data_7HP1
# 
_entry.id   7HP1 
# 
_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   7HP1         pdb_00007hp1 10.2210/pdb7hp1/pdb 
WWPDB D_1001407751 ?            ?                   
# 
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                        7HP1 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-07 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Ni, X.'              1  
'Marples, P.G.'       2  
'Godoy, A.S.'         3  
'Koekemoer, L.'       4  
'Aschenbrenner, J.C.' 5  
'Balcomb, B.H.'       6  
'Fairhead, M.'        7  
'Lithgo, R.M.'        8  
'Lee, A.'             9  
'Kenton, N.'          10 
'Thompson, W.'        11 
'Tomlinson, C.W.E.'   12 
'Wild, C.'            13 
'Winokan, M.'         14 
'Williams, E.P.'      15 
'Chandran, A.V.'      16 
'Walsh, M.A.'         17 
'Fearon, D.'          18 
'von Delft, F.'       19 
# 
_citation.id                        primary 
_citation.title                     'PanDDA analysis group deposition' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B'                                     5067.486  1  ?                           ?    
? ? 
2 polymer     man 'Serine protease NS3'                                              18117.629 1  3.4.21.91,3.6.1.15,3.6.4.13 None 
? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                               78.133    3  ?                           ?    
? ? 
4 non-polymer syn 'N-(1-methyl-1H-pyrazol-4-yl)-2-(2-methylpyrimidin-5-yl)benzamide' 293.323   1  ?                           ?    
? ? 
5 non-polymer syn 'SULFATE ION'                                                      96.063    1  ?                           ?    
? ? 
6 non-polymer syn 'CHLORIDE ION'                                                     35.453    1  ?                           ?    
? ? 
7 water       nat water                                                              18.015    98 ?                           ?    
? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                               DMS   
4 'N-(1-methyl-1H-pyrazol-4-yl)-2-(2-methylpyrimidin-5-yl)benzamide' A1BG8 
5 'SULFATE ION'                                                      SO4   
6 'CHLORIDE ION'                                                     CL    
7 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 
A1BG8 non-polymer         . 'N-(1-methyl-1H-pyrazol-4-yl)-2-(2-methylpyrimidin-5-yl)benzamide' ? 'C16 H15 N5 O'   293.323 
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 
CL    non-polymer         . 'CHLORIDE ION'                                                     ? 'Cl -1'          35.453  
CYS   'L-peptide linking' y CYSTEINE                                                           ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                               ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                          ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                    ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                            ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                          ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                              ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                         ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                            ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                             ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                         ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                      ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                            ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                             ? 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                                                      ? 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                                          ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                         ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                           ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                             ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BG8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BG8 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS   1  201 201 DMS   DMS B . 
D 3 DMS   1  202 202 DMS   DMS B . 
E 3 DMS   1  203 203 DMS   DMS B . 
F 4 A1BG8 1  204 301 A1BG8 LIG B . 
G 5 SO4   1  205 302 SO4   SO4 B . 
H 6 CL    1  206 1   CL    CL  B . 
I 7 HOH   1  101 105 HOH   HOH A . 
I 7 HOH   2  102 48  HOH   HOH A . 
I 7 HOH   3  103 98  HOH   HOH A . 
I 7 HOH   4  104 118 HOH   HOH A . 
I 7 HOH   5  105 117 HOH   HOH A . 
I 7 HOH   6  106 65  HOH   HOH A . 
I 7 HOH   7  107 34  HOH   HOH A . 
I 7 HOH   8  108 77  HOH   HOH A . 
I 7 HOH   9  109 110 HOH   HOH A . 
I 7 HOH   10 110 16  HOH   HOH A . 
I 7 HOH   11 111 28  HOH   HOH A . 
I 7 HOH   12 112 54  HOH   HOH A . 
I 7 HOH   13 113 49  HOH   HOH A . 
I 7 HOH   14 114 70  HOH   HOH A . 
I 7 HOH   15 115 120 HOH   HOH A . 
I 7 HOH   16 116 121 HOH   HOH A . 
I 7 HOH   17 117 50  HOH   HOH A . 
I 7 HOH   18 118 119 HOH   HOH A . 
I 7 HOH   19 119 29  HOH   HOH A . 
I 7 HOH   20 120 27  HOH   HOH A . 
I 7 HOH   21 121 87  HOH   HOH A . 
I 7 HOH   22 122 127 HOH   HOH A . 
J 7 HOH   1  301 51  HOH   HOH B . 
J 7 HOH   2  302 90  HOH   HOH B . 
J 7 HOH   3  303 11  HOH   HOH B . 
J 7 HOH   4  304 40  HOH   HOH B . 
J 7 HOH   5  305 57  HOH   HOH B . 
J 7 HOH   6  306 92  HOH   HOH B . 
J 7 HOH   7  307 5   HOH   HOH B . 
J 7 HOH   8  308 122 HOH   HOH B . 
J 7 HOH   9  309 4   HOH   HOH B . 
J 7 HOH   10 310 14  HOH   HOH B . 
J 7 HOH   11 311 58  HOH   HOH B . 
J 7 HOH   12 312 123 HOH   HOH B . 
J 7 HOH   13 313 9   HOH   HOH B . 
J 7 HOH   14 314 89  HOH   HOH B . 
