data_7HPH
# 
_entry.id   7HPH 
# 
_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   7HPH         pdb_00007hph 10.2210/pdb7hph/pdb 
WWPDB D_1001407767 ?            ?                   
# 
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                        7HPH 
_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    2  ? ?    ? ? 
4 non-polymer syn '4-methoxy-2-(piperazin-1-yl)-6-{[2-(piperazin-1-yl)pyridin-4-yl]methyl}pyrimidine' 369.464   1  ? ?    ? ? 
5 water       nat water                                                                               18.015    39 ? ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                                                DMS   
4 '4-methoxy-2-(piperazin-1-yl)-6-{[2-(piperazin-1-yl)pyridin-4-yl]methyl}pyrimidine' A1BGS 
5 water                                                                               HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   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 
A1BGS non-polymer         . '4-methoxy-2-(piperazin-1-yl)-6-{[2-(piperazin-1-yl)pyridin-4-yl]methyl}pyrimidine' ? 'C19 H27 N7 O'   
369.464 
ALA   'L-peptide linking' y ALANINE                                                                             ? 'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                            ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                          ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                     ? 'C4 H7 N O4'     
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                            ? 'C3 H7 N O2 S'   
121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                ? 'C2 H6 O S'      
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                           ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                     ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                             ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                           ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                               ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                          ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                             ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                              ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                          ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                       ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                             ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                              ? 'C3 H7 N O3'     
105.093 
THR   'L-peptide linking' y THREONINE                                                                           ? 'C4 H9 N O3'     
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                          ? 'C11 H12 N2 O2'  
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                            ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                              ? 'C5 H11 N O2'    
117.146 
# 
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        A1BGS 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BGS 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS   1  201 202 DMS   DMS B . 
D 4 A1BGS 1  202 301 A1BGS LIG B . 
E 3 DMS   1  203 302 DMS   DMS B . 
F 5 HOH   1  101 118 HOH   HOH A . 
F 5 HOH   2  102 98  HOH   HOH A . 
F 5 HOH   3  103 20  HOH   HOH A . 
F 5 HOH   4  104 105 HOH   HOH A . 
F 5 HOH   5  105 50  HOH   HOH A . 
F 5 HOH   6  106 87  HOH   HOH A . 
F 5 HOH   7  107 12  HOH   HOH A . 
F 5 HOH   8  108 120 HOH   HOH A . 
F 5 HOH   9  109 121 HOH   HOH A . 
F 5 HOH   10 110 119 HOH   HOH A . 
G 5 HOH   1  301 11  HOH   HOH B . 
G 5 HOH   2  302 5   HOH   HOH B . 
G 5 HOH   3  303 46  HOH   HOH B . 
G 5 HOH   4  304 14  HOH   HOH B . 
G 5 HOH   5  305 39  HOH   HOH B . 
G 5 HOH   6  306 108 HOH   HOH B . 
G 5 HOH   7  307 30  HOH   HOH B . 
G 5 HOH   8  308 63  HOH   HOH B . 
G 5 HOH   9  309 2   HOH   HOH B . 
G 5 HOH   10 310 103 HOH   HOH B . 
G 5 HOH   11 311 36  HOH   HOH B . 
G 5 HOH   12 312 102 HOH   HOH B . 
G 5 HOH   13 313 26  HOH   HOH B . 
G 5 HOH   14 314 64  HOH   HOH B . 
G 5 HOH   15 315 58  HOH   HOH B . 
G 5 HOH   16 316 3   HOH   HOH B . 
G 5 HOH   17 317 49  HOH   HOH B . 
G 5 HOH   18 318 115 HOH   HOH B . 
G 5 HOH   19 319 35  HOH   HOH B . 
G 5 HOH   20 320 21  HOH   HOH B . 
G 5 HOH   21 321 29  HOH   HOH B . 
G 5 HOH   22 322 61  HOH   HOH B . 
G 5 HOH   23 323 23  HOH   HOH B . 
G 5 HOH   24 324 17  HOH   HOH B . 
G 5 HOH   25 325 67  HOH   HOH B . 
G 5 HOH   26 326 80  HOH   HOH B . 
G 5 HOH   27 327 116 HOH   HOH B . 
G 5 HOH   28 328 75  HOH   HOH B . 
G 5 HOH   29 329 122 HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (20-OCT-2021)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
'data reduction' XDS     .                      ? 5 
'data reduction' XDS     .                      ? 6 
'data reduction' XDS     .                      ? 7 
'data reduction' XDS     .                      ? 8 
# 
_cell.entry_id           7HPH 
_cell.length_a           42.647 
_cell.length_b           42.647 
_cell.length_c           216.930 
_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                         7HPH 
_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          7HPH 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.13 
_exptl_crystal.density_percent_sol   42.18 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-11-22 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92124 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92124 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HPH 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             54.232 
_reflns.d_resolution_high            2.337 
_reflns.number_obs                   5472 
_reflns.percent_possible_obs         59.1 
_reflns.pdbx_Rmerge_I_obs            0.196 
_reflns.pdbx_netI_over_sigmaI        5.5 
_reflns.pdbx_redundancy              10.7 
_reflns.pdbx_Rrim_I_all              0.205 
_reflns.pdbx_Rpim_I_all              0.056 
_reflns.pdbx_number_measured_all     58751 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  2.337 
_reflns_shell.d_res_low                   2.609 
_reflns_shell.number_measured_all         1839 
_reflns_shell.number_unique_obs           274 
_reflns_shell.Rmerge_I_obs                0.647 
_reflns_shell.pdbx_redundancy             6.7 
_reflns_shell.percent_possible_obs        11.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.5 
_reflns_shell.pdbx_Rrim_I_all             0.703 
_reflns_shell.pdbx_Rpim_I_all             0.269 
_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                                 7HPH 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     5472 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             54.23 
_refine.ls_d_res_high                            2.337 
_refine.ls_percent_reflns_obs                    59.1 
_refine.ls_R_factor_obs                          0.2308 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2276 
_refine.ls_R_factor_R_free                       0.2922 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.920 
_refine.ls_number_reflns_R_free                  269 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.873 
_refine.correlation_coeff_Fo_to_Fc_free          0.805 
_refine.B_iso_mean                               53.03 
_refine.aniso_B[1][1]                            8.82460 
_refine.aniso_B[2][2]                            8.82460 
_refine.aniso_B[3][3]                            -17.64920 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.450 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HPH 
_refine_analyze.Luzzati_coordinate_error_obs    0.43 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         35 
_refine_hist.number_atoms_solvent             39 
_refine_hist.number_atoms_total               1550 
_refine_hist.d_res_high                       2.337 
_refine_hist.d_res_low                        54.23 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.008 ? 2.00  1579 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.00  ? 2.00  2148 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  547  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  272  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1579 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           2.89  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           20.08 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  196  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  1162 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   14 
_refine_ls_shell.d_res_high                       2.34 
_refine_ls_shell.d_res_low                        2.70 
_refine_ls_shell.number_reflns_R_work             401 
_refine_ls_shell.R_factor_R_work                  0.2473 
_refine_ls_shell.percent_reflns_obs               13.30 
_refine_ls_shell.R_factor_R_free                  0.4078 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.75 
_refine_ls_shell.number_reflns_R_free             421 
_refine_ls_shell.number_reflns_all                421 
_refine_ls_shell.R_factor_all                     0.2551 
# 
_struct.entry_id                  7HPH 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0015442-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HPH 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, XChemExplorer, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 3 ? 
F N N 5 ? 
G N N 5 ? 
# 
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 7HPH A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HPH 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 7HPH SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HPH MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HPH MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HPH LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5170 ? 
1 MORE         -22  ? 
1 'SSA (A^2)'  9640 ? 
# 
_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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 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 ? LYS B 108 ? GLY B 114 LYS B 117 
AA3 4 ASP B 113 ? VAL B 117 ? ASP B 122 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 TYR A 9   ? N TYR A 52  O MET B 17  ? O MET B 26  
AA1 4 5 N GLY B 12  ? N GLY B 21  O MET B 32  ? O MET B 41  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N PHE B 37  ? N PHE B 46  O TYR B 70  ? O TYR B 79  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
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                   7HPH 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU B 30 ? ? -112.75 -158.29 
2 1 CYS B 80 ? ? 78.00   -22.67  
# 
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 -13.8532 -2.0172 -19.4334 -0.0744 0.0284 -0.4773 0.2777 0.1598 0.0584 4.7030 5.4856 6.1006 -1.2954 
2.2952 -0.0418 0.6225 0.5982 0.1434 -0.5364 -0.4660 -0.4248 0.0341 0.4307 -0.1565 
'X-RAY DIFFRACTION' 2 ? refined -18.3587 0.5083  -15.6088 0.2080  0.1298 -0.3771 0.2862 0.0327 0.0367 2.6514 1.9343 3.2242 -0.9111 
1.1256 -0.4092 0.4852 0.3297 0.1564 -0.1623 -0.4639 0.0470  0.0866 0.1525 -0.0213 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ B|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 1 Y 1 B GLU 177 ? B GLU 168 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BGS N1   N Y N 1   
A1BGS N3   N N N 2   
A1BGS C4   C Y N 3   
A1BGS C5   C N N 4   
A1BGS C6   C Y N 5   
A1BGS C7   C Y N 6   
A1BGS C8   C Y N 7   
A1BGS C10  C N N 8   
A1BGS C13  C N N 9   
A1BGS C15  C Y N 10  
A1BGS C17  C N N 11  
A1BGS C1   C N N 12  
A1BGS O1   O N N 13  
A1BGS C2   C Y N 14  
A1BGS C3   C Y N 15  
A1BGS C9   C Y N 16  
A1BGS N2   N N N 17  
A1BGS C11  C N N 18  
A1BGS C12  C N N 19  
A1BGS C14  C Y N 20  
A1BGS N4   N Y N 21  
A1BGS N5   N N N 22  
A1BGS C16  C N N 23  
A1BGS N6   N N N 24  
A1BGS C18  C N N 25  
A1BGS C19  C N N 26  
A1BGS N7   N Y N 27  
A1BGS H13  H N N 28  
A1BGS H5   H N N 29  
A1BGS H6   H N N 30  
A1BGS H7   H N N 31  
A1BGS H8   H N N 32  
A1BGS H10  H N N 33  
A1BGS H9   H N N 34  
A1BGS H16  H N N 35  
A1BGS H17  H N N 36  
A1BGS H22  H N N 37  
A1BGS H21  H N N 38  
A1BGS H1   H N N 39  
A1BGS H2   H N N 40  
A1BGS H3   H N N 41  
A1BGS H4   H N N 42  
A1BGS H11  H N N 43  
A1BGS H12  H N N 44  
A1BGS H14  H N N 45  
A1BGS H15  H N N 46  
A1BGS H18  H N N 47  
A1BGS H20  H N N 48  
A1BGS H19  H N N 49  
A1BGS H29  H N N 50  
A1BGS H25  H N N 51  
A1BGS H24  H N N 52  
A1BGS H27  H N N 53  
A1BGS H26  H N N 54  
ALA   N    N N N 55  
ALA   CA   C N S 56  
ALA   C    C N N 57  
ALA   O    O N N 58  
ALA   CB   C N N 59  
ALA   OXT  O N N 60  
ALA   H    H N N 61  
ALA   H2   H N N 62  
ALA   HA   H N N 63  
ALA   HB1  H N N 64  
ALA   HB2  H N N 65  
ALA   HB3  H N N 66  
ALA   HXT  H N N 67  
ARG   N    N N N 68  
ARG   CA   C N S 69  
ARG   C    C N N 70  
ARG   O    O N N 71  
ARG   CB   C N N 72  
ARG   CG   C N N 73  
ARG   CD   C N N 74  
ARG   NE   N N N 75  
ARG   CZ   C N N 76  
ARG   NH1  N N N 77  
ARG   NH2  N N N 78  
ARG   OXT  O N N 79  
ARG   H    H N N 80  
ARG   H2   H N N 81  
ARG   HA   H N N 82  
ARG   HB2  H N N 83  
ARG   HB3  H N N 84  
ARG   HG2  H N N 85  
ARG   HG3  H N N 86  
ARG   HD2  H N N 87  
ARG   HD3  H N N 88  
ARG   HE   H N N 89  
ARG   HH11 H N N 90  
ARG   HH12 H N N 91  
ARG   HH21 H N N 92  
ARG   HH22 H N N 93  
ARG   HXT  H N N 94  
ASN   N    N N N 95  
ASN   CA   C N S 96  
ASN   C    C N N 97  
ASN   O    O N N 98  
ASN   CB   C N N 99  
ASN   CG   C N N 100 
ASN   OD1  O N N 101 
ASN   ND2  N N N 102 
ASN   OXT  O N N 103 
ASN   H    H N N 104 
ASN   H2   H N N 105 
ASN   HA   H N N 106 
ASN   HB2  H N N 107 
ASN   HB3  H N N 108 
ASN   HD21 H N N 109 
ASN   HD22 H N N 110 
ASN   HXT  H N N 111 
ASP   N    N N N 112 
ASP   CA   C N S 113 
ASP   C    C N N 114 
ASP   O    O N N 115 
ASP   CB   C N N 116 
ASP   CG   C N N 117 
ASP   OD1  O N N 118 
ASP   OD2  O N N 119 
ASP   OXT  O N N 120 
ASP   H    H N N 121 
ASP   H2   H N N 122 
ASP   HA   H N N 123 
ASP   HB2  H N N 124 
ASP   HB3  H N N 125 
ASP   HD2  H N N 126 
ASP   HXT  H N N 127 
CYS   N    N N N 128 
CYS   CA   C N R 129 
CYS   C    C N N 130 
CYS   O    O N N 131 
CYS   CB   C N N 132 
CYS   SG   S N N 133 
CYS   OXT  O N N 134 
CYS   H    H N N 135 
CYS   H2   H N N 136 
CYS   HA   H N N 137 
CYS   HB2  H N N 138 
CYS   HB3  H N N 139 
CYS   HG   H N N 140 
CYS   HXT  H N N 141 
DMS   S    S N N 142 
DMS   O    O N N 143 
DMS   C1   C N N 144 
DMS   C2   C N N 145 
DMS   H11  H N N 146 
DMS   H12  H N N 147 
DMS   H13  H N N 148 
DMS   H21  H N N 149 
DMS   H22  H N N 150 
DMS   H23  H N N 151 
GLN   N    N N N 152 
GLN   CA   C N S 153 
GLN   C    C N N 154 
GLN   O    O N N 155 
GLN   CB   C N N 156 
GLN   CG   C N N 157 
GLN   CD   C N N 158 
GLN   OE1  O N N 159 
GLN   NE2  N N N 160 
GLN   OXT  O N N 161 
GLN   H    H N N 162 
GLN   H2   H N N 163 
GLN   HA   H N N 164 
GLN   HB2  H N N 165 
GLN   HB3  H N N 166 
GLN   HG2  H N N 167 
GLN   HG3  H N N 168 
GLN   HE21 H N N 169 
GLN   HE22 H N N 170 
GLN   HXT  H N N 171 
GLU   N    N N N 172 
GLU   CA   C N S 173 
GLU   C    C N N 174 
GLU   O    O N N 175 
GLU   CB   C N N 176 
GLU   CG   C N N 177 
GLU   CD   C N N 178 
GLU   OE1  O N N 179 
GLU   OE2  O N N 180 
GLU   OXT  O N N 181 
GLU   H    H N N 182 
GLU   H2   H N N 183 
GLU   HA   H N N 184 
GLU   HB2  H N N 185 
GLU   HB3  H N N 186 
GLU   HG2  H N N 187 
GLU   HG3  H N N 188 
GLU   HE2  H N N 189 
GLU   HXT  H N N 190 
GLY   N    N N N 191 
GLY   CA   C N N 192 
GLY   C    C N N 193 
GLY   O    O N N 194 
GLY   OXT  O N N 195 
GLY   H    H N N 196 
GLY   H2   H N N 197 
GLY   HA2  H N N 198 
GLY   HA3  H N N 199 
GLY   HXT  H N N 200 
HIS   N    N N N 201 
HIS   CA   C N S 202 
HIS   C    C N N 203 
HIS   O    O N N 204 
HIS   CB   C N N 205 
HIS   CG   C Y N 206 
HIS   ND1  N Y N 207 
HIS   CD2  C Y N 208 
HIS   CE1  C Y N 209 
HIS   NE2  N Y N 210 
HIS   OXT  O N N 211 
HIS   H    H N N 212 
HIS   H2   H N N 213 
HIS   HA   H N N 214 
HIS   HB2  H N N 215 
HIS   HB3  H N N 216 
HIS   HD1  H N N 217 
HIS   HD2  H N N 218 
HIS   HE1  H N N 219 
HIS   HE2  H N N 220 
HIS   HXT  H N N 221 
HOH   O    O N N 222 
HOH   H1   H N N 223 
HOH   H2   H N N 224 
ILE   N    N N N 225 
ILE   CA   C N S 226 
ILE   C    C N N 227 
ILE   O    O N N 228 
ILE   CB   C N S 229 
ILE   CG1  C N N 230 
ILE   CG2  C N N 231 
ILE   CD1  C N N 232 
ILE   OXT  O N N 233 
ILE   H    H N N 234 
ILE   H2   H N N 235 
ILE   HA   H N N 236 
ILE   HB   H N N 237 
ILE   HG12 H N N 238 
ILE   HG13 H N N 239 
ILE   HG21 H N N 240 
ILE   HG22 H N N 241 
ILE   HG23 H N N 242 
ILE   HD11 H N N 243 
ILE   HD12 H N N 244 
ILE   HD13 H N N 245 
ILE   HXT  H N N 246 
LEU   N    N N N 247 
LEU   CA   C N S 248 
LEU   C    C N N 249 
LEU   O    O N N 250 
LEU   CB   C N N 251 
LEU   CG   C N N 252 
LEU   CD1  C N N 253 
LEU   CD2  C N N 254 
LEU   OXT  O N N 255 
LEU   H    H N N 256 
LEU   H2   H N N 257 
LEU   HA   H N N 258 
LEU   HB2  H N N 259 
LEU   HB3  H N N 260 
LEU   HG   H N N 261 
LEU   HD11 H N N 262 
LEU   HD12 H N N 263 
LEU   HD13 H N N 264 
LEU   HD21 H N N 265 
LEU   HD22 H N N 266 
LEU   HD23 H N N 267 
LEU   HXT  H N N 268 
LYS   N    N N N 269 
LYS   CA   C N S 270 
LYS   C    C N N 271 
LYS   O    O N N 272 
LYS   CB   C N N 273 
LYS   CG   C N N 274 
LYS   CD   C N N 275 
LYS   CE   C N N 276 
LYS   NZ   N N N 277 
LYS   OXT  O N N 278 
LYS   H    H N N 279 
LYS   H2   H N N 280 
LYS   HA   H N N 281 
LYS   HB2  H N N 282 
LYS   HB3  H N N 283 
LYS   HG2  H N N 284 
LYS   HG3  H N N 285 
LYS   HD2  H N N 286 
LYS   HD3  H N N 287 
LYS   HE2  H N N 288 
LYS   HE3  H N N 289 
LYS   HZ1  H N N 290 
LYS   HZ2  H N N 291 
LYS   HZ3  H N N 292 
LYS   HXT  H N N 293 
MET   N    N N N 294 
MET   CA   C N S 295 
MET   C    C N N 296 
MET   O    O N N 297 
MET   CB   C N N 298 
MET   CG   C N N 299 
MET   SD   S N N 300 
MET   CE   C N N 301 
MET   OXT  O N N 302 
MET   H    H N N 303 
MET   H2   H N N 304 
MET   HA   H N N 305 
MET   HB2  H N N 306 
MET   HB3  H N N 307 
MET   HG2  H N N 308 
MET   HG3  H N N 309 
MET   HE1  H N N 310 
MET   HE2  H N N 311 
MET   HE3  H N N 312 
MET   HXT  H N N 313 
PHE   N    N N N 314 
PHE   CA   C N S 315 
PHE   C    C N N 316 
PHE   O    O N N 317 
PHE   CB   C N N 318 
PHE   CG   C Y N 319 
PHE   CD1  C Y N 320 
PHE   CD2  C Y N 321 
PHE   CE1  C Y N 322 
PHE   CE2  C Y N 323 
PHE   CZ   C Y N 324 
PHE   OXT  O N N 325 
PHE   H    H N N 326 
PHE   H2   H N N 327 
PHE   HA   H N N 328 
PHE   HB2  H N N 329 
PHE   HB3  H N N 330 
PHE   HD1  H N N 331 
PHE   HD2  H N N 332 
PHE   HE1  H N N 333 
PHE   HE2  H N N 334 
PHE   HZ   H N N 335 
PHE   HXT  H N N 336 
PRO   N    N N N 337 
PRO   CA   C N S 338 
PRO   C    C N N 339 
PRO   O    O N N 340 
PRO   CB   C N N 341 
PRO   CG   C N N 342 
PRO   CD   C N N 343 
PRO   OXT  O N N 344 
PRO   H    H N N 345 
PRO   HA   H N N 346 
PRO   HB2  H N N 347 
PRO   HB3  H N N 348 
PRO   HG2  H N N 349 
PRO   HG3  H N N 350 
PRO   HD2  H N N 351 
PRO   HD3  H N N 352 
PRO   HXT  H N N 353 
SER   N    N N N 354 
SER   CA   C N S 355 
SER   C    C N N 356 
SER   O    O N N 357 
SER   CB   C N N 358 
SER   OG   O N N 359 
SER   OXT  O N N 360 
SER   H    H N N 361 
SER   H2   H N N 362 
SER   HA   H N N 363 
SER   HB2  H N N 364 
SER   HB3  H N N 365 
SER   HG   H N N 366 
SER   HXT  H N N 367 
THR   N    N N N 368 
THR   CA   C N S 369 
THR   C    C N N 370 
THR   O    O N N 371 
THR   CB   C N R 372 
THR   OG1  O N N 373 
THR   CG2  C N N 374 
THR   OXT  O N N 375 
THR   H    H N N 376 
THR   H2   H N N 377 
THR   HA   H N N 378 
THR   HB   H N N 379 
THR   HG1  H N N 380 
THR   HG21 H N N 381 
THR   HG22 H N N 382 
THR   HG23 H N N 383 
THR   HXT  H N N 384 
TRP   N    N N N 385 
TRP   CA   C N S 386 
TRP   C    C N N 387 
TRP   O    O N N 388 
TRP   CB   C N N 389 
TRP   CG   C Y N 390 
TRP   CD1  C Y N 391 
TRP   CD2  C Y N 392 
TRP   NE1  N Y N 393 
TRP   CE2  C Y N 394 
TRP   CE3  C Y N 395 
TRP   CZ2  C Y N 396 
TRP   CZ3  C Y N 397 
TRP   CH2  C Y N 398 
TRP   OXT  O N N 399 
TRP   H    H N N 400 
TRP   H2   H N N 401 
TRP   HA   H N N 402 
TRP   HB2  H N N 403 
TRP   HB3  H N N 404 
TRP   HD1  H N N 405 
TRP   HE1  H N N 406 
TRP   HE3  H N N 407 
TRP   HZ2  H N N 408 
TRP   HZ3  H N N 409 
TRP   HH2  H N N 410 
TRP   HXT  H N N 411 
TYR   N    N N N 412 
TYR   CA   C N S 413 
TYR   C    C N N 414 
TYR   O    O N N 415 
TYR   CB   C N N 416 
TYR   CG   C Y N 417 
TYR   CD1  C Y N 418 
TYR   CD2  C Y N 419 
TYR   CE1  C Y N 420 
TYR   CE2  C Y N 421 
TYR   CZ   C Y N 422 
TYR   OH   O N N 423 
TYR   OXT  O N N 424 
TYR   H    H N N 425 
TYR   H2   H N N 426 
TYR   HA   H N N 427 
TYR   HB2  H N N 428 
TYR   HB3  H N N 429 
TYR   HD1  H N N 430 
TYR   HD2  H N N 431 
TYR   HE1  H N N 432 
TYR   HE2  H N N 433 
TYR   HH   H N N 434 
TYR   HXT  H N N 435 
VAL   N    N N N 436 
VAL   CA   C N S 437 
VAL   C    C N N 438 
VAL   O    O N N 439 
VAL   CB   C N N 440 
VAL   CG1  C N N 441 
VAL   CG2  C N N 442 
VAL   OXT  O N N 443 
VAL   H    H N N 444 
VAL   H2   H N N 445 
VAL   HA   H N N 446 
VAL   HB   H N N 447 
VAL   HG11 H N N 448 
VAL   HG12 H N N 449 
VAL   HG13 H N N 450 
VAL   HG21 H N N 451 
VAL   HG22 H N N 452 
VAL   HG23 H N N 453 
VAL   HXT  H N N 454 
# 
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 
A1BGS C1  O1   sing N N 1   
A1BGS O1  C2   sing N N 2   
A1BGS C2  C3   doub Y N 3   
A1BGS C3  C4   sing Y N 4   
A1BGS C4  C5   sing N N 5   
A1BGS C5  C6   sing N N 6   
A1BGS C6  C7   doub Y N 7   
A1BGS C7  C8   sing Y N 8   
A1BGS C8  N1   doub Y N 9   
A1BGS N1  C9   sing Y N 10  
A1BGS C9  N2   sing N N 11  
A1BGS N2  C10  sing N N 12  
A1BGS C10 C11  sing N N 13  
A1BGS C11 N3   sing N N 14  
A1BGS N3  C12  sing N N 15  
A1BGS C12 C13  sing N N 16  
A1BGS C9  C14  doub Y N 17  
A1BGS C4  N4   doub Y N 18  
A1BGS N4  C15  sing Y N 19  
A1BGS C15 N5   sing N N 20  
A1BGS N5  C16  sing N N 21  
A1BGS C16 C17  sing N N 22  
A1BGS C17 N6   sing N N 23  
A1BGS N6  C18  sing N N 24  
A1BGS C18 C19  sing N N 25  
A1BGS C15 N7   doub Y N 26  
A1BGS C2  N7   sing Y N 27  
A1BGS C6  C14  sing Y N 28  
A1BGS N5  C19  sing N N 29  
A1BGS N2  C13  sing N N 30  
A1BGS N3  H13  sing N N 31  
A1BGS C5  H5   sing N N 32  
A1BGS C5  H6   sing N N 33  
A1BGS C7  H7   sing N N 34  
A1BGS C8  H8   sing N N 35  
A1BGS C10 H10  sing N N 36  
A1BGS C10 H9   sing N N 37  
A1BGS C13 H16  sing N N 38  
A1BGS C13 H17  sing N N 39  
A1BGS C17 H22  sing N N 40  
A1BGS C17 H21  sing N N 41  
A1BGS C1  H1   sing N N 42  
A1BGS C1  H2   sing N N 43  
A1BGS C1  H3   sing N N 44  
A1BGS C3  H4   sing N N 45  
A1BGS C11 H11  sing N N 46  
A1BGS C11 H12  sing N N 47  
A1BGS C12 H14  sing N N 48  
A1BGS C12 H15  sing N N 49  
A1BGS C14 H18  sing N N 50  
A1BGS C16 H20  sing N N 51  
A1BGS C16 H19  sing N N 52  
A1BGS N6  H29  sing N N 53  
A1BGS C18 H25  sing N N 54  
A1BGS C18 H24  sing N N 55  
A1BGS C19 H27  sing N N 56  
A1BGS C19 H26  sing N N 57  
ALA   N   CA   sing N N 58  
ALA   N   H    sing N N 59  
ALA   N   H2   sing N N 60  
ALA   CA  C    sing N N 61  
ALA   CA  CB   sing N N 62  
ALA   CA  HA   sing N N 63  
ALA   C   O    doub N N 64  
ALA   C   OXT  sing N N 65  
ALA   CB  HB1  sing N N 66  
ALA   CB  HB2  sing N N 67  
ALA   CB  HB3  sing N N 68  
ALA   OXT HXT  sing N N 69  
ARG   N   CA   sing N N 70  
ARG   N   H    sing N N 71  
ARG   N   H2   sing N N 72  
ARG   CA  C    sing N N 73  
ARG   CA  CB   sing N N 74  
ARG   CA  HA   sing N N 75  
ARG   C   O    doub N N 76  
ARG   C   OXT  sing N N 77  
ARG   CB  CG   sing N N 78  
ARG   CB  HB2  sing N N 79  
ARG   CB  HB3  sing N N 80  
ARG   CG  CD   sing N N 81  
ARG   CG  HG2  sing N N 82  
ARG   CG  HG3  sing N N 83  
ARG   CD  NE   sing N N 84  
ARG   CD  HD2  sing N N 85  
ARG   CD  HD3  sing N N 86  
ARG   NE  CZ   sing N N 87  
ARG   NE  HE   sing N N 88  
ARG   CZ  NH1  sing N N 89  
ARG   CZ  NH2  doub N N 90  
ARG   NH1 HH11 sing N N 91  
ARG   NH1 HH12 sing N N 92  
ARG   NH2 HH21 sing N N 93  
ARG   NH2 HH22 sing N N 94  
ARG   OXT HXT  sing N N 95  
ASN   N   CA   sing N N 96  
ASN   N   H    sing N N 97  
ASN   N   H2   sing N N 98  
ASN   CA  C    sing N N 99  
ASN   CA  CB   sing N N 100 
ASN   CA  HA   sing N N 101 
ASN   C   O    doub N N 102 
ASN   C   OXT  sing N N 103 
ASN   CB  CG   sing N N 104 
ASN   CB  HB2  sing N N 105 
ASN   CB  HB3  sing N N 106 
ASN   CG  OD1  doub N N 107 
ASN   CG  ND2  sing N N 108 
ASN   ND2 HD21 sing N N 109 
ASN   ND2 HD22 sing N N 110 
ASN   OXT HXT  sing N N 111 
ASP   N   CA   sing N N 112 
ASP   N   H    sing N N 113 
ASP   N   H2   sing N N 114 
ASP   CA  C    sing N N 115 
ASP   CA  CB   sing N N 116 
ASP   CA  HA   sing N N 117 
ASP   C   O    doub N N 118 
ASP   C   OXT  sing N N 119 
ASP   CB  CG   sing N N 120 
ASP   CB  HB2  sing N N 121 
ASP   CB  HB3  sing N N 122 
ASP   CG  OD1  doub N N 123 
ASP   CG  OD2  sing N N 124 
ASP   OD2 HD2  sing N N 125 
ASP   OXT HXT  sing N N 126 
CYS   N   CA   sing N N 127 
CYS   N   H    sing N N 128 
CYS   N   H2   sing N N 129 
CYS   CA  C    sing N N 130 
CYS   CA  CB   sing N N 131 
CYS   CA  HA   sing N N 132 
CYS   C   O    doub N N 133 
CYS   C   OXT  sing N N 134 
CYS   CB  SG   sing N N 135 
CYS   CB  HB2  sing N N 136 
CYS   CB  HB3  sing N N 137 
CYS   SG  HG   sing N N 138 
CYS   OXT HXT  sing N N 139 
DMS   S   O    doub N N 140 
DMS   S   C1   sing N N 141 
DMS   S   C2   sing N N 142 
DMS   C1  H11  sing N N 143 
DMS   C1  H12  sing N N 144 
DMS   C1  H13  sing N N 145 
DMS   C2  H21  sing N N 146 
DMS   C2  H22  sing N N 147 
DMS   C2  H23  sing N N 148 
GLN   N   CA   sing N N 149 
GLN   N   H    sing N N 150 
GLN   N   H2   sing N N 151 
GLN   CA  C    sing N N 152 
GLN   CA  CB   sing N N 153 
GLN   CA  HA   sing N N 154 
GLN   C   O    doub N N 155 
GLN   C   OXT  sing N N 156 
GLN   CB  CG   sing N N 157 
GLN   CB  HB2  sing N N 158 
GLN   CB  HB3  sing N N 159 
GLN   CG  CD   sing N N 160 
GLN   CG  HG2  sing N N 161 
GLN   CG  HG3  sing N N 162 
GLN   CD  OE1  doub N N 163 
GLN   CD  NE2  sing N N 164 
GLN   NE2 HE21 sing N N 165 
GLN   NE2 HE22 sing N N 166 
GLN   OXT HXT  sing N N 167 
GLU   N   CA   sing N N 168 
GLU   N   H    sing N N 169 
GLU   N   H2   sing N N 170 
GLU   CA  C    sing N N 171 
GLU   CA  CB   sing N N 172 
GLU   CA  HA   sing N N 173 
GLU   C   O    doub N N 174 
GLU   C   OXT  sing N N 175 
GLU   CB  CG   sing N N 176 
GLU   CB  HB2  sing N N 177 
GLU   CB  HB3  sing N N 178 
GLU   CG  CD   sing N N 179 
GLU   CG  HG2  sing N N 180 
GLU   CG  HG3  sing N N 181 
GLU   CD  OE1  doub N N 182 
GLU   CD  OE2  sing N N 183 
GLU   OE2 HE2  sing N N 184 
GLU   OXT HXT  sing N N 185 
GLY   N   CA   sing N N 186 
GLY   N   H    sing N N 187 
GLY   N   H2   sing N N 188 
GLY   CA  C    sing N N 189 
GLY   CA  HA2  sing N N 190 
GLY   CA  HA3  sing N N 191 
GLY   C   O    doub N N 192 
GLY   C   OXT  sing N N 193 
GLY   OXT HXT  sing N N 194 
HIS   N   CA   sing N N 195 
HIS   N   H    sing N N 196 
HIS   N   H2   sing N N 197 
HIS   CA  C    sing N N 198 
HIS   CA  CB   sing N N 199 
HIS   CA  HA   sing N N 200 
HIS   C   O    doub N N 201 
HIS   C   OXT  sing N N 202 
HIS   CB  CG   sing N N 203 
HIS   CB  HB2  sing N N 204 
HIS   CB  HB3  sing N N 205 
HIS   CG  ND1  sing Y N 206 
HIS   CG  CD2  doub Y N 207 
HIS   ND1 CE1  doub Y N 208 
HIS   ND1 HD1  sing N N 209 
HIS   CD2 NE2  sing Y N 210 
HIS   CD2 HD2  sing N N 211 
HIS   CE1 NE2  sing Y N 212 
HIS   CE1 HE1  sing N N 213 
HIS   NE2 HE2  sing N N 214 
HIS   OXT HXT  sing N N 215 
HOH   O   H1   sing N N 216 
HOH   O   H2   sing N N 217 
ILE   N   CA   sing N N 218 
ILE   N   H    sing N N 219 
ILE   N   H2   sing N N 220 
ILE   CA  C    sing N N 221 
ILE   CA  CB   sing N N 222 
ILE   CA  HA   sing N N 223 
ILE   C   O    doub N N 224 
ILE   C   OXT  sing N N 225 
ILE   CB  CG1  sing N N 226 
ILE   CB  CG2  sing N N 227 
ILE   CB  HB   sing N N 228 
ILE   CG1 CD1  sing N N 229 
ILE   CG1 HG12 sing N N 230 
ILE   CG1 HG13 sing N N 231 
ILE   CG2 HG21 sing N N 232 
ILE   CG2 HG22 sing N N 233 
ILE   CG2 HG23 sing N N 234 
ILE   CD1 HD11 sing N N 235 
ILE   CD1 HD12 sing N N 236 
ILE   CD1 HD13 sing N N 237 
ILE   OXT HXT  sing N N 238 
LEU   N   CA   sing N N 239 
LEU   N   H    sing N N 240 
LEU   N   H2   sing N N 241 
LEU   CA  C    sing N N 242 
LEU   CA  CB   sing N N 243 
LEU   CA  HA   sing N N 244 
LEU   C   O    doub N N 245 
LEU   C   OXT  sing N N 246 
LEU   CB  CG   sing N N 247 
LEU   CB  HB2  sing N N 248 
LEU   CB  HB3  sing N N 249 
LEU   CG  CD1  sing N N 250 
LEU   CG  CD2  sing N N 251 
LEU   CG  HG   sing N N 252 
LEU   CD1 HD11 sing N N 253 
LEU   CD1 HD12 sing N N 254 
LEU   CD1 HD13 sing N N 255 
LEU   CD2 HD21 sing N N 256 
LEU   CD2 HD22 sing N N 257 
LEU   CD2 HD23 sing N N 258 
LEU   OXT HXT  sing N N 259 
LYS   N   CA   sing N N 260 
LYS   N   H    sing N N 261 
LYS   N   H2   sing N N 262 
LYS   CA  C    sing N N 263 
LYS   CA  CB   sing N N 264 
LYS   CA  HA   sing N N 265 
LYS   C   O    doub N N 266 
LYS   C   OXT  sing N N 267 
LYS   CB  CG   sing N N 268 
LYS   CB  HB2  sing N N 269 
LYS   CB  HB3  sing N N 270 
LYS   CG  CD   sing N N 271 
LYS   CG  HG2  sing N N 272 
LYS   CG  HG3  sing N N 273 
LYS   CD  CE   sing N N 274 
LYS   CD  HD2  sing N N 275 
LYS   CD  HD3  sing N N 276 
LYS   CE  NZ   sing N N 277 
LYS   CE  HE2  sing N N 278 
LYS   CE  HE3  sing N N 279 
LYS   NZ  HZ1  sing N N 280 
LYS   NZ  HZ2  sing N N 281 
LYS   NZ  HZ3  sing N N 282 
LYS   OXT HXT  sing N N 283 
MET   N   CA   sing N N 284 
MET   N   H    sing N N 285 
MET   N   H2   sing N N 286 
MET   CA  C    sing N N 287 
MET   CA  CB   sing N N 288 
MET   CA  HA   sing N N 289 
MET   C   O    doub N N 290 
MET   C   OXT  sing N N 291 
MET   CB  CG   sing N N 292 
MET   CB  HB2  sing N N 293 
MET   CB  HB3  sing N N 294 
MET   CG  SD   sing N N 295 
MET   CG  HG2  sing N N 296 
MET   CG  HG3  sing N N 297 
MET   SD  CE   sing N N 298 
MET   CE  HE1  sing N N 299 
MET   CE  HE2  sing N N 300 
MET   CE  HE3  sing N N 301 
MET   OXT HXT  sing N N 302 
PHE   N   CA   sing N N 303 
PHE   N   H    sing N N 304 
PHE   N   H2   sing N N 305 
PHE   CA  C    sing N N 306 
PHE   CA  CB   sing N N 307 
PHE   CA  HA   sing N N 308 
PHE   C   O    doub N N 309 
PHE   C   OXT  sing N N 310 
PHE   CB  CG   sing N N 311 
PHE   CB  HB2  sing N N 312 
PHE   CB  HB3  sing N N 313 
PHE   CG  CD1  doub Y N 314 
PHE   CG  CD2  sing Y N 315 
PHE   CD1 CE1  sing Y N 316 
PHE   CD1 HD1  sing N N 317 
PHE   CD2 CE2  doub Y N 318 
PHE   CD2 HD2  sing N N 319 
PHE   CE1 CZ   doub Y N 320 
PHE   CE1 HE1  sing N N 321 
PHE   CE2 CZ   sing Y N 322 
PHE   CE2 HE2  sing N N 323 
PHE   CZ  HZ   sing N N 324 
PHE   OXT HXT  sing N N 325 
PRO   N   CA   sing N N 326 
PRO   N   CD   sing N N 327 
PRO   N   H    sing N N 328 
PRO   CA  C    sing N N 329 
PRO   CA  CB   sing N N 330 
PRO   CA  HA   sing N N 331 
PRO   C   O    doub N N 332 
PRO   C   OXT  sing N N 333 
PRO   CB  CG   sing N N 334 
PRO   CB  HB2  sing N N 335 
PRO   CB  HB3  sing N N 336 
PRO   CG  CD   sing N N 337 
PRO   CG  HG2  sing N N 338 
PRO   CG  HG3  sing N N 339 
PRO   CD  HD2  sing N N 340 
PRO   CD  HD3  sing N N 341 
PRO   OXT HXT  sing N N 342 
SER   N   CA   sing N N 343 
SER   N   H    sing N N 344 
SER   N   H2   sing N N 345 
SER   CA  C    sing N N 346 
SER   CA  CB   sing N N 347 
SER   CA  HA   sing N N 348 
SER   C   O    doub N N 349 
SER   C   OXT  sing N N 350 
SER   CB  OG   sing N N 351 
SER   CB  HB2  sing N N 352 
SER   CB  HB3  sing N N 353 
SER   OG  HG   sing N N 354 
SER   OXT HXT  sing N N 355 
THR   N   CA   sing N N 356 
THR   N   H    sing N N 357 
THR   N   H2   sing N N 358 
THR   CA  C    sing N N 359 
THR   CA  CB   sing N N 360 
THR   CA  HA   sing N N 361 
THR   C   O    doub N N 362 
THR   C   OXT  sing N N 363 
THR   CB  OG1  sing N N 364 
THR   CB  CG2  sing N N 365 
THR   CB  HB   sing N N 366 
THR   OG1 HG1  sing N N 367 
THR   CG2 HG21 sing N N 368 
THR   CG2 HG22 sing N N 369 
THR   CG2 HG23 sing N N 370 
THR   OXT HXT  sing N N 371 
TRP   N   CA   sing N N 372 
TRP   N   H    sing N N 373 
TRP   N   H2   sing N N 374 
TRP   CA  C    sing N N 375 
TRP   CA  CB   sing N N 376 
TRP   CA  HA   sing N N 377 
TRP   C   O    doub N N 378 
TRP   C   OXT  sing N N 379 
TRP   CB  CG   sing N N 380 
TRP   CB  HB2  sing N N 381 
TRP   CB  HB3  sing N N 382 
TRP   CG  CD1  doub Y N 383 
TRP   CG  CD2  sing Y N 384 
TRP   CD1 NE1  sing Y N 385 
TRP   CD1 HD1  sing N N 386 
TRP   CD2 CE2  doub Y N 387 
TRP   CD2 CE3  sing Y N 388 
TRP   NE1 CE2  sing Y N 389 
TRP   NE1 HE1  sing N N 390 
TRP   CE2 CZ2  sing Y N 391 
TRP   CE3 CZ3  doub Y N 392 
TRP   CE3 HE3  sing N N 393 
TRP   CZ2 CH2  doub Y N 394 
TRP   CZ2 HZ2  sing N N 395 
TRP   CZ3 CH2  sing Y N 396 
TRP   CZ3 HZ3  sing N N 397 
TRP   CH2 HH2  sing N N 398 
TRP   OXT HXT  sing N N 399 
TYR   N   CA   sing N N 400 
TYR   N   H    sing N N 401 
TYR   N   H2   sing N N 402 
TYR   CA  C    sing N N 403 
TYR   CA  CB   sing N N 404 
TYR   CA  HA   sing N N 405 
TYR   C   O    doub N N 406 
TYR   C   OXT  sing N N 407 
TYR   CB  CG   sing N N 408 
TYR   CB  HB2  sing N N 409 
TYR   CB  HB3  sing N N 410 
TYR   CG  CD1  doub Y N 411 
TYR   CG  CD2  sing Y N 412 
TYR   CD1 CE1  sing Y N 413 
TYR   CD1 HD1  sing N N 414 
TYR   CD2 CE2  doub Y N 415 
TYR   CD2 HD2  sing N N 416 
TYR   CE1 CZ   doub Y N 417 
TYR   CE1 HE1  sing N N 418 
TYR   CE2 CZ   sing Y N 419 
TYR   CE2 HE2  sing N N 420 
TYR   CZ  OH   sing N N 421 
TYR   OH  HH   sing N N 422 
TYR   OXT HXT  sing N N 423 
VAL   N   CA   sing N N 424 
VAL   N   H    sing N N 425 
VAL   N   H2   sing N N 426 
VAL   CA  C    sing N N 427 
VAL   CA  CB   sing N N 428 
VAL   CA  HA   sing N N 429 
VAL   C   O    doub N N 430 
VAL   C   OXT  sing N N 431 
VAL   CB  CG1  sing N N 432 
VAL   CB  CG2  sing N N 433 
VAL   CB  HB   sing N N 434 
VAL   CG1 HG11 sing N N 435 
VAL   CG1 HG12 sing N N 436 
VAL   CG1 HG13 sing N N 437 
VAL   CG2 HG21 sing N N 438 
VAL   CG2 HG22 sing N N 439 
VAL   CG2 HG23 sing N N 440 
VAL   OXT HXT  sing N N 441 
# 
_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                    7HPH 
_atom_sites.fract_transf_matrix[1][1]   0.023448 
_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]   0.023448 
_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]   0.004610 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 7   ? -22.545 19.148  -7.044  1.00 52.64  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -23.335 17.932  -7.253  1.00 52.89  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -23.166 17.319  -8.653  1.00 51.99  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -23.426 17.961  -9.680  1.00 51.61  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -24.828 18.167  -6.924  1.00 55.42  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -25.331 17.404  -5.706  1.00 60.83  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -25.691 18.058  -4.701  1.00 61.82  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.362 16.153  -5.759  1.00 63.08  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.721 16.065  -8.679  1.00 51.45  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.581 15.329  -9.925  1.00 51.29  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.972 15.020  -10.495 1.00 50.92  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.940 14.907  -9.744  1.00 50.86  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.811 14.019  -9.709  1.00 51.80  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.325 14.201  -9.596  1.00 53.89  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.480 12.641  -9.225  1.00 57.34  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.764 13.183  -9.251  1.00 54.62  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -24.065 14.881  -11.827 1.00 50.35  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.321 14.585  -12.506 1.00 49.68  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.156 13.552  -13.649 1.00 48.62  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -24.041 13.305  -14.115 1.00 48.70  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -26.022 15.873  -12.970 1.00 49.69  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.241 16.683  -13.981 1.00 50.75  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.334 17.654  -13.574 1.00 51.48  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.468 16.536  -15.345 1.00 52.05  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.632 18.418  -14.499 1.00 52.37  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.780 17.303  -16.280 1.00 52.75  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.878 18.259  -15.852 1.00 53.48  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -23.182 19.000  -16.775 1.00 54.79  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.265 12.905  -14.058 1.00 47.28  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.235 11.892  -15.113 1.00 46.11  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.981 12.356  -16.385 1.00 46.28  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.910 13.151  -16.276 1.00 46.67  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.708 10.501  -14.606 1.00 45.07  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.213 10.440  -14.365 1.00 44.53  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.931 10.076  -13.379 1.00 45.49  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.737 9.048   -14.173 1.00 44.72  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.540 11.903  -17.582 1.00 45.85  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.143 12.273  -18.880 1.00 46.42  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.141 11.068  -19.811 1.00 46.42  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.076 10.536  -20.087 1.00 46.26  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.345 13.391  -19.575 1.00 48.21  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.514 14.765  -18.962 1.00 52.01  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.791 15.877  -19.696 1.00 56.70  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.973 15.579  -20.597 1.00 54.65  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -26.050 17.058  -19.367 1.00 60.21  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.304 10.668  -20.333 1.00 46.26  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.382 9.500   -21.193 1.00 46.81  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.538 9.653   -22.443 1.00 48.22  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.540 10.724  -23.048 1.00 48.93  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.829 9.156   -21.531 1.00 47.32  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -29.992 7.689   -21.868 1.00 48.85  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.441 7.267   -21.874 1.00 50.52  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.588 5.843   -22.162 1.00 52.83  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.598 5.323   -23.386 1.00 56.06  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.446 6.103   -24.449 1.00 56.46  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.731 4.015   -23.555 1.00 56.10  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.746 8.617   -22.778 1.00 48.27  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.872 8.635   -23.946 1.00 48.66  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.108 7.471   -24.931 1.00 49.82  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.410 7.382   -25.942 1.00 49.99  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.423 8.688   -23.514 1.00 48.45  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.104 6.622   -24.667 1.00 50.68  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.421 5.522   -25.570 1.00 52.15  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.147 4.323   -24.992 1.00 53.60  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.467 4.282   -23.800 1.00 53.76  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.395 3.324   -25.861 1.00 54.39  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.056 2.060   -25.540 1.00 55.71  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.049 0.947   -25.375 1.00 56.98  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -27.078 0.910   -26.125 1.00 57.32  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -29.957 1.643   -26.697 1.00 57.21  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.347 2.176   -26.598 1.00 61.84  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.514 3.279   -26.056 1.00 62.48  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.269 1.512   -27.100 1.00 64.49  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.325 -0.029  -24.494 1.00 57.37  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.431 -1.182  -24.342 1.00 58.16  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.796 -2.243  -25.401 1.00 58.72  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.704 -3.044  -25.177 1.00 58.41  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.512 -1.778  -22.929 1.00 58.70  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -27.444 -0.695  -21.827 1.00 59.70  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.441 -2.817  -22.758 1.00 59.17  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -28.128 -1.115  -20.488 1.00 60.81  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -27.098 -2.223  -26.549 0.50 58.97  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -27.116 -2.234  -26.560 0.50 59.08  ? 60  THR   A N   1 
