOM   643  O O   A TRP   B 2 41  ? -16.014 6.386   -6.694  0.25 32.32  ? 50  TRP   B O   1 
ATOM   644  O O   B TRP   B 2 41  ? -15.886 6.351   -6.627  0.25 32.05  ? 50  TRP   B O   1 
ATOM   645  O O   C TRP   B 2 41  ? -16.014 6.386   -6.694  0.25 32.32  ? 50  TRP   B O   1 
ATOM   646  O O   D TRP   B 2 41  ? -15.886 6.351   -6.627  0.25 32.05  ? 50  TRP   B O   1 
ATOM   647  C CB  A TRP   B 2 41  ? -15.934 3.099   -5.946  0.25 31.76  ? 50  TRP   B CB  1 
ATOM   648  C CB  B TRP   B 2 41  ? -16.047 3.111   -5.914  0.25 31.05  ? 50  TRP   B CB  1 
ATOM   649  C CB  C TRP   B 2 41  ? -15.934 3.099   -5.946  0.25 31.76  ? 50  TRP   B CB  1 
ATOM   650  C CB  D TRP   B 2 41  ? -16.047 3.111   -5.914  0.25 31.05  ? 50  TRP   B CB  1 
ATOM   651  C CG  A TRP   B 2 41  ? -16.098 3.827   -4.652  0.25 31.86  ? 50  TRP   B CG  1 
ATOM   652  C CG  B TRP   B 2 41  ? -15.892 3.927   -4.670  0.25 30.90  ? 50  TRP   B CG  1 
ATOM   653  C CG  C TRP   B 2 41  ? -16.098 3.827   -4.652  0.25 31.86  ? 50  TRP   B CG  1 
ATOM   654  C CG  D TRP   B 2 41  ? -15.892 3.927   -4.670  0.25 30.90  ? 50  TRP   B CG  1 
ATOM   655  C CD1 A TRP   B 2 41  ? -17.177 3.768   -3.824  0.25 31.78  ? 50  TRP   B CD1 1 
ATOM   656  C CD1 B TRP   B 2 41  ? -14.823 4.700   -4.321  0.25 30.89  ? 50  TRP   B CD1 1 
ATOM   657  C CD1 C TRP   B 2 41  ? -17.177 3.768   -3.824  0.25 31.78  ? 50  TRP   B CD1 1 
ATOM   658  C CD1 D TRP   B 2 41  ? -14.823 4.700   -4.321  0.25 30.89  ? 50  TRP   B CD1 1 
ATOM   659  C CD2 A TRP   B 2 41  ? -15.224 4.837   -4.114  0.25 32.11  ? 50  TRP   B CD2 1 
ATOM   660  C CD2 B TRP   B 2 41  ? -16.882 4.123   -3.649  0.25 30.78  ? 50  TRP   B CD2 1 
ATOM   661  C CD2 C TRP   B 2 41  ? -15.224 4.837   -4.114  0.25 32.11  ? 50  TRP   B CD2 1 
ATOM   662  C CD2 D TRP   B 2 41  ? -16.882 4.123   -3.649  0.25 30.78  ? 50  TRP   B CD2 1 
ATOM   663  N NE1 A TRP   B 2 41  ? -17.016 4.644   -2.783  0.25 31.94  ? 50  TRP   B NE1 1 
ATOM   664  N NE1 B TRP   B 2 41  ? -15.075 5.352   -3.145  0.25 30.74  ? 50  TRP   B NE1 1 
ATOM   665  N NE1 C TRP   B 2 41  ? -17.016 4.644   -2.783  0.25 31.94  ? 50  TRP   B NE1 1 
ATOM   666  N NE1 D TRP   B 2 41  ? -15.075 5.352   -3.145  0.25 30.74  ? 50  TRP   B NE1 1 
ATOM   667  C CE2 A TRP   B 2 41  ? -15.829 5.312   -2.935  0.25 32.00  ? 50  TRP   B CE2 1 
ATOM   668  C CE2 B TRP   B 2 41  ? -16.329 5.019   -2.708  0.25 30.71  ? 50  TRP   B CE2 1 
ATOM   669  C CE2 C TRP   B 2 41  ? -15.829 5.312   -2.935  0.25 32.00  ? 50  TRP   B CE2 1 
ATOM   670  C CE2 D TRP   B 2 41  ? -16.329 5.019   -2.708  0.25 30.71  ? 50  TRP   B CE2 1 
ATOM   671  C CE3 A TRP   B 2 41  ? -13.985 5.366   -4.495  0.25 32.36  ? 50  TRP   B CE3 1 
ATOM   672  C CE3 B TRP   B 2 41  ? -18.179 3.644   -3.439  0.25 30.80  ? 50  TRP   B CE3 1 
ATOM   673  C CE3 C TRP   B 2 41  ? -13.985 5.366   -4.495  0.25 32.36  ? 50  TRP   B CE3 1 
ATOM   674  C CE3 D TRP   B 2 41  ? -18.179 3.644   -3.439  0.25 30.80  ? 50  TRP   B CE3 1 
ATOM   675  C CZ2 A TRP   B 2 41  ? -15.231 6.285   -2.136  0.25 32.50  ? 50  TRP   B CZ2 1 
ATOM   676  C CZ2 B TRP   B 2 41  ? -17.012 5.408   -1.554  0.25 30.76  ? 50  TRP   B CZ2 1 
ATOM   677  C CZ2 C TRP   B 2 41  ? -15.231 6.285   -2.136  0.25 32.50  ? 50  TRP   B CZ2 1 
ATOM   678  C CZ2 D TRP   B 2 41  ? -17.012 5.408   -1.554  0.25 30.76  ? 50  TRP   B CZ2 1 
ATOM   679  C CZ3 A TRP   B 2 41  ? -13.396 6.330   -3.707  0.25 32.57  ? 50  TRP   B CZ3 1 
ATOM   680  C CZ3 B TRP   B 2 41  ? -18.850 4.024   -2.291  0.25 30.79  ? 50  TRP   B CZ3 1 
ATOM   681  C CZ3 C TRP   B 2 41  ? -13.396 6.330   -3.707  0.25 32.57  ? 50  TRP   B CZ3 1 
ATOM   682  C CZ3 D TRP   B 2 41  ? -18.850 4.024   -2.291  0.25 30.79  ? 50  TRP   B CZ3 1 
ATOM   683  C CH2 A TRP   B 2 41  ? -14.011 6.779   -2.539  0.25 32.64  ? 50  TRP   B CH2 1 
ATOM   684  C CH2 B TRP   B 2 41  ? -18.280 4.906   -1.372  0.25 30.76  ? 50  TRP   B CH2 1 
ATOM   685  C CH2 C TRP   B 2 41  ? -14.011 6.779   -2.539  0.25 32.64  ? 50  TRP   B CH2 1 
ATOM   686  C CH2 D TRP   B 2 41  ? -18.280 4.906   -1.372  0.25 30.76  ? 50  TRP   B CH2 1 
ATOM   687  N N   . HIS   B 2 42  ? -14.539 4.954   -8.148  1.00 32.15  ? 51  HIS   B N   1 
ATOM   688  C CA  . HIS   B 2 42  ? -13.548 6.057   -8.355  1.00 32.79  ? 51  HIS   B CA  1 
ATOM   689  C C   . HIS   B 2 42  ? -14.187 7.221   -9.172  1.00 33.30  ? 51  HIS   B C   1 
ATOM   690  O O   . HIS   B 2 42  ? -13.658 8.308   -9.120  1.00 33.84  ? 51  HIS   B O   1 
ATOM   691  C CB  . HIS   B 2 42  ? -12.217 5.555   -8.903  1.00 33.69  ? 51  HIS   B CB  1 
ATOM   692  C CG  . HIS   B 2 42  ? -12.264 5.259   -10.358 1.00 33.81  ? 51  HIS   B CG  1 
ATOM   693  N ND1 . HIS   B 2 42  ? -12.510 3.983   -10.854 1.00 34.16  ? 51  HIS   B ND1 1 
ATOM   694  C CD2 . HIS   B 2 42  ? -12.110 6.063   -11.447 1.00 35.20  ? 51  HIS   B CD2 1 
ATOM   695  C CE1 . HIS   B 2 42  ? -12.475 4.022   -12.192 1.00 34.52  ? 51  HIS   B CE1 1 
ATOM   696  N NE2 . HIS   B 2 42  ? -12.264 5.289   -12.562 1.00 34.41  ? 51  HIS   B NE2 1 
ATOM   697  N N   . VAL   B 2 43  ? -15.340 7.048   -9.810  1.00 33.59  ? 52  VAL   B N   1 
ATOM   698  C CA  . VAL   B 2 43  ? -16.009 8.137   -10.586 1.00 33.72  ? 52  VAL   B CA  1 
ATOM   699  C C   . VAL   B 2 43  ? -16.691 9.106   -9.612  1.00 34.70  ? 52  VAL   B C   1 
ATOM   700  O O   . VAL   B 2 43  ? -16.496 10.329  -9.779  1.00 35.14  ? 52  VAL   B O   1 
ATOM   701  C CB  . VAL   B 2 43  ? -16.986 7.525   -11.599 1.00 34.16  ? 52  VAL   B CB  1 
ATOM   702  C CG1 . VAL   B 2 43  ? -17.948 8.519   -12.226 1.00 34.24  ? 52  VAL   B CG1 1 
ATOM   703  C CG2 . VAL   B 2 43  ? -16.212 6.805   -12.691 1.00 34.18  ? 52  VAL   B CG2 1 
ATOM   704  N N   . THR   B 2 44  ? -17.511 8.590   -8.681  1.00 32.90  ? 53  THR   B N   1 
ATOM   705  C CA  . THR   B 2 44  ? -18.399 9.427   -7.814  1.00 33.86  ? 53  THR   B CA  1 
ATOM   706  C C   . THR   B 2 44  ? -17.796 9.577   -6.417  1.00 34.51  ? 53  THR   B C   1 
ATOM   707  O O   . THR   B 2 44  ? -18.127 10.597  -5.747  1.00 35.03  ? 53  THR   B O   1 
ATOM   708  C CB  . THR   B 2 44  ? -19.820 8.871   -7.714  1.00 32.93  ? 53  THR   B CB  1 
ATOM   709  O OG1 . THR   B 2 44  ? -19.744 7.623   -7.019  1.00 31.97  ? 53  THR   B OG1 1 
ATOM   710  C CG2 . THR   B 2 44  ? -20.445 8.703   -9.092  1.00 32.93  ? 53  THR   B CG2 1 
ATOM   711  N N   . LYS   B 2 45  ? -16.902 8.674   -6.042  1.00 36.16  ? 54  LYS   B N   1 
ATOM   712  C CA  . LYS   B 2 45  ? -16.404 8.498   -4.639  1.00 39.43  ? 54  LYS   B CA  1 
ATOM   713  C C   . LYS   B 2 45  ? -17.598 8.355   -3.675  1.00 39.39  ? 54  LYS   B C   1 
ATOM   714  O O   . LYS   B 2 45  ? -17.485 8.779   -2.483  1.00 39.89  ? 54  LYS   B O   1 
ATOM   715  C CB  . LYS   B 2 45  ? -15.538 9.681   -4.192  1.00 43.21  ? 54  LYS   B CB  1 
ATOM   716  C CG  . LYS   B 2 45  ? -14.515 10.194  -5.190  1.00 47.77  ? 54  LYS   B CG  1 
ATOM   717  C CD  . LYS   B 2 45  ? -13.252 9.384   -5.272  1.00 51.05  ? 54  LYS   B CD  1 
ATOM   718  C CE  . LYS   B 2 45  ? -12.169 10.145  -6.013  1.00 54.31  ? 54  LYS   B CE  1 
ATOM   719  N NZ  . LYS   B 2 45  ? -11.579 9.326   -7.100  1.00 57.01  ? 54  LYS   B NZ  1 
ATOM   720  N N   . GLY   B 2 46  ? -18.721 7.809   -4.124  1.00 38.38  ? 55  GLY   B N   1 
ATOM   721  C CA  . GLY   B 2 46  ? -19.905 7.569   -3.283  1.00 38.42  ? 55  GLY   B CA  1 
ATOM   722  C C   . GLY   B 2 46  ? -20.768 8.811   -3.082  1.00 38.89  ? 55  GLY   B C   1 
ATOM   723  O O   . GLY   B 2 46  ? -21.690 8.722   -2.301  1.00 38.53  ? 55  GLY   B O   1 
ATOM   724  N N   . ALA   B 2 47  ? -20.539 9.923   -3.795  1.00 40.41  ? 56  ALA   B N   1 
ATOM   725  C CA  . ALA   B 2 47  ? -21.359 11.160  -3.674  1.00 39.89  ? 56  ALA   B CA  1 
ATOM   726  C C   . ALA   B 2 47  ? -22.743 10.948  -4.285  1.00 39.01  ? 56  ALA   B C   1 
ATOM   727  O O   . ALA   B 2 47  ? -22.905 10.106  -5.152  1.00 37.74  ? 56  ALA   B O   1 
ATOM   728  C CB  . ALA   B 2 47  ? -20.664 12.353  -4.307  1.00 40.22  ? 56  ALA   B CB  1 
ATOM   729  N N   . ALA   B 2 48  ? -23.721 11.726  -3.847  1.00 38.42  ? 57  ALA   B N   1 
ATOM   730  C CA  . ALA   B 2 48  ? -25.058 11.773  -4.467  1.00 38.47  ? 57  ALA   B CA  1 
ATOM   731  C C   . ALA   B 2 48  ? -24.957 12.372  -5.870  1.00 38.22  ? 57  ALA   B C   1 
ATOM   732  O O   . ALA   B 2 48  ? -23.973 13.071  -6.161  1.00 38.56  ? 57  ALA   B O   1 
ATOM   733  C CB  . ALA   B 2 48  ? -26.019 12.572  -3.620  1.00 39.74  ? 57  ALA   B CB  1 
ATOM   734  N N   . LEU   B 2 49  ? -25.950 12.060  -6.692  1.00 38.07  ? 58  LEU   B N   1 
ATOM   735  C CA  . LEU   B 2 49  ? -26.056 12.477  -8.115  1.00 39.24  ? 58  LEU   B CA  1 
ATOM   736  C C   . LEU   B 2 49  ? -27.400 13.158  -8.325  1.00 41.06  ? 58  LEU   B C   1 
ATOM   737  O O   . LEU   B 2 49  ? -28.395 12.828  -7.621  1.00 42.96  ? 58  LEU   B O   1 
ATOM   738  C CB  . LEU   B 2 49  ? -25.954 11.283  -9.070  1.00 37.25  ? 58  LEU   B CB  1 
ATOM   739  C CG  . LEU   B 2 49  ? -24.719 10.411  -8.904  1.00 36.88  ? 58  LEU   B CG  1 
ATOM   740  C CD1 . LEU   B 2 49  ? -24.823 9.119   -9.689  1.00 36.45  ? 58  LEU   B CD1 1 
ATOM   741  C CD2 . LEU   B 2 49  ? -23.454 11.165  -9.255  1.00 37.59  ? 58  LEU   B CD2 1 
ATOM   742  N N   . ARG   B 2 50  ? -27.411 14.095  -9.251  1.00 42.12  ? 59  ARG   B N   1 
ATOM   743  C CA  . ARG   B 2 50  ? -28.636 14.753  -9.714  1.00 44.81  ? 59  ARG   B CA  1 
ATOM   744  C C   . ARG   B 2 50  ? -29.010 14.125  -11.065 1.00 45.73  ? 59  ARG   B C   1 
ATOM   745  O O   . ARG   B 2 50  ? -28.099 13.849  -11.876 1.00 43.25  ? 59  ARG   B O   1 
ATOM   746  C CB  . ARG   B 2 50  ? -28.324 16.245  -9.735  1.00 47.79  ? 59  ARG   B CB  1 
ATOM   747  C CG  . ARG   B 2 50  ? -29.457 17.102  -10.266 1.00 52.26  ? 59  ARG   B CG  1 
ATOM   748  C CD  . ARG   B 2 50  ? -29.175 18.567  -10.011 1.00 55.49  ? 59  ARG   B CD  1 
ATOM   749  N NE  . ARG   B 2 50  ? -27.778 18.907  -10.291 1.00 57.10  ? 59  ARG   B NE  1 
ATOM   750  C CZ  . ARG   B 2 50  ? -27.316 19.370  -11.448 1.00 59.29  ? 59  ARG   B CZ  1 
ATOM   751  N NH1 . ARG   B 2 50  ? -28.110 19.490  -12.502 1.00 59.35  ? 59  ARG   B NH1 1 
ATOM   752  N NH2 . ARG   B 2 50  ? -26.033 19.676  -11.559 1.00 63.28  ? 59  ARG   B NH2 1 
ATOM   753  N N   . SER   B 2 51  ? -30.289 13.832  -11.259 1.00 47.09  ? 60  SER   B N   1 
ATOM   754  C CA  . SER   B 2 51  ? -30.914 13.542  -12.574 1.00 50.24  ? 60  SER   B CA  1 
ATOM   755  C C   . SER   B 2 51  ? -32.076 14.527  -12.800 1.00 53.21  ? 60  SER   B C   1 
ATOM   756  O O   . SER   B 2 51  ? -33.157 14.321  -12.195 1.00 54.12  ? 60  SER   B O   1 
ATOM   757  C CB  . SER   B 2 51  ? -31.384 12.119  -12.604 1.00 49.68  ? 60  SER   B CB  1 
ATOM   758  O OG  . SER   B 2 51  ? -31.982 11.816  -13.845 1.00 50.13  ? 60  SER   B OG  1 
ATOM   759  N N   . GLY   B 2 52  ? -31.869 15.582  -13.595 1.00 55.86  ? 61  GLY   B N   1 
ATOM   760  C CA  . GLY   B 2 52  ? -32.829 16.701  -13.690 1.00 58.17  ? 61  GLY   B CA  1 
ATOM   761  C C   . GLY   B 2 52  ? -32.974 17.385  -12.340 1.00 59.86  ? 61  GLY   B C   1 
ATOM   762  O O   . GLY   B 2 52  ? -31.962 17.855  -11.809 1.00 63.08  ? 61  GLY   B O   1 
ATOM   763  N N   . GLU   B 2 53  ? -34.170 17.406  -11.762 1.00 61.95  ? 62  GLU   B N   1 
ATOM   764  C CA  . GLU   B 2 53  ? -34.368 17.949  -10.395 1.00 64.49  ? 62  GLU   B CA  1 
ATOM   765  C C   . GLU   B 2 53  ? -34.424 16.813  -9.366  1.00 61.59  ? 62  GLU   B C   1 
ATOM   766  O O   . GLU   B 2 53  ? -34.489 17.135  -8.167  1.00 61.82  ? 62  GLU   B O   1 
ATOM   767  C CB  . GLU   B 2 53  ? -35.586 18.863  -10.371 1.00 69.30  ? 62  GLU   B CB  1 
ATOM   768  C CG  . GLU   B 2 53  ? -35.198 20.322  -10.492 1.00 75.32  ? 62  GLU   B CG  1 
ATOM   769  C CD  . GLU   B 2 53  ? -36.370 21.275  -10.351 1.00 83.33  ? 62  GLU   B CD  1 
ATOM   770  O OE1 . GLU   B 2 53  ? -37.434 20.986  -10.965 1.00 90.76  ? 62  GLU   B OE1 1 
ATOM   771  O OE2 . GLU   B 2 53  ? -36.230 22.293  -9.612  1.00 86.24  ? 62  GLU   B OE2 1 
ATOM   772  N N   . GLY   B 2 54  ? -34.304 15.557  -9.811  1.00 57.99  ? 63  GLY   B N   1 
ATOM   773  C CA  . GLY   B 2 54  ? -34.280 14.351  -8.961  1.00 56.77  ? 63  GLY   B CA  1 
ATOM   774  C C   . GLY   B 2 54  ? -32.915 14.124  -8.329  1.00 55.30  ? 63  GLY   B C   1 
ATOM   775  O O   . GLY   B 2 54  ? -31.902 14.552  -8.915  1.00 54.63  ? 63  GLY   B O   1 
ATOM   776  N N   . ARG   B 2 55  ? -32.882 13.502  -7.147  1.00 52.47  ? 64  ARG   B N   1 
ATOM   777  C CA  . ARG   B 2 55  ? -31.623 13.119  -6.463  1.00 49.77  ? 64  ARG   B CA  1 
ATOM   778  C C   . ARG   B 2 55  ? -31.444 11.595  -6.546  1.00 46.98  ? 64  ARG   B C   1 
ATOM   779  O O   . ARG   B 2 55  ? -32.425 10.865  -6.441  1.00 50.28  ? 64  ARG   B O   1 
ATOM   780  C CB  . ARG   B 2 55  ? -31.638 13.644  -5.024  1.00 51.51  ? 64  ARG   B CB  1 
ATOM   781  C CG  . ARG   B 2 55  ? -30.266 13.617  -4.377  1.00 52.33  ? 64  ARG   B CG  1 
ATOM   782  C CD  . ARG   B 2 55  ? -30.308 14.317  -3.032  1.00 54.55  ? 64  ARG   B CD  1 
ATOM   783  N NE  . ARG   B 2 55  ? -29.259 13.827  -2.159  1.00 55.12  ? 64  ARG   B NE  1 
ATOM   784  C CZ  . ARG   B 2 55  ? -28.524 14.579  -1.341  1.00 56.23  ? 64  ARG   B CZ  1 
ATOM   785  N NH1 . ARG   B 2 55  ? -28.738 15.881  -1.259  1.00 56.75  ? 64  ARG   B NH1 1 
ATOM   786  N NH2 . ARG   B 2 55  ? -27.577 14.020  -0.603  1.00 55.63  ? 64  ARG   B NH2 1 
ATOM   787  N N   . LEU   B 2 56  ? -30.231 11.114  -6.762  1.00 41.57  ? 65  LEU   B N   1 
ATOM   788  C CA  . LEU   B 2 56  ? -29.947 9.668   -6.700  1.00 40.42  ? 65  LEU   B CA  1 
ATOM   789  C C   . LEU   B 2 56  ? -29.056 9.467   -5.484  1.00 37.74  ? 65  LEU   B C   1 
ATOM   790  O O   . LEU   B 2 56  ? -27.993 10.091  -5.458  1.00 36.26  ? 65  LEU   B O   1 
ATOM   791  C CB  . LEU   B 2 56  ? -29.219 9.195   -7.978  1.00 40.47  ? 65  LEU   B CB  1 
ATOM   792  C CG  . LEU   B 2 56  ? -29.890 9.389   -9.334  1.00 41.82  ? 65  LEU   B CG  1 
ATOM   793  C CD1 . LEU   B 2 56  ? -29.185 8.515   -10.369 1.00 42.06  ? 65  LEU   B CD1 1 
ATOM   794  C CD2 . LEU   B 2 56  ? -31.363 9.040   -9.330  1.00 42.89  ? 65  LEU   B CD2 1 
ATOM   795  N N   . ASP   B 2 57  ? -29.488 8.692   -4.486  1.00 37.27  ? 66  ASP   B N   1 
ATOM   796  C CA  . ASP   B 2 57  ? -28.622 8.416   -3.316  1.00 36.18  ? 66  ASP   B CA  1 
ATOM   797  C C   . ASP   B 2 57  ? -27.902 7.086   -3.486  1.00 33.86  ? 66  ASP   B C   1 
ATOM   798  O O   . ASP   B 2 57  ? -28.494 6.081   -3.959  1.00 33.76  ? 66  ASP   B O   1 
ATOM   799  C CB  . ASP   B 2 57  ? -29.442 8.476   -2.022  1.00 38.95  ? 66  ASP   B CB  1 
ATOM   800  C CG  . ASP   B 2 57  ? -29.982 9.889   -1.835  1.00 41.90  ? 66  ASP   B CG  1 
ATOM   801  O OD1 . ASP   B 2 57  ? -29.222 10.846  -2.125  1.00 44.18  ? 66  ASP   B OD1 1 
ATOM   802  O OD2 . ASP   B 2 57  ? -31.157 10.028  -1.494  1.00 45.53  ? 66  ASP   B OD2 1 
ATOM   803  N N   . PRO   B 2 58  ? -26.634 7.006   -3.036  1.00 32.10  ? 67  PRO   B N   1 
ATOM   804  C CA  . PRO   B 2 58  ? -25.905 5.742   -2.997  1.00 31.33  ? 67  PRO   B CA  1 
ATOM   805  C C   . PRO   B 2 58  ? -26.687 4.724   -2.155  1.00 31.17  ? 67  PRO   B C   1 
ATOM   806  O O   . PRO   B 2 58  ? -27.324 5.128   -1.139  1.00 30.65  ? 67  PRO   B O   1 
ATOM   807  C CB  . PRO   B 2 58  ? -24.542 6.153   -2.433  1.00 31.41  ? 67  PRO   B CB  1 
ATOM   808  C CG  . PRO   B 2 58  ? -24.840 7.374   -1.593  1.00 32.14  ? 67  PRO   B CG  1 
ATOM   809  C CD  . PRO   B 2 58  ? -25.859 8.112   -2.435  1.00 32.86  ? 67  PRO   B CD  1 
ATOM   810  N N   . TYR   B 2 59  ? -26.674 3.472   -2.571  1.00 30.17  ? 68  TYR   B N   1 
ATOM   811  C CA  . TYR   B 2 59  ? -27.348 2.353   -1.897  1.00 30.25  ? 68  TYR   B CA  1 
ATOM   812  C C   . TYR   B 2 59  ? -26.323 1.316   -1.439  1.00 29.54  ? 68  TYR   B C   1 
ATOM   813  O O   . TYR   B 2 59  ? -26.478 0.748   -0.312  1.00 29.27  ? 68  TYR   B O   1 
ATOM   814  C CB  . TYR   B 2 59  ? -28.403 1.732   -2.808  1.00 31.12  ? 68  TYR   B CB  1 
ATOM   815  C CG  . TYR   B 2 59  ? -29.227 0.651   -2.150  1.00 31.65  ? 68  TYR   B CG  1 
ATOM   816  C CD1 . TYR   B 2 59  ? -28.704 -0.632  -2.080  1.00 32.04  ? 68  TYR   B CD1 1 
ATOM   817  C CD2 . TYR   B 2 59  ? -30.578 0.898   -1.678  1.00 32.46  ? 68  TYR   B CD2 1 
ATOM   818  C CE1 . TYR   B 2 59  ? -29.471 -1.659  -1.536  1.00 32.76  ? 68  TYR   B CE1 1 
ATOM   819  C CE2 . TYR   B 2 59  ? -31.373 -0.119  -1.135  1.00 33.49  ? 68  TYR   B CE2 1 
ATOM   820  C CZ  . TYR   B 2 59  ? -30.841 -1.401  -1.042  1.00 33.55  ? 68  TYR   B CZ  1 
ATOM   821  O OH  . TYR   B 2 59  ? -31.549 -2.444  -0.529  1.00 35.84  ? 68  TYR   B OH  1 
ATOM   822  N N   . TRP   B 2 60  ? -25.402 0.957   -2.303  1.00 28.79  ? 69  TRP   B N   1 
ATOM   823  C CA  . TRP   B 2 60  ? -24.341 -0.059  -2.066  1.00 28.49  ? 69  TRP   B CA  1 
ATOM   824  C C   . TRP   B 2 60  ? -23.032 0.400   -2.699  1.00 28.71  ? 69  TRP   B C   1 
ATOM   825  O O   . TRP   B 2 60  ? -23.060 0.941   -3.856  1.00 27.98  ? 69  TRP   B O   1 
ATOM   826  C CB  . TRP   B 2 60  ? -24.760 -1.450  -2.523  1.00 28.24  ? 69  TRP   B CB  1 
ATOM   827  C CG  . TRP   B 2 60  ? -23.633 -2.431  -2.510  1.00 28.07  ? 69  TRP   B CG  1 
ATOM   828  C CD1 . TRP   B 2 60  ? -23.183 -3.192  -1.458  1.00 28.00  ? 69  TRP   B CD1 1 
ATOM   829  C CD2 . TRP   B 2 60  ? -22.745 -2.708  -3.606  1.00 27.57  ? 69  TRP   B CD2 1 
ATOM   830  N NE1 . TRP   B 2 60  ? -22.087 -3.926  -1.836  1.00 27.81  ? 69  TRP   B NE1 1 
ATOM   831  C CE2 . TRP   B 2 60  ? -21.805 -3.656  -3.162  1.00 27.75  ? 69  TRP   B CE2 1 
ATOM   832  C CE3 . TRP   B 2 60  ? -22.671 -2.261  -4.938  1.00 27.75  ? 69  TRP   B CE3 1 
ATOM   833  C CZ2 . TRP   B 2 60  ? -20.774 -4.135  -3.958  1.00 27.60  ? 69  TRP   B CZ2 1 
ATOM   834  C CZ3 . TRP   B 2 60  ? -21.649 -2.738  -5.734  1.00 27.52  ? 69  TRP   B CZ3 1 
ATOM   835  C CH2 . TRP   B 2 60  ? -20.740 -3.695  -5.277  1.00 27.78  ? 69  TRP   B CH2 1 
ATOM   836  N N   . GLY   B 2 61  ? -21.908 0.155   -2.037  1.00 28.88  ? 70  GLY   B N   1 
ATOM   837  C CA  . GLY   B 2 61  ? -20.591 0.425   -2.643  1.00 29.19  ? 70  GLY   B CA  1 
ATOM   838  C C   . GLY   B 2 61  ? -19.501 -0.365  -1.999  1.00 29.89  ? 70  GLY   B C   1 
ATOM   839  O O   . GLY   B 2 61  ? -19.713 -0.804  -0.796  1.00 29.69  ? 70  GLY   B O   1 
ATOM   840  N N   . ASP   B 2 62  ? -18.390 -0.488  -2.693  1.00 30.32  ? 71  ASP   B N   1 
ATOM   841  C CA  . ASP   B 2 62  ? -17.198 -1.249  -2.230  1.00 31.22  ? 71  ASP   B CA  1 
ATOM   842  C C   . ASP   B 2 62  ? -15.986 -0.704  -2.970  1.00 30.93  ? 71  ASP   B C   1 
ATOM   843  O O   . ASP   B 2 62  ? -15.902 -0.958  -4.202  1.00 30.75  ? 71  ASP   B O   1 
ATOM   844  C CB  . ASP   B 2 62  ? -17.418 -2.740  -2.407  1.00 32.41  ? 71  ASP   B CB  1 
ATOM   845  C CG  . ASP   B 2 62  ? -16.337 -3.601  -1.786  1.00 34.87  ? 71  ASP   B CG  1 
ATOM   846  O OD1 . ASP   B 2 62  ? -15.195 -3.577  -2.225  1.00 36.60  ? 71  ASP   B OD1 1 
ATOM   847  O OD2 . ASP   B 2 62  ? -16.646 -4.205  -0.775  1.00 39.49  ? 71  ASP   B OD2 1 
ATOM   848  N N   . VAL   B 2 63  ? -15.084 -0.036  -2.242  1.00 30.16  ? 72  VAL   B N   1 
ATOM   849  C CA  . VAL   B 2 63  ? -13.835 0.549   -2.785  1.00 30.05  ? 72  VAL   B CA  1 
ATOM   850  C C   . VAL   B 2 63  ? -12.967 -0.570  -3.362  1.00 30.80  ? 72  VAL   B C   1 
ATOM   851  O O   . VAL   B 2 63  ? -12.358 -0.327  -4.474  1.00 29.56  ? 72  VAL   B O   1 
ATOM   852  C CB  . VAL   B 2 63  ? -13.071 1.414   -1.770  1.00 30.15  ? 72  VAL   B CB  1 
ATOM   853  C CG1 . VAL   B 2 63  ? -11.645 1.634   -2.196  1.00 30.83  ? 72  VAL   B CG1 1 
ATOM   854  C CG2 . VAL   B 2 63  ? -13.752 2.739   -1.533  1.00 29.79  ? 72  VAL   B CG2 1 
ATOM   855  N N   . LYS   B 2 64  ? -13.019 -1.793  -2.857  1.00 31.07  ? 73  LYS   B N   1 
ATOM   856  C CA  . LYS   B 2 64  ? -12.066 -2.817  -3.379  1.00 32.76  ? 73  LYS   B CA  1 
ATOM   857  C C   . LYS   B 2 64  ? -12.549 -3.352  -4.748  1.00 32.31  ? 73  LYS   B C   1 
ATOM   858  O O   . LYS   B 2 64  ? -11.726 -3.521  -5.712  1.00 33.80  ? 73  LYS   B O   1 
ATOM   859  C CB  . LYS   B 2 64  ? -11.862 -3.986  -2.427  1.00 33.05  ? 73  LYS   B CB  1 
ATOM   860  C CG  . LYS   B 2 64  ? -10.774 -4.909  -2.937  1.00 34.39  ? 73  LYS   B CG  1 
ATOM   861  C CD  . LYS   B 2 64  ? -10.349 -5.909  -1.947  1.00 34.85  ? 73  LYS   B CD  1 
ATOM   862  C CE  . LYS   B 2 64  ? -9.335  -6.878  -2.509  1.00 35.86  ? 73  LYS   B CE  1 
ATOM   863  N NZ  . LYS   B 2 64  ? -9.051  -7.916  -1.497  1.00 36.53  ? 73  LYS   B NZ  1 
ATOM   864  N N   . GLN   B 2 65  ? -13.847 -3.612  -4.856  1.00 32.52  ? 74  GLN   B N   1 
ATOM   865  C CA  . GLN   B 2 65  ? -14.485 -3.981  -6.147  1.00 32.84  ? 74  GLN   B CA  1 
ATOM   866  C C   . GLN   B 2 65  ? -14.506 -2.775  -7.092  1.00 32.10  ? 74  GLN   B C   1 
ATOM   867  O O   . GLN   B 2 65  ? -14.650 -3.047  -8.359  1.00 31.29  ? 74  GLN   B O   1 
ATOM   868  C CB  . GLN   B 2 65  ? -15.918 -4.465  -5.954  1.00 34.38  ? 74  GLN   B CB  1 
ATOM   869  C CG  . GLN   B 2 65  ? -16.008 -5.771  -5.166  1.00 36.74  ? 74  GLN   B CG  1 
ATOM   870  C CD  . GLN   B 2 65  ? -17.436 -6.258  -5.050  1.00 38.95  ? 74  GLN   B CD  1 
ATOM   871  O OE1 . GLN   B 2 65  ? -18.200 -6.348  -6.039  1.00 40.47  ? 74  GLN   B OE1 1 
ATOM   872  N NE2 . GLN   B 2 65  ? -17.835 -6.532  -3.822  1.00 40.72  ? 74  GLN   B NE2 1 
ATOM   873  N N   . ASP   B 2 66  ? -14.333 -1.553  -6.566  1.00 30.71  ? 75  ASP   B N   1 
ATOM   874  C CA  . ASP   B 2 66  ? -14.458 -0.239  -7.271  1.00 30.76  ? 75  ASP   B CA  1 
ATOM   875  C C   . ASP   B 2 66  ? -15.810 -0.112  -7.963  1.00 29.96  ? 75  ASP   B C   1 
ATOM   876  O O   . ASP   B 2 66  ? -15.808 0.365   -9.144  1.00 29.67  ? 75  ASP   B O   1 
ATOM   877  C CB  . ASP   B 2 66  ? -13.342 -0.037  -8.304  1.00 31.33  ? 75  ASP   B CB  1 
ATOM   878  C CG  . ASP   B 2 66  ? -13.196 1.380   -8.829  1.00 31.83  ? 75  ASP   B CG  1 
ATOM   879  O OD1 . ASP   B 2 66  ? -13.476 2.347   -8.092  1.00 31.26  ? 75  ASP   B OD1 1 
ATOM   880  O OD2 . ASP   B 2 66  ? -12.706 1.501   -10.005 1.00 32.23  ? 75  ASP   B OD2 1 
ATOM   881  N N   . LEU   B 2 67  ? -16.923 -0.467  -7.317  1.00 28.93  ? 76  LEU   B N   1 
ATOM   882  C CA  . LEU   B 2 67  ? -18.334 -0.417  -7.805  1.00 28.58  ? 76  LEU   B CA  1 
ATOM   883  C C   . LEU   B 2 67  ? -19.232 0.327   -6.816  1.00 29.16  ? 76  LEU   B C   1 
ATOM   884  O O   . LEU   B 2 67  ? -18.942 0.247   -5.559  1.00 28.38  ? 76  LEU   B O   1 
ATOM   885  C CB  . LEU   B 2 67  ? -18.857 -1.838  -8.022  1.00 28.54  ? 76  LEU   B CB  1 
ATOM   886  C CG  . LEU   B 2 67  ? -18.228 -2.638  -9.174  1.00 28.71  ? 76  LEU   B CG  1 
ATOM   887  C CD1 . LEU   B 2 67  ? -18.872 -4.011  -9.280  1.00 28.78  ? 76  LEU   B CD1 1 
ATOM   888  C CD2 . LEU   B 2 67  ? -18.421 -1.859  -10.514 1.00 28.70  ? 76  LEU   B CD2 1 
ATOM   889  N N   . VAL   B 2 68  ? -20.323 0.913   -7.319  1.00 29.04  ? 77  VAL   B N   1 
ATOM   890  C CA  . VAL   B 2 68  ? -21.344 1.607   -6.487  1.00 28.85  ? 77  VAL   B CA  1 
ATOM   891  C C   . VAL   B 2 68  ? -22.676 1.552   -7.237  1.00 29.09  ? 77  VAL   B C   1 
ATOM   892  O O   . VAL   B 2 68  ? -22.683 1.644   -8.514  1.00 28.60  ? 77  VAL   B O   1 
ATOM   893  C CB  . VAL   B 2 68  ? -20.900 3.040   -6.125  1.00 28.77  ? 77  VAL   B CB  1 
ATOM   894  C CG1 . VAL   B 2 68  ? -20.581 3.884   -7.361  1.00 28.94  ? 77  VAL   B CG1 1 
ATOM   895  C CG2 . VAL   B 2 68  ? -21.948 3.782   -5.310  1.00 28.87  ? 77  VAL   B CG2 1 
ATOM   896  N N   . SER   B 2 69  ? -23.778 1.363   -6.528  1.00 28.45  ? 78  SER   B N   1 
ATOM   897  C CA  . SER   B 2 69  ? -25.158 1.386   -7.071  1.00 28.61  ? 78  SER   B CA  1 
ATOM   898  C C   . SER   B 2 69  ? -25.937 2.512   -6.396  1.00 29.20  ? 78  SER   B C   1 
ATOM   899  O O   . SER   B 2 69  ? -25.669 2.822   -5.157  1.00 28.48  ? 78  SER   B O   1 
ATOM   900  C CB  . SER   B 2 69  ? -25.831 0.016   -6.958  1.00 28.89  ? 78  SER   B CB  1 
ATOM   901  O OG  . SER   B 2 69  ? -26.112 -0.380  -5.600  1.00 29.34  ? 78  SER   B OG  1 
ATOM   902  N N   . TYR   B 2 70  ? -26.897 3.082   -7.106  1.00 29.31  ? 79  TYR   B N   1 
ATOM   903  C CA  . TYR   B 2 70  ? -27.742 4.213   -6.646  1.00 30.01  ? 79  TYR   B CA  1 
ATOM   904  C C   . TYR   B 2 70  ? -29.193 3.754   -6.737  1.00 31.10  ? 79  TYR   B C   1 
ATOM   905  O O   . TYR   B 2 70  ? -29.554 3.086   -7.736  1.00 30.80  ? 79  TYR   B O   1 
ATOM   906  C CB  . TYR   B 2 70  ? -27.477 5.483   -7.473  1.00 30.01  ? 79  TYR   B CB  1 
ATOM   907  C CG  . TYR   B 2 70  ? -26.145 6.125   -7.189  1.00 29.65  ? 79  TYR   B CG  1 
ATOM   908  C CD1 . TYR   B 2 70  ? -24.980 5.633   -7.749  1.00 29.65  ? 79  TYR   B CD1 1 
ATOM   909  C CD2 . TYR   B 2 70  ? -26.031 7.198   -6.326  1.00 29.97  ? 79  TYR   B CD2 1 
ATOM   910  C CE1 . TYR   B 2 70  ? -23.741 6.199   -7.486  1.00 29.53  ? 79  TYR   B CE1 1 
ATOM   911  C CE2 . TYR   B 2 70  ? -24.809 7.794   -6.055  1.00 29.97  ? 79  TYR   B CE2 1 
ATOM   912  C CZ  . TYR   B 2 70  ? -23.661 7.282   -6.633  1.00 29.78  ? 79  TYR   B CZ  1 
ATOM   913  O OH  . TYR   B 2 70  ? -22.458 7.847   -6.347  1.00 30.24  ? 79  TYR   B OH  1 
ATOM   914  N N   . CYS   B 2 71  ? -30.008 4.075   -5.705  1.00 31.76  ? 80  CYS   B N   1 
ATOM   915  C CA  . CYS   B 2 71  ? -31.475 3.899   -5.694  1.00 33.66  ? 80  CYS   B CA  1 
ATOM   916  C C   . CYS   B 2 71  ? -31.815 2.407   -5.406  1.00 34.65  ? 80  CYS   B C   1 
ATOM   917  O O   . CYS   B 2 71  ? -32.968 2.161   -5.093  1.00 36.95  ? 80  CYS   B O   1 
ATOM   918  C CB  . CYS   B 2 71  ? -32.152 4.299   -7.008  1.00 35.40  ? 80  CYS   B CB  1 
ATOM   919  S SG  . CYS   B 2 71  ? -31.665 5.985   -7.440  1.00 38.84  ? 80  CYS   B SG  1 
ATOM   920  N N   . GLY   B 2 72  ? -30.844 1.482   -5.270  1.00 34.78  ? 81  GLY   B N   1 
ATOM   921  C CA  . GLY   B 2 72  ? -31.206 0.067   -5.118  1.00 34.61  ? 81  GLY   B CA  1 
ATOM   922  C C   . GLY   B 2 72  ? -29.947 -0.762  -5.092  1.00 33.92  ? 81  GLY   B C   1 
ATOM   923  O O   . GLY   B 2 72  ? -28.844 -0.245  -5.258  1.00 33.86  ? 81  GLY   B O   1 
ATOM   924  N N   . PRO   B 2 73  ? -30.100 -2.042  -4.901  1.00 34.17  ? 82  PRO   B N   1 
ATOM   925  C CA  . PRO   B 2 73  ? -28.975 -3.030  -4.985  1.00 33.98  ? 82  PRO   B CA  1 
ATOM   926  C C   . PRO   B 2 73  ? -28.473 -3.253  -6.429  1.00 33.59  ? 82  PRO   B C   1 
ATOM   927  O O   . PRO   B 2 73  ? -29.288 -3.068  -7.327  1.00 33.75  ? 82  PRO   B O   1 
ATOM   928  C CB  . PRO   B 2 73  ? -29.609 -4.296  -4.370  1.00 34.55  ? 82  PRO   B CB  1 
ATOM   929  C CG  . PRO   B 2 73  ? -31.069 -4.195  -4.747  1.00 34.84  ? 82  PRO   B CG  1 
ATOM   930  C CD  . PRO   B 2 73  ? -31.399 -2.714  -4.649  1.00 34.31  ? 82  PRO   B CD  1 
ATOM   931  N N   . TRP   B 2 74  ? -27.193 -3.635  -6.557  1.00 32.83  ? 83  TRP   B N   1 
ATOM   932  C CA  . TRP   B 2 74  ? -26.561 -4.002  -7.851  1.00 32.79  ? 83  TRP   B CA  1 
ATOM   933  C C   . TRP   B 2 74  ? -27.464 -5.000  -8.603  1.00 33.75  ? 83  TRP   B C   1 
ATOM   934  O O   . TRP   B 2 74  ? -27.750 -6.052  -8.055  1.00 33.47  ? 83  TRP   B O   1 
ATOM   935  C CB  . TRP   B 2 74  ? -25.150 -4.555  -7.626  1.00 32.20  ? 83  TRP   B CB  1 
ATOM   936  C CG  . TRP   B 2 74  ? -24.366 -4.712  -8.890  1.00 31.41  ? 83  TRP   B CG  1 
ATOM   937  C CD1 . TRP   B 2 74  ? -24.301 -5.827  -9.670  1.00 31.46  ? 83  TRP   B CD1 1 
ATOM   938  C CD2 . TRP   B 2 74  ? -23.499 -3.731  -9.496  1.00 30.77  ? 83  TRP   B CD2 1 
ATOM   939  N NE1 . TRP   B 2 74  ? -23.452 -5.612  -10.723 1.00 31.57  ? 83  TRP   B NE1 1 
ATOM   940  C CE2 . TRP   B 2 74  ? -22.983 -4.326  -10.671 1.00 31.03  ? 83  TRP   B CE2 1 
ATOM   941  C CE3 . TRP   B 2 74  ? -23.178 -2.391  -9.220  1.00 30.07  ? 83  TRP   B CE3 1 
ATOM   942  C CZ2 . TRP   B 2 74  ? -22.142 -3.641  -11.557 1.00 30.52  ? 83  TRP   B CZ2 1 
ATOM   943  C CZ3 . TRP   B 2 74  ? -22.313 -1.724  -10.062 1.00 30.19  ? 83  TRP   B CZ3 1 
ATOM   944  C CH2 . TRP   B 2 74  ? -21.824 -2.344  -11.239 1.00 30.38  ? 83  TRP   B CH2 1 
ATOM   945  N N   . LYS   B 2 75  ? -27.817 -4.717  -9.871  1.00 34.29  ? 84  LYS   B N   1 
ATOM   946  C CA  . LYS   B 2 75  ? -28.759 -5.552  -10.688 1.00 35.60  ? 84  LYS   B CA  1 
ATOM   947  C C   . LYS   B 2 75  ? -28.043 -6.374  -11.779 1.00 36.39  ? 84  LYS   B C   1 
ATOM   948  O O   . LYS   B 2 75  ? -28.669 -7.321  -12.285 1.00 37.60  ? 84  LYS   B O   1 
ATOM   949  C CB  . LYS   B 2 75  ? -29.781 -4.641  -11.369 1.00 36.41  ? 84  LYS   B CB  1 
ATOM   950  C CG  . LYS   B 2 75  ? -30.642 -3.774  -10.470 1.00 37.08  ? 84  LYS   B CG  1 
ATOM   951  C CD  . LYS   B 2 75  ? -31.629 -4.593  -9.699  1.00 38.74  ? 84  LYS   B CD  1 
ATOM   952  C CE  . LYS   B 2 75  ? -32.361 -3.739  -8.690  1.00 39.91  ? 84  LYS   B CE  1 
ATOM   953  N NZ  . LYS   B 2 75  ? -33.776 -4.117  -8.605  1.00 42.05  ? 84  LYS   B NZ  1 
ATOM   954  N N   . LEU   B 2 76  ? -26.810 -6.044  -12.157 1.00 36.43  ? 85  LEU   B N   1 
ATOM   955  C CA  . LEU   B 2 76  ? -26.122 -6.614  -13.356 1.00 37.88  ? 85  LEU   B CA  1 
ATOM   956  C C   . LEU   B 2 76  ? -25.393 -7.896  -12.968 1.00 39.83  ? 85  LEU   B C   1 
ATOM   957  O O   . LEU   B 2 76  ? -24.502 -7.843  -12.094 1.00 38.94  ? 85  LEU   B O   1 
ATOM   958  C CB  . LEU   B 2 76  ? -25.156 -5.564  -13.903 1.00 36.84  ? 85  LEU   B CB  1 
ATOM   959  C CG  . LEU   B 2 76  ? -25.773 -4.174  -14.042 1.00 36.22  ? 85  LEU   B CG  1 
ATOM   960  C CD1 . LEU   B 2 76  ? -24.822 -3.202  -14.696 1.00 36.21  ? 85  LEU   B CD1 1 
ATOM   961  C CD2 . LEU   B 2 76  ? -27.104 -4.218  -14.767 1.00 37.32  ? 85  LEU   B CD2 1 
ATOM   962  N N   . ASP   B 2 77  ? -25.776 -9.020  -13.577 1.00 42.61  ? 86  ASP   B N   1 
ATOM   963  C CA  . ASP   B 2 77  ? -25.267 -10.336 -13.117 1.00 46.18  ? 86  ASP   B CA  1 
ATOM   964  C C   . ASP   B 2 77  ? -24.725 -11.171 -14.281 1.00 44.80  ? 86  ASP   B C   1 
ATOM   965  O O   . ASP   B 2 77  ? -24.233 -12.257 -14.038 1.00 44.23  ? 86  ASP   B O   1 
ATOM   966  C CB  . ASP   B 2 77  ? -26.324 -11.086 -12.305 1.00 50.73  ? 86  ASP   B CB  1 
ATOM   967  C CG  . ASP   B 2 77  ? -27.668 -11.193 -12.994 1.00 55.42  ? 86  ASP   B CG  1 
ATOM   968  O OD1 . ASP   B 2 77  ? -27.829 -10.608 -14.112 1.00 60.39  ? 86  ASP   B OD1 1 
ATOM   969  O OD2 . ASP   B 2 77  ? -28.562 -11.836 -12.401 1.00 60.97  ? 86  ASP   B OD2 1 
ATOM   970  N N   . ALA   B 2 78  ? -24.695 -10.662 -15.497 1.00 42.92  ? 87  ALA   B N   1 
ATOM   971  C CA  . ALA   B 2 78  ? -24.165 -11.448 -16.620 1.00 42.48  ? 87  ALA   B CA  1 
ATOM   972  C C   . ALA   B 2 78  ? -22.637 -11.520 -16.504 1.00 41.82  ? 87  ALA   B C   1 
ATOM   973  O O   . ALA   B 2 78  ? -21.978 -10.541 -16.010 1.00 40.66  ? 87  ALA   B O   1 
ATOM   974  C CB  . ALA   B 2 78  ? -24.627 -10.872 -17.958 1.00 41.95  ? 87  ALA   B CB  1 
ATOM   975  N N   . ALA   B 2 79  ? -22.074 -12.610 -17.040 1.00 42.67  ? 88  ALA   B N   1 
ATOM   976  C CA  . ALA   B 2 79  ? -20.628 -12.910 -16.973 1.00 43.36  ? 88  ALA   B CA  1 
ATOM   977  C C   . ALA   B 2 79  ? -20.076 -13.151 -18.378 1.00 42.49  ? 88  ALA   B C   1 
ATOM   978  O O   . ALA   B 2 79  ? -20.761 -13.813 -19.142 1.00 42.98  ? 88  ALA   B O   1 
ATOM   979  C CB  . ALA   B 2 79  ? -20.411 -14.117 -16.090 1.00 44.16  ? 88  ALA   B CB  1 
ATOM   980  N N   . TRP   B 2 80  ? -18.873 -12.647 -18.668 1.00 41.93  ? 89  TRP   B N   1 
ATOM   981  C CA  . TRP   B 2 80  ? -18.031 -13.079 -19.806 1.00 43.63  ? 89  TRP   B CA  1 
ATOM   982  C C   . TRP   B 2 80  ? -18.017 -14.608 -19.841 1.00 45.41  ? 89  TRP   B C   1 
ATOM   983  O O   . TRP   B 2 80  ? -17.916 -15.228 -18.737 1.00 41.48  ? 89  TRP   B O   1 
ATOM   984  C CB  . TRP   B 2 80  ? -16.604 -12.507 -19.778 1.00 43.22  ? 89  TRP   B CB  1 
ATOM   985  C CG  . TRP   B 2 80  ? -15.832 -12.864 -21.019 1.00 43.16  ? 89  TRP   B CG  1 
ATOM   986  C CD1 . TRP   B 2 80  ? -16.317 -12.891 -22.309 1.00 44.32  ? 89  TRP   B CD1 1 
ATOM   987  C CD2 . TRP   B 2 80  ? -14.439 -13.207 -21.113 1.00 43.43  ? 89  TRP   B CD2 1 
ATOM   988  N NE1 . TRP   B 2 80  ? -15.339 -13.273 -23.184 1.00 43.79  ? 89  TRP   B NE1 1 
ATOM   989  C CE2 . TRP   B 2 80  ? -14.180 -13.492 -22.483 1.00 44.30  ? 89  TRP   B CE2 1 
ATOM   990  C CE3 . TRP   B 2 80  ? -13.404 -13.388 -20.179 1.00 43.48  ? 89  TRP   B CE3 1 
ATOM   991  C CZ2 . TRP   B 2 80  ? -12.920 -13.861 -22.933 1.00 44.50  ? 89  TRP   B CZ2 1 
ATOM   992  C CZ3 . TRP   B 2 80  ? -12.155 -13.766 -20.646 1.00 44.08  ? 89  TRP   B CZ3 1 
ATOM   993  C CH2 . TRP   B 2 80  ? -11.923 -13.996 -22.002 1.00 44.29  ? 89  TRP   B CH2 1 
ATOM   994  N N   . ASP   B 2 81  ? -18.219 -15.180 -21.038 1.00 46.18  ? 90  ASP   B N   1 
ATOM   995  C CA  . ASP   B 2 81  ? -18.294 -16.653 -21.247 1.00 49.63  ? 90  ASP   B CA  1 
ATOM   996  C C   . ASP   B 2 81  ? -16.884 -17.251 -21.108 1.00 50.67  ? 90  ASP   B C   1 
ATOM   997  O O   . ASP   B 2 81  ? -16.818 -18.447 -20.772 1.00 53.63  ? 90  ASP   B O   1 
ATOM   998  C CB  . ASP   B 2 81  ? -18.979 -17.052 -22.577 1.00 48.92  ? 90  ASP   B CB  1 
ATOM   999  C CG  . ASP   B 2 81  ? -18.315 -16.602 -23.863 1.00 52.09  ? 90  ASP   B CG  1 
ATOM   1000 O OD1 . ASP   B 2 81  ? -17.195 -16.074 -23.798 1.00 54.33  ? 90  ASP   B OD1 1 
ATOM   1001 O OD2 . ASP   B 2 81  ? -18.968 -16.704 -24.947 1.00 53.24  ? 90  ASP   B OD2 1 
ATOM   1002 N N   . GLY   B 2 82  ? -15.823 -16.462 -21.350 1.00 51.36  ? 91  GLY   B N   1 
ATOM   1003 C CA  . GLY   B 2 82  ? -14.406 -16.885 -21.339 1.00 52.18  ? 91  GLY   B CA  1 
ATOM   1004 C C   . GLY   B 2 82  ? -13.876 -17.172 -22.752 1.00 55.45  ? 91  GLY   B C   1 
ATOM   1005 O O   . GLY   B 2 82  ? -12.677 -17.535 -22.878 1.00 55.71  ? 91  GLY   B O   1 
ATOM   1006 N N   . LEU   B 2 83  ? -14.727 -17.027 -23.777 1.00 55.45  ? 92  LEU   B N   1 
ATOM   1007 C CA  . LEU   B 2 83  ? -14.482 -17.469 -25.183 1.00 59.34  ? 92  LEU   B CA  1 
ATOM   1008 C C   . LEU   B 2 83  ? -14.767 -16.360 -26.205 1.00 58.73  ? 92  LEU   B C   1 
ATOM   1009 O O   . LEU   B 2 83  ? -13.964 -16.179 -27.157 1.00 59.54  ? 92  LEU   B O   1 
ATOM   1010 C CB  . LEU   B 2 83  ? -15.426 -18.635 -25.483 1.00 62.37  ? 92  LEU   B CB  1 
ATOM   1011 C CG  . LEU   B 2 83  ? -15.013 -20.011 -24.969 1.00 65.26  ? 92  LEU   B CG  1 
ATOM   1012 C CD1 . LEU   B 2 83  ? -16.024 -21.040 -25.454 1.00 66.24  ? 92  LEU   B CD1 1 
ATOM   1013 C CD2 . LEU   B 2 83  ? -13.612 -20.398 -25.434 1.00 65.61  ? 92  LEU   B CD2 1 
ATOM   1014 N N   . SER   B 2 84  ? -15.948 -15.749 -26.137 1.00 57.53  ? 93  SER   B N   1 
ATOM   1015 C CA  . SER   B 2 84  ? -16.511 -14.915 -27.232 1.00 56.15  ? 93  SER   B CA  1 
ATOM   1016 C C   . SER   B 2 84  ? -15.953 -13.495 -27.171 1.00 53.51  ? 93  SER   B C   1 
ATOM   1017 O O   . SER   B 2 84  ? -15.564 -13.042 -26.071 1.00 51.67  ? 93  SER   B O   1 
ATOM   1018 C CB  . SER   B 2 84  ? -18.002 -14.874 -27.178 1.00 56.87  ? 93  SER   B CB  1 
ATOM   1019 O OG  . SER   B 2 84  ? -18.504 -16.053 -26.548 1.00 58.15  ? 93  SER   B OG  1 
ATOM   1020 N N   . GLU   B 2 85  ? -15.939 -12.810 -28.317 1.00 51.25  ? 94  GLU   B N   1 
ATOM   1021 C CA  . GLU   B 2 85  ? -15.683 -11.346 -28.372 1.00 49.34  ? 94  GLU   B CA  1 
ATOM   1022 C C   . GLU   B 2 85  ? -16.930 -10.678 -27.548 1.00 47.68  ? 94  GLU   B C   1 
ATOM   1023 O O   . GLU   B 2 85  ? -18.077 -11.298 -27.616 1.00 47.68  ? 94  GLU   B O   1 
ATOM   1024 C CB  . GLU   B 2 85  ? -15.447 -10.832 -29.813 1.00 50.84  ? 94  GLU   B CB  1 
ATOM   1025 C CG  . GLU   B 2 85  ? -14.068 -11.216 -30.397 1.00 51.28  ? 94  GLU   B CG  1 
ATOM   1026 C CD  . GLU   B 2 85  ? -13.666 -10.623 -31.761 1.00 53.19  ? 94  GLU   B CD  1 
ATOM   1027 O OE1 . GLU   B 2 85  ? -14.465 -9.895  -32.367 1.00 53.48  ? 94  GLU   B OE1 1 
ATOM   1028 O OE2 . GLU   B 2 85  ? -12.527 -10.886 -32.209 1.00 55.30  ? 94  GLU   B OE2 1 
ATOM   1029 N N   . VAL   B 2 86  ? -16.558 -9.449  -27.140 1.00 45.13  ? 95  VAL   B N   1 
ATOM   1030 C CA  . VAL   B 2 86  ? -17.454 -8.529  -26.390 1.00 43.07  ? 95  VAL   B CA  1 
ATOM   1031 C C   . VAL   B 2 86  ? -17.396 -7.168  -27.043 1.00 42.36  ? 95  VAL   B C   1 
ATOM   1032 O O   . VAL   B 2 86  ? -16.453 -6.917  -27.905 1.00 44.85  ? 95  VAL   B O   1 
ATOM   1033 C CB  . VAL   B 2 86  ? -17.019 -8.437  -24.913 1.00 40.75  ? 95  VAL   B CB  1 
ATOM   1034 C CG1 . VAL   B 2 86  ? -16.871 -9.824  -24.368 1.00 41.31  ? 95  VAL   B CG1 1 
ATOM   1035 C CG2 . VAL   B 2 86  ? -15.715 -7.657  -24.806 1.00 40.56  ? 95  VAL   B CG2 1 
ATOM   1036 N N   . GLN   B 2 87  ? -18.334 -6.301  -26.653 1.00 40.89  ? 96  GLN   B N   1 
ATOM   1037 C CA  . GLN   B 2 87  ? -18.255 -4.877  -27.090 1.00 40.27  ? 96  GLN   B CA  1 
ATOM   1038 C C   . GLN   B 2 87  ? -18.136 -3.935  -25.881 1.00 38.55  ? 96  GLN   B C   1 
ATOM   1039 O O   . GLN   B 2 87  ? -18.976 -4.036  -25.028 1.00 37.47  ? 96  GLN   B O   1 
ATOM   1040 C CB  . GLN   B 2 87  ? -19.453 -4.541  -27.994 1.00 40.10  ? 96  GLN   B CB  1 
ATOM   1041 C CG  . GLN   B 2 87  ? -19.422 -5.382  -29.258 1.00 41.66  ? 96  GLN   B CG  1 
ATOM   1042 C CD  . GLN   B 2 87  ? -20.440 -4.785  -30.248 1.00 41.60  ? 96  GLN   B CD  1 
ATOM   1043 O OE1 . GLN   B 2 87  ? -21.266 -3.834  -30.193 1.00 42.48  ? 96  GLN   B OE1 1 
ATOM   1044 N NE2 . GLN   B 2 87  ? -20.349 -5.291  -31.549 1.00 42.81  ? 96  GLN   B NE2 1 
ATOM   1045 N N   . LEU   B 2 88  ? -17.132 -3.049  -25.880 1.00 38.20  ? 97  LEU   B N   1 
ATOM   1046 C CA  . LEU   B 2 88  ? -17.130 -1.858  -25.008 1.00 37.23  ? 97  LEU   B CA  1 
ATOM   1047 C C   . LEU   B 2 88  ? -18.052 -0.828  -25.641 1.00 37.83  ? 97  LEU   B C   1 
ATOM   1048 O O   . LEU   B 2 88  ? -17.799 -0.415  -26.812 1.00 38.98  ? 97  LEU   B O   1 
ATOM   1049 C CB  . LEU   B 2 88  ? -15.706 -1.313  -24.842 1.00 37.62  ? 97  LEU   B CB  1 
ATOM   1050 C CG  . LEU   B 2 88  ? -15.598 0.036   -24.145 1.00 37.48  ? 97  LEU   B CG  1 
ATOM   1051 C CD1 . LEU   B 2 88  ? -16.073 -0.070  -22.688 1.00 37.25  ? 97  LEU   B CD1 1 
ATOM   1052 C CD2 . LEU   B 2 88  ? -14.185 0.588   -24.204 1.00 37.99  ? 97  LEU   B CD2 1 
ATOM   1053 N N   . LEU   B 2 89  ? -19.132 -0.461  -24.961 1.00 36.83  ? 98  LEU   B N   1 
ATOM   1054 C CA  . LEU   B 2 89  ? -19.901 0.713   -25.366 1.00 37.09  ? 98  LEU   B CA  1 
ATOM   1055 C C   . LEU   B 2 89  ? -19.208 1.912   -24.727 1.00 37.18  ? 98  LEU   B C   1 
ATOM   1056 O O   . LEU   B 2 89  ? -19.634 2.369   -23.588 1.00 35.88  ? 98  LEU   B O   1 
ATOM   1057 C CB  . LEU   B 2 89  ? -21.352 0.480   -24.956 1.00 37.38  ? 98  LEU   B CB  1 
ATOM   1058 C CG  . LEU   B 2 89  ? -22.350 1.609   -25.247 1.00 38.28  ? 98  LEU   B CG  1 
ATOM   1059 C CD1 . LEU   B 2 89  ? -22.135 2.280   -26.566 1.00 40.63  ? 98  LEU   B CD1 1 
ATOM   1060 C CD2 . LEU   B 2 89  ? -23.768 1.071   -25.166 1.00 39.01  ? 98  LEU   B CD2 1 
ATOM   1061 N N   . ALA   B 2 90  ? -18.143 2.373   -25.399 1.00 37.52  ? 99  ALA   B N   1 
ATOM   1062 C CA  . ALA   B 2 90  ? -17.354 3.561   -25.008 1.00 37.45  ? 99  ALA   B CA  1 
ATOM   1063 C C   . ALA   B 2 90  ? -18.239 4.792   -25.170 1.00 37.70  ? 99  ALA   B C   1 
ATOM   1064 O O   . ALA   B 2 90  ? -18.827 5.029   -26.304 1.00 38.09  ? 99  ALA   B O   1 
ATOM   1065 C CB  . ALA   B 2 90  ? -16.062 3.712   -25.778 1.00 38.51  ? 99  ALA   B CB  1 
ATOM   1066 N N   . VAL   B 2 91  ? -18.308 5.581   -24.090 1.00 37.42  ? 100 VAL   B N   1 
ATOM   1067 C CA  . VAL   B 2 91  ? -18.911 6.929   -24.064 1.00 36.81  ? 100 VAL   B CA  1 
ATOM   1068 C C   . VAL   B 2 91  ? -17.811 7.909   -23.650 1.00 37.62  ? 100 VAL   B C   1 
ATOM   1069 O O   . VAL   B 2 91  ? -17.749 8.335   -22.503 1.00 36.59  ? 100 VAL   B O   1 
ATOM   1070 C CB  . VAL   B 2 91  ? -20.121 6.952   -23.121 1.00 35.97  ? 100 VAL   B CB  1 
ATOM   1071 C CG1 . VAL   B 2 91  ? -20.863 8.282   -23.136 1.00 36.24  ? 100 VAL   B CG1 1 
ATOM   1072 C CG2 . VAL   B 2 91  ? -21.105 5.819   -23.411 1.00 35.85  ? 100 VAL   B CG2 1 
ATOM   1073 N N   . PRO   B 2 92  ? -16.925 8.350   -24.573 1.00 38.24  ? 101 PRO   B N   1 
ATOM   1074 C CA  . PRO   B 2 92  ? -15.828 9.264   -24.240 1.00 38.58  ? 101 PRO   B CA  1 
ATOM   1075 C C   . PRO   B 2 92  ? -16.315 10.698  -24.040 1.00 39.18  ? 101 PRO   B C   1 
ATOM   1076 O O   . PRO   B 2 92  ? -17.422 11.097  -24.435 1.00 40.66  ? 101 PRO   B O   1 
ATOM   1077 C CB  . PRO   B 2 92  ? -14.874 9.179   -25.454 1.00 39.78  ? 101 PRO   B CB  1 
ATOM   1078 C CG  . PRO   B 2 92  ? -15.372 7.989   -26.270 1.00 39.48  ? 101 PRO   B CG  1 
ATOM   1079 C CD  . PRO   B 2 92  ? -16.847 7.891   -25.983 1.00 39.09  ? 101 PRO   B CD  1 
ATOM   1080 N N   . PRO   B 2 93  ? -15.499 11.533  -23.321 1.00 40.13  ? 102 PRO   B N   1 
ATOM   1081 C CA  . PRO   B 2 93  ? -15.899 12.906  -23.020 1.00 40.86  ? 102 PRO   B CA  1 
ATOM   1082 C C   . PRO   B 2 93  ? -16.059 13.726  -24.316 1.00 42.30  ? 102 PRO   B C   1 
ATOM   1083 O O   . PRO   B 2 93  ? -15.179 13.707  -25.134 1.00 42.50  ? 102 PRO   B O   1 
ATOM   1084 C CB  . PRO   B 2 93  ? -14.766 13.395  -22.102 1.00 40.94  ? 102 PRO   B CB  1 
ATOM   1085 C CG  . PRO   B 2 93  ? -14.330 12.126  -21.425 1.00 40.39  ? 102 PRO   B CG  1 
ATOM   1086 C CD  . PRO   B 2 93  ? -14.280 11.154  -22.590 1.00 40.90  ? 102 PRO   B CD  1 
ATOM   1087 N N   . GLY   B 2 94  ? -17.221 14.349  -24.482 1.00 42.80  ? 103 GLY   B N   1 
ATOM   1088 C CA  . GLY   B 2 94  ? -17.583 15.179  -25.641 1.00 43.93  ? 103 GLY   B CA  1 
ATOM   1089 C C   . GLY   B 2 94  ? -17.838 14.397  -26.929 1.00 44.80  ? 103 GLY   B C   1 
ATOM   1090 O O   . GLY   B 2 94  ? -18.020 15.055  -27.939 1.00 44.99  ? 103 GLY   B O   1 
ATOM   1091 N N   . GLU   B 2 95  ? -17.853 13.066  -26.930 1.00 45.07  ? 104 GLU   B N   1 
ATOM   1092 C CA  . GLU   B 2 95  ? -17.957 12.263  -28.178 1.00 46.46  ? 104 GLU   B CA  1 
ATOM   1093 C C   . GLU   B 2 95  ? -19.140 11.311  -28.028 1.00 46.47  ? 104 GLU   B C   1 
ATOM   1094 O O   . GLU   B 2 95  ? -19.556 11.016  -26.867 1.00 43.45  ? 104 GLU   B O   1 
ATOM   1095 C CB  . GLU   B 2 95  ? -16.634 11.550  -28.489 1.00 47.59  ? 104 GLU   B CB  1 
ATOM   1096 C CG  . GLU   B 2 95  ? -15.425 12.496  -28.432 1.00 49.64  ? 104 GLU   B CG  1 
ATOM   1097 C CD  . GLU   B 2 95  ? -14.005 11.845  -28.614 1.00 51.97  ? 104 GLU   B CD  1 
ATOM   1098 O OE1 . GLU   B 2 95  ? -13.978 10.598  -28.542 1.00 52.60  ? 104 GLU   B OE1 1 
ATOM   1099 O OE2 . GLU   B 2 95  ? -12.939 12.589  -28.913 1.00 54.64  ? 104 GLU   B OE2 1 
ATOM   1100 N N   . ARG   B 2 96  ? -19.743 10.935  -29.144 1.00 46.11  ? 105 ARG   B N   1 
ATOM   1101 C CA  . ARG   B 2 96  ? -20.945 10.072  -29.197 1.00 47.60  ? 105 ARG   B CA  1 
ATOM   1102 C C   . ARG   B 2 96  ? -20.571 8.684   -28.678 1.00 46.33  ? 105 ARG   B C   1 
ATOM   1103 O O   . ARG   B 2 96  ? -19.369 8.240   -28.890 1.00 45.90  ? 105 ARG   B O   1 
ATOM   1104 C CB  . ARG   B 2 96  ? -21.424 9.921   -30.645 1.00 51.95  ? 105 ARG   B CB  1 
ATOM   1105 C CG  . ARG   B 2 96  ? -22.766 9.218   -30.787 1.00 54.79  ? 105 ARG   B CG  1 
ATOM   1106 C CD  . ARG   B 2 96  ? -23.593 9.751   -31.954 1.00 58.32  ? 105 ARG   B CD  1 
ATOM   1107 N NE  . ARG   B 2 96  ? -22.907 9.826   -33.243 1.00 61.66  ? 105 ARG   B NE  1 
ATOM   1108 C CZ  . ARG   B 2 96  ? -22.438 10.947  -33.813 1.00 65.36  ? 105 ARG   B CZ  1 
ATOM   1109 N NH1 . ARG   B 2 96  ? -22.578 12.130  -33.231 1.00 65.78  ? 105 ARG   B NH1 1 
ATOM   1110 N NH2 . ARG   B 2 96  ? -21.858 10.887  -35.007 1.00 68.37  ? 105 ARG   B NH2 1 
ATOM   1111 N N   . ALA   B 2 97  ? -21.552 8.028   -28.006 1.00 45.81  ? 106 ALA   B N   1 
ATOM   1112 C CA  . ALA   B 2 97  ? -21.441 6.596   -27.650 1.00 45.35  ? 106 ALA   B CA  1 
ATOM   1113 C C   . ALA   B 2 97  ? -20.957 5.848   -28.896 1.00 45.68  ? 106 ALA   B C   1 
ATOM   1114 O O   . ALA   B 2 97  ? -21.508 6.113   -29.972 1.00 44.04  ? 106 ALA   B O   1 
ATOM   1115 C CB  . ALA   B 2 97  ? -22.762 6.061   -27.161 1.00 45.74  ? 106 ALA   B CB  1 
ATOM   1116 N N   . LYS   B 2 98  ? -19.986 4.947   -28.761 1.00 45.24  ? 107 LYS   B N   1 
ATOM   1117 C CA  . LYS   B 2 98  ? -19.461 4.142   -29.910 1.00 48.45  ? 107 LYS   B CA  1 
ATOM   1118 C C   . LYS   B 2 98  ? -19.171 2.723   -29.401 1.00 47.28  ? 107 LYS   B C   1 
ATOM   1119 O O   . LYS   B 2 98  ? -18.508 2.609   -28.309 1.00 44.55  ? 107 LYS   B O   1 
ATOM   1120 C CB  . LYS   B 2 98  ? -18.213 4.860   -30.431 1.00 51.67  ? 107 LYS   B CB  1 
ATOM   1121 C CG  . LYS   B 2 98  ? -17.561 4.298   -31.700 1.00 56.16  ? 107 LYS   B CG  1 
ATOM   1122 C CD  . LYS   B 2 98  ? -16.138 4.843   -31.880 1.00 60.44  ? 107 LYS   B CD  1 
ATOM   1123 C CE  . LYS   B 2 98  ? -15.440 5.090   -30.542 1.00 62.18  ? 107 LYS   B CE  1 
ATOM   1124 N NZ  . LYS   B 2 98  ? -13.970 5.213   -30.694 1.00 64.91  ? 107 LYS   B NZ  1 
ATOM   1125 N N   . ASN   B 2 99  ? -19.724 1.692   -30.061 1.00 44.69  ? 108 ASN   B N   1 
ATOM   1126 C CA  . ASN   B 2 99  ? -19.366 0.268   -29.820 1.00 45.31  ? 108 ASN   B CA  1 
ATOM   1127 C C   . ASN   B 2 99  ? -17.990 -0.053  -30.394 1.00 45.75  ? 108 ASN   B C   1 
ATOM   1128 O O   . ASN   B 2 99  ? -17.738 0.191   -31.624 1.00 45.18  ? 108 ASN   B O   1 
ATOM   1129 C CB  . ASN   B 2 99  ? -20.397 -0.747  -30.333 1.00 46.23  ? 108 ASN   B CB  1 
ATOM   1130 C CG  . ASN   B 2 99  ? -21.775 -0.506  -29.746 1.00 47.77  ? 108 ASN   B CG  1 
ATOM   1131 O OD1 . ASN   B 2 99  ? -22.325 0.621   -29.863 1.00 50.34  ? 108 ASN   B OD1 1 
ATOM   1132 N ND2 . ASN   B 2 99  ? -22.338 -1.521  -29.073 1.00 47.58  ? 108 ASN   B ND2 1 
ATOM   1133 N N   . ILE   B 2 100 ? -17.169 -0.739  -29.614 1.00 43.75  ? 109 ILE   B N   1 
ATOM   1134 C CA  . ILE   B 2 100 ? -15.849 -1.260  -30.024 1.00 44.42  ? 109 ILE   B CA  1 
ATOM   1135 C C   . ILE   B 2 100 ? -15.804 -2.733  -29.646 1.00 44.07  ? 109 ILE   B C   1 
ATOM   1136 O O   . ILE   B 2 100 ? -15.946 -3.094  -28.425 1.00 43.27  ? 109 ILE   B O   1 
ATOM   1137 C CB  . ILE   B 2 100 ? -14.705 -0.439  -29.419 1.00 45.43  ? 109 ILE   B CB  1 
ATOM   1138 C CG1 . ILE   B 2 100 ? -14.914 1.067   -29.585 1.00 47.22  ? 109 ILE   B CG1 1 
ATOM   1139 C CG2 . ILE   B 2 100 ? -13.364 -0.870  -29.953 1.00 46.40  ? 109 ILE   B CG2 1 
ATOM   1140 C CD1 . ILE   B 2 100 ? -14.595 1.578   -30.960 1.00 48.72  ? 109 ILE   B CD1 1 
ATOM   1141 N N   . GLN   B 2 101 ? -15.599 -3.602  -30.617 1.00 44.95  ? 110 GLN   B N   1 
ATOM   1142 C CA  . GLN   B 2 101 ? -15.697 -5.059  -30.419 1.00 46.12  ? 110 GLN   B CA  1 
ATOM   1143 C C   . GLN   B 2 101 ? -14.280 -5.600  -30.227 1.00 46.59  ? 110 GLN   B C   1 
ATOM   1144 O O   . GLN   B 2 101 ? -13.369 -5.131  -30.931 1.00 47.52  ? 110 GLN   B O   1 
ATOM   1145 C CB  . GLN   B 2 101 ? -16.409 -5.739  -31.574 1.00 48.51  ? 110 GLN   B CB  1 
ATOM   1146 C CG  . GLN   B 2 101 ? -16.328 -7.256  -31.480 1.00 49.14  ? 110 GLN   B CG  1 
ATOM   1147 C CD  . GLN   B 2 101 ? -17.347 -7.871  -32.459 1.00 50.32  ? 110 GLN   B CD  1 
ATOM   1148 O OE1 . GLN   B 2 101 ? -18.529 -7.345  -32.618 1.00 50.91  ? 110 GLN   B OE1 1 
ATOM   1149 N NE2 . GLN   B 2 101 ? -16.864 -9.007  -33.076 1.00 51.69  ? 110 GLN   B NE2 1 
ATOM   1150 N N   . THR   B 2 102 ? -14.082 -6.507  -29.240 1.00 45.21  ? 111 THR   B N   1 
ATOM   1151 C CA  . THR   B 2 102 ? -12.731 -6.978  -28.848 1.00 45.75  ? 111 THR   B CA  1 
ATOM   1152 C C   . THR   B 2 102 ? -12.852 -8.335  -28.149 1.00 44.37  ? 111 THR   B C   1 
ATOM   1153 O O   . THR   B 2 102 ? -13.983 -8.703  -27.673 1.00 46.60  ? 111 THR   B O   1 
ATOM   1154 C CB  . THR   B 2 102 ? -11.969 -5.917  -28.038 1.00 44.81  ? 111 THR   B CB  1 
ATOM   1155 O OG1 . THR   B 2 102 ? -10.444 -6.232  -27.862 1.00 47.04  ? 111 THR   B OG1 1 
ATOM   1156 C CG2 . THR   B 2 102 ? -12.342 -5.838  -26.557 1.00 44.58  ? 111 THR   B CG2 1 
ATOM   1157 N N   . LEU   B 2 103 ? -11.752 -9.113  -28.229 1.00 44.66  ? 112 LEU   B N   1 
ATOM   1158 C CA  . LEU   B 2 103 ? -11.628 -10.406 -27.516 1.00 44.21  ? 112 LEU   B CA  1 
ATOM   1159 C C   . LEU   B 2 103 ? -10.859 -10.116 -26.234 1.00 43.51  ? 112 LEU   B C   1 
ATOM   1160 O O   . LEU   B 2 103 ? -9.670  -9.704  -26.278 1.00 43.23  ? 112 LEU   B O   1 
ATOM   1161 C CB  . LEU   B 2 103 ? -10.866 -11.476 -28.320 1.00 45.21  ? 112 LEU   B CB  1 
ATOM   1162 C CG  . LEU   B 2 103 ? -10.782 -12.803 -27.553 1.00 45.82  ? 112 LEU   B CG  1 
ATOM   1163 C CD1 . LEU   B 2 103 ? -12.119 -13.536 -27.602 1.00 46.18  ? 112 LEU   B CD1 1 
ATOM   1164 C CD2 . LEU   B 2 103 ? -9.664  -13.699 -28.049 1.00 47.11  ? 112 LEU   B CD2 1 
ATOM   1165 N N   . PRO   B 2 104 ? -11.522 -10.239 -25.054 1.00 42.41  ? 113 PRO   B N   1 
ATOM   1166 C CA  . PRO   B 2 104 ? -10.828 -9.971  -23.803 1.00 42.32  ? 113 PRO   B CA  1 
ATOM   1167 C C   . PRO   B 2 104 ? -9.616  -10.913 -23.633 1.00 43.75  ? 113 PRO   B C   1 
ATOM   1168 O O   . PRO   B 2 104 ? -9.702  -12.136 -23.965 1.00 45.17  ? 113 PRO   B O   1 
ATOM   1169 C CB  . PRO   B 2 104 ? -11.874 -10.286 -22.714 1.00 41.12  ? 113 PRO   B CB  1 
ATOM   1170 C CG  . PRO   B 2 104 ? -13.212 -10.196 -23.423 1.00 40.97  ? 113 PRO   B CG  1 
ATOM   1171 C CD  . PRO   B 2 104 ? -12.919 -10.671 -24.858 1.00 41.77  ? 113 PRO   B CD  1 
ATOM   1172 N N   . GLY   B 2 105 ? -8.547  -10.345 -23.071 1.00 44.56  ? 114 GLY   B N   1 
ATOM   1173 C CA  . GLY   B 2 105 ? -7.514  -11.108 -22.346 1.00 45.04  ? 114 GLY   B CA  1 
ATOM   1174 C C   . GLY   B 2 105 ? -7.967  -11.440 -20.927 1.00 44.95  ? 114 GLY   B C   1 
ATOM   1175 O O   . GLY   B 2 105 ? -9.205  -11.394 -20.637 1.00 44.50  ? 114 GLY   B O   1 
ATOM   1176 N N   . ILE   B 2 106 ? -6.989  -11.836 -20.106 1.00 46.25  ? 115 ILE   B N   1 
ATOM   1177 C CA  . ILE   B 2 106 ? -7.175  -12.388 -18.729 1.00 46.81  ? 115 ILE   B CA  1 
ATOM   1178 C C   . ILE   B 2 106 ? -6.235  -11.679 -17.753 1.00 46.95  ? 115 ILE   B C   1 
ATOM   1179 O O   . ILE   B 2 106 ? -5.021  -11.612 -17.974 1.00 48.55  ? 115 ILE   B O   1 
ATOM   1180 C CB  . ILE   B 2 106 ? -6.873  -13.892 -18.707 1.00 48.92  ? 115 ILE   B CB  1 
ATOM   1181 C CG1 . ILE   B 2 106 ? -7.650  -14.674 -19.770 1.00 52.18  ? 115 ILE   B CG1 1 
ATOM   1182 C CG2 . ILE   B 2 106 ? -7.087  -14.456 -17.315 1.00 49.81  ? 115 ILE   B CG2 1 
ATOM   1183 C CD1 . ILE   B 2 106 ? -9.041  -15.045 -19.380 1.00 52.44  ? 115 ILE   B CD1 1 
ATOM   1184 N N   . PHE   B 2 107 ? -6.795  -11.216 -16.649 1.00 44.53  ? 116 PHE   B N   1 
ATOM   1185 C CA  . PHE   B 2 107 ? -6.058  -10.875 -15.406 1.00 44.20  ? 116 PHE   B CA  1 
ATOM   1186 C C   . PHE   B 2 107 ? -6.018  -12.166 -14.561 1.00 45.53  ? 116 PHE   B C   1 
ATOM   1187 O O   . PHE   B 2 107 ? -7.136  -12.663 -14.137 1.00 47.97  ? 116 PHE   B O   1 
ATOM   1188 C CB  . PHE   B 2 107 ? -6.831  -9.785  -14.666 1.00 42.47  ? 116 PHE   B CB  1 
ATOM   1189 C CG  . PHE   B 2 107 ? -6.571  -8.355  -15.044 1.00 42.22  ? 116 PHE   B CG  1 
ATOM   1190 C CD1 . PHE   B 2 107 ? -5.869  -8.014  -16.190 1.00 42.54  ? 116 PHE   B CD1 1 
ATOM   1191 C CD2 . PHE   B 2 107 ? -7.132  -7.339  -14.279 1.00 41.44  ? 116 PHE   B CD2 1 
ATOM   1192 C CE1 . PHE   B 2 107 ? -5.674  -6.684  -16.522 1.00 42.92  ? 116 PHE   B CE1 1 
ATOM   1193 C CE2 . PHE   B 2 107 ? -6.916  -6.006  -14.606 1.00 41.19  ? 116 PHE   B CE2 1 
ATOM   1194 C CZ  . PHE   B 2 107 ? -6.225  -5.684  -15.758 1.00 42.35  ? 116 PHE   B CZ  1 
ATOM   1195 N N   . LYS   B 2 108 ? -4.784  -12.673 -14.323 1.00 47.27  ? 117 LYS   B N   1 
ATOM   1196 C CA  . LYS   B 2 108 ? -4.551  -13.838 -13.415 1.00 47.95  ? 117 LYS   B CA  1 
ATOM   1197 C C   . LYS   B 2 108 ? -4.220  -13.282 -12.020 1.00 45.33  ? 117 LYS   B C   1 
ATOM   1198 O O   . LYS   B 2 108 ? -3.218  -12.540 -11.901 1.00 42.44  ? 117 LYS   B O   1 
ATOM   1199 C CB  . LYS   B 2 108 ? -3.454  -14.777 -13.947 1.00 51.97  ? 117 LYS   B CB  1 
ATOM   1200 C CG  . LYS   B 2 108 ? -3.728  -15.391 -15.323 1.00 57.43  ? 117 LYS   B CG  1 
ATOM   1201 C CD  . LYS   B 2 108 ? -2.780  -16.501 -15.847 1.00 62.02  ? 117 LYS   B CD  1 
ATOM   1202 C CE  . LYS   B 2 108 ? -3.371  -17.248 -17.046 1.00 66.99  ? 117 LYS   B CE  1 
ATOM   1203 N NZ  . LYS   B 2 108 ? -2.399  -17.772 -18.066 1.00 70.07  ? 117 LYS   B NZ  1 
ATOM   1204 N N   . THR   B 2 109 ? -5.081  -13.552 -11.037 1.00 45.10  ? 118 THR   B N   1 
ATOM   1205 C CA  . THR   B 2 109 ? -4.868  -13.152 -9.620  1.00 45.27  ? 118 THR   B CA  1 
ATOM   1206 C C   . THR   B 2 109 ? -4.878  -14.382 -8.695  1.00 46.12  ? 118 THR   B C   1 
ATOM   1207 O O   . THR   B 2 109 ? -5.370  -15.479 -9.056  1.00 45.24  ? 118 THR   B O   1 
ATOM   1208 C CB  . THR   B 2 109 ? -5.917  -12.157 -9.099  1.00 44.14  ? 118 THR   B CB  1 
ATOM   1209 O OG1 . THR   B 2 109 ? -7.072  -12.904 -8.685  1.00 43.58  ? 118 THR   B OG1 1 
ATOM   1210 C CG2 . THR   B 2 109 ? -6.262  -11.066 -10.094 1.00 43.61  ? 118 THR   B CG2 1 
ATOM   1211 N N   . LYS   B 2 110 ? -4.362  -14.196 -7.497  1.00 48.71  ? 119 LYS   B N   1 
ATOM   1212 C CA  . LYS   B 2 110 ? -4.344  -15.283 -6.483  1.00 49.59  ? 119 LYS   B CA  1 
ATOM   1213 C C   . LYS   B 2 110 ? -5.780  -15.790 -6.239  1.00 50.92  ? 119 LYS   B C   1 
ATOM   1214 O O   . LYS   B 2 110 ? -5.917  -16.982 -5.863  1.00 54.91  ? 119 LYS   B O   1 
ATOM   1215 C CB  . LYS   B 2 110 ? -3.664  -14.786 -5.202  1.00 50.36  ? 119 LYS   B CB  1 
ATOM   1216 C CG  . LYS   B 2 110 ? -4.161  -13.457 -4.666  1.00 50.69  ? 119 LYS   B CG  1 
ATOM   1217 C CD  . LYS   B 2 110 ? -3.508  -13.086 -3.363  1.00 53.87  ? 119 LYS   B CD  1 
ATOM   1218 C CE  . LYS   B 2 110 ? -4.433  -13.322 -2.202  1.00 54.64  ? 119 LYS   B CE  1 
ATOM   1219 N NZ  . LYS   B 2 110 ? -5.369  -12.191 -2.035  1.00 55.05  ? 119 LYS   B NZ  1 
ATOM   1220 N N   . ASP   B 2 111 ? -6.808  -14.941 -6.406  1.00 49.14  ? 120 ASP   B N   1 
ATOM   1221 C CA  . ASP   B 2 111 ? -8.223  -15.290 -6.106  1.00 50.18  ? 120 ASP   B CA  1 
ATOM   1222 C C   . ASP   B 2 111 ? -8.998  -15.663 -7.362  1.00 51.33  ? 120 ASP   B C   1 
ATOM   1223 O O   . ASP   B 2 111 ? -10.221 -15.848 -7.249  1.00 53.00  ? 120 ASP   B O   1 
ATOM   1224 C CB  . ASP   B 2 111 ? -8.935  -14.140 -5.397  1.00 50.21  ? 120 ASP   B CB  1 
ATOM   1225 C CG  . ASP   B 2 111 ? -8.332  -13.902 -4.028  1.00 51.06  ? 120 ASP   B CG  1 
ATOM   1226 O OD1 . ASP   B 2 111 ? -7.994  -14.899 -3.365  1.00 51.64  ? 120 ASP   B OD1 1 
ATOM   1227 O OD2 . ASP   B 2 111 ? -8.155  -12.739 -3.670  1.00 52.20  ? 120 ASP   B OD2 1 
ATOM   1228 N N   . GLY   B 2 112 ? -8.334  -15.768 -8.512  1.00 50.54  ? 121 GLY   B N   1 
ATOM   1229 C CA  . GLY   B 2 112 ? -9.021  -16.179 -9.740  1.00 51.46  ? 121 GLY   B CA  1 
ATOM   1230 C C   . GLY   B 2 112 ? -8.688  -15.317 -10.944 1.00 50.93  ? 121 GLY   B C   1 
ATOM   1231 O O   . GLY   B 2 112 ? -8.080  -14.248 -10.802 1.00 50.96  ? 121 GLY   B O   1 
ATOM   1232 N N   . ASP   B 2 113 ? -9.121  -15.802 -12.095 1.00 51.15  ? 122 ASP   B N   1 
ATOM   1233 C CA  . ASP   B 2 113 ? -8.962  -15.151 -13.422 1.00 51.00  ? 122 ASP   B CA  1 
ATOM   1234 C C   . ASP   B 2 113 ? -10.123 -14.173 -13.647 1.00 49.93  ? 122 ASP   B C   1 
ATOM   1235 O O   . ASP   B 2 113 ? -11.259 -14.471 -13.225 1.00 47.95  ? 122 ASP   B O   1 
ATOM   1236 C CB  . ASP   B 2 113 ? -8.890  -16.227 -14.493 1.00 54.67  ? 122 ASP   B CB  1 
ATOM   1237 C CG  . ASP   B 2 113 ? -7.557  -16.953 -14.585 1.00 56.56  ? 122 ASP   B CG  1 
ATOM   1238 O OD1 . ASP   B 2 113 ? -6.657  -16.614 -13.820 1.00 57.96  ? 122 ASP   B OD1 1 
ATOM   1239 O OD2 . ASP   B 2 113 ? -7.432  -17.836 -15.475 1.00 61.09  ? 122 ASP   B OD2 1 
ATOM   1240 N N   . ILE   B 2 114 ? -9.842  -13.026 -14.278 1.00 48.39  ? 123 ILE   B N   1 
ATOM   1241 C CA  . ILE   B 2 114 ? -10.870 -11.999 -14.618 1.00 47.85  ? 123 ILE   B CA  1 
ATOM   1242 C C   . ILE   B 2 114 ? -10.656 -11.617 -16.083 1.00 44.74  ? 123 ILE   B C   1 
ATOM   1243 O O   . ILE   B 2 114 ? -9.487  -11.450 -16.423 1.00 42.76  ? 123 ILE   B O   1 
ATOM   1244 C CB  . ILE   B 2 114 ? -10.724 -10.757 -13.710 1.00 48.20  ? 123 ILE   B CB  1 
ATOM   1245 C CG1 . ILE   B 2 114 ? -10.511 -11.115 -12.246 1.00 51.45  ? 123 ILE   B CG1 1 
ATOM   1246 C CG2 . ILE   B 2 114 ? -11.900 -9.829  -13.889 1.00 49.73  ? 123 ILE   B CG2 1 
ATOM   1247 C CD1 . ILE   B 2 114 ? -10.204 -9.902  -11.358 1.00 51.55  ? 123 ILE   B CD1 1 
ATOM   1248 N N   . GLY   B 2 115 ? -11.728 -11.417 -16.864 1.00 43.59  ? 124 GLY   B N   1 
ATOM   1249 C CA  . GLY   B 2 115 ? -11.631 -10.882 -18.239 1.00 41.91  ? 124 GLY   B CA  1 
ATOM   1250 C C   . GLY   B 2 115 ? -10.966 -9.514  -18.218 1.00 41.03  ? 124 GLY   B C   1 
ATOM   1251 O O   . GLY   B 2 115 ? -11.111 -8.783  -17.215 1.00 38.52  ? 124 GLY   B O   1 
ATOM   1252 N N   . ALA   B 2 116 ? -10.226 -9.141  -19.267 1.00 40.32  ? 125 ALA   B N   1 
ATOM   1253 C CA  . ALA   B 2 116 ? -9.620  -7.795  -19.345 1.00 40.64  ? 125 ALA   B CA  1 
ATOM   1254 C C   . ALA   B 2 116 ? -9.753  -7.277  -20.763 1.00 41.96  ? 125 ALA   B C   1 
ATOM   1255 O O   . ALA   B 2 116 ? -9.669  -8.097  -21.680 1.00 41.50  ? 125 ALA   B O   1 
ATOM   1256 C CB  . ALA   B 2 116 ? -8.180  -7.848  -18.906 1.00 41.08  ? 125 ALA   B CB  1 
ATOM   1257 N N   A VAL   B 2 117 ? -9.950  -5.965  -20.937 0.11 41.67  ? 126 VAL   B N   1 
ATOM   1258 N N   B VAL   B 2 117 ? -9.902  -5.955  -20.920 0.09 41.76  ? 126 VAL   B N   1 
ATOM   1259 N N   C VAL   B 2 117 ? -9.957  -5.965  -20.935 0.41 41.65  ? 126 VAL   B N   1 
ATOM   1260 N N   D VAL   B 2 117 ? -9.909  -5.956  -20.918 0.39 41.75  ? 126 VAL   B N   1 
ATOM   1261 C CA  A VAL   B 2 117 ? -10.072 -5.346  -22.293 0.11 42.41  ? 126 VAL   B CA  1 
ATOM   1262 C CA  B VAL   B 2 117 ? -10.097 -5.271  -22.236 0.09 42.50  ? 126 VAL   B CA  1 
ATOM   1263 C CA  C VAL   B 2 117 ? -10.071 -5.339  -22.286 0.41 42.38  ? 126 VAL   B CA  1 
ATOM   1264 C CA  D VAL   B 2 117 ? -10.095 -5.264  -22.230 0.39 42.47  ? 126 VAL   B CA  1 
ATOM   1265 C C   A VAL   B 2 117 ? -8.949  -4.325  -22.520 0.11 42.98  ? 126 VAL   B C   1 
ATOM   1266 C C   B VAL   B 2 117 ? -8.927  -4.312  -22.502 0.09 43.05  ? 126 VAL   B C   1 
ATOM   1267 C C   C VAL   B 2 117 ? -8.944  -4.320  -22.513 0.41 43.08  ? 126 VAL   B C   1 
ATOM   1268 C C   D VAL   B 2 117 ? -8.917  -4.312  -22.495 0.39 43.15  ? 126 VAL   B C   1 
ATOM   1269 O O   A VAL   B 2 117 ? -8.802  -3.392  -21.697 0.11 42.40  ? 126 VAL   B O   1 
ATOM   1270 O O   B VAL   B 2 117 ? -8.734  -3.384  -21.680 0.09 42.52  ? 126 VAL   B O   1 
ATOM   1271 O O   C VAL   B 2 117 ? -8.816  -3.352  -21.747 0.41 42.32  ? 126 VAL   B O   1 
ATOM   1272 O O   D VAL   B 2 117 ? -8.712  -3.371  -21.714 0.39 42.46  ? 126 VAL   B O   1 
ATOM   1273 C CB  A VAL   B 2 117 ? -11.470 -4.749  -22.546 0.11 42.07  ? 126 VAL   B CB  1 
ATOM   1274 C CB  B VAL   B 2 117 ? -11.457 -4.548  -22.266 0.09 42.20  ? 126 VAL   B CB  1 
ATOM   1275 C CB  C VAL   B 2 117 ? -11.465 -4.747  -22.557 0.41 42.02  ? 126 VAL   B CB  1 
ATOM   1276 C CB  D VAL   B 2 117 ? -11.456 -4.546  -22.271 0.39 42.24  ? 126 VAL   B CB  1 
ATOM   1277 C CG1 A VAL   B 2 117 ? -12.526 -5.845  -22.556 0.11 41.97  ? 126 VAL   B CG1 1 
ATOM   1278 C CG1 B VAL   B 2 117 ? -11.548 -3.508  -23.370 0.09 42.72  ? 126 VAL   B CG1 1 
ATOM   1279 C CG1 C VAL   B 2 117 ? -12.512 -5.855  -22.586 0.41 41.93  ? 126 VAL   B CG1 1 
ATOM   1280 C CG1 D VAL   B 2 117 ? -11.556 -3.503  -23.364 0.39 42.90  ? 126 VAL   B CG1 1 
ATOM   1281 C CG2 A VAL   B 2 117 ? -11.843 -3.649  -21.562 0.11 41.50  ? 126 VAL   B CG2 1 
ATOM   1282 C CG2 B VAL   B 2 117 ? -12.599 -5.546  -22.376 0.09 42.18  ? 126 VAL   B CG2 1 
ATOM   1283 C CG2 C VAL   B 2 117 ? -11.852 -3.643  -21.578 0.41 41.61  ? 126 VAL   B CG2 1 
ATOM   1284 C CG2 D VAL   B 2 117 ? -12.592 -5.552  -22.392 0.39 42.30  ? 126 VAL   B CG2 1 
ATOM   1285 N N   . ALA   B 2 118 ? -8.206  -4.496  -23.628 1.00 43.85  ? 127 ALA   B N   1 
ATOM   1286 C CA  . ALA   B 2 118 ? -7.021  -3.664  -23.946 1.00 45.12  ? 127 ALA   B CA  1 
ATOM   1287 C C   . ALA   B 2 118 ? -7.435  -2.574  -24.928 1.00 47.64  ? 127 ALA   B C   1 
ATOM   1288 O O   . ALA   B 2 118 ? -7.163  -2.721  -26.142 1.00 48.06  ? 127 ALA   B O   1 
ATOM   1289 C CB  . ALA   B 2 118 ? -5.874  -4.535  -24.437 1.00 46.23  ? 127 ALA   B CB  1 
ATOM   1290 N N   . LEU   B 2 119 ? -8.209  -1.598  -24.455 1.00 47.48  ? 128 LEU   B N   1 
ATOM   1291 C CA  . LEU   B 2 119 ? -8.691  -0.460  -25.255 1.00 48.81  ? 128 LEU   B CA  1 
ATOM   1292 C C   . LEU   B 2 119 ? -8.367  0.812   -24.474 1.00 52.21  ? 128 LEU   B C   1 
ATOM   1293 O O   . LEU   B 2 119 ? -8.609  0.833   -23.235 1.00 55.75  ? 128 LEU   B O   1 
ATOM   1294 C CB  . LEU   B 2 119 ? -10.189 -0.640  -25.528 1.00 47.70  ? 128 LEU   B CB  1 
ATOM   1295 C CG  . LEU   B 2 119 ? -10.597 -1.897  -26.305 1.00 46.51  ? 128 LEU   B CG  1 
ATOM   1296 C CD1 . LEU   B 2 119 ? -12.102 -2.079  -26.278 1.00 44.93  ? 128 LEU   B CD1 1 
ATOM   1297 C CD2 . LEU   B 2 119 ? -10.096 -1.846  -27.761 1.00 48.07  ? 128 LEU   B CD2 1 
ATOM   1298 N N   . ASP   B 2 120 ? -7.800  1.812   -25.147 1.00 56.65  ? 129 ASP   B N   1 
ATOM   1299 C CA  . ASP   B 2 120 ? -7.253  3.019   -24.481 1.00 58.61  ? 129 ASP   B CA  1 
ATOM   1300 C C   . ASP   B 2 120 ? -8.262  4.144   -24.678 1.00 56.14  ? 129 ASP   B C   1 
ATOM   1301 O O   . ASP   B 2 120 ? -8.540  4.472   -25.824 1.00 58.31  ? 129 ASP   B O   1 
ATOM   1302 C CB  . ASP   B 2 120 ? -5.868  3.370   -25.037 1.00 63.09  ? 129 ASP   B CB  1 
ATOM   1303 C CG  . ASP   B 2 120 ? -4.791  3.606   -23.971 1.00 66.52  ? 129 ASP   B CG  1 
ATOM   1304 O OD1 . ASP   B 2 120 ? -5.117  4.071   -22.840 1.00 62.11  ? 129 ASP   B OD1 1 
ATOM   1305 O OD2 . ASP   B 2 120 ? -3.621  3.310   -24.273 1.00 72.37  ? 129 ASP   B OD2 1 
ATOM   1306 N N   . TYR   B 2 121 ? -8.809  4.695   -23.603 1.00 53.23  ? 130 TYR   B N   1 
ATOM   1307 C CA  . TYR   B 2 121 ? -9.760  5.825   -23.660 1.00 51.73  ? 130 TYR   B CA  1 
ATOM   1308 C C   . TYR   B 2 121 ? -9.422  6.785   -22.536 1.00 49.00  ? 130 TYR   B C   1 
ATOM   1309 O O   . TYR   B 2 121 ? -8.751  6.383   -21.584 1.00 49.12  ? 130 TYR   B O   1 
ATOM   1310 C CB  . TYR   B 2 121 ? -11.200 5.328   -23.576 1.00 52.95  ? 130 TYR   B CB  1 
ATOM   1311 C CG  . TYR   B 2 121 ? -11.729 4.756   -24.863 1.00 54.07  ? 130 TYR   B CG  1 
ATOM   1312 C CD1 . TYR   B 2 121 ? -12.202 5.589   -25.861 1.00 56.71  ? 130 TYR   B CD1 1 
ATOM   1313 C CD2 . TYR   B 2 121 ? -11.730 3.391   -25.108 1.00 55.57  ? 130 TYR   B CD2 1 
ATOM   1314 C CE1 . TYR   B 2 121 ? -12.668 5.085   -27.062 1.00 58.14  ? 130 TYR   B CE1 1 
ATOM   1315 C CE2 . TYR   B 2 121 ? -12.190 2.870   -26.314 1.00 57.73  ? 130 TYR   B CE2 1 
ATOM   1316 C CZ  . TYR   B 2 121 ? -12.655 3.723   -27.298 1.00 58.62  ? 130 TYR   B CZ  1 
ATOM   1317 O OH  . TYR   B 2 121 ? -13.136 3.261   -28.491 1.00 63.62  ? 130 TYR   B OH  1 
ATOM   1318 N N   . PRO   B 2 122 ? -9.864  8.056   -22.595 1.00 46.95  ? 131 PRO   B N   1 
ATOM   1319 C CA  . PRO   B 2 122 ? -9.590  8.997   -21.517 1.00 46.91  ? 131 PRO   B CA  1 
ATOM   1320 C C   . PRO   B 2 122 ? -10.240 8.449   -20.227 1.00 44.62  ? 131 PRO   B C   1 
ATOM   1321 O O   . PRO   B 2 122 ? -11.128 7.586   -20.312 1.00 42.09  ? 131 PRO   B O   1 
ATOM   1322 C CB  . PRO   B 2 122 ? -10.212 10.320  -22.013 1.00 48.23  ? 131 PRO   B CB  1 
ATOM   1323 C CG  . PRO   B 2 122 ? -10.301 10.164  -23.527 1.00 49.39  ? 131 PRO   B CG  1 
ATOM   1324 C CD  . PRO   B 2 122 ? -10.593 8.687   -23.714 1.00 49.75  ? 131 PRO   B CD  1 
ATOM   1325 N N   . ALA   B 2 123 ? -9.728  8.894   -19.081 1.00 43.61  ? 132 ALA   B N   1 
ATOM   1326 C CA  . ALA   B 2 123 ? -10.163 8.425   -17.748 1.00 42.16  ? 132 ALA   B CA  1 
ATOM   1327 C C   . ALA   B 2 123 ? -11.656 8.707   -17.547 1.00 40.95  ? 132 ALA   B C   1 
ATOM   1328 O O   . ALA   B 2 123 ? -12.380 7.846   -16.890 1.00 39.69  ? 132 ALA   B O   1 
ATOM   1329 C CB  . ALA   B 2 123 ? -9.290  9.040   -16.676 1.00 42.40  ? 132 ALA   B CB  1 
ATOM   1330 N N   . GLY   B 2 124 ? -12.156 9.782   -18.179 1.00 39.82  ? 133 GLY   B N   1 
ATOM   1331 C CA  . GLY   B 2 124 ? -13.570 10.189  -18.067 1.00 38.34  ? 133 GLY   B CA  1 
ATOM   1332 C C   . GLY   B 2 124 ? -14.517 9.175   -18.707 1.00 36.88  ? 133 GLY   B C   1 
ATOM   1333 O O   . GLY   B 2 124 ? -15.772 9.374   -18.421 1.00 36.93  ? 133 GLY   B O   1 
ATOM   1334 N N   . THR   B 2 125 ? -13.936 8.133   -19.434 1.00 35.74  ? 134 THR   B N   1 
ATOM   1335 C CA  . THR   B 2 125 ? -14.724 6.989   -20.000 1.00 36.00  ? 134 THR   B CA  1 
ATOM   1336 C C   . THR   B 2 125 ? -15.035 5.889   -18.953 1.00 35.88  ? 134 THR   B C   1 
ATOM   1337 O O   . THR   B 2 125 ? -15.844 4.935   -19.254 1.00 35.33  ? 134 THR   B O   1 
ATOM   1338 C CB  . THR   B 2 125 ? -13.990 6.402   -21.222 1.00 37.83  ? 134 THR   B CB  1 
ATOM   1339 O OG1 . THR   B 2 125 ? -13.663 7.446   -22.141 1.00 38.68  ? 134 THR   B OG1 1 
ATOM   1340 C CG2 . THR   B 2 125 ? -14.805 5.448   -22.063 1.00 37.60  ? 134 THR   B CG2 1 
ATOM   1341 N N   . SER   B 2 126 ? -14.392 5.977   -17.781 1.00 35.20  ? 135 SER   B N   1 
ATOM   1342 C CA  . SER   B 2 126 ? -14.598 5.014   -16.639 1.00 34.86  ? 135 SER   B CA  1 
ATOM   1343 C C   . SER   B 2 126 ? -16.114 4.792   -16.369 1.00 33.90  ? 135 SER   B C   1 
ATOM   1344 O O   . SER   B 2 126 ? -16.852 5.789   -16.221 1.00 34.60  ? 135 SER   B O   1 
ATOM   1345 C CB  . SER   B 2 126 ? -13.947 5.479   -15.396 1.00 35.21  ? 135 SER   B CB  1 
ATOM   1346 O OG  . SER   B 2 126 ? -12.557 5.447   -15.449 1.00 35.74  ? 135 SER   B OG  1 
ATOM   1347 N N   . GLY   B 2 127 ? -16.542 3.525   -16.334 1.00 33.39  ? 136 GLY   B N   1 
ATOM   1348 C CA  . GLY   B 2 127 ? -17.959 3.110   -16.074 1.00 33.02  ? 136 GLY   B CA  1 
ATOM   1349 C C   . GLY   B 2 127 ? -18.716 2.741   -17.323 1.00 33.23  ? 136 GLY   B C   1 
ATOM   1350 O O   . GLY   B 2 127 ? -19.880 2.251   -17.211 1.00 32.82  ? 136 GLY   B O   1 
ATOM   1351 N N   . SER   B 2 128 ? -18.087 2.945   -18.495 1.00 33.74  ? 137 SER   B N   1 
ATOM   1352 C CA  . SER   B 2 128 ? -18.702 2.441   -19.735 1.00 33.60  ? 137 SER   B CA  1 
ATOM   1353 C C   . SER   B 2 128 ? -18.886 0.901   -19.550 1.00 33.26  ? 137 SER   B C   1 
ATOM   1354 O O   . SER   B 2 128 ? -17.983 0.165   -19.061 1.00 34.56  ? 137 SER   B O   1 
ATOM   1355 C CB  . SER   B 2 128 ? -17.899 2.812   -20.982 1.00 33.91  ? 137 SER   B CB  1 
ATOM   1356 O OG  . SER   B 2 128 ? -17.814 4.255   -21.066 1.00 34.20  ? 137 SER   B OG  1 
ATOM   1357 N N   . PRO   B 2 129 ? -20.104 0.434   -19.978 1.00 32.73  ? 138 PRO   B N   1 
ATOM   1358 C CA  . PRO   B 2 129 ? -20.434 -0.988  -19.959 1.00 32.87  ? 138 PRO   B CA  1 
ATOM   1359 C C   . PRO   B 2 129 ? -19.808 -1.827  -21.072 1.00 34.55  ? 138 PRO   B C   1 
ATOM   1360 O O   . PRO   B 2 129 ? -19.757 -1.345  -22.231 1.00 34.51  ? 138 PRO   B O   1 
ATOM   1361 C CB  . PRO   B 2 129 ? -21.943 -1.032  -20.170 1.00 33.03  ? 138 PRO   B CB  1 
ATOM   1362 C CG  . PRO   B 2 129 ? -22.241 0.193   -21.045 1.00 33.24  ? 138 PRO   B CG  1 
ATOM   1363 C CD  . PRO   B 2 129 ? -21.243 1.231   -20.554 1.00 33.31  ? 138 PRO   B CD  1 
ATOM   1364 N N   . ILE   B 2 130 ? -19.449 -3.039  -20.682 1.00 35.14  ? 139 ILE   B N   1 
ATOM   1365 C CA  . ILE   B 2 130 ? -18.958 -4.122  -21.570 1.00 36.80  ? 139 ILE   B CA  1 
ATOM   1366 C C   . ILE   B 2 130 ? -20.136 -5.070  -21.745 1.00 37.96  ? 139 ILE   B C   1 
ATOM   1367 O O   . ILE   B 2 130 ? -20.836 -5.306  -20.784 1.00 36.66  ? 139 ILE   B O   1 
ATOM   1368 C CB  . ILE   B 2 130 ? -17.726 -4.818  -20.998 1.00 37.20  ? 139 ILE   B CB  1 
ATOM   1369 C CG1 . ILE   B 2 130 ? -16.561 -3.847  -20.766 1.00 37.73  ? 139 ILE   B CG1 1 
ATOM   1370 C CG2 . ILE   B 2 130 ? -17.331 -5.989  -21.885 1.00 37.92  ? 139 ILE   B CG2 1 
ATOM   1371 C CD1 . ILE   B 2 130 ? -15.644 -4.303  -19.657 1.00 37.89  ? 139 ILE   B CD1 1 
ATOM   1372 N N   . LEU   B 2 131 ? -20.470 -5.376  -23.015 1.00 39.89  ? 140 LEU   B N   1 
ATOM   1373 C CA  . LEU   B 2 131 ? -21.686 -6.143  -23.416 1.00 42.32  ? 140 LEU   B CA  1 
ATOM   1374 C C   . LEU   B 2 131 ? -21.303 -7.543  -24.018 1.00 43.27  ? 140 LEU   B C   1 
ATOM   1375 O O   . LEU   B 2 131 ? -20.239 -7.660  -24.946 1.00 44.18  ? 140 LEU   B O   1 
ATOM   1376 C CB  . LEU   B 2 131 ? -22.390 -5.424  -24.587 1.00 44.72  ? 140 LEU   B CB  1 
ATOM   1377 C CG  . LEU   B 2 131 ? -22.842 -3.983  -24.368 1.00 45.41  ? 140 LEU   B CG  1 
ATOM   1378 C CD1 . LEU   B 2 131 ? -23.862 -3.533  -25.454 1.00 46.46  ? 140 LEU   B CD1 1 
ATOM   1379 C CD2 . LEU   B 2 131 ? -23.423 -3.858  -22.963 1.00 45.09  ? 140 LEU   B CD2 1 
ATOM   1380 N N   . ASP   B 2 132 ? -22.236 -8.493  -23.830 1.00 43.60  ? 141 ASP   B N   1 
ATOM   1381 C CA  . ASP   B 2 132 ? -22.173 -9.787  -24.548 1.00 45.41  ? 141 ASP   B CA  1 
ATOM   1382 C C   . ASP   B 2 132 ? -23.063 -9.661  -25.789 1.00 47.79  ? 141 ASP   B C   1 
ATOM   1383 O O   . ASP   B 2 132 ? -23.652 -8.552  -25.995 1.00 47.02  ? 141 ASP   B O   1 
ATOM   1384 C CB  . ASP   B 2 132 ? -22.540 -11.022 -23.720 1.00 45.76  ? 141 ASP   B CB  1 
ATOM   1385 C CG  . ASP   B 2 132 ? -23.979 -11.108 -23.227 1.00 46.30  ? 141 ASP   B CG  1 
ATOM   1386 O OD1 . ASP   B 2 132 ? -24.852 -10.365 -23.670 1.00 46.01  ? 141 ASP   B OD1 1 
ATOM   1387 O OD2 . ASP   B 2 132 ? -24.170 -11.853 -22.257 1.00 49.16  ? 141 ASP   B OD2 1 
ATOM   1388 N N   . LYS   B 2 133 ? -23.190 -10.768 -26.526 1.00 50.88  ? 142 LYS   B N   1 
ATOM   1389 C CA  . LYS   B 2 133 ? -23.824 -10.765 -27.868 1.00 56.12  ? 142 LYS   B CA  1 
ATOM   1390 C C   . LYS   B 2 133 ? -25.332 -10.580 -27.725 1.00 55.49  ? 142 LYS   B C   1 
ATOM   1391 O O   . LYS   B 2 133 ? -25.948 -10.208 -28.737 1.00 55.56  ? 142 LYS   B O   1 
ATOM   1392 C CB  . LYS   B 2 133 ? -23.507 -12.058 -28.638 1.00 60.07  ? 142 LYS   B CB  1 
ATOM   1393 C CG  . LYS   B 2 133 ? -22.119 -12.093 -29.269 1.00 65.08  ? 142 LYS   B CG  1 
ATOM   1394 C CD  . LYS   B 2 133 ? -21.516 -13.495 -29.422 1.00 69.47  ? 142 LYS   B CD  1 
ATOM   1395 C CE  . LYS   B 2 133 ? -20.057 -13.450 -29.840 1.00 72.83  ? 142 LYS   B CE  1 
ATOM   1396 N NZ  . LYS   B 2 133 ? -19.556 -14.751 -30.359 1.00 74.15  ? 142 LYS   B NZ  1 
ATOM   1397 N N   . CYS   B 2 134 ? -25.892 -10.833 -26.532 1.00 55.27  ? 143 CYS   B N   1 
ATOM   1398 C CA  . CYS   B 2 134 ? -27.336 -10.647 -26.250 1.00 55.31  ? 143 CYS   B CA  1 
ATOM   1399 C C   . CYS   B 2 134 ? -27.597 -9.236  -25.690 1.00 51.08  ? 143 CYS   B C   1 
ATOM   1400 O O   . CYS   B 2 134 ? -28.741 -8.962  -25.330 1.00 51.40  ? 143 CYS   B O   1 
ATOM   1401 C CB  . CYS   B 2 134 ? -27.844 -11.704 -25.278 1.00 58.78  ? 143 CYS   B CB  1 
ATOM   1402 S SG  . CYS   B 2 134 ? -28.052 -13.339 -26.030 1.00 62.20  ? 143 CYS   B SG  1 
ATOM   1403 N N   . GLY   B 2 135 ? -26.581 -8.367  -25.668 1.00 47.76  ? 144 GLY   B N   1 
ATOM   1404 C CA  . GLY   B 2 135 ? -26.681 -6.982  -25.184 1.00 45.67  ? 144 GLY   B CA  1 
ATOM   1405 C C   . GLY   B 2 135 ? -26.708 -6.898  -23.649 1.00 43.85  ? 144 GLY   B C   1 