ATOM   84   C CA  A THR   A 1 17  ? -27.330 -3.151  -27.658 0.50 59.80  ? 60  THR   A CA  1 
ATOM   85   C CA  B THR   A 1 17  ? -27.399 -3.183  -27.643 0.50 60.01  ? 60  THR   A CA  1 
ATOM   86   C C   A THR   A 1 17  ? -26.022 -3.649  -28.282 0.50 60.75  ? 60  THR   A C   1 
ATOM   87   C C   B THR   A 1 17  ? -26.107 -3.618  -28.372 0.50 60.91  ? 60  THR   A C   1 
ATOM   88   O O   A THR   A 1 17  ? -25.065 -2.885  -28.396 0.50 60.73  ? 60  THR   A O   1 
ATOM   89   O O   B THR   A 1 17  ? -25.216 -2.798  -28.579 0.50 60.97  ? 60  THR   A O   1 
ATOM   90   C CB  A THR   A 1 17  ? -28.138 -2.461  -28.774 0.50 60.76  ? 60  THR   A CB  1 
ATOM   91   C CB  B THR   A 1 17  ? -28.480 -2.596  -28.584 0.50 61.21  ? 60  THR   A CB  1 
ATOM   92   O OG1 A THR   A 1 17  ? -27.539 -1.201  -29.095 0.50 61.38  ? 60  THR   A OG1 1 
ATOM   93   O OG1 B THR   A 1 17  ? -29.724 -2.531  -27.883 0.50 62.16  ? 60  THR   A OG1 1 
ATOM   94   C CG2 A THR   A 1 17  ? -29.612 -2.292  -28.433 0.50 61.23  ? 60  THR   A CG2 1 
ATOM   95   C CG2 B THR   A 1 17  ? -28.679 -3.414  -29.850 0.50 61.55  ? 60  THR   A CG2 1 
ATOM   96   N N   . TRP   A 1 18  ? -25.996 -4.908  -28.732 1.00 61.52  ? 61  TRP   A N   1 
ATOM   97   C CA  . TRP   A 1 18  ? -24.838 -5.436  -29.447 1.00 64.00  ? 61  TRP   A CA  1 
ATOM   98   C C   . TRP   A 1 18  ? -25.030 -4.972  -30.916 1.00 67.73  ? 61  TRP   A C   1 
ATOM   99   O O   . TRP   A 1 18  ? -26.117 -5.141  -31.489 1.00 67.77  ? 61  TRP   A O   1 
ATOM   100  C CB  . TRP   A 1 18  ? -24.796 -6.978  -29.350 1.00 63.62  ? 61  TRP   A CB  1 
ATOM   101  C CG  . TRP   A 1 18  ? -23.798 -7.678  -30.242 1.00 64.27  ? 61  TRP   A CG  1 
ATOM   102  C CD1 . TRP   A 1 18  ? -23.982 -8.058  -31.546 1.00 65.05  ? 61  TRP   A CD1 1 
ATOM   103  C CD2 . TRP   A 1 18  ? -22.522 -8.212  -29.850 1.00 64.37  ? 61  TRP   A CD2 1 
ATOM   104  N NE1 . TRP   A 1 18  ? -22.877 -8.742  -32.002 1.00 65.10  ? 61  TRP   A NE1 1 
ATOM   105  C CE2 . TRP   A 1 18  ? -21.967 -8.852  -30.982 1.00 64.93  ? 61  TRP   A CE2 1 
ATOM   106  C CE3 . TRP   A 1 18  ? -21.763 -8.150  -28.674 1.00 64.80  ? 61  TRP   A CE3 1 
ATOM   107  C CZ2 . TRP   A 1 18  ? -20.717 -9.462  -30.951 1.00 65.44  ? 61  TRP   A CZ2 1 
ATOM   108  C CZ3 . TRP   A 1 18  ? -20.529 -8.767  -28.644 1.00 65.55  ? 61  TRP   A CZ3 1 
ATOM   109  C CH2 . TRP   A 1 18  ? -20.013 -9.401  -29.776 1.00 65.66  ? 61  TRP   A CH2 1 
ATOM   110  N N   . GLU   A 1 19  ? -23.997 -4.353  -31.506 1.00 70.31  ? 62  GLU   A N   1 
ATOM   111  C CA  . GLU   A 1 19  ? -24.095 -3.879  -32.874 1.00 73.22  ? 62  GLU   A CA  1 
ATOM   112  C C   . GLU   A 1 19  ? -23.358 -4.782  -33.806 1.00 76.14  ? 62  GLU   A C   1 
ATOM   113  O O   . GLU   A 1 19  ? -22.156 -4.968  -33.655 1.00 76.23  ? 62  GLU   A O   1 
ATOM   114  C CB  . GLU   A 1 19  ? -23.569 -2.449  -33.020 1.00 76.28  ? 62  GLU   A CB  1 
ATOM   115  C CG  . GLU   A 1 19  ? -24.316 -1.431  -32.170 1.00 83.16  ? 62  GLU   A CG  1 
ATOM   116  C CD  . GLU   A 1 19  ? -25.780 -1.201  -32.496 1.00 90.94  ? 62  GLU   A CD  1 
ATOM   117  O OE1 . GLU   A 1 19  ? -26.116 -1.013  -33.691 1.00 92.97  ? 62  GLU   A OE1 1 
ATOM   118  O OE2 . GLU   A 1 19  ? -26.590 -1.180  -31.541 1.00 92.93  ? 62  GLU   A OE2 1 
ATOM   119  N N   . LYS   A 1 20  ? -24.076 -5.322  -34.800 1.00 78.28  ? 63  LYS   A N   1 
ATOM   120  C CA  . LYS   A 1 20  ? -23.497 -6.146  -35.856 1.00 80.75  ? 63  LYS   A CA  1 
ATOM   121  C C   . LYS   A 1 20  ? -22.603 -5.237  -36.698 1.00 82.27  ? 63  LYS   A C   1 
ATOM   122  O O   . LYS   A 1 20  ? -22.887 -4.038  -36.807 1.00 82.73  ? 63  LYS   A O   1 
ATOM   123  C CB  . LYS   A 1 20  ? -24.615 -6.702  -36.766 1.00 84.01  ? 63  LYS   A CB  1 
ATOM   124  C CG  . LYS   A 1 20  ? -25.166 -8.062  -36.350 1.00 89.73  ? 63  LYS   A CG  1 
ATOM   125  C CD  . LYS   A 1 20  ? -24.915 -9.128  -37.423 1.00 95.04  ? 63  LYS   A CD  1 
ATOM   126  C CE  . LYS   A 1 20  ? -25.492 -10.468 -37.033 1.00 99.61  ? 63  LYS   A CE  1 
ATOM   127  N NZ  . LYS   A 1 20  ? -26.961 -10.383 -36.805 1.00 102.50 ? 63  LYS   A NZ  1 
ATOM   128  N N   . ASP   A 1 21  ? -21.533 -5.785  -37.299 1.00 82.81  ? 64  ASP   A N   1 
ATOM   129  C CA  . ASP   A 1 21  ? -20.631 -4.984  -38.133 1.00 83.96  ? 64  ASP   A CA  1 
ATOM   130  C C   . ASP   A 1 21  ? -20.039 -3.798  -37.328 1.00 84.30  ? 64  ASP   A C   1 
ATOM   131  O O   . ASP   A 1 21  ? -20.297 -2.635  -37.649 1.00 84.83  ? 64  ASP   A O   1 
ATOM   132  C CB  . ASP   A 1 21  ? -21.343 -4.465  -39.413 1.00 86.50  ? 64  ASP   A CB  1 
ATOM   133  C CG  . ASP   A 1 21  ? -22.014 -5.503  -40.316 1.00 92.77  ? 64  ASP   A CG  1 
ATOM   134  O OD1 . ASP   A 1 21  ? -21.425 -6.598  -40.511 1.00 93.56  ? 64  ASP   A OD1 1 
ATOM   135  O OD2 . ASP   A 1 21  ? -23.102 -5.192  -40.880 1.00 95.19  ? 64  ASP   A OD2 1 
ATOM   136  N N   . ALA   A 1 22  ? -19.334 -4.096  -36.237 1.00 83.68  ? 65  ALA   A N   1 
ATOM   137  C CA  . ALA   A 1 22  ? -18.710 -3.060  -35.413 1.00 83.49  ? 65  ALA   A CA  1 
ATOM   138  C C   . ALA   A 1 22  ? -17.174 -3.061  -35.626 1.00 83.39  ? 65  ALA   A C   1 
ATOM   139  O O   . ALA   A 1 22  ? -16.628 -4.014  -36.193 1.00 83.23  ? 65  ALA   A O   1 
ATOM   140  C CB  . ALA   A 1 22  ? -19.057 -3.278  -33.949 1.00 83.33  ? 65  ALA   A CB  1 
ATOM   141  N N   . GLU   A 1 23  ? -16.485 -1.982  -35.219 1.00 83.12  ? 66  GLU   A N   1 
ATOM   142  C CA  . GLU   A 1 23  ? -15.037 -1.889  -35.399 1.00 83.10  ? 66  GLU   A CA  1 
ATOM   143  C C   . GLU   A 1 23  ? -14.297 -2.863  -34.461 1.00 82.66  ? 66  GLU   A C   1 
ATOM   144  O O   . GLU   A 1 23  ? -14.413 -2.751  -33.240 1.00 82.64  ? 66  GLU   A O   1 
ATOM   145  C CB  . GLU   A 1 23  ? -14.577 -0.443  -35.181 1.00 85.42  ? 66  GLU   A CB  1 
ATOM   146  C CG  . GLU   A 1 23  ? -13.157 -0.194  -35.641 1.00 90.33  ? 66  GLU   A CG  1 
ATOM   147  C CD  . GLU   A 1 23  ? -12.277 0.396   -34.560 1.00 96.76  ? 66  GLU   A CD  1 
ATOM   148  O OE1 . GLU   A 1 23  ? -12.773 1.266   -33.804 1.00 98.14  ? 66  GLU   A OE1 1 
ATOM   149  O OE2 . GLU   A 1 23  ? -11.096 -0.015  -34.466 1.00 97.98  ? 66  GLU   A OE2 1 
ATOM   150  N N   . VAL   A 1 24  ? -13.569 -3.838  -35.034 1.00 82.01  ? 67  VAL   A N   1 
ATOM   151  C CA  . VAL   A 1 24  ? -12.858 -4.855  -34.255 1.00 81.84  ? 67  VAL   A CA  1 
ATOM   152  C C   . VAL   A 1 24  ? -11.389 -4.518  -34.023 1.00 81.85  ? 67  VAL   A C   1 
ATOM   153  O O   . VAL   A 1 24  ? -10.594 -4.552  -34.956 1.00 82.18  ? 67  VAL   A O   1 
ATOM   154  C CB  . VAL   A 1 24  ? -13.007 -6.279  -34.846 1.00 82.16  ? 67  VAL   A CB  1 
ATOM   155  C CG1 . VAL   A 1 24  ? -12.474 -7.323  -33.875 1.00 82.67  ? 67  VAL   A CG1 1 
ATOM   156  C CG2 . VAL   A 1 24  ? -14.454 -6.582  -35.218 1.00 82.47  ? 67  VAL   A CG2 1 
ATOM   157  N N   . THR   A 1 25  ? -11.021 -4.226  -32.776 1.00 81.36  ? 68  THR   A N   1 
ATOM   158  C CA  . THR   A 1 25  ? -9.639  -3.921  -32.417 1.00 81.46  ? 68  THR   A CA  1 
ATOM   159  C C   . THR   A 1 25  ? -9.341  -4.388  -31.003 1.00 81.35  ? 68  THR   A C   1 
ATOM   160  O O   . THR   A 1 25  ? -10.258 -4.530  -30.194 1.00 81.61  ? 68  THR   A O   1 
ATOM   161  C CB  . THR   A 1 25  ? -9.338  -2.425  -32.566 1.00 82.89  ? 68  THR   A CB  1 
ATOM   162  O OG1 . THR   A 1 25  ? -7.930  -2.243  -32.473 1.00 84.21  ? 68  THR   A OG1 1 
ATOM   163  C CG2 . THR   A 1 25  ? -9.996  -1.590  -31.491 1.00 83.10  ? 68  THR   A CG2 1 
ATOM   164  N N   . GLY   A 1 26  ? -8.068  -4.628  -30.706 1.00 80.85  ? 69  GLY   A N   1 
ATOM   165  C CA  . GLY   A 1 26  ? -7.671  -5.041  -29.364 1.00 80.70  ? 69  GLY   A CA  1 
ATOM   166  C C   . GLY   A 1 26  ? -7.194  -6.470  -29.243 1.00 80.01  ? 69  GLY   A C   1 
ATOM   167  O O   . GLY   A 1 26  ? -7.877  -7.406  -29.666 1.00 79.66  ? 69  GLY   A O   1 
ATOM   168  N N   . ASN   A 1 27  ? -6.023  -6.637  -28.623 1.00 79.61  ? 70  ASN   A N   1 
ATOM   169  C CA  . ASN   A 1 27  ? -5.396  -7.948  -28.416 1.00 79.23  ? 70  ASN   A CA  1 
ATOM   170  C C   . ASN   A 1 27  ? -5.916  -8.665  -27.128 1.00 76.99  ? 70  ASN   A C   1 
ATOM   171  O O   . ASN   A 1 27  ? -6.685  -8.069  -26.373 1.00 77.00  ? 70  ASN   A O   1 
ATOM   172  C CB  . ASN   A 1 27  ? -3.852  -7.822  -28.454 1.00 81.18  ? 70  ASN   A CB  1 
ATOM   173  C CG  . ASN   A 1 27  ? -3.245  -7.279  -27.177 1.00 85.50  ? 70  ASN   A CG  1 
ATOM   174  O OD1 . ASN   A 1 27  ? -3.559  -6.169  -26.725 1.00 86.89  ? 70  ASN   A OD1 1 
ATOM   175  N ND2 . ASN   A 1 27  ? -2.360  -8.053  -26.563 1.00 86.34  ? 70  ASN   A ND2 1 
ATOM   176  N N   . SER   A 1 28  ? -5.539  -9.951  -26.924 1.00 74.94  ? 71  SER   A N   1 
ATOM   177  C CA  . SER   A 1 28  ? -5.963  -10.767 -25.781 1.00 73.77  ? 71  SER   A CA  1 
ATOM   178  C C   . SER   A 1 28  ? -4.770  -11.158 -24.907 1.00 72.44  ? 71  SER   A C   1 
ATOM   179  O O   . SER   A 1 28  ? -4.213  -12.248 -25.072 1.00 73.22  ? 71  SER   A O   1 
ATOM   180  C CB  . SER   A 1 28  ? -6.662  -12.035 -26.265 1.00 74.57  ? 71  SER   A CB  1 
ATOM   181  O OG  . SER   A 1 28  ? -7.867  -11.756 -26.949 1.00 76.30  ? 71  SER   A OG  1 
ATOM   182  N N   . PRO   A 1 29  ? -4.356  -10.301 -23.965 1.00 70.38  ? 72  PRO   A N   1 
ATOM   183  C CA  . PRO   A 1 29  ? -3.172  -10.626 -23.159 1.00 69.11  ? 72  PRO   A CA  1 
ATOM   184  C C   . PRO   A 1 29  ? -3.460  -11.374 -21.861 1.00 67.52  ? 72  PRO   A C   1 
ATOM   185  O O   . PRO   A 1 29  ? -4.455  -11.088 -21.209 1.00 67.44  ? 72  PRO   A O   1 
ATOM   186  C CB  . PRO   A 1 29  ? -2.531  -9.255  -22.910 1.00 69.93  ? 72  PRO   A CB  1 
ATOM   187  C CG  . PRO   A 1 29  ? -3.625  -8.228  -23.208 1.00 70.80  ? 72  PRO   A CG  1 
ATOM   188  C CD  . PRO   A 1 29  ? -4.863  -8.954  -23.655 1.00 69.64  ? 72  PRO   A CD  1 
ATOM   189  N N   . ARG   A 1 30  ? -2.590  -12.329 -21.479 1.00 66.18  ? 73  ARG   A N   1 
ATOM   190  C CA  . ARG   A 1 30  ? -2.744  -13.041 -20.203 1.00 65.51  ? 73  ARG   A CA  1 
ATOM   191  C C   . ARG   A 1 30  ? -1.718  -12.500 -19.221 1.00 63.81  ? 73  ARG   A C   1 
ATOM   192  O O   . ARG   A 1 30  ? -0.518  -12.636 -19.444 1.00 63.60  ? 73  ARG   A O   1 
ATOM   193  C CB  . ARG   A 1 30  ? -2.621  -14.558 -20.359 1.00 67.26  ? 73  ARG   A CB  1 
ATOM   194  C CG  . ARG   A 1 30  ? -3.733  -15.126 -21.217 1.00 71.19  ? 73  ARG   A CG  1 
ATOM   195  C CD  . ARG   A 1 30  ? -3.812  -16.636 -21.152 1.00 74.65  ? 73  ARG   A CD  1 
ATOM   196  N NE  . ARG   A 1 30  ? -4.255  -17.178 -22.434 1.00 77.80  ? 73  ARG   A NE  1 
ATOM   197  C CZ  . ARG   A 1 30  ? -4.303  -18.473 -22.730 1.00 81.71  ? 73  ARG   A CZ  1 
ATOM   198  N NH1 . ARG   A 1 30  ? -3.938  -19.382 -21.833 1.00 81.60  ? 73  ARG   A NH1 1 
ATOM   199  N NH2 . ARG   A 1 30  ? -4.684  -18.868 -23.936 1.00 82.80  ? 73  ARG   A NH2 1 
ATOM   200  N N   . LEU   A 1 31  ? -2.189  -11.831 -18.168 1.00 62.49  ? 74  LEU   A N   1 
ATOM   201  C CA  . LEU   A 1 31  ? -1.314  -11.182 -17.202 1.00 61.99  ? 74  LEU   A CA  1 
ATOM   202  C C   . LEU   A 1 31  ? -1.382  -11.782 -15.792 1.00 60.98  ? 74  LEU   A C   1 
ATOM   203  O O   . LEU   A 1 31  ? -2.398  -12.348 -15.407 1.00 61.20  ? 74  LEU   A O   1 
ATOM   204  C CB  . LEU   A 1 31  ? -1.667  -9.684  -17.135 1.00 62.19  ? 74  LEU   A CB  1 
ATOM   205  C CG  . LEU   A 1 31  ? -1.574  -8.934  -18.454 1.00 63.63  ? 74  LEU   A CG  1 
ATOM   206  C CD1 . LEU   A 1 31  ? -2.432  -7.696  -18.448 1.00 63.95  ? 74  LEU   A CD1 1 
ATOM   207  C CD2 . LEU   A 1 31  ? -0.140  -8.603  -18.788 1.00 64.48  ? 74  LEU   A CD2 1 
ATOM   208  N N   . ASP   A 1 32  ? -0.302  -11.632 -15.020 1.00 59.48  ? 75  ASP   A N   1 
ATOM   209  C CA  . ASP   A 1 32  ? -0.266  -12.066 -13.630 1.00 58.58  ? 75  ASP   A CA  1 
ATOM   210  C C   . ASP   A 1 32  ? -0.406  -10.788 -12.770 1.00 56.40  ? 75  ASP   A C   1 
ATOM   211  O O   . ASP   A 1 32  ? 0.562   -10.039 -12.656 1.00 56.47  ? 75  ASP   A O   1 
ATOM   212  C CB  . ASP   A 1 32  ? 1.077   -12.763 -13.330 1.00 61.05  ? 75  ASP   A CB  1 
ATOM   213  C CG  . ASP   A 1 32  ? 1.053   -14.283 -13.388 1.00 66.31  ? 75  ASP   A CG  1 
ATOM   214  O OD1 . ASP   A 1 32  ? 0.349   -14.902 -12.556 1.00 66.50  ? 75  ASP   A OD1 1 
ATOM   215  O OD2 . ASP   A 1 32  ? 1.767   -14.855 -14.242 1.00 69.38  ? 75  ASP   A OD2 1 
ATOM   216  N N   . VAL   A 1 33  ? -1.609  -10.500 -12.218 1.00 54.32  ? 76  VAL   A N   1 
ATOM   217  C CA  . VAL   A 1 33  ? -1.826  -9.280  -11.414 1.00 52.88  ? 76  VAL   A CA  1 
ATOM   218  C C   . VAL   A 1 33  ? -2.194  -9.577  -9.917  1.00 50.94  ? 76  VAL   A C   1 
ATOM   219  O O   . VAL   A 1 33  ? -2.390  -10.739 -9.553  1.00 50.64  ? 76  VAL   A O   1 
ATOM   220  C CB  . VAL   A 1 33  ? -2.858  -8.326  -12.084 1.00 53.42  ? 76  VAL   A CB  1 
ATOM   221  C CG1 . VAL   A 1 33  ? -2.521  -8.079  -13.549 1.00 53.93  ? 76  VAL   A CG1 1 
ATOM   222  C CG2 . VAL   A 1 33  ? -4.271  -8.864  -11.938 1.00 53.82  ? 76  VAL   A CG2 1 
ATOM   223  N N   . ALA   A 1 34  ? -2.236  -8.526  -9.053  1.00 49.33  ? 77  ALA   A N   1 
ATOM   224  C CA  . ALA   A 1 34  ? -2.610  -8.636  -7.636  1.00 48.30  ? 77  ALA   A CA  1 
ATOM   225  C C   . ALA   A 1 34  ? -3.527  -7.485  -7.247  1.00 47.01  ? 77  ALA   A C   1 
ATOM   226  O O   . ALA   A 1 34  ? -3.237  -6.326  -7.534  1.00 47.33  ? 77  ALA   A O   1 
ATOM   227  C CB  . ALA   A 1 34  ? -1.386  -8.650  -6.737  1.00 48.15  ? 77  ALA   A CB  1 
ATOM   228  N N   . LEU   A 1 35  ? -4.640  -7.807  -6.598  1.00 45.27  ? 78  LEU   A N   1 
ATOM   229  C CA  . LEU   A 1 35  ? -5.615  -6.813  -6.193  1.00 43.84  ? 78  LEU   A CA  1 
ATOM   230  C C   . LEU   A 1 35  ? -5.446  -6.474  -4.697  1.00 43.56  ? 78  LEU   A C   1 
ATOM   231  O O   . LEU   A 1 35  ? -5.355  -7.369  -3.845  1.00 43.73  ? 78  LEU   A O   1 
ATOM   232  C CB  . LEU   A 1 35  ? -7.020  -7.340  -6.500  1.00 42.85  ? 78  LEU   A CB  1 
ATOM   233  C CG  . LEU   A 1 35  ? -8.152  -6.392  -6.220  1.00 42.83  ? 78  LEU   A CG  1 
ATOM   234  C CD1 . LEU   A 1 35  ? -8.063  -5.171  -7.102  1.00 42.91  ? 78  LEU   A CD1 1 
ATOM   235  C CD2 . LEU   A 1 35  ? -9.480  -7.095  -6.360  1.00 42.86  ? 78  LEU   A CD2 1 
ATOM   236  N N   . ASP   A 1 36  ? -5.360  -5.183  -4.391  1.00 42.62  ? 79  ASP   A N   1 
ATOM   237  C CA  . ASP   A 1 36  ? -5.173  -4.747  -3.027  1.00 42.14  ? 79  ASP   A CA  1 
ATOM   238  C C   . ASP   A 1 36  ? -6.509  -4.294  -2.375  1.00 42.28  ? 79  ASP   A C   1 
ATOM   239  O O   . ASP   A 1 36  ? -7.533  -4.159  -3.060  1.00 41.82  ? 79  ASP   A O   1 
ATOM   240  C CB  . ASP   A 1 36  ? -4.037  -3.692  -2.951  1.00 42.95  ? 79  ASP   A CB  1 
ATOM   241  C CG  . ASP   A 1 36  ? -4.320  -2.300  -3.488  1.00 46.60  ? 79  ASP   A CG  1 
ATOM   242  O OD1 . ASP   A 1 36  ? -5.487  -2.006  -3.799  1.00 46.86  ? 79  ASP   A OD1 1 
ATOM   243  O OD2 . ASP   A 1 36  ? -3.374  -1.501  -3.581  1.00 48.94  ? 79  ASP   A OD2 1 
ATOM   244  N N   . GLU   A 1 37  ? -6.486  -4.062  -1.050  1.00 42.59  ? 80  GLU   A N   1 
ATOM   245  C CA  . GLU   A 1 37  ? -7.631  -3.585  -0.279  1.00 43.54  ? 80  GLU   A CA  1 
ATOM   246  C C   . GLU   A 1 37  ? -8.181  -2.281  -0.848  1.00 44.55  ? 80  GLU   A C   1 
ATOM   247  O O   . GLU   A 1 37  ? -9.382  -2.056  -0.776  1.00 45.17  ? 80  GLU   A O   1 
ATOM   248  C CB  . GLU   A 1 37  ? -7.213  -3.368  1.169   1.00 45.42  ? 80  GLU   A CB  1 
ATOM   249  C CG  . GLU   A 1 37  ? -8.288  -3.634  2.202   1.00 48.79  ? 80  GLU   A CG  1 
ATOM   250  C CD  . GLU   A 1 37  ? -7.828  -3.233  3.593   1.00 51.49  ? 80  GLU   A CD  1 
ATOM   251  O OE1 . GLU   A 1 37  ? -7.604  -2.019  3.814   1.00 50.74  ? 80  GLU   A OE1 1 
ATOM   252  O OE2 . GLU   A 1 37  ? -7.665  -4.132  4.450   1.00 52.84  ? 80  GLU   A OE2 1 
ATOM   253  N N   . SER   A 1 38  ? -7.323  -1.433  -1.441  1.00 44.20  ? 81  SER   A N   1 
ATOM   254  C CA  . SER   A 1 38  ? -7.754  -0.182  -2.062  1.00 43.91  ? 81  SER   A CA  1 
ATOM   255  C C   . SER   A 1 38  ? -8.407  -0.365  -3.444  1.00 42.98  ? 81  SER   A C   1 
ATOM   256  O O   . SER   A 1 38  ? -8.950  0.590   -3.981  1.00 42.80  ? 81  SER   A O   1 
ATOM   257  C CB  . SER   A 1 38  ? -6.583  0.790   -2.153  1.00 45.95  ? 81  SER   A CB  1 
ATOM   258  O OG  . SER   A 1 38  ? -6.040  1.020   -0.860  1.00 49.19  ? 81  SER   A OG  1 
ATOM   259  N N   . GLY   A 1 39  ? -8.348  -1.565  -4.012  1.00 42.50  ? 82  GLY   A N   1 
ATOM   260  C CA  . GLY   A 1 39  ? -8.928  -1.849  -5.325  1.00 42.78  ? 82  GLY   A CA  1 
ATOM   261  C C   . GLY   A 1 39  ? -8.005  -1.617  -6.518  1.00 42.40  ? 82  GLY   A C   1 
ATOM   262  O O   . GLY   A 1 39  ? -8.440  -1.699  -7.660  1.00 42.10  ? 82  GLY   A O   1 
ATOM   263  N N   . ASP   A 1 40  ? -6.728  -1.320  -6.260  1.00 42.34  ? 83  ASP   A N   1 
ATOM   264  C CA  . ASP   A 1 40  ? -5.700  -1.030  -7.243  1.00 42.67  ? 83  ASP   A CA  1 
ATOM   265  C C   . ASP   A 1 40  ? -4.992  -2.302  -7.703  1.00 43.31  ? 83  ASP   A C   1 
ATOM   266  O O   . ASP   A 1 40  ? -4.336  -2.966  -6.893  1.00 43.40  ? 83  ASP   A O   1 
ATOM   267  C CB  . ASP   A 1 40  ? -4.663  -0.085  -6.618  1.00 44.50  ? 83  ASP   A CB  1 
ATOM   268  C CG  . ASP   A 1 40  ? -5.134  1.342   -6.418  1.00 50.12  ? 83  ASP   A CG  1 
ATOM   269  O OD1 . ASP   A 1 40  ? -5.659  1.925   -7.371  1.00 51.19  ? 83  ASP   A OD1 1 
ATOM   270  O OD2 . ASP   A 1 40  ? -4.939  1.887   -5.306  1.00 53.42  ? 83  ASP   A OD2 1 
ATOM   271  N N   . PHE   A 1 41  ? -5.079  -2.611  -9.016  1.00 43.55  ? 84  PHE   A N   1 
ATOM   272  C CA  . PHE   A 1 41  ? -4.432  -3.764  -9.645  1.00 44.18  ? 84  PHE   A CA  1 
ATOM   273  C C   . PHE   A 1 41  ? -2.981  -3.445  -9.913  1.00 46.12  ? 84  PHE   A C   1 
ATOM   274  O O   . PHE   A 1 41  ? -2.674  -2.422  -10.507 1.00 46.05  ? 84  PHE   A O   1 
ATOM   275  C CB  . PHE   A 1 41  ? -5.111  -4.128  -10.972 1.00 43.25  ? 84  PHE   A CB  1 
ATOM   276  C CG  . PHE   A 1 41  ? -6.405  -4.904  -10.863 1.00 42.80  ? 84  PHE   A CG  1 
ATOM   277  C CD1 . PHE   A 1 41  ? -6.396  -6.272  -10.648 1.00 42.92  ? 84  PHE   A CD1 1 
ATOM   278  C CD2 . PHE   A 1 41  ? -7.629  -4.271  -11.020 1.00 42.73  ? 84  PHE   A CD2 1 
ATOM   279  C CE1 . PHE   A 1 41  ? -7.584  -6.985  -10.570 1.00 43.07  ? 84  PHE   A CE1 1 
ATOM   280  C CE2 . PHE   A 1 41  ? -8.812  -4.990  -10.949 1.00 42.97  ? 84  PHE   A CE2 1 
ATOM   281  C CZ  . PHE   A 1 41  ? -8.782  -6.341  -10.727 1.00 42.71  ? 84  PHE   A CZ  1 
ATOM   282  N N   . SER   A 1 42  ? -2.086  -4.324  -9.483  1.00 48.03  ? 85  SER   A N   1 
ATOM   283  C CA  . SER   A 1 42  ? -0.645  -4.153  -9.655  1.00 50.36  ? 85  SER   A CA  1 
ATOM   284  C C   . SER   A 1 42  ? -0.091  -5.314  -10.451 1.00 52.54  ? 85  SER   A C   1 
ATOM   285  O O   . SER   A 1 42  ? -0.437  -6.456  -10.161 1.00 52.91  ? 85  SER   A O   1 
ATOM   286  C CB  . SER   A 1 42  ? 0.064   -4.068  -8.300  1.00 52.19  ? 85  SER   A CB  1 
ATOM   287  O OG  . SER   A 1 42  ? -0.573  -4.744  -7.222  1.00 54.62  ? 85  SER   A OG  1 
ATOM   288  N N   . LEU   A 1 43  ? 0.750   -5.038  -11.460 1.00 53.81  ? 86  LEU   A N   1 
ATOM   289  C CA  . LEU   A 1 43  ? 1.340   -6.100  -12.273 1.00 55.42  ? 86  LEU   A CA  1 
ATOM   290  C C   . LEU   A 1 43  ? 2.396   -6.863  -11.491 1.00 57.04  ? 86  LEU   A C   1 
ATOM   291  O O   . LEU   A 1 43  ? 3.389   -6.283  -11.053 1.00 57.14  ? 86  LEU   A O   1 
ATOM   292  C CB  . LEU   A 1 43  ? 1.969   -5.529  -13.541 1.00 55.82  ? 86  LEU   A CB  1 
ATOM   293  C CG  . LEU   A 1 43  ? 1.273   -5.880  -14.834 1.00 57.89  ? 86  LEU   A CG  1 
ATOM   294  C CD1 . LEU   A 1 43  ? 1.927   -5.194  -16.000 1.00 58.43  ? 86  LEU   A CD1 1 
ATOM   295  C CD2 . LEU   A 1 43  ? 1.260   -7.372  -15.060 1.00 59.05  ? 86  LEU   A CD2 1 
ATOM   296  N N   . VAL   A 1 44  ? 2.174   -8.164  -11.311 1.00 58.09  ? 87  VAL   A N   1 
ATOM   297  C CA  . VAL   A 1 44  ? 3.076   -9.065  -10.596 1.00 59.54  ? 87  VAL   A CA  1 
ATOM   298  C C   . VAL   A 1 44  ? 3.997   -9.743  -11.615 1.00 61.11  ? 87  VAL   A C   1 
ATOM   299  O O   . VAL   A 1 44  ? 3.525   -10.166 -12.675 1.00 61.35  ? 87  VAL   A O   1 
ATOM   300  C CB  . VAL   A 1 44  ? 2.246   -10.089 -9.787  1.00 60.07  ? 87  VAL   A CB  1 
ATOM   301  C CG1 . VAL   A 1 44  ? 3.083   -11.291 -9.364  1.00 60.62  ? 87  VAL   A CG1 1 
ATOM   302  C CG2 . VAL   A 1 44  ? 1.612   -9.421  -8.581  1.00 60.60  ? 87  VAL   A CG2 1 
ATOM   303  N N   . GLU   A 1 45  ? 5.309   -9.806  -11.328 1.00 61.87  ? 88  GLU   A N   1 
ATOM   304  C CA  . GLU   A 1 45  ? 6.251   -10.429 -12.261 1.00 63.43  ? 88  GLU   A CA  1 
ATOM   305  C C   . GLU   A 1 45  ? 7.210   -11.428 -11.544 1.00 64.51  ? 88  GLU   A C   1 
ATOM   306  O O   . GLU   A 1 45  ? 8.090   -12.042 -12.164 1.00 64.71  ? 88  GLU   A O   1 
ATOM   307  C CB  . GLU   A 1 45  ? 7.033   -9.354  -13.047 1.00 65.97  ? 88  GLU   A CB  1 
ATOM   308  C CG  . GLU   A 1 45  ? 6.172   -8.319  -13.762 1.00 70.57  ? 88  GLU   A CG  1 
ATOM   309  C CD  . GLU   A 1 45  ? 5.542   -8.762  -15.070 1.00 76.06  ? 88  GLU   A CD  1 
ATOM   310  O OE1 . GLU   A 1 45  ? 6.281   -8.872  -16.076 1.00 77.54  ? 88  GLU   A OE1 1 
ATOM   311  O OE2 . GLU   A 1 45  ? 4.310   -8.989  -15.092 1.00 77.30  ? 88  GLU   A OE2 1 
ATOM   312  N N   . GLY   B 2 7   ? -35.674 11.387  -10.998 1.00 62.96  ? 16  GLY   B N   1 
ATOM   313  C CA  . GLY   B 2 7   ? -35.954 11.906  -12.329 1.00 63.60  ? 16  GLY   B CA  1 
ATOM   314  C C   . GLY   B 2 7   ? -36.067 10.813  -13.377 1.00 64.12  ? 16  GLY   B C   1 
ATOM   315  O O   . GLY   B 2 7   ? -36.831 9.856   -13.192 1.00 64.55  ? 16  GLY   B O   1 
ATOM   316  N N   . GLU   B 2 8   ? -35.309 10.940  -14.494 1.00 63.58  ? 17  GLU   B N   1 
ATOM   317  C CA  . GLU   B 2 8   ? -35.346 9.929   -15.548 1.00 63.35  ? 17  GLU   B CA  1 
ATOM   318  C C   . GLU   B 2 8   ? -34.655 8.621   -15.148 1.00 62.40  ? 17  GLU   B C   1 
ATOM   319  O O   . GLU   B 2 8   ? -33.467 8.602   -14.825 1.00 62.37  ? 17  GLU   B O   1 
ATOM   320  C CB  . GLU   B 2 8   ? -34.800 10.450  -16.877 1.00 65.88  ? 17  GLU   B CB  1 
ATOM   321  C CG  . GLU   B 2 8   ? -35.106 9.502   -18.026 1.00 71.11  ? 17  GLU   B CG  1 
ATOM   322  C CD  . GLU   B 2 8   ? -34.034 9.443   -19.095 1.00 78.20  ? 17  GLU   B CD  1 
ATOM   323  O OE1 . GLU   B 2 8   ? -32.861 9.743   -18.773 1.00 79.24  ? 17  GLU   B OE1 1 
ATOM   324  O OE2 . GLU   B 2 8   ? -34.368 9.105   -20.256 1.00 80.81  ? 17  GLU   B OE2 1 
ATOM   325  N N   A THR   B 2 9   ? -35.415 7.526   -15.170 0.50 61.82  ? 18  THR   B N   1 
ATOM   326  N N   B THR   B 2 9   ? -35.416 7.526   -15.170 0.50 61.82  ? 18  THR   B N   1 
ATOM   327  C CA  A THR   B 2 9   ? -34.913 6.205   -14.804 0.50 61.57  ? 18  THR   B CA  1 
ATOM   328  C CA  B THR   B 2 9   ? -34.914 6.205   -14.804 0.50 61.57  ? 18  THR   B CA  1 
ATOM   329  C C   A THR   B 2 9   ? -35.006 5.221   -15.966 0.50 60.74  ? 18  THR   B C   1 
ATOM   330  C C   B THR   B 2 9   ? -35.007 5.220   -15.966 0.50 60.73  ? 18  THR   B C   1 
ATOM   331  O O   A THR   B 2 9   ? -35.174 4.026   -15.734 0.50 60.95  ? 18  THR   B O   1 
ATOM   332  O O   B THR   B 2 9   ? -35.174 4.026   -15.734 0.50 60.94  ? 18  THR   B O   1 
ATOM   333  C CB  A THR   B 2 9   ? -35.664 5.672   -13.569 0.50 63.07  ? 18  THR   B CB  1 
ATOM   334  C CB  B THR   B 2 9   ? -35.666 5.672   -13.570 0.50 63.05  ? 18  THR   B CB  1 
ATOM   335  O OG1 A THR   B 2 9   ? -37.075 5.854   -13.754 0.50 64.30  ? 18  THR   B OG1 1 
ATOM   336  O OG1 B THR   B 2 9   ? -37.076 5.855   -13.755 0.50 64.29  ? 18  THR   B OG1 1 
ATOM   337  C CG2 A THR   B 2 9   ? -35.211 6.340   -12.280 0.50 63.43  ? 18  THR   B CG2 1 
ATOM   338  C CG2 B THR   B 2 9   ? -35.213 6.338   -12.279 0.50 63.43  ? 18  THR   B CG2 1 
ATOM   339  N N   . THR   B 2 10  ? -34.892 5.706   -17.207 1.00 59.72  ? 19  THR   B N   1 
ATOM   340  C CA  . THR   B 2 10  ? -34.977 4.847   -18.386 1.00 58.43  ? 19  THR   B CA  1 
ATOM   341  C C   . THR   B 2 10  ? -33.723 3.964   -18.540 1.00 56.29  ? 19  THR   B C   1 
ATOM   342  O O   . THR   B 2 10  ? -32.600 4.455   -18.426 1.00 56.33  ? 19  THR   B O   1 
ATOM   343  C CB  . THR   B 2 10  ? -35.265 5.712   -19.632 1.00 60.36  ? 19  THR   B CB  1 
ATOM   344  O OG1 . THR   B 2 10  ? -36.464 6.473   -19.418 1.00 62.21  ? 19  THR   B OG1 1 
ATOM   345  C CG2 . THR   B 2 10  ? -35.382 4.894   -20.915 1.00 60.32  ? 19  THR   B CG2 1 
ATOM   346  N N   . ASP   B 2 11  ? -33.902 2.662   -18.808 1.00 54.16  ? 20  ASP   B N   1 
ATOM   347  C CA  . ASP   B 2 11  ? -32.783 1.739   -18.998 1.00 52.76  ? 20  ASP   B CA  1 
ATOM   348  C C   . ASP   B 2 11  ? -31.781 2.251   -20.051 1.00 50.71  ? 20  ASP   B C   1 
ATOM   349  O O   . ASP   B 2 11  ? -32.199 2.940   -20.983 1.00 50.47  ? 20  ASP   B O   1 
ATOM   350  C CB  . ASP   B 2 11  ? -33.314 0.354   -19.405 1.00 54.76  ? 20  ASP   B CB  1 
ATOM   351  C CG  . ASP   B 2 11  ? -33.530 -0.585  -18.239 1.00 60.59  ? 20  ASP   B CG  1 
ATOM   352  O OD1 . ASP   B 2 11  ? -34.141 -0.155  -17.236 1.00 61.27  ? 20  ASP   B OD1 1 
ATOM   353  O OD2 . ASP   B 2 11  ? -33.083 -1.752  -18.325 1.00 63.24  ? 20  ASP   B OD2 1 
ATOM   354  N N   . GLY   B 2 12  ? -30.487 1.960   -19.876 1.00 48.95  ? 21  GLY   B N   1 
ATOM   355  C CA  . GLY   B 2 12  ? -29.480 2.400   -20.839 1.00 47.60  ? 21  GLY   B CA  1 
ATOM   356  C C   . GLY   B 2 12  ? -28.144 2.811   -20.257 1.00 45.75  ? 21  GLY   B C   1 
ATOM   357  O O   . GLY   B 2 12  ? -27.847 2.494   -19.116 1.00 45.39  ? 21  GLY   B O   1 
ATOM   358  N N   . VAL   B 2 13  ? -27.324 3.520   -21.048 1.00 44.69  ? 22  VAL   B N   1 
ATOM   359  C CA  . VAL   B 2 13  ? -25.979 3.963   -20.652 1.00 44.01  ? 22  VAL   B CA  1 
ATOM   360  C C   . VAL   B 2 13  ? -25.951 5.483   -20.450 1.00 43.54  ? 22  VAL   B C   1 
ATOM   361  O O   . VAL   B 2 13  ? -26.570 6.223   -21.209 1.00 43.10  ? 22  VAL   B O   1 
ATOM   362  C CB  . VAL   B 2 13  ? -24.868 3.431   -21.613 1.00 44.32  ? 22  VAL   B CB  1 
ATOM   363  C CG1 . VAL   B 2 13  ? -25.040 3.947   -23.051 1.00 44.73  ? 22  VAL   B CG1 1 
ATOM   364  C CG2 . VAL   B 2 13  ? -23.470 3.718   -21.078 1.00 44.34  ? 22  VAL   B CG2 1 
ATOM   365  N N   . TYR   B 2 14  ? -25.325 5.934   -19.354 1.00 43.66  ? 23  TYR   B N   1 
ATOM   366  C CA  . TYR   B 2 14  ? -25.321 7.343   -18.965 1.00 43.88  ? 23  TYR   B CA  1 
ATOM   367  C C   . TYR   B 2 14  ? -23.940 7.934   -18.744 1.00 44.22  ? 23  TYR   B C   1 
ATOM   368  O O   . TYR   B 2 14  ? -22.998 7.212   -18.447 1.00 44.57  ? 23  TYR   B O   1 
ATOM   369  C CB  . TYR   B 2 14  ? -26.147 7.516   -17.684 1.00 43.48  ? 23  TYR   B CB  1 
ATOM   370  C CG  . TYR   B 2 14  ? -27.628 7.339   -17.902 1.00 43.67  ? 23  TYR   B CG  1 
ATOM   371  C CD1 . TYR   B 2 14  ? -28.169 6.087   -18.155 1.00 44.21  ? 23  TYR   B CD1 1 
ATOM   372  C CD2 . TYR   B 2 14  ? -28.500 8.409   -17.775 1.00 44.43  ? 23  TYR   B CD2 1 
ATOM   373  C CE1 . TYR   B 2 14  ? -29.526 5.920   -18.376 1.00 45.16  ? 23  TYR   B CE1 1 
ATOM   374  C CE2 . TYR   B 2 14  ? -29.863 8.252   -17.972 1.00 45.40  ? 23  TYR   B CE2 1 
ATOM   375  C CZ  . TYR   B 2 14  ? -30.370 7.007   -18.284 1.00 46.38  ? 23  TYR   B CZ  1 
ATOM   376  O OH  . TYR   B 2 14  ? -31.716 6.837   -18.484 1.00 48.44  ? 23  TYR   B OH  1 
ATOM   377  N N   . ARG   B 2 15  ? -23.837 9.257   -18.835 1.00 44.07  ? 24  ARG   B N   1 
ATOM   378  C CA  . ARG   B 2 15  ? -22.599 9.981   -18.599 1.00 44.48  ? 24  ARG   B CA  1 
ATOM   379  C C   . ARG   B 2 15  ? -22.665 10.558  -17.190 1.00 44.55  ? 24  ARG   B C   1 
ATOM   380  O O   . ARG   B 2 15  ? -23.664 11.184  -16.858 1.00 44.55  ? 24  ARG   B O   1 
ATOM   381  C CB  . ARG   B 2 15  ? -22.470 11.169  -19.577 1.00 45.74  ? 24  ARG   B CB  1 
ATOM   382  C CG  . ARG   B 2 15  ? -22.373 10.843  -21.070 1.00 48.28  ? 24  ARG   B CG  1 
ATOM   383  C CD  . ARG   B 2 15  ? -22.004 12.127  -21.810 1.00 51.51  ? 24  ARG   B CD  1 
ATOM   384  N NE  . ARG   B 2 15  ? -22.130 12.014  -23.260 1.00 54.88  ? 24  ARG   B NE  1 
ATOM   385  C CZ  . ARG   B 2 15  ? -21.150 11.627  -24.072 1.00 57.05  ? 24  ARG   B CZ  1 
ATOM   386  N NH1 . ARG   B 2 15  ? -19.951 11.317  -23.582 1.00 56.53  ? 24  ARG   B NH1 1 
ATOM   387  N NH2 . ARG   B 2 15  ? -21.363 11.534  -25.378 1.00 56.07  ? 24  ARG   B NH2 1 
ATOM   388  N N   . VAL   B 2 16  ? -21.592 10.412  -16.392 1.00 44.40  ? 25  VAL   B N   1 
ATOM   389  C CA  . VAL   B 2 16  ? -21.487 10.967  -15.029 1.00 44.86  ? 25  VAL   B CA  1 
ATOM   390  C C   . VAL   B 2 16  ? -20.679 12.281  -15.168 1.00 45.05  ? 25  VAL   B C   1 
ATOM   391  O O   . VAL   B 2 16  ? -19.532 12.241  -15.624 1.00 45.05  ? 25  VAL   B O   1 
ATOM   392  C CB  . VAL   B 2 16  ? -20.827 9.962   -14.036 1.00 45.48  ? 25  VAL   B CB  1 
ATOM   393  C CG1 . VAL   B 2 16  ? -21.023 10.396  -12.586 1.00 45.82  ? 25  VAL   B CG1 1 
ATOM   394  C CG2 . VAL   B 2 16  ? -21.361 8.548   -14.238 1.00 45.99  ? 25  VAL   B CG2 1 
ATOM   395  N N   . MET   B 2 17  ? -21.311 13.443  -14.878 1.00 44.92  ? 26  MET   B N   1 
ATOM   396  C CA  . MET   B 2 17  ? -20.720 14.765  -15.115 1.00 45.58  ? 26  MET   B CA  1 
ATOM   397  C C   . MET   B 2 17  ? -20.553 15.608  -13.884 1.00 47.73  ? 26  MET   B C   1 
ATOM   398  O O   . MET   B 2 17  ? -21.313 15.451  -12.943 1.00 48.21  ? 26  MET   B O   1 
ATOM   399  C CB  . MET   B 2 17  ? -21.620 15.570  -16.071 1.00 44.86  ? 26  MET   B CB  1 
ATOM   400  C CG  . MET   B 2 17  ? -21.984 14.869  -17.353 1.00 44.49  ? 26  MET   B CG  1 
ATOM   401  S SD  . MET   B 2 17  ? -20.687 14.921  -18.604 1.00 40.35  ? 26  MET   B SD  1 
ATOM   402  C CE  . MET   B 2 17  ? -20.426 16.624  -18.762 1.00 34.17  ? 26  MET   B CE  1 
ATOM   403  N N   . THR   B 2 18  ? -19.632 16.582  -13.919 1.00 49.32  ? 27  THR   B N   1 
ATOM   404  C CA  . THR   B 2 18  ? -19.468 17.506  -12.800 1.00 51.51  ? 27  THR   B CA  1 
ATOM   405  C C   . THR   B 2 18  ? -19.360 18.995  -13.240 1.00 54.31  ? 27  THR   B C   1 
ATOM   406  O O   . THR   B 2 18  ? -18.701 19.336  -14.235 1.00 54.33  ? 27  THR   B O   1 
ATOM   407  C CB  . THR   B 2 18  ? -18.321 17.092  -11.895 1.00 52.19  ? 27  THR   B CB  1 
ATOM   408  O OG1 . THR   B 2 18  ? -18.486 17.764  -10.653 1.00 53.50  ? 27  THR   B OG1 1 
ATOM   409  C CG2 . THR   B 2 18  ? -16.970 17.433  -12.472 1.00 52.35  ? 27  THR   B CG2 1 
ATOM   410  N N   . ARG   B 2 19  ? -20.038 19.882  -12.499 1.00 55.95  ? 28  ARG   B N   1 
ATOM   411  C CA  . ARG   B 2 19  ? -19.959 21.325  -12.770 1.00 57.60  ? 28  ARG   B CA  1 
ATOM   412  C C   . ARG   B 2 19  ? -18.954 22.045  -11.794 1.00 58.25  ? 28  ARG   B C   1 
ATOM   413  O O   . ARG   B 2 19  ? -18.817 23.271  -11.820 1.00 58.30  ? 28  ARG   B O   1 
ATOM   414  C CB  . ARG   B 2 19  ? -21.371 21.956  -12.753 1.00 59.65  ? 28  ARG   B CB  1 
ATOM   415  C CG  . ARG   B 2 19  ? -22.167 21.693  -14.039 1.00 64.09  ? 28  ARG   B CG  1 
ATOM   416  C CD  . ARG   B 2 19  ? -23.666 21.991  -13.911 1.00 68.69  ? 28  ARG   B CD  1 
ATOM   417  N NE  . ARG   B 2 19  ? -24.348 22.012  -15.217 1.00 72.18  ? 28  ARG   B NE  1 
ATOM   418  C CZ  . ARG   B 2 19  ? -25.631 21.698  -15.403 1.00 74.13  ? 28  ARG   B CZ  1 
ATOM   419  N NH1 . ARG   B 2 19  ? -26.386 21.318  -14.377 1.00 73.90  ? 28  ARG   B NH1 1 
ATOM   420  N NH2 . ARG   B 2 19  ? -26.161 21.739  -16.618 1.00 73.65  ? 28  ARG   B NH2 1 
ATOM   421  N N   . ARG   B 2 20  ? -18.203 21.246  -11.005 1.00 58.55  ? 29  ARG   B N   1 
ATOM   422  C CA  . ARG   B 2 20  ? -17.246 21.621  -9.967  1.00 59.41  ? 29  ARG   B CA  1 
ATOM   423  C C   . ARG   B 2 20  ? -15.931 22.244  -10.495 1.00 59.52  ? 29  ARG   B C   1 
ATOM   424  O O   . ARG   B 2 20  ? -15.266 22.991  -9.766  1.00 59.71  ? 29  ARG   B O   1 
ATOM   425  C CB  . ARG   B 2 20  ? -16.982 20.377  -9.106  1.00 61.13  ? 29  ARG   B CB  1 
ATOM   426  C CG  . ARG   B 2 20  ? -16.303 20.594  -7.767  1.00 64.67  ? 29  ARG   B CG  1 
ATOM   427  C CD  . ARG   B 2 20  ? -15.948 19.243  -7.159  1.00 68.51  ? 29  ARG   B CD  1 
ATOM   428  N NE  . ARG   B 2 20  ? -15.080 18.452  -8.041  1.00 71.47  ? 29  ARG   B NE  1 
ATOM   429  C CZ  . ARG   B 2 20  ? -13.833 18.099  -7.746  1.00 73.81  ? 29  ARG   B CZ  1 
ATOM   430  N NH1 . ARG   B 2 20  ? -13.303 18.422  -6.572  1.00 74.09  ? 29  ARG   B NH1 1 
ATOM   431  N NH2 . ARG   B 2 20  ? -13.115 17.397  -8.613  1.00 73.30  ? 29  ARG   B NH2 1 
ATOM   432  N N   . LEU   B 2 21  ? -15.563 21.956  -11.749 1.00 59.08  ? 30  LEU   B N   1 
ATOM   433  C CA  . LEU   B 2 21  ? -14.342 22.528  -12.329 1.00 59.16  ? 30  LEU   B CA  1 
ATOM   434  C C   . LEU   B 2 21  ? -14.694 23.514  -13.470 1.00 58.79  ? 30  LEU   B C   1 
ATOM   435  O O   . LEU   B 2 21  ? -15.803 24.056  -13.482 1.00 58.68  ? 30  LEU   B O   1 
ATOM   436  C CB  . LEU   B 2 21  ? -13.356 21.408  -12.785 1.00 59.41  ? 30  LEU   B CB  1 
ATOM   437  C CG  . LEU   B 2 21  ? -12.468 20.663  -11.755 1.00 60.76  ? 30  LEU   B CG  1 
ATOM   438  C CD1 . LEU   B 2 21  ? -12.411 21.344  -10.364 1.00 61.29  ? 30  LEU   B CD1 1 
ATOM   439  C CD2 . LEU   B 2 21  ? -12.828 19.189  -11.679 1.00 61.16  ? 30  LEU   B CD2 1 
ATOM   440  N N   . LEU   B 2 22  ? -13.741 23.781  -14.388 1.00 58.44  ? 31  LEU   B N   1 
ATOM   441  C CA  . LEU   B 2 22  ? -13.918 24.658  -15.544 1.00 58.47  ? 31  LEU   B CA  1 
ATOM   442  C C   . LEU   B 2 22  ? -14.763 23.895  -16.543 1.00 58.24  ? 31  LEU   B C   1 
ATOM   443  O O   . LEU   B 2 22  ? -14.402 22.781  -16.912 1.00 58.71  ? 31  LEU   B O   1 
ATOM   444  C CB  . LEU   B 2 22  ? -12.549 24.947  -16.163 1.00 58.54  ? 31  LEU   B CB  1 
ATOM   445  C CG  . LEU   B 2 22  ? -12.566 25.774  -17.411 1.00 59.77  ? 31  LEU   B CG  1 
ATOM   446  C CD1 . LEU   B 2 22  ? -12.159 27.188  -17.103 1.00 60.43  ? 31  LEU   B CD1 1 
ATOM   447  C CD2 . LEU   B 2 22  ? -11.684 25.158  -18.484 1.00 60.22  ? 31  LEU   B CD2 1 
ATOM   448  N N   . GLY   B 2 23  ? -15.895 24.459  -16.932 1.00 57.51  ? 32  GLY   B N   1 
ATOM   449  C CA  . GLY   B 2 23  ? -16.808 23.777  -17.838 1.00 57.50  ? 32  GLY   B CA  1 
ATOM   450  C C   . GLY   B 2 23  ? -17.484 22.582  -17.177 1.00 56.96  ? 32  GLY   B C   1 
ATOM   451  O O   . GLY   B 2 23  ? -17.453 22.444  -15.952 1.00 57.06  ? 32  GLY   B O   1 
ATOM   452  N N   . SER   B 2 24  ? -18.113 21.712  -17.986 1.00 56.02  ? 33  SER   B N   1 
ATOM   453  C CA  . SER   B 2 24  ? -18.786 20.511  -17.494 1.00 55.28  ? 33  SER   B CA  1 
ATOM   454  C C   . SER   B 2 24  ? -17.890 19.332  -17.835 1.00 54.54  ? 33  SER   B C   1 
ATOM   455  O O   . SER   B 2 24  ? -17.879 18.885  -18.982 1.00 55.28  ? 33  SER   B O   1 
ATOM   456  C CB  . SER   B 2 24  ? -20.137 20.335  -18.183 1.00 55.91  ? 33  SER   B CB  1 
ATOM   457  O OG  . SER   B 2 24  ? -20.987 21.449  -17.991 1.00 57.29  ? 33  SER   B OG  1 
ATOM   458  N N   . THR   B 2 25  ? -17.106 18.860  -16.874 1.00 53.07  ? 34  THR   B N   1 
ATOM   459  C CA  . THR   B 2 25  ? -16.156 17.760  -17.089 1.00 52.18  ? 34  THR   B CA  1 
ATOM   460  C C   . THR   B 2 25  ? -16.837 16.377  -16.916 1.00 50.60  ? 34  THR   B C   1 
ATOM   461  O O   . THR   B 2 25  ? -17.636 16.222  -15.990 1.00 51.16  ? 34  THR   B O   1 
ATOM   462  C CB  . THR   B 2 25  ? -14.960 17.953  -16.120 1.00 53.32  ? 34  THR   B CB  1 
ATOM   463  O OG1 . THR   B 2 25  ? -14.220 19.139  -16.456 1.00 53.65  ? 34  THR   B OG1 1 
ATOM   464  C CG2 . THR   B 2 25  ? -14.040 16.758  -16.088 1.00 54.09  ? 34  THR   B CG2 1 
ATOM   465  N N   . GLN   B 2 26  ? -16.537 15.384  -17.788 1.00 48.39  ? 35  GLN   B N   1 
ATOM   466  C CA  . GLN   B 2 26  ? -17.127 14.036  -17.666 1.00 47.07  ? 35  GLN   B CA  1 
ATOM   467  C C   . GLN   B 2 26  ? -16.211 13.120  -16.854 1.00 46.33  ? 35  GLN   B C   1 
ATOM   468  O O   . GLN   B 2 26  ? -15.218 12.604  -17.377 1.00 46.78  ? 35  GLN   B O   1 
ATOM   469  C CB  . GLN   B 2 26  ? -17.396 13.400  -19.042 1.00 47.29  ? 35  GLN   B CB  1 
ATOM   470  C CG  . GLN   B 2 26  ? -18.369 12.232  -18.978 1.00 48.36  ? 35  GLN   B CG  1 
ATOM   471  C CD  . GLN   B 2 26  ? -18.194 11.309  -20.143 1.00 51.56  ? 35  GLN   B CD  1 
ATOM   472  O OE1 . GLN   B 2 26  ? -19.053 11.168  -21.010 1.00 53.06  ? 35  GLN   B OE1 1 
ATOM   473  N NE2 . GLN   B 2 26  ? -17.066 10.659  -20.199 1.00 52.37  ? 35  GLN   B NE2 1 
ATOM   474  N N   . VAL   B 2 27  ? -16.556 12.903  -15.587 1.00 44.96  ? 36  VAL   B N   1 
ATOM   475  C CA  . VAL   B 2 27  ? -15.756 12.112  -14.653 1.00 43.95  ? 36  VAL   B CA  1 
ATOM   476  C C   . VAL   B 2 27  ? -15.841 10.574  -14.840 1.00 42.53  ? 36  VAL   B C   1 
ATOM   477  O O   . VAL   B 2 27  ? -14.986 9.833   -14.340 1.00 42.61  ? 36  VAL   B O   1 
ATOM   478  C CB  . VAL   B 2 27  ? -16.162 12.524  -13.224 1.00 44.48  ? 36  VAL   B CB  1 
ATOM   479  C CG1 . VAL   B 2 27  ? -15.878 14.000  -12.999 1.00 45.15  ? 36  VAL   B CG1 1 
ATOM   480  C CG2 . VAL   B 2 27  ? -17.631 12.235  -12.976 1.00 44.63  ? 36  VAL   B CG2 1 
ATOM   481  N N   . GLY   B 2 28  ? -16.876 10.118  -15.535 1.00 40.76  ? 37  GLY   B N   1 
ATOM   482  C CA  . GLY   B 2 28  ? -17.124 8.699   -15.736 1.00 39.34  ? 37  GLY   B CA  1 
ATOM   483  C C   . GLY   B 2 28  ? -18.415 8.414   -16.476 1.00 37.53  ? 37  GLY   B C   1 
ATOM   484  O O   . GLY   B 2 28  ? -19.062 9.330   -16.987 1.00 37.40  ? 37  GLY   B O   1 
ATOM   485  N N   . VAL   B 2 29  ? -18.786 7.121   -16.544 1.00 35.85  ? 38  VAL   B N   1 
ATOM   486  C CA  . VAL   B 2 29  ? -19.941 6.558   -17.261 1.00 34.31  ? 38  VAL   B CA  1 
ATOM   487  C C   . VAL   B 2 29  ? -20.654 5.505   -16.342 1.00 32.64  ? 38  VAL   B C   1 
ATOM   488  O O   . VAL   B 2 29  ? -20.037 4.950   -15.437 1.00 31.04  ? 38  VAL   B O   1 
ATOM   489  C CB  . VAL   B 2 29  ? -19.426 5.941   -18.622 1.00 34.55  ? 38  VAL   B CB  1 
ATOM   490  C CG1 . VAL   B 2 29  ? -20.488 5.118   -19.355 1.00 34.93  ? 38  VAL   B CG1 1 
ATOM   491  C CG2 . VAL   B 2 29  ? -18.841 7.008   -19.544 1.00 34.32  ? 38  VAL   B CG2 1 
ATOM   492  N N   . GLY   B 2 30  ? -21.943 5.266   -16.571 1.00 32.66  ? 39  GLY   B N   1 
ATOM   493  C CA  . GLY   B 2 30  ? -22.698 4.284   -15.796 1.00 33.13  ? 39  GLY   B CA  1 
ATOM   494  C C   . GLY   B 2 30  ? -23.799 3.576   -16.572 1.00 33.34  ? 39  GLY   B C   1 
ATOM   495  O O   . GLY   B 2 30  ? -24.076 3.933   -17.719 1.00 32.74  ? 39  GLY   B O   1 
ATOM   496  N N   . VAL   B 2 31  ? -24.439 2.559   -15.951 1.00 33.52  ? 40  VAL   B N   1 
ATOM   497  C CA  . VAL   B 2 31  ? -25.512 1.767   -16.578 1.00 34.29  ? 40  VAL   B CA  1 
ATOM   498  C C   . VAL   B 2 31  ? -26.800 1.762   -15.739 1.00 35.13  ? 40  VAL   B C   1 
ATOM   499  O O   . VAL   B 2 31  ? -26.761 1.417   -14.566 1.00 35.88  ? 40  VAL   B O   1 
ATOM   500  C CB  . VAL   B 2 31  ? -25.052 0.308   -16.836 1.00 34.81  ? 40  VAL   B CB  1 
ATOM   501  C CG1 . VAL   B 2 31  ? -26.191 -0.553  -17.371 1.00 34.93  ? 40  VAL   B CG1 1 
ATOM   502  C CG2 . VAL   B 2 31  ? -23.845 0.256   -17.763 1.00 35.47  ? 40  VAL   B CG2 1 
ATOM   503  N N   . MET   B 2 32  ? -27.936 2.105   -16.334 1.00 34.87  ? 41  MET   B N   1 
ATOM   504  C CA  . MET   B 2 32  ? -29.229 2.038   -15.656 1.00 35.25  ? 41  MET   B CA  1 
ATOM   505  C C   . MET   B 2 32  ? -29.848 0.704   -16.106 1.00 35.75  ? 41  MET   B C   1 
ATOM   506  O O   . MET   B 2 32  ? -29.764 0.361   -17.280 1.00 36.55  ? 41  MET   B O   1 
ATOM   507  C CB  . MET   B 2 32  ? -30.131 3.245   -16.045 1.00 35.68  ? 41  MET   B CB  1 
ATOM   508  C CG  . MET   B 2 32  ? -31.416 3.393   -15.225 1.00 37.79  ? 41  MET   B CG  1 
ATOM   509  S SD  . MET   B 2 32  ? -31.211 4.205   -13.593 1.00 43.83  ? 41  MET   B SD  1 
ATOM   510  C CE  . MET   B 2 32  ? -30.462 5.765   -14.122 1.00 40.41  ? 41  MET   B CE  1 
ATOM   511  N N   . GLN   B 2 33  ? -30.385 -0.076  -15.175 1.00 35.55  ? 42  GLN   B N   1 
ATOM   512  C CA  . GLN   B 2 33  ? -31.043 -1.347  -15.465 1.00 35.97  ? 42  GLN   B CA  1 
ATOM   513  C C   . GLN   B 2 33  ? -31.945 -1.667  -14.281 1.00 36.24  ? 42  GLN   B C   1 
ATOM   514  O O   . GLN   B 2 33  ? -31.471 -1.623  -13.142 1.00 36.53  ? 42  GLN   B O   1 
ATOM   515  C CB  . GLN   B 2 33  ? -30.036 -2.491  -15.705 1.00 37.78  ? 42  GLN   B CB  1 
ATOM   516  C CG  . GLN   B 2 33  ? -30.758 -3.810  -16.015 1.00 41.81  ? 42  GLN   B CG  1 
ATOM   517  C CD  . GLN   B 2 33  ? -29.911 -4.895  -16.623 1.00 45.63  ? 42  GLN   B CD  1 
ATOM   518  O OE1 . GLN   B 2 33  ? -29.924 -6.050  -16.181 1.00 45.98  ? 42  GLN   B OE1 1 
ATOM   519  N NE2 . GLN   B 2 33  ? -29.176 -4.557  -17.669 1.00 47.42  ? 42  GLN   B NE2 1 
ATOM   520  N N   . GLU   B 2 34  ? -33.246 -1.937  -14.537 1.00 35.91  ? 43  GLU   B N   1 
ATOM   521  C CA  . GLU   B 2 34  ? -34.250 -2.209  -13.498 1.00 36.61  ? 43  GLU   B CA  1 
ATOM   522  C C   . GLU   B 2 34  ? -34.323 -1.119  -12.379 1.00 36.32  ? 43  GLU   B C   1 
ATOM   523  O O   . GLU   B 2 34  ? -34.544 -1.436  -11.207 1.00 36.60  ? 43  GLU   B O   1 
ATOM   524  C CB  . GLU   B 2 34  ? -34.080 -3.611  -12.882 1.00 39.73  ? 43  GLU   B CB  1 
ATOM   525  C CG  . GLU   B 2 34  ? -34.182 -4.766  -13.862 1.00 45.49  ? 43  GLU   B CG  1 
ATOM   526  C CD  . GLU   B 2 34  ? -33.330 -5.964  -13.476 1.00 53.26  ? 43  GLU   B CD  1 
ATOM   527  O OE1 . GLU   B 2 34  ? -33.534 -6.517  -12.368 1.00 54.17  ? 43  GLU   B OE1 1 
ATOM   528  O OE2 . GLU   B 2 34  ? -32.449 -6.346  -14.282 1.00 55.69  ? 43  GLU   B OE2 1 
ATOM   529  N N   . GLY   B 2 35  ? -34.121 0.139   -12.758 1.00 35.34  ? 44  GLY   B N   1 
ATOM   530  C CA  . GLY   B 2 35  ? -34.197 1.265   -11.838 1.00 34.93  ? 44  GLY   B CA  1 
ATOM   531  C C   . GLY   B 2 35  ? -32.995 1.433   -10.933 1.00 34.73  ? 44  GLY   B C   1 
ATOM   532  O O   . GLY   B 2 35  ? -33.118 2.025   -9.853  1.00 35.23  ? 44  GLY   B O   1 
ATOM   533  N N   . VAL   B 2 36  ? -31.824 0.876   -11.341 1.00 33.50  ? 45  VAL   B N   1 
ATOM   534  C CA  . VAL   B 2 36  ? -30.577 0.961   -10.561 1.00 32.05  ? 45  VAL   B CA  1 
ATOM   535  C C   . VAL   B 2 36  ? -29.427 1.534   -11.428 1.00 31.08  ? 45  VAL   B C   1 
ATOM   536  O O   . VAL   B 2 36  ? -29.209 1.088   -12.569 1.00 30.56  ? 45  VAL   B O   1 
ATOM   537  C CB  . VAL   B 2 36  ? -30.203 -0.384  -9.852  1.00 31.85  ? 45  VAL   B CB  1 
ATOM   538  C CG1 . VAL   B 2 36  ? -28.846 -0.315  -9.172  1.00 32.15  ? 45  VAL   B CG1 1 
ATOM   539  C CG2 . VAL   B 2 36  ? -31.252 -0.784  -8.841  1.00 31.93  ? 45  VAL   B CG2 1 
ATOM   540  N N   . PHE   B 2 37  ? -28.736 2.566   -10.903 1.00 30.20  ? 46  PHE   B N   1 
ATOM   541  C CA  . PHE   B 2 37  ? -27.604 3.138   -11.608 1.00 30.17  ? 46  PHE   B CA  1 
ATOM   542  C C   . PHE   B 2 37  ? -26.387 2.363   -11.158 1.00 31.09  ? 46  PHE   B C   1 
ATOM   543  O O   . PHE   B 2 37  ? -26.122 2.293   -9.967  1.00 32.16  ? 46  PHE   B O   1 
ATOM   544  C CB  . PHE   B 2 37  ? -27.413 4.604   -11.267 1.00 29.73  ? 46  PHE   B CB  1 
ATOM   545  C CG  . PHE   B 2 37  ? -26.465 5.265   -12.230 1.00 30.04  ? 46  PHE   B CG  1 
ATOM   546  C CD1 . PHE   B 2 37  ? -26.748 5.305   -13.590 1.00 30.96  ? 46  PHE   B CD1 1 
ATOM   547  C CD2 . PHE   B 2 37  ? -25.304 5.869   -11.781 1.00 30.63  ? 46  PHE   B CD2 1 
ATOM   548  C CE1 . PHE   B 2 37  ? -25.889 5.943   -14.479 1.00 31.60  ? 46  PHE   B CE1 1 
ATOM   549  C CE2 . PHE   B 2 37  ? -24.441 6.501   -12.674 1.00 31.33  ? 46  PHE   B CE2 1 
ATOM   550  C CZ  . PHE   B 2 37  ? -24.751 6.551   -14.014 1.00 31.37  ? 46  PHE   B CZ  1 
ATOM   551  N N   . HIS   B 2 38  ? -25.652 1.775   -12.084 1.00 30.59  ? 47  HIS   B N   1 
ATOM   552  C CA  . HIS   B 2 38  ? -24.489 0.971   -11.775 1.00 30.59  ? 47  HIS   B CA  1 
ATOM   553  C C   . HIS   B 2 38  ? -23.265 1.662   -12.307 1.00 30.45  ? 47  HIS   B C   1 
ATOM   554  O O   . HIS   B 2 38  ? -23.173 1.832   -13.499 1.00 29.98  ? 47  HIS   B O   1 
ATOM   555  C CB  . HIS   B 2 38  ? -24.613 -0.396  -12.472 1.00 31.00  ? 47  HIS   B CB  1 
ATOM   556  C CG  . HIS   B 2 38  ? -25.839 -1.173  -12.095 1.00 31.83  ? 47  HIS   B CG  1 
ATOM   557  N ND1 . HIS   B 2 38  ? -27.045 -0.976  -12.741 1.00 33.09  ? 47  HIS   B ND1 1 
ATOM   558  C CD2 . HIS   B 2 38  ? -25.998 -2.142  -11.164 1.00 32.15  ? 47  HIS   B CD2 1 
ATOM   559  C CE1 . HIS   B 2 38  ? -27.895 -1.822  -12.179 1.00 33.10  ? 47  HIS   B CE1 1 
ATOM   560  N NE2 . HIS   B 2 38  ? -27.303 -2.561  -11.248 1.00 32.72  ? 47  HIS   B NE2 1 
ATOM   561  N N   . THR   B 2 39  ? -22.316 2.031   -11.450 1.00 30.63  ? 48  THR   B N   1 
ATOM   562  C CA  . THR   B 2 39  ? -21.070 2.650   -11.907 1.00 31.13  ? 48  THR   B CA  1 
ATOM   563  C C   . THR   B 2 39  ? -19.848 2.118   -11.086 1.00 33.02  ? 48  THR   B C   1 
ATOM   564  O O   . THR   B 2 39  ? -20.015 1.272   -10.197 1.00 33.27  ? 48  THR   B O   1 
ATOM   565  C CB  . THR   B 2 39  ? -21.205 4.192   -11.936 1.00 30.51  ? 48  THR   B CB  1 
ATOM   566  O OG1 . THR   B 2 39  ? -20.185 4.722   -12.775 1.00 29.65  ? 48  THR   B OG1 1 
ATOM   567  C CG2 . THR   B 2 39  ? -21.051 4.807   -10.555 1.00 31.06  ? 48  THR   B CG2 1 
ATOM   568  N N   . MET   B 2 40  ? -18.623 2.576   -11.427 1.00 33.98  ? 49  MET   B N   1 
ATOM   569  C CA  . MET   B 2 40  ? -17.409 2.222   -10.712 1.00 35.16  ? 49  MET   B CA  1 
ATOM   570  C C   . MET   B 2 40  ? -17.245 3.225   -9.563  1.00 36.33  ? 49  MET   B C   1 
ATOM   571  O O   . MET   B 2 40  ? -17.451 4.419   -9.756  1.00 36.79  ? 49  MET   B O   1 
ATOM   572  C CB  . MET   B 2 40  ? -16.215 2.291   -11.663 1.00 36.27  ? 49  MET   B CB  1 
ATOM   573  C CG  . MET   B 2 40  ? -16.383 1.428   -12.910 1.00 38.34  ? 49  MET   B CG  1 
ATOM   574  S SD  . MET   B 2 40  ? -14.916 0.400   -13.227 1.00 40.42  ? 49  MET   B SD  1 
ATOM   575  C CE  . MET   B 2 40  ? -15.093 -0.787  -11.996 1.00 32.18  ? 49  MET   B CE  1 
ATOM   576  N N   . TRP   B 2 41  ? -16.893 2.750   -8.372  1.00 36.79  ? 50  TRP   B N   1 
ATOM   577  C CA  A TRP   B 2 41  ? -16.746 3.612   -7.207  0.50 37.78  ? 50  TRP   B CA  1 
ATOM   578  C CA  B TRP   B 2 41  ? -16.745 3.609   -7.198  0.50 37.49  ? 50  TRP   B CA  1 
ATOM   579  C C   . TRP   B 2 41  ? -15.790 4.785   -7.419  1.00 38.22  ? 50  TRP   B C   1 
ATOM   580  O O   . TRP   B 2 41  ? -16.099 5.894   -6.992  1.00 39.22  ? 50  TRP   B O   1 
ATOM   581  C CB  A TRP   B 2 41  ? -16.351 2.802   -5.972  0.50 37.87  ? 50  TRP   B CB  1 
ATOM   582  C CB  B TRP   B 2 41  ? -16.351 2.797   -5.942  0.50 37.21  ? 50  TRP   B CB  1 
ATOM   583  C CG  A TRP   B 2 41  ? -16.417 3.585   -4.699  0.50 38.66  ? 50  TRP   B CG  1 
ATOM   584  C CG  B TRP   B 2 41  ? -16.216 3.618   -4.687  0.50 37.42  ? 50  TRP   B CG  1 
ATOM   585  C CD1 A TRP   B 2 41  ? -17.506 3.757   -3.900  0.50 39.77  ? 50  TRP   B CD1 1 
ATOM   586  C CD1 B TRP   B 2 41  ? -15.194 4.462   -4.365  0.50 38.10  ? 50  TRP   B CD1 1 
ATOM   587  C CD2 A TRP   B 2 41  ? -15.337 4.276   -4.062  0.50 38.81  ? 50  TRP   B CD2 1 
ATOM   588  C CD2 B TRP   B 2 41  ? -17.088 3.595   -3.549  0.50 37.49  ? 50  TRP   B CD2 1 
ATOM   589  N NE1 A TRP   B 2 41  ? -17.174 4.522   -2.808  0.50 40.09  ? 50  TRP   B NE1 1 
ATOM   590  N NE1 B TRP   B 2 41  ? -15.423 5.033   -3.140  0.50 38.33  ? 50  TRP   B NE1 1 
ATOM   591  C CE2 A TRP   B 2 41  ? -15.847 4.855   -2.884  0.50 39.81  ? 50  TRP   B CE2 1 
ATOM   592  C CE2 B TRP   B 2 41  ? -16.573 4.509   -2.609  0.50 38.12  ? 50  TRP   B CE2 1 
ATOM   593  C CE3 A TRP   B 2 41  ? -13.991 4.477   -4.382  0.50 39.40  ? 50  TRP   B CE3 1 
ATOM   594  C CE3 B TRP   B 2 41  ? -18.277 2.918   -3.244  0.50 38.05  ? 50  TRP   B CE3 1 
ATOM   595  C CZ2 A TRP   B 2 41  ? -15.053 5.602   -2.015  0.50 40.71  ? 50  TRP   B CZ2 1 
ATOM   596  C CZ2 B TRP   B 2 41  ? -17.204 4.762   -1.388  0.50 38.63  ? 50  TRP   B CZ2 1 
ATOM   597  C CZ3 A TRP   B 2 41  ? -13.209 5.221   -3.526  0.50 40.50  ? 50  TRP   B CZ3 1 
ATOM   598  C CZ3 B TRP   B 2 41  ? -18.891 3.161   -2.027  0.50 38.66  ? 50  TRP   B CZ3 1 
ATOM   599  C CH2 A TRP   B 2 41  ? -13.736 5.763   -2.351  0.50 40.88  ? 50  TRP   B CH2 1 
ATOM   600  C CH2 B TRP   B 2 41  ? -18.354 4.069   -1.115  0.50 38.63  ? 50  TRP   B CH2 1 
ATOM   601  N N   . HIS   B 2 42  ? -14.638 4.558   -8.067  1.00 37.53  ? 51  HIS   B N   1 
ATOM   602  C CA  . HIS   B 2 42  ? -13.658 5.624   -8.272  1.00 37.61  ? 51  HIS   B CA  1 
ATOM   603  C C   . HIS   B 2 42  ? -14.164 6.819   -9.096  1.00 38.42  ? 51  HIS   B C   1 
ATOM   604  O O   . HIS   B 2 42  ? -13.442 7.799   -9.248  1.00 39.15  ? 51  HIS   B O   1 
ATOM   605  C CB  . HIS   B 2 42  ? -12.357 5.070   -8.866  1.00 37.69  ? 51  HIS   B CB  1 
ATOM   606  C CG  . HIS   B 2 42  ? -12.422 4.724   -10.329 1.00 39.66  ? 51  HIS   B CG  1 
ATOM   607  N ND1 . HIS   B 2 42  ? -12.245 3.420   -10.775 1.00 41.17  ? 51  HIS   B ND1 1 
ATOM   608  C CD2 . HIS   B 2 42  ? -12.569 5.530   -11.405 1.00 40.46  ? 51  HIS   B CD2 1 
ATOM   609  C CE1 . HIS   B 2 42  ? -12.306 3.479   -12.089 1.00 41.42  ? 51  HIS   B CE1 1 
ATOM   610  N NE2 . HIS   B 2 42  ? -12.510 4.725   -12.512 1.00 41.55  ? 51  HIS   B NE2 1 
ATOM   611  N N   . VAL   B 2 43  ? -15.370 6.732   -9.657  1.00 38.07  ? 52  VAL   B N   1 
ATOM   612  C CA  . VAL   B 2 43  ? -15.933 7.795   -10.484 1.00 37.70  ? 52  VAL   B CA  1 
ATOM   613  C C   . VAL   B 2 43  ? -16.707 8.804   -9.628  1.00 37.51  ? 52  VAL   B C   1 
ATOM   614  O O   . VAL   B 2 43  ? -16.410 9.996   -9.662  1.00 37.19  ? 52  VAL   B O   1 
ATOM   615  C CB  . VAL   B 2 43  ? -16.820 7.164   -11.571 1.00 38.26  ? 52  VAL   B CB  1 
ATOM   616  C CG1 . VAL   B 2 43  ? -17.543 8.237   -12.368 1.00 39.12  ? 52  VAL   B CG1 1 
ATOM   617  C CG2 . VAL   B 2 43  ? -16.014 6.216   -12.465 1.00 38.30  ? 52  VAL   B CG2 1 
ATOM   618  N N   . THR   B 2 44  ? -17.641 8.304   -8.797  1.00 37.45  ? 53  THR   B N   1 
ATOM   619  C CA  . THR   B 2 44  ? -18.483 9.113   -7.925  1.00 37.72  ? 53  THR   B CA  1 
ATOM   620  C C   . THR   B 2 44  ? -17.962 9.232   -6.496  1.00 38.37  ? 53  THR   B C   1 
ATOM   621  O O   . THR   B 2 44  ? -18.485 10.057  -5.746  1.00 38.67  ? 53  THR   B O   1 
ATOM   622  C CB  . THR   B 2 44  ? -19.914 8.546   -7.874  1.00 38.69  ? 53  THR   B CB  1 
ATOM   623  O OG1 . THR   B 2 44  ? -19.970 7.400   -7.013  1.00 39.43  ? 53  THR   B OG1 1 
ATOM   624  C CG2 . THR   B 2 44  ? -20.473 8.192   -9.246  1.00 38.89  ? 53  THR   B CG2 1 
ATOM   625  N N   . LYS   B 2 45  ? -17.020 8.367   -6.089  1.00 38.28  ? 54  LYS   B N   1 
ATOM   626  C CA  . LYS   B 2 45  ? -16.499 8.339   -4.722  1.00 39.10  ? 54  LYS   B CA  1 
ATOM   627  C C   . LYS   B 2 45  ? -17.583 8.046   -3.655  1.00 39.75  ? 54  LYS   B C   1 
ATOM   628  O O   . LYS   B 2 45  ? -17.416 8.408   -2.485  1.00 39.82  ? 54  LYS   B O   1 
ATOM   629  C CB  . LYS   B 2 45  ? -15.746 9.631   -4.398  1.00 41.04  ? 54  LYS   B CB  1 
ATOM   630  C CG  . LYS   B 2 45  ? -14.394 9.713   -5.056  1.00 45.57  ? 54  LYS   B CG  1 
ATOM   631  C CD  . LYS   B 2 45  ? -13.448 8.730   -4.414  1.00 51.62  ? 54  LYS   B CD  1 
ATOM   632  C CE  . LYS   B 2 45  ? -12.251 8.466   -5.290  1.00 57.29  ? 54  LYS   B CE  1 
ATOM   633  N NZ  . LYS   B 2 45  ? -12.627 8.364   -6.725  1.00 59.61  ? 54  LYS   B NZ  1 
ATOM   634  N N   . GLY   B 2 46  ? -18.665 7.393   -4.084  1.00 40.05  ? 55  GLY   B N   1 
ATOM   635  C CA  . GLY   B 2 46  ? -19.815 7.049   -3.263  1.00 41.00  ? 55  GLY   B CA  1 
ATOM   636  C C   . GLY   B 2 46  ? -20.825 8.169   -3.095  1.00 42.38  ? 55  GLY   B C   1 
ATOM   637  O O   . GLY   B 2 46  ? -21.835 7.979   -2.422  1.00 43.24  ? 55  GLY   B O   1 
ATOM   638  N N   . ALA   B 2 47  ? -20.573 9.352   -3.687  1.00 42.67  ? 56  ALA   B N   1 
ATOM   639  C CA  . ALA   B 2 47  ? -21.438 10.527  -3.540  1.00 43.05  ? 56  ALA   B CA  1 
ATOM   640  C C   . ALA   B 2 47  ? -22.737 10.442  -4.309  1.00 43.64  ? 56  ALA   B C   1 
ATOM   641  O O   . ALA   B 2 47  ? -22.784 9.792   -5.358  1.00 43.68  ? 56  ALA   B O   1 
ATOM   642  C CB  . ALA   B 2 47  ? -20.685 11.787  -3.949  1.00 42.89  ? 56  ALA   B CB  1 
ATOM   643  N N   . ALA   B 2 48  ? -23.777 11.150  -3.806  1.00 43.71  ? 57  ALA   B N   1 
ATOM   644  C CA  . ALA   B 2 48  ? -25.089 11.239  -4.434  1.00 44.47  ? 57  ALA   B CA  1 
ATOM   645  C C   . ALA   B 2 48  ? -24.991 11.959  -5.754  1.00 46.14  ? 57  ALA   B C   1 
ATOM   646  O O   . ALA   B 2 48  ? -24.212 12.901  -5.885  1.00 46.47  ? 57  ALA   B O   1 
ATOM   647  C CB  . ALA   B 2 48  ? -26.049 11.982  -3.543  1.00 44.11  ? 57  ALA   B CB  1 
ATOM   648  N N   . LEU   B 2 49  ? -25.803 11.529  -6.727  1.00 46.92  ? 58  LEU   B N   1 
ATOM   649  C CA  . LEU   B 2 49  ? -25.866 12.114  -8.070  1.00 48.15  ? 58  LEU   B CA  1 
ATOM   650  C C   . LEU   B 2 49  ? -27.221 12.833  -8.275  1.00 49.92  ? 58  LEU   B C   1 
ATOM   651  O O   . LEU   B 2 49  ? -28.097 12.765  -7.425  1.00 50.57  ? 58  LEU   B O   1 
ATOM   652  C CB  . LEU   B 2 49  ? -25.678 11.005  -9.141  1.00 47.91  ? 58  LEU   B CB  1 
ATOM   653  C CG  . LEU   B 2 49  ? -24.556 10.007  -8.900  1.00 48.69  ? 58  LEU   B CG  1 
ATOM   654  C CD1 . LEU   B 2 49  ? -24.763 8.768   -9.704  1.00 49.06  ? 58  LEU   B CD1 1 
ATOM   655  C CD2 . LEU   B 2 49  ? -23.204 10.624  -9.157  1.00 49.11  ? 58  LEU   B CD2 1 
ATOM   656  N N   . ARG   B 2 50  ? -27.393 13.512  -9.398  1.00 50.88  ? 59  ARG   B N   1 
ATOM   657  C CA  . ARG   B 2 50  ? -28.623 14.217  -9.737  1.00 52.32  ? 59  ARG   B CA  1 
ATOM   658  C C   . ARG   B 2 50  ? -29.039 13.814  -11.180 1.00 52.53  ? 59  ARG   B C   1 
ATOM   659  O O   . ARG   B 2 50  ? -28.192 13.468  -11.991 1.00 52.05  ? 59  ARG   B O   1 
ATOM   660  C CB  . ARG   B 2 50  ? -28.400 15.738  -9.548  1.00 55.10  ? 59  ARG   B CB  1 
ATOM   661  C CG  . ARG   B 2 50  ? -29.217 16.680  -10.431 1.00 60.76  ? 59  ARG   B CG  1 
ATOM   662  C CD  . ARG   B 2 50  ? -29.027 18.146  -10.046 1.00 65.87  ? 59  ARG   B CD  1 
ATOM   663  N NE  . ARG   B 2 50  ? -27.632 18.584  -10.163 1.00 70.36  ? 59  ARG   B NE  1 
ATOM   664  C CZ  . ARG   B 2 50  ? -27.171 19.376  -11.129 1.00 73.66  ? 59  ARG   B CZ  1 
ATOM   665  N NH1 . ARG   B 2 50  ? -27.988 19.831  -12.073 1.00 73.03  ? 59  ARG   B NH1 1 
ATOM   666  N NH2 . ARG   B 2 50  ? -25.888 19.715  -11.161 1.00 74.41  ? 59  ARG   B NH2 1 
ATOM   667  N N   . SER   B 2 51  ? -30.337 13.759  -11.463 1.00 53.11  ? 60  SER   B N   1 
ATOM   668  C CA  . SER   B 2 51  ? -30.844 13.368  -12.780 1.00 54.04  ? 60  SER   B CA  1 
ATOM   669  C C   . SER   B 2 51  ? -32.077 14.238  -13.018 1.00 56.20  ? 60  SER   B C   1 
ATOM   670  O O   . SER   B 2 51  ? -33.173 13.892  -12.576 1.00 57.11  ? 60  SER   B O   1 
ATOM   671  C CB  . SER   B 2 51  ? -31.225 11.893  -12.765 1.00 53.98  ? 60  SER   B CB  1 
ATOM   672  O OG  . SER   B 2 51  ? -31.544 11.427  -14.061 1.00 55.20  ? 60  SER   B OG  1 
ATOM   673  N N   . GLY   B 2 52  ? -31.881 15.393  -13.642 1.00 56.88  ? 61  GLY   B N   1 
ATOM   674  C CA  . GLY   B 2 52  ? -32.946 16.376  -13.805 1.00 58.04  ? 61  GLY   B CA  1 
ATOM   675  C C   . GLY   B 2 52  ? -33.081 17.054  -12.460 1.00 59.15  ? 61  GLY   B C   1 
ATOM   676  O O   . GLY   B 2 52  ? -32.074 17.498  -11.898 1.00 59.57  ? 61  GLY   B O   1 
ATOM   677  N N   . GLU   B 2 53  ? -34.288 17.067  -11.885 1.00 59.49  ? 62  GLU   B N   1 
ATOM   678  C CA  . GLU   B 2 53  ? -34.455 17.565  -10.505 1.00 60.15  ? 62  GLU   B CA  1 
ATOM   679  C C   . GLU   B 2 53  ? -34.324 16.428  -9.454  1.00 60.07  ? 62  GLU   B C   1 
ATOM   680  O O   . GLU   B 2 53  ? -34.146 16.707  -8.259  1.00 60.18  ? 62  GLU   B O   1 
ATOM   681  C CB  . GLU   B 2 53  ? -35.755 18.362  -10.319 1.00 62.70  ? 62  GLU   B CB  1 
ATOM   682  C CG  . GLU   B 2 53  ? -35.525 19.858  -10.438 1.00 69.54  ? 62  GLU   B CG  1 
ATOM   683  C CD  . GLU   B 2 53  ? -36.765 20.723  -10.312 1.00 80.00  ? 62  GLU   B CD  1 
ATOM   684  O OE1 . GLU   B 2 53  ? -37.698 20.534  -11.126 1.00 82.44  ? 62  GLU   B OE1 1 
ATOM   685  O OE2 . GLU   B 2 53  ? -36.804 21.593  -9.408  1.00 83.10  ? 62  GLU   B OE2 1 
ATOM   686  N N   . GLY   B 2 54  ? -34.376 15.169  -9.919  1.00 59.25  ? 63  GLY   B N   1 
ATOM   687  C CA  . GLY   B 2 54  ? -34.282 13.988  -9.075  1.00 58.76  ? 63  GLY   B CA  1 
ATOM   688  C C   . GLY   B 2 54  ? -32.922 13.748  -8.458  1.00 57.67  ? 63  GLY   B C   1 
ATOM   689  O O   . GLY   B 2 54  ? -31.898 14.235  -8.950  1.00 58.11  ? 63  GLY   B O   1 
ATOM   690  N N   . ARG   B 2 55  ? -32.906 12.969  -7.374  1.00 55.87  ? 64  ARG   B N   1 
ATOM   691  C CA  . ARG   B 2 55  ? -31.663 12.655  -6.685  1.00 54.10  ? 64  ARG   B CA  1 
ATOM   692  C C   . ARG   B 2 55  ? -31.422 11.166  -6.563  1.00 51.34  ? 64  ARG   B C   1 
ATOM   693  O O   . ARG   B 2 55  ? -32.302 10.423  -6.141  1.00 50.93  ? 64  ARG   B O   1 
ATOM   694  C CB  . ARG   B 2 55  ? -31.616 13.314  -5.307  1.00 55.30  ? 64  ARG   B CB  1 
ATOM   695  C CG  . ARG   B 2 55  ? -30.216 13.369  -4.745  1.00 58.73  ? 64  ARG   B CG  1 
ATOM   696  C CD  . ARG   B 2 55  ? -30.274 13.353  -3.236  1.00 63.28  ? 64  ARG   B CD  1 
ATOM   697  N NE  . ARG   B 2 55  ? -28.943 13.452  -2.638  1.00 66.42  ? 64  ARG   B NE  1 
ATOM   698  C CZ  . ARG   B 2 55  ? -28.611 14.319  -1.688  1.00 68.75  ? 64  ARG   B CZ  1 
ATOM   699  N NH1 . ARG   B 2 55  ? -29.513 15.169  -1.211  1.00 68.50  ? 64  ARG   B NH1 1 
ATOM   700  N NH2 . ARG   B 2 55  ? -27.376 14.344  -1.208  1.00 68.73  ? 64  ARG   B NH2 1 
ATOM   701  N N   . LEU   B 2 56  ? -30.216 10.740  -6.939  1.00 49.34  ? 65  LEU   B N   1 
ATOM   702  C CA  . LEU   B 2 56  ? -29.796 9.356   -6.848  1.00 47.70  ? 65  LEU   B CA  1 
ATOM   703  C C   . LEU   B 2 56  ? -28.929 9.194   -5.615  1.00 45.95  ? 65  LEU   B C   1 
ATOM   704  O O   . LEU   B 2 56  ? -27.835 9.748   -5.557  1.00 45.39  ? 65  LEU   B O   1 
ATOM   705  C CB  . LEU   B 2 56  ? -28.983 8.949   -8.083  1.00 47.62  ? 65  LEU   B CB  1 
ATOM   706  C CG  . LEU   B 2 56  ? -29.573 9.203   -9.454  1.00 48.84  ? 65  LEU   B CG  1 
ATOM   707  C CD1 . LEU   B 2 56  ? -28.715 8.543   -10.516 1.00 48.88  ? 65  LEU   B CD1 1 
ATOM   708  C CD2 . LEU   B 2 56  ? -30.999 8.666   -9.565  1.00 49.87  ? 65  LEU   B CD2 1 
ATOM   709  N N   . ASP   B 2 57  ? -29.418 8.448   -4.632  1.00 45.08  ? 66  ASP   B N   1 
ATOM   710  C CA  . ASP   B 2 57  ? -28.683 8.191   -3.402  1.00 44.92  ? 66  ASP   B CA  1 
ATOM   711  C C   . ASP   B 2 57  ? -28.094 6.782   -3.453  1.00 43.56  ? 66  ASP   B C   1 
ATOM   712  O O   . ASP   B 2 57  ? -28.744 5.860   -3.949  1.00 43.84  ? 66  ASP   B O   1 
ATOM   713  C CB  . ASP   B 2 57  ? -29.618 8.342   -2.212  1.00 48.54  ? 66  ASP   B CB  1 
ATOM   714  C CG  . ASP   B 2 57  ? -29.963 9.787   -1.912  1.00 56.74  ? 66  ASP   B CG  1 
ATOM   715  O OD1 . ASP   B 2 57  ? -29.027 10.574  -1.646  1.00 58.95  ? 66  ASP   B OD1 1 
ATOM   716  O OD2 . ASP   B 2 57  ? -31.178 10.129  -1.922  1.00 59.08  ? 66  ASP   B OD2 1 
ATOM   717  N N   . PRO   B 2 58  ? -26.845 6.594   -3.003  1.00 42.02  ? 67  PRO   B N   1 
ATOM   718  C CA  . PRO   B 2 58  ? -26.236 5.256   -3.075  1.00 41.40  ? 67  PRO   B CA  1 
ATOM   719  C C   . PRO   B 2 58  ? -26.957 4.198   -2.237  1.00 41.15  ? 67  PRO   B C   1 
ATOM   720  O O   . PRO   B 2 58  ? -27.633 4.512   -1.231  1.00 41.43  ? 67  PRO   B O   1 
ATOM   721  C CB  . PRO   B 2 58  ? -24.809 5.491   -2.575  1.00 41.98  ? 67  PRO   B CB  1 
ATOM   722  C CG  . PRO   B 2 58  ? -24.905 6.716   -1.728  1.00 42.57  ? 67  PRO   B CG  1 
ATOM   723  C CD  . PRO   B 2 58  ? -25.927 7.578   -2.403  1.00 41.24  ? 67  PRO   B CD  1 
ATOM   724  N N   . TYR   B 2 59  ? -26.829 2.928   -2.659  1.00 39.78  ? 68  TYR   B N   1 
ATOM   725  C CA  . TYR   B 2 59  ? -27.470 1.837   -1.925  1.00 38.59  ? 68  TYR   B CA  1 
ATOM   726  C C   . TYR   B 2 59  ? -26.421 0.840   -1.430  1.00 37.67  ? 68  TYR   B C   1 
ATOM   727  O O   . TYR   B 2 59  ? -26.457 0.440   -0.261  1.00 37.31  ? 68  TYR   B O   1 
ATOM   728  C CB  . TYR   B 2 59  ? -28.532 1.169   -2.796  1.00 37.69  ? 68  TYR   B CB  1 
ATOM   729  C CG  . TYR   B 2 59  ? -29.239 -0.011  -2.167  1.00 37.00  ? 68  TYR   B CG  1 
ATOM   730  C CD1 . TYR   B 2 59  ? -28.631 -1.262  -2.110  1.00 37.59  ? 68  TYR   B CD1 1 
ATOM   731  C CD2 . TYR   B 2 59  ? -30.566 0.079   -1.784  1.00 36.98  ? 68  TYR   B CD2 1 
ATOM   732  C CE1 . TYR   B 2 59  ? -29.298 -2.370  -1.611  1.00 38.15  ? 68  TYR   B CE1 1 
ATOM   733  C CE2 . TYR   B 2 59  ? -31.250 -1.025  -1.300  1.00 38.07  ? 68  TYR   B CE2 1 
ATOM   734  C CZ  . TYR   B 2 59  ? -30.616 -2.254  -1.224  1.00 39.20  ? 68  TYR   B CZ  1 
ATOM   735  O OH  . TYR   B 2 59  ? -31.303 -3.354  -0.756  1.00 40.51  ? 68  TYR   B OH  1 
ATOM   736  N N   . TRP   B 2 60  ? -25.497 0.439   -2.329  1.00 36.58  ? 69  TRP   B N   1 
ATOM   737  C CA  . TRP   B 2 60  ? -24.392 -0.474  -2.033  1.00 36.01  ? 69  TRP   B CA  1 
ATOM   738  C C   . TRP   B 2 60  ? -23.094 0.048   -2.677  1.00 36.01  ? 69  TRP   B C   1 
ATOM   739  O O   . TRP   B 2 60  ? -23.142 0.718   -3.698  1.00 36.15  ? 69  TRP   B O   1 
ATOM   740  C CB  . TRP   B 2 60  ? -24.707 -1.883  -2.559  1.00 35.51  ? 69  TRP   B CB  1 
ATOM   741  C CG  . TRP   B 2 60  ? -23.515 -2.795  -2.572  1.00 35.69  ? 69  TRP   B CG  1 
ATOM   742  C CD1 . TRP   B 2 60  ? -22.977 -3.457  -1.508  1.00 36.66  ? 69  TRP   B CD1 1 
ATOM   743  C CD2 . TRP   B 2 60  ? -22.625 -3.015  -3.674  1.00 35.43  ? 69  TRP   B CD2 1 
ATOM   744  N NE1 . TRP   B 2 60  ? -21.839 -4.126  -1.898  1.00 36.89  ? 69  TRP   B NE1 1 
ATOM   745  C CE2 . TRP   B 2 60  ? -21.597 -3.861  -3.221  1.00 36.20  ? 69  TRP   B CE2 1 
ATOM   746  C CE3 . TRP   B 2 60  ? -22.604 -2.588  -5.004  1.00 35.69  ? 69  TRP   B CE3 1 
ATOM   747  C CZ2 . TRP   B 2 60  ? -20.578 -4.304  -4.059  1.00 36.60  ? 69  TRP   B CZ2 1 
ATOM   748  C CZ3 . TRP   B 2 60  ? -21.589 -3.026  -5.827  1.00 36.20  ? 69  TRP   B CZ3 1 
ATOM   749  C CH2 . TRP   B 2 60  ? -20.603 -3.889  -5.359  1.00 36.33  ? 69  TRP   B CH2 1 
ATOM   750  N N   . GLY   B 2 61  ? -21.955 -0.322  -2.117  1.00 35.57  ? 70  GLY   B N   1 
ATOM   751  C CA  . GLY   B 2 61  ? -20.662 0.052   -2.671  1.00 35.55  ? 70  GLY   B CA  1 
ATOM   752  C C   . GLY   B 2 61  ? -19.535 -0.732  -2.035  1.00 35.62  ? 70  GLY   B C   1 
ATOM   753  O O   . GLY   B 2 61  ? -19.659 -1.183  -0.891  1.00 36.04  ? 70  GLY   B O   1 
ATOM   754  N N   . ASP   B 2 62  ? -18.423 -0.884  -2.755  1.00 34.90  ? 71  ASP   B N   1 
ATOM   755  C CA  . ASP   B 2 62  ? -17.258 -1.614  -2.244  1.00 34.82  ? 71  ASP   B CA  1 
ATOM   756  C C   . ASP   B 2 62  ? -15.989 -1.119  -2.962  1.00 34.50  ? 71  ASP   B C   1 
ATOM   757  O O   . ASP   B 2 62  ? -15.892 -1.173  -4.192  1.00 35.39  ? 71  ASP   B O   1 
ATOM   758  C CB  . ASP   B 2 62  ? -17.457 -3.124  -2.440  1.00 36.70  ? 71  ASP   B CB  1 
ATOM   759  C CG  . ASP   B 2 62  ? -16.415 -4.000  -1.802  1.00 42.54  ? 71  ASP   B CG  1 
ATOM   760  O OD1 . ASP   B 2 62  ? -15.237 -3.897  -2.185  1.00 43.27  ? 71  ASP   B OD1 1 
ATOM   761  O OD2 . ASP   B 2 62  ? -16.782 -4.816  -0.941  1.00 46.48  ? 71  ASP   B OD2 1 
ATOM   762  N N   . VAL   B 2 63  ? -15.033 -0.630  -2.196  1.00 33.19  ? 72  VAL   B N   1 
ATOM   763  C CA  . VAL   B 2 63  ? -13.807 -0.082  -2.722  1.00 32.75  ? 72  VAL   B CA  1 
ATOM   764  C C   . VAL   B 2 63  ? -12.959 -1.161  -3.387  1.00 34.09  ? 72  VAL   B C   1 
ATOM   765  O O   . VAL   B 2 63  ? -12.556 -0.951  -4.536  1.00 34.75  ? 72  VAL   B O   1 
ATOM   766  C CB  . VAL   B 2 63  ? -13.079 0.735   -1.639  1.00 32.46  ? 72  VAL   B CB  1 
ATOM   767  C CG1 . VAL   B 2 63  ? -11.583 0.816   -1.866  1.00 32.57  ? 72  VAL   B CG1 1 
ATOM   768  C CG2 . VAL   B 2 63  ? -13.677 2.128   -1.531  1.00 32.68  ? 72  VAL   B CG2 1 
ATOM   769  N N   . LYS   B 2 64  ? -12.753 -2.326  -2.743  1.00 34.27  ? 73  LYS   B N   1 
ATOM   770  C CA  . LYS   B 2 64  ? -11.973 -3.424  -3.348  1.00 34.57  ? 73  LYS   B CA  1 
ATOM   771  C C   . LYS   B 2 64  ? -12.531 -3.848  -4.726  1.00 35.28  ? 73  LYS   B C   1 
ATOM   772  O O   . LYS   B 2 64  ? -11.784 -3.951  -5.702  1.00 35.55  ? 73  LYS   B O   1 
ATOM   773  C CB  . LYS   B 2 64  ? -11.892 -4.618  -2.379  1.00 35.60  ? 73  LYS   B CB  1 
ATOM   774  C CG  . LYS   B 2 64  ? -11.072 -5.761  -2.943  1.00 38.23  ? 73  LYS   B CG  1 
ATOM   775  C CD  . LYS   B 2 64  ? -10.035 -6.281  -1.990  1.00 40.57  ? 73  LYS   B CD  1 
ATOM   776  C CE  . LYS   B 2 64  ? -9.623  -7.677  -2.368  1.00 43.66  ? 73  LYS   B CE  1 
ATOM   777  N NZ  . LYS   B 2 64  ? -9.378  -8.502  -1.153  1.00 46.99  ? 73  LYS   B NZ  1 
ATOM   778  N N   . GLN   B 2 65  ? -13.854 -4.030  -4.823  1.00 35.54  ? 74  GLN   B N   1 
ATOM   779  C CA  . GLN   B 2 65  ? -14.496 -4.347  -6.103  1.00 36.08  ? 74  GLN   B CA  1 
ATOM   780  C C   . GLN   B 2 65  ? -14.540 -3.139  -7.062  1.00 36.52  ? 74  GLN   B C   1 
ATOM   781  O O   . GLN   B 2 65  ? -14.717 -3.313  -8.280  1.00 37.37  ? 74  GLN   B O   1 
ATOM   782  C CB  . GLN   B 2 65  ? -15.940 -4.791  -5.879  1.00 37.59  ? 74  GLN   B CB  1 
ATOM   783  C CG  . GLN   B 2 65  ? -16.094 -5.988  -4.983  1.00 40.92  ? 74  GLN   B CG  1 
ATOM   784  C CD  . GLN   B 2 65  ? -17.550 -6.388  -4.911  1.00 44.95  ? 74  GLN   B CD  1 
ATOM   785  O OE1 . GLN   B 2 65  ? -18.251 -6.521  -5.945  1.00 45.81  ? 74  GLN   B OE1 1 
ATOM   786  N NE2 . GLN   B 2 65  ? -18.028 -6.595  -3.681  1.00 44.26  ? 74  GLN   B NE2 1 
ATOM   787  N N   . ASP   B 2 66  ? -14.472 -1.922  -6.503  1.00 35.62  ? 75  ASP   B N   1 
ATOM   788  C CA  . ASP   B 2 66  ? -14.562 -0.663  -7.230  1.00 34.98  ? 75  ASP   B CA  1 
ATOM   789  C C   . ASP   B 2 66  ? -15.917 -0.575  -7.902  1.00 34.48  ? 75  ASP   B C   1 
ATOM   790  O O   . ASP   B 2 66  ? -15.995 -0.230  -9.058  1.00 34.73  ? 75  ASP   B O   1 
ATOM   791  C CB  . ASP   B 2 66  ? -13.405 -0.468  -8.227  1.00 34.80  ? 75  ASP   B CB  1 
ATOM   792  C CG  . ASP   B 2 66  ? -13.335 0.929   -8.796  1.00 37.12  ? 75  ASP   B CG  1 
ATOM   793  O OD1 . ASP   B 2 66  ? -13.772 1.860   -8.123  1.00 37.08  ? 75  ASP   B OD1 1 
ATOM   794  O OD2 . ASP   B 2 66  ? -12.862 1.081   -9.926  1.00 40.59  ? 75  ASP   B OD2 1 
ATOM   795  N N   . LEU   B 2 67  ? -16.997 -0.884  -7.173  1.00 33.64  ? 76  LEU   B N   1 
ATOM   796  C CA  . LEU   B 2 67  ? -18.354 -0.813  -7.716  1.00 33.01  ? 76  LEU   B CA  1 
ATOM   797  C C   . LEU   B 2 67  ? -19.285 -0.156  -6.709  1.00 33.10  ? 76  LEU   B C   1 
ATOM   798  O O   . LEU   B 2 67  ? -19.011 -0.182  -5.505  1.00 33.64  ? 76  LEU   B O   1 
ATOM   799  C CB  . LEU   B 2 67  ? -18.876 -2.204  -8.089  1.00 32.79  ? 76  LEU   B CB  1 
ATOM   800  C CG  . LEU   B 2 67  ? -18.074 -2.968  -9.140  1.00 34.01  ? 76  LEU   B CG  1 
ATOM   801  C CD1 . LEU   B 2 67  ? -18.514 -4.408  -9.216  1.00 34.15  ? 76  LEU   B CD1 1 
ATOM   802  C CD2 . LEU   B 2 67  ? -18.197 -2.306  -10.521 1.00 35.08  ? 76  LEU   B CD2 1 
ATOM   803  N N   . VAL   B 2 68  ? -20.367 0.474   -7.201  1.00 32.44  ? 77  VAL   B N   1 
ATOM   804  C CA  . VAL   B 2 68  ? -21.357 1.186   -6.382  1.00 31.80  ? 77  VAL   B CA  1 
ATOM   805  C C   . VAL   B 2 68  ? -22.682 1.221   -7.146  1.00 32.04  ? 77  VAL   B C   1 
ATOM   806  O O   . VAL   B 2 68  ? -22.685 1.481   -8.351  1.00 32.23  ? 77  VAL   B O   1 
ATOM   807  C CB  . VAL   B 2 68  ? -20.863 2.612   -5.989  1.00 31.90  ? 77  VAL   B CB  1 
ATOM   808  C CG1 . VAL   B 2 68  ? -20.598 3.479   -7.219  1.00 32.50  ? 77  VAL   B CG1 1 
ATOM   809  C CG2 . VAL   B 2 68  ? -21.836 3.304   -5.053  1.00 31.97  ? 77  VAL   B CG2 1 
ATOM   810  N N   . SER   B 2 69  ? -23.797 0.888   -6.480  1.00 31.75  ? 78  SER   B N   1 
ATOM   811  C CA  . SER   B 2 69  ? -25.104 0.894   -7.142  1.00 32.16  ? 78  SER   B CA  1 
ATOM   812  C C   . SER   B 2 69  ? -26.028 1.923   -6.510  1.00 32.89  ? 78  SER   B C   1 
ATOM   813  O O   . SER   B 2 69  ? -25.927 2.167   -5.307  1.00 33.84  ? 78  SER   B O   1 
ATOM   814  C CB  . SER   B 2 69  ? -25.726 -0.497  -7.137  1.00 32.86  ? 78  SER   B CB  1 
ATOM   815  O OG  . SER   B 2 69  ? -26.135 -0.914  -5.849  1.00 34.37  ? 78  SER   B OG  1 
ATOM   816  N N   . TYR   B 2 70  ? -26.896 2.565   -7.304  1.00 32.38  ? 79  TYR   B N   1 
ATOM   817  C CA  . TYR   B 2 70  ? -27.771 3.620   -6.784  1.00 32.78  ? 79  TYR   B CA  1 
ATOM   818  C C   . TYR   B 2 70  ? -29.237 3.248   -6.879  1.00 33.92  ? 79  TYR   B C   1 
ATOM   819  O O   . TYR   B 2 70  ? -29.639 2.643   -7.867  1.00 34.29  ? 79  TYR   B O   1 
ATOM   820  C CB  . TYR   B 2 70  ? -27.544 4.950   -7.524  1.00 32.21  ? 79  TYR   B CB  1 
ATOM   821  C CG  . TYR   B 2 70  ? -26.209 5.597   -7.240  1.00 32.25  ? 79  TYR   B CG  1 
ATOM   822  C CD1 . TYR   B 2 70  ? -25.035 5.087   -7.781  1.00 32.97  ? 79  TYR   B CD1 1 
ATOM   823  C CD2 . TYR   B 2 70  ? -26.127 6.755   -6.486  1.00 32.91  ? 79  TYR   B CD2 1 
ATOM   824  C CE1 . TYR   B 2 70  ? -23.805 5.676   -7.518  1.00 33.89  ? 79  TYR   B CE1 1 
ATOM   825  C CE2 . TYR   B 2 70  ? -24.907 7.350   -6.211  1.00 33.88  ? 79  TYR   B CE2 1 
ATOM   826  C CZ  . TYR   B 2 70  ? -23.746 6.810   -6.729  1.00 35.14  ? 79  TYR   B CZ  1 
ATOM   827  O OH  . TYR   B 2 70  ? -22.544 7.409   -6.437  1.00 37.26  ? 79  TYR   B OH  1 
ATOM   828  N N   . CYS   B 2 71  ? -30.035 3.611   -5.846  1.00 34.13  ? 80  CYS   B N   1 
ATOM   829  C CA  . CYS   B 2 71  ? -31.481 3.378   -5.750  1.00 34.73  ? 80  CYS   B CA  1 
ATOM   830  C C   . CYS   B 2 71  ? -31.869 1.941   -5.364  1.00 33.91  ? 80  CYS   B C   1 
ATOM   831  O O   . CYS   B 2 71  ? -32.950 1.721   -4.798  1.00 34.52  ? 80  CYS   B O   1 
ATOM   832  C CB  . CYS   B 2 71  ? -32.203 3.834   -7.007  1.00 37.07  ? 80  CYS   B CB  1 
ATOM   833  S SG  . CYS   B 2 71  ? -31.711 5.486   -7.564  1.00 46.12  ? 80  CYS   B SG  1 
ATOM   834  N N   . GLY   B 2 72  ? -30.981 0.993   -5.606  1.00 32.20  ? 81  GLY   B N   1 
ATOM   835  C CA  . GLY   B 2 72  ? -31.240 -0.390  -5.256  1.00 31.55  ? 81  GLY   B CA  1 
ATOM   836  C C   . GLY   B 2 72  ? -30.005 -1.242  -5.344  1.00 31.24  ? 81  GLY   B C   1 
ATOM   837  O O   . GLY   B 2 72  ? -28.910 -0.753  -5.631  1.00 31.09  ? 81  GLY   B O   1 
ATOM   838  N N   . PRO   B 2 73  ? -30.161 -2.535  -5.055  1.00 31.11  ? 82  PRO   B N   1 
ATOM   839  C CA  . PRO   B 2 73  ? -29.008 -3.431  -5.129  1.00 31.68  ? 82  PRO   B CA  1 
ATOM   840  C C   . PRO   B 2 73  ? -28.541 -3.668  -6.551  1.00 33.85  ? 82  PRO   B C   1 
ATOM   841  O O   . PRO   B 2 73  ? -29.299 -3.490  -7.514  1.00 34.41  ? 82  PRO   B O   1 
ATOM   842  C CB  . PRO   B 2 73  ? -29.525 -4.722  -4.507  1.00 31.60  ? 82  PRO   B CB  1 
ATOM   843  C CG  . PRO   B 2 73  ? -30.992 -4.660  -4.637  1.00 31.49  ? 82  PRO   B CG  1 
ATOM   844  C CD  . PRO   B 2 73  ? -31.389 -3.235  -4.639  1.00 30.20  ? 82  PRO   B CD  1 
ATOM   845  N N   . TRP   B 2 74  ? -27.289 -4.133  -6.688  1.00 34.89  ? 83  TRP   B N   1 
ATOM   846  C CA  . TRP   B 2 74  ? -26.672 -4.476  -7.969  1.00 35.94  ? 83  TRP   B CA  1 
ATOM   847  C C   . TRP   B 2 74  ? -27.541 -5.483  -8.706  1.00 38.37  ? 83  TRP   B C   1 
ATOM   848  O O   . TRP   B 2 74  ? -27.910 -6.498  -8.124  1.00 38.57  ? 83  TRP   B O   1 
ATOM   849  C CB  . TRP   B 2 74  ? -25.280 -5.068  -7.738  1.00 35.31  ? 83  TRP   B CB  1 
ATOM   850  C CG  . TRP   B 2 74  ? -24.462 -5.165  -8.986  1.00 35.38  ? 83  TRP   B CG  1 
ATOM   851  C CD1 . TRP   B 2 74  ? -24.396 -6.223  -9.835  1.00 36.04  ? 83  TRP   B CD1 1 
ATOM   852  C CD2 . TRP   B 2 74  ? -23.561 -4.173  -9.506  1.00 35.34  ? 83  TRP   B CD2 1 
ATOM   853  N NE1 . TRP   B 2 74  ? -23.520 -5.953  -10.859 1.00 36.42  ? 83  TRP   B NE1 1 
ATOM   854  C CE2 . TRP   B 2 74  ? -23.016 -4.689  -10.697 1.00 36.09  ? 83  TRP   B CE2 1 
ATOM   855  C CE3 . TRP   B 2 74  ? -23.192 -2.885  -9.100  1.00 35.93  ? 83  TRP   B CE3 1 
ATOM   856  C CZ2 . TRP   B 2 74  ? -22.129 -3.962  -11.493 1.00 36.67  ? 83  TRP   B CZ2 1 
ATOM   857  C CZ3 . TRP   B 2 74  ? -22.295 -2.176  -9.876  1.00 36.99  ? 83  TRP   B CZ3 1 
ATOM   858  C CH2 . TRP   B 2 74  ? -21.781 -2.711  -11.063 1.00 36.94  ? 83  TRP   B CH2 1 
ATOM   859  N N   . LYS   B 2 75  ? -27.939 -5.149  -9.950  1.00 40.19  ? 84  LYS   B N   1 
ATOM   860  C CA  . LYS   B 2 75  ? -28.820 -5.958  -10.788 1.00 41.48  ? 84  LYS   B CA  1 
ATOM   861  C C   . LYS   B 2 75  ? -28.092 -6.724  -11.880 1.00 42.69  ? 84  LYS   B C   1 
ATOM   862  O O   . LYS   B 2 75  ? -28.617 -7.736  -12.332 1.00 43.35  ? 84  LYS   B O   1 
ATOM   863  C CB  . LYS   B 2 75  ? -29.923 -5.091  -11.427 1.00 42.94  ? 84  LYS   B CB  1 
ATOM   864  C CG  . LYS   B 2 75  ? -30.741 -4.269  -10.432 1.00 46.50  ? 84  LYS   B CG  1 
ATOM   865  C CD  . LYS   B 2 75  ? -31.952 -5.011  -9.854  1.00 50.66  ? 84  LYS   B CD  1 
ATOM   866  C CE  . LYS   B 2 75  ? -32.597 -4.217  -8.732  1.00 54.28  ? 84  LYS   B CE  1 
ATOM   867  N NZ  . LYS   B 2 75  ? -33.925 -4.745  -8.328  1.00 56.26  ? 84  LYS   B NZ  1 
ATOM   868  N N   . LEU   B 2 76  ? -26.921 -6.255  -12.335 1.00 42.83  ? 85  LEU   B N   1 
ATOM   869  C CA  . LEU   B 2 76  ? -26.210 -6.917  -13.448 1.00 43.28  ? 85  LEU   B CA  1 
ATOM   870  C C   . LEU   B 2 76  ? -25.590 -8.237  -12.997 1.00 45.15  ? 85  LEU   B C   1 
ATOM   871  O O   . LEU   B 2 76  ? -24.782 -8.237  -12.088 1.00 45.53  ? 85  LEU   B O   1 
ATOM   872  C CB  . LEU   B 2 76  ? -25.156 -5.988  -14.086 1.00 42.33  ? 85  LEU   B CB  1 
ATOM   873  C CG  . LEU   B 2 76  ? -25.548 -4.506  -14.232 1.00 42.39  ? 85  LEU   B CG  1 
ATOM   874  C CD1 . LEU   B 2 76  ? -24.384 -3.655  -14.627 1.00 42.53  ? 85  LEU   B CD1 1 
ATOM   875  C CD2 . LEU   B 2 76  ? -26.711 -4.313  -15.167 1.00 42.35  ? 85  LEU   B CD2 1 
ATOM   876  N N   . ASP   B 2 77  ? -25.973 -9.359  -13.613 1.00 46.52  ? 86  ASP   B N   1 
ATOM   877  C CA  . ASP   B 2 77  ? -25.487 -10.666 -13.180 1.00 48.43  ? 86  ASP   B CA  1 
ATOM   878  C C   . ASP   B 2 77  ? -24.891 -11.573 -14.291 1.00 49.81  ? 86  ASP   B C   1 
ATOM   879  O O   . ASP   B 2 77  ? -24.412 -12.656 -13.960 1.00 50.54  ? 86  ASP   B O   1 
ATOM   880  C CB  . ASP   B 2 77  ? -26.594 -11.413 -12.409 1.00 50.93  ? 86  ASP   B CB  1 
ATOM   881  C CG  . ASP   B 2 77  ? -27.852 -11.728 -13.210 1.00 57.91  ? 86  ASP   B CG  1 
ATOM   882  O OD1 . ASP   B 2 77  ? -28.077 -11.071 -14.267 1.00 58.40  ? 86  ASP   B OD1 1 
ATOM   883  O OD2 . ASP   B 2 77  ? -28.616 -12.624 -12.783 1.00 61.18  ? 86  ASP   B OD2 1 
ATOM   884  N N   . ALA   B 2 78  ? -24.872 -11.146 -15.568 1.00 49.95  ? 87  ALA   B N   1 
ATOM   885  C CA  . ALA   B 2 78  ? -24.293 -11.968 -16.637 1.00 50.65  ? 87  ALA   B CA  1 
ATOM   886  C C   . ALA   B 2 78  ? -22.760 -11.956 -16.612 1.00 51.52  ? 87  ALA   B C   1 
ATOM   887  O O   . ALA   B 2 78  ? -22.163 -11.018 -16.085 1.00 51.62  ? 87  ALA   B O   1 
ATOM   888  C CB  . ALA   B 2 78  ? -24.785 -11.493 -17.989 1.00 50.86  ? 87  ALA   B CB  1 
ATOM   889  N N   . ALA   B 2 79  ? -22.115 -12.997 -17.184 1.00 51.74  ? 88  ALA   B N   1 
ATOM   890  C CA  . ALA   B 2 79  ? -20.653 -13.073 -17.208 1.00 52.01  ? 88  ALA   B CA  1 
ATOM   891  C C   . ALA   B 2 79  ? -20.084 -13.624 -18.512 1.00 52.74  ? 88  ALA   B C   1 
ATOM   892  O O   . ALA   B 2 79  ? -20.709 -14.460 -19.169 1.00 52.36  ? 88  ALA   B O   1 
ATOM   893  C CB  . ALA   B 2 79  ? -20.159 -13.907 -16.052 1.00 52.04  ? 88  ALA   B CB  1 
ATOM   894  N N   . TRP   B 2 80  ? -18.862 -13.175 -18.853 1.00 53.39  ? 89  TRP   B N   1 
ATOM   895  C CA  . TRP   B 2 80  ? -18.085 -13.614 -20.001 1.00 54.44  ? 89  TRP   B CA  1 
ATOM   896  C C   . TRP   B 2 80  ? -17.903 -15.135 -19.959 1.00 56.18  ? 89  TRP   B C   1 
ATOM   897  O O   . TRP   B 2 80  ? -17.678 -15.696 -18.882 1.00 55.75  ? 89  TRP   B O   1 
ATOM   898  C CB  . TRP   B 2 80  ? -16.711 -12.920 -20.015 1.00 54.08  ? 89  TRP   B CB  1 
ATOM   899  C CG  . TRP   B 2 80  ? -15.840 -13.316 -21.180 1.00 54.58  ? 89  TRP   B CG  1 
ATOM   900  C CD1 . TRP   B 2 80  ? -16.201 -13.379 -22.498 1.00 55.32  ? 89  TRP   B CD1 1 
ATOM   901  C CD2 . TRP   B 2 80  ? -14.435 -13.592 -21.135 1.00 54.53  ? 89  TRP   B CD2 1 
ATOM   902  N NE1 . TRP   B 2 80  ? -15.117 -13.736 -23.268 1.00 55.61  ? 89  TRP   B NE1 1 
ATOM   903  C CE2 . TRP   B 2 80  ? -14.018 -13.863 -22.455 1.00 55.17  ? 89  TRP   B CE2 1 
ATOM   904  C CE3 . TRP   B 2 80  ? -13.488 -13.641 -20.106 1.00 54.83  ? 89  TRP   B CE3 1 
ATOM   905  C CZ2 . TRP   B 2 80  ? -12.704 -14.207 -22.763 1.00 55.36  ? 89  TRP   B CZ2 1 
ATOM   906  C CZ3 . TRP   B 2 80  ? -12.187 -13.977 -20.420 1.00 55.44  ? 89  TRP   B CZ3 1 
ATOM   907  C CH2 . TRP   B 2 80  ? -11.808 -14.252 -21.734 1.00 55.30  ? 89  TRP   B CH2 1 
ATOM   908  N N   . ASP   B 2 81  ? -18.042 -15.808 -21.124 1.00 57.84  ? 90  ASP   B N   1 
ATOM   909  C CA  . ASP   B 2 81  ? -17.900 -17.259 -21.154 1.00 59.87  ? 90  ASP   B CA  1 
ATOM   910  C C   . ASP   B 2 81  ? -16.438 -17.743 -21.289 1.00 61.38  ? 90  ASP   B C   1 
ATOM   911  O O   . ASP   B 2 81  ? -16.197 -18.946 -21.291 1.00 62.02  ? 90  ASP   B O   1 
ATOM   912  C CB  . ASP   B 2 81  ? -18.808 -17.894 -22.219 1.00 61.92  ? 90  ASP   B CB  1 
ATOM   913  C CG  . ASP   B 2 81  ? -18.630 -17.370 -23.626 1.00 67.96  ? 90  ASP   B CG  1 
ATOM   914  O OD1 . ASP   B 2 81  ? -17.702 -16.564 -23.848 1.00 70.34  ? 90  ASP   B OD1 1 
ATOM   915  O OD2 . ASP   B 2 81  ? -19.417 -17.772 -24.515 1.00 68.64  ? 90  ASP   B OD2 1 
ATOM   916  N N   . GLY   B 2 82  ? -15.485 -16.820 -21.362 1.00 61.67  ? 91  GLY   B N   1 
ATOM   917  C CA  . GLY   B 2 82  ? -14.083 -17.168 -21.512 1.00 62.43  ? 91  GLY   B CA  1 
ATOM   918  C C   . GLY   B 2 82  ? -13.711 -17.579 -22.925 1.00 63.42  ? 91  GLY   B C   1 
ATOM   919  O O   . GLY   B 2 82  ? -12.551 -17.912 -23.175 1.00 64.02  ? 91  GLY   B O   1 