ATOM   1406 O O   . GLY   B 2 135 ? -27.055 -5.852  -23.144 1.00 43.23  ? 144 GLY   B O   1 
ATOM   1407 N N   . ARG   B 2 136 ? -26.364 -7.969  -22.948 1.00 43.23  ? 145 ARG   B N   1 
ATOM   1408 C CA  . ARG   B 2 136 ? -26.315 -7.976  -21.450 1.00 43.18  ? 145 ARG   B CA  1 
ATOM   1409 C C   . ARG   B 2 136 ? -25.006 -7.357  -20.957 1.00 40.62  ? 145 ARG   B C   1 
ATOM   1410 O O   . ARG   B 2 136 ? -23.902 -7.638  -21.572 1.00 40.71  ? 145 ARG   B O   1 
ATOM   1411 C CB  . ARG   B 2 136 ? -26.545 -9.389  -20.950 1.00 45.53  ? 145 ARG   B CB  1 
ATOM   1412 C CG  . ARG   B 2 136 ? -28.026 -9.729  -20.985 1.00 48.82  ? 145 ARG   B CG  1 
ATOM   1413 C CD  . ARG   B 2 136 ? -28.231 -11.150 -20.573 1.00 52.35  ? 145 ARG   B CD  1 
ATOM   1414 N NE  . ARG   B 2 136 ? -27.416 -11.935 -21.466 1.00 58.03  ? 145 ARG   B NE  1 
ATOM   1415 C CZ  . ARG   B 2 136 ? -26.856 -13.108 -21.198 1.00 60.78  ? 145 ARG   B CZ  1 
ATOM   1416 N NH1 . ARG   B 2 136 ? -26.980 -13.684 -20.007 1.00 62.26  ? 145 ARG   B NH1 1 
ATOM   1417 N NH2 . ARG   B 2 136 ? -26.159 -13.693 -22.154 1.00 63.90  ? 145 ARG   B NH2 1 
ATOM   1418 N N   . VAL   B 2 137 ? -25.096 -6.556  -19.870 1.00 37.78  ? 146 VAL   B N   1 
ATOM   1419 C CA  . VAL   B 2 137 ? -23.892 -5.870  -19.312 1.00 36.62  ? 146 VAL   B CA  1 
ATOM   1420 C C   . VAL   B 2 137 ? -23.166 -6.940  -18.496 1.00 36.48  ? 146 VAL   B C   1 
ATOM   1421 O O   . VAL   B 2 137 ? -23.779 -7.464  -17.486 1.00 36.89  ? 146 VAL   B O   1 
ATOM   1422 C CB  . VAL   B 2 137 ? -24.223 -4.585  -18.523 1.00 35.69  ? 146 VAL   B CB  1 
ATOM   1423 C CG1 . VAL   B 2 137 ? -22.973 -3.931  -17.944 1.00 35.11  ? 146 VAL   B CG1 1 
ATOM   1424 C CG2 . VAL   B 2 137 ? -24.940 -3.578  -19.444 1.00 35.99  ? 146 VAL   B CG2 1 
ATOM   1425 N N   . ILE   B 2 138 ? -21.956 -7.289  -18.927 1.00 35.93  ? 147 ILE   B N   1 
ATOM   1426 C CA  . ILE   B 2 138 ? -21.094 -8.285  -18.226 1.00 35.89  ? 147 ILE   B CA  1 
ATOM   1427 C C   . ILE   B 2 138 ? -20.076 -7.593  -17.294 1.00 34.98  ? 147 ILE   B C   1 
ATOM   1428 O O   . ILE   B 2 138 ? -19.325 -8.339  -16.594 1.00 35.09  ? 147 ILE   B O   1 
ATOM   1429 C CB  . ILE   B 2 138 ? -20.413 -9.236  -19.245 1.00 36.51  ? 147 ILE   B CB  1 
ATOM   1430 C CG1 . ILE   B 2 138 ? -19.589 -8.460  -20.270 1.00 36.52  ? 147 ILE   B CG1 1 
ATOM   1431 C CG2 . ILE   B 2 138 ? -21.436 -10.146 -19.892 1.00 36.59  ? 147 ILE   B CG2 1 
ATOM   1432 C CD1 . ILE   B 2 138 ? -18.597 -9.312  -21.033 1.00 38.06  ? 147 ILE   B CD1 1 
ATOM   1433 N N   . GLY   B 2 139 ? -20.030 -6.261  -17.262 1.00 34.94  ? 148 GLY   B N   1 
ATOM   1434 C CA  . GLY   B 2 139 ? -19.192 -5.474  -16.329 1.00 33.97  ? 148 GLY   B CA  1 
ATOM   1435 C C   . GLY   B 2 139 ? -18.908 -4.080  -16.843 1.00 33.88  ? 148 GLY   B C   1 
ATOM   1436 O O   . GLY   B 2 139 ? -19.394 -3.724  -17.974 1.00 33.15  ? 148 GLY   B O   1 
ATOM   1437 N N   . LEU   B 2 140 ? -18.063 -3.354  -16.124 1.00 32.81  ? 149 LEU   B N   1 
ATOM   1438 C CA  . LEU   B 2 140 ? -17.791 -1.927  -16.387 1.00 32.81  ? 149 LEU   B CA  1 
ATOM   1439 C C   . LEU   B 2 140 ? -16.291 -1.791  -16.626 1.00 33.43  ? 149 LEU   B C   1 
ATOM   1440 O O   . LEU   B 2 140 ? -15.487 -2.540  -16.015 1.00 32.49  ? 149 LEU   B O   1 
ATOM   1441 C CB  . LEU   B 2 140 ? -18.250 -1.011  -15.237 1.00 32.34  ? 149 LEU   B CB  1 
ATOM   1442 C CG  . LEU   B 2 140 ? -19.715 -1.076  -14.809 1.00 31.83  ? 149 LEU   B CG  1 
ATOM   1443 C CD1 . LEU   B 2 140 ? -20.000 0.033   -13.765 1.00 31.71  ? 149 LEU   B CD1 1 
ATOM   1444 C CD2 . LEU   B 2 140 ? -20.676 -0.977  -15.994 1.00 32.27  ? 149 LEU   B CD2 1 
ATOM   1445 N N   . TYR   B 2 141 ? -15.963 -0.893  -17.561 1.00 33.68  ? 150 TYR   B N   1 
ATOM   1446 C CA  . TYR   B 2 141 ? -14.594 -0.576  -18.008 1.00 35.32  ? 150 TYR   B CA  1 
ATOM   1447 C C   . TYR   B 2 141 ? -14.092 0.616   -17.200 1.00 35.79  ? 150 TYR   B C   1 
ATOM   1448 O O   . TYR   B 2 141 ? -14.893 1.574   -17.067 1.00 37.04  ? 150 TYR   B O   1 
ATOM   1449 C CB  . TYR   B 2 141 ? -14.696 -0.130  -19.494 1.00 36.49  ? 150 TYR   B CB  1 
ATOM   1450 C CG  . TYR   B 2 141 ? -13.458 0.518   -20.059 1.00 37.62  ? 150 TYR   B CG  1 
ATOM   1451 C CD1 . TYR   B 2 141 ? -13.296 1.899   -20.020 1.00 38.07  ? 150 TYR   B CD1 1 
ATOM   1452 C CD2 . TYR   B 2 141 ? -12.465 -0.253  -20.669 1.00 38.82  ? 150 TYR   B CD2 1 
ATOM   1453 C CE1 . TYR   B 2 141 ? -12.143 2.491   -20.545 1.00 39.83  ? 150 TYR   B CE1 1 
ATOM   1454 C CE2 . TYR   B 2 141 ? -11.310 0.322   -21.197 1.00 39.54  ? 150 TYR   B CE2 1 
ATOM   1455 C CZ  . TYR   B 2 141 ? -11.145 1.702   -21.131 1.00 40.55  ? 150 TYR   B CZ  1 
ATOM   1456 O OH  . TYR   B 2 141 ? -10.022 2.294   -21.688 1.00 45.17  ? 150 TYR   B OH  1 
ATOM   1457 N N   A GLY   B 2 142 ? -12.833 0.543   -16.683 0.11 36.00  ? 151 GLY   B N   1 
ATOM   1458 N N   B GLY   B 2 142 ? -12.834 0.541   -16.679 0.09 36.00  ? 151 GLY   B N   1 
ATOM   1459 N N   C GLY   B 2 142 ? -12.800 0.570   -16.810 0.41 36.47  ? 151 GLY   B N   1 
ATOM   1460 N N   D GLY   B 2 142 ? -12.801 0.569   -16.806 0.39 36.47  ? 151 GLY   B N   1 
ATOM   1461 C CA  A GLY   B 2 142 ? -12.258 1.662   -15.897 0.11 35.97  ? 151 GLY   B CA  1 
ATOM   1462 C CA  B GLY   B 2 142 ? -12.259 1.662   -15.895 0.09 35.96  ? 151 GLY   B CA  1 
ATOM   1463 C CA  C GLY   B 2 142 ? -12.125 1.725   -16.171 0.41 37.06  ? 151 GLY   B CA  1 
ATOM   1464 C CA  D GLY   B 2 142 ? -12.126 1.725   -16.168 0.39 37.06  ? 151 GLY   B CA  1 
ATOM   1465 C C   A GLY   B 2 142 ? -11.166 1.253   -14.910 0.11 35.92  ? 151 GLY   B C   1 
ATOM   1466 C C   B GLY   B 2 142 ? -11.172 1.256   -14.905 0.09 35.92  ? 151 GLY   B C   1 
ATOM   1467 C C   C GLY   B 2 142 ? -11.366 1.412   -14.876 0.41 37.05  ? 151 GLY   B C   1 
ATOM   1468 C C   D GLY   B 2 142 ? -11.366 1.412   -14.875 0.39 37.04  ? 151 GLY   B C   1 
ATOM   1469 O O   A GLY   B 2 142 ? -10.159 2.058   -14.728 0.11 35.99  ? 151 GLY   B O   1 
ATOM   1470 O O   B GLY   B 2 142 ? -10.178 2.066   -14.732 0.09 36.00  ? 151 GLY   B O   1 
ATOM   1471 O O   C GLY   B 2 142 ? -10.702 2.470   -14.376 0.41 38.27  ? 151 GLY   B O   1 
ATOM   1472 O O   D GLY   B 2 142 ? -10.697 2.470   -14.374 0.39 38.23  ? 151 GLY   B O   1 
ATOM   1473 N N   A ASN   B 2 143 ? -11.328 0.080   -14.259 0.11 35.92  ? 152 ASN   B N   1 
ATOM   1474 N N   B ASN   B 2 143 ? -11.327 0.081   -14.256 0.09 35.92  ? 152 ASN   B N   1 
ATOM   1475 N N   C ASN   B 2 143 ? -11.305 0.066   -14.504 0.41 36.93  ? 152 ASN   B N   1 
ATOM   1476 N N   D ASN   B 2 143 ? -11.307 0.066   -14.501 0.39 36.94  ? 152 ASN   B N   1 
ATOM   1477 C CA  A ASN   B 2 143 ? -10.370 -0.368  -13.203 0.11 36.02  ? 152 ASN   B CA  1 
ATOM   1478 C CA  B ASN   B 2 143 ? -10.369 -0.367  -13.200 0.09 36.01  ? 152 ASN   B CA  1 
ATOM   1479 C CA  C ASN   B 2 143 ? -10.410 -0.320  -13.356 0.41 37.10  ? 152 ASN   B CA  1 
ATOM   1480 C CA  D ASN   B 2 143 ? -10.411 -0.320  -13.353 0.39 37.10  ? 152 ASN   B CA  1 
ATOM   1481 C C   A ASN   B 2 143 ? -9.429  -1.434  -13.838 0.11 36.48  ? 152 ASN   B C   1 
ATOM   1482 C C   B ASN   B 2 143 ? -9.429  -1.431  -13.834 0.09 36.49  ? 152 ASN   B C   1 
ATOM   1483 C C   C ASN   B 2 143 ? -9.510  -1.561  -13.927 0.41 36.91  ? 152 ASN   B C   1 
ATOM   1484 C C   D ASN   B 2 143 ? -9.511  -1.563  -13.928 0.39 36.93  ? 152 ASN   B C   1 
ATOM   1485 O O   A ASN   B 2 143 ? -9.953  -2.615  -14.457 0.11 36.69  ? 152 ASN   B O   1 
ATOM   1486 O O   B ASN   B 2 143 ? -9.955  -2.610  -14.454 0.09 36.68  ? 152 ASN   B O   1 
ATOM   1487 O O   C ASN   B 2 143 ? -9.963  -2.727  -14.429 0.41 37.83  ? 152 ASN   B O   1 
ATOM   1488 O O   D ASN   B 2 143 ? -9.964  -2.731  -14.429 0.39 37.81  ? 152 ASN   B O   1 
ATOM   1489 C CB  A ASN   B 2 143 ? -11.081 -0.883  -11.944 0.11 35.58  ? 152 ASN   B CB  1 
ATOM   1490 C CB  B ASN   B 2 143 ? -11.082 -0.880  -11.941 0.09 35.58  ? 152 ASN   B CB  1 
ATOM   1491 C CB  C ASN   B 2 143 ? -11.134 -0.660  -12.042 0.41 36.73  ? 152 ASN   B CB  1 
ATOM   1492 C CB  D ASN   B 2 143 ? -11.135 -0.657  -12.039 0.39 36.73  ? 152 ASN   B CB  1 
ATOM   1493 C CG  A ASN   B 2 143 ? -10.177 -0.879  -10.730 0.11 35.55  ? 152 ASN   B CG  1 
ATOM   1494 C CG  B ASN   B 2 143 ? -10.178 -0.878  -10.726 0.09 35.53  ? 152 ASN   B CG  1 
ATOM   1495 C CG  C ASN   B 2 143 ? -10.158 -0.746  -10.883 0.41 36.95  ? 152 ASN   B CG  1 
ATOM   1496 C CG  D ASN   B 2 143 ? -10.159 -0.746  -10.879 0.39 36.94  ? 152 ASN   B CG  1 
ATOM   1497 O OD1 A ASN   B 2 143 ? -9.204  -0.112  -10.685 0.11 35.82  ? 152 ASN   B OD1 1 
ATOM   1498 O OD1 B ASN   B 2 143 ? -9.207  -0.111  -10.676 0.09 35.80  ? 152 ASN   B OD1 1 
ATOM   1499 O OD1 C ASN   B 2 143 ? -10.336 -1.574  -9.971  0.41 36.45  ? 152 ASN   B OD1 1 
ATOM   1500 O OD1 D ASN   B 2 143 ? -10.335 -1.577  -9.970  0.39 36.45  ? 152 ASN   B OD1 1 
ATOM   1501 N ND2 A ASN   B 2 143 ? -10.477 -1.739  -9.758  0.11 35.25  ? 152 ASN   B ND2 1 
ATOM   1502 N ND2 B ASN   B 2 143 ? -10.477 -1.739  -9.756  0.09 35.25  ? 152 ASN   B ND2 1 
ATOM   1503 N ND2 C ASN   B 2 143 ? -9.134  0.105   -10.924 0.41 36.93  ? 152 ASN   B ND2 1 
ATOM   1504 N ND2 D ASN   B 2 143 ? -9.136  0.105   -10.920 0.39 36.94  ? 152 ASN   B ND2 1 
ATOM   1505 N N   . GLY   B 2 144 ? -8.104  -0.985  -13.957 1.00 36.98  ? 153 GLY   B N   1 
ATOM   1506 C CA  . GLY   B 2 144 ? -7.089  -1.931  -14.458 1.00 38.41  ? 153 GLY   B CA  1 
ATOM   1507 C C   . GLY   B 2 144 ? -5.687  -1.402  -14.283 1.00 40.39  ? 153 GLY   B C   1 
ATOM   1508 O O   . GLY   B 2 144 ? -5.378  -0.857  -13.186 1.00 39.70  ? 153 GLY   B O   1 
ATOM   1509 N N   . VAL   B 2 145 ? -4.831  -1.608  -15.299 1.00 41.99  ? 154 VAL   B N   1 
ATOM   1510 C CA  . VAL   B 2 145 ? -3.365  -1.451  -15.139 1.00 44.06  ? 154 VAL   B CA  1 
ATOM   1511 C C   . VAL   B 2 145 ? -2.758  -0.839  -16.411 1.00 48.52  ? 154 VAL   B C   1 
ATOM   1512 O O   . VAL   B 2 145 ? -3.335  -1.045  -17.498 1.00 45.70  ? 154 VAL   B O   1 
ATOM   1513 C CB  . VAL   B 2 145 ? -2.799  -2.827  -14.761 1.00 45.42  ? 154 VAL   B CB  1 
ATOM   1514 C CG1 . VAL   B 2 145 ? -2.616  -3.779  -15.926 1.00 44.87  ? 154 VAL   B CG1 1 
ATOM   1515 C CG2 . VAL   B 2 145 ? -1.545  -2.692  -13.930 1.00 47.48  ? 154 VAL   B CG2 1 
ATOM   1516 N N   . VAL   B 2 146 ? -1.652  -0.107  -16.241 1.00 52.40  ? 155 VAL   B N   1 
ATOM   1517 C CA  . VAL   B 2 146 ? -0.810  0.441   -17.343 1.00 56.39  ? 155 VAL   B CA  1 
ATOM   1518 C C   . VAL   B 2 146 ? 0.258   -0.601  -17.655 1.00 58.81  ? 155 VAL   B C   1 
ATOM   1519 O O   . VAL   B 2 146 ? 0.854   -1.102  -16.708 1.00 57.06  ? 155 VAL   B O   1 
ATOM   1520 C CB  . VAL   B 2 146 ? -0.234  1.807   -16.934 1.00 57.79  ? 155 VAL   B CB  1 
ATOM   1521 C CG1 . VAL   B 2 146 ? 0.668   2.393   -17.998 1.00 59.72  ? 155 VAL   B CG1 1 
ATOM   1522 C CG2 . VAL   B 2 146 ? -1.361  2.780   -16.621 1.00 58.76  ? 155 VAL   B CG2 1 
ATOM   1523 N N   . ILE   B 2 147 ? 0.457   -0.968  -18.930 1.00 64.75  ? 156 ILE   B N   1 
ATOM   1524 C CA  . ILE   B 2 147 ? 1.282   -2.170  -19.261 1.00 69.81  ? 156 ILE   B CA  1 
ATOM   1525 C C   . ILE   B 2 147 ? 2.640   -1.709  -19.792 1.00 75.30  ? 156 ILE   B C   1 
ATOM   1526 O O   . ILE   B 2 147 ? 2.830   -0.497  -19.994 1.00 75.40  ? 156 ILE   B O   1 
ATOM   1527 C CB  . ILE   B 2 147 ? 0.532   -3.141  -20.200 1.00 70.87  ? 156 ILE   B CB  1 
ATOM   1528 C CG1 . ILE   B 2 147 ? -0.003  -2.479  -21.480 1.00 71.40  ? 156 ILE   B CG1 1 
ATOM   1529 C CG2 . ILE   B 2 147 ? -0.578  -3.839  -19.429 1.00 70.09  ? 156 ILE   B CG2 1 
ATOM   1530 C CD1 . ILE   B 2 147 ? -0.330  -3.460  -22.575 1.00 70.52  ? 156 ILE   B CD1 1 
ATOM   1531 N N   A LYS   B 2 148 ? 3.556   -2.663  -20.004 0.11 76.66  ? 157 LYS   B N   1 
ATOM   1532 N N   B LYS   B 2 148 ? 3.555   -2.663  -20.004 0.09 76.65  ? 157 LYS   B N   1 
ATOM   1533 N N   C LYS   B 2 148 ? 3.565   -2.660  -19.972 0.41 78.15  ? 157 LYS   B N   1 
ATOM   1534 N N   D LYS   B 2 148 ? 3.565   -2.660  -19.972 0.39 78.14  ? 157 LYS   B N   1 
ATOM   1535 C CA  A LYS   B 2 148 ? 4.929   -2.438  -20.538 0.11 78.93  ? 157 LYS   B CA  1 
ATOM   1536 C CA  B LYS   B 2 148 ? 4.929   -2.438  -20.539 0.09 78.92  ? 157 LYS   B CA  1 
ATOM   1537 C CA  C LYS   B 2 148 ? 4.925   -2.428  -20.532 0.41 81.45  ? 157 LYS   B CA  1 
ATOM   1538 C CA  D LYS   B 2 148 ? 4.925   -2.428  -20.532 0.39 81.43  ? 157 LYS   B CA  1 
ATOM   1539 C C   A LYS   B 2 148 ? 4.899   -1.351  -21.621 0.11 80.41  ? 157 LYS   B C   1 
ATOM   1540 C C   B LYS   B 2 148 ? 4.899   -1.351  -21.621 0.09 80.38  ? 157 LYS   B C   1 
ATOM   1541 C C   C LYS   B 2 148 ? 4.864   -1.314  -21.584 0.41 82.66  ? 157 LYS   B C   1 
ATOM   1542 C C   D LYS   B 2 148 ? 4.864   -1.314  -21.585 0.39 82.62  ? 157 LYS   B C   1 
ATOM   1543 O O   A LYS   B 2 148 ? 5.799   -0.488  -21.617 0.11 81.85  ? 157 LYS   B O   1 
ATOM   1544 O O   B LYS   B 2 148 ? 5.799   -0.488  -21.618 0.09 81.77  ? 157 LYS   B O   1 
ATOM   1545 O O   C LYS   B 2 148 ? 5.684   -0.382  -21.502 0.41 86.03  ? 157 LYS   B O   1 
ATOM   1546 O O   D LYS   B 2 148 ? 5.685   -0.383  -21.503 0.39 85.91  ? 157 LYS   B O   1 
ATOM   1547 C CB  A LYS   B 2 148 ? 5.496   -3.739  -21.115 0.11 79.87  ? 157 LYS   B CB  1 
ATOM   1548 C CB  B LYS   B 2 148 ? 5.496   -3.739  -21.116 0.09 79.86  ? 157 LYS   B CB  1 
ATOM   1549 C CB  C LYS   B 2 148 ? 5.472   -3.713  -21.159 0.41 83.73  ? 157 LYS   B CB  1 
ATOM   1550 C CB  D LYS   B 2 148 ? 5.472   -3.714  -21.159 0.39 83.70  ? 157 LYS   B CB  1 
ATOM   1551 C CG  A LYS   B 2 148 ? 5.834   -4.817  -20.093 0.11 79.81  ? 157 LYS   B CG  1 
ATOM   1552 C CG  B LYS   B 2 148 ? 5.835   -4.817  -20.093 0.09 79.79  ? 157 LYS   B CG  1 
ATOM   1553 C CG  C LYS   B 2 148 ? 5.805   -4.829  -20.177 0.41 85.05  ? 157 LYS   B CG  1 
ATOM   1554 C CG  D LYS   B 2 148 ? 5.806   -4.829  -20.177 0.39 85.01  ? 157 LYS   B CG  1 
ATOM   1555 C CD  A LYS   B 2 148 ? 6.068   -6.185  -20.706 0.11 80.52  ? 157 LYS   B CD  1 
ATOM   1556 C CD  B LYS   B 2 148 ? 6.069   -6.184  -20.706 0.09 80.51  ? 157 LYS   B CD  1 
ATOM   1557 C CD  C LYS   B 2 148 ? 6.209   -6.127  -20.851 0.41 86.92  ? 157 LYS   B CD  1 
ATOM   1558 C CD  D LYS   B 2 148 ? 6.210   -6.127  -20.851 0.39 86.87  ? 157 LYS   B CD  1 
ATOM   1559 C CE  A LYS   B 2 148 ? 7.354   -6.280  -21.502 0.11 81.93  ? 157 LYS   B CE  1 
ATOM   1560 C CE  B LYS   B 2 148 ? 7.354   -6.281  -21.503 0.09 81.90  ? 157 LYS   B CE  1 
ATOM   1561 C CE  C LYS   B 2 148 ? 7.434   -5.986  -21.733 0.41 89.57  ? 157 LYS   B CE  1 
ATOM   1562 C CE  D LYS   B 2 148 ? 7.435   -5.986  -21.733 0.39 89.49  ? 157 LYS   B CE  1 
ATOM   1563 N NZ  A LYS   B 2 148 ? 8.549   -6.301  -20.625 0.11 82.06  ? 157 LYS   B NZ  1 
ATOM   1564 N NZ  B LYS   B 2 148 ? 8.549   -6.301  -20.626 0.09 82.05  ? 157 LYS   B NZ  1 
ATOM   1565 N NZ  C LYS   B 2 148 ? 7.956   -7.302  -22.173 0.41 90.91  ? 157 LYS   B NZ  1 
ATOM   1566 N NZ  D LYS   B 2 148 ? 7.956   -7.302  -22.173 0.39 90.83  ? 157 LYS   B NZ  1 
ATOM   1567 N N   . ASN   B 2 149 ? 3.892   -1.398  -22.501 1.00 81.72  ? 158 ASN   B N   1 
ATOM   1568 C CA  . ASN   B 2 149 ? 3.747   -0.485  -23.671 1.00 79.54  ? 158 ASN   B CA  1 
ATOM   1569 C C   . ASN   B 2 149 ? 3.341   0.961   -23.336 1.00 75.85  ? 158 ASN   B C   1 
ATOM   1570 O O   . ASN   B 2 149 ? 3.506   1.848   -24.201 1.00 76.53  ? 158 ASN   B O   1 
ATOM   1571 C CB  . ASN   B 2 149 ? 2.657   -0.984  -24.633 1.00 82.89  ? 158 ASN   B CB  1 
ATOM   1572 C CG  . ASN   B 2 149 ? 2.505   -2.492  -24.678 1.00 83.46  ? 158 ASN   B CG  1 
ATOM   1573 O OD1 . ASN   B 2 149 ? 3.261   -3.220  -24.033 1.00 84.99  ? 158 ASN   B OD1 1 
ATOM   1574 N ND2 . ASN   B 2 149 ? 1.535   -2.971  -25.445 1.00 85.52  ? 158 ASN   B ND2 1 
ATOM   1575 N N   A GLY   B 2 150 ? 2.824   1.191   -22.125 0.11 73.15  ? 159 GLY   B N   1 
ATOM   1576 N N   B GLY   B 2 150 ? 2.822   1.189   -22.126 0.09 73.14  ? 159 GLY   B N   1 
ATOM   1577 N N   C GLY   B 2 150 ? 2.756   1.176   -22.152 0.41 73.66  ? 159 GLY   B N   1 
ATOM   1578 N N   D GLY   B 2 150 ? 2.759   1.180   -22.151 0.39 73.59  ? 159 GLY   B N   1 
ATOM   1579 C CA  A GLY   B 2 150 ? 2.255   2.486   -21.704 0.11 70.85  ? 159 GLY   B CA  1 
ATOM   1580 C CA  B GLY   B 2 150 ? 2.254   2.485   -21.705 0.09 70.87  ? 159 GLY   B CA  1 
ATOM   1581 C CA  C GLY   B 2 150 ? 2.256   2.490   -21.695 0.41 70.97  ? 159 GLY   B CA  1 
ATOM   1582 C CA  D GLY   B 2 150 ? 2.256   2.494   -21.694 0.39 70.87  ? 159 GLY   B CA  1 
ATOM   1583 C C   A GLY   B 2 150 ? 0.761   2.548   -21.977 0.11 68.62  ? 159 GLY   B C   1 
ATOM   1584 C C   B GLY   B 2 150 ? 0.760   2.553   -21.977 0.09 68.63  ? 159 GLY   B C   1 
ATOM   1585 C C   C GLY   B 2 150 ? 0.744   2.627   -21.838 0.41 68.91  ? 159 GLY   B C   1 
ATOM   1586 C C   D GLY   B 2 150 ? 0.742   2.616   -21.834 0.39 68.73  ? 159 GLY   B C   1 
ATOM   1587 O O   A GLY   B 2 150 ? 0.101   3.466   -21.443 0.11 67.64  ? 159 GLY   B O   1 
ATOM   1588 O O   B GLY   B 2 150 ? 0.104   3.466   -21.436 0.09 67.68  ? 159 GLY   B O   1 
ATOM   1589 O O   C GLY   B 2 150 ? 0.184   3.596   -21.262 0.41 66.31  ? 159 GLY   B O   1 
ATOM   1590 O O   D GLY   B 2 150 ? 0.173   3.593   -21.276 0.39 66.29  ? 159 GLY   B O   1 
ATOM   1591 N N   A SER   B 2 151 ? 0.249   1.600   -22.775 0.11 66.64  ? 160 SER   B N   1 
ATOM   1592 N N   B SER   B 2 151 ? 0.238   1.627   -22.791 0.09 66.69  ? 160 SER   B N   1 
ATOM   1593 N N   C SER   B 2 151 ? 0.092   1.714   -22.574 0.41 67.15  ? 160 SER   B N   1 
ATOM   1594 N N   D SER   B 2 151 ? 0.115   1.640   -22.515 0.39 66.68  ? 160 SER   B N   1 
ATOM   1595 C CA  A SER   B 2 151 ? -1.195  1.386   -23.059 0.11 64.35  ? 160 SER   B CA  1 
ATOM   1596 C CA  B SER   B 2 151 ? -1.213  1.451   -23.058 0.09 64.43  ? 160 SER   B CA  1 
ATOM   1597 C CA  C SER   B 2 151 ? -1.385  1.681   -22.762 0.41 64.61  ? 160 SER   B CA  1 
ATOM   1598 C CA  D SER   B 2 151 ? -1.348  1.524   -22.776 0.39 64.09  ? 160 SER   B CA  1 
ATOM   1599 C C   A SER   B 2 151 ? -1.902  0.900   -21.788 0.11 61.80  ? 160 SER   B C   1 
ATOM   1600 C C   B SER   B 2 151 ? -1.905  0.925   -21.795 0.09 61.85  ? 160 SER   B C   1 
ATOM   1601 C C   C SER   B 2 151 ? -2.081  1.262   -21.451 0.41 62.45  ? 160 SER   B C   1 
ATOM   1602 C C   D SER   B 2 151 ? -2.096  1.028   -21.523 0.39 62.29  ? 160 SER   B C   1 
ATOM   1603 O O   A SER   B 2 151 ? -1.209  0.417   -20.864 0.11 61.23  ? 160 SER   B O   1 
ATOM   1604 O O   B SER   B 2 151 ? -1.201  0.436   -20.884 0.09 61.35  ? 160 SER   B O   1 
ATOM   1605 O O   C SER   B 2 151 ? -1.368  0.932   -20.470 0.41 60.21  ? 160 SER   B O   1 
ATOM   1606 O O   D SER   B 2 151 ? -1.444  0.383   -20.667 0.39 60.86  ? 160 SER   B O   1 
ATOM   1607 C CB  A SER   B 2 151 ? -1.383  0.416   -24.201 0.11 64.98  ? 160 SER   B CB  1 
ATOM   1608 C CB  B SER   B 2 151 ? -1.445  0.540   -24.235 0.09 65.11  ? 160 SER   B CB  1 
ATOM   1609 C CB  C SER   B 2 151 ? -1.757  0.767   -23.903 0.41 65.11  ? 160 SER   B CB  1 
ATOM   1610 C CB  D SER   B 2 151 ? -1.569  0.585   -23.927 0.39 64.14  ? 160 SER   B CB  1 
ATOM   1611 O OG  A SER   B 2 151 ? -2.750  0.321   -24.573 0.11 64.53  ? 160 SER   B OG  1 
ATOM   1612 O OG  B SER   B 2 151 ? -0.780  -0.699  -24.048 0.09 65.31  ? 160 SER   B OG  1 
ATOM   1613 O OG  C SER   B 2 151 ? -3.129  0.908   -24.240 0.41 65.08  ? 160 SER   B OG  1 
ATOM   1614 O OG  D SER   B 2 151 ? -0.789  -0.590  -23.744 0.39 63.34  ? 160 SER   B OG  1 
ATOM   1615 N N   A TYR   B 2 152 ? -3.231  1.021   -21.752 0.11 59.13  ? 161 TYR   B N   1 
ATOM   1616 N N   B TYR   B 2 152 ? -3.235  1.023   -21.754 0.09 59.15  ? 161 TYR   B N   1 
ATOM   1617 N N   C TYR   B 2 152 ? -3.420  1.291   -21.440 0.41 60.67  ? 161 TYR   B N   1 
ATOM   1618 N N   D TYR   B 2 152 ? -3.411  1.288   -21.436 0.39 60.63  ? 161 TYR   B N   1 
ATOM   1619 C CA  A TYR   B 2 152 ? -4.083  0.730   -20.569 0.11 56.73  ? 161 TYR   B CA  1 
ATOM   1620 C CA  B TYR   B 2 152 ? -4.082  0.730   -20.569 0.09 56.72  ? 161 TYR   B CA  1 
ATOM   1621 C CA  C TYR   B 2 152 ? -4.292  0.852   -20.314 0.41 58.86  ? 161 TYR   B CA  1 
ATOM   1622 C CA  D TYR   B 2 152 ? -4.293  0.852   -20.316 0.39 58.82  ? 161 TYR   B CA  1 
ATOM   1623 C C   A TYR   B 2 152 ? -4.877  -0.561  -20.803 0.11 54.93  ? 161 TYR   B C   1 
ATOM   1624 C C   B TYR   B 2 152 ? -4.877  -0.560  -20.802 0.09 54.93  ? 161 TYR   B C   1 
ATOM   1625 C C   C TYR   B 2 152 ? -5.006  -0.451  -20.699 0.41 56.30  ? 161 TYR   B C   1 
ATOM   1626 C C   D TYR   B 2 152 ? -5.006  -0.451  -20.700 0.39 56.27  ? 161 TYR   B C   1 
ATOM   1627 O O   A TYR   B 2 152 ? -5.351  -0.770  -21.934 0.11 55.10  ? 161 TYR   B O   1 
ATOM   1628 O O   B TYR   B 2 152 ? -5.354  -0.767  -21.934 0.09 55.12  ? 161 TYR   B O   1 
ATOM   1629 O O   C TYR   B 2 152 ? -5.538  -0.570  -21.809 0.41 55.87  ? 161 TYR   B O   1 
ATOM   1630 O O   D TYR   B 2 152 ? -5.537  -0.570  -21.811 0.39 55.88  ? 161 TYR   B O   1 
ATOM   1631 C CB  A TYR   B 2 152 ? -5.014  1.911   -20.295 0.11 56.34  ? 161 TYR   B CB  1 
ATOM   1632 C CB  B TYR   B 2 152 ? -5.013  1.911   -20.293 0.09 56.33  ? 161 TYR   B CB  1 
ATOM   1633 C CB  C TYR   B 2 152 ? -5.314  1.927   -19.923 0.41 59.91  ? 161 TYR   B CB  1 
ATOM   1634 C CB  D TYR   B 2 152 ? -5.313  1.928   -19.925 0.39 59.88  ? 161 TYR   B CB  1 
ATOM   1635 C CG  A TYR   B 2 152 ? -5.985  1.659   -19.174 0.11 55.42  ? 161 TYR   B CG  1 
ATOM   1636 C CG  B TYR   B 2 152 ? -5.985  1.659   -19.172 0.09 55.42  ? 161 TYR   B CG  1 
ATOM   1637 C CG  C TYR   B 2 152 ? -5.841  1.822   -18.509 0.41 60.56  ? 161 TYR   B CG  1 
ATOM   1638 C CG  D TYR   B 2 152 ? -5.840  1.823   -18.510 0.39 60.52  ? 161 TYR   B CG  1 
ATOM   1639 C CD1 A TYR   B 2 152 ? -5.535  1.488   -17.874 0.11 54.90  ? 161 TYR   B CD1 1 
ATOM   1640 C CD1 B TYR   B 2 152 ? -5.534  1.488   -17.873 0.09 54.91  ? 161 TYR   B CD1 1 
ATOM   1641 C CD1 C TYR   B 2 152 ? -5.072  2.226   -17.428 0.41 60.57  ? 161 TYR   B CD1 1 
ATOM   1642 C CD1 D TYR   B 2 152 ? -5.071  2.227   -17.430 0.39 60.55  ? 161 TYR   B CD1 1 
ATOM   1643 C CD2 A TYR   B 2 152 ? -7.346  1.557   -19.413 0.11 54.96  ? 161 TYR   B CD2 1 
ATOM   1644 C CD2 B TYR   B 2 152 ? -7.346  1.558   -19.411 0.09 54.96  ? 161 TYR   B CD2 1 
ATOM   1645 C CD2 C TYR   B 2 152 ? -7.112  1.335   -18.237 0.41 60.46  ? 161 TYR   B CD2 1 
ATOM   1646 C CD2 D TYR   B 2 152 ? -7.111  1.336   -18.238 0.39 60.43  ? 161 TYR   B CD2 1 
ATOM   1647 C CE1 A TYR   B 2 152 ? -6.414  1.240   -16.835 0.11 54.23  ? 161 TYR   B CE1 1 
ATOM   1648 C CE1 B TYR   B 2 152 ? -6.412  1.240   -16.833 0.09 54.22  ? 161 TYR   B CE1 1 
ATOM   1649 C CE1 C TYR   B 2 152 ? -5.538  2.139   -16.124 0.41 60.95  ? 161 TYR   B CE1 1 
ATOM   1650 C CE1 D TYR   B 2 152 ? -5.537  2.140   -16.125 0.39 60.89  ? 161 TYR   B CE1 1 
ATOM   1651 C CE2 A TYR   B 2 152 ? -8.239  1.310   -18.384 0.11 54.09  ? 161 TYR   B CE2 1 
ATOM   1652 C CE2 B TYR   B 2 152 ? -8.238  1.312   -18.381 0.09 54.10  ? 161 TYR   B CE2 1 
ATOM   1653 C CE2 C TYR   B 2 152 ? -7.597  1.247   -16.937 0.41 60.19  ? 161 TYR   B CE2 1 
ATOM   1654 C CE2 D TYR   B 2 152 ? -7.596  1.248   -16.939 0.39 60.15  ? 161 TYR   B CE2 1 
ATOM   1655 C CZ  A TYR   B 2 152 ? -7.771  1.154   -17.091 0.11 53.82  ? 161 TYR   B CZ  1 
ATOM   1656 C CZ  B TYR   B 2 152 ? -7.769  1.154   -17.088 0.09 53.82  ? 161 TYR   B CZ  1 
ATOM   1657 C CZ  C TYR   B 2 152 ? -6.808  1.646   -15.868 0.41 60.17  ? 161 TYR   B CZ  1 
ATOM   1658 C CZ  D TYR   B 2 152 ? -6.807  1.647   -15.870 0.39 60.13  ? 161 TYR   B CZ  1 
ATOM   1659 O OH  A TYR   B 2 152 ? -8.646  0.907   -16.076 0.11 52.82  ? 161 TYR   B OH  1 
ATOM   1660 O OH  B TYR   B 2 152 ? -8.643  0.908   -16.072 0.09 52.85  ? 161 TYR   B OH  1 
ATOM   1661 O OH  C TYR   B 2 152 ? -7.264  1.566   -14.572 0.41 57.97  ? 161 TYR   B OH  1 
ATOM   1662 O OH  D TYR   B 2 152 ? -7.263  1.566   -14.575 0.39 58.00  ? 161 TYR   B OH  1 
ATOM   1663 N N   . VAL   B 2 153 ? -5.001  -1.407  -19.771 1.00 53.06  ? 162 VAL   B N   1 
ATOM   1664 C CA  . VAL   B 2 153 ? -5.800  -2.656  -19.855 1.00 48.84  ? 162 VAL   B CA  1 
ATOM   1665 C C   . VAL   B 2 153 ? -6.751  -2.640  -18.646 1.00 45.12  ? 162 VAL   B C   1 
ATOM   1666 O O   . VAL   B 2 153 ? -6.246  -2.597  -17.509 1.00 43.51  ? 162 VAL   B O   1 
ATOM   1667 C CB  . VAL   B 2 153 ? -4.878  -3.883  -19.851 1.00 47.46  ? 162 VAL   B CB  1 
ATOM   1668 C CG1 . VAL   B 2 153 ? -5.674  -5.167  -20.015 1.00 46.40  ? 162 VAL   B CG1 1 
ATOM   1669 C CG2 . VAL   B 2 153 ? -3.767  -3.765  -20.893 1.00 50.59  ? 162 VAL   B CG2 1 
ATOM   1670 N N   . SER   B 2 154 ? -8.057  -2.675  -18.906 1.00 42.84  ? 163 SER   B N   1 
ATOM   1671 C CA  . SER   B 2 154 ? -9.133  -2.616  -17.882 1.00 40.30  ? 163 SER   B CA  1 
ATOM   1672 C C   . SER   B 2 154 ? -9.611  -4.061  -17.586 1.00 39.61  ? 163 SER   B C   1 
ATOM   1673 O O   . SER   B 2 154 ? -9.807  -4.862  -18.509 1.00 39.17  ? 163 SER   B O   1 
ATOM   1674 C CB  . SER   B 2 154 ? -10.300 -1.748  -18.294 1.00 39.71  ? 163 SER   B CB  1 
ATOM   1675 O OG  . SER   B 2 154 ? -11.437 -1.888  -17.370 1.00 38.57  ? 163 SER   B OG  1 
ATOM   1676 N N   . ALA   B 2 155 ? -9.843  -4.341  -16.288 1.00 37.38  ? 164 ALA   B N   1 
ATOM   1677 C CA  . ALA   B 2 155 ? -10.648 -5.519  -15.914 1.00 37.11  ? 164 ALA   B CA  1 
ATOM   1678 C C   . ALA   B 2 155 ? -12.045 -5.302  -16.638 1.00 37.67  ? 164 ALA   B C   1 
ATOM   1679 O O   . ALA   B 2 155 ? -12.479 -4.139  -16.834 1.00 39.96  ? 164 ALA   B O   1 
ATOM   1680 C CB  . ALA   B 2 155 ? -10.714 -5.646  -14.343 1.00 36.43  ? 164 ALA   B CB  1 
ATOM   1681 N N   . ILE   B 2 156 ? -12.703 -6.442  -16.940 1.00 38.06  ? 165 ILE   B N   1 
ATOM   1682 C CA  . ILE   B 2 156 ? -14.211 -6.454  -16.843 1.00 37.55  ? 165 ILE   B CA  1 
ATOM   1683 C C   . ILE   B 2 156 ? -14.749 -6.580  -15.425 1.00 35.95  ? 165 ILE   B C   1 
ATOM   1684 O O   . ILE   B 2 156 ? -14.886 -7.765  -14.951 1.00 37.46  ? 165 ILE   B O   1 
ATOM   1685 C CB  . ILE   B 2 156 ? -14.660 -7.670  -17.686 1.00 37.88  ? 165 ILE   B CB  1 
ATOM   1686 C CG1 . ILE   B 2 156 ? -13.937 -7.633  -19.041 1.00 39.28  ? 165 ILE   B CG1 1 
ATOM   1687 C CG2 . ILE   B 2 156 ? -16.194 -7.705  -17.816 1.00 37.85  ? 165 ILE   B CG2 1 
ATOM   1688 C CD1 . ILE   B 2 156 ? -14.310 -8.779  -19.910 1.00 39.47  ? 165 ILE   B CD1 1 
ATOM   1689 N N   . THR   B 2 157 ? -14.979 -5.446  -14.752 1.00 35.51  ? 166 THR   B N   1 
ATOM   1690 C CA  . THR   B 2 157 ? -15.443 -5.431  -13.324 1.00 33.57  ? 166 THR   B CA  1 
ATOM   1691 C C   . THR   B 2 157 ? -16.985 -5.656  -13.313 1.00 33.63  ? 166 THR   B C   1 
ATOM   1692 O O   . THR   B 2 157 ? -17.749 -4.780  -13.867 1.00 33.92  ? 166 THR   B O   1 
ATOM   1693 C CB  . THR   B 2 157 ? -15.046 -4.116  -12.645 1.00 33.71  ? 166 THR   B CB  1 
ATOM   1694 O OG1 . THR   B 2 157 ? -13.570 -3.925  -12.888 1.00 34.12  ? 166 THR   B OG1 1 
ATOM   1695 C CG2 . THR   B 2 157 ? -15.542 -4.070  -11.199 1.00 32.96  ? 166 THR   B CG2 1 
ATOM   1696 N N   . GLN   B 2 158 ? -17.446 -6.830  -12.686 1.00 32.50  ? 167 GLN   B N   1 
ATOM   1697 C CA  . GLN   B 2 158 ? -18.877 -7.119  -12.465 1.00 32.72  ? 167 GLN   B CA  1 
ATOM   1698 C C   . GLN   B 2 158 ? -19.165 -7.181  -10.949 1.00 33.76  ? 167 GLN   B C   1 
ATOM   1699 O O   . GLN   B 2 158 ? -18.290 -7.656  -10.250 1.00 32.07  ? 167 GLN   B O   1 
ATOM   1700 C CB  . GLN   B 2 158 ? -19.216 -8.464  -13.087 1.00 33.06  ? 167 GLN   B CB  1 
ATOM   1701 C CG  . GLN   B 2 158 ? -20.696 -8.806  -13.136 1.00 33.08  ? 167 GLN   B CG  1 
ATOM   1702 C CD  . GLN   B 2 158 ? -21.565 -7.686  -13.671 1.00 33.22  ? 167 GLN   B CD  1 
ATOM   1703 O OE1 . GLN   B 2 158 ? -21.684 -6.596  -13.083 1.00 32.73  ? 167 GLN   B OE1 1 
ATOM   1704 N NE2 . GLN   B 2 158 ? -22.190 -7.948  -14.813 1.00 32.91  ? 167 GLN   B NE2 1 
ATOM   1705 N N   . GLY   B 2 159 ? -20.340 -6.755  -10.512 1.00 35.57  ? 168 GLY   B N   1 
ATOM   1706 C CA  . GLY   B 2 159 ? -20.746 -6.903  -9.095  1.00 38.47  ? 168 GLY   B CA  1 
ATOM   1707 C C   . GLY   B 2 159 ? -21.445 -8.226  -8.906  1.00 42.31  ? 168 GLY   B C   1 
ATOM   1708 O O   . GLY   B 2 159 ? -21.345 -9.090  -9.760  1.00 46.22  ? 168 GLY   B O   1 
ATOM   1709 N N   . LYS   B 2 160 ? -22.127 -8.408  -7.787  1.00 47.83  ? 169 LYS   B N   1 
ATOM   1710 C CA  . LYS   B 2 160 ? -22.950 -9.609  -7.514  1.00 52.47  ? 169 LYS   B CA  1 
ATOM   1711 C C   . LYS   B 2 160 ? -24.380 -9.101  -7.291  1.00 54.99  ? 169 LYS   B C   1 
ATOM   1712 O O   . LYS   B 2 160 ? -24.529 -8.001  -6.729  1.00 53.94  ? 169 LYS   B O   1 
ATOM   1713 C CB  . LYS   B 2 160 ? -22.350 -10.376 -6.330  1.00 57.06  ? 169 LYS   B CB  1 
ATOM   1714 C CG  . LYS   B 2 160 ? -23.255 -11.449 -5.737  1.00 60.67  ? 169 LYS   B CG  1 
ATOM   1715 C CD  . LYS   B 2 160 ? -22.575 -12.365 -4.738  1.00 62.87  ? 169 LYS   B CD  1 
ATOM   1716 C CE  . LYS   B 2 160 ? -23.482 -13.500 -4.310  1.00 64.75  ? 169 LYS   B CE  1 
ATOM   1717 N NZ  . LYS   B 2 160 ? -23.522 -13.611 -2.836  1.00 67.37  ? 169 LYS   B NZ  1 
ATOM   1718 N N   . ARG   B 2 161 ? -25.392 -9.855  -7.725  1.00 58.22  ? 170 ARG   B N   1 
ATOM   1719 C CA  . ARG   B 2 161 ? -26.830 -9.525  -7.503  1.00 62.67  ? 170 ARG   B CA  1 
ATOM   1720 C C   . ARG   B 2 161 ? -27.360 -10.435 -6.377  1.00 67.50  ? 170 ARG   B C   1 
ATOM   1721 O O   . ARG   B 2 161 ? -27.273 -11.666 -6.532  1.00 67.24  ? 170 ARG   B O   1 
ATOM   1722 C CB  . ARG   B 2 161 ? -27.545 -9.645  -8.857  1.00 63.87  ? 170 ARG   B CB  1 
ATOM   1723 C CG  . ARG   B 2 161 ? -29.030 -9.324  -8.849  1.00 63.68  ? 170 ARG   B CG  1 
ATOM   1724 C CD  . ARG   B 2 161 ? -29.701 -9.803  -10.124 1.00 64.79  ? 170 ARG   B CD  1 
ATOM   1725 N NE  . ARG   B 2 161 ? -31.131 -9.543  -10.052 1.00 66.41  ? 170 ARG   B NE  1 
ATOM   1726 C CZ  . ARG   B 2 161 ? -31.818 -8.698  -10.823 1.00 67.14  ? 170 ARG   B CZ  1 
ATOM   1727 N NH1 . ARG   B 2 161 ? -31.226 -7.998  -11.780 1.00 64.42  ? 170 ARG   B NH1 1 
ATOM   1728 N NH2 . ARG   B 2 161 ? -33.118 -8.560  -10.624 1.00 69.00  ? 170 ARG   B NH2 1 
ATOM   1729 N N   . GLU   B 2 162 ? -27.818 -9.856  -5.259  1.00 74.46  ? 171 GLU   B N   1 
ATOM   1730 C CA  . GLU   B 2 162 ? -28.341 -10.586 -4.066  1.00 79.49  ? 171 GLU   B CA  1 
ATOM   1731 C C   . GLU   B 2 162 ? -29.859 -10.759 -4.203  1.00 80.18  ? 171 GLU   B C   1 
ATOM   1732 O O   . GLU   B 2 162 ? -30.407 -11.894 -4.229  1.00 84.66  ? 171 GLU   B O   1 
ATOM   1733 C CB  . GLU   B 2 162 ? -28.019 -9.823  -2.776  1.00 84.39  ? 171 GLU   B CB  1 
ATOM   1734 C CG  . GLU   B 2 162 ? -26.529 -9.616  -2.502  1.00 87.49  ? 171 GLU   B CG  1 
ATOM   1735 C CD  . GLU   B 2 162 ? -25.828 -10.734 -1.737  1.00 91.71  ? 171 GLU   B CD  1 
ATOM   1736 O OE1 . GLU   B 2 162 ? -25.963 -10.779 -0.488  1.00 90.21  ? 171 GLU   B OE1 1 
ATOM   1737 O OE2 . GLU   B 2 162 ? -25.142 -11.554 -2.391  1.00 96.07  ? 171 GLU   B OE2 1 
HETATM 1738 S S   A DMS   C 3 .   ? -7.882  5.872   -17.911 0.11 46.59  ? 201 DMS   B S   1 
HETATM 1739 S S   B DMS   C 3 .   ? -7.881  5.871   -17.912 0.09 46.60  ? 201 DMS   B S   1 
HETATM 1740 O O   A DMS   C 3 .   ? -6.509  5.270   -18.012 0.11 47.22  ? 201 DMS   B O   1 
HETATM 1741 O O   B DMS   C 3 .   ? -6.508  5.269   -18.012 0.09 47.21  ? 201 DMS   B O   1 
HETATM 1742 C C1  A DMS   C 3 .   ? -8.459  5.530   -16.272 0.11 45.86  ? 201 DMS   B C1  1 
HETATM 1743 C C1  B DMS   C 3 .   ? -8.458  5.531   -16.273 0.09 45.85  ? 201 DMS   B C1  1 
HETATM 1744 C C2  A DMS   C 3 .   ? -8.973  4.775   -18.783 0.11 46.56  ? 201 DMS   B C2  1 
HETATM 1745 C C2  B DMS   C 3 .   ? -8.973  4.774   -18.784 0.09 46.56  ? 201 DMS   B C2  1 
HETATM 1746 S S   A DMS   D 3 .   ? -17.929 11.605  -0.313  0.50 527.21 ? 202 DMS   B S   1 
HETATM 1747 S S   B DMS   D 3 .   ? -17.929 11.605  -0.313  0.50 527.21 ? 202 DMS   B S   1 
HETATM 1748 O O   A DMS   D 3 .   ? -18.350 10.162  -0.323  0.50 521.31 ? 202 DMS   B O   1 
HETATM 1749 O O   B DMS   D 3 .   ? -18.350 10.162  -0.323  0.50 521.31 ? 202 DMS   B O   1 
HETATM 1750 C C1  A DMS   D 3 .   ? -19.398 12.549  -0.628  0.50 522.65 ? 202 DMS   B C1  1 
HETATM 1751 C C1  B DMS   D 3 .   ? -19.398 12.549  -0.628  0.50 522.65 ? 202 DMS   B C1  1 
HETATM 1752 C C2  A DMS   D 3 .   ? -17.122 11.902  -1.865  0.50 512.86 ? 202 DMS   B C2  1 
HETATM 1753 C C2  B DMS   D 3 .   ? -17.122 11.902  -1.865  0.50 512.86 ? 202 DMS   B C2  1 
HETATM 1754 S S   A DMS   E 3 .   ? -7.098  2.618   -13.744 0.11 34.81  ? 203 DMS   B S   1 
HETATM 1755 S S   B DMS   E 3 .   ? -7.100  2.622   -13.745 0.09 34.82  ? 203 DMS   B S   1 
HETATM 1756 O O   A DMS   E 3 .   ? -6.041  1.701   -13.230 0.11 34.97  ? 203 DMS   B O   1 
HETATM 1757 O O   B DMS   E 3 .   ? -6.042  1.700   -13.237 0.09 34.98  ? 203 DMS   B O   1 
HETATM 1758 C C1  A DMS   E 3 .   ? -8.186  2.910   -12.375 0.11 34.15  ? 203 DMS   B C1  1 
HETATM 1759 C C1  B DMS   E 3 .   ? -8.185  2.911   -12.375 0.09 34.15  ? 203 DMS   B C1  1 
HETATM 1760 C C2  A DMS   E 3 .   ? -6.346  4.228   -13.800 0.11 35.21  ? 203 DMS   B C2  1 
HETATM 1761 C C2  B DMS   E 3 .   ? -6.346  4.230   -13.799 0.09 35.22  ? 203 DMS   B C2  1 
HETATM 1762 N N1  C A1BG3 F 4 .   ? -8.698  4.603   -13.846 0.42 62.28  ? 204 A1BG3 B N1  1 
HETATM 1763 N N1  D A1BG3 F 4 .   ? -8.698  4.604   -13.845 0.39 62.30  ? 204 A1BG3 B N1  1 
HETATM 1764 N N3  C A1BG3 F 4 .   ? -8.526  5.631   -10.418 0.42 61.54  ? 204 A1BG3 B N3  1 
HETATM 1765 N N3  D A1BG3 F 4 .   ? -8.526  5.631   -10.418 0.39 61.53  ? 204 A1BG3 B N3  1 
HETATM 1766 C C4  C A1BG3 F 4 .   ? -6.217  6.073   -16.863 0.42 69.86  ? 204 A1BG3 B C4  1 
HETATM 1767 C C4  D A1BG3 F 4 .   ? -6.217  6.072   -16.863 0.39 69.82  ? 204 A1BG3 B C4  1 
HETATM 1768 C C5  C A1BG3 F 4 .   ? -7.543  5.457   -17.191 0.42 67.04  ? 204 A1BG3 B C5  1 
HETATM 1769 C C5  D A1BG3 F 4 .   ? -7.543  5.457   -17.191 0.39 67.05  ? 204 A1BG3 B C5  1 
HETATM 1770 C C6  C A1BG3 F 4 .   ? -7.798  5.061   -18.508 0.42 67.32  ? 204 A1BG3 B C6  1 
HETATM 1771 C C6  D A1BG3 F 4 .   ? -7.798  5.060   -18.507 0.39 67.31  ? 204 A1BG3 B C6  1 
HETATM 1772 C C7  C A1BG3 F 4 .   ? -8.988  4.457   -18.867 0.42 66.13  ? 204 A1BG3 B C7  1 
HETATM 1773 C C7  D A1BG3 F 4 .   ? -8.988  4.457   -18.866 0.39 66.15  ? 204 A1BG3 B C7  1 
HETATM 1774 C C8  C A1BG3 F 4 .   ? -9.952  4.218   -17.915 0.42 64.92  ? 204 A1BG3 B C8  1 
HETATM 1775 C C8  D A1BG3 F 4 .   ? -9.952  4.218   -17.914 0.39 64.95  ? 204 A1BG3 B C8  1 
HETATM 1776 C C10 C A1BG3 F 4 .   ? -8.529  5.193   -16.218 0.42 65.49  ? 204 A1BG3 B C10 1 
HETATM 1777 C C10 D A1BG3 F 4 .   ? -8.528  5.193   -16.217 0.39 65.48  ? 204 A1BG3 B C10 1 
HETATM 1778 C C13 C A1BG3 F 4 .   ? -8.840  3.799   -11.475 0.42 60.44  ? 204 A1BG3 B C13 1 
HETATM 1779 C C13 D A1BG3 F 4 .   ? -8.840  3.800   -11.475 0.39 60.48  ? 204 A1BG3 B C13 1 
HETATM 1780 C C15 C A1BG3 F 4 .   ? -8.469  5.970   -11.729 0.42 61.87  ? 204 A1BG3 B C15 1 
HETATM 1781 C C15 D A1BG3 F 4 .   ? -8.469  5.970   -11.729 0.39 61.87  ? 204 A1BG3 B C15 1 
HETATM 1782 C C17 C A1BG3 F 4 .   ? -3.763  7.076   -16.230 0.42 72.65  ? 204 A1BG3 B C17 1 
HETATM 1783 C C17 D A1BG3 F 4 .   ? -3.764  7.076   -16.230 0.39 72.61  ? 204 A1BG3 B C17 1 
HETATM 1784 C C1  C A1BG3 F 4 .   ? -3.995  9.003   -17.864 0.42 72.95  ? 204 A1BG3 B C1  1 
HETATM 1785 C C1  D A1BG3 F 4 .   ? -3.996  9.002   -17.864 0.39 72.93  ? 204 A1BG3 B C1  1 
HETATM 1786 C C2  C A1BG3 F 4 .   ? -4.509  7.752   -17.193 0.42 72.23  ? 204 A1BG3 B C2  1 
HETATM 1787 C C2  D A1BG3 F 4 .   ? -4.509  7.752   -17.193 0.39 72.21  ? 204 A1BG3 B C2  1 