ATOM   920  N N   . LEU   B 2 83  ? -14.671 -17.559 -23.875 1.00 63.26  ? 92  LEU   B N   1 
ATOM   921  C CA  . LEU   B 2 83  ? -14.414 -17.999 -25.234 1.00 63.68  ? 92  LEU   B CA  1 
ATOM   922  C C   . LEU   B 2 83  ? -14.836 -16.996 -26.297 1.00 64.62  ? 92  LEU   B C   1 
ATOM   923  O O   . LEU   B 2 83  ? -14.217 -16.930 -27.359 1.00 65.47  ? 92  LEU   B O   1 
ATOM   924  C CB  . LEU   B 2 83  ? -15.231 -19.278 -25.511 1.00 63.94  ? 92  LEU   B CB  1 
ATOM   925  C CG  . LEU   B 2 83  ? -14.867 -20.635 -24.901 1.00 65.54  ? 92  LEU   B CG  1 
ATOM   926  C CD1 . LEU   B 2 83  ? -15.346 -21.763 -25.831 1.00 66.08  ? 92  LEU   B CD1 1 
ATOM   927  C CD2 . LEU   B 2 83  ? -13.376 -20.785 -24.653 1.00 65.94  ? 92  LEU   B CD2 1 
ATOM   928  N N   . SER   B 2 84  ? -15.956 -16.308 -26.083 1.00 64.01  ? 93  SER   B N   1 
ATOM   929  C CA  . SER   B 2 84  ? -16.532 -15.445 -27.106 1.00 63.46  ? 93  SER   B CA  1 
ATOM   930  C C   . SER   B 2 84  ? -16.022 -14.019 -27.123 1.00 62.37  ? 93  SER   B C   1 
ATOM   931  O O   . SER   B 2 84  ? -15.561 -13.505 -26.108 1.00 62.79  ? 93  SER   B O   1 
ATOM   932  C CB  . SER   B 2 84  ? -18.051 -15.447 -26.981 1.00 65.38  ? 93  SER   B CB  1 
ATOM   933  O OG  . SER   B 2 84  ? -18.545 -16.751 -26.726 1.00 68.16  ? 93  SER   B OG  1 
ATOM   934  N N   . GLU   B 2 85  ? -16.128 -13.370 -28.283 1.00 61.26  ? 94  GLU   B N   1 
ATOM   935  C CA  . GLU   B 2 85  ? -15.761 -11.967 -28.424 1.00 60.46  ? 94  GLU   B CA  1 
ATOM   936  C C   . GLU   B 2 85  ? -16.817 -11.129 -27.711 1.00 59.15  ? 94  GLU   B C   1 
ATOM   937  O O   . GLU   B 2 85  ? -17.968 -11.548 -27.545 1.00 59.44  ? 94  GLU   B O   1 
ATOM   938  C CB  . GLU   B 2 85  ? -15.636 -11.547 -29.909 1.00 62.32  ? 94  GLU   B CB  1 
ATOM   939  C CG  . GLU   B 2 85  ? -14.332 -11.975 -30.576 1.00 66.39  ? 94  GLU   B CG  1 
ATOM   940  C CD  . GLU   B 2 85  ? -13.924 -11.199 -31.820 1.00 70.85  ? 94  GLU   B CD  1 
ATOM   941  O OE1 . GLU   B 2 85  ? -14.822 -10.680 -32.522 1.00 70.15  ? 94  GLU   B OE1 1 
ATOM   942  O OE2 . GLU   B 2 85  ? -12.703 -11.112 -32.094 1.00 72.44  ? 94  GLU   B OE2 1 
ATOM   943  N N   . VAL   B 2 86  ? -16.407 -9.976  -27.227 1.00 57.61  ? 95  VAL   B N   1 
ATOM   944  C CA  . VAL   B 2 86  ? -17.296 -9.082  -26.493 1.00 56.20  ? 95  VAL   B CA  1 
ATOM   945  C C   . VAL   B 2 86  ? -17.308 -7.684  -27.147 1.00 55.20  ? 95  VAL   B C   1 
ATOM   946  O O   . VAL   B 2 86  ? -16.579 -7.443  -28.113 1.00 55.29  ? 95  VAL   B O   1 
ATOM   947  C CB  . VAL   B 2 86  ? -16.900 -9.038  -24.986 1.00 55.68  ? 95  VAL   B CB  1 
ATOM   948  C CG1 . VAL   B 2 86  ? -16.950 -10.419 -24.358 1.00 55.94  ? 95  VAL   B CG1 1 
ATOM   949  C CG2 . VAL   B 2 86  ? -15.536 -8.398  -24.802 1.00 55.69  ? 95  VAL   B CG2 1 
ATOM   950  N N   . GLN   B 2 87  ? -18.150 -6.771  -26.641 1.00 54.21  ? 96  GLN   B N   1 
ATOM   951  C CA  . GLN   B 2 87  ? -18.203 -5.412  -27.153 1.00 53.44  ? 96  GLN   B CA  1 
ATOM   952  C C   . GLN   B 2 87  ? -18.178 -4.412  -26.005 1.00 51.94  ? 96  GLN   B C   1 
ATOM   953  O O   . GLN   B 2 87  ? -19.037 -4.457  -25.138 1.00 51.53  ? 96  GLN   B O   1 
ATOM   954  C CB  . GLN   B 2 87  ? -19.437 -5.186  -28.057 1.00 54.18  ? 96  GLN   B CB  1 
ATOM   955  C CG  . GLN   B 2 87  ? -19.132 -5.385  -29.528 1.00 57.15  ? 96  GLN   B CG  1 
ATOM   956  C CD  . GLN   B 2 87  ? -20.328 -5.153  -30.432 1.00 61.21  ? 96  GLN   B CD  1 
ATOM   957  O OE1 . GLN   B 2 87  ? -21.354 -4.593  -30.038 1.00 61.74  ? 96  GLN   B OE1 1 
ATOM   958  N NE2 . GLN   B 2 87  ? -20.219 -5.595  -31.677 1.00 61.94  ? 96  GLN   B NE2 1 
ATOM   959  N N   . LEU   B 2 88  ? -17.198 -3.509  -26.008 1.00 50.81  ? 97  LEU   B N   1 
ATOM   960  C CA  . LEU   B 2 88  ? -17.144 -2.428  -25.036 1.00 50.02  ? 97  LEU   B CA  1 
ATOM   961  C C   . LEU   B 2 88  ? -18.031 -1.331  -25.626 1.00 48.91  ? 97  LEU   B C   1 
ATOM   962  O O   . LEU   B 2 88  ? -17.694 -0.823  -26.698 1.00 49.69  ? 97  LEU   B O   1 
ATOM   963  C CB  . LEU   B 2 88  ? -15.690 -1.895  -24.905 1.00 50.09  ? 97  LEU   B CB  1 
ATOM   964  C CG  . LEU   B 2 88  ? -15.508 -0.524  -24.224 1.00 51.39  ? 97  LEU   B CG  1 
ATOM   965  C CD1 . LEU   B 2 88  ? -15.948 -0.573  -22.780 1.00 52.58  ? 97  LEU   B CD1 1 
ATOM   966  C CD2 . LEU   B 2 88  ? -14.077 -0.036  -24.323 1.00 51.60  ? 97  LEU   B CD2 1 
ATOM   967  N N   . LEU   B 2 89  ? -19.165 -1.006  -24.995 1.00 47.11  ? 98  LEU   B N   1 
ATOM   968  C CA  . LEU   B 2 89  ? -19.968 0.105   -25.481 1.00 46.62  ? 98  LEU   B CA  1 
ATOM   969  C C   . LEU   B 2 89  ? -19.327 1.331   -24.833 1.00 46.81  ? 98  LEU   B C   1 
ATOM   970  O O   . LEU   B 2 89  ? -19.722 1.743   -23.726 1.00 46.99  ? 98  LEU   B O   1 
ATOM   971  C CB  . LEU   B 2 89  ? -21.461 -0.034  -25.131 1.00 46.38  ? 98  LEU   B CB  1 
ATOM   972  C CG  . LEU   B 2 89  ? -22.373 1.209   -25.310 1.00 47.12  ? 98  LEU   B CG  1 
ATOM   973  C CD1 . LEU   B 2 89  ? -22.108 1.945   -26.604 1.00 48.10  ? 98  LEU   B CD1 1 
ATOM   974  C CD2 . LEU   B 2 89  ? -23.825 0.833   -25.231 1.00 47.19  ? 98  LEU   B CD2 1 
ATOM   975  N N   . ALA   B 2 90  ? -18.268 1.859   -25.485 1.00 46.06  ? 99  ALA   B N   1 
ATOM   976  C CA  . ALA   B 2 90  ? -17.514 2.982   -24.944 1.00 46.14  ? 99  ALA   B CA  1 
ATOM   977  C C   . ALA   B 2 90  ? -18.203 4.311   -25.141 1.00 46.41  ? 99  ALA   B C   1 
ATOM   978  O O   . ALA   B 2 90  ? -18.497 4.668   -26.278 1.00 46.74  ? 99  ALA   B O   1 
ATOM   979  C CB  . ALA   B 2 90  ? -16.130 3.038   -25.552 1.00 45.79  ? 99  ALA   B CB  1 
ATOM   980  N N   . VAL   B 2 91  ? -18.407 5.073   -24.037 1.00 45.44  ? 100 VAL   B N   1 
ATOM   981  C CA  . VAL   B 2 91  ? -18.971 6.424   -24.076 1.00 44.95  ? 100 VAL   B CA  1 
ATOM   982  C C   . VAL   B 2 91  ? -17.842 7.428   -23.709 1.00 45.32  ? 100 VAL   B C   1 
ATOM   983  O O   . VAL   B 2 91  ? -17.656 7.766   -22.546 1.00 45.11  ? 100 VAL   B O   1 
ATOM   984  C CB  . VAL   B 2 91  ? -20.189 6.553   -23.138 1.00 44.80  ? 100 VAL   B CB  1 
ATOM   985  C CG1 . VAL   B 2 91  ? -20.830 7.926   -23.261 1.00 45.28  ? 100 VAL   B CG1 1 
ATOM   986  C CG2 . VAL   B 2 91  ? -21.206 5.453   -23.403 1.00 44.64  ? 100 VAL   B CG2 1 
ATOM   987  N N   . PRO   B 2 92  ? -17.039 7.879   -24.695 1.00 45.83  ? 101 PRO   B N   1 
ATOM   988  C CA  . PRO   B 2 92  ? -15.914 8.786   -24.369 1.00 46.49  ? 101 PRO   B CA  1 
ATOM   989  C C   . PRO   B 2 92  ? -16.287 10.262  -24.148 1.00 48.03  ? 101 PRO   B C   1 
ATOM   990  O O   . PRO   B 2 92  ? -17.281 10.750  -24.696 1.00 48.28  ? 101 PRO   B O   1 
ATOM   991  C CB  . PRO   B 2 92  ? -14.969 8.599   -25.553 1.00 46.29  ? 101 PRO   B CB  1 
ATOM   992  C CG  . PRO   B 2 92  ? -15.854 8.171   -26.663 1.00 46.26  ? 101 PRO   B CG  1 
ATOM   993  C CD  . PRO   B 2 92  ? -17.084 7.553   -26.135 1.00 44.59  ? 101 PRO   B CD  1 
ATOM   994  N N   . PRO   B 2 93  ? -15.502 10.998  -23.334 1.00 48.87  ? 102 PRO   B N   1 
ATOM   995  C CA  . PRO   B 2 93  ? -15.829 12.414  -23.086 1.00 49.63  ? 102 PRO   B CA  1 
ATOM   996  C C   . PRO   B 2 93  ? -15.910 13.242  -24.369 1.00 51.04  ? 102 PRO   B C   1 
ATOM   997  O O   . PRO   B 2 93  ? -15.069 13.080  -25.254 1.00 51.80  ? 102 PRO   B O   1 
ATOM   998  C CB  . PRO   B 2 93  ? -14.684 12.890  -22.176 1.00 49.99  ? 102 PRO   B CB  1 
ATOM   999  C CG  . PRO   B 2 93  ? -14.156 11.661  -21.541 1.00 50.12  ? 102 PRO   B CG  1 
ATOM   1000 C CD  . PRO   B 2 93  ? -14.320 10.571  -22.560 1.00 48.53  ? 102 PRO   B CD  1 
ATOM   1001 N N   . GLY   B 2 94  ? -16.944 14.077  -24.485 1.00 51.11  ? 103 GLY   B N   1 
ATOM   1002 C CA  . GLY   B 2 94  ? -17.157 14.924  -25.655 1.00 51.81  ? 103 GLY   B CA  1 
ATOM   1003 C C   . GLY   B 2 94  ? -17.393 14.189  -26.968 1.00 52.76  ? 103 GLY   B C   1 
ATOM   1004 O O   . GLY   B 2 94  ? -17.396 14.800  -28.048 1.00 52.98  ? 103 GLY   B O   1 
ATOM   1005 N N   . GLU   B 2 95  ? -17.554 12.865  -26.900 1.00 52.83  ? 104 GLU   B N   1 
ATOM   1006 C CA  . GLU   B 2 95  ? -17.763 12.058  -28.091 1.00 53.47  ? 104 GLU   B CA  1 
ATOM   1007 C C   . GLU   B 2 95  ? -18.944 11.119  -27.905 1.00 53.55  ? 104 GLU   B C   1 
ATOM   1008 O O   . GLU   B 2 95  ? -19.279 10.752  -26.774 1.00 53.75  ? 104 GLU   B O   1 
ATOM   1009 C CB  . GLU   B 2 95  ? -16.485 11.274  -28.433 1.00 56.30  ? 104 GLU   B CB  1 
ATOM   1010 C CG  . GLU   B 2 95  ? -15.300 12.171  -28.747 1.00 61.91  ? 104 GLU   B CG  1 
ATOM   1011 C CD  . GLU   B 2 95  ? -13.933 11.543  -28.569 1.00 69.67  ? 104 GLU   B CD  1 
ATOM   1012 O OE1 . GLU   B 2 95  ? -13.868 10.355  -28.182 1.00 70.45  ? 104 GLU   B OE1 1 
ATOM   1013 O OE2 . GLU   B 2 95  ? -12.922 12.238  -28.822 1.00 73.09  ? 104 GLU   B OE2 1 
ATOM   1014 N N   . ARG   B 2 96  ? -19.562 10.725  -29.017 1.00 53.22  ? 105 ARG   B N   1 
ATOM   1015 C CA  . ARG   B 2 96  ? -20.710 9.830   -29.079 1.00 54.29  ? 105 ARG   B CA  1 
ATOM   1016 C C   . ARG   B 2 96  ? -20.371 8.406   -28.617 1.00 54.81  ? 105 ARG   B C   1 
ATOM   1017 O O   . ARG   B 2 96  ? -19.215 7.987   -28.746 1.00 55.50  ? 105 ARG   B O   1 
ATOM   1018 C CB  . ARG   B 2 96  ? -21.164 9.779   -30.539 1.00 56.82  ? 105 ARG   B CB  1 
ATOM   1019 C CG  . ARG   B 2 96  ? -22.595 9.336   -30.764 1.00 61.98  ? 105 ARG   B CG  1 
ATOM   1020 C CD  . ARG   B 2 96  ? -23.275 10.212  -31.802 1.00 67.41  ? 105 ARG   B CD  1 
ATOM   1021 N NE  . ARG   B 2 96  ? -22.575 10.253  -33.091 1.00 72.52  ? 105 ARG   B NE  1 
ATOM   1022 C CZ  . ARG   B 2 96  ? -22.109 11.363  -33.661 1.00 76.74  ? 105 ARG   B CZ  1 
ATOM   1023 N NH1 . ARG   B 2 96  ? -22.253 12.538  -33.058 1.00 76.98  ? 105 ARG   B NH1 1 
ATOM   1024 N NH2 . ARG   B 2 96  ? -21.499 11.307  -34.838 1.00 77.20  ? 105 ARG   B NH2 1 
ATOM   1025 N N   . ALA   B 2 97  ? -21.376 7.643   -28.116 1.00 54.28  ? 106 ALA   B N   1 
ATOM   1026 C CA  . ALA   B 2 97  ? -21.175 6.238   -27.728 1.00 54.34  ? 106 ALA   B CA  1 
ATOM   1027 C C   . ALA   B 2 97  ? -20.735 5.421   -28.965 1.00 55.01  ? 106 ALA   B C   1 
ATOM   1028 O O   . ALA   B 2 97  ? -21.178 5.694   -30.078 1.00 55.00  ? 106 ALA   B O   1 
ATOM   1029 C CB  . ALA   B 2 97  ? -22.452 5.660   -27.144 1.00 54.04  ? 106 ALA   B CB  1 
ATOM   1030 N N   . LYS   B 2 98  ? -19.859 4.435   -28.770 1.00 55.42  ? 107 LYS   B N   1 
ATOM   1031 C CA  . LYS   B 2 98  ? -19.253 3.654   -29.844 1.00 55.95  ? 107 LYS   B CA  1 
ATOM   1032 C C   . LYS   B 2 98  ? -19.088 2.200   -29.403 1.00 56.06  ? 107 LYS   B C   1 
ATOM   1033 O O   . LYS   B 2 98  ? -18.582 1.976   -28.310 1.00 56.26  ? 107 LYS   B O   1 
ATOM   1034 C CB  . LYS   B 2 98  ? -17.863 4.265   -30.054 1.00 58.52  ? 107 LYS   B CB  1 
ATOM   1035 C CG  . LYS   B 2 98  ? -17.167 4.036   -31.391 1.00 64.52  ? 107 LYS   B CG  1 
ATOM   1036 C CD  . LYS   B 2 98  ? -15.805 4.806   -31.418 1.00 70.41  ? 107 LYS   B CD  1 
ATOM   1037 C CE  . LYS   B 2 98  ? -15.028 4.754   -30.092 1.00 74.15  ? 107 LYS   B CE  1 
ATOM   1038 N NZ  . LYS   B 2 98  ? -13.866 5.688   -30.050 1.00 76.30  ? 107 LYS   B NZ  1 
ATOM   1039 N N   . ASN   B 2 99  ? -19.491 1.214   -30.225 1.00 55.91  ? 108 ASN   B N   1 
ATOM   1040 C CA  . ASN   B 2 99  ? -19.303 -0.198  -29.849 1.00 56.32  ? 108 ASN   B CA  1 
ATOM   1041 C C   . ASN   B 2 99  ? -17.990 -0.665  -30.413 1.00 56.76  ? 108 ASN   B C   1 
ATOM   1042 O O   . ASN   B 2 99  ? -17.783 -0.497  -31.592 1.00 57.31  ? 108 ASN   B O   1 
ATOM   1043 C CB  . ASN   B 2 99  ? -20.407 -1.090  -30.401 1.00 56.84  ? 108 ASN   B CB  1 
ATOM   1044 C CG  . ASN   B 2 99  ? -21.718 -0.936  -29.690 1.00 59.66  ? 108 ASN   B CG  1 
ATOM   1045 O OD1 . ASN   B 2 99  ? -22.238 0.171   -29.519 1.00 61.27  ? 108 ASN   B OD1 1 
ATOM   1046 N ND2 . ASN   B 2 99  ? -22.298 -2.045  -29.281 1.00 59.66  ? 108 ASN   B ND2 1 
ATOM   1047 N N   . ILE   B 2 100 ? -17.099 -1.235  -29.603 1.00 56.84  ? 109 ILE   B N   1 
ATOM   1048 C CA  . ILE   B 2 100 ? -15.807 -1.725  -30.083 1.00 57.22  ? 109 ILE   B CA  1 
ATOM   1049 C C   . ILE   B 2 100 ? -15.666 -3.202  -29.757 1.00 58.72  ? 109 ILE   B C   1 
ATOM   1050 O O   . ILE   B 2 100 ? -15.551 -3.572  -28.588 1.00 59.24  ? 109 ILE   B O   1 
ATOM   1051 C CB  . ILE   B 2 100 ? -14.643 -0.964  -29.444 1.00 57.16  ? 109 ILE   B CB  1 
ATOM   1052 C CG1 . ILE   B 2 100 ? -14.842 0.556   -29.490 1.00 57.93  ? 109 ILE   B CG1 1 
ATOM   1053 C CG2 . ILE   B 2 100 ? -13.334 -1.408  -30.064 1.00 57.44  ? 109 ILE   B CG2 1 
ATOM   1054 C CD1 . ILE   B 2 100 ? -14.779 1.154   -30.860 1.00 59.33  ? 109 ILE   B CD1 1 
ATOM   1055 N N   . GLN   B 2 101 ? -15.649 -4.043  -30.770 1.00 59.51  ? 110 GLN   B N   1 
ATOM   1056 C CA  . GLN   B 2 101 ? -15.541 -5.485  -30.589 1.00 60.95  ? 110 GLN   B CA  1 
ATOM   1057 C C   . GLN   B 2 101 ? -14.092 -5.934  -30.340 1.00 62.23  ? 110 GLN   B C   1 
ATOM   1058 O O   . GLN   B 2 101 ? -13.175 -5.507  -31.045 1.00 62.73  ? 110 GLN   B O   1 
ATOM   1059 C CB  . GLN   B 2 101 ? -16.103 -6.189  -31.830 1.00 62.88  ? 110 GLN   B CB  1 
ATOM   1060 C CG  . GLN   B 2 101 ? -16.192 -7.695  -31.700 1.00 66.08  ? 110 GLN   B CG  1 
ATOM   1061 C CD  . GLN   B 2 101 ? -17.329 -8.216  -32.521 1.00 69.39  ? 110 GLN   B CD  1 
ATOM   1062 O OE1 . GLN   B 2 101 ? -18.406 -7.621  -32.573 1.00 70.23  ? 110 GLN   B OE1 1 
ATOM   1063 N NE2 . GLN   B 2 101 ? -17.118 -9.342  -33.174 1.00 70.16  ? 110 GLN   B NE2 1 
ATOM   1064 N N   . THR   B 2 102 ? -13.887 -6.818  -29.357 1.00 62.42  ? 111 THR   B N   1 
ATOM   1065 C CA  . THR   B 2 102 ? -12.563 -7.344  -29.041 1.00 63.22  ? 111 THR   B CA  1 
ATOM   1066 C C   . THR   B 2 102 ? -12.675 -8.734  -28.402 1.00 64.29  ? 111 THR   B C   1 
ATOM   1067 O O   . THR   B 2 102 ? -13.757 -9.105  -27.928 1.00 64.90  ? 111 THR   B O   1 
ATOM   1068 C CB  . THR   B 2 102 ? -11.821 -6.379  -28.091 1.00 64.58  ? 111 THR   B CB  1 
ATOM   1069 O OG1 . THR   B 2 102 ? -10.433 -6.711  -28.073 1.00 65.73  ? 111 THR   B OG1 1 
ATOM   1070 C CG2 . THR   B 2 102 ? -12.383 -6.394  -26.660 1.00 64.98  ? 111 THR   B CG2 1 
ATOM   1071 N N   . LEU   B 2 103 ? -11.560 -9.507  -28.372 1.00 64.11  ? 112 LEU   B N   1 
ATOM   1072 C CA  . LEU   B 2 103 ? -11.573 -10.782 -27.662 1.00 64.20  ? 112 LEU   B CA  1 
ATOM   1073 C C   . LEU   B 2 103 ? -10.847 -10.553 -26.350 1.00 63.93  ? 112 LEU   B C   1 
ATOM   1074 O O   . LEU   B 2 103 ? -9.703  -10.093 -26.348 1.00 64.20  ? 112 LEU   B O   1 
ATOM   1075 C CB  . LEU   B 2 103 ? -10.928 -11.934 -28.421 1.00 64.51  ? 112 LEU   B CB  1 
ATOM   1076 C CG  . LEU   B 2 103 ? -11.066 -13.251 -27.653 1.00 66.34  ? 112 LEU   B CG  1 
ATOM   1077 C CD1 . LEU   B 2 103 ? -12.428 -13.869 -27.876 1.00 67.01  ? 112 LEU   B CD1 1 
ATOM   1078 C CD2 . LEU   B 2 103 ? -9.942  -14.202 -27.953 1.00 66.90  ? 112 LEU   B CD2 1 
ATOM   1079 N N   . PRO   B 2 104 ? -11.479 -10.880 -25.222 1.00 63.28  ? 113 PRO   B N   1 
ATOM   1080 C CA  . PRO   B 2 104 ? -10.852 -10.577 -23.931 1.00 62.81  ? 113 PRO   B CA  1 
ATOM   1081 C C   . PRO   B 2 104 ? -9.621  -11.389 -23.560 1.00 62.26  ? 113 PRO   B C   1 
ATOM   1082 O O   . PRO   B 2 104 ? -9.388  -12.505 -24.026 1.00 62.70  ? 113 PRO   B O   1 
ATOM   1083 C CB  . PRO   B 2 104 ? -11.984 -10.772 -22.915 1.00 63.60  ? 113 PRO   B CB  1 
ATOM   1084 C CG  . PRO   B 2 104 ? -13.234 -10.758 -23.711 1.00 64.41  ? 113 PRO   B CG  1 
ATOM   1085 C CD  . PRO   B 2 104 ? -12.857 -11.364 -25.047 1.00 62.84  ? 113 PRO   B CD  1 
ATOM   1086 N N   . GLY   B 2 105 ? -8.819  -10.763 -22.720 1.00 61.15  ? 114 GLY   B N   1 
ATOM   1087 C CA  . GLY   B 2 105 ? -7.607  -11.329 -22.157 1.00 60.08  ? 114 GLY   B CA  1 
ATOM   1088 C C   . GLY   B 2 105 ? -7.890  -11.939 -20.803 1.00 58.44  ? 114 GLY   B C   1 
ATOM   1089 O O   . GLY   B 2 105 ? -9.035  -12.280 -20.490 1.00 58.38  ? 114 GLY   B O   1 
ATOM   1090 N N   . ILE   B 2 106 ? -6.857  -12.076 -19.985 1.00 57.06  ? 115 ILE   B N   1 
ATOM   1091 C CA  . ILE   B 2 106 ? -6.980  -12.744 -18.704 1.00 56.44  ? 115 ILE   B CA  1 
ATOM   1092 C C   . ILE   B 2 106 ? -6.168  -12.055 -17.611 1.00 55.89  ? 115 ILE   B C   1 
ATOM   1093 O O   . ILE   B 2 106 ? -5.027  -11.658 -17.826 1.00 56.14  ? 115 ILE   B O   1 
ATOM   1094 C CB  . ILE   B 2 106 ? -6.567  -14.234 -18.942 1.00 57.13  ? 115 ILE   B CB  1 
ATOM   1095 C CG1 . ILE   B 2 106 ? -7.764  -15.102 -19.351 1.00 57.83  ? 115 ILE   B CG1 1 
ATOM   1096 C CG2 . ILE   B 2 106 ? -5.787  -14.875 -17.793 1.00 58.13  ? 115 ILE   B CG2 1 
ATOM   1097 C CD1 . ILE   B 2 106 ? -8.791  -15.174 -18.360 1.00 59.03  ? 115 ILE   B CD1 1 
ATOM   1098 N N   . PHE   B 2 107 ? -6.761  -11.920 -16.440 1.00 55.14  ? 116 PHE   B N   1 
ATOM   1099 C CA  . PHE   B 2 107 ? -6.081  -11.398 -15.280 1.00 55.18  ? 116 PHE   B CA  1 
ATOM   1100 C C   . PHE   B 2 107 ? -5.988  -12.584 -14.360 1.00 55.66  ? 116 PHE   B C   1 
ATOM   1101 O O   . PHE   B 2 107 ? -6.978  -12.933 -13.726 1.00 55.88  ? 116 PHE   B O   1 
ATOM   1102 C CB  . PHE   B 2 107 ? -6.903  -10.296 -14.605 1.00 54.98  ? 116 PHE   B CB  1 
ATOM   1103 C CG  . PHE   B 2 107 ? -6.617  -8.876  -15.040 1.00 55.44  ? 116 PHE   B CG  1 
ATOM   1104 C CD1 . PHE   B 2 107 ? -5.865  -8.615  -16.178 1.00 55.95  ? 116 PHE   B CD1 1 
ATOM   1105 C CD2 . PHE   B 2 107 ? -7.131  -7.801  -14.331 1.00 55.79  ? 116 PHE   B CD2 1 
ATOM   1106 C CE1 . PHE   B 2 107 ? -5.610  -7.309  -16.575 1.00 56.43  ? 116 PHE   B CE1 1 
ATOM   1107 C CE2 . PHE   B 2 107 ? -6.873  -6.499  -14.734 1.00 56.32  ? 116 PHE   B CE2 1 
ATOM   1108 C CZ  . PHE   B 2 107 ? -6.122  -6.262  -15.856 1.00 56.21  ? 116 PHE   B CZ  1 
ATOM   1109 N N   . LYS   B 2 108 ? -4.841  -13.258 -14.345 1.00 55.62  ? 117 LYS   B N   1 
ATOM   1110 C CA  . LYS   B 2 108 ? -4.612  -14.396 -13.475 1.00 56.23  ? 117 LYS   B CA  1 
ATOM   1111 C C   . LYS   B 2 108 ? -4.217  -13.877 -12.095 1.00 56.41  ? 117 LYS   B C   1 
ATOM   1112 O O   . LYS   B 2 108 ? -3.161  -13.267 -11.949 1.00 56.35  ? 117 LYS   B O   1 
ATOM   1113 C CB  . LYS   B 2 108 ? -3.491  -15.274 -14.039 1.00 58.71  ? 117 LYS   B CB  1 
ATOM   1114 C CG  . LYS   B 2 108 ? -3.970  -16.428 -14.911 1.00 63.92  ? 117 LYS   B CG  1 
ATOM   1115 C CD  . LYS   B 2 108 ? -3.268  -17.728 -14.513 1.00 69.38  ? 117 LYS   B CD  1 
ATOM   1116 C CE  . LYS   B 2 108 ? -3.257  -18.761 -15.618 1.00 74.60  ? 117 LYS   B CE  1 
ATOM   1117 N NZ  . LYS   B 2 108 ? -2.354  -19.913 -15.307 1.00 77.46  ? 117 LYS   B NZ  1 
ATOM   1118 N N   . THR   B 2 109 ? -5.079  -14.083 -11.093 1.00 56.61  ? 118 THR   B N   1 
ATOM   1119 C CA  . THR   B 2 109 ? -4.852  -13.648 -9.710  1.00 57.16  ? 118 THR   B CA  1 
ATOM   1120 C C   . THR   B 2 109 ? -4.817  -14.880 -8.776  1.00 58.32  ? 118 THR   B C   1 
ATOM   1121 O O   . THR   B 2 109 ? -5.109  -15.990 -9.214  1.00 58.81  ? 118 THR   B O   1 
ATOM   1122 C CB  . THR   B 2 109 ? -5.950  -12.618 -9.259  1.00 57.82  ? 118 THR   B CB  1 
ATOM   1123 O OG1 . THR   B 2 109 ? -7.186  -13.282 -8.988  1.00 58.37  ? 118 THR   B OG1 1 
ATOM   1124 C CG2 . THR   B 2 109 ? -6.163  -11.493 -10.244 1.00 58.14  ? 118 THR   B CG2 1 
ATOM   1125 N N   . LYS   B 2 110 ? -4.471  -14.694 -7.493  1.00 58.77  ? 119 LYS   B N   1 
ATOM   1126 C CA  . LYS   B 2 110 ? -4.485  -15.785 -6.521  1.00 59.66  ? 119 LYS   B CA  1 
ATOM   1127 C C   . LYS   B 2 110 ? -5.938  -16.243 -6.226  1.00 60.66  ? 119 LYS   B C   1 
ATOM   1128 O O   . LYS   B 2 110 ? -6.177  -17.435 -6.024  1.00 60.98  ? 119 LYS   B O   1 
ATOM   1129 C CB  . LYS   B 2 110 ? -3.750  -15.376 -5.232  1.00 60.74  ? 119 LYS   B CB  1 
ATOM   1130 C CG  . LYS   B 2 110 ? -4.136  -13.999 -4.690  1.00 64.63  ? 119 LYS   B CG  1 
ATOM   1131 C CD  . LYS   B 2 110 ? -3.191  -13.544 -3.559  1.00 68.52  ? 119 LYS   B CD  1 
ATOM   1132 C CE  . LYS   B 2 110 ? -3.873  -12.744 -2.470  1.00 71.53  ? 119 LYS   B CE  1 
ATOM   1133 N NZ  . LYS   B 2 110 ? -3.946  -11.292 -2.789  1.00 73.60  ? 119 LYS   B NZ  1 
ATOM   1134 N N   . ASP   B 2 111 ? -6.911  -15.299 -6.270  1.00 60.66  ? 120 ASP   B N   1 
ATOM   1135 C CA  . ASP   B 2 111 ? -8.326  -15.569 -6.008  1.00 60.70  ? 120 ASP   B CA  1 
ATOM   1136 C C   . ASP   B 2 111 ? -9.119  -16.081 -7.211  1.00 60.88  ? 120 ASP   B C   1 
ATOM   1137 O O   . ASP   B 2 111 ? -10.260 -16.499 -7.041  1.00 61.41  ? 120 ASP   B O   1 
ATOM   1138 C CB  . ASP   B 2 111 ? -9.013  -14.320 -5.459  1.00 62.00  ? 120 ASP   B CB  1 
ATOM   1139 C CG  . ASP   B 2 111 ? -8.435  -13.808 -4.163  1.00 64.95  ? 120 ASP   B CG  1 
ATOM   1140 O OD1 . ASP   B 2 111 ? -7.803  -14.606 -3.441  1.00 64.45  ? 120 ASP   B OD1 1 
ATOM   1141 O OD2 . ASP   B 2 111 ? -8.622  -12.606 -3.867  1.00 67.26  ? 120 ASP   B OD2 1 
ATOM   1142 N N   . GLY   B 2 112 ? -8.549  -16.017 -8.404  1.00 60.30  ? 121 GLY   B N   1 
ATOM   1143 C CA  . GLY   B 2 112 ? -9.230  -16.495 -9.600  1.00 60.34  ? 121 GLY   B CA  1 
ATOM   1144 C C   . GLY   B 2 112 ? -8.882  -15.718 -10.846 1.00 60.28  ? 121 GLY   B C   1 
ATOM   1145 O O   . GLY   B 2 112 ? -8.268  -14.658 -10.753 1.00 60.75  ? 121 GLY   B O   1 
ATOM   1146 N N   . ASP   B 2 113 ? -9.271  -16.230 -12.019 1.00 59.66  ? 122 ASP   B N   1 
ATOM   1147 C CA  . ASP   B 2 113 ? -9.000  -15.539 -13.279 1.00 59.81  ? 122 ASP   B CA  1 
ATOM   1148 C C   . ASP   B 2 113 ? -10.163 -14.616 -13.617 1.00 59.41  ? 122 ASP   B C   1 
ATOM   1149 O O   . ASP   B 2 113 ? -11.324 -14.988 -13.456 1.00 59.90  ? 122 ASP   B O   1 
ATOM   1150 C CB  . ASP   B 2 113 ? -8.781  -16.530 -14.441 1.00 61.85  ? 122 ASP   B CB  1 
ATOM   1151 C CG  . ASP   B 2 113 ? -7.543  -17.400 -14.333 1.00 67.91  ? 122 ASP   B CG  1 
ATOM   1152 O OD1 . ASP   B 2 113 ? -7.015  -17.548 -13.210 1.00 69.18  ? 122 ASP   B OD1 1 
ATOM   1153 O OD2 . ASP   B 2 113 ? -7.114  -17.951 -15.368 1.00 70.98  ? 122 ASP   B OD2 1 
ATOM   1154 N N   . ILE   B 2 114 ? -9.858  -13.413 -14.083 1.00 58.21  ? 123 ILE   B N   1 
ATOM   1155 C CA  . ILE   B 2 114 ? -10.894 -12.449 -14.473 1.00 57.47  ? 123 ILE   B CA  1 
ATOM   1156 C C   . ILE   B 2 114 ? -10.655 -12.102 -15.951 1.00 56.70  ? 123 ILE   B C   1 
ATOM   1157 O O   . ILE   B 2 114 ? -9.553  -12.303 -16.464 1.00 56.74  ? 123 ILE   B O   1 
ATOM   1158 C CB  . ILE   B 2 114 ? -10.924 -11.155 -13.593 1.00 57.70  ? 123 ILE   B CB  1 
ATOM   1159 C CG1 . ILE   B 2 114 ? -10.339 -11.343 -12.199 1.00 59.27  ? 123 ILE   B CG1 1 
ATOM   1160 C CG2 . ILE   B 2 114 ? -12.316 -10.600 -13.481 1.00 57.91  ? 123 ILE   B CG2 1 
ATOM   1161 C CD1 . ILE   B 2 114 ? -9.798  -10.107 -11.636 1.00 61.25  ? 123 ILE   B CD1 1 
ATOM   1162 N N   . GLY   B 2 115 ? -11.677 -11.605 -16.625 1.00 55.75  ? 124 GLY   B N   1 
ATOM   1163 C CA  . GLY   B 2 115 ? -11.527 -11.180 -18.010 1.00 55.85  ? 124 GLY   B CA  1 
ATOM   1164 C C   . GLY   B 2 115 ? -10.769 -9.867  -18.089 1.00 55.48  ? 124 GLY   B C   1 
ATOM   1165 O O   . GLY   B 2 115 ? -10.599 -9.171  -17.076 1.00 55.23  ? 124 GLY   B O   1 
ATOM   1166 N N   . ALA   B 2 116 ? -10.310 -9.510  -19.297 1.00 54.94  ? 125 ALA   B N   1 
ATOM   1167 C CA  . ALA   B 2 116 ? -9.605  -8.240  -19.484 1.00 54.99  ? 125 ALA   B CA  1 
ATOM   1168 C C   . ALA   B 2 116 ? -9.806  -7.653  -20.883 1.00 54.62  ? 125 ALA   B C   1 
ATOM   1169 O O   . ALA   B 2 116 ? -10.092 -8.370  -21.822 1.00 54.83  ? 125 ALA   B O   1 
ATOM   1170 C CB  . ALA   B 2 116 ? -8.126  -8.368  -19.139 1.00 55.06  ? 125 ALA   B CB  1 
ATOM   1171 N N   . VAL   B 2 117 ? -9.689  -6.341  -21.009 1.00 54.08  ? 126 VAL   B N   1 
ATOM   1172 C CA  A VAL   B 2 117 ? -9.854  -5.646  -22.283 0.50 54.23  ? 126 VAL   B CA  1 
ATOM   1173 C CA  B VAL   B 2 117 ? -9.882  -5.640  -22.267 0.50 54.25  ? 126 VAL   B CA  1 
ATOM   1174 C C   . VAL   B 2 117 ? -8.673  -4.709  -22.511 1.00 54.73  ? 126 VAL   B C   1 
ATOM   1175 O O   . VAL   B 2 117 ? -8.342  -3.882  -21.652 1.00 54.73  ? 126 VAL   B O   1 
ATOM   1176 C CB  A VAL   B 2 117 ? -11.220 -4.921  -22.435 0.50 54.51  ? 126 VAL   B CB  1 
ATOM   1177 C CB  B VAL   B 2 117 ? -11.275 -4.935  -22.231 0.50 54.60  ? 126 VAL   B CB  1 
ATOM   1178 C CG1 A VAL   B 2 117 ? -12.327 -5.895  -22.822 0.50 54.77  ? 126 VAL   B CG1 1 
ATOM   1179 C CG1 B VAL   B 2 117 ? -11.268 -3.552  -22.864 0.50 55.24  ? 126 VAL   B CG1 1 
ATOM   1180 C CG2 A VAL   B 2 117 ? -11.589 -4.143  -21.177 0.50 55.03  ? 126 VAL   B CG2 1 
ATOM   1181 C CG2 B VAL   B 2 117 ? -12.356 -5.818  -22.842 0.50 54.76  ? 126 VAL   B CG2 1 
ATOM   1182 N N   . ALA   B 2 118 ? -7.987  -4.880  -23.649 1.00 55.05  ? 127 ALA   B N   1 
ATOM   1183 C CA  . ALA   B 2 118 ? -6.831  -4.056  -23.949 1.00 55.76  ? 127 ALA   B CA  1 
ATOM   1184 C C   . ALA   B 2 118 ? -7.240  -2.966  -24.899 1.00 56.27  ? 127 ALA   B C   1 
ATOM   1185 O O   . ALA   B 2 118 ? -6.896  -2.985  -26.081 1.00 57.52  ? 127 ALA   B O   1 
ATOM   1186 C CB  . ALA   B 2 118 ? -5.715  -4.902  -24.519 1.00 56.19  ? 127 ALA   B CB  1 
ATOM   1187 N N   . LEU   B 2 119 ? -8.070  -2.050  -24.389 1.00 55.68  ? 128 LEU   B N   1 
ATOM   1188 C CA  . LEU   B 2 119 ? -8.583  -0.892  -25.115 1.00 55.62  ? 128 LEU   B CA  1 
ATOM   1189 C C   . LEU   B 2 119 ? -8.272  0.332   -24.262 1.00 55.62  ? 128 LEU   B C   1 
ATOM   1190 O O   . LEU   B 2 119 ? -8.579  0.332   -23.063 1.00 55.75  ? 128 LEU   B O   1 
ATOM   1191 C CB  . LEU   B 2 119 ? -10.094 -1.034  -25.364 1.00 55.73  ? 128 LEU   B CB  1 
ATOM   1192 C CG  . LEU   B 2 119 ? -10.497 -2.217  -26.265 1.00 57.29  ? 128 LEU   B CG  1 
ATOM   1193 C CD1 . LEU   B 2 119 ? -11.998 -2.453  -26.248 1.00 57.74  ? 128 LEU   B CD1 1 
ATOM   1194 C CD2 . LEU   B 2 119 ? -9.954  -2.055  -27.696 1.00 57.59  ? 128 LEU   B CD2 1 
ATOM   1195 N N   . ASP   B 2 120 ? -7.587  1.335   -24.840 1.00 55.35  ? 129 ASP   B N   1 
ATOM   1196 C CA  . ASP   B 2 120 ? -7.195  2.510   -24.073 1.00 55.83  ? 129 ASP   B CA  1 
ATOM   1197 C C   . ASP   B 2 120 ? -8.007  3.732   -24.402 1.00 55.66  ? 129 ASP   B C   1 
ATOM   1198 O O   . ASP   B 2 120 ? -7.966  4.221   -25.506 1.00 55.89  ? 129 ASP   B O   1 
ATOM   1199 C CB  . ASP   B 2 120 ? -5.692  2.799   -24.177 1.00 58.23  ? 129 ASP   B CB  1 
ATOM   1200 C CG  . ASP   B 2 120 ? -5.101  3.360   -22.885 1.00 65.04  ? 129 ASP   B CG  1 
ATOM   1201 O OD1 . ASP   B 2 120 ? -5.885  3.849   -22.024 1.00 65.03  ? 129 ASP   B OD1 1 
ATOM   1202 O OD2 . ASP   B 2 120 ? -3.857  3.299   -22.724 1.00 68.56  ? 129 ASP   B OD2 1 
ATOM   1203 N N   . TYR   B 2 121 ? -8.730  4.239   -23.427 1.00 55.69  ? 130 TYR   B N   1 
ATOM   1204 C CA  . TYR   B 2 121 ? -9.609  5.389   -23.599 1.00 55.91  ? 130 TYR   B CA  1 
ATOM   1205 C C   . TYR   B 2 121 ? -9.324  6.461   -22.552 1.00 55.25  ? 130 TYR   B C   1 
ATOM   1206 O O   . TYR   B 2 121 ? -8.686  6.155   -21.547 1.00 55.70  ? 130 TYR   B O   1 
ATOM   1207 C CB  . TYR   B 2 121 ? -11.066 4.902   -23.500 1.00 56.27  ? 130 TYR   B CB  1 
ATOM   1208 C CG  . TYR   B 2 121 ? -11.511 4.253   -24.784 1.00 57.09  ? 130 TYR   B CG  1 
ATOM   1209 C CD1 . TYR   B 2 121 ? -12.004 5.012   -25.831 1.00 57.98  ? 130 TYR   B CD1 1 
ATOM   1210 C CD2 . TYR   B 2 121 ? -11.403 2.882   -24.968 1.00 58.01  ? 130 TYR   B CD2 1 
ATOM   1211 C CE1 . TYR   B 2 121 ? -12.358 4.430   -27.038 1.00 59.28  ? 130 TYR   B CE1 1 
ATOM   1212 C CE2 . TYR   B 2 121 ? -11.781 2.283   -26.162 1.00 59.06  ? 130 TYR   B CE2 1 
ATOM   1213 C CZ  . TYR   B 2 121 ? -12.242 3.064   -27.205 1.00 60.05  ? 130 TYR   B CZ  1 
ATOM   1214 O OH  . TYR   B 2 121 ? -12.590 2.501   -28.412 1.00 61.13  ? 130 TYR   B OH  1 
ATOM   1215 N N   . PRO   B 2 122 ? -9.764  7.723   -22.744 1.00 53.89  ? 131 PRO   B N   1 
ATOM   1216 C CA  . PRO   B 2 122 ? -9.518  8.748   -21.708 1.00 53.16  ? 131 PRO   B CA  1 
ATOM   1217 C C   . PRO   B 2 122 ? -10.209 8.355   -20.401 1.00 52.39  ? 131 PRO   B C   1 
ATOM   1218 O O   . PRO   B 2 122 ? -11.326 7.867   -20.481 1.00 52.86  ? 131 PRO   B O   1 
ATOM   1219 C CB  . PRO   B 2 122 ? -10.133 10.012  -22.309 1.00 54.24  ? 131 PRO   B CB  1 
ATOM   1220 C CG  . PRO   B 2 122 ? -10.290 9.729   -23.774 1.00 54.83  ? 131 PRO   B CG  1 
ATOM   1221 C CD  . PRO   B 2 122 ? -10.543 8.264   -23.871 1.00 53.24  ? 131 PRO   B CD  1 
ATOM   1222 N N   . ALA   B 2 123 ? -9.547  8.507   -19.223 1.00 51.08  ? 132 ALA   B N   1 
ATOM   1223 C CA  . ALA   B 2 123 ? -10.043 8.069   -17.898 1.00 50.37  ? 132 ALA   B CA  1 
ATOM   1224 C C   . ALA   B 2 123 ? -11.525 8.390   -17.578 1.00 49.32  ? 132 ALA   B C   1 
ATOM   1225 O O   . ALA   B 2 123 ? -12.105 7.723   -16.712 1.00 49.75  ? 132 ALA   B O   1 
ATOM   1226 C CB  . ALA   B 2 123 ? -9.152  8.595   -16.781 1.00 50.46  ? 132 ALA   B CB  1 
ATOM   1227 N N   . GLY   B 2 124 ? -12.111 9.376   -18.279 1.00 47.20  ? 133 GLY   B N   1 
ATOM   1228 C CA  . GLY   B 2 124 ? -13.519 9.753   -18.171 1.00 45.30  ? 133 GLY   B CA  1 
ATOM   1229 C C   . GLY   B 2 124 ? -14.478 8.717   -18.737 1.00 42.83  ? 133 GLY   B C   1 
ATOM   1230 O O   . GLY   B 2 124 ? -15.685 8.801   -18.521 1.00 42.22  ? 133 GLY   B O   1 
ATOM   1231 N N   . THR   B 2 125 ? -13.956 7.739   -19.483 1.00 41.44  ? 134 THR   B N   1 
ATOM   1232 C CA  . THR   B 2 125 ? -14.726 6.634   -20.056 1.00 40.92  ? 134 THR   B CA  1 
ATOM   1233 C C   . THR   B 2 125 ? -14.989 5.539   -18.978 1.00 40.21  ? 134 THR   B C   1 
ATOM   1234 O O   . THR   B 2 125 ? -15.821 4.667   -19.204 1.00 40.96  ? 134 THR   B O   1 
ATOM   1235 C CB  . THR   B 2 125 ? -14.050 6.117   -21.371 1.00 42.12  ? 134 THR   B CB  1 
ATOM   1236 O OG1 . THR   B 2 125 ? -13.606 7.231   -22.160 1.00 43.39  ? 134 THR   B OG1 1 
ATOM   1237 C CG2 . THR   B 2 125 ? -14.974 5.255   -22.234 1.00 42.11  ? 134 THR   B CG2 1 
ATOM   1238 N N   . SER   B 2 126 ? -14.321 5.602   -17.798 1.00 38.63  ? 135 SER   B N   1 
ATOM   1239 C CA  . SER   B 2 126 ? -14.496 4.654   -16.696 1.00 37.95  ? 135 SER   B CA  1 
ATOM   1240 C C   . SER   B 2 126 ? -15.950 4.471   -16.327 1.00 37.53  ? 135 SER   B C   1 
ATOM   1241 O O   . SER   B 2 126 ? -16.625 5.433   -16.003 1.00 37.15  ? 135 SER   B O   1 
ATOM   1242 C CB  . SER   B 2 126 ? -13.754 5.136   -15.460 1.00 38.53  ? 135 SER   B CB  1 
ATOM   1243 O OG  . SER   B 2 126 ? -12.413 4.683   -15.421 1.00 39.96  ? 135 SER   B OG  1 
ATOM   1244 N N   . GLY   B 2 127 ? -16.405 3.235   -16.376 1.00 37.41  ? 136 GLY   B N   1 
ATOM   1245 C CA  . GLY   B 2 127 ? -17.778 2.857   -16.073 1.00 37.72  ? 136 GLY   B CA  1 
ATOM   1246 C C   . GLY   B 2 127 ? -18.573 2.393   -17.280 1.00 37.83  ? 136 GLY   B C   1 
ATOM   1247 O O   . GLY   B 2 127 ? -19.760 2.083   -17.152 1.00 38.29  ? 136 GLY   B O   1 
ATOM   1248 N N   . SER   B 2 128 ? -17.935 2.331   -18.456 1.00 37.03  ? 137 SER   B N   1 
ATOM   1249 C CA  . SER   B 2 128 ? -18.568 1.890   -19.690 1.00 37.25  ? 137 SER   B CA  1 
ATOM   1250 C C   . SER   B 2 128 ? -18.823 0.381   -19.689 1.00 37.73  ? 137 SER   B C   1 
ATOM   1251 O O   . SER   B 2 128 ? -17.948 -0.402  -19.337 1.00 37.42  ? 137 SER   B O   1 
ATOM   1252 C CB  . SER   B 2 128 ? -17.703 2.274   -20.885 1.00 37.86  ? 137 SER   B CB  1 
ATOM   1253 O OG  . SER   B 2 128 ? -17.644 3.686   -20.990 1.00 39.30  ? 137 SER   B OG  1 
ATOM   1254 N N   . PRO   B 2 129 ? -20.037 -0.039  -20.082 1.00 38.28  ? 138 PRO   B N   1 
ATOM   1255 C CA  . PRO   B 2 129 ? -20.354 -1.475  -20.080 1.00 38.55  ? 138 PRO   B CA  1 
ATOM   1256 C C   . PRO   B 2 129 ? -19.617 -2.335  -21.096 1.00 39.11  ? 138 PRO   B C   1 
ATOM   1257 O O   . PRO   B 2 129 ? -19.175 -1.877  -22.153 1.00 39.01  ? 138 PRO   B O   1 
ATOM   1258 C CB  . PRO   B 2 129 ? -21.857 -1.499  -20.382 1.00 39.29  ? 138 PRO   B CB  1 
ATOM   1259 C CG  . PRO   B 2 129 ? -22.110 -0.233  -21.151 1.00 39.62  ? 138 PRO   B CG  1 
ATOM   1260 C CD  . PRO   B 2 129 ? -21.201 0.775   -20.495 1.00 37.90  ? 138 PRO   B CD  1 
ATOM   1261 N N   . ILE   B 2 130 ? -19.527 -3.619  -20.765 1.00 39.34  ? 139 ILE   B N   1 
ATOM   1262 C CA  . ILE   B 2 130 ? -18.953 -4.640  -21.621 1.00 39.94  ? 139 ILE   B CA  1 
ATOM   1263 C C   . ILE   B 2 130 ? -20.084 -5.613  -21.891 1.00 41.41  ? 139 ILE   B C   1 
ATOM   1264 O O   . ILE   B 2 130 ? -20.683 -6.150  -20.964 1.00 41.01  ? 139 ILE   B O   1 
ATOM   1265 C CB  . ILE   B 2 130 ? -17.733 -5.304  -20.987 1.00 39.52  ? 139 ILE   B CB  1 
ATOM   1266 C CG1 . ILE   B 2 130 ? -16.613 -4.267  -20.818 1.00 40.10  ? 139 ILE   B CG1 1 
ATOM   1267 C CG2 . ILE   B 2 130 ? -17.284 -6.485  -21.844 1.00 39.44  ? 139 ILE   B CG2 1 
ATOM   1268 C CD1 . ILE   B 2 130 ? -15.725 -4.533  -19.655 1.00 41.10  ? 139 ILE   B CD1 1 
ATOM   1269 N N   . LEU   B 2 131 ? -20.399 -5.793  -23.171 1.00 42.68  ? 140 LEU   B N   1 
ATOM   1270 C CA  . LEU   B 2 131 ? -21.537 -6.550  -23.669 1.00 44.38  ? 140 LEU   B CA  1 
ATOM   1271 C C   . LEU   B 2 131 ? -21.197 -7.894  -24.287 1.00 45.98  ? 140 LEU   B C   1 
ATOM   1272 O O   . LEU   B 2 131 ? -20.226 -8.006  -25.027 1.00 46.12  ? 140 LEU   B O   1 
ATOM   1273 C CB  . LEU   B 2 131 ? -22.270 -5.715  -24.754 1.00 44.44  ? 140 LEU   B CB  1 
ATOM   1274 C CG  . LEU   B 2 131 ? -22.339 -4.209  -24.508 1.00 45.63  ? 140 LEU   B CG  1 
ATOM   1275 C CD1 . LEU   B 2 131 ? -22.856 -3.465  -25.709 1.00 45.55  ? 140 LEU   B CD1 1 
ATOM   1276 C CD2 . LEU   B 2 131 ? -23.085 -3.897  -23.203 1.00 46.47  ? 140 LEU   B CD2 1 
ATOM   1277 N N   . ASP   B 2 132 ? -22.069 -8.889  -24.045 1.00 46.71  ? 141 ASP   B N   1 
ATOM   1278 C CA  . ASP   B 2 132 ? -22.035 -10.190 -24.696 1.00 47.69  ? 141 ASP   B CA  1 
ATOM   1279 C C   . ASP   B 2 132 ? -22.918 -10.109 -25.987 1.00 49.60  ? 141 ASP   B C   1 
ATOM   1280 O O   . ASP   B 2 132 ? -23.565 -9.084  -26.207 1.00 49.13  ? 141 ASP   B O   1 
ATOM   1281 C CB  . ASP   B 2 132 ? -22.469 -11.311 -23.729 1.00 48.30  ? 141 ASP   B CB  1 
ATOM   1282 C CG  . ASP   B 2 132 ? -23.944 -11.435 -23.401 1.00 51.74  ? 141 ASP   B CG  1 
ATOM   1283 O OD1 . ASP   B 2 132 ? -24.754 -10.779 -24.065 1.00 53.17  ? 141 ASP   B OD1 1 
ATOM   1284 O OD2 . ASP   B 2 132 ? -24.284 -12.212 -22.487 1.00 53.10  ? 141 ASP   B OD2 1 
ATOM   1285 N N   . LYS   B 2 133 ? -22.970 -11.186 -26.808 1.00 51.54  ? 142 LYS   B N   1 
ATOM   1286 C CA  . LYS   B 2 133 ? -23.713 -11.258 -28.082 1.00 53.81  ? 142 LYS   B CA  1 
ATOM   1287 C C   . LYS   B 2 133 ? -25.233 -11.034 -27.959 1.00 54.60  ? 142 LYS   B C   1 
ATOM   1288 O O   . LYS   B 2 133 ? -25.912 -10.874 -28.982 1.00 54.52  ? 142 LYS   B O   1 
ATOM   1289 C CB  . LYS   B 2 133 ? -23.429 -12.569 -28.838 1.00 57.24  ? 142 LYS   B CB  1 
ATOM   1290 C CG  . LYS   B 2 133 ? -21.943 -12.938 -28.917 1.00 64.09  ? 142 LYS   B CG  1 
ATOM   1291 C CD  . LYS   B 2 133 ? -21.722 -14.177 -29.818 1.00 71.06  ? 142 LYS   B CD  1 
ATOM   1292 C CE  . LYS   B 2 133 ? -20.326 -14.768 -29.730 1.00 75.90  ? 142 LYS   B CE  1 
ATOM   1293 N NZ  . LYS   B 2 133 ? -20.156 -15.957 -30.622 1.00 78.03  ? 142 LYS   B NZ  1 
ATOM   1294 N N   . CYS   B 2 134 ? -25.761 -11.007 -26.719 1.00 54.59  ? 143 CYS   B N   1 
ATOM   1295 C CA  . CYS   B 2 134 ? -27.178 -10.697 -26.484 1.00 55.27  ? 143 CYS   B CA  1 
ATOM   1296 C C   . CYS   B 2 134 ? -27.401 -9.267  -26.003 1.00 54.26  ? 143 CYS   B C   1 
ATOM   1297 O O   . CYS   B 2 134 ? -28.542 -8.901  -25.740 1.00 54.54  ? 143 CYS   B O   1 
ATOM   1298 C CB  . CYS   B 2 134 ? -27.792 -11.678 -25.495 1.00 57.81  ? 143 CYS   B CB  1 
ATOM   1299 S SG  . CYS   B 2 134 ? -27.583 -13.407 -25.949 1.00 65.95  ? 143 CYS   B SG  1 
ATOM   1300 N N   . GLY   B 2 135 ? -26.334 -8.500  -25.817 1.00 53.08  ? 144 GLY   B N   1 
ATOM   1301 C CA  . GLY   B 2 135 ? -26.424 -7.170  -25.250 1.00 52.59  ? 144 GLY   B CA  1 
ATOM   1302 C C   . GLY   B 2 135 ? -26.564 -7.213  -23.739 1.00 51.99  ? 144 GLY   B C   1 
ATOM   1303 O O   . GLY   B 2 135 ? -26.912 -6.199  -23.135 1.00 52.70  ? 144 GLY   B O   1 
ATOM   1304 N N   . ARG   B 2 136 ? -26.313 -8.376  -23.103 1.00 50.51  ? 145 ARG   B N   1 
ATOM   1305 C CA  . ARG   B 2 136 ? -26.389 -8.479  -21.654 1.00 50.16  ? 145 ARG   B CA  1 
ATOM   1306 C C   . ARG   B 2 136 ? -25.094 -7.917  -21.047 1.00 49.01  ? 145 ARG   B C   1 
ATOM   1307 O O   . ARG   B 2 136 ? -24.013 -8.136  -21.617 1.00 49.52  ? 145 ARG   B O   1 
ATOM   1308 C CB  . ARG   B 2 136 ? -26.661 -9.924  -21.218 1.00 51.73  ? 145 ARG   B CB  1 
ATOM   1309 C CG  . ARG   B 2 136 ? -28.121 -10.301 -21.402 1.00 55.56  ? 145 ARG   B CG  1 
ATOM   1310 C CD  . ARG   B 2 136 ? -28.453 -11.647 -20.789 1.00 60.46  ? 145 ARG   B CD  1 
ATOM   1311 N NE  . ARG   B 2 136 ? -28.461 -12.699 -21.803 1.00 65.42  ? 145 ARG   B NE  1 
ATOM   1312 C CZ  . ARG   B 2 136 ? -27.504 -13.611 -21.955 1.00 67.92  ? 145 ARG   B CZ  1 
ATOM   1313 N NH1 . ARG   B 2 136 ? -26.464 -13.638 -21.128 1.00 66.99  ? 145 ARG   B NH1 1 
ATOM   1314 N NH2 . ARG   B 2 136 ? -27.584 -14.511 -22.931 1.00 67.84  ? 145 ARG   B NH2 1 
ATOM   1315 N N   . VAL   B 2 137 ? -25.201 -7.127  -19.947 1.00 46.78  ? 146 VAL   B N   1 
ATOM   1316 C CA  . VAL   B 2 137 ? -24.010 -6.531  -19.354 1.00 45.16  ? 146 VAL   B CA  1 
ATOM   1317 C C   . VAL   B 2 137 ? -23.297 -7.526  -18.499 1.00 44.31  ? 146 VAL   B C   1 
ATOM   1318 O O   . VAL   B 2 137 ? -23.869 -8.051  -17.551 1.00 44.41  ? 146 VAL   B O   1 
ATOM   1319 C CB  . VAL   B 2 137 ? -24.240 -5.199  -18.628 1.00 45.05  ? 146 VAL   B CB  1 
ATOM   1320 C CG1 . VAL   B 2 137 ? -22.909 -4.540  -18.296 1.00 44.92  ? 146 VAL   B CG1 1 
ATOM   1321 C CG2 . VAL   B 2 137 ? -25.089 -4.271  -19.479 1.00 45.70  ? 146 VAL   B CG2 1 
ATOM   1322 N N   . ILE   B 2 138 ? -22.060 -7.829  -18.878 1.00 43.31  ? 147 ILE   B N   1 
ATOM   1323 C CA  . ILE   B 2 138 ? -21.201 -8.800  -18.217 1.00 42.49  ? 147 ILE   B CA  1 
ATOM   1324 C C   . ILE   B 2 138 ? -20.073 -8.168  -17.379 1.00 42.34  ? 147 ILE   B C   1 
ATOM   1325 O O   . ILE   B 2 138 ? -19.307 -8.904  -16.766 1.00 42.61  ? 147 ILE   B O   1 
ATOM   1326 C CB  . ILE   B 2 138 ? -20.647 -9.791  -19.273 1.00 42.24  ? 147 ILE   B CB  1 
ATOM   1327 C CG1 . ILE   B 2 138 ? -19.841 -9.045  -20.348 1.00 42.44  ? 147 ILE   B CG1 1 
ATOM   1328 C CG2 . ILE   B 2 138 ? -21.781 -10.593 -19.911 1.00 42.76  ? 147 ILE   B CG2 1 
ATOM   1329 C CD1 . ILE   B 2 138 ? -19.091 -9.896  -21.265 1.00 43.28  ? 147 ILE   B CD1 1 
ATOM   1330 N N   . GLY   B 2 139 ? -19.973 -6.841  -17.357 1.00 41.92  ? 148 GLY   B N   1 
ATOM   1331 C CA  . GLY   B 2 139 ? -18.948 -6.165  -16.577 1.00 42.64  ? 148 GLY   B CA  1 
ATOM   1332 C C   . GLY   B 2 139 ? -18.717 -4.718  -16.952 1.00 43.32  ? 148 GLY   B C   1 
ATOM   1333 O O   . GLY   B 2 139 ? -19.245 -4.257  -17.954 1.00 44.06  ? 148 GLY   B O   1 
ATOM   1334 N N   . LEU   B 2 140 ? -17.940 -3.981  -16.148 1.00 43.03  ? 149 LEU   B N   1 
ATOM   1335 C CA  . LEU   B 2 140 ? -17.643 -2.582  -16.430 1.00 43.02  ? 149 LEU   B CA  1 
ATOM   1336 C C   . LEU   B 2 140 ? -16.145 -2.336  -16.639 1.00 42.73  ? 149 LEU   B C   1 
ATOM   1337 O O   . LEU   B 2 140 ? -15.297 -2.901  -15.941 1.00 43.19  ? 149 LEU   B O   1 
ATOM   1338 C CB  . LEU   B 2 140 ? -18.178 -1.662  -15.327 1.00 43.16  ? 149 LEU   B CB  1 
ATOM   1339 C CG  . LEU   B 2 140 ? -19.691 -1.603  -15.117 1.00 44.41  ? 149 LEU   B CG  1 
ATOM   1340 C CD1 . LEU   B 2 140 ? -20.044 -0.580  -14.036 1.00 44.93  ? 149 LEU   B CD1 1 
ATOM   1341 C CD2 . LEU   B 2 140 ? -20.411 -1.234  -16.381 1.00 44.99  ? 149 LEU   B CD2 1 
ATOM   1342 N N   . TYR   B 2 141 ? -15.838 -1.457  -17.585 1.00 41.69  ? 150 TYR   B N   1 
ATOM   1343 C CA  . TYR   B 2 141 ? -14.487 -1.060  -17.971 1.00 41.41  ? 150 TYR   B CA  1 
ATOM   1344 C C   . TYR   B 2 141 ? -14.052 0.164   -17.159 1.00 39.82  ? 150 TYR   B C   1 
ATOM   1345 O O   . TYR   B 2 141 ? -14.875 1.002   -16.872 1.00 39.35  ? 150 TYR   B O   1 
ATOM   1346 C CB  . TYR   B 2 141 ? -14.496 -0.747  -19.499 1.00 42.34  ? 150 TYR   B CB  1 
ATOM   1347 C CG  . TYR   B 2 141 ? -13.374 0.137   -20.000 1.00 44.19  ? 150 TYR   B CG  1 
ATOM   1348 C CD1 . TYR   B 2 141 ? -13.463 1.524   -19.924 1.00 45.20  ? 150 TYR   B CD1 1 
ATOM   1349 C CD2 . TYR   B 2 141 ? -12.221 -0.411  -20.539 1.00 46.34  ? 150 TYR   B CD2 1 
ATOM   1350 C CE1 . TYR   B 2 141 ? -12.399 2.336   -20.290 1.00 46.90  ? 150 TYR   B CE1 1 
ATOM   1351 C CE2 . TYR   B 2 141 ? -11.181 0.396   -20.991 1.00 48.06  ? 150 TYR   B CE2 1 
ATOM   1352 C CZ  . TYR   B 2 141 ? -11.277 1.773   -20.873 1.00 49.23  ? 150 TYR   B CZ  1 
ATOM   1353 O OH  . TYR   B 2 141 ? -10.248 2.564   -21.337 1.00 51.64  ? 150 TYR   B OH  1 
ATOM   1354 N N   . GLY   B 2 142 ? -12.767 0.294   -16.865 1.00 39.48  ? 151 GLY   B N   1 
ATOM   1355 C CA  . GLY   B 2 142 ? -12.248 1.454   -16.155 1.00 40.53  ? 151 GLY   B CA  1 
ATOM   1356 C C   . GLY   B 2 142 ? -11.301 1.156   -15.002 1.00 42.09  ? 151 GLY   B C   1 
ATOM   1357 O O   . GLY   B 2 142 ? -10.694 2.086   -14.459 1.00 42.40  ? 151 GLY   B O   1 
ATOM   1358 N N   . ASN   B 2 143 ? -11.167 -0.131  -14.588 1.00 42.41  ? 152 ASN   B N   1 
ATOM   1359 C CA  . ASN   B 2 143 ? -10.243 -0.491  -13.512 1.00 43.10  ? 152 ASN   B CA  1 
ATOM   1360 C C   . ASN   B 2 143 ? -9.397  -1.638  -13.978 1.00 44.62  ? 152 ASN   B C   1 
ATOM   1361 O O   . ASN   B 2 143 ? -9.920  -2.712  -14.244 1.00 44.60  ? 152 ASN   B O   1 
ATOM   1362 C CB  . ASN   B 2 143 ? -10.968 -0.872  -12.214 1.00 43.25  ? 152 ASN   B CB  1 
ATOM   1363 C CG  . ASN   B 2 143 ? -10.040 -1.051  -11.013 1.00 44.07  ? 152 ASN   B CG  1 
ATOM   1364 O OD1 . ASN   B 2 143 ? -9.069  -0.304  -10.826 1.00 43.94  ? 152 ASN   B OD1 1 
ATOM   1365 N ND2 . ASN   B 2 143 ? -10.322 -2.046  -10.165 1.00 43.81  ? 152 ASN   B ND2 1 
ATOM   1366 N N   . GLY   B 2 144 ? -8.098  -1.400  -14.073 1.00 45.81  ? 153 GLY   B N   1 
ATOM   1367 C CA  . GLY   B 2 144 ? -7.140  -2.389  -14.538 1.00 47.58  ? 153 GLY   B CA  1 
ATOM   1368 C C   . GLY   B 2 144 ? -5.706  -2.010  -14.241 1.00 49.73  ? 153 GLY   B C   1 
ATOM   1369 O O   . GLY   B 2 144 ? -5.423  -1.354  -13.236 1.00 49.65  ? 153 GLY   B O   1 
ATOM   1370 N N   . VAL   B 2 145 ? -4.795  -2.377  -15.137 1.00 51.64  ? 154 VAL   B N   1 
ATOM   1371 C CA  . VAL   B 2 145 ? -3.369  -2.169  -14.931 1.00 54.37  ? 154 VAL   B CA  1 
ATOM   1372 C C   . VAL   B 2 145 ? -2.621  -1.589  -16.163 1.00 57.77  ? 154 VAL   B C   1 
ATOM   1373 O O   . VAL   B 2 145 ? -3.115  -1.673  -17.283 1.00 58.76  ? 154 VAL   B O   1 
ATOM   1374 C CB  . VAL   B 2 145 ? -2.803  -3.539  -14.518 1.00 54.81  ? 154 VAL   B CB  1 
ATOM   1375 C CG1 . VAL   B 2 145 ? -2.846  -4.520  -15.685 1.00 54.93  ? 154 VAL   B CG1 1 
ATOM   1376 C CG2 . VAL   B 2 145 ? -1.402  -3.422  -13.931 1.00 55.60  ? 154 VAL   B CG2 1 
ATOM   1377 N N   . VAL   B 2 146 ? -1.449  -0.970  -15.953 1.00 59.38  ? 155 VAL   B N   1 
ATOM   1378 C CA  . VAL   B 2 146 ? -0.638  -0.436  -17.042 1.00 61.38  ? 155 VAL   B CA  1 
ATOM   1379 C C   . VAL   B 2 146 ? 0.449   -1.463  -17.292 1.00 64.56  ? 155 VAL   B C   1 
ATOM   1380 O O   . VAL   B 2 146 ? 1.155   -1.844  -16.359 1.00 65.16  ? 155 VAL   B O   1 
ATOM   1381 C CB  . VAL   B 2 146 ? -0.061  0.970   -16.720 1.00 61.65  ? 155 VAL   B CB  1 
ATOM   1382 C CG1 . VAL   B 2 146 ? 1.152   1.306   -17.580 1.00 62.10  ? 155 VAL   B CG1 1 
ATOM   1383 C CG2 . VAL   B 2 146 ? -1.124  2.043   -16.879 1.00 62.15  ? 155 VAL   B CG2 1 
ATOM   1384 N N   . ILE   B 2 147 ? 0.567   -1.939  -18.536 1.00 66.69  ? 156 ILE   B N   1 
ATOM   1385 C CA  . ILE   B 2 147 ? 1.582   -2.933  -18.906 1.00 68.82  ? 156 ILE   B CA  1 
ATOM   1386 C C   . ILE   B 2 147 ? 2.893   -2.282  -19.383 1.00 69.61  ? 156 ILE   B C   1 
ATOM   1387 O O   . ILE   B 2 147 ? 2.918   -1.071  -19.596 1.00 69.56  ? 156 ILE   B O   1 
ATOM   1388 C CB  . ILE   B 2 147 ? 1.010   -3.945  -19.930 1.00 70.13  ? 156 ILE   B CB  1 
ATOM   1389 C CG1 . ILE   B 2 147 ? 0.371   -3.217  -21.127 1.00 71.43  ? 156 ILE   B CG1 1 
ATOM   1390 C CG2 . ILE   B 2 147 ? 0.027   -4.901  -19.236 1.00 70.79  ? 156 ILE   B CG2 1 
ATOM   1391 C CD1 . ILE   B 2 147 ? 0.254   -4.092  -22.359 1.00 73.08  ? 156 ILE   B CD1 1 
ATOM   1392 N N   . LYS   B 2 148 ? 3.981   -3.078  -19.537 1.00 70.02  ? 157 LYS   B N   1 
ATOM   1393 C CA  . LYS   B 2 148 ? 5.297   -2.585  -19.966 1.00 70.99  ? 157 LYS   B CA  1 
ATOM   1394 C C   . LYS   B 2 148 ? 5.254   -1.766  -21.270 1.00 71.01  ? 157 LYS   B C   1 
ATOM   1395 O O   . LYS   B 2 148 ? 6.133   -0.943  -21.510 1.00 71.00  ? 157 LYS   B O   1 
ATOM   1396 C CB  . LYS   B 2 148 ? 6.328   -3.727  -20.035 1.00 73.92  ? 157 LYS   B CB  1 
ATOM   1397 C CG  . LYS   B 2 148 ? 6.969   -4.016  -18.651 1.00 79.76  ? 157 LYS   B CG  1 
ATOM   1398 C CD  . LYS   B 2 148 ? 7.946   -5.206  -18.610 1.00 85.58  ? 157 LYS   B CD  1 
ATOM   1399 C CE  . LYS   B 2 148 ? 8.821   -5.357  -19.853 1.00 90.61  ? 157 LYS   B CE  1 
ATOM   1400 N NZ  . LYS   B 2 148 ? 9.838   -4.276  -19.995 1.00 93.26  ? 157 LYS   B NZ  1 
ATOM   1401 N N   . ASN   B 2 149 ? 4.191   -1.936  -22.058 1.00 70.95  ? 158 ASN   B N   1 
ATOM   1402 C CA  . ASN   B 2 149 ? 3.914   -1.197  -23.285 1.00 71.29  ? 158 ASN   B CA  1 
ATOM   1403 C C   . ASN   B 2 149 ? 3.590   0.305   -23.043 1.00 71.23  ? 158 ASN   B C   1 
ATOM   1404 O O   . ASN   B 2 149 ? 3.607   1.111   -23.985 1.00 71.79  ? 158 ASN   B O   1 
ATOM   1405 C CB  . ASN   B 2 149 ? 2.688   -1.828  -23.945 1.00 72.80  ? 158 ASN   B CB  1 
ATOM   1406 C CG  . ASN   B 2 149 ? 3.001   -2.887  -24.956 1.00 76.88  ? 158 ASN   B CG  1 
ATOM   1407 O OD1 . ASN   B 2 149 ? 4.148   -3.321  -25.097 1.00 79.20  ? 158 ASN   B OD1 1 
ATOM   1408 N ND2 . ASN   B 2 149 ? 1.988   -3.319  -25.696 1.00 76.97  ? 158 ASN   B ND2 1 
ATOM   1409 N N   . GLY   B 2 150 ? 3.237   0.648   -21.806 1.00 70.08  ? 159 GLY   B N   1 
ATOM   1410 C CA  . GLY   B 2 150 ? 2.778   1.981   -21.440 1.00 69.17  ? 159 GLY   B CA  1 
ATOM   1411 C C   . GLY   B 2 150 ? 1.264   2.074   -21.537 1.00 67.90  ? 159 GLY   B C   1 
ATOM   1412 O O   . GLY   B 2 150 ? 0.645   2.913   -20.878 1.00 67.79  ? 159 GLY   B O   1 
ATOM   1413 N N   . SER   B 2 151 ? 0.653   1.196   -22.372 1.00 66.70  ? 160 SER   B N   1 
ATOM   1414 C CA  A SER   B 2 151 ? -0.792  1.172   -22.576 0.50 66.48  ? 160 SER   B CA  1 
ATOM   1415 C CA  B SER   B 2 151 ? -0.790  1.153   -22.584 0.50 66.46  ? 160 SER   B CA  1 
ATOM   1416 C C   . SER   B 2 151 ? -1.545  0.560   -21.377 1.00 65.81  ? 160 SER   B C   1 
ATOM   1417 O O   . SER   B 2 151 ? -0.932  -0.072  -20.502 1.00 65.70  ? 160 SER   B O   1 
ATOM   1418 C CB  A SER   B 2 151 ? -1.138  0.452   -23.880 0.50 67.58  ? 160 SER   B CB  1 
ATOM   1419 C CB  B SER   B 2 151 ? -1.115  0.396   -23.873 0.50 67.52  ? 160 SER   B CB  1 
ATOM   1420 O OG  A SER   B 2 151 ? -2.466  0.746   -24.286 0.50 69.48  ? 160 SER   B OG  1 
ATOM   1421 O OG  B SER   B 2 151 ? -0.551  -0.905  -23.887 0.50 69.34  ? 160 SER   B OG  1 
ATOM   1422 N N   . TYR   B 2 152 ? -2.876  0.771   -21.333 1.00 64.06  ? 161 TYR   B N   1 
ATOM   1423 C CA  . TYR   B 2 152 ? -3.762  0.303   -20.278 1.00 62.84  ? 161 TYR   B CA  1 
ATOM   1424 C C   . TYR   B 2 152 ? -4.514  -0.984  -20.641 1.00 60.42  ? 161 TYR   B C   1 
ATOM   1425 O O   . TYR   B 2 152 ? -4.981  -1.151  -21.768 1.00 60.16  ? 161 TYR   B O   1 
ATOM   1426 C CB  . TYR   B 2 152 ? -4.786  1.409   -19.955 1.00 63.20  ? 161 TYR   B CB  1 
ATOM   1427 C CG  . TYR   B 2 152 ? -5.355  1.330   -18.557 1.00 64.22  ? 161 TYR   B CG  1 
ATOM   1428 C CD1 . TYR   B 2 152 ? -4.547  1.504   -17.448 1.00 64.94  ? 161 TYR   B CD1 1 
ATOM   1429 C CD2 . TYR   B 2 152 ? -6.708  1.096   -18.347 1.00 65.18  ? 161 TYR   B CD2 1 
ATOM   1430 C CE1 . TYR   B 2 152 ? -5.059  1.420   -16.164 1.00 65.84  ? 161 TYR   B CE1 1 
ATOM   1431 C CE2 . TYR   B 2 152 ? -7.232  1.010   -17.064 1.00 65.89  ? 161 TYR   B CE2 1 
ATOM   1432 C CZ  . TYR   B 2 152 ? -6.406  1.190   -15.973 1.00 66.91  ? 161 TYR   B CZ  1 
ATOM   1433 O OH  . TYR   B 2 152 ? -6.911  1.147   -14.689 1.00 69.05  ? 161 TYR   B OH  1 
ATOM   1434 N N   . VAL   B 2 153 ? -4.663  -1.876  -19.663 1.00 58.19  ? 162 VAL   B N   1 
ATOM   1435 C CA  . VAL   B 2 153 ? -5.440  -3.092  -19.838 1.00 56.50  ? 162 VAL   B CA  1 
ATOM   1436 C C   . VAL   B 2 153 ? -6.399  -3.140  -18.667 1.00 53.98  ? 162 VAL   B C   1 
ATOM   1437 O O   . VAL   B 2 153 ? -5.967  -3.348  -17.559 1.00 54.02  ? 162 VAL   B O   1 
ATOM   1438 C CB  . VAL   B 2 153 ? -4.575  -4.374  -19.947 1.00 57.36  ? 162 VAL   B CB  1 
ATOM   1439 C CG1 . VAL   B 2 153 ? -5.441  -5.633  -19.853 1.00 57.70  ? 162 VAL   B CG1 1 
ATOM   1440 C CG2 . VAL   B 2 153 ? -3.759  -4.377  -21.240 1.00 57.86  ? 162 VAL   B CG2 1 
ATOM   1441 N N   . SER   B 2 154 ? -7.678  -2.861  -18.897 1.00 52.15  ? 163 SER   B N   1 
ATOM   1442 C CA  . SER   B 2 154 ? -8.706  -2.852  -17.858 1.00 50.86  ? 163 SER   B CA  1 
ATOM   1443 C C   . SER   B 2 154 ? -9.311  -4.239  -17.658 1.00 49.93  ? 163 SER   B C   1 
ATOM   1444 O O   . SER   B 2 154 ? -9.339  -5.025  -18.582 1.00 50.20  ? 163 SER   B O   1 
ATOM   1445 C CB  . SER   B 2 154 ? -9.802  -1.853  -18.224 1.00 51.16  ? 163 SER   B CB  1 
ATOM   1446 O OG  . SER   B 2 154 ? -11.089 -2.233  -17.765 1.00 52.30  ? 163 SER   B OG  1 
ATOM   1447 N N   . ALA   B 2 155 ? -9.849  -4.515  -16.476 1.00 48.78  ? 164 ALA   B N   1 
ATOM   1448 C CA  . ALA   B 2 155 ? -10.503 -5.790  -16.195 1.00 48.07  ? 164 ALA   B CA  1 
ATOM   1449 C C   . ALA   B 2 155 ? -12.011 -5.729  -16.556 1.00 47.33  ? 164 ALA   B C   1 
ATOM   1450 O O   . ALA   B 2 155 ? -12.552 -4.636  -16.774 1.00 47.72  ? 164 ALA   B O   1 
ATOM   1451 C CB  . ALA   B 2 155 ? -10.335 -6.116  -14.723 1.00 48.32  ? 164 ALA   B CB  1 
ATOM   1452 N N   . ILE   B 2 156 ? -12.690 -6.892  -16.640 1.00 45.90  ? 165 ILE   B N   1 
ATOM   1453 C CA  . ILE   B 2 156 ? -14.134 -6.901  -16.859 1.00 44.80  ? 165 ILE   B CA  1 
ATOM   1454 C C   . ILE   B 2 156 ? -14.723 -7.049  -15.452 1.00 43.96  ? 165 ILE   B C   1 
ATOM   1455 O O   . ILE   B 2 156 ? -14.818 -8.170  -14.945 1.00 43.52  ? 165 ILE   B O   1 
ATOM   1456 C CB  . ILE   B 2 156 ? -14.589 -8.028  -17.828 1.00 44.61  ? 165 ILE   B CB  1 
ATOM   1457 C CG1 . ILE   B 2 156 ? -13.892 -7.904  -19.208 1.00 44.63  ? 165 ILE   B CG1 1 
ATOM   1458 C CG2 . ILE   B 2 156 ? -16.124 -8.036  -17.981 1.00 44.83  ? 165 ILE   B CG2 1 
ATOM   1459 C CD1 . ILE   B 2 156 ? -14.073 -9.092  -20.016 1.00 44.89  ? 165 ILE   B CD1 1 
ATOM   1460 N N   . THR   B 2 157 ? -15.049 -5.903  -14.798 1.00 43.53  ? 166 THR   B N   1 
ATOM   1461 C CA  . THR   B 2 157 ? -15.546 -5.844  -13.402 1.00 43.41  ? 166 THR   B CA  1 
ATOM   1462 C C   . THR   B 2 157 ? -17.049 -6.089  -13.242 1.00 43.32  ? 166 THR   B C   1 
ATOM   1463 O O   . THR   B 2 157 ? -17.839 -5.272  -13.697 1.00 43.52  ? 166 THR   B O   1 
ATOM   1464 C CB  . THR   B 2 157 ? -15.217 -4.501  -12.751 1.00 43.76  ? 166 THR   B CB  1 
ATOM   1465 O OG1 . THR   B 2 157 ? -13.916 -4.048  -13.130 1.00 44.63  ? 166 THR   B OG1 1 
ATOM   1466 C CG2 . THR   B 2 157 ? -15.327 -4.562  -11.272 1.00 43.87  ? 166 THR   B CG2 1 
ATOM   1467 N N   . GLN   B 2 158 ? -17.446 -7.169  -12.560 1.00 42.68  ? 167 GLN   B N   1 
ATOM   1468 C CA  . GLN   B 2 158 ? -18.856 -7.483  -12.381 1.00 42.63  ? 167 GLN   B CA  1 
ATOM   1469 C C   . GLN   B 2 158 ? -19.190 -7.810  -10.902 1.00 45.02  ? 167 GLN   B C   1 
ATOM   1470 O O   . GLN   B 2 158 ? -18.433 -8.497  -10.220 1.00 45.14  ? 167 GLN   B O   1 
ATOM   1471 C CB  . GLN   B 2 158 ? -19.255 -8.613  -13.350 1.00 40.97  ? 167 GLN   B CB  1 
ATOM   1472 C CG  . GLN   B 2 158 ? -20.679 -9.134  -13.228 1.00 40.16  ? 167 GLN   B CG  1 
ATOM   1473 C CD  . GLN   B 2 158 ? -21.744 -8.174  -13.706 1.00 41.14  ? 167 GLN   B CD  1 
ATOM   1474 O OE1 . GLN   B 2 158 ? -21.874 -7.049  -13.223 1.00 42.09  ? 167 GLN   B OE1 1 
ATOM   1475 N NE2 . GLN   B 2 158 ? -22.565 -8.610  -14.629 1.00 39.92  ? 167 GLN   B NE2 1 
ATOM   1476 N N   . GLY   B 2 159 ? -20.311 -7.295  -10.421 1.00 46.58  ? 168 GLY   B N   1 
ATOM   1477 C CA  . GLY   B 2 159 ? -20.742 -7.522  -9.056  1.00 48.75  ? 168 GLY   B CA  1 
ATOM   1478 C C   . GLY   B 2 159 ? -21.678 -8.697  -8.880  1.00 51.32  ? 168 GLY   B C   1 
ATOM   1479 O O   . GLY   B 2 159 ? -22.023 -9.387  -9.842  1.00 51.00  ? 168 GLY   B O   1 
ATOM   1480 N N   . LYS   B 2 160 ? -22.099 -8.925  -7.620  1.00 53.80  ? 169 LYS   B N   1 
ATOM   1481 C CA  . LYS   B 2 160 ? -23.002 -10.012 -7.268  1.00 56.37  ? 169 LYS   B CA  1 
ATOM   1482 C C   . LYS   B 2 160 ? -24.484 -9.577  -7.202  1.00 59.20  ? 169 LYS   B C   1 
ATOM   1483 O O   . LYS   B 2 160 ? -24.794 -8.492  -6.704  1.00 59.67  ? 169 LYS   B O   1 
ATOM   1484 C CB  . LYS   B 2 160 ? -22.574 -10.652 -5.937  1.00 57.70  ? 169 LYS   B CB  1 
ATOM   1485 C CG  . LYS   B 2 160 ? -23.235 -12.008 -5.694  1.00 61.79  ? 169 LYS   B CG  1 
ATOM   1486 C CD  . LYS   B 2 160 ? -22.942 -12.598 -4.311  1.00 66.56  ? 169 LYS   B CD  1 
ATOM   1487 C CE  . LYS   B 2 160 ? -23.598 -13.953 -4.137  1.00 70.26  ? 169 LYS   B CE  1 
ATOM   1488 N NZ  . LYS   B 2 160 ? -23.560 -14.420 -2.722  1.00 72.56  ? 169 LYS   B NZ  1 
ATOM   1489 N N   . ARG   B 2 161 ? -25.394 -10.428 -7.716  1.00 60.68  ? 170 ARG   B N   1 
ATOM   1490 C CA  . ARG   B 2 161 ? -26.837 -10.214 -7.624  1.00 62.17  ? 170 ARG   B CA  1 
ATOM   1491 C C   . ARG   B 2 161 ? -27.377 -11.149 -6.504  1.00 63.51  ? 170 ARG   B C   1 
ATOM   1492 O O   . ARG   B 2 161 ? -26.921 -12.291 -6.385  1.00 63.86  ? 170 ARG   B O   1 
ATOM   1493 C CB  . ARG   B 2 161 ? -27.508 -10.520 -8.958  1.00 63.52  ? 170 ARG   B CB  1 
ATOM   1494 C CG  . ARG   B 2 161 ? -28.955 -10.095 -9.007  1.00 67.54  ? 170 ARG   B CG  1 
ATOM   1495 C CD  . ARG   B 2 161 ? -29.660 -10.622 -10.242 1.00 72.38  ? 170 ARG   B CD  1 
ATOM   1496 N NE  . ARG   B 2 161 ? -31.108 -10.467 -10.111 1.00 77.03  ? 170 ARG   B NE  1 
ATOM   1497 C CZ  . ARG   B 2 161 ? -31.816 -9.496  -10.682 1.00 80.61  ? 170 ARG   B CZ  1 
ATOM   1498 N NH1 . ARG   B 2 161 ? -31.224 -8.608  -11.474 1.00 80.26  ? 170 ARG   B NH1 1 
ATOM   1499 N NH2 . ARG   B 2 161 ? -33.124 -9.412  -10.476 1.00 81.17  ? 170 ARG   B NH2 1 
ATOM   1500 N N   . GLU   B 2 162 ? -28.304 -10.661 -5.663  1.00 63.90  ? 171 GLU   B N   1 
ATOM   1501 C CA  . GLU   B 2 162 ? -28.833 -11.466 -4.564  1.00 64.79  ? 171 GLU   B CA  1 
ATOM   1502 C C   . GLU   B 2 162 ? -30.348 -11.708 -4.647  1.00 64.88  ? 171 GLU   B C   1 
ATOM   1503 O O   . GLU   B 2 162 ? -30.921 -12.385 -3.788  1.00 64.75  ? 171 GLU   B O   1 
ATOM   1504 C CB  . GLU   B 2 162 ? -28.432 -10.854 -3.214  1.00 67.88  ? 171 GLU   B CB  1 
ATOM   1505 C CG  . GLU   B 2 162 ? -26.966 -11.073 -2.880  1.00 74.66  ? 171 GLU   B CG  1 
ATOM   1506 C CD  . GLU   B 2 162 ? -26.715 -11.762 -1.547  1.00 83.22  ? 171 GLU   B CD  1 
ATOM   1507 O OE1 . GLU   B 2 162 ? -25.660 -12.425 -1.404  1.00 84.57  ? 171 GLU   B OE1 1 
ATOM   1508 O OE2 . GLU   B 2 162 ? -27.579 -11.640 -0.647  1.00 85.72  ? 171 GLU   B OE2 1 
HETATM 1509 S S   . DMS   C 3 .   ? -18.404 11.120  -0.232  1.00 83.16  ? 201 DMS   B S   1 
HETATM 1510 O O   . DMS   C 3 .   ? -19.616 10.367  -0.580  1.00 83.08  ? 201 DMS   B O   1 
HETATM 1511 C C1  . DMS   C 3 .   ? -18.990 12.586  0.566   1.00 83.13  ? 201 DMS   B C1  1 
HETATM 1512 C C2  . DMS   C 3 .   ? -17.821 11.851  -1.737  1.00 83.06  ? 201 DMS   B C2  1 
HETATM 1513 N N1  . A1BGS D 4 .   ? -7.992  5.865   -9.163  1.00 71.54  ? 202 A1BGS B N1  1 
HETATM 1514 N N3  . A1BGS D 4 .   ? -8.156  1.739   -6.641  1.00 70.37  ? 202 A1BGS B N3  1 
HETATM 1515 C C4  . A1BGS D 4 .   ? -7.849  4.737   -14.014 1.00 73.70  ? 202 A1BGS B C4  1 
HETATM 1516 C C5  . A1BGS D 4 .   ? -9.102  4.820   -13.179 1.00 72.84  ? 202 A1BGS B C5  1 
HETATM 1517 C C6  . A1BGS D 4 .   ? -8.725  5.196   -11.762 1.00 71.94  ? 202 A1BGS B C6  1 
HETATM 1518 C C7  . A1BGS D 4 .   ? -8.184  6.439   -11.475 1.00 71.73  ? 202 A1BGS B C7  1 
HETATM 1519 C C8  . A1BGS D 4 .   ? -7.832  6.731   -10.177 1.00 71.72  ? 202 A1BGS B C8  1 
HETATM 1520 C C10 . A1BGS D 4 .   ? -9.598  2.641   -8.466  1.00 70.43  ? 202 A1BGS B C10 1 
HETATM 1521 C C13 . A1BGS D 4 .   ? -8.305  4.143   -6.992  1.00 70.54  ? 202 A1BGS B C13 1 
HETATM 1522 C C15 . A1BGS D 4 .   ? -6.825  5.086   -16.046 1.00 74.67  ? 202 A1BGS B C15 1 
HETATM 1523 C C17 . A1BGS D 4 .   ? -7.897  4.426   -19.376 1.00 75.30  ? 202 A1BGS B C17 1 
HETATM 1524 C C1  . A1BGS D 4 .   ? -3.140  4.092   -14.482 1.00 75.81  ? 202 A1BGS B C1  1 
HETATM 1525 O O1  . A1BGS D 4 .   ? -4.366  3.950   -13.742 1.00 75.64  ? 202 A1BGS B O1  1 
HETATM 1526 C C2  . A1BGS D 4 .   ? -5.524  4.366   -14.295 1.00 75.04  ? 202 A1BGS B C2  1 
HETATM 1527 C C3  . A1BGS D 4 .   ? -6.633  4.348   -13.479 1.00 74.32  ? 202 A1BGS B C3  1 
HETATM 1528 C C9  . A1BGS D 4 .   ? -8.511  4.649   -9.425  1.00 71.23  ? 202 A1BGS B C9  1 
HETATM 1529 N N2  . A1BGS D 4 .   ? -8.754  3.830   -8.354  1.00 70.74  ? 202 A1BGS B N2  1 
HETATM 1530 C C11 . A1BGS D 4 .   ? -8.957  1.423   -7.828  1.00 70.38  ? 202 A1BGS B C11 1 
HETATM 1531 C C12 . A1BGS D 4 .   ? -8.565  3.001   -6.029  1.00 70.37  ? 202 A1BGS B C12 1 
HETATM 1532 C C14 . A1BGS D 4 .   ? -8.898  4.295   -10.727 1.00 71.53  ? 202 A1BGS B C14 1 
HETATM 1533 N N4  . A1BGS D 4 .   ? -7.950  5.089   -15.299 1.00 74.13  ? 202 A1BGS B N4  1 
HETATM 1534 N N5  . A1BGS D 4 .   ? -6.931  5.404   -17.350 1.00 74.84  ? 202 A1BGS B N5  1 
HETATM 1535 C C16 . A1BGS D 4 .   ? -8.169  5.207   -18.105 1.00 75.10  ? 202 A1BGS B C16 1 
HETATM 1536 N N6  . A1BGS D 4 .   ? -6.736  4.928   -20.126 1.00 75.42  ? 202 A1BGS B N6  1 
HETATM 1537 C C18 . A1BGS D 4 .   ? -6.181  6.167   -19.574 1.00 75.16  ? 202 A1BGS B C18 1 
HETATM 1538 C C19 . A1BGS D 4 .   ? -5.831  6.007   -18.106 1.00 74.88  ? 202 A1BGS B C19 1 
HETATM 1539 N N7  . A1BGS D 4 .   ? -5.619  4.688   -15.584 1.00 74.97  ? 202 A1BGS B N7  1 
HETATM 1540 S S   . DMS   E 3 .   ? -11.236 -11.647 -8.034  1.00 96.99  ? 203 DMS   B S   1 
HETATM 1541 O O   . DMS   E 3 .   ? -11.091 -12.518 -9.208  1.00 96.99  ? 203 DMS   B O   1 
HETATM 1542 C C1  . DMS   E 3 .   ? -11.944 -10.158 -8.669  1.00 96.89  ? 203 DMS   B C1  1 
HETATM 1543 C C2  . DMS   E 3 .   ? -9.604  -11.073 -7.652  1.00 96.98  ? 203 DMS   B C2  1 
HETATM 1544 O O   . HOH   F 5 .   ? -4.026  -14.629 -25.168 1.00 40.13  ? 101 HOH   A O   1 
HETATM 1545 O O   . HOH   F 5 .   ? -23.599 18.589  -19.356 1.00 24.43  ? 102 HOH   A O   1 
HETATM 1546 O O   . HOH   F 5 .   ? -7.091  -9.410  -3.346  1.00 20.18  ? 103 HOH   A O   1 
HETATM 1547 O O   . HOH   F 5 .   ? -28.285 -6.657  -28.391 1.00 48.42  ? 104 HOH   A O   1 
HETATM 1548 O O   . HOH   F 5 .   ? -30.838 -0.329  -22.977 1.00 38.40  ? 105 HOH   A O   1 
HETATM 1549 O O   . HOH   F 5 .   ? -1.033  -15.806 -10.025 1.00 41.10  ? 106 HOH   A O   1 
HETATM 1550 O O   . HOH   F 5 .   ? -6.244  -6.499  0.723   1.00 22.69  ? 107 HOH   A O   1 
HETATM 1551 O O   . HOH   F 5 .   ? -22.456 -9.463  -35.046 1.00 32.36  ? 108 HOH   A O   1 
HETATM 1552 O O   . HOH   F 5 .   ? -5.375  2.104   -10.518 1.00 54.55  ? 109 HOH   A O   1 
HETATM 1553 O O   . HOH   F 5 .   ? -4.170  -2.100  0.056   1.00 33.63  ? 110 HOH   A O   1 
HETATM 1554 O O   . HOH   G 5 .   ? -34.382 1.290   -15.396 1.00 13.28  ? 301 HOH   B O   1 
HETATM 1555 O O   . HOH   G 5 .   ? -26.220 -8.335  -16.915 1.00 33.21  ? 302 HOH   B O   1 
HETATM 1556 O O   . HOH   G 5 .   ? -16.763 20.842  -14.168 1.00 40.96  ? 303 HOH   B O   1 
HETATM 1557 O O   . HOH   G 5 .   ? -6.642  -1.137  -10.820 1.00 17.11  ? 304 HOH   B O   1 
HETATM 1558 O O   . HOH   G 5 .   ? -21.977 6.427   -0.173  0.50 5.59   ? 305 HOH   B O   1 
HETATM 1559 O O   . HOH   G 5 .   ? -21.775 -12.353 -13.089 1.00 38.08  ? 306 HOH   B O   1 
HETATM 1560 O O   . HOH   G 5 .   ? -10.316 11.496  -19.000 1.00 19.48  ? 307 HOH   B O   1 
HETATM 1561 O O   . HOH   G 5 .   ? -28.746 -7.836  -5.394  1.00 44.49  ? 308 HOH   B O   1 
HETATM 1562 O O   . HOH   G 5 .   ? -27.737 -6.928  -18.516 1.00 37.75  ? 309 HOH   B O   1 
HETATM 1563 O O   . HOH   G 5 .   ? -20.182 2.150   -32.915 1.00 41.86  ? 310 HOH   B O   1 
HETATM 1564 O O   . HOH   G 5 .   ? -31.298 11.738  -16.967 1.00 48.34  ? 311 HOH   B O   1 
HETATM 1565 O O   . HOH   G 5 .   ? -31.062 4.596   -2.593  1.00 35.64  ? 312 HOH   B O   1 
HETATM 1566 O O   . HOH   G 5 .   ? -17.744 15.409  -21.949 1.00 32.12  ? 313 HOH   B O   1 
HETATM 1567 O O   . HOH   G 5 .   ? -19.371 -6.367  -0.636  1.00 27.26  ? 314 HOH   B O   1 
HETATM 1568 O O   . HOH   G 5 .   ? -17.230 12.868  -5.790  1.00 27.63  ? 315 HOH   B O   1 
HETATM 1569 O O   . HOH   G 5 .   ? -24.940 -6.466  -4.359  1.00 25.59  ? 316 HOH   B O   1 
HETATM 1570 O O   . HOH   G 5 .   ? -35.254 0.776   -7.961  1.00 36.03  ? 317 HOH   B O   1 
HETATM 1571 O O   . HOH   G 5 .   ? -28.032 8.822   0.776   1.00 45.70  ? 318 HOH   B O   1 
HETATM 1572 O O   . HOH   G 5 .   ? -16.530 -14.837 -31.042 1.00 26.81  ? 319 HOH   B O   1 
HETATM 1573 O O   . HOH   G 5 .   ? -15.197 16.744  -20.422 1.00 39.18  ? 320 HOH   B O   1 
HETATM 1574 O O   . HOH   G 5 .   ? -5.765  -10.942 -5.545  1.00 31.92  ? 321 HOH   B O   1 
HETATM 1575 O O   . HOH   G 5 .   ? -28.923 -5.703  -1.221  1.00 17.87  ? 322 HOH   B O   1 
HETATM 1576 O O   . HOH   G 5 .   ? -32.305 6.592   -4.345  1.00 40.50  ? 323 HOH   B O   1 
HETATM 1577 O O   . HOH   G 5 .   ? 0.184   -0.412  -12.934 1.00 35.35  ? 324 HOH   B O   1 
HETATM 1578 O O   . HOH   G 5 .   ? -24.400 -15.698 -17.597 1.00 21.18  ? 325 HOH   B O   1 
HETATM 1579 O O   . HOH   G 5 .   ? -32.820 -7.990  -7.148  1.00 41.97  ? 326 HOH   B O   1 
HETATM 1580 O O   . HOH   G 5 .   ? -15.194 -13.737 -16.991 1.00 25.76  ? 327 HOH   B O   1 
HETATM 1581 O O   . HOH   G 5 .   ? -12.152 14.112  -14.696 1.00 27.12  ? 328 HOH   B O   1 
HETATM 1582 O O   . HOH   G 5 .   ? -35.353 5.550   -6.037  1.00 32.50  ? 329 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP   A 7   ? 1.0850 0.4711 0.4441 0.4632  0.0399  -0.2584 50  ASP   A N   
2    C CA  . ASP   A 7   ? 1.0395 0.5448 0.4255 0.4704  0.0732  -0.2479 50  ASP   A CA  
3    C C   . ASP   A 7   ? 1.0045 0.5413 0.4297 0.4481  0.0821  -0.2002 50  ASP   A C   
4    O O   . ASP   A 7   ? 1.0126 0.5057 0.4427 0.4653  0.0720  -0.1834 50  ASP   A O   
5    C CB  . ASP   A 7   ? 1.0593 0.6085 0.4380 0.5318  0.0863  -0.2817 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 1.1040 0.7380 0.4694 0.5396  0.1112  -0.3090 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 1.1381 0.7472 0.4635 0.5744  0.1075  -0.3519 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 1.0946 0.8167 0.4855 0.5116  0.1341  -0.2869 50  ASP   A OD2 
9    N N   . MET   A 8   ? 0.9665 0.5750 0.4135 0.4121  0.0992  -0.1792 51  MET   A N   
10   C CA  . MET   A 8   ? 0.9417 0.5874 0.4198 0.3942  0.1089  -0.1394 51  MET   A CA  
11   C C   . MET   A 8   ? 0.9112 0.6180 0.4056 0.4327  0.1209  -0.1420 51  MET   A C   
12   O O   . MET   A 8   ? 0.8946 0.6499 0.3881 0.4613  0.1312  -0.1708 51  MET   A O   
13   C CB  . MET   A 8   ? 0.9232 0.6269 0.4180 0.3514  0.1210  -0.1221 51  MET   A CB  
14   C CG  . MET   A 8   ? 0.9658 0.6208 0.4611 0.3102  0.1077  -0.1082 51  MET   A CG  
15   S SD  . MET   A 8   ? 0.9801 0.7044 0.4942 0.2692  0.1182  -0.0934 51  MET   A SD  
16   C CE  . MET   A 8   ? 0.9611 0.6260 0.4882 0.2273  0.0986  -0.0769 51  MET   A CE  
17   N N   . TYR   A 9   ? 0.8984 0.6068 0.4081 0.4337  0.1194  -0.1117 52  TYR   A N   
18   C CA  . TYR   A 9   ? 0.8649 0.6292 0.3937 0.4682  0.1240  -0.1122 52  TYR   A CA  
19   C C   . TYR   A 9   ? 0.8309 0.6378 0.3784 0.4480  0.1292  -0.0790 52  TYR   A C   
20   O O   . TYR   A 9   ? 0.8431 0.6225 0.3846 0.4146  0.1294  -0.0527 52  TYR   A O   
21   C CB  . TYR   A 9   ? 0.8894 0.5939 0.4045 0.5156  0.1061  -0.1217 52  TYR   A CB  
22   C CG  . TYR   A 9   ? 0.9414 0.5518 0.4352 0.5061  0.0888  -0.0904 52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 0.9902 0.5062 0.4594 0.4897  0.0750  -0.0909 52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 0.9564 0.5696 0.4518 0.5143  0.0845  -0.0599 52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 1.0356 0.4663 0.4880 0.4760  0.0611  -0.0570 52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 1.0024 0.5299 0.4722 0.5056  0.0720  -0.0268 52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 1.0482 0.4851 0.4987 0.4852  0.0616  -0.0237 52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 1.0996 0.4544 0.5279 0.4703  0.0516  0.0146  52  TYR   A OH  
29   N N   . ILE   A 10  ? 0.7815 0.6611 0.3539 0.4682  0.1333  -0.0824 53  ILE   A N   
30   C CA  . ILE   A 10  ? 0.7493 0.6676 0.3352 0.4535  0.1337  -0.0575 53  ILE   A CA  
31   C C   . ILE   A 10  ? 0.7570 0.6615 0.3399 0.4891  0.1173  -0.0466 53  ILE   A C   
32   O O   . ILE   A 10  ? 0.7621 0.6617 0.3495 0.5292  0.1081  -0.0644 53  ILE   A O   
33   C CB  . ILE   A 10  ? 0.6953 0.7054 0.3119 0.4356  0.1463  -0.0651 53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 0.6542 0.7341 0.3036 0.4673  0.1473  -0.0857 53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 0.7014 0.7160 0.3112 0.4036  0.1594  -0.0730 53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 0.6158 0.7832 0.3002 0.4447  0.1563  -0.0846 53  ILE   A CD1 
37   N N   . GLU   A 11  ? 0.7592 0.6533 0.3295 0.4779  0.1125  -0.0183 54  GLU   A N   
38   C CA  . GLU   A 11  ? 0.7773 0.6532 0.3333 0.5102  0.0945  -0.0042 54  GLU   A CA  
39   C C   . GLU   A 11  ? 0.7616 0.6823 0.3198 0.4980  0.0923  0.0104  54  GLU   A C   
40   O O   . GLU   A 11  ? 0.7699 0.6767 0.3111 0.4680  0.1026  0.0290  54  GLU   A O   
41   C CB  . GLU   A 11  ? 0.8471 0.6254 0.3591 0.5126  0.0880  0.0223  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 0.9209 0.6331 0.4223 0.5352  0.0786  0.0088  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 1.0289 0.6379 0.4876 0.5350  0.0685  0.0397  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 1.0151 0.6087 0.4527 0.5105  0.0759  0.0743  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 1.1002 0.6422 0.5454 0.5601  0.0533  0.0295  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 0.7354 0.7080 0.3143 0.5231  0.0766  0.0009  55  ARG   A N   
47   C CA  . ARG   A 12  ? 0.7295 0.7403 0.3088 0.5132  0.0684  0.0094  55  ARG   A CA  
48   C C   . ARG   A 12  ? 0.7848 0.7378 0.3095 0.5140  0.0648  0.0388  55  ARG   A C   
49   O O   . ARG   A 12  ? 0.8244 0.7192 0.3153 0.5386  0.0562  0.0536  55  ARG   A O   
50   C CB  . ARG   A 12  ? 0.7026 0.7772 0.3181 0.5404  0.0463  -0.0070 55  ARG   A CB  
51   C CG  . ARG   A 12  ? 0.6979 0.8266 0.3314 0.5180  0.0385  -0.0088 55  ARG   A CG  
52   C CD  . ARG   A 12  ? 0.6746 0.8815 0.3634 0.5335  0.0184  -0.0279 55  ARG   A CD  
53   N NE  . ARG   A 12  ? 0.6830 0.9335 0.3907 0.5065  0.0071  -0.0299 55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 0.7383 0.9741 0.4175 0.5143  -0.0189 -0.0237 55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 0.7788 0.9608 0.4057 0.5476  -0.0331 -0.0114 55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 0.7223 0.9906 0.4187 0.4889  -0.0321 -0.0293 55  ARG   A NH2 
57   N N   . ALA   A 13  ? 0.7853 0.7506 0.2981 0.4873  0.0732  0.0485  56  ALA   A N   
58   C CA  . ALA   A 13  ? 0.8223 0.7448 0.2818 0.4879  0.0762  0.0759  56  ALA   A CA  
59   C C   . ALA   A 13  ? 0.8323 0.7856 0.2751 0.4944  0.0612  0.0738  56  ALA   A C   
60   O O   . ALA   A 13  ? 0.8607 0.7853 0.2534 0.4988  0.0655  0.0941  56  ALA   A O   
61   C CB  . ALA   A 13  ? 0.8309 0.7275 0.2827 0.4544  0.1031  0.0914  56  ALA   A CB  
62   N N   . GLY   A 14  ? 0.8108 0.8212 0.2937 0.4956  0.0431  0.0497  57  GLY   A N   
63   C CA  . GLY   A 14  ? 0.8264 0.8598 0.2954 0.5012  0.0213  0.0434  57  GLY   A CA  
64   C C   . GLY   A 14  ? 0.8062 0.9013 0.3291 0.4822  0.0075  0.0196  57  GLY   A C   
65   O O   . GLY   A 14  ? 0.7793 0.9097 0.3537 0.4635  0.0185  0.0086  57  GLY   A O   
66   N N   . ASP   A 15  ? 0.8184 0.9233 0.3248 0.4863  -0.0176 0.0124  58  ASP   A N   
67   C CA  . ASP   A 15  ? 0.8040 0.9571 0.3556 0.4652  -0.0379 -0.0072 58  ASP   A CA  
68   C C   . ASP   A 15  ? 0.8304 0.9686 0.3658 0.4385  -0.0282 -0.0074 58  ASP   A C   
69   O O   . ASP   A 15  ? 0.8675 0.9647 0.3456 0.4495  -0.0199 0.0027  58  ASP   A O   
70   C CB  . ASP   A 15  ? 0.8242 0.9865 0.3631 0.4887  -0.0808 -0.0182 58  ASP   A CB  
71   C CG  . ASP   A 15  ? 0.8503 1.0593 0.4402 0.5061  -0.1028 -0.0281 58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 0.8520 1.0636 0.4584 0.5186  -0.0846 -0.0223 58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 0.8649 1.1069 0.4785 0.5098  -0.1412 -0.0429 58  ASP   A OD2 
74   N N   . ILE   A 16  ? 0.8080 0.9804 0.3915 0.4059  -0.0322 -0.0184 59  ILE   A N   
75   C CA  . ILE   A 16  ? 0.8296 0.9826 0.3977 0.3834  -0.0298 -0.0200 59  ILE   A CA  
76   C C   . ILE   A 16  ? 0.8479 0.9902 0.3932 0.3925  -0.0694 -0.0345 59  ILE   A C   
77   O O   . ILE   A 16  ? 0.8200 0.9915 0.4080 0.3735  -0.0967 -0.0469 59  ILE   A O   
78   C CB  . ILE   A 16  ? 0.8093 0.9920 0.4292 0.3438  -0.0186 -0.0218 59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 0.8082 1.0076 0.4524 0.3381  0.0139  -0.0139 59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 0.8327 0.9850 0.4305 0.3262  -0.0159 -0.0209 59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 0.7867 1.0359 0.4878 0.3060  0.0206  -0.0179 59  ILE   A CD1 
82   N N   A THR   A 17  ? 0.8876 0.9884 0.3646 0.4212  -0.0724 -0.0327 60  THR   A N   
83   N N   B THR   A 17  ? 0.8889 0.9899 0.3660 0.4212  -0.0731 -0.0329 60  THR   A N   
84   C CA  A THR   A 17  ? 0.9180 0.9982 0.3560 0.4377  -0.1108 -0.0498 60  THR   A CA  
85   C CA  B THR   A 17  ? 0.9192 1.0011 0.3601 0.4368  -0.1126 -0.0506 60  THR   A CA  
86   C C   A THR   A 17  ? 0.9662 1.0038 0.3381 0.4534  -0.0984 -0.0497 60  THR   A C   
87   C C   B THR   A 17  ? 0.9690 1.0066 0.3389 0.4556  -0.1009 -0.0502 60  THR   A C   
88   O O   A THR   A 17  ? 0.9806 1.0054 0.3214 0.4654  -0.0622 -0.0313 60  THR   A O   
89   O O   B THR   A 17  ? 0.9856 1.0098 0.3213 0.4702  -0.0661 -0.0317 60  THR   A O   
90   C CB  A THR   A 17  ? 0.9411 1.0196 0.3481 0.4739  -0.1353 -0.0515 60  THR   A CB  
91   C CB  B THR   A 17  ? 0.9353 1.0264 0.3639 0.4666  -0.1430 -0.0554 60  THR   A CB  
92   O OG1 A THR   A 17  ? 0.9694 1.0276 0.3352 0.4973  -0.1033 -0.0290 60  THR   A OG1 
93   O OG1 B THR   A 17  ? 0.9035 1.0476 0.4107 0.4474  -0.1589 -0.0616 60  THR   A OG1 
94   C CG2 A THR   A 17  ? 0.9078 1.0357 0.3829 0.4655  -0.1628 -0.0603 60  THR   A CG2 
95   C CG2 B THR   A 17  ? 0.9672 1.0300 0.3413 0.4899  -0.1859 -0.0746 60  THR   A CG2 
96   N N   . TRP   A 18  ? 0.9901 1.0063 0.3409 0.4548  -0.1298 -0.0708 61  TRP   A N   
97   C CA  . TRP   A 18  ? 1.0562 1.0353 0.3402 0.4790  -0.1214 -0.0763 61  TRP   A CA  
98   C C   . TRP   A 18  ? 1.1348 1.0950 0.3435 0.5237  -0.1346 -0.0789 61  TRP   A C   
99   O O   . TRP   A 18  ? 1.1368 1.0966 0.3416 0.5330  -0.1777 -0.0941 61  TRP   A O   
100  C CB  . TRP   A 18  ? 1.0590 1.0132 0.3450 0.4674  -0.1554 -0.1016 61  TRP   A CB  
101  C CG  . TRP   A 18  ? 1.1051 1.0196 0.3172 0.5022  -0.1571 -0.1168 61  TRP   A CG  
102  C CD1 . TRP   A 18  ? 1.1491 1.0333 0.2893 0.5409  -0.1871 -0.1379 61  TRP   A CD1 
103  C CD2 . TRP   A 18  ? 1.1131 1.0154 0.3174 0.5038  -0.1321 -0.1165 61  TRP   A CD2 
104  N NE1 . TRP   A 18  ? 1.1776 1.0333 0.2626 0.5690  -0.1774 -0.1510 61  TRP   A NE1 
105  C CE2 . TRP   A 18  ? 1.1569 1.0255 0.2845 0.5471  -0.1443 -0.1381 61  TRP   A CE2 
106  C CE3 . TRP   A 18  ? 1.0971 1.0159 0.3492 0.4765  -0.1008 -0.1006 61  TRP   A CE3 
107  C CZ2 . TRP   A 18  ? 1.1749 1.0312 0.2802 0.5647  -0.1251 -0.1449 61  TRP   A CZ2 
108  C CZ3 . TRP   A 18  ? 1.1181 1.0227 0.3497 0.4916  -0.0861 -0.1063 61  TRP   A CZ3 
109  C CH2 . TRP   A 18  ? 1.1520 1.0286 0.3140 0.5362  -0.0966 -0.1281 61  TRP   A CH2 
110  N N   . GLU   A 19  ? 1.1911 1.1388 0.3416 0.5500  -0.0979 -0.0619 62  GLU   A N   
111  C CA  . GLU   A 19  ? 1.2618 1.1895 0.3306 0.5923  -0.1050 -0.0589 62  GLU   A CA  
112  C C   . GLU   A 19  ? 1.3337 1.2335 0.3257 0.6247  -0.1097 -0.0773 62  GLU   A C   
113  O O   . GLU   A 19  ? 1.3376 1.2404 0.3185 0.6274  -0.0720 -0.0699 62  GLU   A O   
114  C CB  . GLU   A 19  ? 1.3055 1.2376 0.3553 0.6003  -0.0607 -0.0216 62  GLU   A CB  
115  C CG  . GLU   A 19  ? 1.3633 1.3158 0.4805 0.5765  -0.0572 -0.0061 62  GLU   A CG  
116  C CD  . GLU   A 19  ? 1.4572 1.4148 0.5832 0.5888  -0.1006 -0.0157 62  GLU   A CD  
117  O OE1 . GLU   A 19  ? 1.5140 1.4490 0.5694 0.6250  -0.1210 -0.0153 62  GLU   A OE1 
118  O OE2 . GLU   A 19  ? 1.4461 1.4345 0.6503 0.5634  -0.1134 -0.0230 62  GLU   A OE2 
119  N N   . LYS   A 20  ? 1.3873 1.2619 0.3250 0.6524  -0.1573 -0.1031 63  LYS   A N   
120  C CA  . LYS   A 20  ? 1.4595 1.3014 0.3071 0.6931  -0.1678 -0.1264 63  LYS   A CA  
121  C C   . LYS   A 20  ? 1.5039 1.3480 0.2741 0.7271  -0.1190 -0.0977 63  LYS   A C   
122  O O   . LYS   A 20  ? 1.5070 1.3607 0.2757 0.7255  -0.1024 -0.0666 63  LYS   A O   
123  C CB  . LYS   A 20  ? 1.5257 1.3379 0.3284 0.7155  -0.2348 -0.1589 63  LYS   A CB  
124  C CG  . LYS   A 20  ? 1.5887 1.3829 0.4378 0.6915  -0.2884 -0.1956 63  LYS   A CG  
125  C CD  . LYS   A 20  ? 1.7035 1.4457 0.4620 0.7322  -0.3268 -0.2359 63  LYS   A CD  
126  C CE  . LYS   A 20  ? 1.7561 1.4700 0.5586 0.7058  -0.3919 -0.2715 63  LYS   A CE  
127  N NZ  . LYS   A 20  ? 1.7659 1.5023 0.6265 0.6795  -0.4369 -0.2711 63  LYS   A NZ  
128  N N   . ASP   A 21  ? 1.5352 1.3706 0.2405 0.7586  -0.0957 -0.1069 64  ASP   A N   
129  C CA  . ASP   A 21  ? 1.5712 1.4165 0.2023 0.7891  -0.0442 -0.0766 64  ASP   A CA  
130  C C   . ASP   A 21  ? 1.5427 1.4227 0.2375 0.7540  0.0115  -0.0293 64  ASP   A C   
131  O O   . ASP   A 21  ? 1.5572 1.4350 0.2309 0.7547  0.0264  0.0043  64  ASP   A O   
132  C CB  . ASP   A 21  ? 1.6448 1.4631 0.1788 0.8271  -0.0681 -0.0727 64  ASP   A CB  
133  C CG  . ASP   A 21  ? 1.7615 1.5401 0.2234 0.8636  -0.1306 -0.1202 64  ASP   A CG  
134  O OD1 . ASP   A 21  ? 1.7858 1.5511 0.2181 0.8840  -0.1367 -0.1538 64  ASP   A OD1 
135  O OD2 . ASP   A 21  ? 1.8096 1.5677 0.2394 0.8757  -0.1754 -0.1245 64  ASP   A OD2 
136  N N   . ALA   A 22  ? 1.5001 1.4055 0.2741 0.7223  0.0346  -0.0282 65  ALA   A N   
137  C CA  . ALA   A 22  ? 1.4669 1.4022 0.3032 0.6876  0.0820  0.0114  65  ALA   A CA  
138  C C   . ALA   A 22  ? 1.4601 1.4272 0.2811 0.6989  0.1377  0.0280  65  ALA   A C   
139  O O   . ALA   A 22  ? 1.4727 1.4417 0.2478 0.7325  0.1375  0.0030  65  ALA   A O   
140  C CB  . ALA   A 22  ? 1.4272 1.3730 0.3658 0.6421  0.0676  0.0030  65  ALA   A CB  
141  N N   . GLU   A 23  ? 1.4356 1.4285 0.2943 0.6728  0.1840  0.0692  66  GLU   A N   
142  C CA  . GLU   A 23  ? 1.4214 1.4566 0.2795 0.6782  0.2384  0.0892  66  GLU   A CA  
143  C C   . GLU   A 23  ? 1.3837 1.4467 0.3104 0.6663  0.2389  0.0644  66  GLU   A C   
144  O O   . GLU   A 23  ? 1.3554 1.4214 0.3630 0.6266  0.2292  0.0649  66  GLU   A O   
145  C CB  . GLU   A 23  ? 1.4361 1.4863 0.3230 0.6468  0.2809  0.1411  66  GLU   A CB  
146  C CG  . GLU   A 23  ? 1.4848 1.5846 0.3627 0.6531  0.3400  0.1696  66  GLU   A CG  
147  C CD  . GLU   A 23  ? 1.5215 1.6577 0.4973 0.6059  0.3702  0.1945  66  GLU   A CD  
148  O OE1 . GLU   A 23  ? 1.5326 1.6431 0.5533 0.5688  0.3588  0.2111  66  GLU   A OE1 
149  O OE2 . GLU   A 23  ? 1.5077 1.6990 0.5161 0.6082  0.4027  0.1950  66  GLU   A OE2 
150  N N   . VAL   A 24  ? 1.3825 1.4621 0.2713 0.7047  0.2469  0.0407  67  VAL   A N   
151  C CA  . VAL   A 24  ? 1.3554 1.4547 0.2996 0.7028  0.2418  0.0144  67  VAL   A CA  
152  C C   . VAL   A 24  ? 1.3177 1.4830 0.3091 0.6964  0.2969  0.0389  67  VAL   A C   
153  O O   . VAL   A 24  ? 1.3254 1.5266 0.2705 0.7323  0.3336  0.0446  67  VAL   A O   
154  C CB  . VAL   A 24  ? 1.3889 1.4588 0.2741 0.7499  0.2062  -0.0348 67  VAL   A CB  
155  C CG1 . VAL   A 24  ? 1.3737 1.4468 0.3206 0.7429  0.1888  -0.0614 67  VAL   A CG1 
156  C CG2 . VAL   A 24  ? 1.4291 1.4379 0.2664 0.7558  0.1497  -0.0579 67  VAL   A CG2 
157  N N   . THR   A 25  ? 1.2739 1.4594 0.3580 0.6519  0.3019  0.0519  68  THR   A N   
158  C CA  . THR   A 25  ? 1.2329 1.4851 0.3772 0.6403  0.3474  0.0739  68  THR   A CA  
159  C C   . THR   A 25  ? 1.2000 1.4593 0.4316 0.6104  0.3271  0.0605  68  THR   A C   
160  O O   . THR   A 25  ? 1.2117 1.4260 0.4632 0.5848  0.2877  0.0483  68  THR   A O   
161  C CB  . THR   A 25  ? 1.2379 1.5141 0.3976 0.6088  0.3894  0.1254  68  THR   A CB  
162  O OG1 . THR   A 25  ? 1.2127 1.5633 0.4237 0.6039  0.4357  0.1458  68  THR   A OG1 
163  C CG2 . THR   A 25  ? 1.2325 1.4770 0.4479 0.5568  0.3698  0.1404  68  THR   A CG2 
164  N N   . GLY   A 26  ? 1.1563 1.4760 0.4398 0.6145  0.3540  0.0636  69  GLY   A N   
165  C CA  . GLY   A 26  ? 1.1245 1.4533 0.4883 0.5882  0.3344  0.0535  69  GLY   A CA  
166  C C   . GLY   A 26  ? 1.1144 1.4459 0.4797 0.6258  0.3125  0.0154  69  GLY   A C   
167  O O   . GLY   A 26  ? 1.1468 1.4262 0.4539 0.6562  0.2782  -0.0171 69  GLY   A O   
168  N N   . ASN   A 27  ? 1.0670 1.4559 0.5020 0.6231  0.3277  0.0186  70  ASN   A N   
169  C CA  . ASN   A 27  ? 1.0560 1.4519 0.5023 0.6615  0.3072  -0.0158 70  ASN   A CA  
170  C C   . ASN   A 27  ? 1.0382 1.3745 0.5125 0.6366  0.2527  -0.0340 70  ASN   A C   
171  O O   . ASN   A 27  ? 1.0432 1.3476 0.5349 0.5886  0.2385  -0.0183 70  ASN   A O   
172  C CB  . ASN   A 27  ? 1.0265 1.5214 0.5366 0.6768  0.3489  -0.0044 70  ASN   A CB  
173  C CG  . ASN   A 27  ? 1.0368 1.5675 0.6444 0.6276  0.3483  0.0171  70  ASN   A CG  
174  O OD1 . ASN   A 27  ? 1.0477 1.5730 0.6808 0.5762  0.3567  0.0472  70  ASN   A OD1 
175  N ND2 . ASN   A 27  ? 1.0181 1.5824 0.6799 0.6449  0.3345  0.0000  70  ASN   A ND2 
176  N N   . SER   A 28  ? 1.0195 1.3368 0.4910 0.6717  0.2224  -0.0667 71  SER   A N   
177  C CA  . SER   A 28  ? 1.0194 1.2757 0.5080 0.6521  0.1707  -0.0816 71  SER   A CA  
178  C C   . SER   A 28  ? 0.9652 1.2642 0.5229 0.6571  0.1672  -0.0831 71  SER   A C   
179  O O   . SER   A 28  ? 0.9799 1.2732 0.5291 0.7040  0.1495  -0.1108 71  SER   A O   
180  C CB  . SER   A 28  ? 1.0781 1.2563 0.4988 0.6873  0.1269  -0.1186 71  SER   A CB  
181  O OG  . SER   A 28  ? 1.1344 1.2700 0.4947 0.6814  0.1202  -0.1202 71  SER   A OG  
182  N N   . PRO   A 29  ? 0.9033 1.2422 0.5286 0.6122  0.1796  -0.0559 72  PRO   A N   
183  C CA  . PRO   A 29  ? 0.8483 1.2348 0.5427 0.6182  0.1738  -0.0572 72  PRO   A CA  
184  C C   . PRO   A 29  ? 0.8458 1.1703 0.5495 0.5995  0.1214  -0.0661 72  PRO   A C   
185  O O   . PRO   A 29  ? 0.8687 1.1388 0.5549 0.5564  0.1026  -0.0561 72  PRO   A O   
186  C CB  . PRO   A 29  ? 0.8111 1.2743 0.5717 0.5791  0.2135  -0.0231 72  PRO   A CB  
187  C CG  . PRO   A 29  ? 0.8465 1.2749 0.5686 0.5420  0.2280  -0.0030 72  PRO   A CG  
188  C CD  . PRO   A 29  ? 0.8860 1.2318 0.5283 0.5586  0.1993  -0.0244 72  PRO   A CD  
189  N N   . ARG   A 30  ? 0.8168 1.1511 0.5467 0.6332  0.0982  -0.0837 73  ARG   A N   
190  C CA  . ARG   A 30  ? 0.8260 1.1008 0.5624 0.6160  0.0478  -0.0875 73  ARG   A CA  
191  C C   . ARG   A 30  ? 0.7565 1.0958 0.5722 0.5945  0.0512  -0.0707 73  ARG   A C   
192  O O   . ARG   A 30  ? 0.7121 1.1252 0.5793 0.6286  0.0640  -0.0769 73  ARG   A O   
193  C CB  . ARG   A 30  ? 0.8793 1.0965 0.5799 0.6675  0.0069  -0.1190 73  ARG   A CB  
194  C CG  . ARG   A 30  ? 0.9816 1.1210 0.6022 0.6813  -0.0075 -0.1373 73  ARG   A CG  
195  C CD  . ARG   A 30  ? 1.0672 1.1218 0.6474 0.7189  -0.0604 -0.1664 73  ARG   A CD  
196  N NE  . ARG   A 30  ? 1.1415 1.1583 0.6562 0.7606  -0.0629 -0.1949 73  ARG   A NE  
197  C CZ  . ARG   A 30  ? 1.2320 1.1721 0.7006 0.8042  -0.1063 -0.2275 73  ARG   A CZ  
198  N NH1 . ARG   A 30  ? 1.2437 1.1326 0.7243 0.8110  -0.1512 -0.2327 73  ARG   A NH1 
199  N NH2 . ARG   A 30  ? 1.2771 1.1858 0.6830 0.8431  -0.1080 -0.2558 73  ARG   A NH2 
200  N N   . LEU   A 31  ? 0.7433 1.0608 0.5702 0.5388  0.0410  -0.0504 74  LEU   A N   