HETATM 1788 C C3  C A1BG3 F 4 .   ? -5.753  7.221   -17.513 0.42 70.82  ? 204 A1BG3 B C3  1 
HETATM 1789 C C3  D A1BG3 F 4 .   ? -5.753  7.221   -17.513 0.39 70.81  ? 204 A1BG3 B C3  1 
HETATM 1790 C C9  C A1BG3 F 4 .   ? -9.727  4.580   -16.602 0.42 64.62  ? 204 A1BG3 B C9  1 
HETATM 1791 C C9  D A1BG3 F 4 .   ? -9.727  4.581   -16.601 0.39 64.63  ? 204 A1BG3 B C9  1 
HETATM 1792 C C11 C A1BG3 F 4 .   ? -8.389  5.564   -14.765 0.42 63.25  ? 204 A1BG3 B C11 1 
HETATM 1793 C C11 D A1BG3 F 4 .   ? -8.388  5.564   -14.765 0.39 63.28  ? 204 A1BG3 B C11 1 
HETATM 1794 O O1  C A1BG3 F 4 .   ? -8.024  6.683   -14.437 0.42 62.74  ? 204 A1BG3 B O1  1 
HETATM 1795 O O1  D A1BG3 F 4 .   ? -8.021  6.683   -14.438 0.39 62.78  ? 204 A1BG3 B O1  1 
HETATM 1796 C C12 C A1BG3 F 4 .   ? -8.668  4.789   -12.450 0.42 61.86  ? 204 A1BG3 B C12 1 
HETATM 1797 C C12 D A1BG3 F 4 .   ? -8.668  4.789   -12.450 0.39 61.86  ? 204 A1BG3 B C12 1 
HETATM 1798 N N2  C A1BG3 F 4 .   ? -8.755  4.290   -10.249 0.42 61.16  ? 204 A1BG3 B N2  1 
HETATM 1799 N N2  D A1BG3 F 4 .   ? -8.756  4.290   -10.249 0.39 61.15  ? 204 A1BG3 B N2  1 
HETATM 1800 C C14 C A1BG3 F 4 .   ? -8.385  6.490   -9.244  0.42 61.07  ? 204 A1BG3 B C14 1 
HETATM 1801 C C14 D A1BG3 F 4 .   ? -8.385  6.491   -9.244  0.39 61.07  ? 204 A1BG3 B C14 1 
HETATM 1802 C C16 C A1BG3 F 4 .   ? -5.351  5.503   -15.931 0.42 70.17  ? 204 A1BG3 B C16 1 
HETATM 1803 C C16 D A1BG3 F 4 .   ? -5.351  5.502   -15.931 0.39 70.15  ? 204 A1BG3 B C16 1 
HETATM 1804 N N4  C A1BG3 F 4 .   ? -4.144  5.998   -15.607 0.42 71.56  ? 204 A1BG3 B N4  1 
HETATM 1805 N N4  D A1BG3 F 4 .   ? -4.144  5.998   -15.607 0.39 71.53  ? 204 A1BG3 B N4  1 
HETATM 1806 F F1  C A1BG3 F 4 .   ? -2.550  7.552   -15.886 0.42 74.79  ? 204 A1BG3 B F1  1 
HETATM 1807 F F1  D A1BG3 F 4 .   ? -2.551  7.553   -15.886 0.39 74.71  ? 204 A1BG3 B F1  1 
HETATM 1808 S S   C SO4   G 5 .   ? -18.756 11.622  -0.456  0.50 86.55  ? 205 SO4   B S   1 
HETATM 1809 S S   D SO4   G 5 .   ? -18.756 11.622  -0.456  0.50 86.55  ? 205 SO4   B S   1 
HETATM 1810 O O1  C SO4   G 5 .   ? -17.505 11.822  -1.161  0.50 86.30  ? 205 SO4   B O1  1 
HETATM 1811 O O1  D SO4   G 5 .   ? -17.505 11.822  -1.161  0.50 86.30  ? 205 SO4   B O1  1 
HETATM 1812 O O2  C SO4   G 5 .   ? -18.703 12.262  0.836   0.50 87.98  ? 205 SO4   B O2  1 
HETATM 1813 O O2  D SO4   G 5 .   ? -18.703 12.262  0.836   0.50 87.98  ? 205 SO4   B O2  1 
HETATM 1814 O O3  C SO4   G 5 .   ? -19.816 12.215  -1.219  0.50 88.21  ? 205 SO4   B O3  1 
HETATM 1815 O O3  D SO4   G 5 .   ? -19.816 12.215  -1.219  0.50 88.21  ? 205 SO4   B O3  1 
HETATM 1816 O O4  C SO4   G 5 .   ? -19.005 10.206  -0.276  0.50 83.89  ? 205 SO4   B O4  1 
HETATM 1817 O O4  D SO4   G 5 .   ? -19.005 10.206  -0.276  0.50 83.89  ? 205 SO4   B O4  1 
HETATM 1818 O O   . HOH   H 6 .   ? -27.882 -5.772  -28.185 1.00 46.79  ? 101 HOH   A O   1 
HETATM 1819 O O   . HOH   H 6 .   ? -8.054  0.521   3.321   1.00 47.56  ? 102 HOH   A O   1 
HETATM 1820 O O   . HOH   H 6 .   ? -23.731 19.123  -19.376 1.00 57.38  ? 103 HOH   A O   1 
HETATM 1821 O O   . HOH   H 6 .   ? -2.287  -3.773  -6.447  1.00 49.63  ? 104 HOH   A O   1 
HETATM 1822 O O   . HOH   H 6 .   ? -6.983  -8.880  -3.273  1.00 44.08  ? 105 HOH   A O   1 
HETATM 1823 O O   A HOH   H 6 .   ? 6.352   -5.133  -17.303 0.50 81.19  ? 106 HOH   A O   1 
HETATM 1824 O O   B HOH   H 6 .   ? 6.352   -5.133  -17.303 0.50 81.19  ? 106 HOH   A O   1 
HETATM 1825 O O   C HOH   H 6 .   ? -25.364 12.472  -23.824 0.50 48.60  ? 107 HOH   A O   1 
HETATM 1826 O O   D HOH   H 6 .   ? -25.364 12.472  -23.824 0.50 48.60  ? 107 HOH   A O   1 
HETATM 1827 O O   A HOH   H 6 .   ? -29.109 15.732  -14.975 0.50 53.15  ? 108 HOH   A O   1 
HETATM 1828 O O   B HOH   H 6 .   ? -29.109 15.732  -14.975 0.50 53.15  ? 108 HOH   A O   1 
HETATM 1829 O O   A HOH   H 6 .   ? -8.088  -1.783  6.653   0.50 55.62  ? 109 HOH   A O   1 
HETATM 1830 O O   B HOH   H 6 .   ? -8.088  -1.783  6.653   0.50 55.62  ? 109 HOH   A O   1 
HETATM 1831 O O   . HOH   H 6 .   ? -24.028 9.344   -27.468 1.00 40.13  ? 110 HOH   A O   1 
HETATM 1832 O O   . HOH   H 6 .   ? -4.265  -14.435 -25.461 1.00 43.46  ? 111 HOH   A O   1 
HETATM 1833 O O   . HOH   H 6 .   ? -20.913 2.739   -32.587 1.00 50.80  ? 112 HOH   A O   1 
HETATM 1834 O O   . HOH   H 6 .   ? -3.640  -4.070  0.237   1.00 50.27  ? 113 HOH   A O   1 
HETATM 1835 O O   . HOH   H 6 .   ? -26.532 -3.618  -35.332 1.00 59.64  ? 114 HOH   A O   1 
HETATM 1836 O O   . HOH   H 6 .   ? -22.476 -9.356  -34.569 1.00 49.32  ? 115 HOH   A O   1 
HETATM 1837 O O   . HOH   H 6 .   ? -30.696 12.626  -16.429 1.00 53.37  ? 116 HOH   A O   1 
HETATM 1838 O O   . HOH   H 6 .   ? -30.951 0.404   -23.107 1.00 50.28  ? 117 HOH   A O   1 
HETATM 1839 O O   A HOH   H 6 .   ? -0.552  -12.394 -23.656 0.50 67.14  ? 118 HOH   A O   1 
HETATM 1840 O O   B HOH   H 6 .   ? -0.552  -12.394 -23.656 0.50 67.14  ? 118 HOH   A O   1 
HETATM 1841 O O   . HOH   H 6 .   ? -4.657  -10.115 -5.615  1.00 45.26  ? 119 HOH   A O   1 
HETATM 1842 O O   . HOH   H 6 .   ? -3.986  -0.626  -0.461  1.00 49.63  ? 120 HOH   A O   1 
HETATM 1843 O O   C HOH   H 6 .   ? -5.061  5.495   -7.160  0.42 58.63  ? 121 HOH   A O   1 
HETATM 1844 O O   D HOH   H 6 .   ? -5.060  5.495   -7.156  0.39 58.65  ? 121 HOH   A O   1 
HETATM 1845 O O   . HOH   H 6 .   ? -2.975  -9.194  -3.363  1.00 49.15  ? 122 HOH   A O   1 
HETATM 1846 O O   . HOH   I 6 .   ? -15.796 -9.825  -15.110 1.00 53.80  ? 301 HOH   B O   1 
HETATM 1847 O O   . HOH   I 6 .   ? -30.673 12.858  -19.464 1.00 55.40  ? 302 HOH   B O   1 
HETATM 1848 O O   . HOH   I 6 .   ? -17.239 12.762  -5.488  1.00 49.27  ? 303 HOH   B O   1 
HETATM 1849 O O   C HOH   I 6 .   ? -20.332 13.713  1.739   0.50 56.30  ? 304 HOH   B O   1 
HETATM 1850 O O   D HOH   I 6 .   ? -20.332 13.713  1.739   0.50 56.30  ? 304 HOH   B O   1 
HETATM 1851 O O   . HOH   I 6 .   ? -33.976 1.660   -15.333 1.00 45.50  ? 305 HOH   B O   1 
HETATM 1852 O O   . HOH   I 6 .   ? -25.995 -7.985  -16.658 1.00 40.40  ? 306 HOH   B O   1 
HETATM 1853 O O   . HOH   I 6 .   ? -19.447 -11.993 -25.687 1.00 57.81  ? 307 HOH   B O   1 
HETATM 1854 O O   A HOH   I 6 .   ? -16.661 25.957  -12.444 0.50 64.94  ? 308 HOH   B O   1 
HETATM 1855 O O   B HOH   I 6 .   ? -16.661 25.957  -12.444 0.50 64.94  ? 308 HOH   B O   1 
HETATM 1856 O O   . HOH   I 6 .   ? -8.985  -6.188  -25.305 1.00 55.00  ? 309 HOH   B O   1 
HETATM 1857 O O   . HOH   I 6 .   ? -5.260  2.873   -11.130 1.00 56.82  ? 310 HOH   B O   1 
HETATM 1858 O O   . HOH   I 6 .   ? -13.137 -2.267  -14.808 1.00 33.50  ? 311 HOH   B O   1 
HETATM 1859 O O   . HOH   I 6 .   ? -9.195  2.320   -8.649  1.00 45.54  ? 312 HOH   B O   1 
HETATM 1860 O O   . HOH   I 6 .   ? -6.495  -0.439  -10.896 1.00 38.81  ? 313 HOH   B O   1 
HETATM 1861 O O   . HOH   I 6 .   ? -15.247 -4.527  1.404   1.00 40.01  ? 314 HOH   B O   1 
HETATM 1862 O O   . HOH   I 6 .   ? -12.319 1.960   -5.760  1.00 47.40  ? 315 HOH   B O   1 
HETATM 1863 O O   A HOH   I 6 .   ? -11.286 11.881  -19.494 0.50 53.99  ? 316 HOH   B O   1 
HETATM 1864 O O   B HOH   I 6 .   ? -11.286 11.881  -19.494 0.50 53.99  ? 316 HOH   B O   1 
HETATM 1865 O O   . HOH   I 6 .   ? -18.086 -10.654 -16.508 1.00 38.80  ? 317 HOH   B O   1 
HETATM 1866 O O   . HOH   I 6 .   ? -35.444 -5.274  -10.281 1.00 50.51  ? 318 HOH   B O   1 
HETATM 1867 O O   . HOH   I 6 .   ? -23.772 -14.494 -17.790 1.00 64.64  ? 319 HOH   B O   1 
HETATM 1868 O O   . HOH   I 6 .   ? -31.763 7.329   -4.604  1.00 56.53  ? 320 HOH   B O   1 
HETATM 1869 O O   A HOH   I 6 .   ? -11.992 -17.805 -27.882 0.50 58.16  ? 321 HOH   B O   1 
HETATM 1870 O O   B HOH   I 6 .   ? -11.992 -17.805 -27.882 0.50 58.16  ? 321 HOH   B O   1 
HETATM 1871 O O   . HOH   I 6 .   ? -21.741 -12.233 -13.087 1.00 51.61  ? 322 HOH   B O   1 
HETATM 1872 O O   . HOH   I 6 .   ? -21.154 6.208   -32.619 1.00 58.13  ? 323 HOH   B O   1 
HETATM 1873 O O   . HOH   I 6 .   ? -35.073 4.701   -9.409  1.00 58.89  ? 324 HOH   B O   1 
HETATM 1874 O O   . HOH   I 6 .   ? -27.531 -6.962  -5.528  1.00 56.44  ? 325 HOH   B O   1 
HETATM 1875 O O   . HOH   I 6 .   ? -16.600 -7.220  -8.195  1.00 53.07  ? 326 HOH   B O   1 
HETATM 1876 O O   . HOH   I 6 .   ? -12.524 -3.435  -10.221 1.00 36.24  ? 327 HOH   B O   1 
HETATM 1877 O O   A HOH   I 6 .   ? -16.405 20.851  -14.388 0.50 53.23  ? 328 HOH   B O   1 
HETATM 1878 O O   B HOH   I 6 .   ? -16.405 20.851  -14.388 0.50 53.23  ? 328 HOH   B O   1 
HETATM 1879 O O   . HOH   I 6 .   ? -28.650 -3.753  -22.511 1.00 56.79  ? 329 HOH   B O   1 
HETATM 1880 O O   C HOH   I 6 .   ? -21.436 14.273  -34.441 0.50 65.20  ? 330 HOH   B O   1 
HETATM 1881 O O   D HOH   I 6 .   ? -21.436 14.273  -34.441 0.50 65.20  ? 330 HOH   B O   1 
HETATM 1882 O O   A HOH   I 6 .   ? -18.730 19.305  -21.489 0.50 58.07  ? 331 HOH   B O   1 
HETATM 1883 O O   B HOH   I 6 .   ? -18.730 19.305  -21.489 0.50 58.07  ? 331 HOH   B O   1 
HETATM 1884 O O   C HOH   I 6 .   ? -31.626 12.625  -0.765  0.50 65.05  ? 332 HOH   B O   1 
HETATM 1885 O O   D HOH   I 6 .   ? -31.626 12.625  -0.765  0.50 65.05  ? 332 HOH   B O   1 
HETATM 1886 O O   . HOH   I 6 .   ? -19.996 -7.795  -2.705  1.00 57.31  ? 333 HOH   B O   1 
HETATM 1887 O O   . HOH   I 6 .   ? -14.684 -6.233  -1.769  1.00 64.71  ? 334 HOH   B O   1 
HETATM 1888 O O   A HOH   I 6 .   ? -8.508  -10.843 -7.581  0.50 61.27  ? 335 HOH   B O   1 
HETATM 1889 O O   B HOH   I 6 .   ? -8.508  -10.843 -7.581  0.50 61.27  ? 335 HOH   B O   1 
HETATM 1890 O O   . HOH   I 6 .   ? -16.238 -14.649 -16.617 1.00 49.13  ? 336 HOH   B O   1 
HETATM 1891 O O   . HOH   I 6 .   ? -15.880 -13.822 -30.904 1.00 53.61  ? 337 HOH   B O   1 
HETATM 1892 O O   . HOH   I 6 .   ? -27.973 -6.170  -18.583 1.00 48.14  ? 338 HOH   B O   1 
HETATM 1893 O O   C HOH   I 6 .   ? -3.631  3.631   -27.052 0.42 90.00  ? 339 HOH   B O   1 
HETATM 1894 O O   D HOH   I 6 .   ? -3.627  3.627   -27.051 0.39 89.99  ? 339 HOH   B O   1 
HETATM 1895 O O   . HOH   I 6 .   ? -14.378 -12.295 -16.542 1.00 47.06  ? 340 HOH   B O   1 
HETATM 1896 O O   C HOH   I 6 .   ? -22.162 15.223  -6.194  0.50 44.56  ? 341 HOH   B O   1 
HETATM 1897 O O   D HOH   I 6 .   ? -22.162 15.223  -6.194  0.50 44.56  ? 341 HOH   B O   1 
HETATM 1898 O O   A HOH   I 6 .   ? -29.713 -1.191  -19.015 0.50 55.05  ? 342 HOH   B O   1 
HETATM 1899 O O   B HOH   I 6 .   ? -29.713 -1.191  -19.015 0.50 55.05  ? 342 HOH   B O   1 
HETATM 1900 O O   . HOH   I 6 .   ? -10.178 -18.440 -12.249 1.00 62.24  ? 343 HOH   B O   1 
HETATM 1901 O O   . HOH   I 6 .   ? -15.123 16.569  -20.074 1.00 51.00  ? 344 HOH   B O   1 
HETATM 1902 O O   . HOH   I 6 .   ? -2.985  -11.735 -7.078  1.00 43.30  ? 345 HOH   B O   1 
HETATM 1903 O O   . HOH   I 6 .   ? -7.437  -6.375  0.278   1.00 55.94  ? 346 HOH   B O   1 
HETATM 1904 O O   . HOH   I 6 .   ? -6.977  -10.853 -5.465  1.00 51.08  ? 347 HOH   B O   1 
HETATM 1905 O O   . HOH   I 6 .   ? -21.251 7.085   -0.000  0.50 49.83  ? 348 HOH   B O   1 
HETATM 1906 O O   . HOH   I 6 .   ? -21.694 -13.440 -21.819 1.00 52.20  ? 349 HOH   B O   1 
HETATM 1907 O O   . HOH   I 6 .   ? -30.578 4.596   -2.586  1.00 49.11  ? 350 HOH   B O   1 
HETATM 1908 O O   . HOH   I 6 .   ? -18.788 15.076  -22.142 1.00 38.42  ? 351 HOH   B O   1 
HETATM 1909 O O   . HOH   I 6 .   ? -15.295 9.355   -0.651  1.00 47.83  ? 352 HOH   B O   1 
HETATM 1910 O O   . HOH   I 6 .   ? -26.024 -4.534  -4.036  1.00 36.25  ? 353 HOH   B O   1 
HETATM 1911 O O   . HOH   I 6 .   ? -17.210 14.769  -30.777 1.00 53.86  ? 354 HOH   B O   1 
HETATM 1912 O O   . HOH   I 6 .   ? -11.601 -5.011  -8.281  1.00 44.49  ? 355 HOH   B O   1 
HETATM 1913 O O   C HOH   I 6 .   ? -36.873 2.322   -14.404 0.50 78.46  ? 356 HOH   B O   1 
HETATM 1914 O O   D HOH   I 6 .   ? -36.873 2.322   -14.404 0.50 78.46  ? 356 HOH   B O   1 
HETATM 1915 O O   . HOH   I 6 .   ? -19.318 -5.551  -0.849  1.00 43.01  ? 357 HOH   B O   1 
HETATM 1916 O O   A HOH   I 6 .   ? -0.296  0.244   -13.547 0.14 36.26  ? 358 HOH   B O   1 
HETATM 1917 O O   B HOH   I 6 .   ? -0.296  0.244   -13.547 0.14 36.26  ? 358 HOH   B O   1 
HETATM 1918 O O   A HOH   I 6 .   ? -19.138 25.318  -14.406 0.50 59.23  ? 359 HOH   B O   1 
HETATM 1919 O O   B HOH   I 6 .   ? -19.138 25.318  -14.406 0.50 59.23  ? 359 HOH   B O   1 
HETATM 1920 O O   . HOH   I 6 .   ? -19.550 -13.306 -23.070 1.00 42.81  ? 360 HOH   B O   1 
HETATM 1921 O O   . HOH   I 6 .   ? -10.985 7.719   -13.974 1.00 51.58  ? 361 HOH   B O   1 
HETATM 1922 O O   C HOH   I 6 .   ? -7.145  10.584  -19.197 0.42 53.64  ? 362 HOH   B O   1 
HETATM 1923 O O   D HOH   I 6 .   ? -7.144  10.583  -19.196 0.39 53.66  ? 362 HOH   B O   1 
HETATM 1924 O O   A HOH   I 6 .   ? -30.059 -7.661  -5.204  0.50 58.09  ? 363 HOH   B O   1 
HETATM 1925 O O   B HOH   I 6 .   ? -30.059 -7.661  -5.204  0.50 58.09  ? 363 HOH   B O   1 
HETATM 1926 O O   . HOH   I 6 .   ? -1.381  -14.399 -9.871  1.00 60.07  ? 364 HOH   B O   1 
HETATM 1927 O O   C HOH   I 6 .   ? -9.792  -16.304 -23.968 0.50 57.24  ? 365 HOH   B O   1 
HETATM 1928 O O   D HOH   I 6 .   ? -9.792  -16.304 -23.968 0.50 57.24  ? 365 HOH   B O   1 
HETATM 1929 O O   . HOH   I 6 .   ? -17.191 16.633  -21.892 1.00 49.99  ? 366 HOH   B O   1 
HETATM 1930 O O   A HOH   I 6 .   ? -20.232 25.018  -16.952 0.50 67.29  ? 367 HOH   B O   1 
HETATM 1931 O O   B HOH   I 6 .   ? -20.232 25.018  -16.952 0.50 67.29  ? 367 HOH   B O   1 
HETATM 1932 O O   . HOH   I 6 .   ? -29.598 -5.283  -0.927  1.00 50.02  ? 368 HOH   B O   1 
HETATM 1933 O O   C HOH   I 6 .   ? -21.251 -6.811  -0.000  0.50 76.85  ? 369 HOH   B O   1 
HETATM 1934 O O   D HOH   I 6 .   ? -21.251 -6.811  0.000   0.50 76.73  ? 369 HOH   B O   1 
HETATM 1935 O O   A HOH   I 6 .   ? -12.072 5.172   -5.533  0.50 91.71  ? 370 HOH   B O   1 
HETATM 1936 O O   B HOH   I 6 .   ? -12.072 5.172   -5.533  0.50 91.71  ? 370 HOH   B O   1 
HETATM 1937 O O   . HOH   I 6 .   ? -23.126 -7.316  -2.474  1.00 58.96  ? 371 HOH   B O   1 
HETATM 1938 O O   A HOH   I 6 .   ? -31.757 -6.873  -6.977  0.50 59.68  ? 372 HOH   B O   1 
HETATM 1939 O O   B HOH   I 6 .   ? -31.757 -6.873  -6.977  0.50 59.68  ? 372 HOH   B O   1 
HETATM 1940 O O   A HOH   I 6 .   ? -19.315 -11.915 -13.585 0.50 52.93  ? 373 HOH   B O   1 
HETATM 1941 O O   B HOH   I 6 .   ? -19.315 -11.915 -13.585 0.50 52.93  ? 373 HOH   B O   1 
HETATM 1942 O O   A HOH   I 6 .   ? -30.496 -12.007 -27.052 0.25 113.88 ? 374 HOH   B O   1 
HETATM 1943 O O   B HOH   I 6 .   ? -30.496 -12.007 -27.052 0.25 113.88 ? 374 HOH   B O   1 
HETATM 1944 O O   A HOH   I 6 .   ? -8.707  5.349   -10.410 0.11 24.42  ? 375 HOH   B O   1 
HETATM 1945 O O   B HOH   I 6 .   ? -8.707  5.354   -10.408 0.09 24.42  ? 375 HOH   B O   1 
HETATM 1946 O O   C HOH   I 6 .   ? -12.482 -9.412  0.120   0.50 65.51  ? 376 HOH   B O   1 
HETATM 1947 O O   D HOH   I 6 .   ? -12.482 -9.412  0.120   0.50 65.51  ? 376 HOH   B O   1 
HETATM 1948 O O   A HOH   I 6 .   ? -20.205 4.109   -0.195  0.50 65.80  ? 377 HOH   B O   1 
HETATM 1949 O O   B HOH   I 6 .   ? -20.205 4.109   -0.195  0.50 65.80  ? 377 HOH   B O   1 
HETATM 1950 O O   A HOH   I 6 .   ? -11.709 -7.505  1.726   0.50 70.29  ? 378 HOH   B O   1 
HETATM 1951 O O   B HOH   I 6 .   ? -11.709 -7.505  1.726   0.50 70.29  ? 378 HOH   B O   1 
HETATM 1952 O O   . HOH   I 6 .   ? -11.435 12.451  -14.268 1.00 62.90  ? 379 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   ? 0.7991 0.6875 0.7851 0.0324  0.0794  -0.0379 50  ASP   A N   
2    C CA  . ASP   A 7   ? 0.7753 0.6731 0.7316 0.0398  0.0756  -0.0437 50  ASP   A CA  
3    C C   . ASP   A 7   ? 0.7443 0.6438 0.6807 0.0496  0.0815  -0.0247 50  ASP   A C   
4    O O   . ASP   A 7   ? 0.7655 0.6509 0.7069 0.0576  0.0890  -0.0100 50  ASP   A O   
5    C CB  . ASP   A 7   ? 0.8085 0.6975 0.7692 0.0446  0.0733  -0.0566 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 0.8189 0.7194 0.7545 0.0518  0.0706  -0.0628 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 0.8497 0.7643 0.7736 0.0475  0.0650  -0.0769 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 0.8368 0.7326 0.7654 0.0623  0.0742  -0.0533 50  ASP   A OD2 
9    N N   . MET   A 8   ? 0.6740 0.5891 0.5874 0.0498  0.0779  -0.0251 51  MET   A N   
10   C CA  . MET   A 8   ? 0.6393 0.5579 0.5354 0.0569  0.0819  -0.0084 51  MET   A CA  
11   C C   . MET   A 8   ? 0.6106 0.5309 0.4881 0.0680  0.0802  -0.0084 51  MET   A C   
12   O O   . MET   A 8   ? 0.5969 0.5241 0.4698 0.0669  0.0749  -0.0228 51  MET   A O   
13   C CB  . MET   A 8   ? 0.6295 0.5629 0.5135 0.0509  0.0781  -0.0093 51  MET   A CB  
14   C CG  . MET   A 8   ? 0.6393 0.5735 0.5426 0.0418  0.0792  -0.0080 51  MET   A CG  
15   S SD  . MET   A 8   ? 0.6343 0.5845 0.5215 0.0386  0.0755  -0.0053 51  MET   A SD  
16   C CE  . MET   A 8   ? 0.6338 0.5838 0.5531 0.0295  0.0782  -0.0028 51  MET   A CE  
17   N N   . TYR   A 9   ? 0.5748 0.4893 0.4430 0.0794  0.0848  0.0071  52  TYR   A N   
18   C CA  . TYR   A 9   ? 0.5636 0.4802 0.4154 0.0920  0.0817  0.0075  52  TYR   A CA  
19   C C   . TYR   A 9   ? 0.5506 0.4714 0.3823 0.1005  0.0824  0.0204  52  TYR   A C   
20   O O   . TYR   A 9   ? 0.5301 0.4483 0.3627 0.0990  0.0882  0.0321  52  TYR   A O   
21   C CB  . TYR   A 9   ? 0.5801 0.4814 0.4413 0.1016  0.0848  0.0107  52  TYR   A CB  
22   C CG  . TYR   A 9   ? 0.6037 0.4878 0.4709 0.1080  0.0945  0.0301  52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 0.6139 0.4868 0.5051 0.0984  0.1009  0.0331  52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 0.6227 0.5016 0.4719 0.1242  0.0975  0.0456  52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 0.6436 0.5003 0.5437 0.1033  0.1121  0.0524  52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 0.6440 0.5064 0.4970 0.1311  0.1087  0.0656  52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 0.6541 0.5051 0.5338 0.1199  0.1170  0.0699  52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 0.6904 0.5252 0.5773 0.1249  0.1303  0.0910  52  TYR   A OH  
29   N N   . ILE   A 10  ? 0.5509 0.4801 0.3666 0.1087  0.0760  0.0161  53  ILE   A N   
30   C CA  . ILE   A 10  ? 0.5529 0.4868 0.3476 0.1186  0.0739  0.0247  53  ILE   A CA  
31   C C   . ILE   A 10  ? 0.5721 0.4986 0.3560 0.1375  0.0732  0.0324  53  ILE   A C   
32   O O   . ILE   A 10  ? 0.5606 0.4838 0.3519 0.1422  0.0709  0.0266  53  ILE   A O   
33   C CB  . ILE   A 10  ? 0.5444 0.4939 0.3295 0.1128  0.0656  0.0131  53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 0.5476 0.5055 0.3355 0.1138  0.0588  -0.0007 53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 0.5321 0.4871 0.3236 0.0969  0.0665  0.0081  53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 0.5464 0.5177 0.3253 0.1098  0.0520  -0.0084 53  ILE   A CD1 
37   N N   . GLU   A 11  ? 0.5907 0.5151 0.3563 0.1495  0.0750  0.0453  54  GLU   A N   
38   C CA  . GLU   A 11  ? 0.6263 0.5433 0.3753 0.1708  0.0741  0.0548  54  GLU   A CA  
39   C C   . GLU   A 11  ? 0.6109 0.5370 0.3359 0.1807  0.0674  0.0553  54  GLU   A C   
40   O O   . GLU   A 11  ? 0.5954 0.5237 0.3144 0.1762  0.0719  0.0616  54  GLU   A O   
41   C CB  . GLU   A 11  ? 0.6733 0.5728 0.4217 0.1788  0.0874  0.0755  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 0.7089 0.5934 0.4774 0.1768  0.0935  0.0783  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 0.7550 0.6212 0.5260 0.1828  0.1088  0.1008  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 0.7978 0.6648 0.5545 0.1882  0.1157  0.1145  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 0.7991 0.6498 0.5874 0.1818  0.1147  0.1050  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 0.6181 0.5506 0.3320 0.1931  0.0558  0.0469  55  ARG   A N   
47   C CA  . ARG   A 12  ? 0.6259 0.5673 0.3190 0.2020  0.0470  0.0437  55  ARG   A CA  
48   C C   . ARG   A 12  ? 0.6321 0.5635 0.3032 0.2177  0.0551  0.0625  55  ARG   A C   
49   O O   . ARG   A 12  ? 0.6603 0.5784 0.3297 0.2276  0.0638  0.0762  55  ARG   A O   
50   C CB  . ARG   A 12  ? 0.6504 0.6005 0.3387 0.2141  0.0323  0.0308  55  ARG   A CB  
51   C CG  . ARG   A 12  ? 0.6649 0.6261 0.3400 0.2179  0.0205  0.0214  55  ARG   A CG  
52   C CD  . ARG   A 12  ? 0.6827 0.6577 0.3695 0.2177  0.0059  0.0022  55  ARG   A CD  
53   N NE  . ARG   A 12  ? 0.6904 0.6751 0.3700 0.2188  -0.0057 -0.0084 55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 0.7108 0.6941 0.3664 0.2386  -0.0139 -0.0070 55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 0.7710 0.7441 0.4062 0.2586  -0.0103 0.0063  55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 0.6793 0.6702 0.3304 0.2389  -0.0253 -0.0184 55  ARG   A NH2 
57   N N   . ALA   A 13  ? 0.6226 0.5591 0.2791 0.2191  0.0543  0.0640  56  ALA   A N   
58   C CA  . ALA   A 13  ? 0.6491 0.5784 0.2821 0.2352  0.0631  0.0815  56  ALA   A CA  
59   C C   . ALA   A 13  ? 0.6651 0.6008 0.2703 0.2528  0.0512  0.0756  56  ALA   A C   
60   O O   . ALA   A 13  ? 0.6872 0.6172 0.2687 0.2698  0.0583  0.0898  56  ALA   A O   
61   C CB  . ALA   A 13  ? 0.6424 0.5712 0.2839 0.2228  0.0763  0.0914  56  ALA   A CB  
62   N N   . GLY   A 14  ? 0.6524 0.5991 0.2600 0.2497  0.0348  0.0562  57  GLY   A N   
63   C CA  . GLY   A 14  ? 0.6722 0.6241 0.2553 0.2665  0.0220  0.0486  57  GLY   A CA  
64   C C   . GLY   A 14  ? 0.6670 0.6308 0.2630 0.2548  0.0066  0.0272  57  GLY   A C   
65   O O   . GLY   A 14  ? 0.6229 0.5911 0.2454 0.2313  0.0091  0.0206  57  GLY   A O   
66   N N   . ASP   A 15  ? 0.6868 0.6552 0.2651 0.2700  -0.0078 0.0167  58  ASP   A N   
67   C CA  . ASP   A 15  ? 0.6938 0.6717 0.2813 0.2611  -0.0224 -0.0025 58  ASP   A CA  
68   C C   . ASP   A 15  ? 0.7066 0.6819 0.2868 0.2540  -0.0163 0.0017  58  ASP   A C   
69   O O   . ASP   A 15  ? 0.7301 0.6988 0.2910 0.2643  -0.0048 0.0174  58  ASP   A O   
70   C CB  . ASP   A 15  ? 0.7241 0.7073 0.2971 0.2812  -0.0419 -0.0170 58  ASP   A CB  
71   C CG  . ASP   A 15  ? 0.7408 0.7299 0.3240 0.2890  -0.0521 -0.0255 58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 0.7157 0.7035 0.3157 0.2798  -0.0430 -0.0192 58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 0.7641 0.7593 0.3377 0.3063  -0.0703 -0.0393 58  ASP   A OD2 
74   N N   . ILE   A 16  ? 0.7001 0.6804 0.2959 0.2375  -0.0228 -0.0107 59  ILE   A N   
75   C CA  . ILE   A 16  ? 0.6962 0.6739 0.2843 0.2330  -0.0206 -0.0094 59  ILE   A CA  
76   C C   . ILE   A 16  ? 0.7190 0.6979 0.2911 0.2483  -0.0372 -0.0232 59  ILE   A C   
77   O O   . ILE   A 16  ? 0.6929 0.6769 0.2808 0.2412  -0.0513 -0.0405 59  ILE   A O   
78   C CB  . ILE   A 16  ? 0.6878 0.6675 0.3004 0.2069  -0.0165 -0.0126 59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 0.6715 0.6495 0.2960 0.1957  -0.0009 0.0004  59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 0.6934 0.6702 0.2987 0.2037  -0.0174 -0.0136 59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 0.6592 0.6402 0.3070 0.1719  0.0022  -0.0039 59  ILE   A CD1 
82   N N   A THR   A 17  ? 0.7401 0.7147 0.2826 0.2694  -0.0352 -0.0157 60  THR   A N   
83   N N   B THR   A 17  ? 0.7417 0.7164 0.2846 0.2689  -0.0355 -0.0162 60  THR   A N   
84   N N   C THR   A 17  ? 0.7401 0.7147 0.2826 0.2694  -0.0352 -0.0157 60  THR   A N   
85   N N   D THR   A 17  ? 0.7417 0.7164 0.2846 0.2689  -0.0355 -0.0162 60  THR   A N   
86   C CA  A THR   A 17  ? 0.7689 0.7434 0.2877 0.2912  -0.0507 -0.0276 60  THR   A CA  
87   C CA  B THR   A 17  ? 0.7704 0.7452 0.2915 0.2894  -0.0519 -0.0293 60  THR   A CA  
88   C CA  C THR   A 17  ? 0.7689 0.7434 0.2877 0.2912  -0.0507 -0.0276 60  THR   A CA  
89   C CA  D THR   A 17  ? 0.7704 0.7452 0.2915 0.2894  -0.0519 -0.0293 60  THR   A CA  
90   C C   A THR   A 17  ? 0.7858 0.7553 0.2804 0.3017  -0.0419 -0.0178 60  THR   A C   
91   C C   B THR   A 17  ? 0.7909 0.7606 0.2842 0.3035  -0.0434 -0.0188 60  THR   A C   
92   C C   C THR   A 17  ? 0.7858 0.7553 0.2804 0.3017  -0.0419 -0.0178 60  THR   A C   
93   C C   D THR   A 17  ? 0.7909 0.7606 0.2842 0.3035  -0.0434 -0.0188 60  THR   A C   
94   O O   A THR   A 17  ? 0.7934 0.7604 0.2863 0.2979  -0.0210 0.0031  60  THR   A O   
95   O O   B THR   A 17  ? 0.8018 0.7688 0.2923 0.3011  -0.0223 0.0027  60  THR   A O   
96   O O   C THR   A 17  ? 0.7934 0.7604 0.2863 0.2979  -0.0210 0.0031  60  THR   A O   
97   O O   D THR   A 17  ? 0.8018 0.7688 0.2923 0.3011  -0.0223 0.0027  60  THR   A O   
98   C CB  A THR   A 17  ? 0.7887 0.7647 0.2896 0.3149  -0.0589 -0.0291 60  THR   A CB  
99   C CB  B THR   A 17  ? 0.7888 0.7667 0.2985 0.3097  -0.0630 -0.0348 60  THR   A CB  
100  C CB  C THR   A 17  ? 0.7887 0.7647 0.2896 0.3149  -0.0589 -0.0291 60  THR   A CB  
101  C CB  D THR   A 17  ? 0.7888 0.7667 0.2985 0.3097  -0.0630 -0.0348 60  THR   A CB  
102  O OG1 A THR   A 17  ? 0.8079 0.7779 0.2808 0.3327  -0.0441 -0.0089 60  THR   A OG1 
103  O OG1 B THR   A 17  ? 0.7685 0.7538 0.3082 0.2956  -0.0740 -0.0496 60  THR   A OG1 
104  O OG1 C THR   A 17  ? 0.8079 0.7779 0.2808 0.3327  -0.0441 -0.0089 60  THR   A OG1 
105  O OG1 D THR   A 17  ? 0.7685 0.7538 0.3082 0.2956  -0.0740 -0.0496 60  THR   A OG1 
106  C CG2 A THR   A 17  ? 0.7746 0.7555 0.2996 0.3052  -0.0610 -0.0322 60  THR   A CG2 
107  C CG2 B THR   A 17  ? 0.8216 0.7989 0.3007 0.3366  -0.0780 -0.0452 60  THR   A CG2 
108  C CG2 C THR   A 17  ? 0.7746 0.7555 0.2996 0.3052  -0.0610 -0.0322 60  THR   A CG2 
109  C CG2 D THR   A 17  ? 0.8216 0.7989 0.3007 0.3366  -0.0780 -0.0452 60  THR   A CG2 
110  N N   . TRP   A 18  ? 0.7945 0.7633 0.2828 0.3062  -0.0564 -0.0340 61  TRP   A N   
111  C CA  . TRP   A 18  ? 0.8350 0.8000 0.2941 0.3243  -0.0528 -0.0294 61  TRP   A CA  
112  C C   . TRP   A 18  ? 0.8881 0.8530 0.3133 0.3547  -0.0545 -0.0250 61  TRP   A C   
113  O O   . TRP   A 18  ? 0.9077 0.8752 0.3317 0.3635  -0.0702 -0.0377 61  TRP   A O   
114  C CB  . TRP   A 18  ? 0.8148 0.7773 0.2760 0.3229  -0.0691 -0.0490 61  TRP   A CB  
115  C CG  . TRP   A 18  ? 0.8245 0.7835 0.2582 0.3402  -0.0646 -0.0449 61  TRP   A CG  
116  C CD1 . TRP   A 18  ? 0.8592 0.8175 0.2581 0.3699  -0.0718 -0.0498 61  TRP   A CD1 
117  C CD2 . TRP   A 18  ? 0.8124 0.7694 0.2493 0.3314  -0.0519 -0.0354 61  TRP   A CD2 
118  N NE1 . TRP   A 18  ? 0.8730 0.8291 0.2536 0.3797  -0.0628 -0.0434 61  TRP   A NE1 
119  C CE2 . TRP   A 18  ? 0.8450 0.8005 0.2497 0.3564  -0.0512 -0.0351 61  TRP   A CE2 
120  C CE3 . TRP   A 18  ? 0.7774 0.7342 0.2400 0.3065  -0.0417 -0.0279 61  TRP   A CE3 
121  C CZ2 . TRP   A 18  ? 0.8443 0.7993 0.2448 0.3565  -0.0399 -0.0272 61  TRP   A CZ2 
122  C CZ3 . TRP   A 18  ? 0.7789 0.7347 0.2367 0.3070  -0.0322 -0.0205 61  TRP   A CZ3 
123  C CH2 . TRP   A 18  ? 0.8221 0.7773 0.2511 0.3308  -0.0313 -0.0204 61  TRP   A CH2 
124  N N   A GLU   A 19  ? 0.9177 0.8804 0.3172 0.3705  -0.0385 -0.0074 62  GLU   A N   
125  N N   B GLU   A 19  ? 0.9177 0.8804 0.3172 0.3705  -0.0385 -0.0074 62  GLU   A N   
126  N N   C GLU   A 19  ? 0.9105 0.8733 0.3111 0.3696  -0.0374 -0.0063 62  GLU   A N   
127  N N   D GLU   A 19  ? 0.9105 0.8733 0.3111 0.3696  -0.0374 -0.0063 62  GLU   A N   
128  C CA  A GLU   A 19  ? 0.9725 0.9337 0.3344 0.4018  -0.0364 0.0008  62  GLU   A CA  
129  C CA  B GLU   A 19  ? 0.9725 0.9337 0.3344 0.4018  -0.0364 0.0008  62  GLU   A CA  
130  C CA  C GLU   A 19  ? 0.9632 0.9244 0.3246 0.4018  -0.0353 0.0017  62  GLU   A CA  
131  C CA  D GLU   A 19  ? 0.9632 0.9244 0.3246 0.4018  -0.0353 0.0017  62  GLU   A CA  
132  C C   A GLU   A 19  ? 1.0113 0.9714 0.3398 0.4243  -0.0369 -0.0013 62  GLU   A C   
133  C C   B GLU   A 19  ? 1.0113 0.9714 0.3398 0.4243  -0.0369 -0.0013 62  GLU   A C   
134  C C   C GLU   A 19  ? 1.0018 0.9620 0.3321 0.4228  -0.0379 -0.0029 62  GLU   A C   
135  C C   D GLU   A 19  ? 1.0018 0.9620 0.3321 0.4228  -0.0379 -0.0029 62  GLU   A C   
136  O O   A GLU   A 19  ? 1.0011 0.9613 0.3285 0.4207  -0.0181 0.0136  62  GLU   A O   
137  O O   B GLU   A 19  ? 1.0011 0.9613 0.3285 0.4207  -0.0181 0.0136  62  GLU   A O   
138  O O   C GLU   A 19  ? 0.9891 0.9495 0.3212 0.4169  -0.0217 0.0086  62  GLU   A O   
139  O O   D GLU   A 19  ? 0.9891 0.9495 0.3212 0.4169  -0.0217 0.0086  62  GLU   A O   
140  C CB  A GLU   A 19  ? 0.9775 0.9364 0.3400 0.4004  -0.0128 0.0274  62  GLU   A CB  
141  C CB  B GLU   A 19  ? 0.9775 0.9364 0.3400 0.4004  -0.0128 0.0274  62  GLU   A CB  
142  C CB  C GLU   A 19  ? 0.9671 0.9257 0.3234 0.4042  -0.0102 0.0298  62  GLU   A CB  
143  C CB  D GLU   A 19  ? 0.9671 0.9257 0.3234 0.4042  -0.0102 0.0298  62  GLU   A CB  
144  C CG  A GLU   A 19  ? 0.9572 0.9164 0.3502 0.3811  -0.0133 0.0281  62  GLU   A CG  
145  C CG  B GLU   A 19  ? 0.9572 0.9164 0.3502 0.3811  -0.0133 0.0281  62  GLU   A CG  
146  C CG  C GLU   A 19  ? 1.0136 0.9692 0.3256 0.4386  -0.0040 0.0419  62  GLU   A CG  
147  C CG  D GLU   A 19  ? 1.0136 0.9692 0.3256 0.4386  -0.0040 0.0419  62  GLU   A CG  
148  C CD  A GLU   A 19  ? 0.9835 0.9434 0.3677 0.3960  -0.0302 0.0174  62  GLU   A CD  
149  C CD  B GLU   A 19  ? 0.9835 0.9434 0.3677 0.3960  -0.0302 0.0174  62  GLU   A CD  
150  C CD  C GLU   A 19  ? 1.0231 0.9742 0.3291 0.4428  0.0228  0.0718  62  GLU   A CD  
151  C CD  D GLU   A 19  ? 1.0231 0.9742 0.3291 0.4428  0.0228  0.0718  62  GLU   A CD  
152  O OE1 A GLU   A 19  ? 1.0333 0.9902 0.3820 0.4250  -0.0305 0.0240  62  GLU   A OE1 
153  O OE1 B GLU   A 19  ? 1.0333 0.9902 0.3820 0.4250  -0.0305 0.0240  62  GLU   A OE1 
154  O OE1 C GLU   A 19  ? 1.0194 0.9699 0.3589 0.4178  0.0362  0.0827  62  GLU   A OE1 
155  O OE1 D GLU   A 19  ? 1.0194 0.9699 0.3589 0.4178  0.0362  0.0827  62  GLU   A OE1 
156  O OE2 A GLU   A 19  ? 0.9668 0.9311 0.3793 0.3797  -0.0427 0.0028  62  GLU   A OE2 
157  O OE2 B GLU   A 19  ? 0.9668 0.9311 0.3793 0.3797  -0.0427 0.0028  62  GLU   A OE2 
158  O OE2 C GLU   A 19  ? 1.0703 1.0181 0.3378 0.4719  0.0306  0.0843  62  GLU   A OE2 
159  O OE2 D GLU   A 19  ? 1.0703 1.0181 0.3378 0.4719  0.0306  0.0843  62  GLU   A OE2 
160  N N   . LYS   A 20  ? 1.0595 1.0196 0.3633 0.4473  -0.0581 -0.0204 63  LYS   A N   
161  C CA  . LYS   A 20  ? 1.1197 1.0785 0.3874 0.4730  -0.0619 -0.0265 63  LYS   A CA  
162  C C   . LYS   A 20  ? 1.1425 1.1006 0.3770 0.4945  -0.0379 -0.0001 63  LYS   A C   
163  O O   . LYS   A 20  ? 1.1329 1.0897 0.3595 0.5018  -0.0300 0.0144  63  LYS   A O   
164  C CB  . LYS   A 20  ? 1.1988 1.1578 0.4465 0.4950  -0.0907 -0.0528 63  LYS   A CB  
165  C CG  . LYS   A 20  ? 1.2282 1.1868 0.5051 0.4778  -0.1138 -0.0808 63  LYS   A CG  
166  C CD  . LYS   A 20  ? 1.2851 1.2461 0.5560 0.4935  -0.1433 -0.1070 63  LYS   A CD  
167  C CE  . LYS   A 20  ? 1.2960 1.2561 0.6004 0.4754  -0.1653 -0.1344 63  LYS   A CE  
168  N NZ  . LYS   A 20  ? 1.3278 1.2938 0.6450 0.4798  -0.1903 -0.1562 63  LYS   A NZ  
169  N N   . ASP   A 21  ? 1.1636 1.1224 0.3833 0.5023  -0.0247 0.0074  64  ASP   A N   
170  C CA  . ASP   A 21  ? 1.2363 1.1957 0.4246 0.5239  0.0006  0.0334  64  ASP   A CA  
171  C C   . ASP   A 21  ? 1.1721 1.1313 0.3883 0.5026  0.0251  0.0600  64  ASP   A C   
172  O O   . ASP   A 21  ? 1.2124 1.1687 0.4103 0.5170  0.0388  0.0793  64  ASP   A O   
173  C CB  . ASP   A 21  ? 1.3355 1.2927 0.4733 0.5627  -0.0075 0.0313  64  ASP   A CB  
174  C CG  . ASP   A 21  ? 1.4136 1.3709 0.5219 0.5863  -0.0319 0.0040  64  ASP   A CG  
175  O OD1 . ASP   A 21  ? 1.4678 1.4266 0.5465 0.6066  -0.0226 0.0076  64  ASP   A OD1 
176  O OD2 . ASP   A 21  ? 1.4386 1.3952 0.5543 0.5853  -0.0602 -0.0211 64  ASP   A OD2 
177  N N   . ALA   A 22  ? 1.1071 1.0684 0.3675 0.4690  0.0306  0.0614  65  ALA   A N   
178  C CA  . ALA   A 22  ? 1.0432 1.0055 0.3296 0.4506  0.0572  0.0874  65  ALA   A CA  
179  C C   . ALA   A 22  ? 1.0357 1.0040 0.3250 0.4501  0.0804  0.1035  65  ALA   A C   
180  O O   . ALA   A 22  ? 1.0536 1.0251 0.3297 0.4594  0.0744  0.0930  65  ALA   A O   
181  C CB  . ALA   A 22  ? 1.0119 0.9754 0.3454 0.4146  0.0532  0.0809  65  ALA   A CB  
182  N N   . GLU   A 23  ? 1.0414 1.0100 0.3380 0.4485  0.1070  0.1307  66  GLU   A N   
183  C CA  . GLU   A 23  ? 1.0449 1.0215 0.3499 0.4476  0.1322  0.1488  66  GLU   A CA  
184  C C   . GLU   A 23  ? 1.0224 1.0059 0.3511 0.4298  0.1225  0.1327  66  GLU   A C   
185  O O   . GLU   A 23  ? 0.9224 0.9044 0.2842 0.4025  0.1098  0.1209  66  GLU   A O   
186  C CB  . GLU   A 23  ? 1.0783 1.0540 0.4120 0.4322  0.1563  0.1738  66  GLU   A CB  
187  C CG  . GLU   A 23  ? 1.1276 1.1133 0.4744 0.4315  0.1834  0.1932  66  GLU   A CG  
188  C CD  . GLU   A 23  ? 1.1838 1.1665 0.5529 0.4229  0.2092  0.2203  66  GLU   A CD  
189  O OE1 . GLU   A 23  ? 1.2624 1.2401 0.6036 0.4459  0.2274  0.2412  66  GLU   A OE1 
190  O OE2 . GLU   A 23  ? 1.1615 1.1461 0.5759 0.3937  0.2111  0.2204  66  GLU   A OE2 
191  N N   . VAL   A 24  ? 1.0253 1.0153 0.3346 0.4466  0.1264  0.1303  67  VAL   A N   
192  C CA  . VAL   A 24  ? 1.0017 0.9969 0.3327 0.4312  0.1167  0.1152  67  VAL   A CA  
193  C C   . VAL   A 24  ? 0.9914 0.9986 0.3453 0.4240  0.1417  0.1336  67  VAL   A C   
194  O O   . VAL   A 24  ? 1.0243 1.0372 0.3569 0.4456  0.1605  0.1484  67  VAL   A O   
195  C CB  . VAL   A 24  ? 1.0388 1.0319 0.3386 0.4518  0.0982  0.0941  67  VAL   A CB  
196  C CG1 . VAL   A 24  ? 1.0051 1.0007 0.3284 0.4355  0.0887  0.0802  67  VAL   A CG1 
197  C CG2 . VAL   A 24  ? 1.0637 1.0467 0.3425 0.4610  0.0735  0.0755  67  VAL   A CG2 
198  N N   . THR   A 25  ? 0.9270 0.9387 0.3233 0.3953  0.1423  0.1330  68  THR   A N   
199  C CA  . THR   A 25  ? 0.9124 0.9371 0.3380 0.3859  0.1657  0.1506  68  THR   A CA  
200  C C   . THR   A 25  ? 0.8699 0.8992 0.3328 0.3594  0.1557  0.1395  68  THR   A C   
201  O O   . THR   A 25  ? 0.8511 0.8719 0.3131 0.3502  0.1332  0.1207  68  THR   A O   
202  C CB  . THR   A 25  ? 0.9273 0.9509 0.3640 0.3826  0.1869  0.1738  68  THR   A CB  
203  O OG1 . THR   A 25  ? 0.9472 0.9847 0.4058 0.3816  0.2133  0.1932  68  THR   A OG1 
204  C CG2 . THR   A 25  ? 0.9112 0.9274 0.3776 0.3564  0.1787  0.1709  68  THR   A CG2 
205  N N   . GLY   A 26  ? 0.8573 0.9000 0.3515 0.3490  0.1719  0.1508  69  GLY   A N   
206  C CA  . GLY   A 26  ? 0.8403 0.8891 0.3696 0.3260  0.1636  0.1419  69  GLY   A CA  
207  C C   . GLY   A 26  ? 0.8571 0.9109 0.3770 0.3356  0.1550  0.1299  69  GLY   A C   
208  O O   . GLY   A 26  ? 0.8997 0.9457 0.3848 0.3546  0.1442  0.1193  69  GLY   A O   
209  N N   . ASN   A 27  ? 0.8277 0.8941 0.3789 0.3236  0.1588  0.1308  70  ASN   A N   
210  C CA  . ASN   A 27  ? 0.8301 0.9008 0.3780 0.3301  0.1493  0.1189  70  ASN   A CA  
211  C C   . ASN   A 27  ? 0.7962 0.8565 0.3554 0.3104  0.1263  0.1026  70  ASN   A C   
212  O O   . ASN   A 27  ? 0.7457 0.7963 0.3110 0.2945  0.1189  0.1004  70  ASN   A O   
213  C CB  . ASN   A 27  ? 0.8513 0.9436 0.4233 0.3338  0.1696  0.1317  70  ASN   A CB  
214  C CG  . ASN   A 27  ? 0.8485 0.9513 0.4674 0.3082  0.1724  0.1358  70  ASN   A CG  
215  O OD1 . ASN   A 27  ? 0.8631 0.9626 0.4990 0.2926  0.1764  0.1424  70  ASN   A OD1 
216  N ND2 . ASN   A 27  ? 0.8571 0.9722 0.4969 0.3047  0.1689  0.1306  70  ASN   A ND2 
217  N N   . SER   A 28  ? 0.7903 0.8515 0.3506 0.3125  0.1157  0.0920  71  SER   A N   
218  C CA  . SER   A 28  ? 0.7907 0.8386 0.3526 0.2998  0.0936  0.0763  71  SER   A CA  
219  C C   . SER   A 28  ? 0.7840 0.8428 0.3722 0.2911  0.0927  0.0760  71  SER   A C   
220  O O   . SER   A 28  ? 0.8083 0.8625 0.3880 0.2989  0.0823  0.0665  71  SER   A O   
221  C CB  . SER   A 28  ? 0.8086 0.8405 0.3380 0.3150  0.0778  0.0614  71  SER   A CB  
222  O OG  . SER   A 28  ? 0.8773 0.9040 0.3801 0.3297  0.0807  0.0625  71  SER   A OG  
223  N N   . PRO   A 29  ? 0.7649 0.8380 0.3865 0.2757  0.1025  0.0855  72  PRO   A N   