201  C CA  . LEU   A 31  ? 0.6955 1.0677 0.5922 0.5122  0.0404  -0.0350 74  LEU   A CA  
202  C C   . LEU   A 31  ? 0.7030 1.0196 0.5943 0.4950  -0.0099 -0.0352 74  LEU   A C   
203  O O   . LEU   A 31  ? 0.7536 0.9858 0.5860 0.4815  -0.0364 -0.0370 74  LEU   A O   
204  C CB  . LEU   A 31  ? 0.6831 1.0821 0.5976 0.4616  0.0732  -0.0106 74  LEU   A CB  
205  C CG  . LEU   A 31  ? 0.6828 1.1343 0.6005 0.4713  0.1240  -0.0022 74  LEU   A CG  
206  C CD1 . LEU   A 31  ? 0.6972 1.1316 0.6009 0.4243  0.1444  0.0189  74  LEU   A CD1 
207  C CD2 . LEU   A 31  ? 0.6332 1.1891 0.6276 0.4892  0.1519  0.0036  74  LEU   A CD2 
208  N N   . ASP   A 32  ? 0.6466 1.0133 0.6001 0.4935  -0.0232 -0.0314 75  ASP   A N   
209  C CA  . ASP   A 32  ? 0.6533 0.9728 0.5998 0.4761  -0.0705 -0.0283 75  ASP   A CA  
210  C C   . ASP   A 32  ? 0.6122 0.9495 0.5813 0.4195  -0.0619 -0.0090 75  ASP   A C   
211  O O   . ASP   A 32  ? 0.5637 0.9783 0.6034 0.4113  -0.0490 -0.0032 75  ASP   A O   
212  C CB  . ASP   A 32  ? 0.6520 1.0155 0.6522 0.5167  -0.0976 -0.0397 75  ASP   A CB  
213  C CG  . ASP   A 32  ? 0.7554 1.0520 0.7123 0.5644  -0.1374 -0.0584 75  ASP   A CG  
214  O OD1 . ASP   A 32  ? 0.8084 1.0114 0.7069 0.5468  -0.1757 -0.0533 75  ASP   A OD1 
215  O OD2 . ASP   A 32  ? 0.7724 1.1099 0.7539 0.6199  -0.1308 -0.0776 75  ASP   A OD2 
216  N N   . VAL   A 33  ? 0.6272 0.8972 0.5396 0.3811  -0.0675 0.0001  76  VAL   A N   
217  C CA  . VAL   A 33  ? 0.6023 0.8807 0.5262 0.3327  -0.0603 0.0136  76  VAL   A CA  
218  C C   . VAL   A 33  ? 0.6107 0.8299 0.4951 0.3083  -0.1007 0.0181  76  VAL   A C   
219  O O   . VAL   A 33  ? 0.6377 0.8038 0.4827 0.3248  -0.1324 0.0152  76  VAL   A O   
220  C CB  . VAL   A 33  ? 0.6204 0.8899 0.5194 0.3087  -0.0217 0.0211  76  VAL   A CB  
221  C CG1 . VAL   A 33  ? 0.6001 0.9231 0.5260 0.3332  0.0174  0.0201  76  VAL   A CG1 
222  C CG2 . VAL   A 33  ? 0.6756 0.8683 0.5010 0.3004  -0.0311 0.0202  76  VAL   A CG2 
223  N N   . ALA   A 34  ? 0.5853 0.8114 0.4775 0.2704  -0.1007 0.0253  77  ALA   A N   
224  C CA  . ALA   A 34  ? 0.6046 0.7794 0.4511 0.2468  -0.1333 0.0297  77  ALA   A CA  
225  C C   . ALA   A 34  ? 0.6035 0.7609 0.4217 0.2086  -0.1129 0.0343  77  ALA   A C   
226  O O   . ALA   A 34  ? 0.5810 0.7775 0.4398 0.1934  -0.0919 0.0340  77  ALA   A O   
227  C CB  . ALA   A 34  ? 0.5794 0.7838 0.4665 0.2501  -0.1690 0.0271  77  ALA   A CB  
228  N N   . LEU   A 35  ? 0.6240 0.7226 0.3734 0.1936  -0.1190 0.0393  78  LEU   A N   
229  C CA  . LEU   A 35  ? 0.6219 0.7042 0.3396 0.1640  -0.0994 0.0410  78  LEU   A CA  
230  C C   . LEU   A 35  ? 0.6346 0.6974 0.3231 0.1442  -0.1260 0.0404  78  LEU   A C   
231  O O   . LEU   A 35  ? 0.6599 0.6907 0.3110 0.1476  -0.1574 0.0458  78  LEU   A O   
232  C CB  . LEU   A 35  ? 0.6397 0.6825 0.3058 0.1603  -0.0846 0.0464  78  LEU   A CB  
233  C CG  . LEU   A 35  ? 0.6519 0.6858 0.2897 0.1369  -0.0603 0.0466  78  LEU   A CG  
234  C CD1 . LEU   A 35  ? 0.6277 0.6960 0.3066 0.1367  -0.0311 0.0411  78  LEU   A CD1 
235  C CD2 . LEU   A 35  ? 0.6768 0.6798 0.2718 0.1318  -0.0519 0.0535  78  LEU   A CD2 
236  N N   . ASP   A 36  ? 0.6133 0.6908 0.3153 0.1251  -0.1164 0.0336  79  ASP   A N   
237  C CA  . ASP   A 36  ? 0.6242 0.6823 0.2947 0.1088  -0.1426 0.0282  79  ASP   A CA  
238  C C   . ASP   A 36  ? 0.6621 0.6824 0.2620 0.0923  -0.1260 0.0269  79  ASP   A C   
239  O O   . ASP   A 36  ? 0.6603 0.6780 0.2508 0.0915  -0.0933 0.0297  79  ASP   A O   
240  C CB  . ASP   A 36  ? 0.6008 0.6966 0.3344 0.0995  -0.1539 0.0183  79  ASP   A CB  
241  C CG  . ASP   A 36  ? 0.6357 0.7414 0.3936 0.0828  -0.1247 0.0128  79  ASP   A CG  
242  O OD1 . ASP   A 36  ? 0.6590 0.7418 0.3796 0.0807  -0.0954 0.0139  79  ASP   A OD1 
243  O OD2 . ASP   A 36  ? 0.6362 0.7712 0.4521 0.0712  -0.1334 0.0083  79  ASP   A OD2 
244  N N   . GLU   A 37  ? 0.6909 0.6860 0.2412 0.0816  -0.1492 0.0216  80  GLU   A N   
245  C CA  . GLU   A 37  ? 0.7353 0.7022 0.2167 0.0697  -0.1339 0.0175  80  GLU   A CA  
246  C C   . GLU   A 37  ? 0.7375 0.7150 0.2401 0.0643  -0.1026 0.0046  80  GLU   A C   
247  O O   . GLU   A 37  ? 0.7618 0.7289 0.2256 0.0623  -0.0762 0.0038  80  GLU   A O   
248  C CB  . GLU   A 37  ? 0.7842 0.7275 0.2142 0.0635  -0.1677 0.0090  80  GLU   A CB  
249  C CG  . GLU   A 37  ? 0.8685 0.7801 0.2054 0.0576  -0.1591 0.0142  80  GLU   A CG  
250  C CD  . GLU   A 37  ? 0.9298 0.8173 0.2094 0.0545  -0.1926 0.0014  80  GLU   A CD  
251  O OE1 . GLU   A 37  ? 0.9178 0.8051 0.2049 0.0512  -0.1963 -0.0227 80  GLU   A OE1 
252  O OE2 . GLU   A 37  ? 0.9730 0.8368 0.1979 0.0560  -0.2185 0.0154  80  GLU   A OE2 
253  N N   . SER   A 38  ? 0.7042 0.7039 0.2714 0.0620  -0.1051 -0.0033 81  SER   A N   
254  C CA  . SER   A 38  ? 0.6927 0.6941 0.2815 0.0569  -0.0789 -0.0120 81  SER   A CA  
255  C C   . SER   A 38  ? 0.6662 0.6852 0.2816 0.0664  -0.0432 -0.0003 81  SER   A C   
256  O O   . SER   A 38  ? 0.6629 0.6775 0.2858 0.0652  -0.0208 -0.0048 81  SER   A O   
257  C CB  . SER   A 38  ? 0.6951 0.7089 0.3418 0.0450  -0.0968 -0.0202 81  SER   A CB  
258  O OG  . SER   A 38  ? 0.7524 0.7461 0.3707 0.0365  -0.1349 -0.0346 81  SER   A OG  
259  N N   . GLY   A 39  ? 0.6519 0.6853 0.2776 0.0778  -0.0416 0.0130  82  GLY   A N   
260  C CA  . GLY   A 39  ? 0.6447 0.6919 0.2891 0.0893  -0.0134 0.0216  82  GLY   A CA  
261  C C   . GLY   A 39  ? 0.6070 0.6884 0.3157 0.0971  -0.0040 0.0268  82  GLY   A C   
262  O O   . GLY   A 39  ? 0.5964 0.6879 0.3151 0.1084  0.0195  0.0327  82  GLY   A O   
263  N N   . ASP   A 40  ? 0.5843 0.6874 0.3369 0.0909  -0.0221 0.0252  83  ASP   A N   
264  C CA  . ASP   A 40  ? 0.5509 0.6984 0.3721 0.0944  -0.0120 0.0324  83  ASP   A CA  
265  C C   . ASP   A 40  ? 0.5407 0.7187 0.3864 0.1177  -0.0202 0.0370  83  ASP   A C   
266  O O   . ASP   A 40  ? 0.5406 0.7202 0.3882 0.1213  -0.0519 0.0333  83  ASP   A O   
267  C CB  . ASP   A 40  ? 0.5549 0.7166 0.4193 0.0730  -0.0321 0.0278  83  ASP   A CB  
268  C CG  . ASP   A 40  ? 0.6409 0.7707 0.4927 0.0519  -0.0251 0.0219  83  ASP   A CG  
269  O OD1 . ASP   A 40  ? 0.6553 0.7803 0.5092 0.0530  0.0047  0.0294  83  ASP   A OD1 
270  O OD2 . ASP   A 40  ? 0.6955 0.8014 0.5328 0.0364  -0.0528 0.0085  83  ASP   A OD2 
271  N N   . PHE   A 41  ? 0.5306 0.7313 0.3927 0.1366  0.0064  0.0437  84  PHE   A N   
272  C CA  . PHE   A 41  ? 0.5219 0.7511 0.4056 0.1659  0.0025  0.0443  84  PHE   A CA  
273  C C   . PHE   A 41  ? 0.4991 0.7930 0.4602 0.1678  0.0027  0.0477  84  PHE   A C   
274  O O   . PHE   A 41  ? 0.4753 0.7994 0.4750 0.1531  0.0268  0.0564  84  PHE   A O   
275  C CB  . PHE   A 41  ? 0.5172 0.7446 0.3815 0.1873  0.0310  0.0469  84  PHE   A CB  
276  C CG  . PHE   A 41  ? 0.5505 0.7250 0.3509 0.1920  0.0244  0.0430  84  PHE   A CG  
277  C CD1 . PHE   A 41  ? 0.5669 0.7186 0.3451 0.2098  -0.0003 0.0385  84  PHE   A CD1 
278  C CD2 . PHE   A 41  ? 0.5694 0.7179 0.3362 0.1786  0.0417  0.0446  84  PHE   A CD2 
279  C CE1 . PHE   A 41  ? 0.6023 0.7062 0.3281 0.2077  -0.0072 0.0381  84  PHE   A CE1 
280  C CE2 . PHE   A 41  ? 0.6006 0.7118 0.3202 0.1799  0.0361  0.0425  84  PHE   A CE2 
281  C CZ  . PHE   A 41  ? 0.6110 0.7002 0.3115 0.1915  0.0121  0.0404  84  PHE   A CZ  
282  N N   . SER   A 42  ? 0.5072 0.8239 0.4938 0.1856  -0.0247 0.0425  85  SER   A N   
283  C CA  . SER   A 42  ? 0.4838 0.8748 0.5548 0.1904  -0.0281 0.0445  85  SER   A CA  
284  C C   . SER   A 42  ? 0.4926 0.9198 0.5838 0.2345  -0.0247 0.0401  85  SER   A C   
285  O O   . SER   A 42  ? 0.5270 0.9111 0.5723 0.2576  -0.0487 0.0318  85  SER   A O   
286  C CB  . SER   A 42  ? 0.4998 0.8918 0.5915 0.1742  -0.0723 0.0385  85  SER   A CB  
287  O OG  . SER   A 42  ? 0.5752 0.9028 0.5972 0.1783  -0.1062 0.0317  85  SER   A OG  
288  N N   . LEU   A 43  ? 0.4614 0.9654 0.6179 0.2471  0.0053  0.0461  86  LEU   A N   
289  C CA  . LEU   A 43  ? 0.4613 1.0070 0.6376 0.2959  0.0118  0.0382  86  LEU   A CA  
290  C C   . LEU   A 43  ? 0.4566 1.0331 0.6777 0.3166  -0.0294 0.0279  86  LEU   A C   
291  O O   . LEU   A 43  ? 0.4117 1.0505 0.7088 0.2994  -0.0393 0.0321  86  LEU   A O   
292  C CB  . LEU   A 43  ? 0.4199 1.0486 0.6524 0.3041  0.0604  0.0492  86  LEU   A CB  
293  C CG  . LEU   A 43  ? 0.4706 1.0806 0.6483 0.3312  0.0957  0.0485  86  LEU   A CG  
294  C CD1 . LEU   A 43  ? 0.4333 1.1261 0.6607 0.3343  0.1459  0.0644  86  LEU   A CD1 
295  C CD2 . LEU   A 43  ? 0.5061 1.0913 0.6463 0.3836  0.0765  0.0272  86  LEU   A CD2 
296  N N   . VAL   A 44  ? 0.5010 1.0304 0.6757 0.3530  -0.0571 0.0147  87  VAL   A N   
297  C CA  . VAL   A 44  ? 0.5051 1.0484 0.7087 0.3819  -0.1018 0.0041  87  VAL   A CA  
298  C C   . VAL   A 44  ? 0.4824 1.1002 0.7393 0.4360  -0.0850 -0.0067 87  VAL   A C   
299  O O   . VAL   A 44  ? 0.5026 1.1063 0.7221 0.4635  -0.0569 -0.0127 87  VAL   A O   
300  C CB  . VAL   A 44  ? 0.5769 1.0139 0.6916 0.3893  -0.1433 -0.0010 87  VAL   A CB  
301  C CG1 . VAL   A 44  ? 0.5779 1.0160 0.7094 0.4325  -0.1890 -0.0123 87  VAL   A CG1 
302  C CG2 . VAL   A 44  ? 0.6168 0.9981 0.6874 0.3399  -0.1610 0.0090  87  VAL   A CG2 
303  N N   . GLU   A 45  ? 0.4343 1.1366 0.7798 0.4528  -0.1012 -0.0107 88  GLU   A N   
304  C CA  . GLU   A 45  ? 0.4063 1.1934 0.8102 0.5089  -0.0828 -0.0227 88  GLU   A CA  
305  C C   . GLU   A 45  ? 0.4010 1.2066 0.8434 0.5523  -0.1359 -0.0385 88  GLU   A C   
306  O O   . GLU   A 45  ? 0.3591 1.2411 0.8584 0.6061  -0.1283 -0.0524 88  GLU   A O   
307  C CB  . GLU   A 45  ? 0.3659 1.2761 0.8645 0.4913  -0.0312 -0.0086 88  GLU   A CB  
308  C CG  . GLU   A 45  ? 0.4430 1.3333 0.9052 0.4499  0.0179  0.0100  88  GLU   A CG  
309  C CD  . GLU   A 45  ? 0.5404 1.4097 0.9399 0.4849  0.0579  0.0044  88  GLU   A CD  
310  O OE1 . GLU   A 45  ? 0.5142 1.4724 0.9594 0.5219  0.0947  0.0018  88  GLU   A OE1 
311  O OE2 . GLU   A 45  ? 0.6213 1.3892 0.9265 0.4759  0.0526  0.0022  88  GLU   A OE2 
312  N N   . GLY   B 7   ? 0.9145 0.9751 0.5024 0.3723  0.0995  -0.0924 16  GLY   B N   
313  C CA  . GLY   B 7   ? 0.9240 0.9768 0.5158 0.3946  0.0904  -0.0869 16  GLY   B CA  
314  C C   . GLY   B 7   ? 0.9212 0.9936 0.5217 0.3884  0.0786  -0.0780 16  GLY   B C   
315  O O   . GLY   B 7   ? 0.9066 1.0203 0.5258 0.3778  0.0765  -0.0814 16  GLY   B O   
316  N N   . GLU   B 8   ? 0.9288 0.9717 0.5151 0.3948  0.0704  -0.0663 17  GLU   B N   
317  C CA  . GLU   B 8   ? 0.9204 0.9774 0.5093 0.3923  0.0577  -0.0597 17  GLU   B CA  
318  C C   . GLU   B 8   ? 0.9097 0.9677 0.4936 0.3648  0.0558  -0.0570 17  GLU   B C   
319  O O   . GLU   B 8   ? 0.9252 0.9534 0.4913 0.3531  0.0599  -0.0509 17  GLU   B O   
320  C CB  . GLU   B 8   ? 0.9668 0.9968 0.5396 0.4104  0.0506  -0.0478 17  GLU   B CB  
321  C CG  . GLU   B 8   ? 1.0261 1.0752 0.6006 0.4144  0.0359  -0.0447 17  GLU   B CG  
322  C CD  . GLU   B 8   ? 1.1334 1.1545 0.6835 0.4202  0.0312  -0.0308 17  GLU   B CD  
323  O OE1 . GLU   B 8   ? 1.1613 1.1531 0.6965 0.4102  0.0394  -0.0226 17  GLU   B OE1 
324  O OE2 . GLU   B 8   ? 1.1644 1.1955 0.7105 0.4354  0.0191  -0.0280 17  GLU   B OE2 
325  N N   A THR   B 9   ? 0.8854 0.9774 0.4861 0.3543  0.0482  -0.0612 18  THR   B N   
326  N N   B THR   B 9   ? 0.8853 0.9774 0.4860 0.3543  0.0482  -0.0612 18  THR   B N   
327  C CA  A THR   B 9   ? 0.8833 0.9756 0.4805 0.3290  0.0439  -0.0589 18  THR   B CA  
328  C CA  B THR   B 9   ? 0.8834 0.9756 0.4806 0.3290  0.0439  -0.0589 18  THR   B CA  
329  C C   A THR   B 9   ? 0.8712 0.9685 0.4682 0.3304  0.0258  -0.0567 18  THR   B C   
330  C C   B THR   B 9   ? 0.8711 0.9683 0.4680 0.3304  0.0258  -0.0567 18  THR   B C   
331  O O   A THR   B 9   ? 0.8673 0.9769 0.4717 0.3115  0.0178  -0.0582 18  THR   B O   
332  O O   B THR   B 9   ? 0.8672 0.9768 0.4716 0.3115  0.0178  -0.0582 18  THR   B O   
333  C CB  A THR   B 9   ? 0.8854 1.0095 0.5013 0.3096  0.0509  -0.0649 18  THR   B CB  
334  C CB  B THR   B 9   ? 0.8853 1.0093 0.5011 0.3096  0.0509  -0.0649 18  THR   B CB  
335  O OG1 A THR   B 9   ? 0.8781 1.0440 0.5211 0.3199  0.0489  -0.0713 18  THR   B OG1 
336  O OG1 B THR   B 9   ? 0.8780 1.0439 0.5210 0.3199  0.0489  -0.0713 18  THR   B OG1 
337  C CG2 A THR   B 9   ? 0.8974 1.0091 0.5037 0.3037  0.0675  -0.0675 18  THR   B CG2 
338  C CG2 B THR   B 9   ? 0.8974 1.0091 0.5036 0.3037  0.0675  -0.0675 18  THR   B CG2 
339  N N   . THR   B 10  ? 0.8656 0.9513 0.4521 0.3529  0.0185  -0.0529 19  THR   B N   
340  C CA  . THR   B 10  ? 0.8499 0.9390 0.4313 0.3586  0.0002  -0.0527 19  THR   B CA  
341  C C   . THR   B 10  ? 0.8397 0.9013 0.3977 0.3478  -0.0040 -0.0474 19  THR   B C   
342  O O   . THR   B 10  ? 0.8549 0.8906 0.3948 0.3492  0.0061  -0.0393 19  THR   B O   
343  C CB  . THR   B 10  ? 0.8768 0.9649 0.4518 0.3887  -0.0053 -0.0497 19  THR   B CB  
344  O OG1 . THR   B 10  ? 0.8833 0.9988 0.4817 0.3996  -0.0024 -0.0557 19  THR   B OG1 
345  C CG2 . THR   B 10  ? 0.8782 0.9700 0.4437 0.3986  -0.0254 -0.0511 19  THR   B CG2 
346  N N   . ASP   B 11  ? 0.8105 0.8776 0.3697 0.3374  -0.0199 -0.0519 20  ASP   B N   
347  C CA  . ASP   B 11  ? 0.8089 0.8504 0.3453 0.3306  -0.0260 -0.0488 20  ASP   B CA  
348  C C   . ASP   B 11  ? 0.7988 0.8198 0.3083 0.3536  -0.0246 -0.0407 20  ASP   B C   
349  O O   . ASP   B 11  ? 0.7942 0.8221 0.3013 0.3755  -0.0274 -0.0393 20  ASP   B O   
350  C CB  . ASP   B 11  ? 0.8309 0.8782 0.3715 0.3219  -0.0480 -0.0569 20  ASP   B CB  
351  C CG  . ASP   B 11  ? 0.8991 0.9496 0.4536 0.2916  -0.0487 -0.0585 20  ASP   B CG  
352  O OD1 . ASP   B 11  ? 0.8939 0.9648 0.4694 0.2788  -0.0358 -0.0578 20  ASP   B OD1 
353  O OD2 . ASP   B 11  ? 0.9426 0.9747 0.4856 0.2818  -0.0623 -0.0602 20  ASP   B OD2 
354  N N   . GLY   B 12  ? 0.7902 0.7893 0.2804 0.3489  -0.0196 -0.0341 21  GLY   B N   
355  C CA  . GLY   B 12  ? 0.7855 0.7710 0.2519 0.3690  -0.0165 -0.0240 21  GLY   B CA  
356  C C   . GLY   B 12  ? 0.7709 0.7398 0.2278 0.3612  -0.0014 -0.0128 21  GLY   B C   
357  O O   . GLY   B 12  ? 0.7657 0.7297 0.2293 0.3402  0.0035  -0.0146 21  GLY   B O   
358  N N   . VAL   B 13  ? 0.7648 0.7268 0.2065 0.3778  0.0056  0.0001  22  VAL   B N   
359  C CA  . VAL   B 13  ? 0.7625 0.7124 0.1974 0.3711  0.0189  0.0130  22  VAL   B CA  
360  C C   . VAL   B 13  ? 0.7563 0.6991 0.1991 0.3724  0.0325  0.0234  22  VAL   B C   
361  O O   . VAL   B 13  ? 0.7500 0.6954 0.1924 0.3894  0.0319  0.0269  22  VAL   B O   
362  C CB  . VAL   B 13  ? 0.7739 0.7236 0.1863 0.3857  0.0163  0.0215  22  VAL   B CB  
363  C CG1 . VAL   B 13  ? 0.7816 0.7383 0.1795 0.4131  0.0144  0.0294  22  VAL   B CG1 
364  C CG2 . VAL   B 13  ? 0.7769 0.7203 0.1875 0.3754  0.0290  0.0345  22  VAL   B CG2 
365  N N   . TYR   B 14  ? 0.7589 0.6909 0.2092 0.3540  0.0427  0.0265  23  TYR   B N   
366  C CA  . TYR   B 14  ? 0.7634 0.6823 0.2217 0.3522  0.0532  0.0331  23  TYR   B CA  
367  C C   . TYR   B 14  ? 0.7733 0.6785 0.2282 0.3432  0.0624  0.0485  23  TYR   B C   
368  O O   . TYR   B 14  ? 0.7782 0.6866 0.2289 0.3331  0.0625  0.0510  23  TYR   B O   
369  C CB  . TYR   B 14  ? 0.7535 0.6719 0.2267 0.3379  0.0554  0.0186  23  TYR   B CB  
370  C CG  . TYR   B 14  ? 0.7469 0.6823 0.2299 0.3476  0.0487  0.0064  23  TYR   B CG  
371  C CD1 . TYR   B 14  ? 0.7474 0.7005 0.2318 0.3463  0.0375  -0.0022 23  TYR   B CD1 
372  C CD2 . TYR   B 14  ? 0.7537 0.6879 0.2466 0.3571  0.0525  0.0028  23  TYR   B CD2 
373  C CE1 . TYR   B 14  ? 0.7486 0.7213 0.2459 0.3534  0.0301  -0.0125 23  TYR   B CE1 
374  C CE2 . TYR   B 14  ? 0.7546 0.7106 0.2599 0.3667  0.0463  -0.0080 23  TYR   B CE2 
375  C CZ  . TYR   B 14  ? 0.7588 0.7359 0.2676 0.3638  0.0351  -0.0150 23  TYR   B CZ  
376  O OH  . TYR   B 14  ? 0.7710 0.7734 0.2959 0.3712  0.0277  -0.0249 23  TYR   B OH  
377  N N   . ARG   B 15  ? 0.7755 0.6649 0.2339 0.3462  0.0690  0.0587  24  ARG   B N   
378  C CA  . ARG   B 15  ? 0.7852 0.6603 0.2448 0.3349  0.0766  0.0744  24  ARG   B CA  
379  C C   . ARG   B 15  ? 0.7885 0.6457 0.2584 0.3162  0.0792  0.0640  24  ARG   B C   
380  O O   . ARG   B 15  ? 0.7901 0.6378 0.2647 0.3214  0.0788  0.0537  24  ARG   B O   
381  C CB  . ARG   B 15  ? 0.8061 0.6693 0.2627 0.3484  0.0807  0.0938  24  ARG   B CB  
382  C CG  . ARG   B 15  ? 0.8373 0.7173 0.2797 0.3702  0.0794  0.1071  24  ARG   B CG  
383  C CD  . ARG   B 15  ? 0.8839 0.7491 0.3242 0.3773  0.0857  0.1312  24  ARG   B CD  
384  N NE  . ARG   B 15  ? 0.9270 0.8071 0.3510 0.4017  0.0849  0.1446  24  ARG   B NE  
385  C CZ  . ARG   B 15  ? 0.9519 0.8509 0.3647 0.4078  0.0898  0.1619  24  ARG   B CZ  
386  N NH1 . ARG   B 15  ? 0.9404 0.8474 0.3599 0.3906  0.0957  0.1686  24  ARG   B NH1 
387  N NH2 . ARG   B 15  ? 0.9410 0.8540 0.3353 0.4326  0.0888  0.1723  24  ARG   B NH2 
388  N N   . VAL   B 16  ? 0.7870 0.6403 0.2595 0.2967  0.0815  0.0666  25  VAL   B N   
389  C CA  . VAL   B 16  ? 0.7969 0.6322 0.2756 0.2787  0.0827  0.0566  25  VAL   B CA  
390  C C   . VAL   B 16  ? 0.8058 0.6168 0.2892 0.2729  0.0856  0.0726  25  VAL   B C   
391  O O   . VAL   B 16  ? 0.8030 0.6204 0.2884 0.2669  0.0876  0.0906  25  VAL   B O   
392  C CB  . VAL   B 16  ? 0.8015 0.6473 0.2793 0.2606  0.0810  0.0494  25  VAL   B CB  
393  C CG1 . VAL   B 16  ? 0.8100 0.6410 0.2898 0.2456  0.0813  0.0345  25  VAL   B CG1 
394  C CG2 . VAL   B 16  ? 0.8023 0.6704 0.2748 0.2663  0.0766  0.0409  25  VAL   B CG2 
395  N N   . MET   B 17  ? 0.8123 0.5966 0.2979 0.2764  0.0853  0.0673  26  MET   B N   
396  C CA  . MET   B 17  ? 0.8293 0.5836 0.3189 0.2722  0.0857  0.0830  26  MET   B CA  
397  C C   . MET   B 17  ? 0.8658 0.5890 0.3586 0.2569  0.0824  0.0713  26  MET   B C   
398  O O   . MET   B 17  ? 0.8737 0.5954 0.3628 0.2578  0.0812  0.0487  26  MET   B O   
399  C CB  . MET   B 17  ? 0.8258 0.5667 0.3122 0.2946  0.0856  0.0891  26  MET   B CB  
400  C CG  . MET   B 17  ? 0.8138 0.5826 0.2938 0.3141  0.0869  0.0981  26  MET   B CG  
401  S SD  . MET   B 17  ? 0.7586 0.5385 0.2362 0.3140  0.0919  0.1315  26  MET   B SD  
402  C CE  . MET   B 17  ? 0.6926 0.4306 0.1751 0.3096  0.0922  0.1503  26  MET   B CE  
403  N N   . THR   B 18  ? 0.8927 0.5896 0.3916 0.2439  0.0803  0.0868  27  THR   B N   
404  C CA  . THR   B 18  ? 0.9323 0.5925 0.4324 0.2302  0.0740  0.0745  27  THR   B CA  
405  C C   . THR   B 18  ? 0.9816 0.5973 0.4848 0.2313  0.0696  0.0881  27  THR   B C   
406  O O   . THR   B 18  ? 0.9798 0.5947 0.4897 0.2288  0.0717  0.1158  27  THR   B O   
407  C CB  . THR   B 18  ? 0.9366 0.6043 0.4421 0.2048  0.0709  0.0731  27  THR   B CB  
408  O OG1 . THR   B 18  ? 0.9654 0.6013 0.4661 0.1962  0.0637  0.0524  27  THR   B OG1 
409  C CG2 . THR   B 18  ? 0.9339 0.6022 0.4531 0.1886  0.0704  0.1010  27  THR   B CG2 
410  N N   . ARG   B 19  ? 1.0169 0.5950 0.5139 0.2366  0.0635  0.0688  28  ARG   B N   
411  C CA  . ARG   B 19  ? 1.0546 0.5813 0.5527 0.2372  0.0564  0.0788  28  ARG   B CA  
412  C C   . ARG   B 19  ? 1.0733 0.5637 0.5763 0.2101  0.0456  0.0752  28  ARG   B C   
413  O O   . ARG   B 19  ? 1.0904 0.5305 0.5943 0.2065  0.0365  0.0807  28  ARG   B O   
414  C CB  . ARG   B 19  ? 1.0920 0.5955 0.5790 0.2652  0.0546  0.0609  28  ARG   B CB  
415  C CG  . ARG   B 19  ? 1.1411 0.6674 0.6265 0.2902  0.0610  0.0738  28  ARG   B CG  
416  C CD  . ARG   B 19  ? 1.2038 0.7249 0.6812 0.3193  0.0602  0.0521  28  ARG   B CD  
417  N NE  . ARG   B 19  ? 1.2442 0.7780 0.7203 0.3431  0.0628  0.0672  28  ARG   B NE  
418  C CZ  . ARG   B 19  ? 1.2619 0.8192 0.7357 0.3684  0.0646  0.0525  28  ARG   B CZ  
419  N NH1 . ARG   B 19  ? 1.2533 0.8272 0.7272 0.3727  0.0661  0.0239  28  ARG   B NH1 
420  N NH2 . ARG   B 19  ? 1.2527 0.8209 0.7248 0.3892  0.0650  0.0672  28  ARG   B NH2 
421  N N   . ARG   B 20  ? 1.0673 0.5834 0.5740 0.1907  0.0455  0.0677  29  ARG   B N   
422  C CA  . ARG   B 20  ? 1.0840 0.5784 0.5949 0.1647  0.0346  0.0605  29  ARG   B CA  
423  C C   . ARG   B 20  ? 1.0830 0.5647 0.6138 0.1399  0.0292  0.0910  29  ARG   B C   
424  O O   . ARG   B 20  ? 1.0948 0.5430 0.6310 0.1185  0.0160  0.0868  29  ARG   B O   
425  C CB  . ARG   B 20  ? 1.0933 0.6289 0.6007 0.1565  0.0377  0.0454  29  ARG   B CB  
426  C CG  . ARG   B 20  ? 1.1443 0.6630 0.6499 0.1346  0.0259  0.0294  29  ARG   B CG  
427  C CD  . ARG   B 20  ? 1.1782 0.7434 0.6815 0.1273  0.0302  0.0226  29  ARG   B CD  
428  N NE  . ARG   B 20  ? 1.1968 0.8020 0.7166 0.1196  0.0368  0.0496  29  ARG   B NE  
429  C CZ  . ARG   B 20  ? 1.2160 0.8398 0.7485 0.0979  0.0321  0.0596  29  ARG   B CZ  
430  N NH1 . ARG   B 20  ? 1.2261 0.8322 0.7566 0.0800  0.0196  0.0448  29  ARG   B NH1 
431  N NH2 . ARG   B 20  ? 1.1920 0.8546 0.7385 0.0957  0.0393  0.0835  29  ARG   B NH2 
432  N N   . LEU   B 21  ? 1.0647 0.5738 0.6061 0.1426  0.0388  0.1215  30  LEU   B N   
433  C CA  . LEU   B 21  ? 1.0598 0.5656 0.6223 0.1194  0.0365  0.1545  30  LEU   B CA  
434  C C   . LEU   B 21  ? 1.0648 0.5411 0.6279 0.1299  0.0382  0.1796  30  LEU   B C   
435  O O   . LEU   B 21  ? 1.0798 0.5225 0.6273 0.1516  0.0357  0.1657  30  LEU   B O   
436  C CB  . LEU   B 21  ? 1.0377 0.6067 0.6129 0.1113  0.0468  0.1725  30  LEU   B CB  
437  C CG  . LEU   B 21  ? 1.0429 0.6357 0.6299 0.0869  0.0411  0.1655  30  LEU   B CG  
438  C CD1 . LEU   B 21  ? 1.0656 0.6169 0.6462 0.0736  0.0252  0.1363  30  LEU   B CD1 
439  C CD2 . LEU   B 21  ? 1.0319 0.6795 0.6122 0.0986  0.0508  0.1579  30  LEU   B CD2 
440  N N   . LEU   B 22  ? 1.0500 0.5389 0.6314 0.1147  0.0422  0.2172  31  LEU   B N   
441  C CA  . LEU   B 22  ? 1.0583 0.5232 0.6402 0.1224  0.0449  0.2470  31  LEU   B CA  
442  C C   . LEU   B 22  ? 1.0484 0.5498 0.6145 0.1551  0.0590  0.2506  31  LEU   B C   
443  O O   . LEU   B 22  ? 1.0348 0.5927 0.6031 0.1585  0.0700  0.2571  31  LEU   B O   
444  C CB  . LEU   B 22  ? 1.0452 0.5263 0.6526 0.0948  0.0475  0.2877  31  LEU   B CB  
445  C CG  . LEU   B 22  ? 1.0661 0.5302 0.6747 0.1001  0.0524  0.3251  31  LEU   B CG  
446  C CD1 . LEU   B 22  ? 1.0918 0.4909 0.7133 0.0748  0.0366  0.3382  31  LEU   B CD1 
447  C CD2 . LEU   B 22  ? 1.0464 0.5742 0.6673 0.0971  0.0691  0.3616  31  LEU   B CD2 
448  N N   . GLY   B 23  ? 1.0554 0.5245 0.6051 0.1799  0.0571  0.2439  32  GLY   B N   
449  C CA  . GLY   B 23  ? 1.0497 0.5511 0.5839 0.2118  0.0673  0.2437  32  GLY   B CA  
450  C C   . GLY   B 23  ? 1.0344 0.5703 0.5596 0.2246  0.0701  0.2095  32  GLY   B C   
451  O O   . GLY   B 23  ? 1.0378 0.5654 0.5649 0.2123  0.0641  0.1839  32  GLY   B O   
452  N N   . SER   B 24  ? 1.0134 0.5875 0.5278 0.2490  0.0785  0.2093  33  SER   B N   
453  C CA  . SER   B 24  ? 0.9950 0.6032 0.5023 0.2601  0.0807  0.1806  33  SER   B CA  
454  C C   . SER   B 24  ? 0.9672 0.6260 0.4790 0.2521  0.0883  0.1916  33  SER   B C   
455  O O   . SER   B 24  ? 0.9690 0.6567 0.4746 0.2675  0.0950  0.2081  33  SER   B O   
456  C CB  . SER   B 24  ? 1.0047 0.6210 0.4985 0.2920  0.0820  0.1722  33  SER   B CB  
457  O OG  . SER   B 24  ? 1.0387 0.6104 0.5279 0.3042  0.0753  0.1640  33  SER   B OG  
458  N N   . THR   B 25  ? 0.9421 0.6112 0.4634 0.2299  0.0865  0.1830  34  THR   B N   
459  C CA  . THR   B 25  ? 0.9134 0.6291 0.4399 0.2228  0.0925  0.1926  34  THR   B CA  
460  C C   . THR   B 25  ? 0.8869 0.6341 0.4016 0.2375  0.0938  0.1696  34  THR   B C   
461  O O   . THR   B 25  ? 0.8996 0.6345 0.4097 0.2380  0.0891  0.1430  34  THR   B O   
462  C CB  . THR   B 25  ? 0.9237 0.6353 0.4670 0.1921  0.0880  0.1949  34  THR   B CB  
463  O OG1 . THR   B 25  ? 0.9315 0.6182 0.4888 0.1762  0.0862  0.2208  34  THR   B OG1 
464  C CG2 . THR   B 25  ? 0.9155 0.6751 0.4647 0.1859  0.0926  0.1998  34  THR   B CG2 
465  N N   . GLN   B 26  ? 0.8475 0.6342 0.3569 0.2495  0.0997  0.1796  35  GLN   B N   
466  C CA  . GLN   B 26  ? 0.8258 0.6381 0.3244 0.2618  0.0985  0.1589  35  GLN   B CA  
467  C C   . GLN   B 26  ? 0.8078 0.6406 0.3120 0.2455  0.0973  0.1527  35  GLN   B C   
468  O O   . GLN   B 26  ? 0.8031 0.6642 0.3101 0.2453  0.1015  0.1685  35  GLN   B O   
469  C CB  . GLN   B 26  ? 0.8240 0.6632 0.3097 0.2867  0.1023  0.1687  35  GLN   B CB  
470  C CG  . GLN   B 26  ? 0.8363 0.6904 0.3107 0.3004  0.0974  0.1451  35  GLN   B CG  
471  C CD  . GLN   B 26  ? 0.8710 0.7556 0.3323 0.3199  0.0988  0.1528  35  GLN   B CD  
472  O OE1 . GLN   B 26  ? 0.8925 0.7817 0.3418 0.3412  0.0962  0.1498  35  GLN   B OE1 
473  N NE2 . GLN   B 26  ? 0.8735 0.7803 0.3360 0.3147  0.1020  0.1621  35  GLN   B NE2 
474  N N   . VAL   B 27  ? 0.7944 0.6150 0.2989 0.2339  0.0919  0.1298  36  VAL   B N   
475  C CA  . VAL   B 27  ? 0.7754 0.6106 0.2837 0.2177  0.0890  0.1226  36  VAL   B CA  
476  C C   . VAL   B 27  ? 0.7511 0.6157 0.2493 0.2285  0.0883  0.1148  36  VAL   B C   
477  O O   . VAL   B 27  ? 0.7460 0.6266 0.2465 0.2188  0.0863  0.1144  36  VAL   B O   
478  C CB  . VAL   B 27  ? 0.7908 0.6002 0.2992 0.2030  0.0833  0.1013  36  VAL   B CB  
479  C CG1 . VAL   B 27  ? 0.8074 0.5833 0.3248 0.1914  0.0810  0.1080  36  VAL   B CG1 
480  C CG2 . VAL   B 27  ? 0.7981 0.6023 0.2953 0.2164  0.0827  0.0800  36  VAL   B CG2 
481  N N   . GLY   B 28  ? 0.7307 0.6002 0.2179 0.2482  0.0883  0.1080  37  GLY   B N   
482  C CA  . GLY   B 28  ? 0.7095 0.5992 0.1860 0.2584  0.0847  0.0983  37  GLY   B CA  
483  C C   . GLY   B 28  ? 0.6893 0.5801 0.1564 0.2779  0.0822  0.0894  37  GLY   B C   
484  O O   . GLY   B 28  ? 0.6912 0.5706 0.1593 0.2870  0.0845  0.0931  37  GLY   B O   
485  N N   . VAL   B 29  ? 0.6667 0.5703 0.1249 0.2844  0.0760  0.0779  38  VAL   B N   
486  C CA  . VAL   B 29  ? 0.6482 0.5573 0.0982 0.3016  0.0702  0.0681  38  VAL   B CA  
487  C C   . VAL   B 29  ? 0.6269 0.5364 0.0767 0.2916  0.0626  0.0489  38  VAL   B C   
488  O O   . VAL   B 29  ? 0.6069 0.5156 0.0569 0.2768  0.0615  0.0461  38  VAL   B O   
489  C CB  . VAL   B 29  ? 0.6500 0.5760 0.0866 0.3223  0.0685  0.0784  38  VAL   B CB  
490  C CG1 . VAL   B 29  ? 0.6566 0.5883 0.0823 0.3395  0.0584  0.0659  38  VAL   B CG1 
491  C CG2 . VAL   B 29  ? 0.6461 0.5750 0.0828 0.3318  0.0774  0.1001  38  VAL   B CG2 
492  N N   . GLY   B 30  ? 0.6262 0.5383 0.0764 0.2991  0.0574  0.0374  39  GLY   B N   
493  C CA  . GLY   B 30  ? 0.6304 0.5458 0.0828 0.2886  0.0504  0.0225  39  GLY   B CA  
494  C C   . GLY   B 30  ? 0.6303 0.5552 0.0812 0.3008  0.0401  0.0138  39  GLY   B C   
495  O O   . GLY   B 30  ? 0.6227 0.5519 0.0694 0.3200  0.0382  0.0177  39  GLY   B O   
496  N N   . VAL   B 31  ? 0.6301 0.5587 0.0846 0.2890  0.0323  0.0027  40  VAL   B N   
497  C CA  . VAL   B 31  ? 0.6363 0.5740 0.0927 0.2959  0.0195  -0.0064 40  VAL   B CA  
498  C C   . VAL   B 31  ? 0.6370 0.5862 0.1115 0.2825  0.0200  -0.0159 40  VAL   B C   
499  O O   . VAL   B 31  ? 0.6455 0.5938 0.1241 0.2630  0.0233  -0.0181 40  VAL   B O   
500  C CB  . VAL   B 31  ? 0.6493 0.5807 0.0928 0.2950  0.0057  -0.0094 40  VAL   B CB  
501  C CG1 . VAL   B 31  ? 0.6476 0.5848 0.0948 0.2980  -0.0105 -0.0201 40  VAL   B CG1 
502  C CG2 . VAL   B 31  ? 0.6653 0.5919 0.0905 0.3127  0.0057  -0.0010 40  VAL   B CG2 
503  N N   . MET   B 32  ? 0.6256 0.5887 0.1107 0.2934  0.0165  -0.0209 41  MET   B N   
504  C CA  . MET   B 32  ? 0.6172 0.5996 0.1227 0.2828  0.0166  -0.0294 41  MET   B CA  
505  C C   . MET   B 32  ? 0.6198 0.6097 0.1288 0.2782  -0.0014 -0.0354 41  MET   B C   
506  O O   . MET   B 32  ? 0.6349 0.6203 0.1334 0.2939  -0.0136 -0.0363 41  MET   B O   
507  C CB  . MET   B 32  ? 0.6142 0.6097 0.1318 0.2992  0.0220  -0.0316 41  MET   B CB  
508  C CG  . MET   B 32  ? 0.6246 0.6459 0.1653 0.2907  0.0261  -0.0398 41  MET   B CG  
509  S SD  . MET   B 32  ? 0.7013 0.7196 0.2443 0.2771  0.0451  -0.0414 41  MET   B SD  
510  C CE  . MET   B 32  ? 0.6711 0.6629 0.2014 0.2970  0.0531  -0.0354 41  MET   B CE  
511  N N   . GLN   B 33  ? 0.6102 0.6093 0.1314 0.2563  -0.0038 -0.0387 42  GLN   B N   
512  C CA  . GLN   B 33  ? 0.6115 0.6156 0.1397 0.2468  -0.0222 -0.0435 42  GLN   B CA  
513  C C   . GLN   B 33  ? 0.6004 0.6259 0.1507 0.2223  -0.0175 -0.0439 42  GLN   B C   
514  O O   . GLN   B 33  ? 0.6072 0.6277 0.1532 0.2079  -0.0055 -0.0394 42  GLN   B O   
515  C CB  . GLN   B 33  ? 0.6512 0.6268 0.1574 0.2438  -0.0348 -0.0420 42  GLN   B CB  
516  C CG  . GLN   B 33  ? 0.7005 0.6745 0.2136 0.2320  -0.0567 -0.0478 42  GLN   B CG  
517  C CD  . GLN   B 33  ? 0.7671 0.7108 0.2559 0.2394  -0.0745 -0.0505 42  GLN   B CD  
518  O OE1 . GLN   B 33  ? 0.7775 0.7050 0.2644 0.2224  -0.0878 -0.0512 42  GLN   B OE1 
519  N NE2 . GLN   B 33  ? 0.7992 0.7345 0.2680 0.2659  -0.0755 -0.0517 42  GLN   B NE2 
520  N N   . GLU   B 34  ? 0.5791 0.6317 0.1534 0.2180  -0.0265 -0.0486 43  GLU   B N   
521  C CA  . GLU   B 34  ? 0.5696 0.6520 0.1693 0.1951  -0.0210 -0.0471 43  GLU   B CA  
522  C C   . GLU   B 34  ? 0.5588 0.6579 0.1631 0.1945  0.0036  -0.0455 43  GLU   B C   
523  O O   . GLU   B 34  ? 0.5560 0.6677 0.1667 0.1740  0.0127  -0.0412 43  GLU   B O   
524  C CB  . GLU   B 34  ? 0.6147 0.6830 0.2118 0.1681  -0.0314 -0.0418 43  GLU   B CB  
525  C CG  . GLU   B 34  ? 0.6939 0.7455 0.2891 0.1663  -0.0583 -0.0456 43  GLU   B CG  
526  C CD  . GLU   B 34  ? 0.8110 0.8260 0.3867 0.1506  -0.0693 -0.0409 43  GLU   B CD  
527  O OE1 . GLU   B 34  ? 0.8182 0.8378 0.4022 0.1246  -0.0652 -0.0325 43  GLU   B OE1 
528  O OE2 . GLU   B 34  ? 0.8609 0.8433 0.4118 0.1659  -0.0817 -0.0449 43  GLU   B OE2 
529  N N   . GLY   B 35  ? 0.5490 0.6460 0.1479 0.2176  0.0132  -0.0487 44  GLY   B N   
530  C CA  . GLY   B 35  ? 0.5399 0.6469 0.1405 0.2219  0.0334  -0.0502 44  GLY   B CA  
531  C C   . GLY   B 35  ? 0.5540 0.6336 0.1318 0.2136  0.0439  -0.0463 44  GLY   B C   
532  O O   . GLY   B 35  ? 0.5570 0.6462 0.1353 0.2093  0.0587  -0.0483 44  GLY   B O   
533  N N   . VAL   B 36  ? 0.5562 0.6034 0.1133 0.2120  0.0354  -0.0413 45  VAL   B N   
534  C CA  . VAL   B 36  ? 0.5529 0.5753 0.0895 0.2041  0.0427  -0.0370 45  VAL   B CA  
535  C C   . VAL   B 36  ? 0.5553 0.5506 0.0750 0.2209  0.0411  -0.0336 45  VAL   B C   
536  O O   . VAL   B 36  ? 0.5529 0.5405 0.0677 0.2315  0.0293  -0.0319 45  VAL   B O   
537  C CB  . VAL   B 36  ? 0.5552 0.5701 0.0848 0.1810  0.0362  -0.0316 45  VAL   B CB  
538  C CG1 . VAL   B 36  ? 0.5745 0.5646 0.0825 0.1756  0.0411  -0.0270 45  VAL   B CG1 
539  C CG2 . VAL   B 36  ? 0.5412 0.5850 0.0869 0.1625  0.0417  -0.0312 45  VAL   B CG2 
540  N N   . PHE   B 37  ? 0.5511 0.5338 0.0624 0.2238  0.0527  -0.0327 46  PHE   B N   
541  C CA  . PHE   B 37  ? 0.5625 0.5229 0.0610 0.2355  0.0526  -0.0264 46  PHE   B CA  
542  C C   . PHE   B 37  ? 0.5839 0.5292 0.0681 0.2228  0.0493  -0.0206 46  PHE   B C   
543  O O   . PHE   B 37  ? 0.5992 0.5427 0.0798 0.2074  0.0545  -0.0216 46  PHE   B O   
544  C CB  . PHE   B 37  ? 0.5602 0.5112 0.0582 0.2421  0.0640  -0.0274 46  PHE   B CB  
545  C CG  . PHE   B 37  ? 0.5729 0.5055 0.0630 0.2552  0.0633  -0.0182 46  PHE   B CG  
546  C CD1 . PHE   B 37  ? 0.5830 0.5194 0.0740 0.2733  0.0575  -0.0142 46  PHE   B CD1 
547  C CD2 . PHE   B 37  ? 0.5892 0.5031 0.0714 0.2490  0.0683  -0.0124 46  PHE   B CD2 
548  C CE1 . PHE   B 37  ? 0.5982 0.5211 0.0812 0.2854  0.0586  -0.0029 46  PHE   B CE1 
549  C CE2 . PHE   B 37  ? 0.6038 0.5049 0.0818 0.2590  0.0687  -0.0008 46  PHE   B CE2 
550  C CZ  . PHE   B 37  ? 0.6026 0.5087 0.0805 0.2774  0.0649  0.0047  46  PHE   B CZ  
551  N N   . HIS   B 38  ? 0.5838 0.5197 0.0587 0.2308  0.0407  -0.0149 47  HIS   B N   
552  C CA  . HIS   B 38  ? 0.5923 0.5158 0.0541 0.2228  0.0362  -0.0096 47  HIS   B CA  
553  C C   . HIS   B 38  ? 0.5959 0.5106 0.0506 0.2331  0.0404  -0.0010 47  HIS   B C   
554  O O   . HIS   B 38  ? 0.5886 0.5046 0.0460 0.2504  0.0374  0.0029  47  HIS   B O   
555  C CB  . HIS   B 38  ? 0.6002 0.5214 0.0561 0.2260  0.0209  -0.0108 47  HIS   B CB  
556  C CG  . HIS   B 38  ? 0.6042 0.5348 0.0704 0.2136  0.0142  -0.0170 47  HIS   B CG  
557  N ND1 . HIS   B 38  ? 0.6105 0.5564 0.0904 0.2209  0.0108  -0.0226 47  HIS   B ND1 
558  C CD2 . HIS   B 38  ? 0.6093 0.5373 0.0749 0.1939  0.0098  -0.0165 47  HIS   B CD2 
559  C CE1 . HIS   B 38  ? 0.6044 0.5591 0.0943 0.2041  0.0048  -0.0252 47  HIS   B CE1 
560  N NE2 . HIS   B 38  ? 0.6065 0.5494 0.0874 0.1873  0.0040  -0.0209 47  HIS   B NE2 
561  N N   . THR   B 39  ? 0.6016 0.5092 0.0530 0.2224  0.0462  0.0030  48  THR   B N   
562  C CA  . THR   B 39  ? 0.6104 0.5132 0.0590 0.2287  0.0498  0.0134  48  THR   B CA  
563  C C   . THR   B 39  ? 0.6378 0.5370 0.0800 0.2162  0.0478  0.0176  48  THR   B C   
564  O O   . THR   B 39  ? 0.6431 0.5404 0.0804 0.2040  0.0433  0.0126  48  THR   B O   
565  C CB  . THR   B 39  ? 0.6016 0.4993 0.0584 0.2313  0.0593  0.0153  48  THR   B CB  
566  O OG1 . THR   B 39  ? 0.5896 0.4860 0.0510 0.2398  0.0612  0.0287  48  THR   B OG1 
567  C CG2 . THR   B 39  ? 0.6107 0.5001 0.0691 0.2146  0.0643  0.0100  48  THR   B CG2 
568  N N   . MET   B 40  ? 0.6493 0.5497 0.0923 0.2195  0.0505  0.0283  49  MET   B N   
569  C CA  . MET   B 40  ? 0.6648 0.5662 0.1050 0.2093  0.0483  0.0331  49  MET   B CA  
570  C C   . MET   B 40  ? 0.6803 0.5741 0.1260 0.1925  0.0534  0.0305  49  MET   B C   
571  O O   . MET   B 40  ? 0.6853 0.5736 0.1389 0.1935  0.0595  0.0317  49  MET   B O   
572  C CB  . MET   B 40  ? 0.6744 0.5872 0.1164 0.2212  0.0492  0.0465  49  MET   B CB  
573  C CG  . MET   B 40  ? 0.7014 0.6210 0.1343 0.2424  0.0443  0.0475  49  MET   B CG  
574  S SD  . MET   B 40  ? 0.7258 0.6589 0.1510 0.2532  0.0387  0.0554  49  MET   B SD  
575  C CE  . MET   B 40  ? 0.6290 0.5478 0.0459 0.2396  0.0277  0.0448  49  MET   B CE  
576  N N   . TRP   B 41  ? 0.6889 0.5802 0.1286 0.1781  0.0497  0.0265  50  TRP   B N   
577  C CA  A TRP   B 41  ? 0.7038 0.5872 0.1444 0.1632  0.0525  0.0213  50  TRP   B CA  
578  C CA  B TRP   B 41  ? 0.7002 0.5835 0.1408 0.1631  0.0525  0.0212  50  TRP   B CA  
579  C C   . TRP   B 41  ? 0.7066 0.5871 0.1585 0.1603  0.0548  0.0292  50  TRP   B C   
580  O O   . TRP   B 41  ? 0.7226 0.5901 0.1776 0.1547  0.0580  0.0235  50  TRP   B O   
581  C CB  A TRP   B 41  ? 0.7088 0.5921 0.1381 0.1499  0.0467  0.0180  50  TRP   B CB  
582  C CB  B TRP   B 41  ? 0.7004 0.5837 0.1296 0.1497  0.0466  0.0178  50  TRP   B CB  
583  C CG  A TRP   B 41  ? 0.7230 0.5981 0.1479 0.1363  0.0486  0.0091  50  TRP   B CG  
584  C CG  B TRP   B 41  ? 0.7070 0.5823 0.1326 0.1356  0.0479  0.0102  50  TRP   B CG  
585  C CD1 A TRP   B 41  ? 0.7407 0.6125 0.1579 0.1320  0.0530  -0.0024 50  TRP   B CD1 
586  C CD1 B TRP   B 41  ? 0.7148 0.5863 0.1463 0.1279  0.0457  0.0129  50  TRP   B CD1 
587  C CD2 A TRP   B 41  ? 0.7255 0.5966 0.1526 0.1259  0.0452  0.0104  50  TRP   B CD2 
588  C CD2 B TRP   B 41  ? 0.7130 0.5846 0.1267 0.1275  0.0504  -0.0014 50  TRP   B CD2 
589  N NE1 A TRP   B 41  ? 0.7496 0.6133 0.1603 0.1218  0.0528  -0.0099 50  TRP   B NE1 
590  N NE1 B TRP   B 41  ? 0.7243 0.5857 0.1465 0.1170  0.0454  0.0013  50  TRP   B NE1 
591  C CE2 A TRP   B 41  ? 0.7448 0.6061 0.1617 0.1169  0.0467  -0.0027 50  TRP   B CE2 
592  C CE2 B TRP   B 41  ? 0.7252 0.5881 0.1352 0.1178  0.0493  -0.0076 50  TRP   B CE2 
593  C CE3 A TRP   B 41  ? 0.7273 0.6047 0.1650 0.1234  0.0406  0.0213  50  TRP   B CE3 
594  C CE3 B TRP   B 41  ? 0.7207 0.5975 0.1275 0.1275  0.0535  -0.0068 50  TRP   B CE3 
595  C CZ2 A TRP   B 41  ? 0.7597 0.6125 0.1744 0.1054  0.0416  -0.0070 50  TRP   B CZ2 
596  C CZ2 B TRP   B 41  ? 0.7377 0.5968 0.1333 0.1110  0.0519  -0.0203 50  TRP   B CZ2 
597  C CZ3 A TRP   B 41  ? 0.7423 0.6142 0.1821 0.1097  0.0358  0.0188  50  TRP   B CZ3 
598  C CZ3 B TRP   B 41  ? 0.7320 0.6092 0.1276 0.1192  0.0578  -0.0167 50  TRP   B CZ3 
599  C CH2 A TRP   B 41  ? 0.7563 0.6138 0.1834 0.1008  0.0353  0.0040  50  TRP   B CH2 
600  C CH2 B TRP   B 41  ? 0.7371 0.6055 0.1253 0.1126  0.0573  -0.0240 50  TRP   B CH2 
601  N N   . HIS   B 42  ? 0.6916 0.5843 0.1499 0.1642  0.0528  0.0426  51  HIS   B N   
602  C CA  . HIS   B 42  ? 0.6873 0.5814 0.1602 0.1581  0.0546  0.0535  51  HIS   B CA  
603  C C   . HIS   B 42  ? 0.6983 0.5818 0.1796 0.1643  0.0613  0.0581  51  HIS   B C   
604  O O   . HIS   B 42  ? 0.7045 0.5844 0.1986 0.1568  0.0623  0.0683  51  HIS   B O   
605  C CB  . HIS   B 42  ? 0.6781 0.5955 0.1584 0.1626  0.0527  0.0687  51  HIS   B CB  
606  C CG  . HIS   B 42  ? 0.6983 0.6298 0.1786 0.1833  0.0572  0.0786  51  HIS   B CG  
607  N ND1 . HIS   B 42  ? 0.7166 0.6610 0.1865 0.1975  0.0531  0.0784  51  HIS   B ND1 
608  C CD2 . HIS   B 42  ? 0.7055 0.6390 0.1929 0.1926  0.0644  0.0892  51  HIS   B CD2 
609  C CE1 . HIS   B 42  ? 0.7162 0.6714 0.1862 0.2157  0.0581  0.0871  51  HIS   B CE1 
610  N NE2 . HIS   B 42  ? 0.7160 0.6665 0.1962 0.2132  0.0655  0.0947  51  HIS   B NE2 
611  N N   . VAL   B 43  ? 0.6976 0.5762 0.1727 0.1776  0.0647  0.0519  52  VAL   B N   
612  C CA  . VAL   B 43  ? 0.6945 0.5626 0.1755 0.1868  0.0701  0.0565  52  VAL   B CA  
613  C C   . VAL   B 43  ? 0.7002 0.5446 0.1803 0.1798  0.0708  0.0430  52  VAL   B C   
614  O O   . VAL   B 43  ? 0.6995 0.5265 0.1871 0.1751  0.0714  0.0480  52  VAL   B O   
615  C CB  . VAL   B 43  ? 0.7005 0.5782 0.1752 0.2068  0.0717  0.0561  52  VAL   B CB  
616  C CG1 . VAL   B 43  ? 0.7137 0.5804 0.1922 0.2182  0.0763  0.0599  52  VAL   B CG1 
617  C CG2 . VAL   B 43  ? 0.6948 0.5938 0.1666 0.2173  0.0702  0.0675  52  VAL   B CG2 
618  N N   . THR   B 44  ? 0.7029 0.5466 0.1734 0.1786  0.0701  0.0262  53  THR   B N   
619  C CA  . THR   B 44  ? 0.7133 0.5399 0.1800 0.1760  0.0717  0.0107  53  THR   B CA  
620  C C   . THR   B 44  ? 0.7266 0.5448 0.1864 0.1591  0.0677  0.0010  53  THR   B C   
621  O O   . THR   B 44  ? 0.7379 0.5392 0.1924 0.1579  0.0683  -0.0125 53  THR   B O   
622  C CB  . THR   B 44  ? 0.7236 0.5612 0.1853 0.1858  0.0749  -0.0011 53  THR   B CB  
623  O OG1 . THR   B 44  ? 0.7314 0.5822 0.1846 0.1762  0.0728  -0.0069 53  THR   B OG1 
624  C CG2 . THR   B 44  ? 0.7206 0.5697 0.1872 0.2026  0.0759  0.0063  53  THR   B CG2 
625  N N   . LYS   B 45  ? 0.7222 0.5526 0.1795 0.1484  0.0630  0.0060  54  LYS   B N   
626  C CA  . LYS   B 45  ? 0.7373 0.5627 0.1854 0.1331  0.0577  -0.0028 54  LYS   B CA  
627  C C   . LYS   B 45  ? 0.7507 0.5765 0.1829 0.1329  0.0607  -0.0200 54  LYS   B C   
628  O O   . LYS   B 45  ? 0.7585 0.5751 0.1795 0.1237  0.0576  -0.0311 54  LYS   B O   
629  C CB  . LYS   B 45  ? 0.7668 0.5711 0.2214 0.1231  0.0528  -0.0031 54  LYS   B CB  
630  C CG  . LYS   B 45  ? 0.8160 0.6283 0.2871 0.1160  0.0487  0.0157  54  LYS   B CG  
631  C CD  . LYS   B 45  ? 0.8875 0.7184 0.3553 0.1060  0.0423  0.0183  54  LYS   B CD  
632  C CE  . LYS   B 45  ? 0.9466 0.7986 0.4317 0.1056  0.0412  0.0386  54  LYS   B CE  
633  N NZ  . LYS   B 45  ? 0.9710 0.8312 0.4626 0.1222  0.0496  0.0504  54  LYS   B NZ  
634  N N   . GLY   B 46  ? 0.7505 0.5892 0.1820 0.1430  0.0662  -0.0215 55  GLY   B N   
635  C CA  . GLY   B 46  ? 0.7632 0.6103 0.1843 0.1436  0.0712  -0.0340 55  GLY   B CA  
636  C C   . GLY   B 46  ? 0.7836 0.6218 0.2049 0.1535  0.0775  -0.0472 55  GLY   B C   
637  O O   . GLY   B 46  ? 0.7928 0.6431 0.2071 0.1558  0.0834  -0.0576 55  GLY   B O   
638  N N   . ALA   B 47  ? 0.7914 0.6091 0.2207 0.1599  0.0763  -0.0461 56  ALA   B N   
639  C CA  . ALA   B 47  ? 0.8017 0.6043 0.2298 0.1717  0.0802  -0.0592 56  ALA   B CA  
640  C C   . ALA   B 47  ? 0.8011 0.6190 0.2380 0.1887  0.0869  -0.0603 56  ALA   B C   
641  O O   . ALA   B 47  ? 0.7939 0.6249 0.2407 0.1927  0.0865  -0.0480 56  ALA   B O   
642  C CB  . ALA   B 47  ? 0.8083 0.5792 0.2422 0.1715  0.0745  -0.0553 56  ALA   B CB  
643  N N   . ALA   B 48  ? 0.8038 0.6202 0.2367 0.2005  0.0922  -0.0760 57  ALA   B N   
644  C CA  . ALA   B 48  ? 0.8043 0.6377 0.2475 0.2183  0.0982  -0.0791 57  ALA   B CA  
645  C C   . ALA   B 48  ? 0.8278 0.6434 0.2819 0.2307  0.0949  -0.0691 57  ALA   B C   
646  O O   . ALA   B 48  ? 0.8434 0.6269 0.2953 0.2292  0.0901  -0.0660 57  ALA   B O   
647  C CB  . ALA   B 48  ? 0.8018 0.6367 0.2375 0.2302  0.1044  -0.0986 57  ALA   B CB  
648  N N   . LEU   B 49  ? 0.8267 0.6634 0.2925 0.2426  0.0967  -0.0635 58  LEU   B N   
649  C CA  . LEU   B 49  ? 0.8433 0.6685 0.3175 0.2573  0.0939  -0.0528 58  LEU   B CA  
650  C C   . LEU   B 49  ? 0.8619 0.6926 0.3422 0.2796  0.0973  -0.0635 58  LEU   B C   
651  O O   . LEU   B 49  ? 0.8642 0.7130 0.3441 0.2832  0.1027  -0.0784 58  LEU   B O   
652  C CB  . LEU   B 49  ? 0.8313 0.6770 0.3119 0.2562  0.0909  -0.0383 58  LEU   B CB  
653  C CG  . LEU   B 49  ? 0.8416 0.6914 0.3169 0.2377  0.0878  -0.0300 58  LEU   B CG  
654  C CD1 . LEU   B 49  ? 0.8374 0.7104 0.3164 0.2397  0.0844  -0.0234 58  LEU   B CD1 
655  C CD2 . LEU   B 49  ? 0.8556 0.6816 0.3288 0.2311  0.0850  -0.0177 58  LEU   B CD2 
656  N N   . ARG   B 50  ? 0.8766 0.6942 0.3622 0.2957  0.0945  -0.0550 59  ARG   B N   
657  C CA  . ARG   B 50  ? 0.8913 0.7135 0.3833 0.3196  0.0959  -0.0632 59  ARG   B CA  
658  C C   . ARG   B 50  ? 0.8850 0.7246 0.3865 0.3322  0.0923  -0.0503 59  ARG   B C   
659  O O   . ARG   B 50  ? 0.8818 0.7151 0.3807 0.3260  0.0887  -0.0343 59  ARG   B O   
660  C CB  . ARG   B 50  ? 0.9440 0.7212 0.4282 0.3295  0.0937  -0.0674 59  ARG   B CB  
661  C CG  . ARG   B 50  ? 1.0181 0.7836 0.5069 0.3564  0.0913  -0.0659 59  ARG   B CG  
662  C CD  . ARG   B 50  ? 1.1028 0.8183 0.5819 0.3653  0.0876  -0.0726 59  ARG   B CD  
663  N NE  . ARG   B 50  ? 1.1749 0.8507 0.6477 0.3467  0.0821  -0.0580 59  ARG   B NE  
664  C CZ  . ARG   B 50  ? 1.2276 0.8705 0.7007 0.3514  0.0767  -0.0398 59  ARG   B CZ  
665  N NH1 . ARG   B 50  ? 1.2190 0.8606 0.6953 0.3758  0.0754  -0.0346 59  ARG   B NH1 
666  N NH2 . ARG   B 50  ? 1.2477 0.8608 0.7188 0.3313  0.0724  -0.0254 59  ARG   B NH2 
667  N N   . SER   B 51  ? 0.8799 0.7461 0.3921 0.3499  0.0929  -0.0580 60  SER   B N   
668  C CA  . SER   B 51  ? 0.8826 0.7676 0.4030 0.3631  0.0874  -0.0487 60  SER   B CA  
669  C C   . SER   B 51  ? 0.9050 0.7965 0.4340 0.3895  0.0873  -0.0573 60  SER   B C   
670  O O   . SER   B 51  ? 0.8999 0.8278 0.4422 0.3948  0.0900  -0.0699 60  SER   B O   
671  C CB  . SER   B 51  ? 0.8656 0.7905 0.3949 0.3512  0.0857  -0.0506 60  SER   B CB  
672  O OG  . SER   B 51  ? 0.8746 0.8141 0.4085 0.3620  0.0776  -0.0423 60  SER   B OG  
673  N N   . GLY   B 52  ? 0.9273 0.7842 0.4495 0.4057  0.0843  -0.0500 61  GLY   B N   
674  C CA  . GLY   B 52  ? 0.9410 0.7958 0.4685 0.4334  0.0832  -0.0583 61  GLY   B CA  
675  C C   . GLY   B 52  ? 0.9616 0.8013 0.4845 0.4334  0.0892  -0.0761 61  GLY   B C   
676  O O   . GLY   B 52  ? 0.9840 0.7858 0.4937 0.4192  0.0897  -0.0748 61  GLY   B O   
677  N N   . GLU   B 53  ? 0.9511 0.8241 0.4851 0.4479  0.0937  -0.0934 62  GLU   B N   
678  C CA  . GLU   B 53  ? 0.9641 0.8303 0.4911 0.4489  0.1008  -0.1128 62  GLU   B CA  
679  C C   . GLU   B 53  ? 0.9509 0.8519 0.4798 0.4236  0.1087  -0.1189 62  GLU   B C   
680  O O   . GLU   B 53  ? 0.9592 0.8510 0.4763 0.4186  0.1144  -0.1325 62  GLU   B O   
681  C CB  . GLU   B 53  ? 0.9888 0.8700 0.5235 0.4813  0.1030  -0.1290 62  GLU   B CB  
682  C CG  . GLU   B 53  ? 1.1003 0.9218 0.6200 0.5024  0.0967  -0.1314 62  GLU   B CG  
683  C CD  . GLU   B 53  ? 1.2280 1.0587 0.7528 0.5389  0.0975  -0.1483 62  GLU   B CD  
684  O OE1 . GLU   B 53  ? 1.2414 1.1071 0.7838 0.5578  0.0953  -0.1443 62  GLU   B OE1 
685  O OE2 . GLU   B 53  ? 1.2812 1.0843 0.7919 0.5503  0.0993  -0.1662 62  GLU   B OE2 
686  N N   . GLY   B 54  ? 0.9247 0.8611 0.4656 0.4082  0.1076  -0.1086 63  GLY   B N   
687  C CA  . GLY   B 54  ? 0.9070 0.8751 0.4505 0.3837  0.1133  -0.1106 63  GLY   B CA  
688  C C   . GLY   B 54  ? 0.9098 0.8466 0.4347 0.3594  0.1133  -0.1062 63  GLY   B C   
689  O O   . GLY   B 54  ? 0.9330 0.8280 0.4470 0.3563  0.1074  -0.0967 63  GLY   B O   
690  N N   . ARG   B 55  ? 0.8803 0.8401 0.4026 0.3415  0.1197  -0.1117 64  ARG   B N   
691  C CA  . ARG   B 55  ? 0.8717 0.8072 0.3767 0.3187  0.1190  -0.1084 64  ARG   B CA  
692  C C   . ARG   B 55  ? 0.8267 0.7886 0.3356 0.2955  0.1185  -0.0990 64  ARG   B C   
693  O O   . ARG   B 55  ? 0.8042 0.8069 0.3240 0.2913  0.1238  -0.1021 64  ARG   B O   
694  C CB  . ARG   B 55  ? 0.8959 0.8205 0.3846 0.3199  0.1255  -0.1250 64  ARG   B CB  
695  C CG  . ARG   B 55  ? 0.9577 0.8463 0.4275 0.3006  0.1211  -0.1224 64  ARG   B CG  
696  C CD  . ARG   B 55  ? 1.0180 0.9150 0.4715 0.2947  0.1279  -0.1374 64  ARG   B CD  
697  N NE  . ARG   B 55  ? 1.0750 0.9384 0.5102 0.2768  0.1217  -0.1365 64  ARG   B NE  
698  C CZ  . ARG   B 55  ? 1.1202 0.9561 0.5358 0.2799  0.1202  -0.1522 64  ARG   B CZ  
699  N NH1 . ARG   B 55  ? 1.1189 0.9555 0.5283 0.3024  0.1253  -0.1709 64  ARG   B NH1 
700  N NH2 . ARG   B 55  ? 1.1338 0.9419 0.5357 0.2618  0.1125  -0.1502 64  ARG   B NH2 
701  N N   . LEU   B 56  ? 0.8118 0.7504 0.3127 0.2807  0.1118  -0.0868 65  LEU   B N   
702  C CA  . LEU   B 56  ? 0.7859 0.7398 0.2868 0.2600  0.1090  -0.0778 65  LEU   B CA  
703  C C   . LEU   B 56  ? 0.7736 0.7151 0.2573 0.2424  0.1114  -0.0806 65  LEU   B C   
704  O O   . LEU   B 56  ? 0.7811 0.6901 0.2535 0.2385  0.1077  -0.0781 65  LEU   B O   
705  C CB  . LEU   B 56  ? 0.7898 0.7285 0.2912 0.2585  0.0996  -0.0631 65  LEU   B CB  
706  C CG  . LEU   B 56  ? 0.7999 0.7432 0.3126 0.2773  0.0949  -0.0584 65  LEU   B CG  
707  C CD1 . LEU   B 56  ? 0.8048 0.7388 0.3136 0.2742  0.0865  -0.0444 65  LEU   B CD1 
708  C CD2 . LEU   B 56  ? 0.7940 0.7767 0.3242 0.2831  0.0953  -0.0644 65  LEU   B CD2 
709  N N   . ASP   B 57  ? 0.7540 0.7227 0.2361 0.2314  0.1172  -0.0846 66  ASP   B N   
710  C CA  . ASP   B 57  ? 0.7608 0.7218 0.2242 0.2152  0.1193  -0.0869 66  ASP   B CA  
711  C C   . ASP   B 57  ? 0.7421 0.7090 0.2041 0.1955  0.1133  -0.0735 66  ASP   B C   
712  O O   . ASP   B 57  ? 0.7335 0.7233 0.2090 0.1921  0.1114  -0.0671 66  ASP   B O   
713  C CB  . ASP   B 57  ? 0.7992 0.7871 0.2580 0.2178  0.1307  -0.0992 66  ASP   B CB  
714  C CG  . ASP   B 57  ? 0.9099 0.8837 0.3624 0.2384  0.1353  -0.1156 66  ASP   B CG  
715  O OD1 . ASP   B 57  ? 0.9559 0.8915 0.3925 0.2383  0.1303  -0.1207 66  ASP   B OD1 
716  O OD2 . ASP   B 57  ? 0.9265 0.9275 0.3906 0.2549  0.1430  -0.1238 66  ASP   B OD2 
717  N N   . PRO   B 58  ? 0.7351 0.6800 0.1816 0.1829  0.1083  -0.0693 67  PRO   B N   
718  C CA  . PRO   B 58  ? 0.7273 0.6746 0.1710 0.1672  0.1013  -0.0568 67  PRO   B CA  
719  C C   . PRO   B 58  ? 0.7158 0.6900 0.1579 0.1540  0.1053  -0.0546 67  PRO   B C   
720  O O   . PRO   B 58  ? 0.7152 0.7071 0.1520 0.1536  0.1154  -0.0627 67  PRO   B O   
721  C CB  . PRO   B 58  ? 0.7486 0.6703 0.1763 0.1588  0.0962  -0.0550 67  PRO   B CB  
722  C CG  . PRO   B 58  ? 0.7625 0.6745 0.1805 0.1642  0.1019  -0.0690 67  PRO   B CG  
723  C CD  . PRO   B 58  ? 0.7397 0.6561 0.1712 0.1827  0.1071  -0.0760 67  PRO   B CD  
724  N N   . TYR   B 59  ? 0.6960 0.6733 0.1419 0.1435  0.0973  -0.0432 68  TYR   B N   
725  C CA  . TYR   B 59  ? 0.6738 0.6729 0.1194 0.1278  0.0992  -0.0373 68  TYR   B CA  
726  C C   . TYR   B 59  ? 0.6737 0.6556 0.1020 0.1125  0.0908  -0.0273 68  TYR   B C   
727  O O   . TYR   B 59  ? 0.6708 0.6610 0.0857 0.0999  0.0952  -0.0245 68  TYR   B O   
728  C CB  . TYR   B 59  ? 0.6483 0.6675 0.1164 0.1281  0.0954  -0.0331 68  TYR   B CB  
729  C CG  . TYR   B 59  ? 0.6306 0.6719 0.1032 0.1089  0.0956  -0.0241 68  TYR   B CG  
730  C CD1 . TYR   B 59  ? 0.6468 0.6711 0.1103 0.0935  0.0840  -0.0125 68  TYR   B CD1 
731  C CD2 . TYR   B 59  ? 0.6121 0.6919 0.1011 0.1068  0.1060  -0.0258 68  TYR   B CD2 
732  C CE1 . TYR   B 59  ? 0.6468 0.6872 0.1155 0.0741  0.0824  -0.0018 68  TYR   B CE1 
733  C CE2 . TYR   B 59  ? 0.6155 0.7181 0.1128 0.0866  0.1059  -0.0144 68  TYR   B CE2 
734  C CZ  . TYR   B 59  ? 0.6408 0.7211 0.1277 0.0692  0.0935  -0.0018 68  TYR   B CZ  
735  O OH  . TYR   B 59  ? 0.6483 0.7471 0.1439 0.0473  0.0920  0.0116  68  TYR   B OH  
736  N N   . TRP   B 60  ? 0.6674 0.6272 0.0952 0.1155  0.0788  -0.0215 69  TRP   B N   
737  C CA  . TRP   B 60  ? 0.6712 0.6132 0.0837 0.1057  0.0690  -0.0125 69  TRP   B CA  
738  C C   . TRP   B 60  ? 0.6791 0.6007 0.0883 0.1158  0.0632  -0.0125 69  TRP   B C   
739  O O   . TRP   B 60  ? 0.6779 0.5972 0.0984 0.1293  0.0638  -0.0153 69  TRP   B O   
740  C CB  . TRP   B 60  ? 0.6639 0.6041 0.0814 0.0988  0.0579  -0.0033 69  TRP   B CB  
741  C CG  . TRP   B 60  ? 0.6786 0.5961 0.0815 0.0953  0.0453  0.0049  69  TRP   B CG  
742  C CD1 . TRP   B 60  ? 0.6990 0.6094 0.0844 0.0823  0.0424  0.0119  69  TRP   B CD1 
743  C CD2 . TRP   B 60  ? 0.6808 0.5817 0.0838 0.1081  0.0348  0.0064  69  TRP   B CD2 
744  N NE1 . TRP   B 60  ? 0.7119 0.6015 0.0882 0.0866  0.0295  0.0173  69  TRP   B NE1 
745  C CE2 . TRP   B 60  ? 0.7012 0.5862 0.0882 0.1028  0.0254  0.0137  69  TRP   B CE2 
746  C CE3 . TRP   B 60  ? 0.6809 0.5806 0.0947 0.1250  0.0326  0.0029  69  TRP   B CE3 
747  C CZ2 . TRP   B 60  ? 0.7123 0.5828 0.0954 0.1149  0.0146  0.0166  69  TRP   B CZ2 
748  C CZ3 . TRP   B 60  ? 0.6939 0.5797 0.1019 0.1361  0.0227  0.0066  69  TRP   B CZ3 
749  C CH2 . TRP   B 60  ? 0.7048 0.5773 0.0984 0.1315  0.0140  0.0129  69  TRP   B CH2 
750  N N   . GLY   B 61  ? 0.6825 0.5917 0.0772 0.1092  0.0573  -0.0075 70  GLY   B N   
751  C CA  . GLY   B 61  ? 0.6868 0.5828 0.0812 0.1166  0.0517  -0.0049 70  GLY   B CA  
752  C C   . GLY   B 61  ? 0.6953 0.5829 0.0753 0.1087  0.0428  0.0022  70  GLY   B C   
753  O O   . GLY   B 61  ? 0.7047 0.5939 0.0709 0.0967  0.0429  0.0033  70  GLY   B O   
754  N N   . ASP   B 62  ? 0.6873 0.5686 0.0700 0.1166  0.0355  0.0078  71  ASP   B N   
755  C CA  . ASP   B 62  ? 0.6920 0.5679 0.0631 0.1124  0.0260  0.0147  71  ASP   B CA  
756  C C   . ASP   B 62  ? 0.6841 0.5621 0.0645 0.1220  0.0230  0.0188  71  ASP   B C   
757  O O   . ASP   B 62  ? 0.6915 0.5718 0.0814 0.1354  0.0224  0.0219  71  ASP   B O   
758  C CB  . ASP   B 62  ? 0.7211 0.5893 0.0842 0.1125  0.0161  0.0211  71  ASP   B CB  
759  C CG  . ASP   B 62  ? 0.8024 0.6628 0.1511 0.1094  0.0052  0.0284  71  ASP   B CG  
760  O OD1 . ASP   B 62  ? 0.8099 0.6725 0.1618 0.1185  0.0004  0.0314  71  ASP   B OD1 
761  O OD2 . ASP   B 62  ? 0.8593 0.7128 0.1940 0.0983  0.0013  0.0324  71  ASP   B OD2 
762  N N   . VAL   B 63  ? 0.6679 0.5476 0.0456 0.1149  0.0210  0.0193  72  VAL   B N   
763  C CA  . VAL   B 63  ? 0.6558 0.5427 0.0459 0.1200  0.0187  0.0248  72  VAL   B CA  
764  C C   . VAL   B 63  ? 0.6711 0.5635 0.0608 0.1314  0.0102  0.0342  72  VAL   B C   
765  O O   . VAL   B 63  ? 0.6723 0.5736 0.0744 0.1442  0.0121  0.0395  72  VAL   B O   
766  C CB  . VAL   B 63  ? 0.6516 0.5391 0.0428 0.1071  0.0166  0.0214  72  VAL   B CB  
767  C CG1 . VAL   B 63  ? 0.6458 0.5457 0.0461 0.1082  0.0096  0.0305  72  VAL   B CG1 
768  C CG2 . VAL   B 63  ? 0.6554 0.5361 0.0503 0.1030  0.0249  0.0123  72  VAL   B CG2 
769  N N   . LYS   B 64  ? 0.6804 0.5670 0.0546 0.1291  0.0009  0.0365  73  LYS   B N   
770  C CA  . LYS   B 64  ? 0.6847 0.5729 0.0559 0.1432  -0.0089 0.0436  73  LYS   B CA  
771  C C   . LYS   B 64  ? 0.6937 0.5786 0.0683 0.1599  -0.0079 0.0431  73  LYS   B C   
772  O O   . LYS   B 64  ? 0.6910 0.5873 0.0725 0.1765  -0.0090 0.0477  73  LYS   B O   
773  C CB  . LYS   B 64  ? 0.7089 0.5839 0.0599 0.1376  -0.0199 0.0459  73  LYS   B CB  
774  C CG  . LYS   B 64  ? 0.7449 0.6172 0.0904 0.1546  -0.0318 0.0517  73  LYS   B CG  
775  C CD  . LYS   B 64  ? 0.7772 0.6513 0.1128 0.1523  -0.0424 0.0572  73  LYS   B CD  
776  C CE  . LYS   B 64  ? 0.8246 0.6862 0.1483 0.1694  -0.0561 0.0613  73  LYS   B CE  
777  N NZ  . LYS   B 64  ? 0.8779 0.7255 0.1820 0.1619  -0.0678 0.0663  73  LYS   B NZ  
778  N N   . GLN   B 65  ? 0.7023 0.5752 0.0729 0.1559  -0.0055 0.0375  74  GLN   B N   
779  C CA  . GLN   B 65  ? 0.7092 0.5789 0.0828 0.1706  -0.0061 0.0352  74  GLN   B CA  
780  C C   . GLN   B 65  ? 0.7049 0.5886 0.0941 0.1792  0.0048  0.0350  74  GLN   B C   
781  O O   . GLN   B 65  ? 0.7145 0.6002 0.1052 0.1960  0.0040  0.0349  74  GLN   B O   
782  C CB  . GLN   B 65  ? 0.7339 0.5911 0.1033 0.1611  -0.0071 0.0298  74  GLN   B CB  
783  C CG  . GLN   B 65  ? 0.7865 0.6276 0.1407 0.1496  -0.0171 0.0325  74  GLN   B CG  
784  C CD  . GLN   B 65  ? 0.8394 0.6737 0.1949 0.1391  -0.0173 0.0295  74  GLN   B CD  
785  O OE1 . GLN   B 65  ? 0.8484 0.6813 0.2109 0.1478  -0.0196 0.0251  74  GLN   B OE1 
786  N NE2 . GLN   B 65  ? 0.8334 0.6660 0.1821 0.1199  -0.0150 0.0324  74  GLN   B NE2 
787  N N   . ASP   B 66  ? 0.6882 0.5785 0.0868 0.1680  0.0141  0.0346  75  ASP   B N   
788  C CA  . ASP   B 66  ? 0.6726 0.5709 0.0855 0.1727  0.0240  0.0358  75  ASP   B CA  
789  C C   . ASP   B 66  ? 0.6675 0.5608 0.0817 0.1789  0.0275  0.0297  75  ASP   B C   
790  O O   . ASP   B 66  ? 0.6669 0.5657 0.0870 0.1930  0.0306  0.0326  75  ASP   B O   
791  C CB  . ASP   B 66  ? 0.6624 0.5762 0.0838 0.1868  0.0248  0.0463  75  ASP   B CB  
792  C CG  . ASP   B 66  ? 0.6844 0.6051 0.1211 0.1873  0.0349  0.0514  75  ASP   B CG  
793  O OD1 . ASP   B 66  ? 0.6854 0.5971 0.1265 0.1742  0.0393  0.0466  75  ASP   B OD1 
794  O OD2 . ASP   B 66  ? 0.7220 0.6559 0.1645 0.2020  0.0381  0.0605  75  ASP   B OD2 
795  N N   . LEU   B 67  ? 0.6610 0.5470 0.0702 0.1684  0.0271  0.0221  76  LEU   B N   
796  C CA  . LEU   B 67  ? 0.6514 0.5375 0.0652 0.1727  0.0297  0.0160  76  LEU   B CA  
797  C C   . LEU   B 67  ? 0.6511 0.5388 0.0677 0.1595  0.0376  0.0088  76  LEU   B C   
798  O O   . LEU   B 67  ? 0.6612 0.5468 0.0703 0.1459  0.0384  0.0078  76  LEU   B O   
799  C CB  . LEU   B 67  ? 0.6532 0.5331 0.0597 0.1759  0.0186  0.0147  76  LEU   B CB  
800  C CG  . LEU   B 67  ? 0.6720 0.5486 0.0717 0.1934  0.0091  0.0186  76  LEU   B CG  
801  C CD1 . LEU   B 67  ? 0.6818 0.5443 0.0715 0.1933  -0.0051 0.0156  76  LEU   B CD1 
802  C CD2 . LEU   B 67  ? 0.6804 0.5657 0.0866 0.2123  0.0133  0.0191  76  LEU   B CD2 
803  N N   . VAL   B 68  ? 0.6378 0.5306 0.0640 0.1655  0.0435  0.0035  77  VAL   B N   
804  C CA  . VAL   B 68  ? 0.6267 0.5250 0.0566 0.1581  0.0523  -0.0047 77  VAL   B CA  
805  C C   . VAL   B 68  ? 0.6225 0.5310 0.0638 0.1670  0.0537  -0.0091 77  VAL   B C   
806  O O   . VAL   B 68  ? 0.6233 0.5312 0.0702 0.1819  0.0518  -0.0070 77  VAL   B O   
807  C CB  . VAL   B 68  ? 0.6295 0.5216 0.0611 0.1581  0.0597  -0.0074 77  VAL   B CB  
808  C CG1 . VAL   B 68  ? 0.6352 0.5234 0.0764 0.1728  0.0614  -0.0030 77  VAL   B CG1 
809  C CG2 . VAL   B 68  ? 0.6290 0.5254 0.0602 0.1536  0.0681  -0.0183 77  VAL   B CG2 
810  N N   . SER   B 69  ? 0.6136 0.5344 0.0584 0.1581  0.0566  -0.0141 78  SER   B N   
811  C CA  . SER   B 69  ? 0.6088 0.5449 0.0681 0.1653  0.0570  -0.0183 78  SER   B CA  
812  C C   . SER   B 69  ? 0.6107 0.5612 0.0778 0.1668  0.0692  -0.0267 78  SER   B C   
813  O O   . SER   B 69  ? 0.6249 0.5769 0.0840 0.1571  0.0762  -0.0297 78  SER   B O   
814  C CB  . SER   B 69  ? 0.6145 0.5575 0.0767 0.1549  0.0478  -0.0156 78  SER   B CB  
815  O OG  . SER   B 69  ? 0.6314 0.5838 0.0906 0.1367  0.0524  -0.0145 78  SER   B OG  
816  N N   . TYR   B 70  ? 0.5963 0.5571 0.0771 0.1813  0.0713  -0.0312 79  TYR   B N   
817  C CA  . TYR   B 70  ? 0.5944 0.5685 0.0825 0.1876  0.0824  -0.0403 79  TYR   B CA  
818  C C   . TYR   B 70  ? 0.5923 0.5980 0.0986 0.1883  0.0837  -0.0438 79  TYR   B C   
819  O O   . TYR   B 70  ? 0.5914 0.6035 0.1080 0.1921  0.0743  -0.0408 79  TYR   B O   
820  C CB  . TYR   B 70  ? 0.5919 0.5507 0.0814 0.2063  0.0847  -0.0427 79  TYR   B CB  
821  C CG  . TYR   B 70  ? 0.6060 0.5373 0.0820 0.2037  0.0853  -0.0398 79  TYR   B CG  
822  C CD1 . TYR   B 70  ? 0.6218 0.5396 0.0914 0.2001  0.0782  -0.0293 79  TYR   B CD1 
823  C CD2 . TYR   B 70  ? 0.6200 0.5395 0.0909 0.2061  0.0920  -0.0478 79  TYR   B CD2 
824  C CE1 . TYR   B 70  ? 0.6427 0.5408 0.1043 0.1958  0.0784  -0.0253 79  TYR   B CE1 
825  C CE2 . TYR   B 70  ? 0.6440 0.5383 0.1051 0.2009  0.0904  -0.0451 79  TYR   B CE2 
826  C CZ  . TYR   B 70  ? 0.6637 0.5495 0.1221 0.1947  0.0838  -0.0330 79  TYR   B CZ  
827  O OH  . TYR   B 70  ? 0.6989 0.5649 0.1518 0.1879  0.0818  -0.0293 79  TYR   B OH  
828  N N   . CYS   B 71  ? 0.5863 0.6140 0.0966 0.1851  0.0950  -0.0505 80  CYS   B N   
829  C CA  . CYS   B 71  ? 0.5738 0.6406 0.1050 0.1852  0.0992  -0.0535 80  CYS   B CA  
830  C C   . CYS   B 71  ? 0.5549 0.6406 0.0930 0.1626  0.0946  -0.0447 80  CYS   B C   
831  O O   . CYS   B 71  ? 0.5452 0.6677 0.0986 0.1558  0.1019  -0.0449 80  CYS   B O   
832  C CB  . CYS   B 71  ? 0.5945 0.6702 0.1436 0.2043  0.0941  -0.0565 80  CYS   B CB  
833  S SG  . CYS   B 71  ? 0.7218 0.7686 0.2618 0.2298  0.0973  -0.0628 80  CYS   B SG  
834  N N   . GLY   B 72  ? 0.5454 0.6063 0.0718 0.1513  0.0831  -0.0364 81  GLY   B N   
835  C CA  . GLY   B 72  ? 0.5331 0.6023 0.0632 0.1294  0.0762  -0.0271 81  GLY   B CA  
836  C C   . GLY   B 72  ? 0.5475 0.5817 0.0578 0.1211  0.0645  -0.0198 81  GLY   B C   
837  O O   . GLY   B 72  ? 0.5594 0.5676 0.0544 0.1316  0.0631  -0.0214 81  GLY   B O   
838  N N   . PRO   B 73  ? 0.5458 0.5794 0.0567 0.1017  0.0557  -0.0106 82  PRO   B N   
839  C CA  . PRO   B 73  ? 0.5712 0.5701 0.0623 0.0958  0.0430  -0.0040 82  PRO   B CA  
840  C C   . PRO   B 73  ? 0.6062 0.5835 0.0963 0.1113  0.0280  -0.0070 82  PRO   B C   
841  O O   . PRO   B 73  ? 0.6041 0.5931 0.1102 0.1213  0.0232  -0.0122 82  PRO   B O   
842  C CB  . PRO   B 73  ? 0.5673 0.5710 0.0621 0.0716  0.0363  0.0069  82  PRO   B CB  
843  C CG  . PRO   B 73  ? 0.5442 0.5852 0.0671 0.0662  0.0403  0.0059  82  PRO   B CG  
844  C CD  . PRO   B 73  ? 0.5174 0.5820 0.0480 0.0839  0.0565  -0.0047 82  PRO   B CD  
845  N N   . TRP   B 74  ? 0.6359 0.5835 0.1061 0.1144  0.0197  -0.0037 83  TRP   B N   
846  C CA  . TRP   B 74  ? 0.6581 0.5853 0.1220 0.1308  0.0058  -0.0059 83  TRP   B CA  
847  C C   . TRP   B 74  ? 0.6857 0.6121 0.1602 0.1270  -0.0108 -0.0073 83  TRP   B C   
848  O O   . TRP   B 74  ? 0.6890 0.6113 0.1652 0.1073  -0.0184 -0.0014 83  TRP   B O   
849  C CB  . TRP   B 74  ? 0.6663 0.5669 0.1084 0.1313  -0.0007 -0.0006 83  TRP   B CB  
850  C CG  . TRP   B 74  ? 0.6752 0.5604 0.1086 0.1528  -0.0103 -0.0031 83  TRP   B CG  
851  C CD1 . TRP   B 74  ? 0.6916 0.5595 0.1182 0.1596  -0.0283 -0.0049 83  TRP   B CD1 
852  C CD2 . TRP   B 74  ? 0.6759 0.5622 0.1048 0.1703  -0.0023 -0.0035 83  TRP   B CD2 
853  N NE1 . TRP   B 74  ? 0.7018 0.5634 0.1185 0.1828  -0.0306 -0.0070 83  TRP   B NE1 
854  C CE2 . TRP   B 74  ? 0.6923 0.5668 0.1120 0.1886  -0.0142 -0.0046 83  TRP   B CE2 
855  C CE3 . TRP   B 74  ? 0.6792 0.5748 0.1113 0.1722  0.0130  -0.0028 83  TRP   B CE3 
856  C CZ2 . TRP   B 74  ? 0.7003 0.5775 0.1154 0.2080  -0.0089 -0.0027 83  TRP   B CZ2 
857  C CZ3 . TRP   B 74  ? 0.6942 0.5879 0.1232 0.1888  0.0162  -0.0005 83  TRP   B CZ3 
858  C CH2 . TRP   B 74  ? 0.6983 0.5855 0.1196 0.2062  0.0064  0.0008  83  TRP   B CH2 
859  N N   . LYS   B 75  ? 0.7043 0.6361 0.1867 0.1446  -0.0165 -0.0145 84  LYS   B N   
860  C CA  . LYS   B 75  ? 0.7166 0.6493 0.2101 0.1435  -0.0343 -0.0185 84  LYS   B CA  
861  C C   . LYS   B 75  ? 0.7480 0.6509 0.2230 0.1589  -0.0534 -0.0225 84  LYS   B C   
862  O O   . LYS   B 75  ? 0.7589 0.6513 0.2370 0.1530  -0.0728 -0.0257 84  LYS   B O   
863  C CB  . LYS   B 75  ? 0.7181 0.6805 0.2329 0.1540  -0.0297 -0.0252 84  LYS   B CB  
864  C CG  . LYS   B 75  ? 0.7460 0.7414 0.2794 0.1438  -0.0107 -0.0236 84  LYS   B CG  
865  C CD  . LYS   B 75  ? 0.7828 0.8027 0.3395 0.1202  -0.0146 -0.0200 84  LYS   B CD  
866  C CE  . LYS   B 75  ? 0.8130 0.8666 0.3825 0.1115  0.0071  -0.0175 84  LYS   B CE  
867  N NZ  . LYS   B 75  ? 0.8160 0.9068 0.4148 0.0928  0.0064  -0.0136 84  LYS   B NZ  
868  N N   . LEU   B 76  ? 0.7599 0.6508 0.2166 0.1789  -0.0488 -0.0226 85  LEU   B N   
869  C CA  . LEU   B 76  ? 0.7797 0.6477 0.2171 0.1988  -0.0651 -0.0272 85  LEU   B CA  
870  C C   . LEU   B 76  ? 0.8186 0.6566 0.2402 0.1894  -0.0796 -0.0247 85  LEU   B C   
871  O O   . LEU   B 76  ? 0.8282 0.6600 0.2418 0.1819  -0.0713 -0.0173 85  LEU   B O   
872  C CB  . LEU   B 76  ? 0.7707 0.6418 0.1958 0.2230  -0.0539 -0.0256 85  LEU   B CB  
873  C CG  . LEU   B 76  ? 0.7588 0.6542 0.1975 0.2298  -0.0363 -0.0244 85  LEU   B CG  
874  C CD1 . LEU   B 76  ? 0.7642 0.6595 0.1920 0.2469  -0.0250 -0.0185 85  LEU   B CD1 
875  C CD2 . LEU   B 76  ? 0.7501 0.6590 0.2001 0.2392  -0.0437 -0.0316 85  LEU   B CD2 
876  N N   . ASP   B 77  ? 0.8446 0.6620 0.2611 0.1901  -0.1027 -0.0312 86  ASP   B N   
877  C CA  . ASP   B 77  ? 0.8852 0.6684 0.2866 0.1810  -0.1193 -0.0289 86  ASP   B CA  
878  C C   . ASP   B 77  ? 0.9212 0.6728 0.2984 0.2049  -0.1420 -0.0393 86  ASP   B C   
879  O O   . ASP   B 77  ? 0.9464 0.6651 0.3087 0.2004  -0.1572 -0.0382 86  ASP   B O   
880  C CB  . ASP   B 77  ? 0.9120 0.6923 0.3307 0.1489  -0.1282 -0.0240 86  ASP   B CB  
881  C CG  . ASP   B 77  ? 0.9931 0.7788 0.4286 0.1451  -0.1449 -0.0326 86  ASP   B CG  
882  O OD1 . ASP   B 77  ? 0.9936 0.7945 0.4309 0.1668  -0.1445 -0.0424 86  ASP   B OD1 
883  O OD2 . ASP   B 77  ? 1.0339 0.8094 0.4813 0.1199  -0.1590 -0.0287 86  ASP   B OD2 
884  N N   . ALA   B 78  ? 0.9224 0.6826 0.2929 0.2319  -0.1444 -0.0490 87  ALA   B N   
885  C CA  . ALA   B 78  ? 0.9493 0.6822 0.2931 0.2585  -0.1650 -0.0604 87  ALA   B CA  
886  C C   . ALA   B 78  ? 0.9696 0.6966 0.2913 0.2794  -0.1569 -0.0564 87  ALA   B C   
887  O O   . ALA   B 78  ? 0.9606 0.7113 0.2895 0.2776  -0.1339 -0.0458 87  ALA   B O   
888  C CB  . ALA   B 78  ? 0.9477 0.6952 0.2894 0.2813  -0.1698 -0.0713 87  ALA   B CB  
889  N N   . ALA   B 79  ? 0.9915 0.6875 0.2869 0.3000  -0.1768 -0.0654 88  ALA   B N   
890  C CA  . ALA   B 79  ? 1.0019 0.6966 0.2776 0.3225  -0.1703 -0.0620 88  ALA   B CA  
891  C C   . ALA   B 79  ? 1.0249 0.7072 0.2716 0.3613  -0.1850 -0.0757 88  ALA   B C   
892  O O   . ALA   B 79  ? 1.0336 0.6880 0.2680 0.3680  -0.2098 -0.0904 88  ALA   B O   
893  C CB  . ALA   B 79  ? 1.0126 0.6808 0.2838 0.3061  -0.1769 -0.0551 88  ALA   B CB  
894  N N   . TRP   B 80  ? 1.0296 0.7337 0.2652 0.3868  -0.1701 -0.0707 89  TRP   B N   
895  C CA  . TRP   B 80  ? 1.0537 0.7548 0.2600 0.4276  -0.1787 -0.0812 89  TRP   B CA  
896  C C   . TRP   B 80  ? 1.1001 0.7520 0.2824 0.4367  -0.2079 -0.0945 89  TRP   B C   
897  O O   . TRP   B 80  ? 1.1005 0.7305 0.2872 0.4172  -0.2127 -0.0881 89  TRP   B O   
898  C CB  . TRP   B 80  ? 1.0376 0.7744 0.2430 0.4456  -0.1554 -0.0685 89  TRP   B CB  
899  C CG  . TRP   B 80  ? 1.0516 0.7944 0.2276 0.4898  -0.1606 -0.0773 89  TRP   B CG  
900  C CD1 . TRP   B 80  ? 1.0672 0.8117 0.2229 0.5175  -0.1690 -0.0901 89  TRP   B CD1 
901  C CD2 . TRP   B 80  ? 1.0509 0.8059 0.2150 0.5133  -0.1550 -0.0728 89  TRP   B CD2 
902  N NE1 . TRP   B 80  ? 1.0761 0.8314 0.2053 0.5577  -0.1692 -0.0947 89  TRP   B NE1 
903  C CE2 . TRP   B 80  ? 1.0656 0.8295 0.2013 0.5559  -0.1601 -0.0838 89  TRP   B CE2 
904  C CE3 . TRP   B 80  ? 1.0490 0.8109 0.2236 0.5035  -0.1468 -0.0606 89  TRP   B CE3 
905  C CZ2 . TRP   B 80  ? 1.0678 0.8488 0.1867 0.5893  -0.1562 -0.0830 89  TRP   B CZ2 
906  C CZ3 . TRP   B 80  ? 1.0560 0.8346 0.2159 0.5356  -0.1443 -0.0597 89  TRP   B CZ3 
907  C CH2 . TRP   B 80  ? 1.0595 0.8489 0.1927 0.5782  -0.1482 -0.0705 89  TRP   B CH2 
908  N N   . ASP   B 81  ? 1.1369 0.7685 0.2922 0.4662  -0.2291 -0.1134 90  ASP   B N   
909  C CA  . ASP   B 81  ? 1.1889 0.7670 0.3190 0.4767  -0.2601 -0.1283 90  ASP   B CA  
910  C C   . ASP   B 81  ? 1.2171 0.7930 0.3220 0.5117  -0.2596 -0.1300 90  ASP   B C   
911  O O   . ASP   B 81  ? 1.2484 0.7774 0.3307 0.5233  -0.2851 -0.1419 90  ASP   B O   
912  C CB  . ASP   B 81  ? 1.2308 0.7793 0.3428 0.4894  -0.2887 -0.1507 90  ASP   B CB  
913  C CG  . ASP   B 81  ? 1.3049 0.8814 0.3959 0.5290  -0.2838 -0.1612 90  ASP   B CG  
914  O OD1 . ASP   B 81  ? 1.3212 0.9406 0.4106 0.5491  -0.2576 -0.1501 90  ASP   B OD1 
915  O OD2 . ASP   B 81  ? 1.3252 0.8816 0.4011 0.5396  -0.3068 -0.1799 90  ASP   B OD2 
916  N N   . GLY   B 82  ? 1.2022 0.8281 0.3129 0.5271  -0.2316 -0.1173 91  GLY   B N   
917  C CA  . GLY   B 82  ? 1.2147 0.8504 0.3067 0.5606  -0.2281 -0.1169 91  GLY   B CA  
918  C C   . GLY   B 82  ? 1.2388 0.8757 0.2953 0.6102  -0.2382 -0.1351 91  GLY   B C   
919  O O   . GLY   B 82  ? 1.2479 0.8975 0.2870 0.6438  -0.2353 -0.1364 91  GLY   B O   
920  N N   . LEU   B 83  ? 1.2442 0.8709 0.2886 0.6174  -0.2504 -0.1497 92  LEU   B N   
921  C CA  . LEU   B 83  ? 1.2630 0.8878 0.2689 0.6656  -0.2626 -0.1695 92  LEU   B CA  
922  C C   . LEU   B 83  ? 1.2614 0.9275 0.2664 0.6774  -0.2476 -0.1679 92  LEU   B C   
923  O O   . LEU   B 83  ? 1.2735 0.9635 0.2504 0.7204  -0.2433 -0.1748 92  LEU   B O   
924  C CB  . LEU   B 83  ? 1.2974 0.8538 0.2782 0.6691  -0.3037 -0.1959 92  LEU   B CB  
925  C CG  . LEU   B 83  ? 1.3426 0.8393 0.3085 0.6694  -0.3307 -0.2056 92  LEU   B CG  
926  C CD1 . LEU   B 83  ? 1.3816 0.8198 0.3091 0.6943  -0.3707 -0.2368 92  LEU   B CD1 
927  C CD2 . LEU   B 83  ? 1.3445 0.8607 0.2999 0.6985  -0.3180 -0.1987 92  LEU   B CD2 
928  N N   . SER   B 84  ? 1.2428 0.9143 0.2748 0.6424  -0.2428 -0.1607 93  SER   B N   
929  C CA  . SER   B 84  ? 1.2266 0.9288 0.2559 0.6529  -0.2340 -0.1609 93  SER   B CA  
930  C C   . SER   B 84  ? 1.1856 0.9476 0.2365 0.6496  -0.1967 -0.1355 93  SER   B C   
931  O O   . SER   B 84  ? 1.1757 0.9542 0.2557 0.6236  -0.1773 -0.1163 93  SER   B O   
932  C CB  . SER   B 84  ? 1.2537 0.9309 0.2994 0.6213  -0.2514 -0.1687 93  SER   B CB  
933  O OG  . SER   B 84  ? 1.3127 0.9313 0.3458 0.6148  -0.2865 -0.1885 93  SER   B OG  
934  N N   . GLU   B 85  ? 1.1665 0.9590 0.2020 0.6753  -0.1879 -0.1352 94  GLU   B N   
935  C CA  . GLU   B 85  ? 1.1323 0.9779 0.1869 0.6719  -0.1545 -0.1100 94  GLU   B CA  
936  C C   . GLU   B 85  ? 1.1038 0.9483 0.1953 0.6288  -0.1479 -0.0996 94  GLU   B C   
937  O O   . GLU   B 85  ? 1.1162 0.9293 0.2128 0.6107  -0.1689 -0.1135 94  GLU   B O   
938  C CB  . GLU   B 85  ? 1.1557 1.0319 0.1801 0.7123  -0.1485 -0.1113 94  GLU   B CB  
939  C CG  . GLU   B 85  ? 1.2101 1.1091 0.2034 0.7566  -0.1423 -0.1128 94  GLU   B CG  
940  C CD  . GLU   B 85  ? 1.2567 1.2055 0.2300 0.7905  -0.1222 -0.1007 94  GLU   B CD  
941  O OE1 . GLU   B 85  ? 1.2492 1.2008 0.2153 0.7924  -0.1250 -0.1022 94  GLU   B OE1 
942  O OE2 . GLU   B 85  ? 1.2666 1.2539 0.2318 0.8154  -0.1036 -0.0886 94  GLU   B OE2 
943  N N   . VAL   B 86  ? 1.0638 0.9424 0.1827 0.6113  -0.1195 -0.0754 95  VAL   B N   
944  C CA  . VAL   B 86  ? 1.0338 0.9142 0.1873 0.5734  -0.1103 -0.0649 95  VAL   B CA  
945  C C   . VAL   B 86  ? 1.0060 0.9246 0.1666 0.5797  -0.0873 -0.0467 95  VAL   B C   
946  O O   . VAL   B 86  ? 1.0050 0.9506 0.1450 0.6109  -0.0772 -0.0398 95  VAL   B O   
947  C CB  . VAL   B 86  ? 1.0195 0.8944 0.2015 0.5397  -0.1010 -0.0540 95  VAL   B CB  
948  C CG1 . VAL   B 86  ? 1.0393 0.8740 0.2122 0.5338  -0.1244 -0.0695 95  VAL   B CG1 
949  C CG2 . VAL   B 86  ? 1.0052 0.9161 0.1948 0.5462  -0.0761 -0.0335 95  VAL   B CG2 
950  N N   . GLN   B 87  ? 0.9834 0.9043 0.1719 0.5515  -0.0793 -0.0385 96  GLN   B N   
951  C CA  . GLN   B 87  ? 0.9610 0.9114 0.1579 0.5547  -0.0589 -0.0201 96  GLN   B CA  
952  C C   . GLN   B 87  ? 0.9280 0.8845 0.1608 0.5203  -0.0404 -0.0033 96  GLN   B C   
953  O O   . GLN   B 87  ? 0.9223 0.8607 0.1748 0.4934  -0.0469 -0.0101 96  GLN   B O   
954  C CB  . GLN   B 87  ? 0.9747 0.9216 0.1621 0.5651  -0.0710 -0.0297 96  GLN   B CB  
955  C CG  . GLN   B 87  ? 1.0207 0.9809 0.1700 0.6069  -0.0760 -0.0342 96  GLN   B CG  
956  C CD  . GLN   B 87  ? 1.0761 1.0351 0.2146 0.6187  -0.0889 -0.0431 96  GLN   B CD  
957  O OE1 . GLN   B 87  ? 1.0762 1.0306 0.2390 0.5966  -0.0904 -0.0424 96  GLN   B OE1 
958  N NE2 . GLN   B 87  ? 1.0961 1.0609 0.1963 0.6561  -0.0992 -0.0526 96  GLN   B NE2 
959  N N   . LEU   B 88  ? 0.9022 0.8852 0.1432 0.5213  -0.0179 0.0187  97  LEU   B N   
960  C CA  . LEU   B 88  ? 0.8803 0.8676 0.1527 0.4912  -0.0013 0.0343  97  LEU   B CA  
961  C C   . LEU   B 88  ? 0.8629 0.8555 0.1399 0.4929  0.0046  0.0414  97  LEU   B C   
962  O O   . LEU   B 88  ? 0.8710 0.8837 0.1334 0.5159  0.0130  0.0538  97  LEU   B O   
963  C CB  . LEU   B 88  ? 0.8696 0.8839 0.1497 0.4920  0.0183  0.0560  97  LEU   B CB  
964  C CG  . LEU   B 88  ? 0.8740 0.8955 0.1832 0.4658  0.0362  0.0754  97  LEU   B CG  
965  C CD1 . LEU   B 88  ? 0.8896 0.8884 0.2197 0.4335  0.0316  0.0666  97  LEU   B CD1 
966  C CD2 . LEU   B 88  ? 0.8638 0.9162 0.1805 0.4688  0.0535  0.0982  97  LEU   B CD2 
967  N N   . LEU   B 89  ? 0.8394 0.8160 0.1346 0.4718  -0.0001 0.0342  98  LEU   B N   
968  C CA  . LEU   B 89  ? 0.8295 0.8111 0.1309 0.4744  0.0059  0.0419  98  LEU   B CA  
969  C C   . LEU   B 89  ? 0.8228 0.8105 0.1454 0.4563  0.0265  0.0627  98  LEU   B C   
970  O O   . LEU   B 89  ? 0.8216 0.7971 0.1666 0.4307  0.0292  0.0603  98  LEU   B O   
971  C CB  . LEU   B 89  ? 0.8275 0.7944 0.1405 0.4627  -0.0078 0.0251  98  LEU   B CB  
972  C CG  . LEU   B 89  ? 0.8313 0.8016 0.1575 0.4610  -0.0009 0.0324  98  LEU   B CG  
973  C CD1 . LEU   B 89  ? 0.8450 0.8295 0.1530 0.4877  0.0059  0.0475  98  LEU   B CD1 
974  C CD2 . LEU   B 89  ? 0.8311 0.7953 0.1664 0.4560  -0.0170 0.0143  98  LEU   B CD2 
975  N N   . ALA   B 90  ? 0.8090 0.8167 0.1245 0.4691  0.0405  0.0833  99  ALA   B N   
976  C CA  . ALA   B 90  ? 0.8012 0.8145 0.1375 0.4509  0.0581  0.1046  99  ALA   B CA  
977  C C   . ALA   B 90  ? 0.8039 0.8094 0.1499 0.4467  0.0648  0.1156  99  ALA   B C   
978  O O   . ALA   B 90  ? 0.8106 0.8241 0.1411 0.4684  0.0656  0.1234  99  ALA   B O   
979  C CB  . ALA   B 90  ? 0.7898 0.8311 0.1190 0.4637  0.0705  0.1248  99  ALA   B CB  
980  N N   . VAL   B 91  ? 0.7892 0.7784 0.1591 0.4203  0.0695  0.1166  100 VAL   B N   
981  C CA  . VAL   B 91  ? 0.7836 0.7603 0.1639 0.4155  0.0757  0.1270  100 VAL   B CA  
982  C C   . VAL   B 91  ? 0.7829 0.7602 0.1788 0.3988  0.0899  0.1504  100 VAL   B C   
983  O O   . VAL   B 91  ? 0.7790 0.7422 0.1930 0.3746  0.0914  0.1468  100 VAL   B O   
984  C CB  . VAL   B 91  ? 0.7841 0.7403 0.1778 0.4014  0.0681  0.1073  100 VAL   B CB  
985  C CG1 . VAL   B 91  ? 0.7923 0.7342 0.1940 0.4020  0.0729  0.1159  100 VAL   B CG1 
986  C CG2 . VAL   B 91  ? 0.7846 0.7435 0.1682 0.4125  0.0529  0.0854  100 VAL   B CG2 
987  N N   . PRO   B 92  ? 0.7857 0.7812 0.1744 0.4110  0.1001  0.1753  101 PRO   B N   
988  C CA  . PRO   B 92  ? 0.7868 0.7857 0.1939 0.3922  0.1125  0.1996  101 PRO   B CA  
989  C C   . PRO   B 92  ? 0.8109 0.7823 0.2316 0.3789  0.1163  0.2119  101 PRO   B C   
990  O O   . PRO   B 92  ? 0.8218 0.7791 0.2334 0.3925  0.1132  0.2107  101 PRO   B O   
991  C CB  . PRO   B 92  ? 0.7770 0.8109 0.1709 0.4116  0.1221  0.2221  101 PRO   B CB  
992  C CG  . PRO   B 92  ? 0.7845 0.8223 0.1508 0.4422  0.1159  0.2142  101 PRO   B CG  
993  C CD  . PRO   B 92  ? 0.7716 0.7877 0.1349 0.4420  0.1004  0.1829  101 PRO   B CD  
994  N N   . PRO   B 93  ? 0.8174 0.7792 0.2601 0.3526  0.1213  0.2233  102 PRO   B N   
995  C CA  . PRO   B 93  ? 0.8342 0.7631 0.2886 0.3399  0.1225  0.2336  102 PRO   B CA  
996  C C   . PRO   B 93  ? 0.8550 0.7849 0.2995 0.3561  0.1292  0.2604  102 PRO   B C   
997  O O   . PRO   B 93  ? 0.8562 0.8168 0.2951 0.3647  0.1383  0.2833  102 PRO   B O   
998  C CB  . PRO   B 93  ? 0.8319 0.7577 0.3099 0.3100  0.1258  0.2442  102 PRO   B CB  
999  C CG  . PRO   B 93  ? 0.8254 0.7741 0.3049 0.3052  0.1230  0.2285  102 PRO   B CG  
1000 C CD  . PRO   B 93  ? 0.8029 0.7806 0.2606 0.3337  0.1236  0.2252  102 PRO   B CD  
1001 N N   . GLY   B 94  ? 0.8675 0.7662 0.3081 0.3626  0.1247  0.2575  103 GLY   B N   
1002 C CA  . GLY   B 94  ? 0.8819 0.7757 0.3110 0.3789  0.1292  0.2828  103 GLY   B CA  
1003 C C   . GLY   B 94  ? 0.8920 0.8178 0.2949 0.4103  0.1308  0.2870  103 GLY   B C   
1004 O O   . GLY   B 94  ? 0.8980 0.8272 0.2877 0.4256  0.1362  0.3120  103 GLY   B O   
1005 N N   . GLU   B 95  ? 0.8884 0.8369 0.2818 0.4204  0.1253  0.2633  104 GLU   B N   
1006 C CA  . GLU   B 95  ? 0.8962 0.8730 0.2623 0.4510  0.1240  0.2625  104 GLU   B CA  
1007 C C   . GLU   B 95  ? 0.9016 0.8745 0.2584 0.4631  0.1089  0.2278  104 GLU   B C   
1008 O O   . GLU   B 95  ? 0.9035 0.8633 0.2756 0.4457  0.1024  0.2052  104 GLU   B O   
1009 C CB  . GLU   B 95  ? 0.9210 0.9361 0.2822 0.4541  0.1329  0.2738  104 GLU   B CB  
1010 C CG  . GLU   B 95  ? 0.9837 1.0112 0.3574 0.4413  0.1487  0.3113  104 GLU   B CG  
1011 C CD  . GLU   B 95  ? 1.0665 1.1320 0.4485 0.4349  0.1578  0.3204  104 GLU   B CD  
1012 O OE1 . GLU   B 95  ? 1.0743 1.1532 0.4495 0.4421  0.1513  0.2962  104 GLU   B OE1 
1013 O OE2 . GLU   B 95  ? 1.0997 1.1818 0.4958 0.4226  0.1710  0.3527  104 GLU   B OE2 
1014 N N   . ARG   B 96  ? 0.9016 0.8874 0.2332 0.4922  0.1028  0.2246  105 ARG   B N   
1015 C CA  . ARG   B 96  ? 0.9185 0.9040 0.2403 0.5059  0.0864  0.1944  105 ARG   B CA  
1016 C C   . ARG   B 96  ? 0.9214 0.9196 0.2414 0.5017  0.0797  0.1725  105 ARG   B C   
1017 O O   . ARG   B 96  ? 0.9256 0.9424 0.2407 0.5018  0.0877  0.1827  105 ARG   B O   
1018 C CB  . ARG   B 96  ? 0.9557 0.9557 0.2475 0.5394  0.0819  0.2010  105 ARG   B CB  
1019 C CG  . ARG   B 96  ? 1.0249 1.0198 0.3100 0.5540  0.0635  0.1757  105 ARG   B CG  
1020 C CD  . ARG   B 96  ? 1.0997 1.0923 0.3691 0.5771  0.0617  0.1903  105 ARG   B CD  
1021 N NE  . ARG   B 96  ? 1.1676 1.1814 0.4065 0.6011  0.0690  0.2132  105 ARG   B NE  
1022 C CZ  . ARG   B 96  ? 1.2237 1.2355 0.4565 0.6055  0.0825  0.2468  105 ARG   B CZ  
1023 N NH1 . ARG   B 96  ? 1.2286 1.2129 0.4836 0.5874  0.0882  0.2601  105 ARG   B NH1 
1024 N NH2 . ARG   B 96  ? 1.2312 1.2676 0.4345 0.6283  0.0899  0.2677  105 ARG   B NH2 
1025 N N   . ALA   B 97  ? 0.9162 0.9059 0.2403 0.4990  0.0646  0.1436  106 ALA   B N   
1026 C CA  . ALA   B 97  ? 0.9161 0.9124 0.2363 0.4959  0.0552  0.1226  106 ALA   B CA  
1027 C C   . ALA   B 97  ? 0.9281 0.9453 0.2168 0.5252  0.0509  0.1236  106 ALA   B C   
1028 O O   . ALA   B 97  ? 0.9321 0.9566 0.2010 0.5493  0.0478  0.1289  106 ALA   B O   
1029 C CB  . ALA   B 97  ? 0.9129 0.8976 0.2428 0.4887  0.0392  0.0956  106 ALA   B CB  
1030 N N   . LYS   B 98  ? 0.9323 0.9590 0.2146 0.5251  0.0505  0.1181  107 LYS   B N   
1031 C CA  . LYS   B 98  ? 0.9424 0.9898 0.1937 0.5543  0.0483  0.1186  107 LYS   B CA  
1032 C C   . LYS   B 98  ? 0.9478 0.9896 0.1927 0.5541  0.0340  0.0942  107 LYS   B C   
1033 O O   . LYS   B 98  ? 0.9460 0.9811 0.2104 0.5310  0.0374  0.0922  107 LYS   B O   
1034 C CB  . LYS   B 98  ? 0.9666 1.0370 0.2200 0.5546  0.0698  0.1481  107 LYS   B CB  
1035 C CG  . LYS   B 98  ? 1.0428 1.1441 0.2644 0.5882  0.0761  0.1610  107 LYS   B CG  
1036 C CD  . LYS   B 98  ? 1.1043 1.2326 0.3382 0.5809  0.0998  0.1946  107 LYS   B CD  
1037 C CE  . LYS   B 98  ? 1.1423 1.2664 0.4087 0.5490  0.1051  0.1952  107 LYS   B CE  
1038 N NZ  . LYS   B 98  ? 1.1551 1.3034 0.4404 0.5362  0.1261  0.2289  107 LYS   B NZ  
1039 N N   . ASN   B 99  ? 0.9552 0.9971 0.1718 0.5794  0.0168  0.0755  108 ASN   B N   
1040 C CA  . ASN   B 99  ? 0.9670 0.9978 0.1752 0.5803  0.0010  0.0526  108 ASN   B CA  
1041 C C   . ASN   B 99  ? 0.9726 1.0253 0.1588 0.6033  0.0091  0.0605  108 ASN   B C   
1042 O O   . ASN   B 99  ? 0.9818 1.0543 0.1414 0.6330  0.0129  0.0682  108 ASN   B O   
1043 C CB  . ASN   B 99  ? 0.9850 1.0003 0.1744 0.5948  -0.0251 0.0262  108 ASN   B CB  
1044 C CG  . ASN   B 99  ? 1.0184 1.0148 0.2335 0.5697  -0.0362 0.0141  108 ASN   B CG  
1045 O OD1 . ASN   B 99  ? 1.0315 1.0312 0.2654 0.5588  -0.0265 0.0257  108 ASN   B OD1 
1046 N ND2 . ASN   B 99  ? 1.0245 1.0013 0.2410 0.5610  -0.0573 -0.0091 108 ASN   B ND2 
1047 N N   . ILE   B 100 ? 0.9703 1.0226 0.1666 0.5918  0.0122  0.0592  109 ILE   B N   
1048 C CA  . ILE   B 100 ? 0.9729 1.0505 0.1508 0.6153  0.0201  0.0660  109 ILE   B CA  
1049 C C   . ILE   B 100 ? 1.0031 1.0609 0.1671 0.6227  0.0003  0.0404  109 ILE   B C   
1050 O O   . ILE   B 100 ? 1.0088 1.0486 0.1936 0.5970  -0.0038 0.0345  109 ILE   B O   
1051 C CB  . ILE   B 100 ? 0.9553 1.0566 0.1600 0.5969  0.0434  0.0923  109 ILE   B CB  
1052 C CG1 . ILE   B 100 ? 0.9556 1.0653 0.1801 0.5809  0.0607  0.1178  109 ILE   B CG1 
1053 C CG2 . ILE   B 100 ? 0.9529 1.0895 0.1402 0.6243  0.0531  0.1014  109 ILE   B CG2 
1054 C CD1 . ILE   B 100 ? 0.9726 1.1075 0.1744 0.6087  0.0705  0.1351  109 ILE   B CD1 
1055 N N   . GLN   B 101 ? 1.0249 1.0841 0.1519 0.6584  -0.0126 0.0253  110 GLN   B N   
1056 C CA  . GLN   B 101 ? 1.0575 1.0920 0.1662 0.6697  -0.0347 -0.0006 110 GLN   B CA  
1057 C C   . GLN   B 101 ? 1.0677 1.1228 0.1740 0.6815  -0.0243 0.0065  110 GLN   B C   
1058 O O   . GLN   B 101 ? 1.0636 1.1597 0.1602 0.7043  -0.0054 0.0243  110 GLN   B O   
1059 C CB  . GLN   B 101 ? 1.0989 1.1246 0.1656 0.7064  -0.0550 -0.0218 110 GLN   B CB  
1060 C CG  . GLN   B 101 ? 1.1585 1.1492 0.2030 0.7191  -0.0830 -0.0518 110 GLN   B CG  
1061 C CD  . GLN   B 101 ? 1.2174 1.1817 0.2373 0.7328  -0.1107 -0.0764 110 GLN   B CD  
1062 O OE1 . GLN   B 101 ? 1.2247 1.1840 0.2597 0.7151  -0.1143 -0.0753 110 GLN   B OE1 
1063 N NE2 . GLN   B 101 ? 1.2458 1.1926 0.2274 0.7654  -0.1323 -0.1002 110 GLN   B NE2 
1064 N N   . THR   B 102 ? 1.0759 1.1049 0.1909 0.6672  -0.0368 -0.0065 111 THR   B N   
1065 C CA  . THR   B 102 ? 1.0808 1.1268 0.1944 0.6791  -0.0303 -0.0022 111 THR   B CA  
1066 C C   . THR   B 102 ? 1.1123 1.1147 0.2157 0.6781  -0.0564 -0.0272 111 THR   B C   
1067 O O   . THR   B 102 ? 1.1322 1.0935 0.2404 0.6565  -0.0753 -0.0423 111 THR   B O   
1068 C CB  . THR   B 102 ? 1.0761 1.1481 0.2296 0.6482  -0.0066 0.0244  111 THR   B CB  
1069 O OG1 . THR   B 102 ? 1.0805 1.1847 0.2324 0.6665  0.0034  0.0331  111 THR   B OG1 
1070 C CG2 . THR   B 102 ? 1.0829 1.1206 0.2653 0.6056  -0.0144 0.0198  111 THR   B CG2 
1071 N N   . LEU   B 103 ? 1.1112 1.1229 0.2016 0.7011  -0.0576 -0.0306 112 LEU   B N   
1072 C CA  . LEU   B 103 ? 1.1299 1.0970 0.2123 0.6983  -0.0819 -0.0510 112 LEU   B CA  
1073 C C   . LEU   B 103 ? 1.1122 1.0890 0.2278 0.6697  -0.0699 -0.0349 112 LEU   B C   
1074 O O   . LEU   B 103 ? 1.0972 1.1190 0.2231 0.6794  -0.0497 -0.0170 112 LEU   B O   
1075 C CB  . LEU   B 103 ? 1.1497 1.1100 0.1915 0.7453  -0.0973 -0.0704 112 LEU   B CB  
1076 C CG  . LEU   B 103 ? 1.1942 1.0988 0.2277 0.7395  -0.1256 -0.0911 112 LEU   B CG  
1077 C CD1 . LEU   B 103 ? 1.2260 1.0762 0.2440 0.7315  -0.1549 -0.1145 112 LEU   B CD1 
1078 C CD2 . LEU   B 103 ? 1.2089 1.1179 0.2152 0.7812  -0.1322 -0.1011 112 LEU   B CD2 
1079 N N   . PRO   B 104 ? 1.1113 1.0490 0.2440 0.6344  -0.0823 -0.0403 113 PRO   B N   
1080 C CA  . PRO   B 104 ? 1.0919 1.0394 0.2552 0.6057  -0.0710 -0.0247 113 PRO   B CA  
1081 C C   . PRO   B 104 ? 1.0854 1.0387 0.2417 0.6240  -0.0749 -0.0256 113 PRO   B C   
1082 O O   . PRO   B 104 ? 1.1077 1.0407 0.2337 0.6557  -0.0929 -0.0432 113 PRO   B O   
1083 C CB  . PRO   B 104 ? 1.1117 1.0155 0.2895 0.5663  -0.0842 -0.0315 113 PRO   B CB  
1084 C CG  . PRO   B 104 ? 1.1321 1.0172 0.2982 0.5687  -0.0951 -0.0441 113 PRO   B CG  
1085 C CD  . PRO   B 104 ? 1.1230 1.0125 0.2523 0.6152  -0.1044 -0.0574 113 PRO   B CD  
1086 N N   . GLY   B 105 ? 1.0519 1.0341 0.2372 0.6041  -0.0582 -0.0065 114 GLY   B N   
1087 C CA  . GLY   B 105 ? 1.0333 1.0284 0.2212 0.6148  -0.0594 -0.0030 114 GLY   B CA  
1088 C C   . GLY   B 105 ? 1.0242 0.9763 0.2199 0.5855  -0.0750 -0.0082 114 GLY   B C   
1089 O O   . GLY   B 105 ? 1.0406 0.9469 0.2309 0.5657  -0.0898 -0.0194 114 GLY   B O   
1090 N N   . ILE   B 106 ? 0.9966 0.9656 0.2058 0.5821  -0.0718 0.0012  115 ILE   B N   
1091 C CA  . ILE   B 106 ? 1.0008 0.9309 0.2129 0.5589  -0.0872 -0.0023 115 ILE   B CA  
1092 C C   . ILE   B 106 ? 0.9727 0.9349 0.2159 0.5344  -0.0733 0.0164  115 ILE   B C   
1093 O O   . ILE   B 106 ? 0.9548 0.9671 0.2110 0.5492  -0.0597 0.0285  115 ILE   B O   
1094 C CB  . ILE   B 106 ? 1.0305 0.9295 0.2107 0.5938  -0.1106 -0.0190 115 ILE   B CB  
1095 C CG1 . ILE   B 106 ? 1.0685 0.9082 0.2207 0.5983  -0.1343 -0.0402 115 ILE   B CG1 
1096 C CG2 . ILE   B 106 ? 1.0457 0.9327 0.2303 0.5871  -0.1203 -0.0150 115 ILE   B CG2 