224  C CA  . PRO   A 29  ? 0.7600 0.8471 0.4084 0.2699  0.1020  0.0852  72  PRO   A CA  
225  C C   . PRO   A 29  ? 0.7508 0.8256 0.4010 0.2566  0.0815  0.0732  72  PRO   A C   
226  O O   . PRO   A 29  ? 0.7129 0.7754 0.3616 0.2417  0.0733  0.0697  72  PRO   A O   
227  C CB  . PRO   A 29  ? 0.7450 0.8495 0.4290 0.2568  0.1177  0.0977  72  PRO   A CB  
228  C CG  . PRO   A 29  ? 0.7389 0.8302 0.4161 0.2460  0.1172  0.0997  72  PRO   A CG  
229  C CD  . PRO   A 29  ? 0.7629 0.8386 0.3997 0.2629  0.1129  0.0955  72  PRO   A CD  
230  N N   . ARG   A 30  ? 0.7690 0.8473 0.4219 0.2632  0.0745  0.0679  73  ARG   A N   
231  C CA  . ARG   A 30  ? 0.8090 0.8777 0.4661 0.2521  0.0571  0.0594  73  ARG   A CA  
232  C C   . ARG   A 30  ? 0.7550 0.8434 0.4475 0.2400  0.0601  0.0637  73  ARG   A C   
233  O O   . ARG   A 30  ? 0.7230 0.8300 0.4319 0.2491  0.0674  0.0670  73  ARG   A O   
234  C CB  . ARG   A 30  ? 0.8914 0.9499 0.5301 0.2676  0.0465  0.0509  73  ARG   A CB  
235  C CG  . ARG   A 30  ? 0.9821 1.0177 0.5884 0.2763  0.0382  0.0427  73  ARG   A CG  
236  C CD  . ARG   A 30  ? 1.0900 1.1179 0.6781 0.2968  0.0317  0.0346  73  ARG   A CD  
237  N NE  . ARG   A 30  ? 1.1640 1.1712 0.7234 0.3061  0.0233  0.0249  73  ARG   A NE  
238  C CZ  . ARG   A 30  ? 1.2128 1.1958 0.7600 0.3034  0.0065  0.0140  73  ARG   A CZ  
239  N NH1 . ARG   A 30  ? 1.2466 1.2212 0.8041 0.2922  -0.0029 0.0129  73  ARG   A NH1 
240  N NH2 . ARG   A 30  ? 1.1778 1.1451 0.7031 0.3123  -0.0008 0.0041  73  ARG   A NH2 
241  N N   . LEU   A 31  ? 0.7261 0.8108 0.4301 0.2208  0.0539  0.0625  74  LEU   A N   
242  C CA  . LEU   A 31  ? 0.6986 0.8021 0.4374 0.2084  0.0557  0.0648  74  LEU   A CA  
243  C C   . LEU   A 31  ? 0.6746 0.7692 0.4119 0.1981  0.0380  0.0570  74  LEU   A C   
244  O O   . LEU   A 31  ? 0.6606 0.7352 0.3780 0.1906  0.0297  0.0531  74  LEU   A O   
245  C CB  . LEU   A 31  ? 0.6963 0.8045 0.4506 0.1960  0.0669  0.0711  74  LEU   A CB  
246  C CG  . LEU   A 31  ? 0.7160 0.8332 0.4729 0.2060  0.0865  0.0817  74  LEU   A CG  
247  C CD1 . LEU   A 31  ? 0.7084 0.8236 0.4760 0.1935  0.0954  0.0877  74  LEU   A CD1 
248  C CD2 . LEU   A 31  ? 0.7219 0.8646 0.5072 0.2137  0.0984  0.0877  74  LEU   A CD2 
249  N N   . ASP   A 32  ? 0.6604 0.7703 0.4184 0.1986  0.0328  0.0551  75  ASP   A N   
250  C CA  . ASP   A 32  ? 0.6628 0.7683 0.4225 0.1890  0.0171  0.0489  75  ASP   A CA  
251  C C   . ASP   A 32  ? 0.6048 0.7182 0.3855 0.1718  0.0186  0.0485  75  ASP   A C   
252  O O   . ASP   A 32  ? 0.5851 0.7214 0.3998 0.1688  0.0270  0.0509  75  ASP   A O   
253  C CB  . ASP   A 32  ? 0.6997 0.8211 0.4756 0.1976  0.0100  0.0463  75  ASP   A CB  
254  C CG  . ASP   A 32  ? 0.7586 0.8710 0.5141 0.2156  0.0075  0.0457  75  ASP   A CG  
255  O OD1 . ASP   A 32  ? 0.8145 0.9025 0.5394 0.2184  0.0050  0.0447  75  ASP   A OD1 
256  O OD2 . ASP   A 32  ? 0.8087 0.9392 0.5812 0.2270  0.0082  0.0454  75  ASP   A OD2 
257  N N   . VAL   A 33  ? 0.5946 0.6903 0.3578 0.1611  0.0112  0.0452  76  VAL   A N   
258  C CA  . VAL   A 33  ? 0.5781 0.6785 0.3578 0.1452  0.0122  0.0433  76  VAL   A CA  
259  C C   . VAL   A 33  ? 0.5786 0.6699 0.3465 0.1378  -0.0030 0.0364  76  VAL   A C   
260  O O   . VAL   A 33  ? 0.5766 0.6501 0.3164 0.1424  -0.0118 0.0354  76  VAL   A O   
261  C CB  . VAL   A 33  ? 0.5720 0.6627 0.3447 0.1396  0.0231  0.0473  76  VAL   A CB  
262  C CG1 . VAL   A 33  ? 0.5843 0.6812 0.3605 0.1502  0.0380  0.0553  76  VAL   A CG1 
263  C CG2 . VAL   A 33  ? 0.5811 0.6476 0.3210 0.1374  0.0169  0.0448  76  VAL   A CG2 
264  N N   . ALA   A 34  ? 0.5596 0.6618 0.3482 0.1270  -0.0056 0.0320  77  ALA   A N   
265  C CA  . ALA   A 34  ? 0.5587 0.6540 0.3361 0.1194  -0.0182 0.0250  77  ALA   A CA  
266  C C   . ALA   A 34  ? 0.5433 0.6330 0.3230 0.1065  -0.0128 0.0233  77  ALA   A C   
267  O O   . ALA   A 34  ? 0.5468 0.6454 0.3492 0.1025  -0.0018 0.0260  77  ALA   A O   
268  C CB  . ALA   A 34  ? 0.5558 0.6705 0.3560 0.1206  -0.0285 0.0186  77  ALA   A CB  
269  N N   . LEU   A 35  ? 0.5379 0.6120 0.2931 0.1012  -0.0190 0.0201  78  LEU   A N   
270  C CA  . LEU   A 35  ? 0.5313 0.5994 0.2855 0.0899  -0.0155 0.0170  78  LEU   A CA  
271  C C   . LEU   A 35  ? 0.5432 0.6157 0.2976 0.0848  -0.0269 0.0078  78  LEU   A C   
272  O O   . LEU   A 35  ? 0.5648 0.6294 0.2951 0.0895  -0.0367 0.0070  78  LEU   A O   
273  C CB  . LEU   A 35  ? 0.5325 0.5796 0.2574 0.0895  -0.0120 0.0209  78  LEU   A CB  
274  C CG  . LEU   A 35  ? 0.5262 0.5664 0.2473 0.0792  -0.0083 0.0177  78  LEU   A CG  
275  C CD1 . LEU   A 35  ? 0.5160 0.5644 0.2613 0.0748  0.0013  0.0185  78  LEU   A CD1 
276  C CD2 . LEU   A 35  ? 0.5332 0.5548 0.2284 0.0790  -0.0064 0.0205  78  LEU   A CD2 
277  N N   . ASP   A 36  ? 0.5245 0.6089 0.3050 0.0770  -0.0262 0.0014  79  ASP   A N   
278  C CA  . ASP   A 36  ? 0.5357 0.6267 0.3193 0.0734  -0.0386 -0.0100 79  ASP   A CA  
279  C C   . ASP   A 36  ? 0.5364 0.6138 0.2993 0.0664  -0.0375 -0.0137 79  ASP   A C   
280  O O   . ASP   A 36  ? 0.5234 0.5885 0.2757 0.0632  -0.0272 -0.0079 79  ASP   A O   
281  C CB  . ASP   A 36  ? 0.5324 0.6446 0.3589 0.0696  -0.0406 -0.0171 79  ASP   A CB  
282  C CG  . ASP   A 36  ? 0.5244 0.6384 0.3771 0.0592  -0.0308 -0.0189 79  ASP   A CG  
283  O OD1 . ASP   A 36  ? 0.5238 0.6233 0.3606 0.0550  -0.0230 -0.0157 79  ASP   A OD1 
284  O OD2 . ASP   A 36  ? 0.5418 0.6722 0.4334 0.0553  -0.0315 -0.0239 79  ASP   A OD2 
285  N N   . GLU   A 37  ? 0.5538 0.6343 0.3107 0.0651  -0.0484 -0.0242 80  GLU   A N   
286  C CA  . GLU   A 37  ? 0.5705 0.6391 0.3044 0.0602  -0.0474 -0.0281 80  GLU   A CA  
287  C C   . GLU   A 37  ? 0.5453 0.6138 0.2997 0.0510  -0.0377 -0.0309 80  GLU   A C   
288  O O   . GLU   A 37  ? 0.5567 0.6134 0.2931 0.0475  -0.0319 -0.0301 80  GLU   A O   
289  C CB  . GLU   A 37  ? 0.6038 0.6775 0.3255 0.0638  -0.0619 -0.0391 80  GLU   A CB  
290  C CG  . GLU   A 37  ? 0.6465 0.7076 0.3369 0.0619  -0.0605 -0.0416 80  GLU   A CG  
291  C CD  . GLU   A 37  ? 0.6853 0.7517 0.3602 0.0674  -0.0749 -0.0532 80  GLU   A CD  
292  O OE1 . GLU   A 37  ? 0.6982 0.7742 0.3904 0.0639  -0.0808 -0.0675 80  GLU   A OE1 
293  O OE2 . GLU   A 37  ? 0.7367 0.7976 0.3830 0.0762  -0.0811 -0.0485 80  GLU   A OE2 
294  N N   . SER   A 38  ? 0.5415 0.6220 0.3334 0.0473  -0.0350 -0.0331 81  SER   A N   
295  C CA  . SER   A 38  ? 0.5380 0.6166 0.3517 0.0394  -0.0248 -0.0336 81  SER   A CA  
296  C C   . SER   A 38  ? 0.5268 0.5964 0.3359 0.0408  -0.0107 -0.0198 81  SER   A C   
297  O O   . SER   A 38  ? 0.5151 0.5820 0.3400 0.0361  -0.0018 -0.0182 81  SER   A O   
298  C CB  . SER   A 38  ? 0.5506 0.6437 0.4072 0.0350  -0.0262 -0.0395 81  SER   A CB  
299  O OG  . SER   A 38  ? 0.5947 0.6971 0.4579 0.0344  -0.0412 -0.0546 81  SER   A OG  
300  N N   . GLY   A 39  ? 0.5250 0.5892 0.3126 0.0477  -0.0094 -0.0110 82  GLY   A N   
301  C CA  . GLY   A 39  ? 0.5267 0.5822 0.3069 0.0507  0.0018  0.0000  82  GLY   A CA  
302  C C   . GLY   A 39  ? 0.5158 0.5806 0.3222 0.0537  0.0104  0.0073  82  GLY   A C   
303  O O   . GLY   A 39  ? 0.5073 0.5654 0.3099 0.0561  0.0204  0.0151  82  GLY   A O   
304  N N   . ASP   A 40  ? 0.5249 0.6049 0.3558 0.0543  0.0067  0.0051  83  ASP   A N   
305  C CA  . ASP   A 40  ? 0.5455 0.6375 0.4036 0.0578  0.0159  0.0129  83  ASP   A CA  
306  C C   . ASP   A 40  ? 0.5441 0.6390 0.3880 0.0688  0.0136  0.0183  83  ASP   A C   
307  O O   . ASP   A 40  ? 0.5335 0.6333 0.3715 0.0717  0.0015  0.0125  83  ASP   A O   
308  C CB  . ASP   A 40  ? 0.5658 0.6741 0.4654 0.0510  0.0139  0.0064  83  ASP   A CB  
309  C CG  . ASP   A 40  ? 0.5942 0.6972 0.5097 0.0407  0.0170  0.0013  83  ASP   A CG  
310  O OD1 . ASP   A 40  ? 0.6515 0.7404 0.5504 0.0402  0.0246  0.0061  83  ASP   A OD1 
311  O OD2 . ASP   A 40  ? 0.6487 0.7615 0.5933 0.0338  0.0107  -0.0087 83  ASP   A OD2 
312  N N   . PHE   A 41  ? 0.5398 0.6315 0.3780 0.0761  0.0249  0.0288  84  PHE   A N   
313  C CA  . PHE   A 41  ? 0.5470 0.6432 0.3773 0.0882  0.0253  0.0342  84  PHE   A CA  
314  C C   . PHE   A 41  ? 0.5562 0.6744 0.4232 0.0895  0.0289  0.0356  84  PHE   A C   
315  O O   . PHE   A 41  ? 0.5691 0.6953 0.4660 0.0824  0.0374  0.0372  84  PHE   A O   
316  C CB  . PHE   A 41  ? 0.5305 0.6163 0.3418 0.0965  0.0359  0.0433  84  PHE   A CB  
317  C CG  . PHE   A 41  ? 0.5314 0.5975 0.3075 0.0975  0.0301  0.0410  84  PHE   A CG  
318  C CD1 . PHE   A 41  ? 0.5320 0.5907 0.2864 0.1031  0.0203  0.0384  84  PHE   A CD1 
319  C CD2 . PHE   A 41  ? 0.5271 0.5817 0.2936 0.0934  0.0349  0.0419  84  PHE   A CD2 
320  C CE1 . PHE   A 41  ? 0.5439 0.5844 0.2704 0.1031  0.0162  0.0369  84  PHE   A CE1 
321  C CE2 . PHE   A 41  ? 0.5378 0.5765 0.2766 0.0940  0.0298  0.0392  84  PHE   A CE2 
322  C CZ  . PHE   A 41  ? 0.5470 0.5787 0.2672 0.0985  0.0211  0.0370  84  PHE   A CZ  
323  N N   . SER   A 42  ? 0.5793 0.7070 0.4466 0.0983  0.0231  0.0349  85  SER   A N   
324  C CA  . SER   A 42  ? 0.5871 0.7386 0.4919 0.1012  0.0276  0.0366  85  SER   A CA  
325  C C   . SER   A 42  ? 0.6124 0.7672 0.5041 0.1165  0.0290  0.0416  85  SER   A C   
326  O O   . SER   A 42  ? 0.6107 0.7496 0.4671 0.1230  0.0202  0.0400  85  SER   A O   
327  C CB  . SER   A 42  ? 0.6083 0.7741 0.5382 0.0944  0.0139  0.0250  85  SER   A CB  
328  O OG  . SER   A 42  ? 0.6024 0.7626 0.5063 0.1000  -0.0030 0.0181  85  SER   A OG  
329  N N   . LEU   A 43  ? 0.6443 0.8176 0.5634 0.1223  0.0411  0.0482  86  LEU   A N   
330  C CA  . LEU   A 43  ? 0.6769 0.8559 0.5863 0.1386  0.0432  0.0521  86  LEU   A CA  
331  C C   . LEU   A 43  ? 0.6925 0.8838 0.6116 0.1423  0.0270  0.0433  86  LEU   A C   
332  O O   . LEU   A 43  ? 0.6682 0.8803 0.6256 0.1358  0.0240  0.0383  86  LEU   A O   
333  C CB  . LEU   A 43  ? 0.6939 0.8902 0.6300 0.1439  0.0637  0.0628  86  LEU   A CB  
334  C CG  . LEU   A 43  ? 0.7119 0.8933 0.6263 0.1471  0.0791  0.0731  86  LEU   A CG  
335  C CD1 . LEU   A 43  ? 0.7304 0.9286 0.6772 0.1478  0.1010  0.0849  86  LEU   A CD1 
336  C CD2 . LEU   A 43  ? 0.7436 0.9106 0.6162 0.1632  0.0770  0.0743  86  LEU   A CD2 
337  N N   . VAL   A 44  ? 0.7371 0.9152 0.6232 0.1528  0.0165  0.0412  87  VAL   A N   
338  C CA  . VAL   A 44  ? 0.7833 0.9720 0.6736 0.1630  0.0034  0.0358  87  VAL   A CA  
339  C C   . VAL   A 44  ? 0.8364 1.0417 0.7415 0.1771  0.0155  0.0418  87  VAL   A C   
340  O O   . VAL   A 44  ? 0.8866 1.0858 0.7810 0.1817  0.0312  0.0500  87  VAL   A O   
341  C CB  . VAL   A 44  ? 0.7837 0.9466 0.6301 0.1687  -0.0107 0.0331  87  VAL   A CB  
342  C CG1 . VAL   A 44  ? 0.7946 0.9646 0.6409 0.1812  -0.0242 0.0288  87  VAL   A CG1 
343  C CG2 . VAL   A 44  ? 0.7717 0.9181 0.6010 0.1555  -0.0190 0.0288  87  VAL   A CG2 
344  N N   . GLU   A 45  ? 0.9057 1.1317 0.8332 0.1854  0.0087  0.0377  88  GLU   A N   
345  C CA  . GLU   A 45  ? 0.9526 1.1975 0.8969 0.2001  0.0209  0.0428  88  GLU   A CA  
346  C C   . GLU   A 45  ? 0.9705 1.2215 0.9114 0.2148  0.0061  0.0367  88  GLU   A C   
347  O O   . GLU   A 45  ? 0.9564 1.1951 0.8793 0.2142  -0.0132 0.0298  88  GLU   A O   
348  C CB  . GLU   A 45  ? 0.9767 1.2513 0.9732 0.1922  0.0358  0.0462  88  GLU   A CB  
349  C CG  . GLU   A 45  ? 0.9939 1.2609 0.9892 0.1842  0.0558  0.0564  88  GLU   A CG  
350  C CD  . GLU   A 45  ? 0.9975 1.2651 0.9798 0.1992  0.0750  0.0672  88  GLU   A CD  
351  O OE1 . GLU   A 45  ? 1.0029 1.2655 0.9609 0.2157  0.0699  0.0654  88  GLU   A OE1 
352  O OE2 . GLU   A 45  ? 0.9969 1.2700 0.9938 0.1955  0.0949  0.0774  88  GLU   A OE2 
353  N N   . GLY   B 7   ? 0.8353 0.8568 0.6190 0.0866  0.0393  -0.0843 16  GLY   B N   
354  C CA  . GLY   B 7   ? 0.8537 0.8663 0.6278 0.0936  0.0391  -0.0744 16  GLY   B CA  
355  C C   . GLY   B 7   ? 0.8375 0.8462 0.6033 0.1000  0.0352  -0.0738 16  GLY   B C   
356  O O   . GLY   B 7   ? 0.8625 0.8748 0.6297 0.0970  0.0326  -0.0803 16  GLY   B O   
357  N N   . GLU   B 8   ? 0.8022 0.8042 0.5596 0.1086  0.0347  -0.0661 17  GLU   B N   
358  C CA  . GLU   B 8   ? 0.7650 0.7623 0.5121 0.1160  0.0309  -0.0645 17  GLU   B CA  
359  C C   . GLU   B 8   ? 0.7299 0.7265 0.4712 0.1100  0.0309  -0.0637 17  GLU   B C   
360  O O   . GLU   B 8   ? 0.7224 0.7180 0.4606 0.1062  0.0345  -0.0576 17  GLU   B O   
361  C CB  . GLU   B 8   ? 0.7923 0.7838 0.5313 0.1259  0.0317  -0.0552 17  GLU   B CB  
362  C CG  . GLU   B 8   ? 0.8017 0.7889 0.5302 0.1360  0.0272  -0.0547 17  GLU   B CG  
363  C CD  . GLU   B 8   ? 0.8389 0.8219 0.5601 0.1471  0.0281  -0.0462 17  GLU   B CD  
364  O OE1 . GLU   B 8   ? 0.8308 0.8140 0.5538 0.1457  0.0329  -0.0384 17  GLU   B OE1 
365  O OE2 . GLU   B 8   ? 0.8789 0.8588 0.5931 0.1573  0.0237  -0.0475 17  GLU   B OE2 
366  N N   A THR   B 9   ? 0.7250 0.7219 0.4651 0.1094  0.0263  -0.0696 18  THR   B N   
367  N N   B THR   B 9   ? 0.7167 0.7138 0.4571 0.1093  0.0263  -0.0698 18  THR   B N   
368  N N   C THR   B 9   ? 0.7250 0.7219 0.4651 0.1094  0.0263  -0.0696 18  THR   B N   
369  N N   D THR   B 9   ? 0.7167 0.7138 0.4571 0.1093  0.0263  -0.0698 18  THR   B N   
370  C CA  A THR   B 9   ? 0.7200 0.7157 0.4556 0.1029  0.0251  -0.0699 18  THR   B CA  
371  C CA  B THR   B 9   ? 0.7064 0.7024 0.4426 0.1027  0.0250  -0.0705 18  THR   B CA  
372  C CA  C THR   B 9   ? 0.7200 0.7157 0.4556 0.1029  0.0251  -0.0699 18  THR   B CA  
373  C CA  D THR   B 9   ? 0.7064 0.7024 0.4426 0.1027  0.0250  -0.0705 18  THR   B CA  
374  C C   A THR   B 9   ? 0.7104 0.6996 0.4361 0.1111  0.0191  -0.0698 18  THR   B C   
375  C C   B THR   B 9   ? 0.7027 0.6915 0.4276 0.1114  0.0197  -0.0687 18  THR   B C   
376  C C   C THR   B 9   ? 0.7104 0.6996 0.4361 0.1111  0.0191  -0.0698 18  THR   B C   
377  C C   D THR   B 9   ? 0.7027 0.6915 0.4276 0.1114  0.0197  -0.0687 18  THR   B C   
378  O O   A THR   B 9   ? 0.7166 0.7035 0.4386 0.1065  0.0165  -0.0708 18  THR   B O   
379  O O   B THR   B 9   ? 0.7073 0.6930 0.4264 0.1077  0.0183  -0.0673 18  THR   B O   
380  O O   C THR   B 9   ? 0.7166 0.7035 0.4386 0.1065  0.0165  -0.0708 18  THR   B O   
381  O O   D THR   B 9   ? 0.7073 0.6930 0.4264 0.1077  0.0183  -0.0673 18  THR   B O   
382  C CB  A THR   B 9   ? 0.7232 0.7260 0.4684 0.0920  0.0250  -0.0775 18  THR   B CB  
383  C CB  B THR   B 9   ? 0.7004 0.7032 0.4461 0.0932  0.0238  -0.0788 18  THR   B CB  
384  C CB  C THR   B 9   ? 0.7232 0.7260 0.4684 0.0920  0.0250  -0.0775 18  THR   B CB  
385  C CB  D THR   B 9   ? 0.7004 0.7032 0.4461 0.0932  0.0238  -0.0788 18  THR   B CB  
386  O OG1 A THR   B 9   ? 0.7290 0.7380 0.4836 0.0883  0.0294  -0.0793 18  THR   B OG1 
387  O OG1 B THR   B 9   ? 0.6962 0.7015 0.4476 0.0984  0.0199  -0.0854 18  THR   B OG1 
388  O OG1 C THR   B 9   ? 0.7290 0.7380 0.4836 0.0883  0.0294  -0.0793 18  THR   B OG1 
389  O OG1 D THR   B 9   ? 0.6962 0.7015 0.4476 0.0984  0.0199  -0.0854 18  THR   B OG1 
390  C CG2 A THR   B 9   ? 0.7304 0.7328 0.4725 0.0825  0.0258  -0.0761 18  THR   B CG2 
391  C CG2 B THR   B 9   ? 0.6994 0.7094 0.4536 0.0834  0.0294  -0.0800 18  THR   B CG2 
392  C CG2 C THR   B 9   ? 0.7304 0.7328 0.4725 0.0825  0.0258  -0.0761 18  THR   B CG2 
393  C CG2 D THR   B 9   ? 0.6994 0.7094 0.4536 0.0834  0.0294  -0.0800 18  THR   B CG2 
394  N N   . THR   B 10  ? 0.6993 0.6852 0.4205 0.1230  0.0166  -0.0687 19  THR   B N   
395  C CA  . THR   B 10  ? 0.6812 0.6605 0.3914 0.1329  0.0106  -0.0685 19  THR   B CA  
396  C C   . THR   B 10  ? 0.6442 0.6190 0.3438 0.1336  0.0120  -0.0615 19  THR   B C   
397  O O   . THR   B 10  ? 0.6444 0.6202 0.3425 0.1339  0.0177  -0.0541 19  THR   B O   
398  C CB  . THR   B 10  ? 0.6810 0.6580 0.3870 0.1462  0.0088  -0.0671 19  THR   B CB  
399  O OG1 . THR   B 10  ? 0.6993 0.6807 0.4158 0.1454  0.0087  -0.0724 19  THR   B OG1 
400  C CG2 . THR   B 10  ? 0.6981 0.6694 0.3947 0.1561  0.0012  -0.0701 19  THR   B CG2 
401  N N   . ASP   B 11  ? 0.6360 0.6062 0.3292 0.1338  0.0065  -0.0638 20  ASP   B N   
402  C CA  . ASP   B 11  ? 0.6417 0.6065 0.3227 0.1382  0.0062  -0.0577 20  ASP   B CA  
403  C C   . ASP   B 11  ? 0.6485 0.6127 0.3216 0.1505  0.0092  -0.0505 20  ASP   B C   
404  O O   . ASP   B 11  ? 0.6473 0.6119 0.3204 0.1592  0.0077  -0.0518 20  ASP   B O   
405  C CB  . ASP   B 11  ? 0.6628 0.6208 0.3364 0.1413  -0.0022 -0.0621 20  ASP   B CB  
406  C CG  . ASP   B 11  ? 0.6808 0.6387 0.3610 0.1283  -0.0049 -0.0670 20  ASP   B CG  
407  O OD1 . ASP   B 11  ? 0.6469 0.6111 0.3371 0.1168  0.0003  -0.0674 20  ASP   B OD1 
408  O OD2 . ASP   B 11  ? 0.7039 0.6552 0.3786 0.1299  -0.0125 -0.0702 20  ASP   B OD2 
409  N N   . GLY   B 12  ? 0.6172 0.5812 0.2843 0.1512  0.0132  -0.0430 21  GLY   B N   
410  C CA  . GLY   B 12  ? 0.6135 0.5772 0.2711 0.1633  0.0156  -0.0353 21  GLY   B CA  
411  C C   . GLY   B 12  ? 0.5958 0.5631 0.2548 0.1589  0.0228  -0.0270 21  GLY   B C   
412  O O   . GLY   B 12  ? 0.5781 0.5464 0.2427 0.1472  0.0247  -0.0278 21  GLY   B O   
413  N N   . VAL   B 13  ? 0.5742 0.5438 0.2284 0.1679  0.0266  -0.0190 22  VAL   B N   
414  C CA  . VAL   B 13  ? 0.5590 0.5329 0.2148 0.1654  0.0336  -0.0098 22  VAL   B CA  
415  C C   . VAL   B 13  ? 0.5527 0.5306 0.2190 0.1623  0.0388  -0.0059 22  VAL   B C   
416  O O   . VAL   B 13  ? 0.5567 0.5340 0.2239 0.1682  0.0375  -0.0073 22  VAL   B O   
417  C CB  . VAL   B 13  ? 0.5622 0.5365 0.2054 0.1771  0.0341  -0.0031 22  VAL   B CB  
418  C CG1 . VAL   B 13  ? 0.5690 0.5441 0.2051 0.1913  0.0338  0.0001  22  VAL   B CG1 
419  C CG2 . VAL   B 13  ? 0.5572 0.5366 0.2026 0.1739  0.0405  0.0057  22  VAL   B CG2 
420  N N   . TYR   B 14  ? 0.5396 0.5207 0.2141 0.1528  0.0438  -0.0020 23  TYR   B N   
421  C CA  . TYR   B 14  ? 0.5388 0.5228 0.2249 0.1478  0.0479  0.0006  23  TYR   B CA  
422  C C   . TYR   B 14  ? 0.5380 0.5258 0.2267 0.1462  0.0536  0.0106  23  TYR   B C   
423  O O   . TYR   B 14  ? 0.5438 0.5326 0.2296 0.1428  0.0547  0.0127  23  TYR   B O   
424  C CB  . TYR   B 14  ? 0.5358 0.5201 0.2325 0.1355  0.0472  -0.0072 23  TYR   B CB  
425  C CG  . TYR   B 14  ? 0.5444 0.5268 0.2422 0.1360  0.0422  -0.0169 23  TYR   B CG  
426  C CD1 . TYR   B 14  ? 0.5560 0.5351 0.2457 0.1392  0.0369  -0.0221 23  TYR   B CD1 
427  C CD2 . TYR   B 14  ? 0.5513 0.5352 0.2590 0.1333  0.0423  -0.0208 23  TYR   B CD2 
428  C CE1 . TYR   B 14  ? 0.5672 0.5452 0.2594 0.1388  0.0321  -0.0310 23  TYR   B CE1 
429  C CE2 . TYR   B 14  ? 0.5616 0.5449 0.2715 0.1335  0.0378  -0.0300 23  TYR   B CE2 
430  C CZ  . TYR   B 14  ? 0.5757 0.5565 0.2783 0.1361  0.0328  -0.0348 23  TYR   B CZ  
431  O OH  . TYR   B 14  ? 0.6103 0.5912 0.3165 0.1358  0.0281  -0.0438 23  TYR   B OH  
432  N N   . ARG   B 15  ? 0.5373 0.5271 0.2328 0.1471  0.0568  0.0163  24  ARG   B N   
433  C CA  . ARG   B 15  ? 0.5404 0.5341 0.2425 0.1433  0.0621  0.0257  24  ARG   B CA  
434  C C   . ARG   B 15  ? 0.5328 0.5266 0.2468 0.1303  0.0628  0.0214  24  ARG   B C   
435  O O   . ARG   B 15  ? 0.5172 0.5090 0.2367 0.1264  0.0604  0.0137  24  ARG   B O   
436  C CB  . ARG   B 15  ? 0.5531 0.5482 0.2579 0.1496  0.0648  0.0343  24  ARG   B CB  
437  C CG  . ARG   B 15  ? 0.5712 0.5668 0.2635 0.1634  0.0644  0.0388  24  ARG   B CG  
438  C CD  . ARG   B 15  ? 0.5895 0.5854 0.2855 0.1681  0.0665  0.0461  24  ARG   B CD  
439  N NE  . ARG   B 15  ? 0.6031 0.5990 0.2864 0.1819  0.0656  0.0493  24  ARG   B NE  
440  C CZ  . ARG   B 15  ? 0.6123 0.6133 0.2874 0.1903  0.0691  0.0589  24  ARG   B CZ  
441  N NH1 . ARG   B 15  ? 0.6008 0.6076 0.2802 0.1863  0.0741  0.0671  24  ARG   B NH1 
442  N NH2 . ARG   B 15  ? 0.6357 0.6363 0.2982 0.2033  0.0676  0.0601  24  ARG   B NH2 
443  N N   . VAL   B 16  ? 0.5370 0.5335 0.2549 0.1246  0.0659  0.0266  25  VAL   B N   
444  C CA  . VAL   B 16  ? 0.5382 0.5352 0.2675 0.1132  0.0669  0.0242  25  VAL   B CA  
445  C C   . VAL   B 16  ? 0.5411 0.5403 0.2798 0.1125  0.0703  0.0336  25  VAL   B C   
446  O O   . VAL   B 16  ? 0.5523 0.5550 0.2895 0.1152  0.0733  0.0426  25  VAL   B O   
447  C CB  . VAL   B 16  ? 0.5418 0.5394 0.2685 0.1065  0.0669  0.0220  25  VAL   B CB  
448  C CG1 . VAL   B 16  ? 0.5334 0.5315 0.2710 0.0955  0.0675  0.0186  25  VAL   B CG1 
449  C CG2 . VAL   B 16  ? 0.5444 0.5392 0.2615 0.1075  0.0631  0.0140  25  VAL   B CG2 
450  N N   . MET   B 17  ? 0.5622 0.5595 0.3106 0.1090  0.0695  0.0311  26  MET   B N   
451  C CA  . MET   B 17  ? 0.5828 0.5803 0.3411 0.1089  0.0714  0.0394  26  MET   B CA  
452  C C   . MET   B 17  ? 0.6056 0.6026 0.3761 0.0984  0.0709  0.0366  26  MET   B C   
453  O O   . MET   B 17  ? 0.5900 0.5859 0.3616 0.0925  0.0687  0.0261  26  MET   B O   
454  C CB  . MET   B 17  ? 0.5869 0.5810 0.3462 0.1145  0.0693  0.0379  26  MET   B CB  
455  C CG  . MET   B 17  ? 0.6050 0.5987 0.3519 0.1253  0.0685  0.0383  26  MET   B CG  
456  S SD  . MET   B 17  ? 0.6071 0.6053 0.3461 0.1344  0.0729  0.0526  26  MET   B SD  
457  C CE  . MET   B 17  ? 0.6228 0.6210 0.3749 0.1321  0.0753  0.0636  26  MET   B CE  
458  N N   . THR   B 18  ? 0.6281 0.6257 0.4081 0.0964  0.0726  0.0453  27  THR   B N   
459  C CA  . THR   B 18  ? 0.6769 0.6727 0.4700 0.0877  0.0711  0.0427  27  THR   B CA  
460  C C   . THR   B 18  ? 0.7146 0.7077 0.5175 0.0892  0.0706  0.0503  27  THR   B C   
461  O O   . THR   B 18  ? 0.6867 0.6816 0.4873 0.0953  0.0732  0.0612  27  THR   B O   
462  C CB  . THR   B 18  ? 0.6744 0.6734 0.4703 0.0810  0.0726  0.0451  27  THR   B CB  
463  O OG1 . THR   B 18  ? 0.6783 0.6750 0.4859 0.0732  0.0702  0.0410  27  THR   B OG1 
464  C CG2 . THR   B 18  ? 0.6762 0.6796 0.4725 0.0841  0.0762  0.0581  27  THR   B CG2 
465  N N   . ARG   B 19  ? 0.7711 0.7602 0.5847 0.0838  0.0673  0.0450  28  ARG   B N   
466  C CA  . ARG   B 19  ? 0.8279 0.8130 0.6531 0.0833  0.0658  0.0520  28  ARG   B CA  
467  C C   . ARG   B 19  ? 0.8233 0.8084 0.6609 0.0750  0.0650  0.0550  28  ARG   B C   
468  O O   . ARG   B 19  ? 0.8120 0.7927 0.6608 0.0733  0.0626  0.0598  28  ARG   B O   
469  C CB  . ARG   B 19  ? 0.8605 0.8400 0.6884 0.0852  0.0615  0.0436  28  ARG   B CB  
470  C CG  . ARG   B 19  ? 0.9122 0.8916 0.7290 0.0939  0.0618  0.0418  28  ARG   B CG  
471  C CD  . ARG   B 19  ? 0.9350 0.9088 0.7552 0.0993  0.0594  0.0457  28  ARG   B CD  
472  N NE  . ARG   B 19  ? 0.9663 0.9396 0.7764 0.1074  0.0585  0.0410  28  ARG   B NE  
473  C CZ  . ARG   B 19  ? 1.0071 0.9800 0.8151 0.1075  0.0555  0.0278  28  ARG   B CZ  
474  N NH1 . ARG   B 19  ? 1.0652 1.0387 0.8798 0.1003  0.0536  0.0180  28  ARG   B NH1 
475  N NH2 . ARG   B 19  ? 1.0180 0.9905 0.8174 0.1152  0.0544  0.0246  28  ARG   B NH2 
476  N N   . ARG   B 20  ? 0.8564 0.8456 0.6920 0.0702  0.0665  0.0530  29  ARG   B N   
477  C CA  . ARG   B 20  ? 0.9244 0.9135 0.7709 0.0621  0.0650  0.0536  29  ARG   B CA  
478  C C   . ARG   B 20  ? 0.9179 0.9102 0.7713 0.0620  0.0677  0.0684  29  ARG   B C   
479  O O   . ARG   B 20  ? 0.9284 0.9212 0.7920 0.0556  0.0664  0.0710  29  ARG   B O   
480  C CB  . ARG   B 20  ? 0.9710 0.9633 0.8111 0.0577  0.0655  0.0455  29  ARG   B CB  
481  C CG  . ARG   B 20  ? 1.0563 1.0471 0.9054 0.0496  0.0624  0.0403  29  ARG   B CG  
482  C CD  . ARG   B 20  ? 1.1430 1.1376 0.9843 0.0460  0.0638  0.0356  29  ARG   B CD  
483  N NE  . ARG   B 20  ? 1.2133 1.2128 1.0481 0.0492  0.0678  0.0445  29  ARG   B NE  
484  C CZ  . ARG   B 20  ? 1.2733 1.2761 1.1132 0.0467  0.0690  0.0524  29  ARG   B CZ  
485  N NH1 . ARG   B 20  ? 1.3231 1.3244 1.1750 0.0405  0.0662  0.0527  29  ARG   B NH1 
486  N NH2 . ARG   B 20  ? 1.2690 1.2770 1.1021 0.0508  0.0727  0.0597  29  ARG   B NH2 
487  N N   . LEU   B 21  ? 0.8810 0.8762 0.7288 0.0691  0.0713  0.0778  30  LEU   B N   
488  C CA  . LEU   B 21  ? 0.8438 0.8439 0.6971 0.0704  0.0749  0.0932  30  LEU   B CA  
489  C C   . LEU   B 21  ? 0.8175 0.8140 0.6739 0.0753  0.0747  0.1011  30  LEU   B C   
490  O O   . LEU   B 21  ? 0.8004 0.7894 0.6576 0.0759  0.0705  0.0935  30  LEU   B O   
491  C CB  . LEU   B 21  ? 0.8396 0.8477 0.6806 0.0754  0.0798  0.0966  30  LEU   B CB  
492  C CG  . LEU   B 21  ? 0.8471 0.8609 0.6905 0.0704  0.0812  0.0979  30  LEU   B CG  
493  C CD1 . LEU   B 21  ? 0.8489 0.8584 0.7000 0.0613  0.0768  0.0883  30  LEU   B CD1 
494  C CD2 . LEU   B 21  ? 0.8448 0.8634 0.6728 0.0756  0.0839  0.0950  30  LEU   B CD2 
495  N N   . LEU   B 22  ? 0.8021 0.8039 0.6604 0.0786  0.0789  0.1157  31  LEU   B N   
496  C CA  . LEU   B 22  ? 0.7841 0.7829 0.6445 0.0835  0.0792  0.1251  31  LEU   B CA  
497  C C   . LEU   B 22  ? 0.7798 0.7770 0.6243 0.0929  0.0797  0.1198  31  LEU   B C   
498  O O   . LEU   B 22  ? 0.8055 0.8083 0.6376 0.0974  0.0827  0.1171  31  LEU   B O   
499  C CB  . LEU   B 22  ? 0.7742 0.7814 0.6389 0.0849  0.0845  0.1423  31  LEU   B CB  
500  C CG  . LEU   B 22  ? 0.7695 0.7739 0.6391 0.0880  0.0849  0.1545  31  LEU   B CG  
501  C CD1 . LEU   B 22  ? 0.7543 0.7510 0.6426 0.0794  0.0797  0.1572  31  LEU   B CD1 
502  C CD2 . LEU   B 22  ? 0.7719 0.7879 0.6387 0.0931  0.0922  0.1704  31  LEU   B CD2 
503  N N   . GLY   B 23  ? 0.7697 0.7590 0.6147 0.0958  0.0762  0.1178  32  GLY   B N   
504  C CA  . GLY   B 23  ? 0.7528 0.7396 0.5840 0.1044  0.0755  0.1109  32  GLY   B CA  
505  C C   . GLY   B 23  ? 0.7427 0.7310 0.5645 0.1042  0.0746  0.0964  32  GLY   B C   
506  O O   . GLY   B 23  ? 0.7410 0.7284 0.5687 0.0963  0.0724  0.0879  32  GLY   B O   
507  N N   . SER   B 24  ? 0.7146 0.7045 0.5220 0.1127  0.0758  0.0936  33  SER   B N   
508  C CA  . SER   B 24  ? 0.6868 0.6785 0.4832 0.1139  0.0753  0.0819  33  SER   B CA  
509  C C   . SER   B 24  ? 0.6686 0.6681 0.4564 0.1175  0.0800  0.0885  33  SER   B C   
510  O O   . SER   B 24  ? 0.6580 0.6606 0.4394 0.1256  0.0829  0.0979  33  SER   B O   
511  C CB  . SER   B 24  ? 0.6896 0.6775 0.4769 0.1213  0.0726  0.0745  33  SER   B CB  
512  O OG  . SER   B 24  ? 0.6989 0.6803 0.4944 0.1179  0.0679  0.0669  33  SER   B OG  
513  N N   . THR   B 25  ? 0.6309 0.6337 0.4189 0.1118  0.0806  0.0842  34  THR   B N   
514  C CA  . THR   B 25  ? 0.6259 0.6361 0.4073 0.1143  0.0845  0.0901  34  THR   B CA  
515  C C   . THR   B 25  ? 0.6167 0.6266 0.3855 0.1165  0.0829  0.0796  34  THR   B C   
516  O O   . THR   B 25  ? 0.5859 0.5918 0.3566 0.1101  0.0797  0.0685  34  THR   B O   
517  C CB  . THR   B 25  ? 0.6294 0.6433 0.4223 0.1057  0.0861  0.0949  34  THR   B CB  
518  O OG1 . THR   B 25  ? 0.6429 0.6559 0.4491 0.1027  0.0864  0.1041  34  THR   B OG1 
519  C CG2 . THR   B 25  ? 0.6277 0.6501 0.4147 0.1089  0.0901  0.1017  34  THR   B CG2 
520  N N   . GLN   B 26  ? 0.6025 0.6164 0.3587 0.1253  0.0849  0.0828  35  GLN   B N   
521  C CA  . GLN   B 26  ? 0.5918 0.6045 0.3357 0.1279  0.0826  0.0733  35  GLN   B CA  
522  C C   . GLN   B 26  ? 0.5889 0.6056 0.3333 0.1228  0.0840  0.0740  35  GLN   B C   
523  O O   . GLN   B 26  ? 0.5895 0.6130 0.3329 0.1266  0.0877  0.0838  35  GLN   B O   
524  C CB  . GLN   B 26  ? 0.5852 0.5991 0.3146 0.1406  0.0828  0.0751  35  GLN   B CB  
525  C CG  . GLN   B 26  ? 0.5744 0.5865 0.2916 0.1433  0.0796  0.0660  35  GLN   B CG  
526  C CD  . GLN   B 26  ? 0.5761 0.5882 0.2790 0.1562  0.0784  0.0660  35  GLN   B CD  
527  O OE1 . GLN   B 26  ? 0.5826 0.5923 0.2838 0.1619  0.0775  0.0665  35  GLN   B OE1 
528  N NE2 . GLN   B 26  ? 0.5636 0.5775 0.2556 0.1613  0.0776  0.0647  35  GLN   B NE2 
529  N N   . VAL   B 27  ? 0.5858 0.5990 0.3317 0.1147  0.0811  0.0643  36  VAL   B N   
530  C CA  . VAL   B 27  ? 0.5713 0.5868 0.3174 0.1090  0.0815  0.0635  36  VAL   B CA  
531  C C   . VAL   B 27  ? 0.5565 0.5712 0.2882 0.1141  0.0797  0.0586  36  VAL   B C   
532  O O   . VAL   B 27  ? 0.5546 0.5721 0.2835 0.1131  0.0804  0.0604  36  VAL   B O   
533  C CB  . VAL   B 27  ? 0.5774 0.5895 0.3328 0.0975  0.0794  0.0563  36  VAL   B CB  
534  C CG1 . VAL   B 27  ? 0.5907 0.6037 0.3607 0.0930  0.0808  0.0624  36  VAL   B CG1 
535  C CG2 . VAL   B 27  ? 0.5711 0.5778 0.3238 0.0957  0.0759  0.0449  36  VAL   B CG2 
536  N N   . GLY   B 28  ? 0.5405 0.5511 0.2636 0.1194  0.0768  0.0523  37  GLY   B N   
537  C CA  . GLY   B 28  ? 0.5233 0.5325 0.2325 0.1256  0.0743  0.0483  37  GLY   B CA  
538  C C   . GLY   B 28  ? 0.5164 0.5204 0.2193 0.1298  0.0703  0.0403  37  GLY   B C   
539  O O   . GLY   B 28  ? 0.5310 0.5342 0.2378 0.1322  0.0705  0.0408  37  GLY   B O   
540  N N   . VAL   B 29  ? 0.5111 0.5114 0.2044 0.1312  0.0663  0.0335  38  VAL   B N   
541  C CA  . VAL   B 29  ? 0.5138 0.5095 0.1985 0.1375  0.0616  0.0265  38  VAL   B CA  
542  C C   . VAL   B 29  ? 0.5128 0.5038 0.1957 0.1298  0.0573  0.0171  38  VAL   B C   
543  O O   . VAL   B 29  ? 0.5029 0.4942 0.1861 0.1235  0.0579  0.0177  38  VAL   B O   
544  C CB  . VAL   B 29  ? 0.5302 0.5270 0.2020 0.1509  0.0609  0.0306  38  VAL   B CB  
545  C CG1 . VAL   B 29  ? 0.5330 0.5246 0.1955 0.1582  0.0552  0.0233  38  VAL   B CG1 
546  C CG2 . VAL   B 29  ? 0.5324 0.5354 0.2058 0.1580  0.0660  0.0413  38  VAL   B CG2 
547  N N   . GLY   B 30  ? 0.5140 0.5009 0.1942 0.1309  0.0529  0.0091  39  GLY   B N   
548  C CA  . GLY   B 30  ? 0.5090 0.4915 0.1861 0.1249  0.0483  0.0011  39  GLY   B CA  
549  C C   . GLY   B 30  ? 0.5189 0.4973 0.1911 0.1298  0.0428  -0.0058 39  GLY   B C   
550  O O   . GLY   B 30  ? 0.5237 0.5025 0.1937 0.1394  0.0422  -0.0047 39  GLY   B O   
551  N N   . VAL   B 31  ? 0.5118 0.4862 0.1817 0.1241  0.0384  -0.0122 40  VAL   B N   
552  C CA  . VAL   B 31  ? 0.5243 0.4940 0.1894 0.1275  0.0317  -0.0194 40  VAL   B CA  
553  C C   . VAL   B 31  ? 0.5294 0.4998 0.2038 0.1172  0.0305  -0.0269 40  VAL   B C   
554  O O   . VAL   B 31  ? 0.5119 0.4827 0.1899 0.1061  0.0315  -0.0283 40  VAL   B O   
555  C CB  . VAL   B 31  ? 0.5362 0.5000 0.1906 0.1301  0.0264  -0.0205 40  VAL   B CB  
556  C CG1 . VAL   B 31  ? 0.5463 0.5047 0.1979 0.1317  0.0189  -0.0285 40  VAL   B CG1 
557  C CG2 . VAL   B 31  ? 0.5437 0.5079 0.1882 0.1422  0.0273  -0.0139 40  VAL   B CG2 
558  N N   . MET   B 32  ? 0.5315 0.5023 0.2091 0.1209  0.0281  -0.0316 41  MET   B N   
559  C CA  . MET   B 32  ? 0.5369 0.5092 0.2229 0.1126  0.0260  -0.0397 41  MET   B CA  
560  C C   . MET   B 32  ? 0.5533 0.5202 0.2336 0.1147  0.0182  -0.0453 41  MET   B C   
561  O O   . MET   B 32  ? 0.5497 0.5127 0.2229 0.1259  0.0136  -0.0461 41  MET   B O   
562  C CB  . MET   B 32  ? 0.5389 0.5154 0.2331 0.1151  0.0277  -0.0418 41  MET   B CB  
563  C CG  . MET   B 32  ? 0.5369 0.5175 0.2419 0.1061  0.0270  -0.0497 41  MET   B CG  
564  S SD  . MET   B 32  ? 0.5355 0.5220 0.2497 0.0922  0.0334  -0.0491 41  MET   B SD  
565  C CE  . MET   B 32  ? 0.5478 0.5369 0.2674 0.0972  0.0382  -0.0444 41  MET   B CE  
566  N N   . GLN   B 33  ? 0.5572 0.5231 0.2399 0.1042  0.0163  -0.0487 42  GLN   B N   
567  C CA  . GLN   B 33  ? 0.5882 0.5482 0.2668 0.1039  0.0085  -0.0536 42  GLN   B CA  
568  C C   . GLN   B 33  ? 0.5965 0.5599 0.2843 0.0902  0.0085  -0.0583 42  GLN   B C   
569  O O   . GLN   B 33  ? 0.5869 0.5531 0.2773 0.0804  0.0133  -0.0557 42  GLN   B O   
570  C CB  . GLN   B 33  ? 0.6073 0.5596 0.2738 0.1081  0.0047  -0.0502 42  GLN   B CB  
571  C CG  . GLN   B 33  ? 0.6425 0.5878 0.3060 0.1073  -0.0044 -0.0558 42  GLN   B CG  
572  C CD  . GLN   B 33  ? 0.6800 0.6161 0.3302 0.1159  -0.0106 -0.0542 42  GLN   B CD  
573  O OE1 . GLN   B 33  ? 0.7552 0.6847 0.4025 0.1107  -0.0162 -0.0558 42  GLN   B OE1 
574  N NE2 . GLN   B 33  ? 0.6637 0.5998 0.3057 0.1284  -0.0089 -0.0501 42  GLN   B NE2 
575  N N   . GLU   B 34  ? 0.6131 0.5767 0.3057 0.0894  0.0033  -0.0648 43  GLU   B N   
576  C CA  . GLU   B 34  ? 0.6294 0.5980 0.3322 0.0766  0.0031  -0.0696 43  GLU   B CA  
577  C C   . GLU   B 34  ? 0.6149 0.5933 0.3269 0.0687  0.0114  -0.0692 43  GLU   B C   
578  O O   . GLU   B 34  ? 0.6160 0.5980 0.3322 0.0571  0.0137  -0.0696 43  GLU   B O   
579  C CB  . GLU   B 34  ? 0.6642 0.6268 0.3621 0.0690  -0.0004 -0.0681 43  GLU   B CB  
580  C CG  . GLU   B 34  ? 0.7003 0.6528 0.3905 0.0758  -0.0101 -0.0700 43  GLU   B CG  
581  C CD  . GLU   B 34  ? 0.7311 0.6743 0.4123 0.0724  -0.0144 -0.0670 43  GLU   B CD  
582  O OE1 . GLU   B 34  ? 0.7603 0.7040 0.4458 0.0604  -0.0149 -0.0674 43  GLU   B OE1 
583  O OE2 . GLU   B 34  ? 0.7980 0.7334 0.4678 0.0825  -0.0177 -0.0643 43  GLU   B OE2 
584  N N   . GLY   B 35  ? 0.5880 0.5704 0.3031 0.0746  0.0157  -0.0683 44  GLY   B N   
585  C CA  . GLY   B 35  ? 0.5645 0.5558 0.2891 0.0679  0.0225  -0.0691 44  GLY   B CA  
586  C C   . GLY   B 35  ? 0.5418 0.5330 0.2633 0.0627  0.0279  -0.0632 44  GLY   B C   
587  O O   . GLY   B 35  ? 0.5356 0.5336 0.2645 0.0567  0.0329  -0.0642 44  GLY   B O   
588  N N   . VAL   B 36  ? 0.5256 0.5095 0.2368 0.0656  0.0265  -0.0577 45  VAL   B N   
589  C CA  . VAL   B 36  ? 0.5115 0.4945 0.2190 0.0624  0.0309  -0.0516 45  VAL   B CA  
590  C C   . VAL   B 36  ? 0.5043 0.4845 0.2064 0.0731  0.0323  -0.0455 45  VAL   B C   
591  O O   . VAL   B 36  ? 0.5067 0.4817 0.2013 0.0829  0.0282  -0.0445 45  VAL   B O   
592  C CB  . VAL   B 36  ? 0.5129 0.4908 0.2136 0.0559  0.0283  -0.0502 45  VAL   B CB  
593  C CG1 . VAL   B 36  ? 0.5107 0.4865 0.2060 0.0548  0.0316  -0.0438 45  VAL   B CG1 
594  C CG2 . VAL   B 36  ? 0.5163 0.4990 0.2236 0.0439  0.0285  -0.0549 45  VAL   B CG2 
595  N N   . PHE   B 37  ? 0.4910 0.4747 0.1970 0.0715  0.0378  -0.0416 46  PHE   B N   
596  C CA  . PHE   B 37  ? 0.4938 0.4763 0.1963 0.0796  0.0403  -0.0345 46  PHE   B CA  
597  C C   . PHE   B 37  ? 0.4896 0.4694 0.1856 0.0773  0.0413  -0.0291 46  PHE   B C   
598  O O   . PHE   B 37  ? 0.4777 0.4592 0.1766 0.0680  0.0435  -0.0292 46  PHE   B O   
599  C CB  . PHE   B 37  ? 0.4926 0.4800 0.2042 0.0800  0.0447  -0.0332 46  PHE   B CB  
600  C CG  . PHE   B 37  ? 0.5006 0.4869 0.2092 0.0892  0.0467  -0.0255 46  PHE   B CG  
601  C CD1 . PHE   B 37  ? 0.5106 0.4944 0.2131 0.1004  0.0441  -0.0241 46  PHE   B CD1 
602  C CD2 . PHE   B 37  ? 0.5016 0.4900 0.2136 0.0868  0.0510  -0.0195 46  PHE   B CD2 
603  C CE1 . PHE   B 37  ? 0.5165 0.5005 0.2159 0.1090  0.0464  -0.0162 46  PHE   B CE1 
604  C CE2 . PHE   B 37  ? 0.5092 0.4977 0.2194 0.0947  0.0531  -0.0115 46  PHE   B CE2 
605  C CZ  . PHE   B 37  ? 0.5162 0.5029 0.2201 0.1058  0.0512  -0.0097 46  PHE   B CZ  
606  N N   . HIS   B 38  ? 0.4829 0.4588 0.1700 0.0865  0.0395  -0.0245 47  HIS   B N   
607  C CA  . HIS   B 38  ? 0.4863 0.4591 0.1654 0.0872  0.0392  -0.0195 47  HIS   B CA  
608  C C   . HIS   B 38  ? 0.4902 0.4660 0.1691 0.0943  0.0433  -0.0117 47  HIS   B C   
609  O O   . HIS   B 38  ? 0.4901 0.4666 0.1664 0.1047  0.0432  -0.0093 47  HIS   B O   
610  C CB  . HIS   B 38  ? 0.4917 0.4577 0.1600 0.0931  0.0328  -0.0211 47  HIS   B CB  
611  C CG  . HIS   B 38  ? 0.4937 0.4562 0.1622 0.0873  0.0277  -0.0281 47  HIS   B CG  
612  N ND1 . HIS   B 38  ? 0.4932 0.4573 0.1668 0.0883  0.0260  -0.0334 47  HIS   B ND1 
613  C CD2 . HIS   B 38  ? 0.4980 0.4560 0.1634 0.0793  0.0243  -0.0302 47  HIS   B CD2 
614  C CE1 . HIS   B 38  ? 0.4984 0.4595 0.1724 0.0817  0.0215  -0.0386 47  HIS   B CE1 
615  N NE2 . HIS   B 38  ? 0.5006 0.4577 0.1695 0.0756  0.0205  -0.0364 47  HIS   B NE2 
616  N N   . THR   B 39  ? 0.4917 0.4697 0.1730 0.0893  0.0468  -0.0073 48  THR   B N   
617  C CA  . THR   B 39  ? 0.4945 0.4762 0.1765 0.0951  0.0507  0.0008  48  THR   B CA  
618  C C   . THR   B 39  ? 0.5042 0.4857 0.1839 0.0909  0.0515  0.0044  48  THR   B C   
619  O O   . THR   B 39  ? 0.4983 0.4757 0.1743 0.0840  0.0486  0.0004  48  THR   B O   
620  C CB  . THR   B 39  ? 0.4907 0.4772 0.1835 0.0947  0.0550  0.0031  48  THR   B CB  
621  O OG1 . THR   B 39  ? 0.4899 0.4802 0.1836 0.1011  0.0585  0.0119  48  THR   B OG1 
622  C CG2 . THR   B 39  ? 0.4887 0.4772 0.1913 0.0834  0.0572  0.0005  48  THR   B CG2 
623  N N   . MET   B 40  ? 0.5133 0.4994 0.1954 0.0948  0.0553  0.0119  49  MET   B N   
624  C CA  . MET   B 40  ? 0.5188 0.5058 0.2002 0.0913  0.0563  0.0157  49  MET   B CA  
625  C C   . MET   B 40  ? 0.5080 0.4981 0.2007 0.0812  0.0595  0.0161  49  MET   B C   
626  O O   . MET   B 40  ? 0.4944 0.4877 0.1967 0.0800  0.0623  0.0168  49  MET   B O   
627  C CB  . MET   B 40  ? 0.5413 0.5325 0.2190 0.1010  0.0581  0.0236  49  MET   B CB  
628  C CG  . MET   B 40  ? 0.5604 0.5497 0.2273 0.1129  0.0552  0.0232  49  MET   B CG  
629  S SD  . MET   B 40  ? 0.5958 0.5882 0.2537 0.1231  0.0551  0.0294  49  MET   B SD  
630  C CE  . MET   B 40  ? 0.6043 0.5883 0.2543 0.1170  0.0490  0.0235  49  MET   B CE  
631  N N   A TRP   B 41  ? 0.5077 0.4961 0.1991 0.0741  0.0585  0.0150  50  TRP   B N   
632  N N   B TRP   B 41  ? 0.5045 0.4930 0.1961 0.0740  0.0586  0.0150  50  TRP   B N   
633  N N   C TRP   B 41  ? 0.5077 0.4961 0.1991 0.0741  0.0585  0.0150  50  TRP   B N   
634  N N   D TRP   B 41  ? 0.5045 0.4930 0.1961 0.0740  0.0586  0.0150  50  TRP   B N   
635  C CA  A TRP   B 41  ? 0.5059 0.4964 0.2066 0.0643  0.0607  0.0141  50  TRP   B CA  
636  C CA  B TRP   B 41  ? 0.5005 0.4911 0.2015 0.0642  0.0607  0.0140  50  TRP   B CA  
637  C CA  C TRP   B 41  ? 0.5059 0.4964 0.2066 0.0643  0.0607  0.0141  50  TRP   B CA  
638  C CA  D TRP   B 41  ? 0.5005 0.4911 0.2015 0.0642  0.0607  0.0140  50  TRP   B CA  
639  C C   A TRP   B 41  ? 0.5032 0.4995 0.2142 0.0663  0.0646  0.0209  50  TRP   B C   
640  C C   B TRP   B 41  ? 0.4999 0.4963 0.2110 0.0661  0.0646  0.0209  50  TRP   B C   
641  C C   C TRP   B 41  ? 0.5032 0.4995 0.2142 0.0663  0.0646  0.0209  50  TRP   B C   
642  C C   D TRP   B 41  ? 0.4999 0.4963 0.2110 0.0661  0.0646  0.0209  50  TRP   B C   
643  O O   A TRP   B 41  ? 0.5026 0.5007 0.2246 0.0601  0.0663  0.0190  50  TRP   B O   
644  O O   B TRP   B 41  ? 0.4991 0.4973 0.2211 0.0598  0.0663  0.0194  50  TRP   B O   
645  O O   C TRP   B 41  ? 0.5026 0.5007 0.2246 0.0601  0.0663  0.0190  50  TRP   B O   
646  O O   D TRP   B 41  ? 0.4991 0.4973 0.2211 0.0598  0.0663  0.0194  50  TRP   B O   
647  C CB  A TRP   B 41  ? 0.5076 0.4954 0.2037 0.0580  0.0588  0.0131  50  TRP   B CB  
648  C CB  B TRP   B 41  ? 0.4986 0.4862 0.1948 0.0575  0.0587  0.0125  50  TRP   B CB  
649  C CB  C TRP   B 41  ? 0.5076 0.4954 0.2037 0.0580  0.0588  0.0131  50  TRP   B CB  
650  C CB  D TRP   B 41  ? 0.4986 0.4862 0.1948 0.0575  0.0587  0.0125  50  TRP   B CB  
651  C CG  A TRP   B 41  ? 0.5058 0.4949 0.2097 0.0481  0.0601  0.0101  50  TRP   B CG  
652  C CG  B TRP   B 41  ? 0.4931 0.4829 0.1979 0.0485  0.0605  0.0111  50  TRP   B CG  
653  C CG  C TRP   B 41  ? 0.5058 0.4949 0.2097 0.0481  0.0601  0.0101  50  TRP   B CG  
654  C CG  D TRP   B 41  ? 0.4931 0.4829 0.1979 0.0485  0.0605  0.0111  50  TRP   B CG  
655  C CD1 A TRP   B 41  ? 0.5053 0.4927 0.2092 0.0408  0.0593  0.0033  50  TRP   B CD1 
656  C CD1 B TRP   B 41  ? 0.4891 0.4827 0.2018 0.0473  0.0626  0.0158  50  TRP   B CD1 
657  C CD1 C TRP   B 41  ? 0.5053 0.4927 0.2092 0.0408  0.0593  0.0033  50  TRP   B CD1 
658  C CD1 D TRP   B 41  ? 0.4891 0.4827 0.2018 0.0473  0.0626  0.0158  50  TRP   B CD1 
659  C CD2 A TRP   B 41  ? 0.5044 0.4975 0.2180 0.0452  0.0626  0.0136  50  TRP   B CD2 
660  C CD2 B TRP   B 41  ? 0.4912 0.4799 0.1981 0.0400  0.0602  0.0044  50  TRP   B CD2 
661  C CD2 C TRP   B 41  ? 0.5044 0.4975 0.2180 0.0452  0.0626  0.0136  50  TRP   B CD2 
662  C CD2 D TRP   B 41  ? 0.4912 0.4799 0.1981 0.0400  0.0602  0.0044  50  TRP   B CD2 
663  N NE1 A TRP   B 41  ? 0.5038 0.4939 0.2156 0.0340  0.0610  0.0019  50  TRP   B NE1 
664  N NE1 B TRP   B 41  ? 0.4849 0.4790 0.2039 0.0389  0.0631  0.0120  50  TRP   B NE1 
665  N NE1 C TRP   B 41  ? 0.5038 0.4939 0.2156 0.0340  0.0610  0.0019  50  TRP   B NE1 
666  N NE1 D TRP   B 41  ? 0.4849 0.4790 0.2039 0.0389  0.0631  0.0120  50  TRP   B NE1 
667  C CE2 A TRP   B 41  ? 0.5016 0.4946 0.2196 0.0365  0.0626  0.0079  50  TRP   B CE2 
668  C CE2 B TRP   B 41  ? 0.4866 0.4783 0.2019 0.0345  0.0619  0.0049  50  TRP   B CE2 
669  C CE2 C TRP   B 41  ? 0.5016 0.4946 0.2196 0.0365  0.0626  0.0079  50  TRP   B CE2 
670  C CE2 D TRP   B 41  ? 0.4866 0.4783 0.2019 0.0345  0.0619  0.0049  50  TRP   B CE2 
671  C CE3 A TRP   B 41  ? 0.5043 0.5016 0.2236 0.0490  0.0645  0.0209  50  TRP   B CE3 
672  C CE3 B TRP   B 41  ? 0.4934 0.4799 0.1966 0.0365  0.0586  -0.0020 50  TRP   B CE3 
673  C CE3 C TRP   B 41  ? 0.5043 0.5016 0.2236 0.0490  0.0645  0.0209  50  TRP   B CE3 
674  C CE3 D TRP   B 41  ? 0.4934 0.4799 0.1966 0.0365  0.0586  -0.0020 50  TRP   B CE3 
675  C CZ2 A TRP   B 41  ? 0.5039 0.4995 0.2312 0.0320  0.0638  0.0089  50  TRP   B CZ2 
676  C CZ2 B TRP   B 41  ? 0.4860 0.4782 0.2045 0.0264  0.0620  -0.0010 50  TRP   B CZ2 
677  C CZ2 C TRP   B 41  ? 0.5039 0.4995 0.2312 0.0320  0.0638  0.0089  50  TRP   B CZ2 
678  C CZ2 D TRP   B 41  ? 0.4860 0.4782 0.2045 0.0264  0.0620  -0.0010 50  TRP   B CZ2 
679  C CZ3 A TRP   B 41  ? 0.5026 0.5026 0.2323 0.0438  0.0658  0.0224  50  TRP   B CZ3 
680  C CZ3 B TRP   B 41  ? 0.4915 0.4796 0.1986 0.0280  0.0594  -0.0073 50  TRP   B CZ3 
681  C CZ3 C TRP   B 41  ? 0.5026 0.5026 0.2323 0.0438  0.0658  0.0224  50  TRP   B CZ3 
682  C CZ3 D TRP   B 41  ? 0.4915 0.4796 0.1986 0.0280  0.0594  -0.0073 50  TRP   B CZ3 
683  C CH2 A TRP   B 41  ? 0.5027 0.5014 0.2361 0.0355  0.0651  0.0161  50  TRP   B CH2 
684  C CH2 B TRP   B 41  ? 0.4878 0.4788 0.2020 0.0234  0.0611  -0.0070 50  TRP   B CH2 
685  C CH2 C TRP   B 41  ? 0.5027 0.5014 0.2361 0.0355  0.0651  0.0161  50  TRP   B CH2 
686  C CH2 D TRP   B 41  ? 0.4878 0.4788 0.2020 0.0234  0.0611  -0.0070 50  TRP   B CH2 
687  N N   . HIS   B 42  ? 0.5045 0.5040 0.2129 0.0740  0.0658  0.0283  51  HIS   B N   
688  C CA  . HIS   B 42  ? 0.5070 0.5128 0.2260 0.0751  0.0696  0.0361  51  HIS   B CA  
689  C C   . HIS   B 42  ? 0.5105 0.5182 0.2365 0.0783  0.0717  0.0379  51  HIS   B C   
690  O O   . HIS   B 42  ? 0.5125 0.5239 0.2492 0.0766  0.0742  0.0430  51  HIS   B O   
691  C CB  . HIS   B 42  ? 0.5178 0.5283 0.2337 0.0818  0.0708  0.0435  51  HIS   B CB  
692  C CG  . HIS   B 42  ? 0.5210 0.5337 0.2298 0.0933  0.0716  0.0471  51  HIS   B CG  
693  N ND1 . HIS   B 42  ? 0.5312 0.5401 0.2265 0.0996  0.0682  0.0438  51  HIS   B ND1 
694  C CD2 . HIS   B 42  ? 0.5355 0.5534 0.2483 0.1000  0.0750  0.0537  51  HIS   B CD2 
695  C CE1 . HIS   B 42  ? 0.5361 0.5482 0.2270 0.1104  0.0696  0.0479  51  HIS   B CE1 
696  N NE2 . HIS   B 42  ? 0.5294 0.5473 0.2307 0.1106  0.0740  0.0541  51  HIS   B NE2 
697  N N   . VAL   B 43  ? 0.5170 0.5215 0.2377 0.0821  0.0703  0.0333  52  VAL   B N   
698  C CA  . VAL   B 43  ? 0.5163 0.5218 0.2428 0.0855  0.0717  0.0346  52  VAL   B CA  
699  C C   . VAL   B 43  ? 0.5258 0.5299 0.2625 0.0766  0.0714  0.0293  52  VAL   B C   
700  O O   . VAL   B 43  ? 0.5274 0.5335 0.2742 0.0764  0.0732  0.0335  52  VAL   B O   
701  C CB  . VAL   B 43  ? 0.5261 0.5287 0.2429 0.0931  0.0695  0.0309  52  VAL   B CB  
702  C CG1 . VAL   B 43  ? 0.5257 0.5278 0.2473 0.0957  0.0698  0.0296  52  VAL   B CG1 
703  C CG2 . VAL   B 43  ? 0.5287 0.5336 0.2362 0.1036  0.0700  0.0369  52  VAL   B CG2 
704  N N   . THR   B 44  ? 0.5050 0.5059 0.2391 0.0702  0.0690  0.0206  53  THR   B N   
705  C CA  . THR   B 44  ? 0.5147 0.5149 0.2569 0.0630  0.0685  0.0139  53  THR   B CA  
706  C C   . THR   B 44  ? 0.5211 0.5219 0.2681 0.0542  0.0686  0.0126  53  THR   B C   
707  O O   . THR   B 44  ? 0.5244 0.5257 0.2805 0.0494  0.0686  0.0094  53  THR   B O   
708  C CB  . THR   B 44  ? 0.5052 0.5032 0.2425 0.0617  0.0662  0.0050  53  THR   B CB  
709  O OG1 . THR   B 44  ? 0.4964 0.4925 0.2256 0.0575  0.0646  0.0021  53  THR   B OG1 
710  C CG2 . THR   B 44  ? 0.5072 0.5042 0.2396 0.0707  0.0653  0.0056  53  THR   B CG2 
711  N N   . LYS   B 45  ? 0.5439 0.5446 0.2852 0.0530  0.0683  0.0151  54  LYS   B N   
712  C CA  . LYS   B 45  ? 0.5851 0.5854 0.3276 0.0447  0.0676  0.0128  54  LYS   B CA  
713  C C   . LYS   B 45  ? 0.5856 0.5844 0.3266 0.0380  0.0663  0.0034  54  LYS   B C   
714  O O   . LYS   B 45  ? 0.5902 0.5897 0.3357 0.0310  0.0661  0.0002  54  LYS   B O   
715  C CB  . LYS   B 45  ? 0.6281 0.6310 0.3827 0.0419  0.0687  0.0168  54  LYS   B CB  
716  C CG  . LYS   B 45  ? 0.6830 0.6890 0.4429 0.0479  0.0707  0.0266  54  LYS   B CG  
717  C CD  . LYS   B 45  ? 0.7252 0.7333 0.4808 0.0500  0.0712  0.0326  54  LYS   B CD  
718  C CE  . LYS   B 45  ? 0.7618 0.7752 0.5264 0.0540  0.0737  0.0427  54  LYS   B CE  
719  N NZ  . LYS   B 45  ? 0.7975 0.8141 0.5542 0.0626  0.0753  0.0488  54  LYS   B NZ  
720  N N   . GLY   B 46  ? 0.5751 0.5725 0.3105 0.0398  0.0653  -0.0010 55  GLY   B N   
721  C CA  . GLY   B 46  ? 0.5760 0.5735 0.3101 0.0335  0.0644  -0.0095 55  GLY   B CA  
722  C C   . GLY   B 46  ? 0.5778 0.5782 0.3216 0.0320  0.0652  -0.0144 55  GLY   B C   
723  O O   . GLY   B 46  ? 0.5726 0.5747 0.3164 0.0268  0.0650  -0.0213 55  GLY   B O   
724  N N   . ALA   B 47  ? 0.5941 0.5952 0.3458 0.0367  0.0660  -0.0109 56  ALA   B N   
725  C CA  . ALA   B 47  ? 0.5839 0.5867 0.3450 0.0362  0.0659  -0.0156 56  ALA   B CA  
726  C C   . ALA   B 47  ? 0.5731 0.5767 0.3321 0.0391  0.0651  -0.0212 56  ALA   B C   
727  O O   . ALA   B 47  ? 0.5600 0.5620 0.3119 0.0436  0.0645  -0.0193 56  ALA   B O   
728  C CB  . ALA   B 47  ? 0.5852 0.5875 0.3552 0.0402  0.0664  -0.0093 56  ALA   B CB  
729  N N   . ALA   B 48  ? 0.5627 0.5689 0.3282 0.0369  0.0648  -0.0283 57  ALA   B N   
730  C CA  . ALA   B 48  ? 0.5626 0.5703 0.3287 0.0402  0.0638  -0.0338 57  ALA   B CA  
731  C C   . ALA   B 48  ? 0.5597 0.5647 0.3278 0.0489  0.0632  -0.0286 57  ALA   B C   
732  O O   . ALA   B 48  ? 0.5634 0.5664 0.3353 0.0511  0.0639  -0.0217 57  ALA   B O   
733  C CB  . ALA   B 48  ? 0.5747 0.5867 0.3483 0.0364  0.0635  -0.0425 57  ALA   B CB  
734  N N   . LEU   B 49  ? 0.5586 0.5636 0.3240 0.0535  0.0618  -0.0318 58  LEU   B N   
735  C CA  . LEU   B 49  ? 0.5743 0.5768 0.3395 0.0627  0.0609  -0.0277 58  LEU   B CA  
736  C C   . LEU   B 49  ? 0.5949 0.5992 0.3658 0.0646  0.0591  -0.0353 58  LEU   B C   
737  O O   . LEU   B 49  ? 0.6172 0.6255 0.3894 0.0600  0.0585  -0.0438 58  LEU   B O   
738  C CB  . LEU   B 49  ? 0.5535 0.5537 0.3080 0.0681  0.0600  -0.0245 58  LEU   B CB  
739  C CG  . LEU   B 49  ? 0.5515 0.5503 0.2992 0.0669  0.0612  -0.0181 58  LEU   B CG  
740  C CD1 . LEU   B 49  ? 0.5506 0.5469 0.2873 0.0719  0.0593  -0.0173 58  LEU   B CD1 
741  C CD2 . LEU   B 49  ? 0.5597 0.5579 0.3105 0.0699  0.0634  -0.0088 58  LEU   B CD2 
742  N N   . ARG   B 50  ? 0.6079 0.6098 0.3824 0.0713  0.0583  -0.0319 59  ARG   B N   
743  C CA  . ARG   B 50  ? 0.6403 0.6428 0.4193 0.0753  0.0560  -0.0382 59  ARG   B CA  
744  C C   . ARG   B 50  ? 0.6552 0.6555 0.4265 0.0836  0.0543  -0.0362 59  ARG   B C   
745  O O   . ARG   B 50  ? 0.6270 0.6241 0.3920 0.0887  0.0553  -0.0275 59  ARG   B O   
746  C CB  . ARG   B 50  ? 0.6759 0.6760 0.4639 0.0767  0.0556  -0.0356 59  ARG   B CB  
747  C CG  . ARG   B 50  ? 0.7309 0.7306 0.5241 0.0817  0.0527  -0.0411 59  ARG   B CG  
748  C CD  . ARG   B 50  ? 0.7695 0.7664 0.5724 0.0815  0.0516  -0.0398 59  ARG   B CD  
749  N NE  . ARG   B 50  ? 0.7911 0.7839 0.5943 0.0818  0.0533  -0.0282 59  ARG   B NE  
750  C CZ  . ARG   B 50  ? 0.8208 0.8092 0.6228 0.0884  0.0532  -0.0192 59  ARG   B CZ  
751  N NH1 . ARG   B 50  ? 0.8231 0.8097 0.6220 0.0960  0.0513  -0.0202 59  ARG   B NH1 
752  N NH2 . ARG   B 50  ? 0.8714 0.8578 0.6751 0.0875  0.0552  -0.0087 59  ARG   B NH2 
753  N N   . SER   B 51  ? 0.6717 0.6742 0.4433 0.0850  0.0518  -0.0443 60  SER   B N   
754  C CA  . SER   B 51  ? 0.7141 0.7142 0.4805 0.0940  0.0490  -0.0446 60  SER   B CA  
755  C C   . SER   B 51  ? 0.7487 0.7502 0.5229 0.0970  0.0464  -0.0514 60  SER   B C   
756  O O   . SER   B 51  ? 0.7569 0.7636 0.5356 0.0929  0.0451  -0.0609 60  SER   B O   
757  C CB  . SER   B 51  ? 0.7089 0.7102 0.4685 0.0927  0.0473  -0.0484 60  SER   B CB  
758  O OG  . SER   B 51  ? 0.7171 0.7159 0.4717 0.1015  0.0439  -0.0493 60  SER   B OG  
759  N N   . GLY   B 52  ? 0.7829 0.7803 0.5590 0.1037  0.0457  -0.0467 61  GLY   B N   
760  C CA  . GLY   B 52  ? 0.8093 0.8070 0.5937 0.1064  0.0430  -0.0528 61  GLY   B CA  
761  C C   . GLY   B 52  ? 0.8261 0.8277 0.6203 0.0984  0.0439  -0.0585 61  GLY   B C   
762  O O   . GLY   B 52  ? 0.8668 0.8665 0.6635 0.0946  0.0461  -0.0530 61  GLY   B O   
763  N N   . GLU   B 53  ? 0.8487 0.8564 0.6487 0.0958  0.0424  -0.0694 62  GLU   B N   
764  C CA  . GLU   B 53  ? 0.8763 0.8892 0.6846 0.0885  0.0435  -0.0760 62  GLU   B CA  
765  C C   . GLU   B 53  ? 0.8383 0.8578 0.6440 0.0800  0.0462  -0.0794 62  GLU   B C   
766  O O   . GLU   B 53  ? 0.8378 0.8623 0.6488 0.0738  0.0476  -0.0843 62  GLU   B O   
767  C CB  . GLU   B 53  ? 0.9333 0.9494 0.7502 0.0917  0.0402  -0.0854 62  GLU   B CB  
768  C CG  . GLU   B 53  ? 1.0097 1.0196 0.8326 0.0951  0.0382  -0.0828 62  GLU   B CG  
769  C CD  . GLU   B 53  ? 1.1071 1.1201 0.9388 0.0983  0.0345  -0.0930 62  GLU   B CD  
770  O OE1 . GLU   B 53  ? 1.2002 1.2163 1.0317 0.1028  0.0323  -0.0985 62  GLU   B OE1 
771  O OE2 . GLU   B 53  ? 1.1418 1.1540 0.9807 0.0965  0.0334  -0.0959 62  GLU   B OE2 
772  N N   . GLY   B 54  ? 0.7957 0.8146 0.5931 0.0800  0.0467  -0.0764 63  GLY   B N   
773  C CA  . GLY   B 54  ? 0.7799 0.8034 0.5736 0.0721  0.0488  -0.0781 63  GLY   B CA  
774  C C   . GLY   B 54  ? 0.7637 0.7841 0.5533 0.0672  0.0518  -0.0709 63  GLY   B C   
775  O O   . GLY   B 54  ? 0.7580 0.7722 0.5453 0.0713  0.0521  -0.0626 63  GLY   B O   
776  N N   . ARG   B 55  ? 0.7265 0.7517 0.5153 0.0587  0.0539  -0.0736 64  ARG   B N   
777  C CA  . ARG   B 55  ? 0.6947 0.7173 0.4789 0.0536  0.0564  -0.0674 64  ARG   B CA  
778  C C   . ARG   B 55  ? 0.6628 0.6842 0.4378 0.0511  0.0565  -0.0648 64  ARG   B C   
779  O O   . ARG   B 55  ? 0.7035 0.7290 0.4780 0.0486  0.0555  -0.0702 64  ARG   B O   
780  C CB  . ARG   B 55  ? 0.7132 0.7411 0.5029 0.0465  0.0583  -0.0723 64  ARG   B CB  
781  C CG  . ARG   B 55  ? 0.7257 0.7500 0.5125 0.0426  0.0601  -0.0660 64  ARG   B CG  
782  C CD  . ARG   B 55  ? 0.7503 0.7793 0.5428 0.0370  0.0611  -0.0715 64  ARG   B CD  
783  N NE  . ARG   B 55  ? 0.7596 0.7872 0.5474 0.0313  0.0628  -0.0674 64  ARG   B NE  
784  C CZ  . ARG   B 55  ? 0.7727 0.7995 0.5643 0.0288  0.0629  -0.0671 64  ARG   B CZ  
785  N NH1 . ARG   B 55  ? 0.7764 0.8032 0.5767 0.0314  0.0612  -0.0707 64  ARG   B NH1 
786  N NH2 . ARG   B 55  ? 0.7672 0.7925 0.5538 0.0239  0.0641  -0.0634 64  ARG   B NH2 
787  N N   . LEU   B 56  ? 0.5984 0.6144 0.3666 0.0518  0.0572  -0.0567 65  LEU   B N   
788  C CA  . LEU   B 56  ? 0.5876 0.6015 0.3466 0.0491  0.0568  -0.0544 65  LEU   B CA  
789  C C   . LEU   B 56  ? 0.5540 0.5684 0.3114 0.0415  0.0592  -0.0521 65  LEU   B C   
790  O O   . LEU   B 56  ? 0.5358 0.5476 0.2943 0.0429  0.0604  -0.0467 65  LEU   B O   
791  C CB  . LEU   B 56  ? 0.5930 0.6003 0.3442 0.0572  0.0552  -0.0471 65  LEU   B CB  
792  C CG  . LEU   B 56  ? 0.6109 0.6164 0.3617 0.0664  0.0525  -0.0479 65  LEU   B CG  
793  C CD1 . LEU   B 56  ? 0.6192 0.6191 0.3597 0.0733  0.0509  -0.0416 65  LEU   B CD1 
794  C CD2 . LEU   B 56  ? 0.6221 0.6314 0.3759 0.0650  0.0500  -0.0566 65  LEU   B CD2 
795  N N   . ASP   B 57  ? 0.5474 0.5654 0.3029 0.0336  0.0598  -0.0561 66  ASP   B N   
796  C CA  . ASP   B 57  ? 0.5348 0.5526 0.2872 0.0267  0.0617  -0.0538 66  ASP   B CA  
797  C C   . ASP   B 57  ? 0.5106 0.5228 0.2528 0.0260  0.0604  -0.0484 66  ASP   B C   
798  O O   . ASP   B 57  ? 0.5115 0.5221 0.2490 0.0265  0.0581  -0.0495 66  ASP   B O   
799  C CB  . ASP   B 57  ? 0.5661 0.5917 0.3221 0.0186  0.0634  -0.0609 66  ASP   B CB  
800  C CG  . ASP   B 57  ? 0.5985 0.6291 0.3645 0.0205  0.0642  -0.0663 66  ASP   B CG  
801  O OD1 . ASP   B 57  ? 0.6273 0.6543 0.3968 0.0246  0.0641  -0.0630 66  ASP   B OD1 
802  O OD2 . ASP   B 57  ? 0.6403 0.6783 0.4110 0.0183  0.0647  -0.0735 66  ASP   B OD2 
803  N N   . PRO   B 58  ? 0.4907 0.4997 0.2293 0.0245  0.0614  -0.0430 67  PRO   B N   
804  C CA  . PRO   B 58  ? 0.4859 0.4897 0.2147 0.0232  0.0600  -0.0384 67  PRO   B CA  
805  C C   . PRO   B 58  ? 0.4846 0.4900 0.2095 0.0152  0.0593  -0.0425 67  PRO   B C   
806  O O   . PRO   B 58  ? 0.4744 0.4861 0.2039 0.0088  0.0614  -0.0475 67  PRO   B O   
807  C CB  . PRO   B 58  ? 0.4873 0.4897 0.2162 0.0221  0.0616  -0.0335 67  PRO   B CB  
808  C CG  . PRO   B 58  ? 0.4918 0.4995 0.2297 0.0184  0.0637  -0.0378 67  PRO   B CG  
809  C CD  . PRO   B 58  ? 0.4979 0.5082 0.2423 0.0234  0.0634  -0.0415 67  PRO   B CD  
810  N N   . TYR   B 59  ? 0.4764 0.4765 0.1932 0.0158  0.0562  -0.0406 68  TYR   B N   
811  C CA  . TYR   B 59  ? 0.4788 0.4789 0.1914 0.0082  0.0547  -0.0430 68  TYR   B CA  
812  C C   . TYR   B 59  ? 0.4754 0.4686 0.1781 0.0055  0.0530  -0.0380 68  TYR   B C   
813  O O   . TYR   B 59  ? 0.4727 0.4669 0.1724 -0.0031 0.0535  -0.0387 68  TYR   B O   
814  C CB  . TYR   B 59  ? 0.4902 0.4892 0.2029 0.0109  0.0512  -0.0458 68  TYR   B CB  
815  C CG  . TYR   B 59  ? 0.4975 0.4972 0.2079 0.0024  0.0495  -0.0481 68  TYR   B CG  
816  C CD1 . TYR   B 59  ? 0.5084 0.4998 0.2093 0.0004  0.0458  -0.0443 68  TYR   B CD1 
817  C CD2 . TYR   B 59  ? 0.5020 0.5108 0.2203 -0.0032 0.0512  -0.0541 68  TYR   B CD2 
818  C CE1 . TYR   B 59  ? 0.5182 0.5092 0.2173 -0.0076 0.0437  -0.0456 68  TYR   B CE1 
819  C CE2 . TYR   B 59  ? 0.5149 0.5251 0.2321 -0.0114 0.0497  -0.0554 68  TYR   B CE2 
820  C CZ  . TYR   B 59  ? 0.5219 0.5230 0.2297 -0.0141 0.0459  -0.0509 68  TYR   B CZ  
821  O OH  . TYR   B 59  ? 0.5513 0.5524 0.2578 -0.0225 0.0438  -0.0511 68  TYR   B OH  
822  N N   . TRP   B 60  ? 0.4699 0.4566 0.1671 0.0127  0.0507  -0.0332 69  TRP   B N   
823  C CA  . TRP   B 60  ? 0.4718 0.4513 0.1593 0.0122  0.0483  -0.0284 69  TRP   B CA  
824  C C   . TRP   B 60  ? 0.4754 0.4533 0.1621 0.0202  0.0490  -0.0231 69  TRP   B C   
825  O O   . TRP   B 60  ? 0.4649 0.4437 0.1545 0.0287  0.0492  -0.0221 69  TRP   B O   
826  C CB  . TRP   B 60  ? 0.4735 0.4461 0.1533 0.0126  0.0429  -0.0286 69  TRP   B CB  
827  C CG  . TRP   B 60  ? 0.4774 0.4419 0.1472 0.0145  0.0395  -0.0239 69  TRP   B CG  
828  C CD1 . TRP   B 60  ? 0.4799 0.4405 0.1435 0.0074  0.0383  -0.0222 69  TRP   B CD1 
829  C CD2 . TRP   B 60  ? 0.4743 0.4340 0.1389 0.0249  0.0370  -0.0203 69  TRP   B CD2 
830  N NE1 . TRP   B 60  ? 0.4827 0.4360 0.1379 0.0128  0.0348  -0.0181 69  TRP   B NE1 
831  C CE2 . TRP   B 60  ? 0.4818 0.4349 0.1375 0.0238  0.0341  -0.0170 69  TRP   B CE2 
832  C CE3 . TRP   B 60  ? 0.4759 0.4365 0.1418 0.0356  0.0368  -0.0195 69  TRP   B CE3 
833  C CZ2 . TRP   B 60  ? 0.4836 0.4321 0.1327 0.0329  0.0313  -0.0133 69  TRP   B CZ2 
834  C CZ3 . TRP   B 60  ? 0.4767 0.4331 0.1356 0.0446  0.0344  -0.0154 69  TRP   B CZ3 
835  C CH2 . TRP   B 60  ? 0.4848 0.4353 0.1354 0.0436  0.0315  -0.0127 69  TRP   B CH2 
836  N N   . GLY   B 61  ? 0.4796 0.4552 0.1622 0.0182  0.0493  -0.0193 70  GLY   B N   
837  C CA  . GLY   B 61  ? 0.4842 0.4588 0.1660 0.0256  0.0498  -0.0137 70  GLY   B CA  
838  C C   . GLY   B 61  ? 0.4969 0.4672 0.1715 0.0235  0.0480  -0.0102 70  GLY   B C   
839  O O   . GLY   B 61  ? 0.4958 0.4647 0.1674 0.0146  0.0475  -0.0122 70  GLY   B O   
840  N N   . ASP   B 62  ? 0.5036 0.4726 0.1756 0.0311  0.0474  -0.0053 71  ASP   B N   
841  C CA  . ASP   B 62  ? 0.5187 0.4838 0.1838 0.0310  0.0452  -0.0017 71  ASP   B CA  
842  C C   . ASP   B 62  ? 0.5126 0.4815 0.1810 0.0392  0.0472  0.0038  71  ASP   B C   
843  O O   . ASP   B 62  ? 0.5114 0.4799 0.1768 0.0485  0.0461  0.0057  71  ASP   B O   
844  C CB  . ASP   B 62  ? 0.5403 0.4969 0.1940 0.0318  0.0396  -0.0026 71  ASP   B CB  
845  C CG  . ASP   B 62  ? 0.5757 0.5273 0.2217 0.0307  0.0366  0.0000  71  ASP   B CG  
846  O OD1 . ASP   B 62  ? 0.5975 0.5504 0.2427 0.0374  0.0367  0.0041  71  ASP   B OD1 
847  O OD2 . ASP   B 62  ? 0.6371 0.5844 0.2787 0.0225  0.0347  -0.0016 71  ASP   B OD2 
848  N N   . VAL   B 63  ? 0.4997 0.4723 0.1738 0.0361  0.0496  0.0064  72  VAL   B N   
849  C CA  . VAL   B 63  ? 0.4949 0.4725 0.1742 0.0424  0.0518  0.0125  72  VAL   B CA  
850  C C   . VAL   B 63  ? 0.5085 0.4831 0.1784 0.0496  0.0486  0.0157  72  VAL   B C   
851  O O   . VAL   B 63  ? 0.4908 0.4699 0.1624 0.0588  0.0502  0.0204  72  VAL   B O   
852  C CB  . VAL   B 63  ? 0.4920 0.4735 0.1798 0.0366  0.0540  0.0139  72  VAL   B CB  
853  C CG1 . VAL   B 63  ? 0.4979 0.4839 0.1895 0.0422  0.0550  0.0206  72  VAL   B CG1 
854  C CG2 . VAL   B 63  ? 0.4825 0.4682 0.1812 0.0327  0.0571  0.0116  72  VAL   B CG2 
855  N N   . LYS   B 64  ? 0.5178 0.4851 0.1775 0.0471  0.0441  0.0134  73  LYS   B N   
856  C CA  . LYS   B 64  ? 0.5430 0.5074 0.1940 0.0548  0.0405  0.0163  73  LYS   B CA  
857  C C   . LYS   B 64  ? 0.5401 0.5023 0.1849 0.0645  0.0384  0.0158  73  LYS   B C   
858  O O   . LYS   B 64  ? 0.5587 0.5243 0.2012 0.0749  0.0384  0.0196  73  LYS   B O   
859  C CB  . LYS   B 64  ? 0.5528 0.5088 0.1942 0.0498  0.0354  0.0145  73  LYS   B CB  
860  C CG  . LYS   B 64  ? 0.5731 0.5268 0.2067 0.0584  0.0317  0.0173  73  LYS   B CG  
861  C CD  . LYS   B 64  ? 0.5842 0.5301 0.2095 0.0537  0.0267  0.0163  73  LYS   B CD  
862  C CE  . LYS   B 64  ? 0.6006 0.5438 0.2178 0.0632  0.0222  0.0183  73  LYS   B CE  
863  N NZ  . LYS   B 64  ? 0.6154 0.5489 0.2235 0.0581  0.0165  0.0170  73  LYS   B NZ  
864  N N   . GLN   B 65  ? 0.5451 0.5027 0.1875 0.0616  0.0365  0.0111  74  GLN   B N   
865  C CA  . GLN   B 65  ? 0.5514 0.5070 0.1892 0.0704  0.0342  0.0096  74  GLN   B CA  
866  C C   . GLN   B 65  ? 0.5364 0.5006 0.1824 0.0766  0.0395  0.0124  74  GLN   B C   
867  O O   . GLN   B 65  ? 0.5279 0.4920 0.1689 0.0871  0.0379  0.0128  74  GLN   B O   
868  C CB  . GLN   B 65  ? 0.5738 0.5231 0.2091 0.0647  0.0308  0.0038  74  GLN   B CB  
869  C CG  . GLN   B 65  ? 0.6100 0.5496 0.2363 0.0590  0.0248  0.0016  74  GLN   B CG  
870  C CD  . GLN   B 65  ? 0.6401 0.5745 0.2652 0.0532  0.0216  -0.0033 74  GLN   B CD  
871  O OE1 . GLN   B 65  ? 0.6598 0.5932 0.2844 0.0588  0.0195  -0.0057 74  GLN   B OE1 
872  N NE2 . GLN   B 65  ? 0.6634 0.5951 0.2885 0.0418  0.0212  -0.0048 74  GLN   B NE2 
873  N N   . ASP   B 66  ? 0.5129 0.4838 0.1700 0.0712  0.0448  0.0144  75  ASP   B N   
874  C CA  . ASP   B 66  ? 0.5079 0.4862 0.1745 0.0748  0.0498  0.0172  75  ASP   B CA  
875  C C   . ASP   B 66  ? 0.4986 0.4749 0.1646 0.0768  0.0488  0.0129  75  ASP   B C   
876  O O   . ASP   B 66  ? 0.4934 0.4733 0.1603 0.0858  0.0506  0.0157  75  ASP   B O   
877  C CB  . ASP   B 66  ? 0.5131 0.4974 0.1796 0.0854  0.0521  0.0241  75  ASP   B CB  
878  C CG  . ASP   B 66  ? 0.5132 0.5054 0.1907 0.0874  0.0576  0.0289  75  ASP   B CG  
879  O OD1 . ASP   B 66  ? 0.5021 0.4960 0.1896 0.0794  0.0600  0.0280  75  ASP   B OD1 
880  O OD2 . ASP   B 66  ? 0.5172 0.5141 0.1930 0.0977  0.0593  0.0341  75  ASP   B OD2 
881  N N   . LEU   B 67  ? 0.4875 0.4592 0.1525 0.0693  0.0464  0.0067  76  LEU   B N   
882  C CA  . LEU   B 67  ? 0.4834 0.4534 0.1489 0.0697  0.0449  0.0015  76  LEU   B CA  
883  C C   . LEU   B 67  ? 0.4871 0.4596 0.1612 0.0593  0.0472  -0.0027 76  LEU   B C   
884  O O   . LEU   B 67  ? 0.4769 0.4492 0.1522 0.0505  0.0479  -0.0033 76  LEU   B O   
885  C CB  . LEU   B 67  ? 0.4890 0.4510 0.1441 0.0710  0.0385  -0.0022 76  LEU   B CB  
886  C CG  . LEU   B 67  ? 0.4955 0.4544 0.1409 0.0831  0.0349  0.0002  76  LEU   B CG  
887  C CD1 . LEU   B 67  ? 0.5026 0.4522 0.1387 0.0832  0.0274  -0.0044 76  LEU   B CD1 
888  C CD2 . LEU   B 67  ? 0.4931 0.4568 0.1406 0.0934  0.0372  0.0019  76  LEU   B CD2 
889  N N   . VAL   B 68  ? 0.4833 0.4577 0.1622 0.0605  0.0478  -0.0062 77  VAL   B N   
890  C CA  . VAL   B 68  ? 0.4770 0.4547 0.1642 0.0519  0.0497  -0.0113 77  VAL   B CA  
891  C C   . VAL   B 68  ? 0.4800 0.4572 0.1678 0.0548  0.0475  -0.0163 77  VAL   B C   
892  O O   . VAL   B 68  ? 0.4748 0.4513 0.1603 0.0647  0.0464  -0.0146 77  VAL   B O   
893  C CB  . VAL   B 68  ? 0.4707 0.4541 0.1681 0.0502  0.0544  -0.0091 77  VAL   B CB  
894  C CG1 . VAL   B 68  ? 0.4709 0.4568 0.1717 0.0597  0.0562  -0.0046 77  VAL   B CG1 
895  C CG2 . VAL   B 68  ? 0.4681 0.4551 0.1735 0.0428  0.0560  -0.0151 77  VAL   B CG2 
896  N N   . SER   B 69  ? 0.4707 0.4488 0.1613 0.0470  0.0467  -0.0222 78  SER   B N   
897  C CA  . SER   B 69  ? 0.4715 0.4506 0.1650 0.0482  0.0447  -0.0277 78  SER   B CA  
898  C C   . SER   B 69  ? 0.4729 0.4591 0.1772 0.0425  0.0483  -0.0319 78  SER   B C   
899  O O   . SER   B 69  ? 0.4618 0.4511 0.1692 0.0343  0.0512  -0.0323 78  SER   B O   
900  C CB  . SER   B 69  ? 0.4787 0.4528 0.1661 0.0447  0.0396  -0.0309 78  SER   B CB  
901  O OG  . SER   B 69  ? 0.4837 0.4590 0.1721 0.0331  0.0404  -0.0329 78  SER   B OG  
902  N N   . TYR   B 70  ? 0.4718 0.4606 0.1812 0.0465  0.0478  -0.0356 79  TYR   B N   
903  C CA  . TYR   B 70  ? 0.4748 0.4705 0.1948 0.0430  0.0506  -0.0405 79  TYR   B CA  
904  C C   . TYR   B 70  ? 0.4869 0.4850 0.2094 0.0406  0.0479  -0.0473 79  TYR   B C   
905  O O   . TYR   B 70  ? 0.4860 0.4799 0.2041 0.0464  0.0438  -0.0477 79  TYR   B O   
906  C CB  . TYR   B 70  ? 0.4727 0.4695 0.1977 0.0509  0.0523  -0.0381 79  TYR   B CB  
907  C CG  . TYR   B 70  ? 0.4680 0.4645 0.1941 0.0512  0.0554  -0.0318 79  TYR   B CG  
908  C CD1 . TYR   B 70  ? 0.4717 0.4641 0.1906 0.0563  0.0551  -0.0247 79  TYR   B CD1 
909  C CD2 . TYR   B 70  ? 0.4679 0.4684 0.2023 0.0464  0.0582  -0.0330 79  TYR   B CD2 
910  C CE1 . TYR   B 70  ? 0.4692 0.4623 0.1902 0.0563  0.0578  -0.0186 79  TYR   B CE1 
911  C CE2 . TYR   B 70  ? 0.4674 0.4673 0.2038 0.0464  0.0604  -0.0272 79  TYR   B CE2 
912  C CZ  . TYR   B 70  ? 0.4682 0.4647 0.1983 0.0510  0.0603  -0.0198 79  TYR   B CZ  
913  O OH  . TYR   B 70  ? 0.4729 0.4699 0.2061 0.0505  0.0624  -0.0139 79  TYR   B OH  
914  N N   . CYS   B 71  ? 0.4908 0.4957 0.2201 0.0324  0.0501  -0.0526 80  CYS   B N   
915  C CA  . CYS   B 71  ? 0.5112 0.5214 0.2461 0.0296  0.0486  -0.0595 80  CYS   B CA  
916  C C   . CYS   B 71  ? 0.5266 0.5339 0.2560 0.0236  0.0453  -0.0597 80  CYS   B C   
917  O O   . CYS   B 71  ? 0.5520 0.5650 0.2868 0.0185  0.0447  -0.0648 80  CYS   B O   
918  C CB  . CYS   B 71  ? 0.5324 0.5420 0.2703 0.0388  0.0457  -0.0619 80  CYS   B CB  
919  S SG  . CYS   B 71  ? 0.5737 0.5846 0.3172 0.0459  0.0488  -0.0602 80  CYS   B SG  
920  N N   . GLY   B 72  ? 0.5338 0.5337 0.2537 0.0227  0.0438  -0.0544 81  GLY   B N   
921  C CA  . GLY   B 72  ? 0.5349 0.5304 0.2496 0.0177  0.0395  -0.0546 81  GLY   B CA  
922  C C   . GLY   B 72  ? 0.5329 0.5192 0.2367 0.0190  0.0376  -0.0485 81  GLY   B C   
923  O O   . GLY   B 72  ? 0.5336 0.5181 0.2347 0.0239  0.0397  -0.0444 81  GLY   B O   
924  N N   . PRO   B 73  ? 0.5397 0.5204 0.2380 0.0146  0.0332  -0.0479 82  PRO   B N   
925  C CA  . PRO   B 73  ? 0.5444 0.5150 0.2314 0.0167  0.0297  -0.0428 82  PRO   B CA  
926  C C   . PRO   B 73  ? 0.5438 0.5074 0.2248 0.0295  0.0254  -0.0412 82  PRO   B C   
927  O O   . PRO   B 73  ? 0.5443 0.5091 0.2289 0.0348  0.0231  -0.0447 82  PRO   B O   
928  C CB  . PRO   B 73  ? 0.5538 0.5206 0.2382 0.0075  0.0255  -0.0436 82  PRO   B CB  
929  C CG  . PRO   B 73  ? 0.5527 0.5250 0.2459 0.0060  0.0241  -0.0491 82  PRO   B CG  
930  C CD  . PRO   B 73  ? 0.5393 0.5224 0.2418 0.0075  0.0305  -0.0520 82  PRO   B CD  
931  N N   . TRP   B 74  ? 0.5391 0.4968 0.2115 0.0340  0.0245  -0.0362 83  TRP   B N   
932  C CA  . TRP   B 74  ? 0.5431 0.4945 0.2079 0.0465  0.0204  -0.0342 83  TRP   B CA  
933  C C   . TRP   B 74  ? 0.5585 0.5036 0.2203 0.0492  0.0126  -0.0381 83  TRP   B C   
934  O O   . TRP   B 74  ? 0.5577 0.4973 0.2166 0.0423  0.0082  -0.0389 83  TRP   B O   
935  C CB  . TRP   B 74  ? 0.5404 0.4865 0.1962 0.0487  0.0198  -0.0289 83  TRP   B CB  
936  C CG  . TRP   B 74  ? 0.5340 0.4766 0.1827 0.0622  0.0173  -0.0263 83  TRP   B CG  
937  C CD1 . TRP   B 74  ? 0.5404 0.4746 0.1800 0.0692  0.0099  -0.0272 83  TRP   B CD1 
938  C CD2 . TRP   B 74  ? 0.5237 0.4716 0.1737 0.0705  0.0222  -0.0222 83  TRP   B CD2 
939  N NE1 . TRP   B 74  ? 0.5435 0.4781 0.1779 0.0819  0.0103  -0.0242 83  TRP   B NE1 
940  C CE2 . TRP   B 74  ? 0.5315 0.4749 0.1725 0.0828  0.0180  -0.0207 83  TRP   B CE2 
941  C CE3 . TRP   B 74  ? 0.5094 0.4654 0.1676 0.0692  0.0293  -0.0197 83  TRP   B CE3 
942  C CZ2 . TRP   B 74  ? 0.5240 0.4718 0.1638 0.0933  0.0214  -0.0162 83  TRP   B CZ2 
943  C CZ3 . TRP   B 74  ? 0.5100 0.4694 0.1678 0.0788  0.0323  -0.0149 83  TRP   B CZ3 
944  C CH2 . TRP   B 74  ? 0.5166 0.4724 0.1652 0.0907  0.0287  -0.0130 83  TRP   B CH2 
945  N N   . LYS   B 75  ? 0.5653 0.5103 0.2271 0.0597  0.0104  -0.0401 84  LYS   B N   
946  C CA  . LYS   B 75  ? 0.5845 0.5237 0.2444 0.0633  0.0023  -0.0448 84  LYS   B CA  
947  C C   . LYS   B 75  ? 0.6014 0.5315 0.2494 0.0756  -0.0041 -0.0434 84  LYS   B C   
948  O O   . LYS   B 75  ? 0.6202 0.5432 0.2651 0.0777  -0.0123 -0.0472 84  LYS   B O   
949  C CB  . LYS   B 75  ? 0.5898 0.5354 0.2580 0.0672  0.0036  -0.0490 84  LYS   B CB  
950  C CG  . LYS   B 75  ? 0.5909 0.5464 0.2714 0.0571  0.0092  -0.0517 84  LYS   B CG  
951  C CD  . LYS   B 75  ? 0.6105 0.5659 0.2955 0.0458  0.0061  -0.0552 84  LYS   B CD  
952  C CE  . LYS   B 75  ? 0.6178 0.5845 0.3141 0.0360  0.0125  -0.0575 84  LYS   B CE  
953  N NZ  . LYS   B 75  ? 0.6409 0.6113 0.3454 0.0300  0.0093  -0.0629 84  LYS   B NZ  
954  N N   . LEU   B 76  ? 0.6039 0.5345 0.2458 0.0838  -0.0010 -0.0386 85  LEU   B N   
955  C CA  . LEU   B 76  ? 0.6279 0.5526 0.2586 0.0980  -0.0060 -0.0375 85  LEU   B CA  
956  C C   . LEU   B 76  ? 0.6588 0.5744 0.2802 0.0969  -0.0115 -0.0361 85  LEU   B C   
957  O O   . LEU   B 76  ? 0.6473 0.5643 0.2679 0.0916  -0.0074 -0.0319 85  LEU   B O   
958  C CB  . LEU   B 76  ? 0.6126 0.5443 0.2425 0.1068  0.0008  -0.0323 85  LEU   B CB  
959  C CG  . LEU   B 76  ? 0.5985 0.5389 0.2386 0.1059  0.0070  -0.0327 85  LEU   B CG  
960  C CD1 . LEU   B 76  ? 0.5967 0.5430 0.2358 0.1150  0.0129  -0.0268 85  LEU   B CD1 
961  C CD2 . LEU   B 76  ? 0.6120 0.5510 0.2547 0.1089  0.0021  -0.0389 85  LEU   B CD2 
962  N N   . ASP   B 77  ? 0.6994 0.6053 0.3139 0.1017  -0.0212 -0.0399 86  ASP   B N   
963  C CA  . ASP   B 77  ? 0.7510 0.6464 0.3573 0.0992  -0.0280 -0.0394 86  ASP   B CA  
964  C C   . ASP   B 77  ? 0.7403 0.6276 0.3341 0.1142  -0.0361 -0.0407 86  ASP   B C   
965  O O   . ASP   B 77  ? 0.7388 0.6167 0.3249 0.1142  -0.0426 -0.0406 86  ASP   B O   
966  C CB  . ASP   B 77  ? 0.8088 0.6986 0.4199 0.0859  -0.0331 -0.0425 86  ASP   B CB  
967  C CG  . ASP   B 77  ? 0.8668 0.7555 0.4831 0.0871  -0.0385 -0.0484 86  ASP   B CG  
968  O OD1 . ASP   B 77  ? 0.9289 0.8210 0.5446 0.0986  -0.0381 -0.0504 86  ASP   B OD1 
969  O OD2 . ASP   B 77  ? 0.9368 0.8215 0.5580 0.0765  -0.0429 -0.0507 86  ASP   B OD2 
970  N N   . ALA   B 78  ? 0.7161 0.6072 0.3072 0.1274  -0.0355 -0.0416 87  ALA   B N   
971  C CA  . ALA   B 78  ? 0.7171 0.6014 0.2954 0.1428  -0.0430 -0.0432 87  ALA   B CA  
972  C C   . ALA   B 78  ? 0.7105 0.5970 0.2814 0.1485  -0.0394 -0.0377 87  ALA   B C   
973  O O   . ALA   B 78  ? 0.6906 0.5872 0.2669 0.1448  -0.0293 -0.0321 87  ALA   B O   
974  C CB  . ALA   B 78  ? 0.7095 0.5977 0.2864 0.1555  -0.0434 -0.0456 87  ALA   B CB  
975  N N   . ALA   B 79  ? 0.7281 0.6060 0.2870 0.1585  -0.0479 -0.0395 88  ALA   B N   
976  C CA  . ALA   B 79  ? 0.7392 0.6182 0.2900 0.1650  -0.0464 -0.0352 88  ALA   B CA  
977  C C   . ALA   B 79  ? 0.7317 0.6114 0.2710 0.1846  -0.0499 -0.0364 88  ALA   B C   
978  O O   . ALA   B 79  ? 0.7426 0.6140 0.2762 0.1916  -0.0592 -0.0423 88  ALA   B O   
979  C CB  . ALA   B 79  ? 0.7546 0.6217 0.3013 0.1577  -0.0540 -0.0364 88  ALA   B CB  
980  N N   . TRP   B 80  ? 0.7223 0.6119 0.2586 0.1928  -0.0428 -0.0308 89  TRP   B N   
981  C CA  . TRP   B 80  ? 0.7477 0.6387 0.2712 0.2115  -0.0459 -0.0310 89  TRP   B CA  
982  C C   . TRP   B 80  ? 0.7788 0.6548 0.2917 0.2157  -0.0593 -0.0370 89  TRP   B C   
983  O O   . TRP   B 80  ? 0.7309 0.5991 0.2459 0.2041  -0.0625 -0.0371 89  TRP   B O   
984  C CB  . TRP   B 80  ? 0.7384 0.6421 0.2615 0.2165  -0.0367 -0.0234 89  TRP   B CB  
985  C CG  . TRP   B 80  ? 0.7405 0.6480 0.2511 0.2363  -0.0389 -0.0235 89  TRP   B CG  
986  C CD1 . TRP   B 80  ? 0.7578 0.6652 0.2607 0.2502  -0.0426 -0.0270 89  TRP   B CD1 
987  C CD2 . TRP   B 80  ? 0.7442 0.6575 0.2482 0.2452  -0.0374 -0.0200 89  TRP   B CD2 
988  N NE1 . TRP   B 80  ? 0.7534 0.6658 0.2447 0.2672  -0.0436 -0.0261 89  TRP   B NE1 
989  C CE2 . TRP   B 80  ? 0.7583 0.6746 0.2502 0.2647  -0.0406 -0.0219 89  TRP   B CE2 
990  C CE3 . TRP   B 80  ? 0.7433 0.6589 0.2498 0.2393  -0.0347 -0.0161 89  TRP   B CE3 
991  C CZ2 . TRP   B 80  ? 0.7613 0.6847 0.2446 0.2780  -0.0399 -0.0196 89  TRP   B CZ2 
992  C CZ3 . TRP   B 80  ? 0.7513 0.6735 0.2497 0.2525  -0.0344 -0.0140 89  TRP   B CZ3 
993  C CH2 . TRP   B 80  ? 0.7563 0.6828 0.2435 0.2715  -0.0368 -0.0157 89  TRP   B CH2 
994  N N   . ASP   B 81  ? 0.7937 0.6649 0.2959 0.2311  -0.0675 -0.0422 90  ASP   B N   
995  C CA  . ASP   B 81  ? 0.8462 0.7017 0.3377 0.2372  -0.0821 -0.0490 90  ASP   B CA  
996  C C   . ASP   B 81  ? 0.8621 0.7183 0.3448 0.2448  -0.0830 -0.0468 90  ASP   B C   
997  O O   . ASP   B 81  ? 0.9063 0.7485 0.3828 0.2441  -0.0941 -0.0510 90  ASP   B O   
998  C CB  . ASP   B 81  ? 0.8419 0.6918 0.3248 0.2519  -0.0913 -0.0560 90  ASP   B CB  
999  C CG  . ASP   B 81  ? 0.8816 0.7425 0.3550 0.2714  -0.0872 -0.0546 90  ASP   B CG  
1000 O OD1 . ASP   B 81  ? 0.9060 0.7792 0.3789 0.2750  -0.0777 -0.0479 90  ASP   B OD1 
1001 O OD2 . ASP   B 81  ? 0.8992 0.7572 0.3664 0.2829  -0.0931 -0.0599 90  ASP   B OD2 
1002 N N   . GLY   B 82  ? 0.8657 0.7374 0.3483 0.2515  -0.0723 -0.0403 91  GLY   B N   
1003 C CA  . GLY   B 82  ? 0.8771 0.7531 0.3523 0.2604  -0.0716 -0.0377 91  GLY   B CA  
1004 C C   . GLY   B 82  ? 0.9213 0.8022 0.3832 0.2829  -0.0747 -0.0400 91  GLY   B C   
1005 O O   . GLY   B 82  ? 0.9251 0.8113 0.3801 0.2927  -0.0742 -0.0383 91  GLY   B O   
1006 N N   . LEU   B 83  ? 0.9231 0.8026 0.3811 0.2914  -0.0779 -0.0441 92  LEU   B N   
1007 C CA  . LEU   B 83  ? 0.9768 0.8576 0.4200 0.3136  -0.0836 -0.0484 92  LEU   B CA  
1008 C C   . LEU   B 83  ? 0.9645 0.8587 0.4083 0.3218  -0.0750 -0.0451 92  LEU   B C   
1009 O O   . LEU   B 83  ? 0.9738 0.8797 0.4085 0.3387  -0.0711 -0.0426 92  LEU   B O   
1010 C CB  . LEU   B 83  ? 1.0242 0.8855 0.4599 0.3168  -0.1001 -0.0588 92  LEU   B CB  
1011 C CG  . LEU   B 83  ? 1.0681 0.9145 0.4968 0.3171  -0.1124 -0.0637 92  LEU   B CG  
1012 C CD1 . LEU   B 83  ? 1.0891 0.9167 0.5110 0.3216  -0.1289 -0.0738 92  LEU   B CD1 
1013 C CD2 . LEU   B 83  ? 1.0739 0.9279 0.4911 0.3338  -0.1120 -0.0628 92  LEU   B CD2 
1014 N N   . SER   B 84  ? 0.9473 0.8387 0.3996 0.3123  -0.0737 -0.0460 93  SER   B N   
1015 C CA  . SER   B 84  ? 0.9279 0.8268 0.3785 0.3214  -0.0696 -0.0454 93  SER   B CA  
1016 C C   . SER   B 84  ? 0.8854 0.8026 0.3449 0.3179  -0.0535 -0.0347 93  SER   B C   
1017 O O   . SER   B 84  ? 0.8570 0.7782 0.3279 0.3032  -0.0462 -0.0291 93  SER   B O   
1018 C CB  . SER   B 84  ? 0.9385 0.8270 0.3952 0.3129  -0.0756 -0.0511 93  SER   B CB  
1019 O OG  . SER   B 84  ? 0.9605 0.8318 0.4169 0.3055  -0.0882 -0.0583 93  SER   B OG  
1020 N N   . GLU   B 85  ? 0.8552 0.7825 0.3093 0.3310  -0.0486 -0.0320 94  GLU   B N   