1097 C CD1 . ILE   B 106 ? 1.0942 0.8925 0.2562 0.5569  -0.1435 -0.0404 115 ILE   B CD1 
1098 N N   . PHE   B 107 ? 0.9683 0.9035 0.2233 0.4970  -0.0772 0.0187  116 PHE   B N   
1099 C CA  . PHE   B 107 ? 0.9535 0.9100 0.2330 0.4728  -0.0691 0.0329  116 PHE   B CA  
1100 C C   . PHE   B 107 ? 0.9779 0.8947 0.2421 0.4711  -0.0900 0.0261  116 PHE   B C   
1101 O O   . PHE   B 107 ? 0.9975 0.8708 0.2547 0.4477  -0.1007 0.0206  116 PHE   B O   
1102 C CB  . PHE   B 107 ? 0.9449 0.8985 0.2454 0.4324  -0.0579 0.0398  116 PHE   B CB  
1103 C CG  . PHE   B 107 ? 0.9278 0.9260 0.2528 0.4251  -0.0354 0.0537  116 PHE   B CG  
1104 C CD1 . PHE   B 107 ? 0.9201 0.9593 0.2466 0.4534  -0.0246 0.0604  116 PHE   B CD1 
1105 C CD2 . PHE   B 107 ? 0.9256 0.9234 0.2707 0.3908  -0.0255 0.0603  116 PHE   B CD2 
1106 C CE1 . PHE   B 107 ? 0.9056 0.9834 0.2550 0.4445  -0.0044 0.0762  116 PHE   B CE1 
1107 C CE2 . PHE   B 107 ? 0.9136 0.9458 0.2804 0.3836  -0.0070 0.0736  116 PHE   B CE2 
1108 C CZ  . PHE   B 107 ? 0.8984 0.9695 0.2679 0.4091  0.0032  0.0825  116 PHE   B CZ  
1109 N N   . LYS   B 108 ? 0.9748 0.9061 0.2325 0.4978  -0.0966 0.0268  117 LYS   B N   
1110 C CA  . LYS   B 108 ? 1.0001 0.8943 0.2422 0.4997  -0.1174 0.0222  117 LYS   B CA  
1111 C C   . LYS   B 108 ? 0.9905 0.8986 0.2543 0.4678  -0.1122 0.0359  117 LYS   B C   
1112 O O   . LYS   B 108 ? 0.9657 0.9240 0.2513 0.4704  -0.1004 0.0473  117 LYS   B O   
1113 C CB  . LYS   B 108 ? 1.0319 0.9400 0.2588 0.5448  -0.1263 0.0172  117 LYS   B CB  
1114 C CG  . LYS   B 108 ? 1.1255 0.9868 0.3165 0.5758  -0.1462 -0.0024 117 LYS   B CG  
1115 C CD  . LYS   B 108 ? 1.2114 1.0437 0.3809 0.6013  -0.1686 -0.0089 117 LYS   B CD  
1116 C CE  . LYS   B 108 ? 1.3008 1.0992 0.4346 0.6440  -0.1871 -0.0293 117 LYS   B CE  
1117 N NZ  . LYS   B 108 ? 1.3497 1.1293 0.4639 0.6769  -0.2067 -0.0351 117 LYS   B NZ  
1118 N N   . THR   B 109 ? 1.0088 0.8749 0.2671 0.4368  -0.1209 0.0351  118 THR   B N   
1119 C CA  . THR   B 109 ? 1.0088 0.8815 0.2815 0.4059  -0.1180 0.0460  118 THR   B CA  
1120 C C   . THR   B 109 ? 1.0457 0.8738 0.2963 0.4047  -0.1399 0.0448  118 THR   B C   
1121 O O   . THR   B 109 ? 1.0738 0.8608 0.3000 0.4233  -0.1571 0.0353  118 THR   B O   
1122 C CB  . THR   B 109 ? 1.0139 0.8827 0.3002 0.3680  -0.1051 0.0484  118 THR   B CB  
1123 O OG1 . THR   B 109 ? 1.0437 0.8620 0.3123 0.3535  -0.1165 0.0415  118 THR   B OG1 
1124 C CG2 . THR   B 109 ? 1.0017 0.9025 0.3050 0.3701  -0.0864 0.0492  118 THR   B CG2 
1125 N N   . LYS   B 110 ? 1.0475 0.8807 0.3048 0.3830  -0.1407 0.0544  119 LYS   B N   
1126 C CA  . LYS   B 110 ? 1.0803 0.8709 0.3157 0.3788  -0.1606 0.0564  119 LYS   B CA  
1127 C C   . LYS   B 110 ? 1.1159 0.8535 0.3355 0.3546  -0.1676 0.0532  119 LYS   B C   
1128 O O   . LYS   B 110 ? 1.1439 0.8333 0.3397 0.3603  -0.1875 0.0515  119 LYS   B O   
1129 C CB  . LYS   B 110 ? 1.0826 0.8968 0.3284 0.3614  -0.1589 0.0680  119 LYS   B CB  
1130 C CG  . LYS   B 110 ? 1.1152 0.9573 0.3832 0.3281  -0.1401 0.0726  119 LYS   B CG  
1131 C CD  . LYS   B 110 ? 1.1508 1.0227 0.4301 0.3163  -0.1402 0.0818  119 LYS   B CD  
1132 C CE  . LYS   B 110 ? 1.1910 1.0557 0.4710 0.2794  -0.1336 0.0847  119 LYS   B CE  
1133 N NZ  . LYS   B 110 ? 1.1985 1.0942 0.5037 0.2633  -0.1142 0.0830  119 LYS   B NZ  
1134 N N   . ASP   B 111 ? 1.1079 0.8551 0.3417 0.3290  -0.1519 0.0526  120 ASP   B N   
1135 C CA  . ASP   B 111 ? 1.1239 0.8329 0.3495 0.3043  -0.1553 0.0508  120 ASP   B CA  
1136 C C   . ASP   B 111 ? 1.1376 0.8207 0.3548 0.3178  -0.1629 0.0389  120 ASP   B C   
1137 O O   . ASP   B 111 ? 1.1578 0.8069 0.3685 0.2988  -0.1700 0.0376  120 ASP   B O   
1138 C CB  . ASP   B 111 ? 1.1260 0.8591 0.3705 0.2729  -0.1356 0.0546  120 ASP   B CB  
1139 C CG  . ASP   B 111 ? 1.1551 0.9083 0.4047 0.2558  -0.1301 0.0642  120 ASP   B CG  
1140 O OD1 . ASP   B 111 ? 1.1584 0.8971 0.3933 0.2604  -0.1437 0.0702  120 ASP   B OD1 
1141 O OD2 . ASP   B 111 ? 1.1690 0.9505 0.4360 0.2386  -0.1134 0.0652  120 ASP   B OD2 
1142 N N   . GLY   B 112 ? 1.1237 0.8255 0.3417 0.3494  -0.1613 0.0308  121 GLY   B N   
1143 C CA  . GLY   B 112 ? 1.1358 0.8141 0.3426 0.3659  -0.1701 0.0176  121 GLY   B CA  
1144 C C   . GLY   B 112 ? 1.1183 0.8371 0.3348 0.3897  -0.1559 0.0120  121 GLY   B C   
1145 O O   . GLY   B 112 ? 1.1019 0.8678 0.3386 0.3870  -0.1368 0.0203  121 GLY   B O   
1146 N N   . ASP   B 113 ? 1.1218 0.8220 0.3231 0.4128  -0.1660 -0.0015 122 ASP   B N   
1147 C CA  . ASP   B 113 ? 1.1094 0.8476 0.3155 0.4376  -0.1527 -0.0060 122 ASP   B CA  
1148 C C   . ASP   B 113 ? 1.0969 0.8433 0.3173 0.4163  -0.1404 -0.0068 122 ASP   B C   
1149 O O   . ASP   B 113 ? 1.1162 0.8274 0.3322 0.3982  -0.1512 -0.0128 122 ASP   B O   
1150 C CB  . ASP   B 113 ? 1.1515 0.8685 0.3298 0.4789  -0.1700 -0.0220 122 ASP   B CB  
1151 C CG  . ASP   B 113 ? 1.2349 0.9480 0.3975 0.5094  -0.1819 -0.0233 122 ASP   B CG  
1152 O OD1 . ASP   B 113 ? 1.2492 0.9607 0.4185 0.4948  -0.1835 -0.0127 122 ASP   B OD1 
1153 O OD2 . ASP   B 113 ? 1.2812 0.9927 0.4231 0.5495  -0.1904 -0.0357 122 ASP   B OD2 
1154 N N   . ILE   B 114 ? 1.0598 0.8533 0.2985 0.4183  -0.1184 0.0002  123 ILE   B N   
1155 C CA  . ILE   B 114 ? 1.0427 0.8463 0.2947 0.4022  -0.1061 0.0001  123 ILE   B CA  
1156 C C   . ILE   B 114 ? 1.0266 0.8558 0.2718 0.4345  -0.0995 -0.0041 123 ILE   B C   
1157 O O   . ILE   B 114 ? 1.0224 0.8737 0.2598 0.4639  -0.0978 -0.0028 123 ILE   B O   
1158 C CB  . ILE   B 114 ? 1.0270 0.8588 0.3064 0.3715  -0.0857 0.0136  123 ILE   B CB  
1159 C CG1 . ILE   B 114 ? 1.0471 0.8736 0.3313 0.3518  -0.0880 0.0214  123 ILE   B CG1 
1160 C CG2 . ILE   B 114 ? 1.0294 0.8520 0.3187 0.3478  -0.0807 0.0110  123 ILE   B CG2 
1161 C CD1 . ILE   B 114 ? 1.0522 0.9159 0.3590 0.3374  -0.0699 0.0335  123 ILE   B CD1 
1162 N N   . GLY   B 115 ? 1.0141 0.8427 0.2616 0.4304  -0.0957 -0.0087 124 GLY   B N   
1163 C CA  . GLY   B 115 ? 1.0093 0.8637 0.2490 0.4595  -0.0881 -0.0108 124 GLY   B CA  
1164 C C   . GLY   B 115 ? 0.9806 0.8851 0.2424 0.4569  -0.0626 0.0072  124 GLY   B C   
1165 O O   . GLY   B 115 ? 0.9666 0.8813 0.2508 0.4290  -0.0520 0.0185  124 GLY   B O   
1166 N N   . ALA   B 116 ? 0.9657 0.9013 0.2203 0.4856  -0.0530 0.0103  125 ALA   B N   
1167 C CA  . ALA   B 116 ? 0.9433 0.9265 0.2197 0.4823  -0.0290 0.0301  125 ALA   B CA  
1168 C C   . ALA   B 116 ? 0.9338 0.9402 0.2012 0.5049  -0.0190 0.0332  125 ALA   B C   
1169 O O   . ALA   B 116 ? 0.9495 0.9442 0.1896 0.5332  -0.0304 0.0195  125 ALA   B O   
1170 C CB  . ALA   B 116 ? 0.9304 0.9462 0.2155 0.4921  -0.0227 0.0411  125 ALA   B CB  
1171 N N   . VAL   B 117 ? 0.9100 0.9461 0.1987 0.4921  0.0010  0.0512  126 VAL   B N   
1172 C CA  A VAL   B 117 ? 0.9065 0.9662 0.1878 0.5110  0.0125  0.0588  126 VAL   B CA  
1173 C CA  B VAL   B 117 ? 0.9070 0.9659 0.1885 0.5104  0.0123  0.0586  126 VAL   B CA  
1174 C C   . VAL   B 117 ? 0.8893 1.0000 0.1902 0.5128  0.0347  0.0841  126 VAL   B C   
1175 O O   . VAL   B 117 ? 0.8765 0.9963 0.2066 0.4833  0.0446  0.0982  126 VAL   B O   
1176 C CB  A VAL   B 117 ? 0.9159 0.9544 0.2010 0.4942  0.0124  0.0558  126 VAL   B CB  
1177 C CB  B VAL   B 117 ? 0.9175 0.9519 0.2050 0.4894  0.0113  0.0550  126 VAL   B CB  
1178 C CG1 A VAL   B 117 ? 0.9397 0.9415 0.2000 0.5057  -0.0093 0.0321  126 VAL   B CG1 
1179 C CG1 B VAL   B 117 ? 0.9124 0.9742 0.2122 0.4874  0.0308  0.0745  126 VAL   B CG1 
1180 C CG2 A VAL   B 117 ? 0.9172 0.9428 0.2308 0.4540  0.0173  0.0615  126 VAL   B CG2 
1181 C CG2 B VAL   B 117 ? 0.9391 0.9415 0.2002 0.5049  -0.0085 0.0327  126 VAL   B CG2 
1182 N N   . ALA   B 118 ? 0.8872 1.0325 0.1720 0.5478  0.0419  0.0900  127 ALA   B N   
1183 C CA  . ALA   B 118 ? 0.8714 1.0712 0.1759 0.5505  0.0635  0.1165  127 ALA   B CA  
1184 C C   . ALA   B 118 ? 0.8726 1.0884 0.1770 0.5525  0.0783  0.1324  127 ALA   B C   
1185 O O   . ALA   B 118 ? 0.8844 1.1313 0.1699 0.5843  0.0867  0.1395  127 ALA   B O   
1186 C CB  . ALA   B 118 ? 0.8700 1.1055 0.1594 0.5879  0.0647  0.1161  127 ALA   B CB  
1187 N N   . LEU   B 119 ? 0.8676 1.0585 0.1896 0.5204  0.0800  0.1364  128 LEU   B N   
1188 C CA  . LEU   B 119 ? 0.8639 1.0607 0.1886 0.5169  0.0921  0.1520  128 LEU   B CA  
1189 C C   . LEU   B 119 ? 0.8501 1.0510 0.2122 0.4793  0.1037  0.1720  128 LEU   B C   
1190 O O   . LEU   B 119 ? 0.8561 1.0285 0.2335 0.4516  0.0954  0.1619  128 LEU   B O   
1191 C CB  . LEU   B 119 ? 0.8857 1.0403 0.1915 0.5184  0.0783  0.1323  128 LEU   B CB  
1192 C CG  . LEU   B 119 ? 0.9213 1.0666 0.1889 0.5545  0.0633  0.1106  128 LEU   B CG  
1193 C CD1 . LEU   B 119 ? 0.9449 1.0479 0.2012 0.5490  0.0463  0.0898  128 LEU   B CD1 
1194 C CD2 . LEU   B 119 ? 0.9189 1.1046 0.1645 0.5909  0.0753  0.1239  128 LEU   B CD2 
1195 N N   . ASP   B 120 ? 0.8299 1.0671 0.2063 0.4782  0.1221  0.2008  129 ASP   B N   
1196 C CA  . ASP   B 120 ? 0.8231 1.0627 0.2354 0.4422  0.1312  0.2204  129 ASP   B CA  
1197 C C   . ASP   B 120 ? 0.8268 1.0454 0.2426 0.4299  0.1368  0.2314  129 ASP   B C   
1198 O O   . ASP   B 120 ? 0.8275 1.0645 0.2315 0.4478  0.1468  0.2475  129 ASP   B O   
1199 C CB  . ASP   B 120 ? 0.8276 1.1216 0.2634 0.4404  0.1459  0.2471  129 ASP   B CB  
1200 C CG  . ASP   B 120 ? 0.9024 1.1940 0.3749 0.4026  0.1447  0.2538  129 ASP   B CG  
1201 O OD1 . ASP   B 120 ? 0.9145 1.1619 0.3943 0.3764  0.1361  0.2424  129 ASP   B OD1 
1202 O OD2 . ASP   B 120 ? 0.9250 1.2610 0.4190 0.4000  0.1518  0.2696  129 ASP   B OD2 
1203 N N   . TYR   B 121 ? 0.8353 1.0152 0.2654 0.4012  0.1299  0.2225  130 TYR   B N   
1204 C CA  . TYR   B 121 ? 0.8459 0.9991 0.2793 0.3899  0.1327  0.2293  130 TYR   B CA  
1205 C C   . TYR   B 121 ? 0.8322 0.9698 0.2971 0.3532  0.1348  0.2392  130 TYR   B C   
1206 O O   . TYR   B 121 ? 0.8316 0.9723 0.3124 0.3358  0.1305  0.2334  130 TYR   B O   
1207 C CB  . TYR   B 121 ? 0.8700 0.9850 0.2831 0.3974  0.1186  0.2014  130 TYR   B CB  
1208 C CG  . TYR   B 121 ? 0.8874 1.0128 0.2691 0.4329  0.1162  0.1959  130 TYR   B CG  
1209 C CD1 . TYR   B 121 ? 0.9015 1.0291 0.2723 0.4464  0.1227  0.2098  130 TYR   B CD1 
1210 C CD2 . TYR   B 121 ? 0.9038 1.0353 0.2648 0.4540  0.1061  0.1771  130 TYR   B CD2 
1211 C CE1 . TYR   B 121 ? 0.9246 1.0640 0.2639 0.4805  0.1197  0.2047  130 TYR   B CE1 
1212 C CE2 . TYR   B 121 ? 0.9250 1.0642 0.2546 0.4879  0.1018  0.1701  130 TYR   B CE2 
1213 C CZ  . TYR   B 121 ? 0.9393 1.0846 0.2578 0.5014  0.1089  0.1839  130 TYR   B CZ  
1214 O OH  . TYR   B 121 ? 0.9611 1.1157 0.2459 0.5363  0.1039  0.1768  130 TYR   B OH  
1215 N N   . PRO   B 122 ? 0.8186 0.9371 0.2919 0.3414  0.1399  0.2533  131 PRO   B N   
1216 C CA  . PRO   B 122 ? 0.8072 0.9044 0.3082 0.3069  0.1391  0.2596  131 PRO   B CA  
1217 C C   . PRO   B 122 ? 0.8089 0.8718 0.3097 0.2925  0.1257  0.2296  131 PRO   B C   
1218 O O   . PRO   B 122 ? 0.8280 0.8710 0.3096 0.3057  0.1189  0.2093  131 PRO   B O   
1219 C CB  . PRO   B 122 ? 0.8285 0.9031 0.3293 0.3051  0.1440  0.2753  131 PRO   B CB  
1220 C CG  . PRO   B 122 ? 0.8353 0.9348 0.3131 0.3371  0.1518  0.2874  131 PRO   B CG  
1221 C CD  . PRO   B 122 ? 0.8185 0.9301 0.2744 0.3599  0.1445  0.2626  131 PRO   B CD  
1222 N N   . ALA   B 123 ? 0.7867 0.8462 0.3079 0.2665  0.1216  0.2271  132 ALA   B N   
1223 C CA  . ALA   B 123 ? 0.7872 0.8201 0.3066 0.2527  0.1100  0.2005  132 ALA   B CA  
1224 C C   . ALA   B 123 ? 0.7912 0.7838 0.2988 0.2528  0.1045  0.1810  132 ALA   B C   
1225 O O   . ALA   B 123 ? 0.8041 0.7822 0.3040 0.2490  0.0962  0.1585  132 ALA   B O   
1226 C CB  . ALA   B 123 ? 0.7808 0.8124 0.3241 0.2234  0.1067  0.2047  132 ALA   B CB  
1227 N N   . GLY   B 124 ? 0.7698 0.7474 0.2763 0.2578  0.1092  0.1911  133 GLY   B N   
1228 C CA  . GLY   B 124 ? 0.7596 0.7052 0.2563 0.2626  0.1051  0.1753  133 GLY   B CA  
1229 C C   . GLY   B 124 ? 0.7335 0.6846 0.2094 0.2861  0.1010  0.1595  133 GLY   B C   
1230 O O   . GLY   B 124 ? 0.7345 0.6653 0.2045 0.2896  0.0962  0.1434  133 GLY   B O   
1231 N N   . THR   B 125 ? 0.7100 0.6894 0.1752 0.3031  0.1019  0.1636  134 THR   B N   
1232 C CA  . THR   B 125 ? 0.7088 0.6927 0.1532 0.3253  0.0950  0.1479  134 THR   B CA  
1233 C C   . THR   B 125 ? 0.7035 0.6787 0.1456 0.3158  0.0846  0.1248  134 THR   B C   
1234 O O   . THR   B 125 ? 0.7190 0.6901 0.1473 0.3278  0.0760  0.1090  134 THR   B O   
1235 C CB  . THR   B 125 ? 0.7184 0.7333 0.1485 0.3507  0.0995  0.1615  134 THR   B CB  
1236 O OG1 . THR   B 125 ? 0.7291 0.7545 0.1651 0.3531  0.1114  0.1880  134 THR   B OG1 
1237 C CG2 . THR   B 125 ? 0.7266 0.7412 0.1324 0.3768  0.0911  0.1469  134 THR   B CG2 
1238 N N   . SER   B 126 ? 0.6803 0.6518 0.1358 0.2933  0.0842  0.1235  135 SER   B N   
1239 C CA  . SER   B 126 ? 0.6755 0.6384 0.1280 0.2826  0.0752  0.1053  135 SER   B CA  
1240 C C   . SER   B 126 ? 0.6787 0.6216 0.1255 0.2813  0.0692  0.0866  135 SER   B C   
1241 O O   . SER   B 126 ? 0.6764 0.6045 0.1304 0.2736  0.0723  0.0842  135 SER   B O   
1242 C CB  . SER   B 126 ? 0.6793 0.6377 0.1470 0.2576  0.0761  0.1075  135 SER   B CB  
1243 O OG  . SER   B 126 ? 0.6880 0.6695 0.1608 0.2569  0.0767  0.1181  135 SER   B OG  
1244 N N   . GLY   B 127 ? 0.6814 0.6243 0.1159 0.2889  0.0599  0.0738  136 GLY   B N   
1245 C CA  . GLY   B 127 ? 0.6907 0.6208 0.1219 0.2869  0.0530  0.0572  136 GLY   B CA  
1246 C C   . GLY   B 127 ? 0.6946 0.6284 0.1145 0.3087  0.0468  0.0526  136 GLY   B C   
1247 O O   . GLY   B 127 ? 0.7025 0.6297 0.1228 0.3073  0.0401  0.0399  136 GLY   B O   
1248 N N   . SER   B 128 ? 0.6834 0.6304 0.0932 0.3291  0.0485  0.0630  137 SER   B N   
1249 C CA  . SER   B 128 ? 0.6898 0.6411 0.0846 0.3528  0.0414  0.0583  137 SER   B CA  
1250 C C   . SER   B 128 ? 0.7023 0.6474 0.0839 0.3579  0.0256  0.0426  137 SER   B C   
1251 O O   . SER   B 128 ? 0.7000 0.6455 0.0761 0.3565  0.0225  0.0423  137 SER   B O   
1252 C CB  . SER   B 128 ? 0.6946 0.6642 0.0796 0.3737  0.0492  0.0752  137 SER   B CB  
1253 O OG  . SER   B 128 ? 0.7086 0.6793 0.1055 0.3686  0.0616  0.0909  137 SER   B OG  
1254 N N   . PRO   B 129 ? 0.7129 0.6513 0.0901 0.3639  0.0140  0.0293  138 PRO   B N   
1255 C CA  . PRO   B 129 ? 0.7239 0.6511 0.0896 0.3661  -0.0038 0.0142  138 PRO   B CA  
1256 C C   . PRO   B 129 ? 0.7382 0.6681 0.0797 0.3920  -0.0123 0.0123  138 PRO   B C   
1257 O O   . PRO   B 129 ? 0.7357 0.6808 0.0659 0.4142  -0.0058 0.0211  138 PRO   B O   
1258 C CB  . PRO   B 129 ? 0.7326 0.6566 0.1037 0.3658  -0.0137 0.0026  138 PRO   B CB  
1259 C CG  . PRO   B 129 ? 0.7317 0.6682 0.1055 0.3789  -0.0032 0.0120  138 PRO   B CG  
1260 C CD  . PRO   B 129 ? 0.7052 0.6450 0.0896 0.3675  0.0151  0.0274  138 PRO   B CD  
1261 N N   . ILE   B 130 ? 0.7496 0.6634 0.0816 0.3899  -0.0276 0.0006  139 ILE   B N   
1262 C CA  . ILE   B 130 ? 0.7673 0.6769 0.0735 0.4157  -0.0400 -0.0064 139 ILE   B CA  
1263 C C   . ILE   B 130 ? 0.7956 0.6837 0.0940 0.4162  -0.0631 -0.0251 139 ILE   B C   
1264 O O   . ILE   B 130 ? 0.7924 0.6632 0.1026 0.3923  -0.0718 -0.0315 139 ILE   B O   
1265 C CB  . ILE   B 130 ? 0.7647 0.6711 0.0659 0.4145  -0.0396 -0.0032 139 ILE   B CB  
1266 C CG1 . ILE   B 130 ? 0.7594 0.6924 0.0717 0.4137  -0.0177 0.0164  139 ILE   B CG1 
1267 C CG2 . ILE   B 130 ? 0.7765 0.6735 0.0487 0.4436  -0.0559 -0.0146 139 ILE   B CG2 
1268 C CD1 . ILE   B 130 ? 0.7694 0.7005 0.0916 0.3964  -0.0146 0.0214  139 ILE   B CD1 
1269 N N   . LEU   B 131 ? 0.8174 0.7080 0.0961 0.4428  -0.0730 -0.0329 140 LEU   B N   
1270 C CA  . LEU   B 131 ? 0.8471 0.7205 0.1186 0.4460  -0.0965 -0.0509 140 LEU   B CA  
1271 C C   . LEU   B 131 ? 0.8846 0.7359 0.1266 0.4673  -0.1192 -0.0668 140 LEU   B C   
1272 O O   . LEU   B 131 ? 0.8915 0.7514 0.1096 0.4963  -0.1156 -0.0652 140 LEU   B O   
1273 C CB  . LEU   B 131 ? 0.8427 0.7344 0.1114 0.4628  -0.0945 -0.0503 140 LEU   B CB  
1274 C CG  . LEU   B 131 ? 0.8434 0.7575 0.1330 0.4535  -0.0704 -0.0325 140 LEU   B CG  
1275 C CD1 . LEU   B 131 ? 0.8401 0.7702 0.1203 0.4760  -0.0691 -0.0298 140 LEU   B CD1 
1276 C CD2 . LEU   B 131 ? 0.8450 0.7547 0.1661 0.4189  -0.0660 -0.0319 140 LEU   B CD2 
1277 N N   . ASP   B 132 ? 0.9026 0.7259 0.1463 0.4539  -0.1434 -0.0824 141 ASP   B N   
1278 C CA  . ASP   B 132 ? 0.9342 0.7280 0.1498 0.4727  -0.1710 -0.1013 141 ASP   B CA  
1279 C C   . ASP   B 132 ? 0.9615 0.7598 0.1630 0.4937  -0.1863 -0.1146 141 ASP   B C   
1280 O O   . ASP   B 132 ? 0.9419 0.7655 0.1594 0.4898  -0.1747 -0.1072 141 ASP   B O   
1281 C CB  . ASP   B 132 ? 0.9507 0.7085 0.1760 0.4447  -0.1908 -0.1091 141 ASP   B CB  
1282 C CG  . ASP   B 132 ? 0.9878 0.7398 0.2381 0.4161  -0.2041 -0.1145 141 ASP   B CG  
1283 O OD1 . ASP   B 132 ? 0.9965 0.7695 0.2543 0.4215  -0.2031 -0.1168 141 ASP   B OD1 
1284 O OD2 . ASP   B 132 ? 1.0090 0.7368 0.2716 0.3887  -0.2159 -0.1156 141 ASP   B OD2 
1285 N N   . LYS   B 133 ? 1.0050 0.7770 0.1763 0.5162  -0.2138 -0.1349 142 LYS   B N   
1286 C CA  . LYS   B 133 ? 1.0398 0.8130 0.1916 0.5396  -0.2325 -0.1505 142 LYS   B CA  
1287 C C   . LYS   B 133 ? 1.0393 0.8154 0.2198 0.5141  -0.2448 -0.1552 142 LYS   B C   
1288 O O   . LYS   B 133 ? 1.0396 0.8233 0.2086 0.5317  -0.2585 -0.1659 142 LYS   B O   
1289 C CB  . LYS   B 133 ? 1.1082 0.8462 0.2204 0.5675  -0.2627 -0.1742 142 LYS   B CB  
1290 C CG  . LYS   B 133 ? 1.2048 0.9409 0.2893 0.5948  -0.2526 -0.1715 142 LYS   B CG  
1291 C CD  . LYS   B 133 ? 1.3193 1.0219 0.3587 0.6307  -0.2829 -0.1978 142 LYS   B CD  
1292 C CE  . LYS   B 133 ? 1.3909 1.0865 0.4065 0.6550  -0.2769 -0.1974 142 LYS   B CE  
1293 N NZ  . LYS   B 133 ? 1.4450 1.1059 0.4140 0.6934  -0.3073 -0.2252 142 LYS   B NZ  
1294 N N   . CYS   B 134 ? 1.0275 0.8016 0.2450 0.4742  -0.2392 -0.1466 143 CYS   B N   
1295 C CA  . CYS   B 134 ? 1.0209 0.8074 0.2715 0.4488  -0.2461 -0.1478 143 CYS   B CA  
1296 C C   . CYS   B 134 ? 0.9862 0.8107 0.2649 0.4374  -0.2154 -0.1288 143 CYS   B C   
1297 O O   . CYS   B 134 ? 0.9745 0.8151 0.2826 0.4185  -0.2175 -0.1286 143 CYS   B O   
1298 C CB  . CYS   B 134 ? 1.0542 0.8149 0.3272 0.4123  -0.2634 -0.1520 143 CYS   B CB  
1299 S SG  . CYS   B 134 ? 1.1861 0.8919 0.4278 0.4217  -0.3038 -0.1746 143 CYS   B SG  
1300 N N   . GLY   B 135 ? 0.9688 0.8069 0.2410 0.4470  -0.1883 -0.1133 144 GLY   B N   
1301 C CA  . GLY   B 135 ? 0.9450 0.8111 0.2422 0.4349  -0.1604 -0.0956 144 GLY   B CA  
1302 C C   . GLY   B 135 ? 0.9288 0.7914 0.2551 0.3984  -0.1505 -0.0880 144 GLY   B C   
1303 O O   . GLY   B 135 ? 0.9232 0.8062 0.2730 0.3849  -0.1310 -0.0770 144 GLY   B O   
1304 N N   . ARG   B 136 ? 0.9200 0.7556 0.2434 0.3832  -0.1644 -0.0938 145 ARG   B N   
1305 C CA  . ARG   B 136 ? 0.9089 0.7412 0.2556 0.3497  -0.1550 -0.0852 145 ARG   B CA  
1306 C C   . ARG   B 136 ? 0.8949 0.7317 0.2355 0.3521  -0.1313 -0.0712 145 ARG   B C   
1307 O O   . ARG   B 136 ? 0.9121 0.7420 0.2274 0.3757  -0.1313 -0.0712 145 ARG   B O   
1308 C CB  . ARG   B 136 ? 0.9402 0.7401 0.2852 0.3319  -0.1796 -0.0941 145 ARG   B CB  
1309 C CG  . ARG   B 136 ? 0.9807 0.7836 0.3466 0.3155  -0.1991 -0.1032 145 ARG   B CG  
1310 C CD  . ARG   B 136 ? 1.0521 0.8228 0.4221 0.2907  -0.2219 -0.1076 145 ARG   B CD  
1311 N NE  . ARG   B 136 ? 1.1341 0.8723 0.4792 0.3084  -0.2538 -0.1254 145 ARG   B NE  
1312 C CZ  . ARG   B 136 ? 1.1887 0.8891 0.5030 0.3228  -0.2668 -0.1317 145 ARG   B CZ  
1313 N NH1 . ARG   B 136 ? 1.1819 0.8744 0.4888 0.3200  -0.2509 -0.1203 145 ARG   B NH1 
1314 N NH2 . ARG   B 136 ? 1.2058 0.8761 0.4957 0.3416  -0.2971 -0.1505 145 ARG   B NH2 
1315 N N   . VAL   B 137 ? 0.8540 0.7058 0.2177 0.3297  -0.1110 -0.0596 146 VAL   B N   
1316 C CA  . VAL   B 137 ? 0.8329 0.6897 0.1933 0.3298  -0.0905 -0.0469 146 VAL   B CA  
1317 C C   . VAL   B 137 ? 0.8320 0.6667 0.1847 0.3177  -0.0969 -0.0460 146 VAL   B C   
1318 O O   . VAL   B 137 ? 0.8325 0.6574 0.1975 0.2920  -0.1024 -0.0464 146 VAL   B O   
1319 C CB  . VAL   B 137 ? 0.8170 0.6953 0.1993 0.3160  -0.0675 -0.0363 146 VAL   B CB  
1320 C CG1 . VAL   B 137 ? 0.8157 0.6984 0.1926 0.3197  -0.0497 -0.0241 146 VAL   B CG1 
1321 C CG2 . VAL   B 137 ? 0.8165 0.7135 0.2064 0.3292  -0.0638 -0.0375 146 VAL   B CG2 
1322 N N   . ILE   B 138 ? 0.8287 0.6568 0.1602 0.3375  -0.0968 -0.0442 147 ILE   B N   
1323 C CA  . ILE   B 138 ? 0.8293 0.6359 0.1493 0.3330  -0.1042 -0.0435 147 ILE   B CA  
1324 C C   . ILE   B 138 ? 0.8212 0.6413 0.1464 0.3270  -0.0843 -0.0296 147 ILE   B C   
1325 O O   . ILE   B 138 ? 0.8324 0.6377 0.1491 0.3237  -0.0895 -0.0277 147 ILE   B O   
1326 C CB  . ILE   B 138 ? 0.8421 0.6300 0.1329 0.3629  -0.1231 -0.0546 147 ILE   B CB  
1327 C CG1 . ILE   B 138 ? 0.8405 0.6535 0.1183 0.3947  -0.1102 -0.0505 147 ILE   B CG1 
1328 C CG2 . ILE   B 138 ? 0.8572 0.6245 0.1430 0.3638  -0.1479 -0.0703 147 ILE   B CG2 
1329 C CD1 . ILE   B 138 ? 0.8652 0.6667 0.1125 0.4274  -0.1240 -0.0601 147 ILE   B CD1 
1330 N N   . GLY   B 139 ? 0.8027 0.6486 0.1414 0.3256  -0.0637 -0.0202 148 GLY   B N   
1331 C CA  . GLY   B 139 ? 0.8052 0.6638 0.1511 0.3178  -0.0469 -0.0078 148 GLY   B CA  
1332 C C   . GLY   B 139 ? 0.8019 0.6852 0.1589 0.3228  -0.0276 0.0022  148 GLY   B C   
1333 O O   . GLY   B 139 ? 0.8090 0.7005 0.1647 0.3368  -0.0266 0.0005  148 GLY   B O   
1334 N N   . LEU   B 140 ? 0.7913 0.6847 0.1588 0.3108  -0.0137 0.0130  149 LEU   B N   
1335 C CA  . LEU   B 140 ? 0.7812 0.6932 0.1602 0.3126  0.0032  0.0240  149 LEU   B CA  
1336 C C   . LEU   B 140 ? 0.7723 0.7012 0.1500 0.3221  0.0114  0.0369  149 LEU   B C   
1337 O O   . LEU   B 140 ? 0.7790 0.7068 0.1550 0.3165  0.0084  0.0385  149 LEU   B O   
1338 C CB  . LEU   B 140 ? 0.7777 0.6877 0.1743 0.2878  0.0127  0.0251  149 LEU   B CB  
1339 C CG  . LEU   B 140 ? 0.7932 0.6970 0.1972 0.2788  0.0097  0.0153  149 LEU   B CG  
1340 C CD1 . LEU   B 140 ? 0.7944 0.6996 0.2133 0.2598  0.0217  0.0168  149 LEU   B CD1 
1341 C CD2 . LEU   B 140 ? 0.7991 0.7091 0.2012 0.2978  0.0081  0.0132  149 LEU   B CD2 
1342 N N   . TYR   B 141 ? 0.7526 0.6991 0.1324 0.3359  0.0220  0.0476  150 TYR   B N   
1343 C CA  . TYR   B 141 ? 0.7401 0.7105 0.1227 0.3453  0.0322  0.0634  150 TYR   B CA  
1344 C C   . TYR   B 141 ? 0.7108 0.6866 0.1154 0.3224  0.0446  0.0755  150 TYR   B C   
1345 O O   . TYR   B 141 ? 0.7058 0.6701 0.1192 0.3101  0.0484  0.0737  150 TYR   B O   
1346 C CB  . TYR   B 141 ? 0.7501 0.7369 0.1217 0.3723  0.0370  0.0704  150 TYR   B CB  
1347 C CG  . TYR   B 141 ? 0.7609 0.7768 0.1414 0.3779  0.0526  0.0923  150 TYR   B CG  
1348 C CD1 . TYR   B 141 ? 0.7671 0.7854 0.1649 0.3638  0.0647  0.1062  150 TYR   B CD1 
1349 C CD2 . TYR   B 141 ? 0.7822 0.8238 0.1546 0.3973  0.0549  0.0997  150 TYR   B CD2 
1350 C CE1 . TYR   B 141 ? 0.7761 0.8201 0.1858 0.3638  0.0782  0.1288  150 TYR   B CE1 
1351 C CE2 . TYR   B 141 ? 0.7892 0.8635 0.1733 0.4006  0.0703  0.1225  150 TYR   B CE2 
1352 C CZ  . TYR   B 141 ? 0.7973 0.8723 0.2009 0.3822  0.0818  0.1381  150 TYR   B CZ  
1353 O OH  . TYR   B 141 ? 0.8126 0.9198 0.2297 0.3828  0.0963  0.1631  150 TYR   B OH  
1354 N N   . GLY   B 142 ? 0.6975 0.6915 0.1111 0.3185  0.0499  0.0874  151 GLY   B N   
1355 C CA  . GLY   B 142 ? 0.7022 0.7007 0.1370 0.2964  0.0590  0.0988  151 GLY   B CA  
1356 C C   . GLY   B 142 ? 0.7174 0.7207 0.1613 0.2801  0.0556  0.0996  151 GLY   B C   
1357 O O   . GLY   B 142 ? 0.7131 0.7228 0.1751 0.2624  0.0613  0.1095  151 GLY   B O   
1358 N N   . ASN   B 143 ? 0.7275 0.7255 0.1585 0.2854  0.0446  0.0892  152 ASN   B N   
1359 C CA  . ASN   B 143 ? 0.7324 0.7358 0.1696 0.2726  0.0399  0.0905  152 ASN   B CA  
1360 C C   . ASN   B 143 ? 0.7499 0.7691 0.1762 0.2950  0.0337  0.0913  152 ASN   B C   
1361 O O   . ASN   B 143 ? 0.7620 0.7641 0.1685 0.3090  0.0236  0.0795  152 ASN   B O   
1362 C CB  . ASN   B 143 ? 0.7455 0.7212 0.1766 0.2531  0.0315  0.0769  152 ASN   B CB  
1363 C CG  . ASN   B 143 ? 0.7521 0.7330 0.1893 0.2379  0.0268  0.0792  152 ASN   B CG  
1364 O OD1 . ASN   B 143 ? 0.7380 0.7390 0.1926 0.2297  0.0318  0.0901  152 ASN   B OD1 
1365 N ND2 . ASN   B 143 ? 0.7595 0.7224 0.1825 0.2330  0.0160  0.0698  152 ASN   B ND2 
1366 N N   . GLY   B 144 ? 0.7494 0.8014 0.1898 0.2984  0.0389  0.1052  153 GLY   B N   
1367 C CA  . GLY   B 144 ? 0.7670 0.8415 0.1994 0.3230  0.0346  0.1074  153 GLY   B CA  
1368 C C   . GLY   B 144 ? 0.7734 0.8872 0.2290 0.3180  0.0400  0.1232  153 GLY   B C   
1369 O O   . GLY   B 144 ? 0.7665 0.8798 0.2401 0.2914  0.0399  0.1271  153 GLY   B O   
1370 N N   . VAL   B 145 ? 0.7850 0.9360 0.2411 0.3440  0.0446  0.1324  154 VAL   B N   
1371 C CA  . VAL   B 145 ? 0.7962 0.9929 0.2765 0.3426  0.0492  0.1481  154 VAL   B CA  
1372 C C   . VAL   B 145 ? 0.8178 1.0651 0.3121 0.3590  0.0658  0.1688  154 VAL   B C   
1373 O O   . VAL   B 145 ? 0.8363 1.0835 0.3128 0.3814  0.0717  0.1680  154 VAL   B O   
1374 C CB  . VAL   B 145 ? 0.8062 1.0035 0.2727 0.3609  0.0354  0.1381  154 VAL   B CB  
1375 C CG1 . VAL   B 145 ? 0.8150 1.0166 0.2553 0.4011  0.0337  0.1310  154 VAL   B CG1 
1376 C CG2 . VAL   B 145 ? 0.7929 1.0335 0.2861 0.3548  0.0356  0.1511  154 VAL   B CG2 
1377 N N   . VAL   B 146 ? 0.8126 1.1044 0.3392 0.3468  0.0731  0.1881  155 VAL   B N   
1378 C CA  . VAL   B 146 ? 0.8138 1.1605 0.3577 0.3597  0.0899  0.2116  155 VAL   B CA  
1379 C C   . VAL   B 146 ? 0.8396 1.2308 0.3826 0.3896  0.0884  0.2131  155 VAL   B C   
1380 O O   . VAL   B 146 ? 0.8392 1.2409 0.3959 0.3812  0.0788  0.2108  155 VAL   B O   
1381 C CB  . VAL   B 146 ? 0.7964 1.1658 0.3802 0.3250  0.0987  0.2344  155 VAL   B CB  
1382 C CG1 . VAL   B 146 ? 0.7701 1.2097 0.3798 0.3354  0.1143  0.2622  155 VAL   B CG1 
1383 C CG2 . VAL   B 146 ? 0.8168 1.1468 0.3978 0.3056  0.1034  0.2357  155 VAL   B CG2 
1384 N N   . ILE   B 147 ? 0.8643 1.2810 0.3887 0.4269  0.0967  0.2154  156 ILE   B N   
1385 C CA  . ILE   B 147 ? 0.8781 1.3390 0.3978 0.4624  0.0962  0.2153  156 ILE   B CA  
1386 C C   . ILE   B 147 ? 0.8494 1.3900 0.4055 0.4641  0.1144  0.2451  156 ILE   B C   
1387 O O   . ILE   B 147 ? 0.8352 1.3916 0.4162 0.4388  0.1275  0.2665  156 ILE   B O   
1388 C CB  . ILE   B 147 ? 0.9156 1.3581 0.3908 0.5056  0.0924  0.1974  156 ILE   B CB  
1389 C CG1 . ILE   B 147 ? 0.9348 1.3806 0.3986 0.5129  0.1072  0.2067  156 ILE   B CG1 
1390 C CG2 . ILE   B 147 ? 0.9576 1.3293 0.4026 0.5044  0.0700  0.1683  156 ILE   B CG2 
1391 C CD1 . ILE   B 147 ? 0.9632 1.4229 0.3906 0.5624  0.1090  0.1976  156 ILE   B CD1 
1392 N N   . LYS   B 148 ? 0.8362 1.4275 0.3966 0.4937  0.1148  0.2474  157 LYS   B N   
1393 C CA  . LYS   B 148 ? 0.8077 1.4842 0.4054 0.4980  0.1320  0.2761  157 LYS   B CA  
1394 C C   . LYS   B 148 ? 0.7950 1.5072 0.3957 0.5045  0.1553  0.2996  157 LYS   B C   
1395 O O   . LYS   B 148 ? 0.7615 1.5344 0.4017 0.4889  0.1710  0.3299  157 LYS   B O   
1396 C CB  . LYS   B 148 ? 0.8311 1.5532 0.4243 0.5386  0.1282  0.2702  157 LYS   B CB  
1397 C CG  . LYS   B 148 ? 0.8977 1.6194 0.5137 0.5207  0.1110  0.2644  157 LYS   B CG  
1398 C CD  . LYS   B 148 ? 0.9620 1.7195 0.5700 0.5632  0.1035  0.2553  157 LYS   B CD  
1399 C CE  . LYS   B 148 ? 0.9955 1.8361 0.6110 0.6026  0.1239  0.2723  157 LYS   B CE  
1400 N NZ  . LYS   B 148 ? 0.9811 1.9073 0.6550 0.5809  0.1396  0.3055  157 LYS   B NZ  
1401 N N   . ASN   B 149 ? 0.8212 1.4934 0.3813 0.5237  0.1563  0.2870  158 ASN   B N   
1402 C CA  . ASN   B 149 ? 0.8205 1.5139 0.3744 0.5312  0.1759  0.3065  158 ASN   B CA  
1403 C C   . ASN   B 149 ? 0.8145 1.4935 0.3985 0.4835  0.1835  0.3284  158 ASN   B C   
1404 O O   . ASN   B 149 ? 0.8113 1.5169 0.3996 0.4837  0.2015  0.3528  158 ASN   B O   
1405 C CB  . ASN   B 149 ? 0.8751 1.5149 0.3760 0.5595  0.1683  0.2814  158 ASN   B CB  
1406 C CG  . ASN   B 149 ? 0.9290 1.5970 0.3951 0.6147  0.1698  0.2699  158 ASN   B CG  
1407 O OD1 . ASN   B 149 ? 0.9341 1.6619 0.4134 0.6365  0.1759  0.2779  158 ASN   B OD1 
1408 N ND2 . ASN   B 149 ? 0.9589 1.5857 0.3797 0.6398  0.1634  0.2503  158 ASN   B ND2 
1409 N N   . GLY   B 150 ? 0.8100 1.4427 0.4100 0.4454  0.1689  0.3185  159 GLY   B N   
1410 C CA  . GLY   B 150 ? 0.8007 1.4045 0.4229 0.4021  0.1710  0.3317  159 GLY   B CA  
1411 C C   . GLY   B 150 ? 0.8203 1.3518 0.4079 0.4008  0.1637  0.3117  159 GLY   B C   
1412 O O   . GLY   B 150 ? 0.8296 1.3180 0.4280 0.3668  0.1584  0.3106  159 GLY   B O   
1413 N N   . SER   B 151 ? 0.8234 1.3419 0.3691 0.4394  0.1622  0.2948  160 SER   B N   
1414 C CA  A SER   B 151 ? 0.8520 1.3085 0.3654 0.4418  0.1544  0.2755  160 SER   B CA  
1415 C CA  B SER   B 151 ? 0.8519 1.3086 0.3647 0.4426  0.1543  0.2751  160 SER   B CA  
1416 C C   . SER   B 151 ? 0.8670 1.2637 0.3697 0.4273  0.1331  0.2453  160 SER   B C   
1417 O O   . SER   B 151 ? 0.8607 1.2629 0.3728 0.4234  0.1234  0.2370  160 SER   B O   
1418 C CB  A SER   B 151 ? 0.8763 1.3417 0.3499 0.4866  0.1583  0.2682  160 SER   B CB  
1419 C CB  B SER   B 151 ? 0.8755 1.3416 0.3482 0.4883  0.1577  0.2670  160 SER   B CB  
1420 O OG  A SER   B 151 ? 0.9249 1.3410 0.3740 0.4861  0.1537  0.2569  160 SER   B OG  
1421 O OG  B SER   B 151 ? 0.8980 1.3821 0.3544 0.5201  0.1501  0.2514  160 SER   B OG  
1422 N N   . TYR   B 152 ? 0.8692 1.2115 0.3533 0.4192  0.1263  0.2306  161 TYR   B N   
1423 C CA  . TYR   B 152 ? 0.8758 1.1626 0.3493 0.4040  0.1087  0.2047  161 TYR   B CA  
1424 C C   . TYR   B 152 ? 0.8672 1.1258 0.3026 0.4332  0.0955  0.1791  161 TYR   B C   
1425 O O   . TYR   B 152 ? 0.8711 1.1318 0.2830 0.4595  0.0987  0.1770  161 TYR   B O   
1426 C CB  . TYR   B 152 ? 0.8911 1.1388 0.3714 0.3759  0.1095  0.2051  161 TYR   B CB  
1427 C CG  . TYR   B 152 ? 0.9170 1.1218 0.4014 0.3487  0.0960  0.1870  161 TYR   B CG  
1428 C CD1 . TYR   B 152 ? 0.9151 1.1290 0.4234 0.3251  0.0925  0.1910  161 TYR   B CD1 
1429 C CD2 . TYR   B 152 ? 0.9511 1.1095 0.4158 0.3467  0.0868  0.1668  161 TYR   B CD2 
1430 C CE1 . TYR   B 152 ? 0.9389 1.1155 0.4471 0.3021  0.0806  0.1747  161 TYR   B CE1 
1431 C CE2 . TYR   B 152 ? 0.9707 1.0947 0.4380 0.3229  0.0763  0.1518  161 TYR   B CE2 
1432 C CZ  . TYR   B 152 ? 0.9741 1.1066 0.4615 0.3011  0.0737  0.1558  161 TYR   B CZ  
1433 O OH  . TYR   B 152 ? 1.0120 1.1123 0.4991 0.2786  0.0641  0.1416  161 TYR   B OH  
1434 N N   . VAL   B 153 ? 0.8510 1.0802 0.2796 0.4273  0.0793  0.1597  162 VAL   B N   
1435 C CA  . VAL   B 153 ? 0.8527 1.0462 0.2478 0.4482  0.0635  0.1352  162 VAL   B CA  
1436 C C   . VAL   B 153 ? 0.8366 0.9811 0.2331 0.4187  0.0514  0.1207  162 VAL   B C   
1437 O O   . VAL   B 153 ? 0.8351 0.9745 0.2430 0.4014  0.0452  0.1190  162 VAL   B O   
1438 C CB  . VAL   B 153 ? 0.8633 1.0723 0.2438 0.4778  0.0547  0.1272  162 VAL   B CB  
1439 C CG1 . VAL   B 153 ? 0.8950 1.0540 0.2433 0.4911  0.0337  0.1007  162 VAL   B CG1 
1440 C CG2 . VAL   B 153 ? 0.8545 1.1151 0.2290 0.5128  0.0679  0.1397  162 VAL   B CG2 
1441 N N   . SER   B 154 ? 0.8274 0.9403 0.2139 0.4123  0.0490  0.1119  163 SER   B N   
1442 C CA  . SER   B 154 ? 0.8243 0.8956 0.2124 0.3856  0.0396  0.0988  163 SER   B CA  
1443 C C   . SER   B 154 ? 0.8318 0.8696 0.1957 0.3957  0.0208  0.0780  163 SER   B C   
1444 O O   . SER   B 154 ? 0.8423 0.8806 0.1845 0.4249  0.0141  0.0704  163 SER   B O   
1445 C CB  . SER   B 154 ? 0.8317 0.8891 0.2232 0.3754  0.0462  0.0999  163 SER   B CB  
1446 O OG  . SER   B 154 ? 0.8620 0.8818 0.2434 0.3660  0.0347  0.0822  163 SER   B OG  
1447 N N   . ALA   B 155 ? 0.8264 0.8340 0.1928 0.3715  0.0118  0.0689  164 ALA   B N   
1448 C CA  . ALA   B 155 ? 0.8361 0.8083 0.1822 0.3753  -0.0067 0.0519  164 ALA   B CA  
1449 C C   . ALA   B 155 ? 0.8376 0.7841 0.1768 0.3700  -0.0116 0.0408  164 ALA   B C   
1450 O O   . ALA   B 155 ? 0.8358 0.7900 0.1873 0.3603  -0.0003 0.0460  164 ALA   B O   
1451 C CB  . ALA   B 155 ? 0.8423 0.7990 0.1945 0.3514  -0.0132 0.0508  164 ALA   B CB  
1452 N N   . ILE   B 156 ? 0.8358 0.7517 0.1563 0.3765  -0.0296 0.0258  165 ILE   B N   
1453 C CA  . ILE   B 156 ? 0.8299 0.7242 0.1481 0.3681  -0.0362 0.0155  165 ILE   B CA  
1454 C C   . ILE   B 156 ? 0.8226 0.6967 0.1510 0.3359  -0.0399 0.0138  165 ILE   B C   
1455 O O   . ILE   B 156 ? 0.8292 0.6778 0.1465 0.3320  -0.0553 0.0072  165 ILE   B O   
1456 C CB  . ILE   B 156 ? 0.8426 0.7162 0.1364 0.3920  -0.0551 0.0005  165 ILE   B CB  
1457 C CG1 . ILE   B 156 ? 0.8396 0.7375 0.1189 0.4278  -0.0502 0.0024  165 ILE   B CG1 
1458 C CG2 . ILE   B 156 ? 0.8509 0.7053 0.1472 0.3796  -0.0638 -0.0097 165 ILE   B CG2 
1459 C CD1 . ILE   B 156 ? 0.8592 0.7356 0.1108 0.4540  -0.0702 -0.0138 165 ILE   B CD1 
1460 N N   . THR   B 157 ? 0.8070 0.6921 0.1549 0.3139  -0.0256 0.0206  166 THR   B N   
1461 C CA  . THR   B 157 ? 0.8065 0.6794 0.1635 0.2843  -0.0252 0.0203  166 THR   B CA  
1462 C C   . THR   B 157 ? 0.8099 0.6668 0.1692 0.2709  -0.0314 0.0114  166 THR   B C   
1463 O O   . THR   B 157 ? 0.8061 0.6724 0.1751 0.2708  -0.0239 0.0100  166 THR   B O   
1464 C CB  . THR   B 157 ? 0.7991 0.6899 0.1738 0.2688  -0.0084 0.0292  166 THR   B CB  
1465 O OG1 . THR   B 157 ? 0.8015 0.7142 0.1802 0.2806  -0.0010 0.0396  166 THR   B OG1 
1466 C CG2 . THR   B 157 ? 0.8023 0.6839 0.1804 0.2438  -0.0086 0.0291  166 THR   B CG2 
1467 N N   . GLN   B 158 ? 0.8117 0.6461 0.1638 0.2587  -0.0446 0.0070  167 GLN   B N   
1468 C CA  . GLN   B 158 ? 0.8129 0.6363 0.1705 0.2437  -0.0510 0.0007  167 GLN   B CA  
1469 C C   . GLN   B 158 ? 0.8446 0.6597 0.2061 0.2155  -0.0505 0.0047  167 GLN   B C   
1470 O O   . GLN   B 158 ? 0.8540 0.6563 0.2047 0.2112  -0.0564 0.0092  167 GLN   B O   
1471 C CB  . GLN   B 158 ? 0.8032 0.6059 0.1475 0.2581  -0.0713 -0.0088 167 GLN   B CB  
1472 C CG  . GLN   B 158 ? 0.7942 0.5852 0.1463 0.2412  -0.0822 -0.0148 167 GLN   B CG  
1473 C CD  . GLN   B 158 ? 0.7936 0.6066 0.1631 0.2400  -0.0732 -0.0180 167 GLN   B CD  
1474 O OE1 . GLN   B 158 ? 0.7940 0.6280 0.1772 0.2321  -0.0550 -0.0129 167 GLN   B OE1 
1475 N NE2 . GLN   B 158 ? 0.7803 0.5873 0.1492 0.2476  -0.0874 -0.0272 167 GLN   B NE2 
1476 N N   . GLY   B 159 ? 0.8564 0.6811 0.2322 0.1981  -0.0430 0.0036  168 GLY   B N   
1477 C CA  . GLY   B 159 ? 0.8836 0.7062 0.2624 0.1726  -0.0400 0.0081  168 GLY   B CA  
1478 C C   . GLY   B 159 ? 0.9220 0.7277 0.3001 0.1585  -0.0548 0.0077  168 GLY   B C   
1479 O O   . GLY   B 159 ? 0.9234 0.7154 0.2988 0.1683  -0.0701 0.0017  168 GLY   B O   
1480 N N   . LYS   B 160 ? 0.9525 0.7592 0.3324 0.1345  -0.0509 0.0146  169 LYS   B N   
1481 C CA  . LYS   B 160 ? 0.9890 0.7818 0.3709 0.1153  -0.0633 0.0185  169 LYS   B CA  
1482 C C   . LYS   B 160 ? 1.0086 0.8271 0.4136 0.1010  -0.0555 0.0170  169 LYS   B C   
1483 O O   . LYS   B 160 ? 1.0020 0.8480 0.4170 0.0977  -0.0366 0.0166  169 LYS   B O   
1484 C CB  . LYS   B 160 ? 1.0146 0.7946 0.3832 0.0975  -0.0643 0.0302  169 LYS   B CB  
1485 C CG  . LYS   B 160 ? 1.0751 0.8311 0.4417 0.0788  -0.0814 0.0374  169 LYS   B CG  
1486 C CD  . LYS   B 160 ? 1.1442 0.8884 0.4964 0.0598  -0.0813 0.0520  169 LYS   B CD  
1487 C CE  . LYS   B 160 ? 1.2012 0.9167 0.5514 0.0406  -0.1002 0.0616  169 LYS   B CE  
1488 N NZ  . LYS   B 160 ? 1.2365 0.9461 0.5744 0.0187  -0.0971 0.0791  169 LYS   B NZ  
1489 N N   . ARG   B 161 ? 1.0272 0.8370 0.4414 0.0933  -0.0712 0.0154  170 ARG   B N   
1490 C CA  . ARG   B 161 ? 1.0284 0.8656 0.4679 0.0774  -0.0664 0.0157  170 ARG   B CA  
1491 C C   . ARG   B 161 ? 1.0461 0.8787 0.4885 0.0467  -0.0703 0.0296  170 ARG   B C   
1492 O O   . ARG   B 161 ? 1.0673 0.8641 0.4948 0.0403  -0.0880 0.0354  170 ARG   B O   
1493 C CB  . ARG   B 161 ? 1.0431 0.8769 0.4934 0.0875  -0.0829 0.0054  170 ARG   B CB  
1494 C CG  . ARG   B 161 ? 1.0721 0.9416 0.5525 0.0752  -0.0776 0.0044  170 ARG   B CG  
1495 C CD  . ARG   B 161 ? 1.1321 0.9953 0.6228 0.0815  -0.0992 -0.0052 170 ARG   B CD  
1496 N NE  . ARG   B 161 ? 1.1680 1.0674 0.6913 0.0642  -0.0969 -0.0037 170 ARG   B NE  
1497 C CZ  . ARG   B 161 ? 1.1957 1.1295 0.7376 0.0768  -0.0881 -0.0113 170 ARG   B CZ  
1498 N NH1 . ARG   B 161 ? 1.1958 1.1285 0.7254 0.1057  -0.0816 -0.0202 170 ARG   B NH1 
1499 N NH2 . ARG   B 161 ? 1.1798 1.1507 0.7535 0.0607  -0.0860 -0.0089 170 ARG   B NH2 
1500 N N   . GLU   B 162 ? 1.0332 0.9016 0.4930 0.0290  -0.0534 0.0360  171 GLU   B N   
1501 C CA  . GLU   B 162 ? 1.0428 0.9133 0.5055 -0.0007 -0.0538 0.0523  171 GLU   B CA  
1502 C C   . GLU   B 162 ? 1.0230 0.9241 0.5179 -0.0207 -0.0549 0.0566  171 GLU   B C   
1503 O O   . GLU   B 162 ? 1.0166 0.9251 0.5185 -0.0480 -0.0544 0.0726  171 GLU   B O   
1504 C CB  . GLU   B 162 ? 1.0808 0.9679 0.5304 -0.0065 -0.0324 0.0601  171 GLU   B CB  
1505 C CG  . GLU   B 162 ? 1.1885 1.0412 0.6072 0.0030  -0.0376 0.0622  171 GLU   B CG  
1506 C CD  . GLU   B 162 ? 1.3056 1.1490 0.7075 -0.0178 -0.0364 0.0796  171 GLU   B CD  
1507 O OE1 . GLU   B 162 ? 1.3424 1.1501 0.7209 -0.0134 -0.0489 0.0841  171 GLU   B OE1 
1508 O OE2 . GLU   B 162 ? 1.3239 1.1977 0.7353 -0.0372 -0.0227 0.0895  171 GLU   B OE2 
1509 S S   . DMS   C .   ? 1.3340 1.0990 0.7265 0.1253  0.0556  -0.0760 201 DMS   B S   
1510 O O   . DMS   C .   ? 1.3254 1.1133 0.7181 0.1376  0.0670  -0.0762 201 DMS   B O   
1511 C C1  . DMS   C .   ? 1.3494 1.0818 0.7272 0.1324  0.0529  -0.0999 201 DMS   B C1  
1512 C C2  . DMS   C .   ? 1.3295 1.0793 0.7471 0.1275  0.0530  -0.0585 201 DMS   B C2  
1513 N N1  . A1BGS D .   ? 1.0651 1.0525 0.6008 0.1413  0.0490  0.1159  202 A1BGS B N1  
1514 N N3  . A1BGS D .   ? 1.0724 1.0522 0.5492 0.1523  0.0208  0.0809  202 A1BGS B N3  
1515 C C4  . A1BGS D .   ? 1.0717 1.1311 0.5976 0.2217  0.0777  0.1567  202 A1BGS B C4  
1516 C C5  . A1BGS D .   ? 1.0784 1.0974 0.5918 0.2116  0.0715  0.1361  202 A1BGS B C5  
1517 C C6  . A1BGS D .   ? 1.0675 1.0751 0.5908 0.1858  0.0646  0.1298  202 A1BGS B C6  
1518 C C7  . A1BGS D .   ? 1.0586 1.0642 0.6027 0.1659  0.0661  0.1402  202 A1BGS B C7  
1519 C C8  . A1BGS D .   ? 1.0601 1.0546 0.6103 0.1438  0.0574  0.1320  202 A1BGS B C8  
1520 C C10 . A1BGS D .   ? 1.0759 1.0443 0.5558 0.1688  0.0373  0.0834  202 A1BGS B C10 
1521 C C13 . A1BGS D .   ? 1.0684 1.0395 0.5721 0.1338  0.0315  0.0874  202 A1BGS B C13 
1522 C C15 . A1BGS D .   ? 1.0624 1.1761 0.5988 0.2471  0.0952  0.1908  202 A1BGS B C15 
1523 C C17 . A1BGS D .   ? 1.0782 1.2155 0.5674 0.3177  0.1108  0.2007  202 A1BGS B C17 
1524 C C1  . A1BGS D .   ? 1.0273 1.2365 0.6166 0.2270  0.0859  0.2112  202 A1BGS B C1  
1525 O O1  . A1BGS D .   ? 1.0496 1.2073 0.6168 0.2208  0.0770  0.1876  202 A1BGS B O1  
1526 C C2  . A1BGS D .   ? 1.0564 1.1852 0.6095 0.2256  0.0815  0.1829  202 A1BGS B C2  
1527 C C3  . A1BGS D .   ? 1.0665 1.1523 0.6052 0.2154  0.0739  0.1624  202 A1BGS B C3  
1528 C C9  . A1BGS D .   ? 1.0670 1.0560 0.5836 0.1594  0.0483  0.1081  202 A1BGS B C9  
1529 N N2  . A1BGS D .   ? 1.0696 1.0475 0.5709 0.1546  0.0397  0.0937  202 A1BGS B N2  
1530 C C11 . A1BGS D .   ? 1.0759 1.0520 0.5462 0.1709  0.0274  0.0811  202 A1BGS B C11 
1531 C C12 . A1BGS D .   ? 1.0760 1.0390 0.5588 0.1338  0.0233  0.0754  202 A1BGS B C12 
1532 C C14 . A1BGS D .   ? 1.0698 1.0676 0.5804 0.1816  0.0553  0.1139  202 A1BGS B C14 
1533 N N4  . A1BGS D .   ? 1.0732 1.1456 0.5977 0.2380  0.0875  0.1703  202 A1BGS B N4  
1534 N N5  . A1BGS D .   ? 1.0611 1.1899 0.5927 0.2650  0.1058  0.2056  202 A1BGS B N5  
1535 C C16 . A1BGS D .   ? 1.0799 1.1867 0.5867 0.2845  0.1057  0.1950  202 A1BGS B C16 
1536 N N6  . A1BGS D .   ? 1.0596 1.2416 0.5645 0.3220  0.1244  0.2292  202 A1BGS B N6  
1537 C C18 . A1BGS D .   ? 1.0454 1.2285 0.5819 0.2905  0.1290  0.2476  202 A1BGS B C18 
1538 C C19 . A1BGS D .   ? 1.0410 1.2116 0.5926 0.2656  0.1180  0.2346  202 A1BGS B C19 
1539 N N7  . A1BGS D .   ? 1.0511 1.1952 0.6021 0.2423  0.0928  0.1970  202 A1BGS B N7  
1540 S S   . DMS   E .   ? 1.5394 1.3195 0.8263 0.2674  -0.0957 0.0371  203 DMS   B S   
1541 O O   . DMS   E .   ? 1.5489 1.3145 0.8218 0.2973  -0.1085 0.0291  203 DMS   B O   
1542 C C1  . DMS   E .   ? 1.5212 1.3303 0.8296 0.2603  -0.0751 0.0350  203 DMS   B C1  
1543 C C2  . DMS   E .   ? 1.5236 1.3407 0.8206 0.2747  -0.0884 0.0461  203 DMS   B C2  
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