1021 C CA  . GLU   B 85  ? 0.8227 0.7656 0.2862 0.3270  -0.0342 -0.0220 94  GLU   B CA  
1022 C C   . GLU   B 85  ? 0.7988 0.7353 0.2774 0.3078  -0.0329 -0.0232 94  GLU   B C   
1023 O O   . GLU   B 85  ? 0.8038 0.7268 0.2809 0.3060  -0.0435 -0.0322 94  GLU   B O   
1024 C CB  . GLU   B 85  ? 0.8415 0.7954 0.2946 0.3456  -0.0301 -0.0187 94  GLU   B CB  
1025 C CG  . GLU   B 85  ? 0.8470 0.8121 0.2890 0.3614  -0.0274 -0.0148 94  GLU   B CG  
1026 C CD  . GLU   B 85  ? 0.8698 0.8490 0.3019 0.3795  -0.0211 -0.0094 94  GLU   B CD  
1027 O OE1 . GLU   B 85  ? 0.8731 0.8530 0.3057 0.3811  -0.0192 -0.0086 94  GLU   B OE1 
1028 O OE2 . GLU   B 85  ? 0.8955 0.8859 0.3195 0.3920  -0.0179 -0.0057 94  GLU   B OE2 
1029 N N   . VAL   B 86  ? 0.7586 0.7071 0.2487 0.2994  -0.0204 -0.0141 95  VAL   B N   
1030 C CA  . VAL   B 86  ? 0.7279 0.6754 0.2331 0.2828  -0.0160 -0.0130 95  VAL   B CA  
1031 C C   . VAL   B 86  ? 0.7135 0.6732 0.2226 0.2866  -0.0059 -0.0054 95  VAL   B C   
1032 O O   . VAL   B 86  ? 0.7439 0.7147 0.2454 0.3001  -0.0007 0.0009  95  VAL   B O   
1033 C CB  . VAL   B 86  ? 0.6945 0.6421 0.2115 0.2655  -0.0118 -0.0100 95  VAL   B CB  
1034 C CG1 . VAL   B 86  ? 0.7075 0.6436 0.2185 0.2639  -0.0216 -0.0161 95  VAL   B CG1 
1035 C CG2 . VAL   B 86  ? 0.6858 0.6481 0.2069 0.2665  -0.0006 0.0003  95  VAL   B CG2 
1036 N N   . GLN   B 87  ? 0.6915 0.6500 0.2121 0.2754  -0.0031 -0.0055 96  GLN   B N   
1037 C CA  . GLN   B 87  ? 0.6780 0.6475 0.2046 0.2763  0.0068  0.0026  96  GLN   B CA  
1038 C C   . GLN   B 87  ? 0.6492 0.6228 0.1927 0.2587  0.0148  0.0078  96  GLN   B C   
1039 O O   . GLN   B 87  ? 0.6354 0.6015 0.1868 0.2462  0.0114  0.0022  96  GLN   B O   
1040 C CB  . GLN   B 87  ? 0.6781 0.6436 0.2016 0.2827  0.0029  -0.0018 96  GLN   B CB  
1041 C CG  . GLN   B 87  ? 0.7047 0.6675 0.2106 0.3018  -0.0044 -0.0061 96  GLN   B CG  
1042 C CD  . GLN   B 87  ? 0.7053 0.6668 0.2082 0.3093  -0.0062 -0.0084 96  GLN   B CD  
1043 O OE1 . GLN   B 87  ? 0.7134 0.6752 0.2253 0.3029  -0.0035 -0.0078 96  GLN   B OE1 
1044 N NE2 . GLN   B 87  ? 0.7263 0.6877 0.2125 0.3286  -0.0112 -0.0108 96  GLN   B NE2 
1045 N N   . LEU   B 88  ? 0.6390 0.6246 0.1876 0.2587  0.0247  0.0180  97  LEU   B N   
1046 C CA  . LEU   B 88  ? 0.6199 0.6100 0.1846 0.2444  0.0324  0.0235  97  LEU   B CA  
1047 C C   . LEU   B 88  ? 0.6262 0.6169 0.1942 0.2460  0.0343  0.0242  97  LEU   B C   
1048 O O   . LEU   B 88  ? 0.6411 0.6379 0.2019 0.2589  0.0371  0.0294  97  LEU   B O   
1049 C CB  . LEU   B 88  ? 0.6193 0.6216 0.1885 0.2443  0.0414  0.0343  97  LEU   B CB  
1050 C CG  . LEU   B 88  ? 0.6102 0.6180 0.1956 0.2319  0.0493  0.0410  97  LEU   B CG  
1051 C CD1 . LEU   B 88  ? 0.6064 0.6069 0.2020 0.2151  0.0471  0.0353  97  LEU   B CD1 
1052 C CD2 . LEU   B 88  ? 0.6110 0.6317 0.2007 0.2337  0.0577  0.0524  97  LEU   B CD2 
1053 N N   . LEU   B 89  ? 0.6124 0.5968 0.1899 0.2345  0.0323  0.0188  98  LEU   B N   
1054 C CA  . LEU   B 89  ? 0.6132 0.5991 0.1968 0.2339  0.0351  0.0204  98  LEU   B CA  
1055 C C   . LEU   B 89  ? 0.6074 0.6012 0.2040 0.2247  0.0443  0.0296  98  LEU   B C   
1056 O O   . LEU   B 89  ? 0.5874 0.5789 0.1967 0.2103  0.0453  0.0271  98  LEU   B O   
1057 C CB  . LEU   B 89  ? 0.6186 0.5952 0.2063 0.2268  0.0283  0.0099  98  LEU   B CB  
1058 C CG  . LEU   B 89  ? 0.6275 0.6043 0.2225 0.2252  0.0297  0.0093  98  LEU   B CG  
1059 C CD1 . LEU   B 89  ? 0.6580 0.6396 0.2459 0.2388  0.0326  0.0156  98  LEU   B CD1 
1060 C CD2 . LEU   B 89  ? 0.6395 0.6077 0.2349 0.2226  0.0213  -0.0020 98  LEU   B CD2 
1061 N N   . ALA   B 90  ? 0.6094 0.6127 0.2033 0.2328  0.0506  0.0398  99  ALA   B N   
1062 C CA  . ALA   B 90  ? 0.6017 0.6133 0.2077 0.2260  0.0593  0.0501  99  ALA   B CA  
1063 C C   . ALA   B 90  ? 0.6028 0.6127 0.2168 0.2225  0.0609  0.0510  99  ALA   B C   
1064 O O   . ALA   B 90  ? 0.6106 0.6195 0.2169 0.2332  0.0593  0.0510  99  ALA   B O   
1065 C CB  . ALA   B 90  ? 0.6130 0.6359 0.2141 0.2359  0.0655  0.0611  99  ALA   B CB  
1066 N N   . VAL   B 91  ? 0.5944 0.6040 0.2232 0.2086  0.0636  0.0517  100 VAL   B N   
1067 C CA  . VAL   B 91  ? 0.5835 0.5925 0.2226 0.2037  0.0660  0.0540  100 VAL   B CA  
1068 C C   . VAL   B 91  ? 0.5874 0.6039 0.2379 0.1977  0.0733  0.0650  100 VAL   B C   
1069 O O   . VAL   B 91  ? 0.5707 0.5861 0.2333 0.1852  0.0743  0.0638  100 VAL   B O   
1070 C CB  . VAL   B 91  ? 0.5729 0.5742 0.2196 0.1930  0.0614  0.0432  100 VAL   B CB  
1071 C CG1 . VAL   B 91  ? 0.5735 0.5734 0.2299 0.1893  0.0626  0.0438  100 VAL   B CG1 
1072 C CG2 . VAL   B 91  ? 0.5770 0.5714 0.2137 0.1976  0.0537  0.0324  100 VAL   B CG2 
1073 N N   . PRO   B 92  ? 0.5936 0.6182 0.2412 0.2062  0.0786  0.0764  101 PRO   B N   
1074 C CA  . PRO   B 92  ? 0.5914 0.6237 0.2507 0.2004  0.0853  0.0878  101 PRO   B CA  
1075 C C   . PRO   B 92  ? 0.5957 0.6254 0.2676 0.1934  0.0868  0.0909  101 PRO   B C   
1076 O O   . PRO   B 92  ? 0.6171 0.6405 0.2873 0.1957  0.0836  0.0862  101 PRO   B O   
1077 C CB  . PRO   B 92  ? 0.6062 0.6486 0.2566 0.2134  0.0901  0.0987  101 PRO   B CB  
1078 C CG  . PRO   B 92  ? 0.6094 0.6486 0.2419 0.2260  0.0851  0.0913  101 PRO   B CG  
1079 C CD  . PRO   B 92  ? 0.6085 0.6361 0.2407 0.2222  0.0782  0.0792  101 PRO   B CD  
1080 N N   . PRO   B 93  ? 0.6015 0.6353 0.2877 0.1839  0.0910  0.0982  102 PRO   B N   
1081 C CA  . PRO   B 93  ? 0.6075 0.6379 0.3068 0.1765  0.0915  0.1008  102 PRO   B CA  
1082 C C   . PRO   B 93  ? 0.6265 0.6583 0.3222 0.1857  0.0937  0.1095  102 PRO   B C   
1083 O O   . PRO   B 93  ? 0.6278 0.6680 0.3190 0.1932  0.0984  0.1201  102 PRO   B O   
1084 C CB  . PRO   B 93  ? 0.6022 0.6377 0.3155 0.1664  0.0953  0.1076  102 PRO   B CB  
1085 C CG  . PRO   B 93  ? 0.5964 0.6334 0.3047 0.1646  0.0940  0.1016  102 PRO   B CG  
1086 C CD  . PRO   B 93  ? 0.6074 0.6477 0.2989 0.1786  0.0940  0.1022  102 PRO   B CD  
1087 N N   . GLY   B 94  ? 0.6351 0.6590 0.3320 0.1856  0.0901  0.1043  103 GLY   B N   
1088 C CA  . GLY   B 94  ? 0.6509 0.6740 0.3442 0.1939  0.0909  0.1111  103 GLY   B CA  
1089 C C   . GLY   B 94  ? 0.6674 0.6921 0.3425 0.2089  0.0901  0.1108  103 GLY   B C   
1090 O O   . GLY   B 94  ? 0.6712 0.6960 0.3420 0.2166  0.0913  0.1176  103 GLY   B O   
1091 N N   . GLU   B 95  ? 0.6741 0.6997 0.3383 0.2135  0.0878  0.1034  104 GLU   B N   
1092 C CA  . GLU   B 95  ? 0.6971 0.7247 0.3432 0.2290  0.0867  0.1032  104 GLU   B CA  
1093 C C   . GLU   B 95  ? 0.7027 0.7217 0.3412 0.2307  0.0788  0.0879  104 GLU   B C   
1094 O O   . GLU   B 95  ? 0.6633 0.6776 0.3098 0.2197  0.0757  0.0787  104 GLU   B O   
1095 C CB  . GLU   B 95  ? 0.7100 0.7483 0.3497 0.2348  0.0915  0.1108  104 GLU   B CB  
1096 C CG  . GLU   B 95  ? 0.7292 0.7770 0.3800 0.2304  0.0994  0.1260  104 GLU   B CG  
1097 C CD  . GLU   B 95  ? 0.7555 0.8161 0.4027 0.2350  0.1049  0.1341  104 GLU   B CD  
1098 O OE1 . GLU   B 95  ? 0.7671 0.8274 0.4041 0.2398  0.1016  0.1260  104 GLU   B OE1 
1099 O OE2 . GLU   B 95  ? 0.7835 0.8547 0.4377 0.2346  0.1121  0.1488  104 GLU   B OE2 
1100 N N   . ARG   B 96  ? 0.7035 0.7203 0.3281 0.2436  0.0755  0.0851  105 ARG   B N   
1101 C CA  . ARG   B 96  ? 0.7276 0.7361 0.3448 0.2467  0.0672  0.0709  105 ARG   B CA  
1102 C C   . ARG   B 96  ? 0.7131 0.7219 0.3251 0.2457  0.0647  0.0645  105 ARG   B C   
1103 O O   . ARG   B 96  ? 0.7068 0.7234 0.3137 0.2503  0.0690  0.0717  105 ARG   B O   
1104 C CB  . ARG   B 96  ? 0.7882 0.7955 0.3899 0.2629  0.0644  0.0710  105 ARG   B CB  
1105 C CG  . ARG   B 96  ? 0.8291 0.8275 0.4250 0.2661  0.0553  0.0568  105 ARG   B CG  
1106 C CD  . ARG   B 96  ? 0.8776 0.8725 0.4655 0.2773  0.0523  0.0566  105 ARG   B CD  
1107 N NE  . ARG   B 96  ? 0.9226 0.9234 0.4966 0.2921  0.0558  0.0666  105 ARG   B NE  
1108 C CZ  . ARG   B 96  ? 0.9675 0.9729 0.5426 0.2950  0.0619  0.0793  105 ARG   B CZ  
1109 N NH1 . ARG   B 96  ? 0.9685 0.9722 0.5585 0.2842  0.0647  0.0835  105 ARG   B NH1 
1110 N NH2 . ARG   B 96  ? 1.0085 1.0199 0.5694 0.3092  0.0650  0.0879  105 ARG   B NH2 
1111 N N   . ALA   B 97  ? 0.7085 0.7096 0.3224 0.2397  0.0580  0.0516  106 ALA   B N   
1112 C CA  . ALA   B 97  ? 0.7057 0.7045 0.3126 0.2401  0.0535  0.0441  106 ALA   B CA  
1113 C C   . ALA   B 97  ? 0.7147 0.7164 0.3044 0.2568  0.0524  0.0466  106 ALA   B C   
1114 O O   . ALA   B 97  ? 0.6971 0.6974 0.2786 0.2676  0.0504  0.0467  106 ALA   B O   
1115 C CB  . ALA   B 97  ? 0.7129 0.7029 0.3219 0.2348  0.0458  0.0308  106 ALA   B CB  
1116 N N   . LYS   B 98  ? 0.7098 0.7154 0.2937 0.2593  0.0533  0.0483  107 LYS   B N   
1117 C CA  . LYS   B 98  ? 0.7550 0.7640 0.3217 0.2761  0.0519  0.0499  107 LYS   B CA  
1118 C C   . LYS   B 98  ? 0.7432 0.7487 0.3043 0.2756  0.0465  0.0426  107 LYS   B C   
1119 O O   . LYS   B 98  ? 0.7050 0.7125 0.2752 0.2644  0.0495  0.0443  107 LYS   B O   
1120 C CB  . LYS   B 98  ? 0.7917 0.8132 0.3582 0.2813  0.0613  0.0644  107 LYS   B CB  
1121 C CG  . LYS   B 98  ? 0.8520 0.8804 0.4013 0.2996  0.0621  0.0686  107 LYS   B CG  
1122 C CD  . LYS   B 98  ? 0.9005 0.9432 0.4527 0.3013  0.0722  0.0830  107 LYS   B CD  
1123 C CE  . LYS   B 98  ? 0.9161 0.9615 0.4847 0.2853  0.0763  0.0861  107 LYS   B CE  
1124 N NZ  . LYS   B 98  ? 0.9455 1.0052 0.5155 0.2883  0.0844  0.0980  107 LYS   B NZ  
1125 N N   . ASN   B 99  ? 0.7170 0.7161 0.2648 0.2862  0.0382  0.0339  108 ASN   B N   
1126 C CA  . ASN   B 99  ? 0.7288 0.7242 0.2685 0.2891  0.0321  0.0275  108 ASN   B CA  
1127 C C   . ASN   B 99  ? 0.7342 0.7397 0.2643 0.3004  0.0368  0.0353  108 ASN   B C   
1128 O O   . ASN   B 99  ? 0.7285 0.7403 0.2477 0.3154  0.0390  0.0403  108 ASN   B O   
1129 C CB  . ASN   B 99  ? 0.7476 0.7320 0.2767 0.2966  0.0207  0.0155  108 ASN   B CB  
1130 C CG  . ASN   B 99  ? 0.7667 0.7422 0.3060 0.2853  0.0159  0.0074  108 ASN   B CG  
1131 O OD1 . ASN   B 99  ? 0.7962 0.7736 0.3430 0.2820  0.0197  0.0102  108 ASN   B OD1 
1132 N ND2 . ASN   B 99  ? 0.7670 0.7333 0.3076 0.2786  0.0079  -0.0021 108 ASN   B ND2 
1133 N N   . ILE   B 100 ? 0.7077 0.7145 0.2398 0.2954  0.0370  0.0352  109 ILE   B N   
1134 C CA  . ILE   B 100 ? 0.7160 0.7323 0.2394 0.3058  0.0401  0.0408  109 ILE   B CA  
1135 C C   . ILE   B 100 ? 0.7169 0.7247 0.2327 0.3075  0.0310  0.0312  109 ILE   B C   
1136 O O   . ILE   B 100 ? 0.7061 0.7070 0.2308 0.2933  0.0284  0.0269  109 ILE   B O   
1137 C CB  . ILE   B 100 ? 0.7207 0.7489 0.2563 0.2976  0.0507  0.0524  109 ILE   B CB  
1138 C CG1 . ILE   B 100 ? 0.7381 0.7717 0.2841 0.2925  0.0584  0.0611  109 ILE   B CG1 
1139 C CG2 . ILE   B 100 ? 0.7317 0.7721 0.2591 0.3093  0.0547  0.0589  109 ILE   B CG2 
1140 C CD1 . ILE   B 100 ? 0.7570 0.8002 0.2936 0.3076  0.0631  0.0694  109 ILE   B CD1 
1141 N N   . GLN   B 101 ? 0.7336 0.7412 0.2330 0.3242  0.0258  0.0277  110 GLN   B N   
1142 C CA  . GLN   B 101 ? 0.7548 0.7520 0.2453 0.3277  0.0150  0.0174  110 GLN   B CA  
1143 C C   . GLN   B 101 ? 0.7591 0.7648 0.2460 0.3323  0.0180  0.0218  110 GLN   B C   
1144 O O   . GLN   B 101 ? 0.7674 0.7874 0.2506 0.3423  0.0259  0.0307  110 GLN   B O   
1145 C CB  . GLN   B 101 ? 0.7927 0.7829 0.2674 0.3437  0.0055  0.0093  110 GLN   B CB  
1146 C CG  . GLN   B 101 ? 0.8076 0.7876 0.2719 0.3494  -0.0058 -0.0003 110 GLN   B CG  
1147 C CD  . GLN   B 101 ? 0.8302 0.7998 0.2820 0.3618  -0.0171 -0.0102 110 GLN   B CD  
1148 O OE1 . GLN   B 101 ? 0.8379 0.8018 0.2944 0.3574  -0.0192 -0.0134 110 GLN   B OE1 
1149 N NE2 . GLN   B 101 ? 0.8536 0.8206 0.2897 0.3773  -0.0248 -0.0155 110 GLN   B NE2 
1150 N N   . THR   B 102 ? 0.7435 0.7413 0.2328 0.3241  0.0125  0.0164  111 THR   B N   
1151 C CA  . THR   B 102 ? 0.7481 0.7535 0.2365 0.3260  0.0154  0.0204  111 THR   B CA  
1152 C C   . THR   B 102 ? 0.7367 0.7282 0.2208 0.3227  0.0043  0.0107  111 THR   B C   
1153 O O   . THR   B 102 ? 0.7690 0.7459 0.2556 0.3137  -0.0034 0.0027  111 THR   B O   
1154 C CB  . THR   B 102 ? 0.7271 0.7439 0.2314 0.3132  0.0270  0.0310  111 THR   B CB  
1155 O OG1 . THR   B 102 ? 0.7515 0.7803 0.2552 0.3177  0.0315  0.0369  111 THR   B OG1 
1156 C CG2 . THR   B 102 ? 0.7225 0.7306 0.2405 0.2929  0.0259  0.0285  111 THR   B CG2 
1157 N N   . LEU   B 103 ? 0.7415 0.7375 0.2178 0.3317  0.0029  0.0111  112 LEU   B N   
1158 C CA  . LEU   B 103 ? 0.7413 0.7248 0.2134 0.3289  -0.0071 0.0033  112 LEU   B CA  
1159 C C   . LEU   B 103 ? 0.7267 0.7146 0.2118 0.3140  -0.0010 0.0089  112 LEU   B C   
1160 O O   . LEU   B 103 ? 0.7171 0.7201 0.2052 0.3175  0.0074  0.0170  112 LEU   B O   
1161 C CB  . LEU   B 103 ? 0.7590 0.7441 0.2147 0.3482  -0.0134 -0.0004 112 LEU   B CB  
1162 C CG  . LEU   B 103 ? 0.7729 0.7433 0.2245 0.3448  -0.0248 -0.0086 112 LEU   B CG  
1163 C CD1 . LEU   B 103 ? 0.7855 0.7363 0.2325 0.3425  -0.0376 -0.0191 112 LEU   B CD1 
1164 C CD2 . LEU   B 103 ? 0.7918 0.7672 0.2308 0.3614  -0.0285 -0.0102 112 LEU   B CD2 
1165 N N   . PRO   B 104 ? 0.7137 0.6897 0.2079 0.2966  -0.0044 0.0052  113 PRO   B N   
1166 C CA  . PRO   B 104 ? 0.7076 0.6869 0.2133 0.2826  0.0007  0.0100  113 PRO   B CA  
1167 C C   . PRO   B 104 ? 0.7273 0.7086 0.2261 0.2898  -0.0023 0.0097  113 PRO   B C   
1168 O O   . PRO   B 104 ? 0.7530 0.7241 0.2390 0.2993  -0.0132 0.0019  113 PRO   B O   
1169 C CB  . PRO   B 104 ? 0.6956 0.6593 0.2075 0.2660  -0.0053 0.0038  113 PRO   B CB  
1170 C CG  . PRO   B 104 ? 0.6971 0.6535 0.2058 0.2687  -0.0098 -0.0015 113 PRO   B CG  
1171 C CD  . PRO   B 104 ? 0.7113 0.6709 0.2049 0.2900  -0.0135 -0.0033 113 PRO   B CD  
1172 N N   . GLY   B 105 ? 0.7305 0.7241 0.2384 0.2848  0.0062  0.0175  114 GLY   B N   
1173 C CA  . GLY   B 105 ? 0.7370 0.7303 0.2439 0.2840  0.0035  0.0172  114 GLY   B CA  
1174 C C   . GLY   B 105 ? 0.7383 0.7177 0.2517 0.2662  -0.0010 0.0135  114 GLY   B C   
1175 O O   . GLY   B 105 ? 0.7357 0.7035 0.2513 0.2569  -0.0047 0.0090  114 GLY   B O   
1176 N N   . ILE   B 106 ? 0.7535 0.7344 0.2691 0.2626  -0.0013 0.0150  115 ILE   B N   
1177 C CA  . ILE   B 106 ? 0.7640 0.7316 0.2828 0.2478  -0.0068 0.0115  115 ILE   B CA  
1178 C C   . ILE   B 106 ? 0.7582 0.7360 0.2896 0.2377  0.0012  0.0185  115 ILE   B C   
1179 O O   . ILE   B 106 ? 0.7740 0.7644 0.3061 0.2455  0.0053  0.0231  115 ILE   B O   
1180 C CB  . ILE   B 106 ? 0.7991 0.7547 0.3047 0.2556  -0.0187 0.0047  115 ILE   B CB  
1181 C CG1 . ILE   B 106 ? 0.8480 0.7939 0.3403 0.2680  -0.0280 -0.0026 115 ILE   B CG1 
1182 C CG2 . ILE   B 106 ? 0.8141 0.7558 0.3223 0.2403  -0.0243 0.0019  115 ILE   B CG2 
1183 C CD1 . ILE   B 106 ? 0.8572 0.7858 0.3493 0.2576  -0.0355 -0.0087 115 ILE   B CD1 
1184 N N   . PHE   B 107 ? 0.7262 0.6982 0.2673 0.2207  0.0030  0.0188  116 PHE   B N   
1185 C CA  . PHE   B 107 ? 0.7176 0.6930 0.2686 0.2088  0.0068  0.0227  116 PHE   B CA  
1186 C C   . PHE   B 107 ? 0.7422 0.7023 0.2851 0.2050  -0.0033 0.0168  116 PHE   B C   
1187 O O   . PHE   B 107 ? 0.7794 0.7244 0.3189 0.1970  -0.0098 0.0113  116 PHE   B O   
1188 C CB  . PHE   B 107 ? 0.6916 0.6669 0.2552 0.1932  0.0127  0.0248  116 PHE   B CB  
1189 C CG  . PHE   B 107 ? 0.6792 0.6699 0.2548 0.1927  0.0235  0.0323  116 PHE   B CG  
1190 C CD1 . PHE   B 107 ? 0.6792 0.6835 0.2536 0.2062  0.0284  0.0375  116 PHE   B CD1 
1191 C CD2 . PHE   B 107 ? 0.6653 0.6562 0.2530 0.1787  0.0285  0.0341  116 PHE   B CD2 
1192 C CE1 . PHE   B 107 ? 0.6758 0.6933 0.2616 0.2047  0.0381  0.0451  116 PHE   B CE1 
1193 C CE2 . PHE   B 107 ? 0.6541 0.6577 0.2532 0.1778  0.0375  0.0410  116 PHE   B CE2 
1194 C CZ  . PHE   B 107 ? 0.6649 0.6813 0.2630 0.1906  0.0422  0.0467  116 PHE   B CZ  
1195 N N   . LYS   B 108 ? 0.7638 0.7280 0.3041 0.2103  -0.0048 0.0183  117 LYS   B N   
1196 C CA  . LYS   B 108 ? 0.7794 0.7297 0.3127 0.2063  -0.0142 0.0138  117 LYS   B CA  
1197 C C   . LYS   B 108 ? 0.7421 0.6937 0.2863 0.1907  -0.0099 0.0173  117 LYS   B C   
1198 O O   . LYS   B 108 ? 0.6976 0.6639 0.2509 0.1913  -0.0024 0.0232  117 LYS   B O   
1199 C CB  . LYS   B 108 ? 0.8328 0.7856 0.3561 0.2217  -0.0195 0.0123  117 LYS   B CB  
1200 C CG  . LYS   B 108 ? 0.9066 0.8578 0.4177 0.2386  -0.0247 0.0080  117 LYS   B CG  
1201 C CD  . LYS   B 108 ? 0.9689 0.9198 0.4678 0.2550  -0.0322 0.0045  117 LYS   B CD  
1202 C CE  . LYS   B 108 ? 1.0387 0.9825 0.5240 0.2696  -0.0402 -0.0018 117 LYS   B CE  
1203 N NZ  . LYS   B 108 ? 1.0777 1.0312 0.5534 0.2902  -0.0422 -0.0031 117 LYS   B NZ  
1204 N N   . THR   B 109 ? 0.7439 0.6817 0.2879 0.1772  -0.0140 0.0142  118 THR   B N   
1205 C CA  . THR   B 109 ? 0.7436 0.6805 0.2957 0.1623  -0.0112 0.0164  118 THR   B CA  
1206 C C   . THR   B 109 ? 0.7630 0.6834 0.3058 0.1571  -0.0212 0.0124  118 THR   B C   
1207 O O   . THR   B 109 ? 0.7601 0.6672 0.2914 0.1619  -0.0305 0.0074  118 THR   B O   
1208 C CB  . THR   B 109 ? 0.7260 0.6631 0.2878 0.1487  -0.0054 0.0173  118 THR   B CB  
1209 O OG1 . THR   B 109 ? 0.7264 0.6476 0.2817 0.1414  -0.0125 0.0121  118 THR   B OG1 
1210 C CG2 . THR   B 109 ? 0.7130 0.6619 0.2820 0.1534  0.0023  0.0202  118 THR   B CG2 
1211 N N   . LYS   B 110 ? 0.7942 0.7146 0.3418 0.1472  -0.0197 0.0145  119 LYS   B N   
1212 C CA  . LYS   B 110 ? 0.8134 0.7181 0.3524 0.1409  -0.0287 0.0116  119 LYS   B CA  
1213 C C   . LYS   B 110 ? 0.8370 0.7266 0.3708 0.1324  -0.0339 0.0077  119 LYS   B C   
1214 O O   . LYS   B 110 ? 0.8963 0.7704 0.4196 0.1313  -0.0438 0.0047  119 LYS   B O   
1215 C CB  . LYS   B 110 ? 0.8196 0.7281 0.3657 0.1307  -0.0250 0.0148  119 LYS   B CB  
1216 C CG  . LYS   B 110 ? 0.8166 0.7334 0.3757 0.1191  -0.0156 0.0176  119 LYS   B CG  
1217 C CD  . LYS   B 110 ? 0.8545 0.7732 0.4190 0.1096  -0.0136 0.0199  119 LYS   B CD  
1218 C CE  . LYS   B 110 ? 0.8693 0.7759 0.4308 0.0955  -0.0162 0.0178  119 LYS   B CE  
1219 N NZ  . LYS   B 110 ? 0.8693 0.7817 0.4406 0.0868  -0.0087 0.0183  119 LYS   B NZ  
1220 N N   . ASP   B 111 ? 0.8107 0.7044 0.3520 0.1262  -0.0280 0.0080  120 ASP   B N   
1221 C CA  . ASP   B 111 ? 0.8285 0.7103 0.3675 0.1167  -0.0317 0.0047  120 ASP   B CA  
1222 C C   . ASP   B 111 ? 0.8460 0.7241 0.3801 0.1258  -0.0358 0.0011  120 ASP   B C   
1223 O O   . ASP   B 111 ? 0.8698 0.7400 0.4039 0.1185  -0.0384 -0.0014 120 ASP   B O   
1224 C CB  . ASP   B 111 ? 0.8229 0.7113 0.3733 0.1036  -0.0232 0.0065  120 ASP   B CB  
1225 C CG  . ASP   B 111 ? 0.8324 0.7216 0.3859 0.0935  -0.0208 0.0091  120 ASP   B CG  
1226 O OD1 . ASP   B 111 ? 0.8462 0.7244 0.3912 0.0912  -0.0280 0.0083  120 ASP   B OD1 
1227 O OD2 . ASP   B 111 ? 0.8395 0.7399 0.4037 0.0888  -0.0125 0.0118  120 ASP   B OD2 
1228 N N   . GLY   B 112 ? 0.8352 0.7193 0.3655 0.1413  -0.0364 0.0009  121 GLY   B N   
1229 C CA  . GLY   B 112 ? 0.8502 0.7303 0.3745 0.1514  -0.0412 -0.0029 121 GLY   B CA  
1230 C C   . GLY   B 112 ? 0.8372 0.7327 0.3652 0.1635  -0.0340 -0.0008 121 GLY   B C   
1231 O O   . GLY   B 112 ? 0.8297 0.7394 0.3671 0.1620  -0.0242 0.0043  121 GLY   B O   
1232 N N   . ASP   B 113 ? 0.8437 0.7354 0.3640 0.1751  -0.0393 -0.0047 122 ASP   B N   
1233 C CA  . ASP   B 113 ? 0.8375 0.7420 0.3583 0.1886  -0.0339 -0.0032 122 ASP   B CA  
1234 C C   . ASP   B 113 ? 0.8199 0.7279 0.3491 0.1820  -0.0281 -0.0029 122 ASP   B C   
1235 O O   . ASP   B 113 ? 0.7983 0.6953 0.3281 0.1725  -0.0326 -0.0066 122 ASP   B O   
1236 C CB  . ASP   B 113 ? 0.8908 0.7882 0.3979 0.2047  -0.0437 -0.0085 122 ASP   B CB  
1237 C CG  . ASP   B 113 ? 0.9167 0.8160 0.4161 0.2157  -0.0474 -0.0083 122 ASP   B CG  
1238 O OD1 . ASP   B 113 ? 0.9302 0.8366 0.4354 0.2106  -0.0423 -0.0038 122 ASP   B OD1 
1239 O OD2 . ASP   B 113 ? 0.9798 0.8739 0.4675 0.2302  -0.0557 -0.0130 122 ASP   B OD2 
1240 N N   . ILE   B 114 ? 0.7930 0.7163 0.3291 0.1868  -0.0184 0.0017  123 ILE   B N   
1241 C CA  . ILE   B 114 ? 0.7820 0.7098 0.3260 0.1824  -0.0127 0.0023  123 ILE   B CA  
1242 C C   . ILE   B 114 ? 0.7407 0.6782 0.2808 0.1984  -0.0097 0.0040  123 ILE   B C   
1243 O O   . ILE   B 114 ? 0.7123 0.6605 0.2516 0.2069  -0.0056 0.0085  123 ILE   B O   
1244 C CB  . ILE   B 114 ? 0.7788 0.7157 0.3369 0.1696  -0.0027 0.0077  123 ILE   B CB  
1245 C CG1 . ILE   B 114 ? 0.8212 0.7516 0.3818 0.1562  -0.0046 0.0075  123 ILE   B CG1 
1246 C CG2 . ILE   B 114 ? 0.7949 0.7336 0.3607 0.1637  0.0014  0.0071  123 ILE   B CG2 
1247 C CD1 . ILE   B 114 ? 0.8148 0.7548 0.3888 0.1452  0.0046  0.0125  123 ILE   B CD1 
1248 N N   . GLY   B 115 ? 0.7275 0.6623 0.2662 0.2017  -0.0112 0.0008  124 GLY   B N   
1249 C CA  . GLY   B 115 ? 0.7040 0.6488 0.2396 0.2160  -0.0074 0.0030  124 GLY   B CA  
1250 C C   . GLY   B 115 ? 0.6837 0.6447 0.2303 0.2138  0.0048  0.0117  124 GLY   B C   
1251 O O   . GLY   B 115 ? 0.6475 0.6100 0.2058 0.1995  0.0099  0.0143  124 GLY   B O   
1252 N N   . ALA   B 116 ? 0.6717 0.6450 0.2152 0.2274  0.0097  0.0165  125 ALA   B N   
1253 C CA  . ALA   B 116 ? 0.6668 0.6557 0.2216 0.2255  0.0213  0.0257  125 ALA   B CA  
1254 C C   . ALA   B 116 ? 0.6821 0.6795 0.2324 0.2390  0.0248  0.0287  125 ALA   B C   
1255 O O   . ALA   B 116 ? 0.6813 0.6770 0.2183 0.2534  0.0194  0.0252  125 ALA   B O   
1256 C CB  . ALA   B 116 ? 0.6681 0.6665 0.2261 0.2262  0.0250  0.0312  125 ALA   B CB  
1257 N N   A VAL   B 117 ? 0.6723 0.6781 0.2328 0.2349  0.0333  0.0349  126 VAL   B N   
1258 N N   B VAL   B 117 ? 0.6732 0.6795 0.2340 0.2348  0.0335  0.0352  126 VAL   B N   
1259 N N   C VAL   B 117 ? 0.6720 0.6778 0.2325 0.2348  0.0332  0.0349  126 VAL   B N   
1260 N N   D VAL   B 117 ? 0.6731 0.6793 0.2339 0.2347  0.0334  0.0351  126 VAL   B N   
1261 C CA  A VAL   B 117 ? 0.6801 0.6946 0.2366 0.2473  0.0375  0.0391  126 VAL   B CA  
1262 C CA  B VAL   B 117 ? 0.6809 0.6954 0.2384 0.2463  0.0379  0.0393  126 VAL   B CA  
1263 C CA  C VAL   B 117 ? 0.6797 0.6942 0.2363 0.2472  0.0375  0.0391  126 VAL   B CA  
1264 C CA  D VAL   B 117 ? 0.6805 0.6950 0.2381 0.2462  0.0379  0.0393  126 VAL   B CA  
1265 C C   A VAL   B 117 ? 0.6786 0.7105 0.2437 0.2490  0.0483  0.0507  126 VAL   B C   
1266 C C   B VAL   B 117 ? 0.6794 0.7115 0.2448 0.2489  0.0484  0.0508  126 VAL   B C   
1267 C C   C VAL   B 117 ? 0.6798 0.7117 0.2450 0.2490  0.0483  0.0507  126 VAL   B C   
1268 C C   D VAL   B 117 ? 0.6806 0.7127 0.2460 0.2488  0.0485  0.0509  126 VAL   B C   
1269 O O   A VAL   B 117 ? 0.6653 0.7007 0.2450 0.2360  0.0540  0.0555  126 VAL   B O   
1270 O O   B VAL   B 117 ? 0.6665 0.7024 0.2465 0.2360  0.0543  0.0559  126 VAL   B O   
1271 O O   C VAL   B 117 ? 0.6642 0.6999 0.2438 0.2364  0.0542  0.0558  126 VAL   B O   
1272 O O   D VAL   B 117 ? 0.6657 0.7020 0.2455 0.2364  0.0545  0.0561  126 VAL   B O   
1273 C CB  A VAL   B 117 ? 0.6773 0.6849 0.2362 0.2432  0.0365  0.0357  126 VAL   B CB  
1274 C CB  B VAL   B 117 ? 0.6775 0.6856 0.2402 0.2392  0.0378  0.0366  126 VAL   B CB  
1275 C CB  C VAL   B 117 ? 0.6766 0.6844 0.2355 0.2433  0.0365  0.0358  126 VAL   B CB  
1276 C CB  D VAL   B 117 ? 0.6780 0.6861 0.2407 0.2393  0.0378  0.0366  126 VAL   B CB  
1277 C CG1 A VAL   B 117 ? 0.6843 0.6764 0.2339 0.2441  0.0254  0.0247  126 VAL   B CG1 
1278 C CG1 B VAL   B 117 ? 0.6806 0.6983 0.2440 0.2473  0.0443  0.0432  126 VAL   B CG1 
1279 C CG1 C VAL   B 117 ? 0.6838 0.6761 0.2331 0.2446  0.0253  0.0247  126 VAL   B CG1 
1280 C CG1 D VAL   B 117 ? 0.6829 0.7006 0.2464 0.2472  0.0443  0.0431  126 VAL   B CG1 
1281 C CG2 A VAL   B 117 ? 0.6645 0.6726 0.2396 0.2265  0.0418  0.0386  126 VAL   B CG2 
1282 C CG2 B VAL   B 117 ? 0.6855 0.6784 0.2388 0.2407  0.0271  0.0258  126 VAL   B CG2 
1283 C CG2 C VAL   B 117 ? 0.6659 0.6740 0.2409 0.2267  0.0419  0.0386  126 VAL   B CG2 
1284 C CG2 D VAL   B 117 ? 0.6870 0.6800 0.2402 0.2409  0.0271  0.0258  126 VAL   B CG2 
1285 N N   . ALA   B 118 ? 0.6889 0.7317 0.2454 0.2649  0.0507  0.0550  127 ALA   B N   
1286 C CA  . ALA   B 118 ? 0.6963 0.7576 0.2603 0.2681  0.0610  0.0668  127 ALA   B CA  
1287 C C   . ALA   B 118 ? 0.7254 0.7936 0.2910 0.2727  0.0672  0.0734  127 ALA   B C   
1288 O O   . ALA   B 118 ? 0.7315 0.8080 0.2863 0.2885  0.0688  0.0762  127 ALA   B O   
1289 C CB  . ALA   B 118 ? 0.7105 0.7810 0.2650 0.2820  0.0603  0.0678  127 ALA   B CB  
1290 N N   . LEU   B 119 ? 0.7213 0.7846 0.2980 0.2603  0.0695  0.0744  128 LEU   B N   
1291 C CA  . LEU   B 119 ? 0.7356 0.8035 0.3153 0.2626  0.0749  0.0806  128 LEU   B CA  
1292 C C   . LEU   B 119 ? 0.7706 0.8439 0.3693 0.2482  0.0821  0.0888  128 LEU   B C   
1293 O O   . LEU   B 119 ? 0.8150 0.8803 0.4228 0.2341  0.0797  0.0843  128 LEU   B O   
1294 C CB  . LEU   B 119 ? 0.7285 0.7823 0.3014 0.2630  0.0680  0.0713  128 LEU   B CB  
1295 C CG  . LEU   B 119 ? 0.7219 0.7688 0.2766 0.2770  0.0595  0.0625  128 LEU   B CG  
1296 C CD1 . LEU   B 119 ? 0.7077 0.7396 0.2595 0.2735  0.0519  0.0527  128 LEU   B CD1 
1297 C CD2 . LEU   B 119 ? 0.7416 0.8000 0.2846 0.2954  0.0630  0.0683  128 LEU   B CD2 
1298 N N   . ASP   B 120 ? 0.8206 0.9068 0.4249 0.2518  0.0904  0.1004  129 ASP   B N   
1299 C CA  . ASP   B 120 ? 0.8369 0.9299 0.4599 0.2394  0.0972  0.1096  129 ASP   B CA  
1300 C C   . ASP   B 120 ? 0.8056 0.8930 0.4344 0.2342  0.0984  0.1111  129 ASP   B C   
1301 O O   . ASP   B 120 ? 0.8344 0.9252 0.4559 0.2444  0.1006  0.1152  129 ASP   B O   
1302 C CB  . ASP   B 120 ? 0.8860 0.9977 0.5130 0.2458  0.1054  0.1224  129 ASP   B CB  
1303 C CG  . ASP   B 120 ? 0.9222 1.0407 0.5646 0.2349  0.1086  0.1271  129 ASP   B CG  
1304 O OD1 . ASP   B 120 ? 0.8651 0.9753 0.5194 0.2201  0.1068  0.1241  129 ASP   B OD1 
1305 O OD2 . ASP   B 120 ? 0.9917 1.1242 0.6339 0.2417  0.1125  0.1334  129 ASP   B OD2 
1306 N N   . TYR   B 121 ? 0.7676 0.8464 0.4084 0.2194  0.0968  0.1074  130 TYR   B N   
1307 C CA  . TYR   B 121 ? 0.7481 0.8212 0.3960 0.2136  0.0975  0.1083  130 TYR   B CA  
1308 C C   . TYR   B 121 ? 0.7071 0.7808 0.3738 0.1984  0.1003  0.1120  130 TYR   B C   
1309 O O   . TYR   B 121 ? 0.7064 0.7813 0.3784 0.1915  0.0997  0.1105  130 TYR   B O   
1310 C CB  . TYR   B 121 ? 0.7709 0.8298 0.4109 0.2131  0.0900  0.0957  130 TYR   B CB  
1311 C CG  . TYR   B 121 ? 0.7910 0.8487 0.4145 0.2283  0.0872  0.0930  130 TYR   B CG  
1312 C CD1 . TYR   B 121 ? 0.8246 0.8839 0.4461 0.2347  0.0897  0.0979  130 TYR   B CD1 
1313 C CD2 . TYR   B 121 ? 0.8159 0.8703 0.4252 0.2369  0.0816  0.0856  130 TYR   B CD2 
1314 C CE1 . TYR   B 121 ? 0.8483 0.9066 0.4540 0.2494  0.0869  0.0954  130 TYR   B CE1 
1315 C CE2 . TYR   B 121 ? 0.8488 0.9019 0.4426 0.2517  0.0784  0.0827  130 TYR   B CE2 
1316 C CZ  . TYR   B 121 ? 0.8599 0.9153 0.4517 0.2581  0.0812  0.0876  130 TYR   B CZ  
1317 O OH  . TYR   B 121 ? 0.9291 0.9829 0.5052 0.2730  0.0777  0.0846  130 TYR   B OH  
1318 N N   . PRO   B 122 ? 0.6782 0.7505 0.3549 0.1929  0.1027  0.1165  131 PRO   B N   
1319 C CA  . PRO   B 122 ? 0.6720 0.7437 0.3665 0.1788  0.1043  0.1193  131 PRO   B CA  
1320 C C   . PRO   B 122 ? 0.6463 0.7070 0.3420 0.1687  0.0984  0.1067  131 PRO   B C   
1321 O O   . PRO   B 122 ? 0.6208 0.6735 0.3050 0.1721  0.0932  0.0969  131 PRO   B O   
1322 C CB  . PRO   B 122 ? 0.6873 0.7568 0.3884 0.1775  0.1062  0.1244  131 PRO   B CB  
1323 C CG  . PRO   B 122 ? 0.7046 0.7791 0.3926 0.1924  0.1084  0.1295  131 PRO   B CG  
1324 C CD  . PRO   B 122 ? 0.7158 0.7869 0.3874 0.2006  0.1037  0.1196  131 PRO   B CD  
1325 N N   . ALA   B 123 ? 0.6289 0.6900 0.3380 0.1569  0.0990  0.1076  132 ALA   B N   
1326 C CA  . ALA   B 123 ? 0.6127 0.6652 0.3237 0.1467  0.0942  0.0971  132 ALA   B CA  
1327 C C   . ALA   B 123 ? 0.6014 0.6432 0.3113 0.1429  0.0903  0.0881  132 ALA   B C   
1328 O O   . ALA   B 123 ? 0.5901 0.6241 0.2938 0.1395  0.0854  0.0774  132 ALA   B O   
1329 C CB  . ALA   B 123 ? 0.6096 0.6655 0.3357 0.1359  0.0961  0.1010  132 ALA   B CB  
1330 N N   . GLY   B 124 ? 0.5856 0.6272 0.3002 0.1445  0.0921  0.0921  133 GLY   B N   
1331 C CA  . GLY   B 124 ? 0.5697 0.6024 0.2846 0.1417  0.0885  0.0840  133 GLY   B CA  
1332 C C   . GLY   B 124 ? 0.5578 0.5855 0.2578 0.1498  0.0844  0.0760  133 GLY   B C   
1333 O O   . GLY   B 124 ? 0.5606 0.5808 0.2615 0.1460  0.0808  0.0674  133 GLY   B O   
1334 N N   . THR   B 125 ? 0.5463 0.5778 0.2339 0.1598  0.0845  0.0780  134 THR   B N   
1335 C CA  . THR   B 125 ? 0.5564 0.5823 0.2290 0.1679  0.0794  0.0697  134 THR   B CA  
1336 C C   . THR   B 125 ? 0.5581 0.5774 0.2277 0.1611  0.0743  0.0598  134 THR   B C   
1337 O O   . THR   B 125 ? 0.5568 0.5697 0.2157 0.1656  0.0688  0.0517  134 THR   B O   
1338 C CB  . THR   B 125 ? 0.5813 0.6139 0.2420 0.1822  0.0811  0.0757  134 THR   B CB  
1339 O OG1 . THR   B 125 ? 0.5887 0.6282 0.2526 0.1878  0.0864  0.0860  134 THR   B OG1 
1340 C CG2 . THR   B 125 ? 0.5853 0.6124 0.2308 0.1927  0.0756  0.0684  134 THR   B CG2 
1341 N N   . SER   B 126 ? 0.5462 0.5667 0.2244 0.1509  0.0756  0.0605  135 SER   B N   
1342 C CA  . SER   B 126 ? 0.5447 0.5591 0.2207 0.1429  0.0713  0.0522  135 SER   B CA  
1343 C C   . SER   B 126 ? 0.5360 0.5417 0.2100 0.1389  0.0665  0.0419  135 SER   B C   
1344 O O   . SER   B 126 ? 0.5424 0.5474 0.2248 0.1344  0.0675  0.0405  135 SER   B O   
1345 C CB  . SER   B 126 ? 0.5447 0.5610 0.2319 0.1316  0.0735  0.0540  135 SER   B CB  
1346 O OG  . SER   B 126 ? 0.5482 0.5722 0.2375 0.1340  0.0768  0.0620  135 SER   B OG  
1347 N N   . GLY   B 127 ? 0.5350 0.5348 0.1987 0.1408  0.0611  0.0350  136 GLY   B N   
1348 C CA  . GLY   B 127 ? 0.5335 0.5257 0.1953 0.1369  0.0559  0.0252  136 GLY   B CA  
1349 C C   . GLY   B 127 ? 0.5401 0.5295 0.1928 0.1478  0.0523  0.0223  136 GLY   B C   
1350 O O   . GLY   B 127 ? 0.5377 0.5209 0.1884 0.1455  0.0472  0.0140  136 GLY   B O   
1351 N N   . SER   B 128 ? 0.5468 0.5409 0.1940 0.1597  0.0546  0.0289  137 SER   B N   
1352 C CA  . SER   B 128 ? 0.5497 0.5409 0.1858 0.1719  0.0504  0.0259  137 SER   B CA  
1353 C C   . SER   B 128 ? 0.5512 0.5351 0.1772 0.1732  0.0432  0.0187  137 SER   B C   
1354 O O   . SER   B 128 ? 0.5687 0.5528 0.1914 0.1719  0.0428  0.0202  137 SER   B O   
1355 C CB  . SER   B 128 ? 0.5532 0.5515 0.1836 0.1850  0.0543  0.0346  137 SER   B CB  
1356 O OG  . SER   B 128 ? 0.5516 0.5553 0.1925 0.1822  0.0603  0.0414  137 SER   B OG  
1357 N N   . PRO   B 129 ? 0.5483 0.5254 0.1697 0.1759  0.0369  0.0108  138 PRO   B N   
1358 C CA  . PRO   B 129 ? 0.5558 0.5249 0.1680 0.1778  0.0288  0.0038  138 PRO   B CA  
1359 C C   . PRO   B 129 ? 0.5821 0.5507 0.1799 0.1930  0.0254  0.0050  138 PRO   B C   
1360 O O   . PRO   B 129 ? 0.5818 0.5545 0.1748 0.2047  0.0272  0.0083  138 PRO   B O   
1361 C CB  . PRO   B 129 ? 0.5593 0.5227 0.1730 0.1763  0.0235  -0.0042 138 PRO   B CB  
1362 C CG  . PRO   B 129 ? 0.5592 0.5278 0.1760 0.1827  0.0277  -0.0007 138 PRO   B CG  
1363 C CD  . PRO   B 129 ? 0.5546 0.5311 0.1797 0.1778  0.0364  0.0080  138 PRO   B CD  
1364 N N   . ILE   B 130 ? 0.5936 0.5566 0.1848 0.1925  0.0201  0.0018  139 ILE   B N   
1365 C CA  . ILE   B 130 ? 0.6205 0.5806 0.1971 0.2065  0.0144  0.0004  139 ILE   B CA  
1366 C C   . ILE   B 130 ? 0.6407 0.5893 0.2123 0.2070  0.0042  -0.0093 139 ILE   B C   
1367 O O   . ILE   B 130 ? 0.6238 0.5669 0.2022 0.1943  0.0016  -0.0137 139 ILE   B O   
1368 C CB  . ILE   B 130 ? 0.6263 0.5874 0.1995 0.2057  0.0148  0.0034  139 ILE   B CB  
1369 C CG1 . ILE   B 130 ? 0.6267 0.5998 0.2070 0.2041  0.0248  0.0132  139 ILE   B CG1 
1370 C CG2 . ILE   B 130 ? 0.6419 0.5990 0.1998 0.2204  0.0077  0.0004  139 ILE   B CG2 
1371 C CD1 . ILE   B 130 ? 0.6278 0.6009 0.2108 0.1961  0.0256  0.0149  139 ILE   B CD1 
1372 N N   . LEU   B 131 ? 0.6692 0.6157 0.2305 0.2213  -0.0006 -0.0122 140 LEU   B N   
1373 C CA  . LEU   B 131 ? 0.7049 0.6410 0.2620 0.2237  -0.0110 -0.0216 140 LEU   B CA  
1374 C C   . LEU   B 131 ? 0.7244 0.6528 0.2667 0.2356  -0.0206 -0.0259 140 LEU   B C   
1375 O O   . LEU   B 131 ? 0.7379 0.6720 0.2685 0.2513  -0.0188 -0.0217 140 LEU   B O   
1376 C CB  . LEU   B 131 ? 0.7351 0.6738 0.2900 0.2337  -0.0107 -0.0224 140 LEU   B CB  
1377 C CG  . LEU   B 131 ? 0.7375 0.6833 0.3047 0.2265  -0.0026 -0.0186 140 LEU   B CG  
1378 C CD1 . LEU   B 131 ? 0.7519 0.6966 0.3167 0.2354  -0.0057 -0.0222 140 LEU   B CD1 
1379 C CD2 . LEU   B 131 ? 0.7296 0.6732 0.3103 0.2081  -0.0017 -0.0213 140 LEU   B CD2 
1380 N N   . ASP   B 132 ? 0.7329 0.6496 0.2741 0.2319  -0.0309 -0.0344 141 ASP   B N   
1381 C CA  . ASP   B 132 ? 0.7635 0.6706 0.2910 0.2440  -0.0422 -0.0403 141 ASP   B CA  
1382 C C   . ASP   B 132 ? 0.7962 0.7013 0.3183 0.2559  -0.0475 -0.0453 141 ASP   B C   
1383 O O   . ASP   B 132 ? 0.7818 0.6933 0.3113 0.2537  -0.0416 -0.0434 141 ASP   B O   
1384 C CB  . ASP   B 132 ? 0.7721 0.6663 0.3001 0.2347  -0.0519 -0.0462 141 ASP   B CB  
1385 C CG  . ASP   B 132 ? 0.7778 0.6654 0.3159 0.2223  -0.0568 -0.0520 141 ASP   B CG  
1386 O OD1 . ASP   B 132 ? 0.7710 0.6622 0.3146 0.2228  -0.0551 -0.0537 141 ASP   B OD1 
1387 O OD2 . ASP   B 132 ? 0.8152 0.6953 0.3571 0.2105  -0.0612 -0.0540 141 ASP   B OD2 
1388 N N   . LYS   B 133 ? 0.8425 0.7382 0.3525 0.2676  -0.0590 -0.0520 142 LYS   B N   
1389 C CA  . LYS   B 133 ? 0.9123 0.8060 0.4137 0.2827  -0.0650 -0.0569 142 LYS   B CA  
1390 C C   . LYS   B 133 ? 0.9027 0.7911 0.4143 0.2739  -0.0697 -0.0631 142 LYS   B C   
1391 O O   . LYS   B 133 ? 0.9046 0.7938 0.4124 0.2841  -0.0722 -0.0660 142 LYS   B O   
1392 C CB  . LYS   B 133 ? 0.9707 0.8553 0.4562 0.2979  -0.0769 -0.0631 142 LYS   B CB  
1393 C CG  . LYS   B 133 ? 1.0357 0.9285 0.5083 0.3130  -0.0723 -0.0577 142 LYS   B CG  
1394 C CD  . LYS   B 133 ? 1.0986 0.9821 0.5586 0.3223  -0.0830 -0.0628 142 LYS   B CD  
1395 C CE  . LYS   B 133 ? 1.1411 1.0353 0.5908 0.3351  -0.0765 -0.0566 142 LYS   B CE  
1396 N NZ  . LYS   B 133 ? 1.1655 1.0516 0.6000 0.3496  -0.0880 -0.0630 142 LYS   B NZ  
1397 N N   . CYS   B 134 ? 0.8974 0.7811 0.4212 0.2561  -0.0710 -0.0650 143 CYS   B N   
1398 C CA  . CYS   B 134 ? 0.8951 0.7754 0.4307 0.2458  -0.0747 -0.0705 143 CYS   B CA  
1399 C C   . CYS   B 134 ? 0.8333 0.7250 0.3823 0.2353  -0.0625 -0.0653 143 CYS   B C   
1400 O O   . CYS   B 134 ? 0.8338 0.7249 0.3941 0.2258  -0.0639 -0.0693 143 CYS   B O   
1401 C CB  . CYS   B 134 ? 0.9406 0.8106 0.4822 0.2323  -0.0827 -0.0751 143 CYS   B CB  
1402 S SG  . CYS   B 134 ? 0.9935 0.8473 0.5225 0.2436  -0.1006 -0.0839 143 CYS   B SG  
1403 N N   . GLY   B 135 ? 0.7884 0.6900 0.3362 0.2377  -0.0515 -0.0568 144 GLY   B N   
1404 C CA  . GLY   B 135 ? 0.7545 0.6663 0.3142 0.2291  -0.0402 -0.0514 144 GLY   B CA  
1405 C C   . GLY   B 135 ? 0.7269 0.6399 0.2992 0.2101  -0.0357 -0.0497 144 GLY   B C   
1406 O O   . GLY   B 135 ? 0.7130 0.6328 0.2965 0.2015  -0.0284 -0.0475 144 GLY   B O   
1407 N N   . ARG   B 136 ? 0.7220 0.6282 0.2920 0.2042  -0.0403 -0.0511 145 ARG   B N   
1408 C CA  . ARG   B 136 ? 0.7178 0.6248 0.2980 0.1865  -0.0362 -0.0492 145 ARG   B CA  
1409 C C   . ARG   B 136 ? 0.6827 0.5976 0.2631 0.1849  -0.0262 -0.0407 145 ARG   B C   
1410 O O   . ARG   B 136 ? 0.6870 0.6029 0.2566 0.1966  -0.0259 -0.0370 145 ARG   B O   
1411 C CB  . ARG   B 136 ? 0.7523 0.6479 0.3295 0.1811  -0.0461 -0.0539 145 ARG   B CB  
1412 C CG  . ARG   B 136 ? 0.7934 0.6838 0.3774 0.1757  -0.0536 -0.0614 145 ARG   B CG  
1413 C CD  . ARG   B 136 ? 0.8431 0.7215 0.4242 0.1707  -0.0641 -0.0654 145 ARG   B CD  
1414 N NE  . ARG   B 136 ? 0.9223 0.7939 0.4883 0.1859  -0.0707 -0.0661 145 ARG   B NE  
1415 C CZ  . ARG   B 136 ? 0.9631 0.8249 0.5214 0.1863  -0.0779 -0.0668 145 ARG   B CZ  
1416 N NH1 . ARG   B 136 ? 0.9816 0.8384 0.5454 0.1714  -0.0794 -0.0661 145 ARG   B NH1 
1417 N NH2 . ARG   B 136 ? 1.0087 0.8658 0.5530 0.2024  -0.0837 -0.0681 145 ARG   B NH2 
1418 N N   . VAL   B 137 ? 0.6406 0.5615 0.2331 0.1712  -0.0185 -0.0378 146 VAL   B N   
1419 C CA  . VAL   B 137 ? 0.6227 0.5513 0.2174 0.1684  -0.0091 -0.0298 146 VAL   B CA  
1420 C C   . VAL   B 137 ? 0.6243 0.5472 0.2145 0.1632  -0.0123 -0.0293 146 VAL   B C   
1421 O O   . VAL   B 137 ? 0.6295 0.5472 0.2247 0.1504  -0.0154 -0.0327 146 VAL   B O   
1422 C CB  . VAL   B 137 ? 0.6036 0.5401 0.2121 0.1572  -0.0005 -0.0274 146 VAL   B CB  
1423 C CG1 . VAL   B 137 ? 0.5930 0.5366 0.2044 0.1542  0.0078  -0.0196 146 VAL   B CG1 
1424 C CG2 . VAL   B 137 ? 0.6048 0.5458 0.2167 0.1638  0.0013  -0.0282 146 VAL   B CG2 
1425 N N   . ILE   B 138 ? 0.6201 0.5439 0.2009 0.1730  -0.0119 -0.0253 147 ILE   B N   
1426 C CA  . ILE   B 138 ? 0.6232 0.5418 0.1986 0.1700  -0.0150 -0.0243 147 ILE   B CA  
1427 C C   . ILE   B 138 ? 0.6068 0.5334 0.1886 0.1625  -0.0059 -0.0174 147 ILE   B C   
1428 O O   . ILE   B 138 ? 0.6108 0.5335 0.1889 0.1590  -0.0079 -0.0163 147 ILE   B O   
1429 C CB  . ILE   B 138 ? 0.6373 0.5515 0.1982 0.1860  -0.0216 -0.0254 147 ILE   B CB  
1430 C CG1 . ILE   B 138 ? 0.6352 0.5601 0.1922 0.1995  -0.0151 -0.0198 147 ILE   B CG1 
1431 C CG2 . ILE   B 138 ? 0.6439 0.5472 0.1988 0.1909  -0.0329 -0.0334 147 ILE   B CG2 
1432 C CD1 . ILE   B 138 ? 0.6597 0.5835 0.2029 0.2145  -0.0193 -0.0193 147 ILE   B CD1 
1433 N N   . GLY   B 139 ? 0.6000 0.5365 0.1908 0.1600  0.0029  -0.0130 148 GLY   B N   
1434 C CA  . GLY   B 139 ? 0.5825 0.5264 0.1815 0.1518  0.0112  -0.0070 148 GLY   B CA  
1435 C C   . GLY   B 139 ? 0.5757 0.5302 0.1813 0.1555  0.0195  -0.0012 148 GLY   B C   
1436 O O   . GLY   B 139 ? 0.5668 0.5229 0.1697 0.1651  0.0191  -0.0018 148 GLY   B O   
1437 N N   . LEU   B 140 ? 0.5574 0.5187 0.1704 0.1494  0.0264  0.0045  149 LEU   B N   
1438 C CA  . LEU   B 140 ? 0.5512 0.5220 0.1731 0.1500  0.0344  0.0105  149 LEU   B CA  
1439 C C   . LEU   B 140 ? 0.5571 0.5354 0.1774 0.1562  0.0389  0.0185  149 LEU   B C   
1440 O O   . LEU   B 140 ? 0.5468 0.5236 0.1639 0.1541  0.0373  0.0191  149 LEU   B O   
1441 C CB  . LEU   B 140 ? 0.5404 0.5130 0.1754 0.1359  0.0384  0.0098  149 LEU   B CB  
1442 C CG  . LEU   B 140 ? 0.5345 0.5017 0.1730 0.1282  0.0350  0.0021  149 LEU   B CG  
1443 C CD1 . LEU   B 140 ? 0.5272 0.4986 0.1788 0.1163  0.0401  0.0022  149 LEU   B CD1 
1444 C CD2 . LEU   B 140 ? 0.5417 0.5074 0.1770 0.1370  0.0320  -0.0011 149 LEU   B CD2 
1445 N N   . TYR   B 141 ? 0.5570 0.5433 0.1791 0.1642  0.0440  0.0246  150 TYR   B N   
1446 C CA  . TYR   B 141 ? 0.5745 0.5706 0.1966 0.1712  0.0494  0.0336  150 TYR   B CA  
1447 C C   . TYR   B 141 ? 0.5735 0.5760 0.2100 0.1610  0.0562  0.0395  150 TYR   B C   
1448 O O   . TYR   B 141 ? 0.5868 0.5887 0.2315 0.1554  0.0581  0.0387  150 TYR   B O   
1449 C CB  . TYR   B 141 ? 0.5894 0.5906 0.2062 0.1847  0.0514  0.0374  150 TYR   B CB  
1450 C CG  . TYR   B 141 ? 0.5989 0.6124 0.2181 0.1913  0.0586  0.0481  150 TYR   B CG  
1451 C CD1 . TYR   B 141 ? 0.5983 0.6185 0.2296 0.1866  0.0654  0.0553  150 TYR   B CD1 
1452 C CD2 . TYR   B 141 ? 0.6156 0.6342 0.2251 0.2026  0.0583  0.0510  150 TYR   B CD2 
1453 C CE1 . TYR   B 141 ? 0.6155 0.6476 0.2500 0.1920  0.0721  0.0660  150 TYR   B CE1 
1454 C CE2 . TYR   B 141 ? 0.6193 0.6511 0.2318 0.2086  0.0654  0.0614  150 TYR   B CE2 
1455 C CZ  . TYR   B 141 ? 0.6255 0.6642 0.2509 0.2029  0.0725  0.0693  150 TYR   B CZ  
1456 O OH  . TYR   B 141 ? 0.6783 0.7305 0.3075 0.2084  0.0796  0.0804  150 TYR   B OH  
1457 N N   A GLY   B 142 ? 0.5733 0.5815 0.2130 0.1591  0.0590  0.0447  151 GLY   B N   
1458 N N   B GLY   B 142 ? 0.5733 0.5815 0.2130 0.1590  0.0590  0.0447  151 GLY   B N   
1459 N N   C GLY   B 142 ? 0.5791 0.5879 0.2184 0.1603  0.0593  0.0453  151 GLY   B N   
1460 N N   D GLY   B 142 ? 0.5791 0.5880 0.2185 0.1602  0.0593  0.0453  151 GLY   B N   
1461 C CA  A GLY   B 142 ? 0.5660 0.5803 0.2202 0.1495  0.0648  0.0504  151 GLY   B CA  
1462 C CA  B GLY   B 142 ? 0.5660 0.5802 0.2202 0.1495  0.0648  0.0504  151 GLY   B CA  
1463 C CA  C GLY   B 142 ? 0.5795 0.5956 0.2330 0.1522  0.0656  0.0520  151 GLY   B CA  
1464 C CA  D GLY   B 142 ? 0.5794 0.5955 0.2329 0.1521  0.0656  0.0520  151 GLY   B CA  
1465 C C   A GLY   B 142 ? 0.5637 0.5800 0.2208 0.1439  0.0650  0.0521  151 GLY   B C   
1466 C C   B GLY   B 142 ? 0.5638 0.5800 0.2209 0.1439  0.0650  0.0521  151 GLY   B C   
1467 C C   C GLY   B 142 ? 0.5779 0.5935 0.2362 0.1427  0.0651  0.0516  151 GLY   B C   
1468 C C   D GLY   B 142 ? 0.5778 0.5934 0.2361 0.1427  0.0651  0.0516  151 GLY   B C   
1469 O O   A GLY   B 142 ? 0.5583 0.5836 0.2255 0.1418  0.0703  0.0600  151 GLY   B O   
1470 O O   B GLY   B 142 ? 0.5584 0.5836 0.2256 0.1418  0.0703  0.0599  151 GLY   B O   
1471 O O   C GLY   B 142 ? 0.5868 0.6091 0.2582 0.1364  0.0703  0.0578  151 GLY   B O   
1472 O O   D GLY   B 142 ? 0.5862 0.6086 0.2576 0.1363  0.0703  0.0578  151 GLY   B O   
1473 N N   A ASN   B 143 ? 0.5690 0.5772 0.2184 0.1411  0.0592  0.0455  152 ASN   B N   
1474 N N   B ASN   B 143 ? 0.5690 0.5772 0.2184 0.1411  0.0592  0.0455  152 ASN   B N   
1475 N N   C ASN   B 143 ? 0.5820 0.5909 0.2301 0.1435  0.0593  0.0460  152 ASN   B N   
1476 N N   D ASN   B 143 ? 0.5821 0.5910 0.2302 0.1434  0.0593  0.0460  152 ASN   B N   
1477 C CA  A ASN   B 143 ? 0.5695 0.5780 0.2208 0.1351  0.0585  0.0462  152 ASN   B CA  
1478 C CA  B ASN   B 143 ? 0.5694 0.5779 0.2208 0.1351  0.0585  0.0462  152 ASN   B CA  
1479 C CA  C ASN   B 143 ? 0.5832 0.5922 0.2342 0.1363  0.0587  0.0465  152 ASN   B CA  
1480 C CA  D ASN   B 143 ? 0.5831 0.5921 0.2341 0.1362  0.0587  0.0465  152 ASN   B CA  
1481 C C   A ASN   B 143 ? 0.5781 0.5891 0.2187 0.1466  0.0561  0.0478  152 ASN   B C   
1482 C C   B ASN   B 143 ? 0.5783 0.5893 0.2189 0.1466  0.0561  0.0479  152 ASN   B C   
1483 C C   C ASN   B 143 ? 0.5844 0.5945 0.2233 0.1476  0.0554  0.0472  152 ASN   B C   
1484 C C   D ASN   B 143 ? 0.5846 0.5947 0.2235 0.1476  0.0554  0.0472  152 ASN   B C   
1485 O O   A ASN   B 143 ? 0.5881 0.5913 0.2144 0.1548  0.0497  0.0420  152 ASN   B O   
1486 O O   B ASN   B 143 ? 0.5880 0.5912 0.2143 0.1548  0.0497  0.0420  152 ASN   B O   
1487 O O   C ASN   B 143 ? 0.6031 0.6055 0.2285 0.1549  0.0490  0.0415  152 ASN   B O   
1488 O O   D ASN   B 143 ? 0.6029 0.6053 0.2283 0.1549  0.0490  0.0415  152 ASN   B O   
1489 C CB  A ASN   B 143 ? 0.5677 0.5660 0.2182 0.1235  0.0539  0.0387  152 ASN   B CB  
1490 C CB  B ASN   B 143 ? 0.5677 0.5659 0.2181 0.1235  0.0539  0.0387  152 ASN   B CB  
1491 C CB  C ASN   B 143 ? 0.5813 0.5807 0.2333 0.1237  0.0548  0.0393  152 ASN   B CB  
1492 C CB  D ASN   B 143 ? 0.5813 0.5807 0.2334 0.1236  0.0548  0.0393  152 ASN   B CB  
1493 C CG  A ASN   B 143 ? 0.5650 0.5646 0.2210 0.1152  0.0546  0.0403  152 ASN   B CG  
1494 C CG  B ASN   B 143 ? 0.5648 0.5644 0.2208 0.1152  0.0546  0.0403  152 ASN   B CG  
1495 C CG  C ASN   B 143 ? 0.5821 0.5829 0.2388 0.1162  0.0553  0.0411  152 ASN   B CG  
1496 C CG  D ASN   B 143 ? 0.5819 0.5827 0.2387 0.1162  0.0553  0.0411  152 ASN   B CG  
1497 O OD1 A ASN   B 143 ? 0.5624 0.5709 0.2274 0.1152  0.0593  0.0469  152 ASN   B OD1 
1498 O OD1 B ASN   B 143 ? 0.5622 0.5707 0.2272 0.1151  0.0593  0.0468  152 ASN   B OD1 
1499 O OD1 C ASN   B 143 ? 0.5800 0.5729 0.2318 0.1101  0.0507  0.0361  152 ASN   B OD1 
1500 O OD1 D ASN   B 143 ? 0.5800 0.5730 0.2318 0.1101  0.0507  0.0361  152 ASN   B OD1 
1501 N ND2 A ASN   B 143 ? 0.5659 0.5567 0.2167 0.1083  0.0497  0.0346  152 ASN   B ND2 
1502 N ND2 B ASN   B 143 ? 0.5659 0.5567 0.2166 0.1083  0.0497  0.0346  152 ASN   B ND2 
1503 N ND2 C ASN   B 143 ? 0.5753 0.5861 0.2418 0.1167  0.0605  0.0484  152 ASN   B ND2 
1504 N ND2 D ASN   B 143 ? 0.5754 0.5861 0.2418 0.1167  0.0605  0.0484  152 ASN   B ND2 
1505 N N   . GLY   B 144 ? 0.5784 0.6011 0.2254 0.1496  0.0612  0.0560  153 GLY   B N   
1506 C CA  . GLY   B 144 ? 0.5980 0.6250 0.2362 0.1604  0.0595  0.0577  153 GLY   B CA  
1507 C C   . GLY   B 144 ? 0.6155 0.6555 0.2635 0.1605  0.0650  0.0660  153 GLY   B C   
1508 O O   . GLY   B 144 ? 0.6030 0.6432 0.2620 0.1490  0.0664  0.0672  153 GLY   B O   
1509 N N   . VAL   B 145 ? 0.6335 0.6842 0.2775 0.1732  0.0676  0.0714  154 VAL   B N   
1510 C CA  . VAL   B 145 ? 0.6528 0.7165 0.3044 0.1748  0.0715  0.0785  154 VAL   B CA  
1511 C C   . VAL   B 145 ? 0.7033 0.7827 0.3574 0.1857  0.0786  0.0879  154 VAL   B C   
1512 O O   . VAL   B 145 ? 0.6712 0.7499 0.3150 0.1959  0.0782  0.0869  154 VAL   B O   
1513 C CB  . VAL   B 145 ? 0.6750 0.7343 0.3162 0.1791  0.0651  0.0733  154 VAL   B CB  
1514 C CG1 . VAL   B 145 ? 0.6721 0.7338 0.2986 0.1956  0.0626  0.0718  154 VAL   B CG1 
1515 C CG2 . VAL   B 145 ? 0.6952 0.7624 0.3465 0.1742  0.0670  0.0774  154 VAL   B CG2 
1516 N N   . VAL   B 146 ? 0.7434 0.8364 0.4111 0.1832  0.0845  0.0967  155 VAL   B N   
1517 C CA  . VAL   B 146 ? 0.7865 0.8974 0.4584 0.1928  0.0920  0.1075  155 VAL   B CA  
1518 C C   . VAL   B 146 ? 0.8168 0.9364 0.4810 0.2041  0.0908  0.1076  155 VAL   B C   
1519 O O   . VAL   B 146 ? 0.7945 0.9120 0.4614 0.1991  0.0874  0.1046  155 VAL   B O   
1520 C CB  . VAL   B 146 ? 0.7943 0.9146 0.4866 0.1828  0.0985  0.1170  155 VAL   B CB  
1521 C CG1 . VAL   B 146 ? 0.8105 0.9499 0.5086 0.1913  0.1065  0.1292  155 VAL   B CG1 
1522 C CG2 . VAL   B 146 ? 0.8079 0.9181 0.5064 0.1726  0.0985  0.1154  155 VAL   B CG2 
1523 N N   . ILE   B 147 ? 0.8927 1.0211 0.5465 0.2194  0.0929  0.1102  156 ILE   B N   
1524 C CA  . ILE   B 147 ? 0.9585 1.0926 0.6012 0.2321  0.0898  0.1075  156 ILE   B CA  
1525 C C   . ILE   B 147 ? 1.0171 1.1743 0.6693 0.2385  0.0981  0.1188  156 ILE   B C   
1526 O O   . ILE   B 147 ? 1.0105 1.1778 0.6766 0.2333  0.1057  0.1288  156 ILE   B O   
1527 C CB  . ILE   B 147 ? 0.9814 1.1075 0.6037 0.2458  0.0843  0.1000  156 ILE   B CB  
1528 C CG1 . ILE   B 147 ? 0.9874 1.1194 0.6058 0.2541  0.0895  0.1052  156 ILE   B CG1 
1529 C CG2 . ILE   B 147 ? 0.9815 1.0853 0.5960 0.2383  0.0749  0.0884  156 ILE   B CG2 
1530 C CD1 . ILE   B 147 ? 0.9836 1.1134 0.5822 0.2713  0.0850  0.0995  156 ILE   B CD1 
1531 N N   A LYS   B 148 ? 1.0339 1.1993 0.6793 0.2493  0.0962  0.1173  157 LYS   B N   
1532 N N   B LYS   B 148 ? 1.0338 1.1993 0.6792 0.2494  0.0962  0.1173  157 LYS   B N   
1533 N N   C LYS   B 148 ? 1.0527 1.2180 0.6984 0.2490  0.0962  0.1173  157 LYS   B N   
1534 N N   D LYS   B 148 ? 1.0526 1.2179 0.6982 0.2490  0.0962  0.1173  157 LYS   B N   
1535 C CA  A LYS   B 148 ? 1.0522 1.2415 0.7053 0.2574  0.1036  0.1273  157 LYS   B CA  
1536 C CA  B LYS   B 148 ? 1.0520 1.2414 0.7051 0.2574  0.1036  0.1273  157 LYS   B CA  
1537 C CA  C LYS   B 148 ? 1.0841 1.2734 0.7373 0.2572  0.1037  0.1273  157 LYS   B CA  
1538 C CA  D LYS   B 148 ? 1.0838 1.2731 0.7370 0.2572  0.1037  0.1273  157 LYS   B CA  
1539 C C   A LYS   B 148 ? 1.0643 1.2678 0.7228 0.2613  0.1133  0.1387  157 LYS   B C   
1540 C C   B LYS   B 148 ? 1.0640 1.2675 0.7225 0.2613  0.1133  0.1387  157 LYS   B C   
1541 C C   C LYS   B 148 ? 1.0929 1.2959 0.7519 0.2605  0.1132  0.1387  157 LYS   B C   
1542 C C   D LYS   B 148 ? 1.0924 1.2953 0.7513 0.2605  0.1132  0.1387  157 LYS   B C   
1543 O O   A LYS   B 148 ? 1.0713 1.2919 0.7464 0.2573  0.1211  0.1500  157 LYS   B O   
1544 O O   B LYS   B 148 ? 1.0704 1.2910 0.7455 0.2573  0.1211  0.1500  157 LYS   B O   
1545 O O   C LYS   B 148 ? 1.1246 1.3431 0.8010 0.2551  0.1208  0.1498  157 LYS   B O   
1546 O O   D LYS   B 148 ? 1.1231 1.3416 0.7994 0.2551  0.1208  0.1498  157 LYS   B O   
1547 C CB  A LYS   B 148 ? 1.0676 1.2621 0.7050 0.2743  0.0996  0.1221  157 LYS   B CB  
1548 C CB  B LYS   B 148 ? 1.0674 1.2619 0.7049 0.2743  0.0996  0.1221  157 LYS   B CB  
1549 C CB  C LYS   B 148 ? 1.1164 1.3110 0.7537 0.2746  0.0998  0.1223  157 LYS   B CB  
1550 C CB  D LYS   B 148 ? 1.1161 1.3107 0.7534 0.2746  0.0998  0.1223  157 LYS   B CB  
1551 C CG  A LYS   B 148 ? 1.0716 1.2556 0.7050 0.2718  0.0907  0.1128  157 LYS   B CG  
1552 C CG  B LYS   B 148 ? 1.0713 1.2553 0.7048 0.2718  0.0907  0.1128  157 LYS   B CG  
1553 C CG  C LYS   B 148 ? 1.1382 1.3225 0.7708 0.2727  0.0908  0.1128  157 LYS   B CG  
1554 C CG  D LYS   B 148 ? 1.1377 1.3219 0.7703 0.2727  0.0908  0.1128  157 LYS   B CG  
1555 C CD  A LYS   B 148 ? 1.0871 1.2704 0.7018 0.2891  0.0843  0.1052  157 LYS   B CD  
1556 C CD  B LYS   B 148 ? 1.0869 1.2702 0.7016 0.2891  0.0843  0.1052  157 LYS   B CD  
1557 C CD  C LYS   B 148 ? 1.1667 1.3536 0.7820 0.2908  0.0856  0.1066  157 LYS   B CD  
1558 C CD  D LYS   B 148 ? 1.1661 1.3530 0.7814 0.2908  0.0856  0.1067  157 LYS   B CD  
1559 C CE  A LYS   B 148 ? 1.0960 1.3043 0.7124 0.3032  0.0905  0.1121  157 LYS   B CE  
1560 C CE  B LYS   B 148 ? 1.0957 1.3040 0.7120 0.3033  0.0905  0.1122  157 LYS   B CE  
1561 C CE  C LYS   B 148 ? 1.1902 1.4038 0.8091 0.3039  0.0936  0.1154  157 LYS   B CE  
1562 C CE  D LYS   B 148 ? 1.1892 1.4028 0.8081 0.3039  0.0936  0.1154  157 LYS   B CE  
1563 N NZ  A LYS   B 148 ? 1.0897 1.3080 0.7198 0.2977  0.0914  0.1149  157 LYS   B NZ  
1564 N NZ  B LYS   B 148 ? 1.0896 1.3079 0.7197 0.2977  0.0914  0.1149  157 LYS   B NZ  
1565 N NZ  C LYS   B 148 ? 1.2115 1.4277 0.8148 0.3209  0.0875  0.1083  157 LYS   B NZ  
1566 N NZ  D LYS   B 148 ? 1.2105 1.4266 0.8137 0.3209  0.0875  0.1083  157 LYS   B NZ  
1567 N N   . ASN   B 149 ? 1.0878 1.2841 0.7329 0.2685  0.1123  0.1361  158 ASN   B N   
1568 C CA  . ASN   B 149 ? 1.0559 1.2640 0.7021 0.2746  0.1206  0.1463  158 ASN   B CA  
1569 C C   . ASN   B 149 ? 1.0043 1.2105 0.6672 0.2598  0.1256  0.1540  158 ASN   B C   
1570 O O   . ASN   B 149 ? 1.0070 1.2259 0.6748 0.2632  0.1336  0.1652  158 ASN   B O   
1571 C CB  . ASN   B 149 ? 1.1085 1.3063 0.7346 0.2862  0.1165  0.1396  158 ASN   B CB  
1572 C CG  . ASN   B 149 ? 1.1251 1.3132 0.7327 0.2969  0.1071  0.1270  158 ASN   B CG  
1573 O OD1 . ASN   B 149 ? 1.1436 1.3332 0.7524 0.2968  0.1037  0.1234  158 ASN   B OD1 
1574 N ND2 . ASN   B 149 ? 1.1602 1.3380 0.7510 0.3064  0.1022  0.1202  158 ASN   B ND2 
1575 N N   A GLY   B 150 ? 0.9725 1.1632 0.6436 0.2443  0.1209  0.1483  159 GLY   B N   
1576 N N   B GLY   B 150 ? 0.9724 1.1631 0.6435 0.2443  0.1209  0.1483  159 GLY   B N   
1577 N N   C GLY   B 150 ? 0.9794 1.1694 0.6498 0.2445  0.1207  0.1479  159 GLY   B N   
1578 N N   D GLY   B 150 ? 0.9785 1.1685 0.6489 0.2445  0.1207  0.1480  159 GLY   B N   
1579 C CA  A GLY   B 150 ? 0.9405 1.1256 0.6259 0.2302  0.1236  0.1529  159 GLY   B CA  
1580 C CA  B GLY   B 150 ? 0.9407 1.1258 0.6261 0.2303  0.1236  0.1529  159 GLY   B CA  
1581 C CA  C GLY   B 150 ? 0.9419 1.1269 0.6274 0.2301  0.1236  0.1529  159 GLY   B CA  
1582 C CA  D GLY   B 150 ? 0.9406 1.1257 0.6262 0.2301  0.1236  0.1529  159 GLY   B CA  
1583 C C   A GLY   B 150 ? 0.9214 1.0895 0.5962 0.2299  0.1194  0.1458  159 GLY   B C   
1584 C C   B GLY   B 150 ? 0.9215 1.0896 0.5963 0.2299  0.1194  0.1458  159 GLY   B C   
1585 C C   C GLY   B 150 ? 0.9247 1.0919 0.6013 0.2280  0.1193  0.1457  159 GLY   B C   
1586 C C   D GLY   B 150 ? 0.9225 1.0896 0.5990 0.2280  0.1192  0.1456  159 GLY   B C   
1587 O O   A GLY   B 150 ? 0.9086 1.0680 0.5935 0.2177  0.1195  0.1463  159 GLY   B O   
1588 O O   B GLY   B 150 ? 0.9090 1.0684 0.5939 0.2176  0.1194  0.1462  159 GLY   B O   
1589 O O   C GLY   B 150 ? 0.8906 1.0502 0.5787 0.2152  0.1197  0.1469  159 GLY   B O   
1590 O O   D GLY   B 150 ? 0.8904 1.0499 0.5783 0.2153  0.1197  0.1469  159 GLY   B O   
1591 N N   A SER   B 151 ? 0.9043 1.0678 0.5597 0.2432  0.1155  0.1391  160 SER   B N   
1592 N N   B SER   B 151 ? 0.9049 1.0685 0.5604 0.2432  0.1156  0.1393  160 SER   B N   
1593 N N   C SER   B 151 ? 0.9111 1.0717 0.5683 0.2401  0.1149  0.1383  160 SER   B N   
1594 N N   D SER   B 151 ? 0.9053 1.0656 0.5623 0.2400  0.1145  0.1377  160 SER   B N   
1595 C CA  A SER   B 151 ? 0.8850 1.0316 0.5281 0.2447  0.1099  0.1303  160 SER   B CA  
1596 C CA  B SER   B 151 ? 0.8859 1.0326 0.5296 0.2442  0.1101  0.1306  160 SER   B CA  
1597 C CA  C SER   B 151 ? 0.8879 1.0315 0.5354 0.2393  0.1098  0.1302  160 SER   B CA  
1598 C CA  D SER   B 151 ? 0.8818 1.0253 0.5277 0.2405  0.1093  0.1294  160 SER   B CA  
1599 C C   A SER   B 151 ? 0.8588 0.9870 0.5024 0.2326  0.1018  0.1187  160 SER   B C   
1600 C C   B SER   B 151 ? 0.8593 0.9875 0.5030 0.2326  0.1019  0.1189  160 SER   B C   
1601 C C   C SER   B 151 ? 0.8660 0.9916 0.5150 0.2267  0.1021  0.1190  160 SER   B C   
1602 C C   D SER   B 151 ? 0.8653 0.9901 0.5112 0.2287  0.1011  0.1177  160 SER   B C   
1603 O O   A SER   B 151 ? 0.8500 0.9783 0.4982 0.2273  0.0995  0.1164  160 SER   B O   
1604 O O   B SER   B 151 ? 0.8514 0.9799 0.4996 0.2274  0.0997  0.1167  160 SER   B O   
1605 O O   C SER   B 151 ? 0.8353 0.9615 0.4908 0.2200  0.1005  0.1176  160 SER   B O   
1606 O O   D SER   B 151 ? 0.8467 0.9709 0.4946 0.2249  0.0981  0.1143  160 SER   B O   
1607 C CB  A SER   B 151 ? 0.8994 1.0472 0.5224 0.2626  0.1071  0.1260  160 SER   B CB  
1608 C CB  B SER   B 151 ? 0.9007 1.0484 0.5244 0.2621  0.1076  0.1266  160 SER   B CB  
1609 C CB  C SER   B 151 ? 0.9013 1.0440 0.5285 0.2564  0.1067  0.1254  160 SER   B CB  
1610 C CB  D SER   B 151 ? 0.8888 1.0332 0.5148 0.2582  0.1066  0.1253  160 SER   B CB  
1611 O OG  A SER   B 151 ? 0.9021 1.0351 0.5147 0.2643  0.1020  0.1186  160 SER   B OG  
1612 O OG  B SER   B 151 ? 0.9057 1.0548 0.5209 0.2693  0.1030  0.1208  160 SER   B OG  
1613 O OG  C SER   B 151 ? 0.9080 1.0370 0.5277 0.2563  0.1029  0.1195  160 SER   B OG  
1614 O OG  D SER   B 151 ? 0.8802 1.0276 0.4988 0.2652  0.1028  0.1207  160 SER   B OG  
1615 N N   A TYR   B 152 ? 0.8314 0.9448 0.4703 0.2288  0.0976  0.1120  161 TYR   B N   
1616 N N   B TYR   B 152 ? 0.8316 0.9450 0.4706 0.2288  0.0976  0.1120  161 TYR   B N   
1617 N N   C TYR   B 152 ? 0.8504 0.9611 0.4936 0.2236  0.0976  0.1117  161 TYR   B N   
1618 N N   D TYR   B 152 ? 0.8498 0.9606 0.4930 0.2236  0.0976  0.1117  161 TYR   B N   
1619 C CA  A TYR   B 152 ? 0.8061 0.9025 0.4466 0.2162  0.0908  0.1019  161 TYR   B CA  
1620 C CA  B TYR   B 152 ? 0.8060 0.9024 0.4465 0.2162  0.0908  0.1019  161 TYR   B CA  
1621 C CA  C TYR   B 152 ? 0.8335 0.9268 0.4760 0.2125  0.0902  0.1007  161 TYR   B CA  
1622 C CA  D TYR   B 152 ? 0.8329 0.9263 0.4754 0.2125  0.0902  0.1007  161 TYR   B CA  
1623 C C   A TYR   B 152 ? 0.7936 0.8771 0.4164 0.2234  0.0821  0.0905  161 TYR   B C   
1624 C C   B TYR   B 152 ? 0.7935 0.8770 0.4163 0.2234  0.0821  0.0905  161 TYR   B C   
1625 C C   C TYR   B 152 ? 0.8108 0.8931 0.4350 0.2215  0.0821  0.0902  161 TYR   B C   
1626 C C   D TYR   B 152 ? 0.8105 0.8927 0.4346 0.2215  0.0821  0.0902  161 TYR   B C   
1627 O O   A TYR   B 152 ? 0.7995 0.8832 0.4109 0.2354  0.0813  0.0895  161 TYR   B O   
1628 O O   B TYR   B 152 ? 0.7997 0.8834 0.4111 0.2354  0.0813  0.0895  161 TYR   B O   
1629 O O   C TYR   B 152 ? 0.8090 0.8911 0.4226 0.2326  0.0815  0.0894  161 TYR   B O   
1630 O O   D TYR   B 152 ? 0.8092 0.8913 0.4227 0.2326  0.0815  0.0895  161 TYR   B O   
1631 C CB  A TYR   B 152 ? 0.7998 0.8901 0.4504 0.2055  0.0927  0.1029  161 TYR   B CB  
1632 C CB  B TYR   B 152 ? 0.7997 0.8900 0.4503 0.2055  0.0927  0.1029  161 TYR   B CB  
1633 C CB  C TYR   B 152 ? 0.8463 0.9318 0.4982 0.2011  0.0910  0.1002  161 TYR   B CB  
1634 C CB  D TYR   B 152 ? 0.8458 0.9313 0.4977 0.2011  0.0911  0.1002  161 TYR   B CB  
1635 C CG  A TYR   B 152 ? 0.7933 0.8677 0.4448 0.1936  0.0864  0.0927  161 TYR   B CG  
1636 C CG  B TYR   B 152 ? 0.7932 0.8676 0.4447 0.1936  0.0864  0.0927  161 TYR   B CG  
1637 C CG  C TYR   B 152 ? 0.8567 0.9299 0.5144 0.1866  0.0863  0.0924  161 TYR   B CG  
1638 C CG  D TYR   B 152 ? 0.8561 0.9293 0.5138 0.1866  0.0863  0.0924  161 TYR   B CG  
1639 C CD1 A TYR   B 152 ? 0.7851 0.8566 0.4442 0.1826  0.0846  0.0904  161 TYR   B CD1 
1640 C CD1 B TYR   B 152 ? 0.7851 0.8566 0.4442 0.1826  0.0846  0.0904  161 TYR   B CD1 
1641 C CD1 C TYR   B 152 ? 0.8513 0.9278 0.5222 0.1759  0.0881  0.0954  161 TYR   B CD1 
1642 C CD1 D TYR   B 152 ? 0.8510 0.9275 0.5219 0.1759  0.0882  0.0954  161 TYR   B CD1 
1643 C CD2 A TYR   B 152 ? 0.7935 0.8563 0.4380 0.1937  0.0821  0.0854  161 TYR   B CD2 
1644 C CD2 B TYR   B 152 ? 0.7936 0.8564 0.4381 0.1937  0.0821  0.0854  161 TYR   B CD2 
1645 C CD2 C TYR   B 152 ? 0.8628 0.9214 0.5129 0.1836  0.0800  0.0822  161 TYR   B CD2 
1646 C CD2 D TYR   B 152 ? 0.8624 0.9211 0.5125 0.1836  0.0800  0.0822  161 TYR   B CD2 
1647 C CE1 A TYR   B 152 ? 0.7811 0.8390 0.4404 0.1719  0.0793  0.0815  161 TYR   B CE1 
1648 C CE1 B TYR   B 152 ? 0.7809 0.8389 0.4402 0.1719  0.0793  0.0815  161 TYR   B CE1 
1649 C CE1 C TYR   B 152 ? 0.8582 0.9240 0.5333 0.1632  0.0840  0.0883  161 TYR   B CE1 
1650 C CE1 D TYR   B 152 ? 0.8575 0.9233 0.5326 0.1632  0.0840  0.0884  161 TYR   B CE1 
1651 C CE2 A TYR   B 152 ? 0.7865 0.8363 0.4323 0.1828  0.0768  0.0764  161 TYR   B CE2 
1652 C CE2 B TYR   B 152 ? 0.7867 0.8364 0.4325 0.1827  0.0768  0.0764  161 TYR   B CE2 
1653 C CE2 C TYR   B 152 ? 0.8610 0.9097 0.5161 0.1704  0.0763  0.0756  161 TYR   B CE2 
1654 C CE2 D TYR   B 152 ? 0.8605 0.9092 0.5156 0.1704  0.0763  0.0756  161 TYR   B CE2 
1655 C CZ  A TYR   B 152 ? 0.7815 0.8290 0.4343 0.1719  0.0756  0.0747  161 TYR   B CZ  
1656 C CZ  B TYR   B 152 ? 0.7814 0.8289 0.4343 0.1718  0.0757  0.0747  161 TYR   B CZ  
1657 C CZ  C TYR   B 152 ? 0.8556 0.9077 0.5226 0.1604  0.0784  0.0786  161 TYR   B CZ  
1658 C CZ  D TYR   B 152 ? 0.8551 0.9072 0.5221 0.1604  0.0784  0.0786  161 TYR   B CZ  
1659 O OH  A TYR   B 152 ? 0.7725 0.8082 0.4260 0.1613  0.0709  0.0664  161 TYR   B OH  
1660 O OH  B TYR   B 152 ? 0.7728 0.8086 0.4264 0.1613  0.0709  0.0664  161 TYR   B OH  
1661 O OH  C TYR   B 152 ? 0.8295 0.8724 0.5005 0.1480  0.0749  0.0722  161 TYR   B OH  
1662 O OH  D TYR   B 152 ? 0.8300 0.8728 0.5009 0.1480  0.0749  0.0722  161 TYR   B OH  
1663 N N   . VAL   B 153 ? 0.7742 0.8469 0.3949 0.2166  0.0755  0.0823  162 VAL   B N   
1664 C CA  . VAL   B 153 ? 0.7306 0.7892 0.3359 0.2213  0.0663  0.0713  162 VAL   B CA  
1665 C C   . VAL   B 153 ? 0.6866 0.7307 0.2970 0.2058  0.0618  0.0643  162 VAL   B C   
1666 O O   . VAL   B 153 ? 0.6636 0.7072 0.2822 0.1954  0.0621  0.0647  162 VAL   B O   
1667 C CB  . VAL   B 153 ? 0.7156 0.7759 0.3115 0.2299  0.0620  0.0688  162 VAL   B CB  
1668 C CG1 . VAL   B 153 ? 0.7124 0.7577 0.2927 0.2354  0.0517  0.0579  162 VAL   B CG1 
1669 C CG2 . VAL   B 153 ? 0.7501 0.8282 0.3439 0.2440  0.0679  0.0768  162 VAL   B CG2 
1670 N N   . SER   B 154 ? 0.6627 0.6966 0.2683 0.2050  0.0581  0.0583  163 SER   B N   
1671 C CA  . SER   B 154 ? 0.6332 0.6546 0.2434 0.1911  0.0543  0.0516  163 SER   B CA  
1672 C C   . SER   B 154 ? 0.6329 0.6410 0.2310 0.1921  0.0446  0.0421  163 SER   B C   
1673 O O   . SER   B 154 ? 0.6325 0.6375 0.2180 0.2042  0.0398  0.0386  163 SER   B O   
1674 C CB  . SER   B 154 ? 0.6253 0.6442 0.2391 0.1889  0.0559  0.0507  163 SER   B CB  
1675 O OG  . SER   B 154 ? 0.6139 0.6210 0.2303 0.1769  0.0514  0.0429  163 SER   B OG  
1676 N N   . ALA   B 155 ? 0.6060 0.6059 0.2082 0.1790  0.0416  0.0381  164 ALA   B N   
1677 C CA  . ALA   B 155 ? 0.6105 0.5959 0.2036 0.1765  0.0325  0.0292  164 ALA   B CA  
1678 C C   . ALA   B 155 ? 0.6201 0.6003 0.2108 0.1786  0.0304  0.0248  164 ALA   B C   
1679 O O   . ALA   B 155 ? 0.6444 0.6300 0.2438 0.1756  0.0361  0.0278  164 ALA   B O   
1680 C CB  . ALA   B 155 ? 0.6020 0.5810 0.2012 0.1608  0.0311  0.0270  164 ALA   B CB  
1681 N N   . ILE   B 156 ? 0.6323 0.6015 0.2121 0.1830  0.0215  0.0176  165 ILE   B N   
1682 C CA  . ILE   B 156 ? 0.6285 0.5886 0.2095 0.1767  0.0175  0.0111  165 ILE   B CA  
1683 C C   . ILE   B 156 ? 0.6083 0.5615 0.1959 0.1602  0.0160  0.0079  165 ILE   B C   
1684 O O   . ILE   B 156 ? 0.6333 0.5760 0.2140 0.1576  0.0084  0.0033  165 ILE   B O   
1685 C CB  . ILE   B 156 ? 0.6403 0.5910 0.2077 0.1874  0.0078  0.0047  165 ILE   B CB  
1686 C CG1 . ILE   B 156 ? 0.6582 0.6169 0.2173 0.2051  0.0094  0.0081  165 ILE   B CG1 
1687 C CG2 . ILE   B 156 ? 0.6422 0.5849 0.2110 0.1831  0.0032  -0.0017 165 ILE   B CG2 
1688 C CD1 . ILE   B 156 ? 0.6682 0.6180 0.2135 0.2171  -0.0003 0.0015  165 ILE   B CD1 
1689 N N   . THR   B 157 ? 0.5968 0.5555 0.1967 0.1498  0.0228  0.0105  166 THR   B N   
1690 C CA  . THR   B 157 ? 0.5715 0.5256 0.1781 0.1340  0.0225  0.0079  166 THR   B CA  
1691 C C   . THR   B 157 ? 0.5746 0.5215 0.1817 0.1291  0.0181  0.0011  166 THR   B C   
1692 O O   . THR   B 157 ? 0.5751 0.5260 0.1877 0.1305  0.0211  0.0005  166 THR   B O   
1693 C CB  . THR   B 157 ? 0.5661 0.5292 0.1854 0.1262  0.0309  0.0128  166 THR   B CB  
1694 O OG1 . THR   B 157 ? 0.5686 0.5397 0.1879 0.1327  0.0347  0.0197  166 THR   B OG1 
1695 C CG2 . THR   B 157 ? 0.5560 0.5152 0.1812 0.1110  0.0308  0.0097  166 THR   B CG2 
1696 N N   . GLN   B 158 ? 0.5656 0.5018 0.1673 0.1232  0.0108  -0.0038 167 GLN   B N   
1697 C CA  . GLN   B 158 ? 0.5699 0.4998 0.1735 0.1161  0.0066  -0.0098 167 GLN   B CA  
1698 C C   . GLN   B 158 ? 0.5818 0.5097 0.1911 0.1003  0.0077  -0.0107 167 GLN   B C   
1699 O O   . GLN   B 158 ? 0.5623 0.4879 0.1681 0.0974  0.0071  -0.0083 167 GLN   B O   
1700 C CB  . GLN   B 158 ? 0.5813 0.5005 0.1742 0.1227  -0.0033 -0.0144 167 GLN   B CB  
1701 C CG  . GLN   B 158 ? 0.5828 0.4960 0.1780 0.1176  -0.0086 -0.0205 167 GLN   B CG  
1702 C CD  . GLN   B 158 ? 0.5794 0.4998 0.1828 0.1187  -0.0040 -0.0217 167 GLN   B CD  
1703 O OE1 . GLN   B 158 ? 0.5673 0.4956 0.1806 0.1114  0.0035  -0.0197 167 GLN   B OE1 
1704 N NE2 . GLN   B 158 ? 0.5780 0.4953 0.1771 0.1283  -0.0092 -0.0255 167 GLN   B NE2 
1705 N N   . GLY   B 159 ? 0.6019 0.5309 0.2188 0.0914  0.0090  -0.0141 168 GLY   B N   
1706 C CA  . GLY   B 159 ? 0.6376 0.5651 0.2588 0.0768  0.0098  -0.0153 168 GLY   B CA  
1707 C C   . GLY   B 159 ? 0.6917 0.6086 0.3070 0.0728  0.0014  -0.0191 168 GLY   B C   
1708 O O   . GLY   B 159 ? 0.7464 0.6562 0.3534 0.0816  -0.0054 -0.0205 168 GLY   B O   
1709 N N   . LYS   B 160 ? 0.7607 0.6766 0.3800 0.0598  0.0016  -0.0206 169 LYS   B N   
1710 C CA  . LYS   B 160 ? 0.8238 0.7302 0.4395 0.0537  -0.0059 -0.0237 169 LYS   B CA  
1711 C C   . LYS   B 160 ? 0.8504 0.7624 0.4763 0.0458  -0.0037 -0.0275 169 LYS   B C   
1712 O O   . LYS   B 160 ? 0.8311 0.7529 0.4653 0.0408  0.0040  -0.0271 169 LYS   B O   
1713 C CB  . LYS   B 160 ? 0.8857 0.7861 0.4962 0.0451  -0.0077 -0.0210 169 LYS   B CB  
1714 C CG  . LYS   B 160 ? 0.9346 0.8267 0.5436 0.0352  -0.0140 -0.0228 169 LYS   B CG  
1715 C CD  . LYS   B 160 ? 0.9678 0.8516 0.5691 0.0287  -0.0173 -0.0196 169 LYS   B CD  
1716 C CE  . LYS   B 160 ? 0.9954 0.8698 0.5949 0.0196  -0.0245 -0.0207 169 LYS   B CE  
1717 N NZ  . LYS   B 160 ? 1.0281 0.9034 0.6281 0.0059  -0.0213 -0.0178 169 LYS   B NZ  
1718 N N   . ARG   B 161 ? 0.8933 0.7996 0.5191 0.0451  -0.0105 -0.0314 170 ARG   B N   
1719 C CA  . ARG   B 161 ? 0.9444 0.8563 0.5805 0.0372  -0.0093 -0.0353 170 ARG   B CA  
1720 C C   . ARG   B 161 ? 1.0068 0.9143 0.6432 0.0235  -0.0122 -0.0349 170 ARG   B C   
1721 O O   . ARG   B 161 ? 1.0099 0.9057 0.6390 0.0239  -0.0207 -0.0346 170 ARG   B O   
1722 C CB  . ARG   B 161 ? 0.9602 0.8697 0.5968 0.0469  -0.0148 -0.0396 170 ARG   B CB  
1723 C CG  . ARG   B 161 ? 0.9522 0.8676 0.5998 0.0409  -0.0146 -0.0443 170 ARG   B CG  
1724 C CD  . ARG   B 161 ? 0.9684 0.8783 0.6147 0.0499  -0.0228 -0.0488 170 ARG   B CD  
1725 N NE  . ARG   B 161 ? 0.9832 0.8991 0.6409 0.0435  -0.0229 -0.0534 170 ARG   B NE  
1726 C CZ  . ARG   B 161 ? 0.9881 0.9107 0.6522 0.0495  -0.0214 -0.0572 170 ARG   B CZ  
1727 N NH1 . ARG   B 161 ? 0.9546 0.8784 0.6145 0.0623  -0.0194 -0.0565 170 ARG   B NH1 
1728 N NH2 . ARG   B 161 ? 1.0060 0.9345 0.6811 0.0425  -0.0218 -0.0614 170 ARG   B NH2 
1729 N N   . GLU   B 162 ? 1.0896 1.0059 0.7334 0.0122  -0.0054 -0.0345 171 GLU   B N   
1730 C CA  . GLU   B 162 ? 1.1536 1.0683 0.7982 -0.0017 -0.0064 -0.0332 171 GLU   B CA  
1731 C C   . GLU   B 162 ? 1.1580 1.0765 0.8119 -0.0076 -0.0086 -0.0372 171 GLU   B C   
1732 O O   . GLU   B 162 ? 1.2179 1.1282 0.8704 -0.0122 -0.0162 -0.0374 171 GLU   B O   
1733 C CB  . GLU   B 162 ? 1.2117 1.1354 0.8590 -0.0100 0.0023  -0.0309 171 GLU   B CB  
1734 C CG  . GLU   B 162 ? 1.2545 1.1754 0.8942 -0.0056 0.0045  -0.0269 171 GLU   B CG  
1735 C CD  . GLU   B 162 ? 1.3148 1.2253 0.9443 -0.0107 0.0002  -0.0229 171 GLU   B CD  
1736 O OE1 . GLU   B 162 ? 1.2947 1.2081 0.9245 -0.0216 0.0034  -0.0210 171 GLU   B OE1 
1737 O OE2 . GLU   B 162 ? 1.3765 1.2762 0.9974 -0.0032 -0.0066 -0.0217 171 GLU   B OE2 
1738 S S   A DMS   C .   ? 0.6702 0.7359 0.3638 0.1602  0.0942  0.0996  201 DMS   B S   
1739 S S   B DMS   C .   ? 0.6704 0.7361 0.3640 0.1602  0.0942  0.0996  201 DMS   B S   
1740 O O   A DMS   C .   ? 0.6751 0.7514 0.3676 0.1654  0.0964  0.1051  201 DMS   B O   
1741 O O   B DMS   C .   ? 0.6750 0.7512 0.3675 0.1655  0.0964  0.1051  201 DMS   B O   
1742 C C1  A DMS   C .   ? 0.6637 0.7176 0.3610 0.1462  0.0886  0.0887  201 DMS   B C1  
1743 C C1  B DMS   C .   ? 0.6636 0.7175 0.3609 0.1462  0.0886  0.0887  201 DMS   B C1  
1744 C C2  A DMS   C .   ? 0.6790 0.7366 0.3532 0.1713  0.0889  0.0908  201 DMS   B C2  
1745 C C2  B DMS   C .   ? 0.6791 0.7366 0.3532 0.1713  0.0889  0.0908  201 DMS   B C2  
1746 S S   A DMS   D .   ? 6.7533 6.7561 6.5222 0.0197  0.0652  -0.0099 202 DMS   B S   
1747 S S   B DMS   D .   ? 6.7533 6.7561 6.5222 0.0197  0.0652  -0.0099 202 DMS   B S   
1748 O O   A DMS   D .   ? 6.6829 6.6849 6.4393 0.0191  0.0654  -0.0116 202 DMS   B O   
1749 O O   B DMS   D .   ? 6.6829 6.6849 6.4393 0.0191  0.0654  -0.0116 202 DMS   B O   
1750 C C1  A DMS   D .   ? 6.6931 6.6972 6.4679 0.0214  0.0651  -0.0167 202 DMS   B C1  
1751 C C1  B DMS   D .   ? 6.6931 6.6972 6.4679 0.0214  0.0651  -0.0167 202 DMS   B C1  
1752 C C2  A DMS   D .   ? 6.5705 6.5729 6.3430 0.0276  0.0664  0.0004  202 DMS   B C2  
1753 C C2  B DMS   D .   ? 6.5705 6.5729 6.3430 0.0276  0.0664  0.0004  202 DMS   B C2  
1754 S S   A DMS   E .   ? 0.5307 0.5755 0.2162 0.1371  0.0779  0.0751  203 DMS   B S   
1755 S S   B DMS   E .   ? 0.5308 0.5757 0.2163 0.1371  0.0779  0.0751  203 DMS   B S   
1756 O O   A DMS   E .   ? 0.5331 0.5801 0.2153 0.1381  0.0758  0.0750  203 DMS   B O   
1757 O O   B DMS   E .   ? 0.5332 0.5802 0.2154 0.1381  0.0758  0.0750  203 DMS   B O   
1758 C C1  A DMS   E .   ? 0.5245 0.5577 0.2149 0.1224  0.0745  0.0666  203 DMS   B C1  
1759 C C1  B DMS   E .   ? 0.5246 0.5578 0.2150 0.1224  0.0745  0.0666  203 DMS   B C1  
1760 C C2  A DMS   E .   ? 0.5259 0.5821 0.2299 0.1328  0.0850  0.0860  203 DMS   B C2  
1761 C C2  B DMS   E .   ? 0.5259 0.5821 0.2300 0.1328  0.0850  0.0860  203 DMS   B C2  
1762 N N1  C A1BG3 F .   ? 0.8754 0.9161 0.5745 0.1283  0.0812  0.0751  204 A1BG3 B N1  
1763 N N1  D A1BG3 F .   ? 0.8757 0.9164 0.5748 0.1283  0.0812  0.0751  204 A1BG3 B N1  
1764 N N3  C A1BG3 F .   ? 0.8609 0.8938 0.5835 0.0978  0.0785  0.0679  204 A1BG3 B N3  
1765 N N3  D A1BG3 F .   ? 0.8607 0.8936 0.5833 0.0978  0.0785  0.0679  204 A1BG3 B N3  
1766 C C4  C A1BG3 F .   ? 0.9567 1.0323 0.6650 0.1520  0.0973  0.1065  204 A1BG3 B C4  
1767 C C4  D A1BG3 F .   ? 0.9563 1.0319 0.6646 0.1520  0.0973  0.1065  204 A1BG3 B C4  
1768 C C5  C A1BG3 F .   ? 0.9293 0.9937 0.6242 0.1559  0.0925  0.0970  204 A1BG3 B C5  
1769 C C5  D A1BG3 F .   ? 0.9294 0.9939 0.6243 0.1559  0.0925  0.0970  204 A1BG3 B C5  
1770 C C6  C A1BG3 F .   ? 0.9361 1.0030 0.6187 0.1692  0.0929  0.0982  204 A1BG3 B C6  
1771 C C6  D A1BG3 F .   ? 0.9360 1.0029 0.6186 0.1692  0.0929  0.0982  204 A1BG3 B C6  
1772 C C7  C A1BG3 F .   ? 0.9284 0.9852 0.5989 0.1733  0.0878  0.0894  204 A1BG3 B C7  
1773 C C7  D A1BG3 F .   ? 0.9286 0.9854 0.5992 0.1733  0.0878  0.0894  204 A1BG3 B C7  
1774 C C8  C A1BG3 F .   ? 0.9167 0.9619 0.5879 0.1639  0.0828  0.0796  204 A1BG3 B C8  
1775 C C8  D A1BG3 F .   ? 0.9171 0.9622 0.5882 0.1639  0.0828  0.0796  204 A1BG3 B C8  
1776 C C10 C A1BG3 F .   ? 0.9140 0.9663 0.6080 0.1469  0.0873  0.0866  204 A1BG3 B C10 
1777 C C10 D A1BG3 F .   ? 0.9139 0.9661 0.6079 0.1469  0.0873  0.0866  204 A1BG3 B C10 
1778 C C13 C A1BG3 F .   ? 0.8556 0.8847 0.5559 0.1110  0.0747  0.0637  204 A1BG3 B C13 
1779 C C13 D A1BG3 F .   ? 0.8561 0.8852 0.5564 0.1110  0.0747  0.0637  204 A1BG3 B C13 
1780 C C15 C A1BG3 F .   ? 0.8635 0.9020 0.5852 0.1070  0.0818  0.0740  204 A1BG3 B C15 
1781 C C15 D A1BG3 F .   ? 0.8635 0.9020 0.5851 0.1070  0.0818  0.0740  204 A1BG3 B C15 
1782 C C17 C A1BG3 F .   ? 0.9765 1.0731 0.7106 0.1448  0.1051  0.1235  204 A1BG3 B C17 
1783 C C17 D A1BG3 F .   ? 0.9760 1.0726 0.7101 0.1447  0.1051  0.1235  204 A1BG3 B C17 
1784 C C1  C A1BG3 F .   ? 0.9737 1.0796 0.7182 0.1494  0.1136  0.1397  204 A1BG3 B C1  
1785 C C1  D A1BG3 F .   ? 0.9736 1.0795 0.7180 0.1494  0.1136  0.1397  204 A1BG3 B C1  
1786 C C2  C A1BG3 F .   ? 0.9721 1.0679 0.7042 0.1492  0.1074  0.1267  204 A1BG3 B C2  
1787 C C2  D A1BG3 F .   ? 0.9718 1.0676 0.7039 0.1492  0.1074  0.1267  204 A1BG3 B C2  
1788 C C3  C A1BG3 F .   ? 0.9623 1.0474 0.6809 0.1532  0.1033  0.1177  204 A1BG3 B C3  
1789 C C3  D A1BG3 F .   ? 0.9623 1.0474 0.6808 0.1532  0.1033  0.1177  204 A1BG3 B C3  
1790 C C9  C A1BG3 F .   ? 0.9098 0.9530 0.5923 0.1509  0.0828  0.0783  204 A1BG3 B C9  
1791 C C9  D A1BG3 F .   ? 0.9100 0.9532 0.5925 0.1509  0.0828  0.0783  204 A1BG3 B C9  
1792 C C11 C A1BG3 F .   ? 0.8830 0.9318 0.5883 0.1332  0.0862  0.0839  204 A1BG3 B C11 
1793 C C11 D A1BG3 F .   ? 0.8834 0.9322 0.5887 0.1332  0.0862  0.0839  204 A1BG3 B C11 
1794 O O1  C A1BG3 F .   ? 0.8705 0.9233 0.5896 0.1269  0.0895  0.0894  204 A1BG3 B O1  
1795 O O1  D A1BG3 F .   ? 0.8711 0.9239 0.5902 0.1269  0.0895  0.0894  204 A1BG3 B O1  
1796 C C12 C A1BG3 F .   ? 0.8690 0.9055 0.5757 0.1162  0.0795  0.0713  204 A1BG3 B C12 
1797 C C12 D A1BG3 F .   ? 0.8690 0.9055 0.5758 0.1162  0.0795  0.0713  204 A1BG3 B C12 
1798 N N2  C A1BG3 F .   ? 0.8624 0.8895 0.5717 0.1000  0.0744  0.0618  204 A1BG3 B N2  
1799 N N2  D A1BG3 F .   ? 0.8623 0.8895 0.5717 0.1000  0.0744  0.0618  204 A1BG3 B N2  
1800 C C14 C A1BG3 F .   ? 0.8510 0.8830 0.5861 0.0868  0.0786  0.0670  204 A1BG3 B C14 
1801 C C14 D A1BG3 F .   ? 0.8510 0.8831 0.5861 0.0868  0.0786  0.0670  204 A1BG3 B C14 
1802 C C16 C A1BG3 F .   ? 0.9591 1.0364 0.6703 0.1474  0.0958  0.1051  204 A1BG3 B C16 
1803 C C16 D A1BG3 F .   ? 0.9589 1.0362 0.6701 0.1474  0.0958  0.1051  204 A1BG3 B C16 
1804 N N4  C A1BG3 F .   ? 0.9691 1.0567 0.6929 0.1439  0.0995  0.1132  204 A1BG3 B N4  
1805 N N4  D A1BG3 F .   ? 0.9687 1.0563 0.6925 0.1439  0.0995  0.1132  204 A1BG3 B N4  
1806 F F1  C A1BG3 F .   ? 0.9955 1.1026 0.7433 0.1407  0.1084  0.1316  204 A1BG3 B F1  
1807 F F1  D A1BG3 F .   ? 0.9944 1.1016 0.7423 0.1407  0.1084  0.1316  204 A1BG3 B F1  
1808 S S   C SO4   G .   ? 1.1724 1.1757 0.9403 0.0202  0.0654  -0.0137 205 SO4   B S   
1809 S S   D SO4   G .   ? 1.1724 1.1757 0.9403 0.0202  0.0654  -0.0137 205 SO4   B S   
1810 O O1  C SO4   G .   ? 1.1683 1.1708 0.9396 0.0240  0.0658  -0.0044 205 SO4   B O1  
1811 O O1  D SO4   G .   ? 1.1683 1.1708 0.9396 0.0240  0.0658  -0.0044 205 SO4   B O1  
1812 O O2  C SO4   G .   ? 1.1885 1.1928 0.9613 0.0144  0.0642  -0.0188 205 SO4   B O2  
1813 O O2  D SO4   G .   ? 1.1885 1.1928 0.9613 0.0144  0.0642  -0.0188 205 SO4   B O2  
1814 O O3  C SO4   G .   ? 1.1919 1.1959 0.9635 0.0240  0.0655  -0.0165 205 SO4   B O3  
1815 O O3  D SO4   G .   ? 1.1919 1.1959 0.9635 0.0240  0.0655  -0.0165 205 SO4   B O3  
1816 O O4  C SO4   G .   ? 1.1428 1.1454 0.8989 0.0185  0.0655  -0.0150 205 SO4   B O4  
1817 O O4  D SO4   G .   ? 1.1428 1.1454 0.8989 0.0185  0.0655  -0.0150 205 SO4   B O4  
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