J 7 HOH   15 315 81  HOH   HOH B . 
J 7 HOH   16 316 42  HOH   HOH B . 
J 7 HOH   17 317 23  HOH   HOH B . 
J 7 HOH   18 318 69  HOH   HOH B . 
J 7 HOH   19 319 63  HOH   HOH B . 
J 7 HOH   20 320 131 HOH   HOH B . 
J 7 HOH   21 321 31  HOH   HOH B . 
J 7 HOH   22 322 67  HOH   HOH B . 
J 7 HOH   23 323 1   HOH   HOH B . 
J 7 HOH   24 324 100 HOH   HOH B . 
J 7 HOH   25 325 130 HOH   HOH B . 
J 7 HOH   26 326 20  HOH   HOH B . 
J 7 HOH   27 327 35  HOH   HOH B . 
J 7 HOH   28 328 106 HOH   HOH B . 
J 7 HOH   29 329 66  HOH   HOH B . 
J 7 HOH   30 330 108 HOH   HOH B . 
J 7 HOH   31 331 30  HOH   HOH B . 
J 7 HOH   32 332 24  HOH   HOH B . 
J 7 HOH   33 333 46  HOH   HOH B . 
J 7 HOH   34 334 115 HOH   HOH B . 
J 7 HOH   35 335 36  HOH   HOH B . 
J 7 HOH   36 336 60  HOH   HOH B . 
J 7 HOH   37 337 39  HOH   HOH B . 
J 7 HOH   38 338 21  HOH   HOH B . 
J 7 HOH   39 339 2   HOH   HOH B . 
J 7 HOH   40 340 32  HOH   HOH B . 
J 7 HOH   41 341 107 HOH   HOH B . 
J 7 HOH   42 342 116 HOH   HOH B . 
J 7 HOH   43 343 62  HOH   HOH B . 
J 7 HOH   44 344 17  HOH   HOH B . 
J 7 HOH   45 345 68  HOH   HOH B . 
J 7 HOH   46 346 10  HOH   HOH B . 
J 7 HOH   47 347 82  HOH   HOH B . 
J 7 HOH   48 348 12  HOH   HOH B . 
J 7 HOH   49 349 13  HOH   HOH B . 
J 7 HOH   50 350 129 HOH   HOH B . 
J 7 HOH   51 351 56  HOH   HOH B . 
J 7 HOH   52 352 3   HOH   HOH B . 
J 7 HOH   53 353 103 HOH   HOH B . 
J 7 HOH   54 354 72  HOH   HOH B . 
J 7 HOH   55 355 128 HOH   HOH B . 
J 7 HOH   56 356 102 HOH   HOH B . 
J 7 HOH   57 357 18  HOH   HOH B . 
J 7 HOH   58 358 43  HOH   HOH B . 
J 7 HOH   59 359 73  HOH   HOH B . 
J 7 HOH   60 360 94  HOH   HOH B . 
J 7 HOH   61 361 112 HOH   HOH B . 
J 7 HOH   62 362 125 HOH   HOH B . 
J 7 HOH   63 363 64  HOH   HOH B . 
J 7 HOH   64 364 26  HOH   HOH B . 
J 7 HOH   65 365 80  HOH   HOH B . 
J 7 HOH   66 366 75  HOH   HOH B . 
J 7 HOH   67 367 79  HOH   HOH B . 
J 7 HOH   68 368 132 HOH   HOH B . 
J 7 HOH   69 369 61  HOH   HOH B . 
J 7 HOH   70 370 124 HOH   HOH B . 
J 7 HOH   71 371 45  HOH   HOH B . 
J 7 HOH   72 372 59  HOH   HOH B . 
J 7 HOH   73 373 83  HOH   HOH B . 
J 7 HOH   74 374 44  HOH   HOH B . 
J 7 HOH   75 375 85  HOH   HOH B . 
J 7 HOH   76 376 109 HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0267 ? 1 
refinement       BUSTER  .        ? 2 
'data scaling'   Aimless .        ? 3 
phasing          PHASER  .        ? 4 
'data reduction' XDS     .        ? 5 
'data reduction' XDS     .        ? 6 
'data reduction' XDS     .        ? 7 
'data reduction' XDS     .        ? 8 
'data reduction' XDS     .        ? 9 
# 
_cell.entry_id           7HP1 
_cell.length_a           42.320 
_cell.length_b           42.320 
_cell.length_c           215.300 
_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                         7HP1 
_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          7HP1 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.08 
_exptl_crystal.density_percent_sol   40.83 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-09-29 
_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                     7HP1 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             42.32 
_reflns.d_resolution_high            1.84 
_reflns.number_obs                   18135 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.190 
_reflns.pdbx_netI_over_sigmaI        10.4 
_reflns.pdbx_redundancy              19.2 
_reflns.pdbx_Rrim_I_all              0.195 
_reflns.pdbx_Rpim_I_all              0.043 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     347957 
_reflns.pdbx_chi_squared             1.00 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.84 
_reflns_shell.d_res_low                   1.89 
_reflns_shell.number_measured_all         23139 
_reflns_shell.number_unique_obs           1274 
_reflns_shell.Rmerge_I_obs                4.605 
_reflns_shell.pdbx_chi_squared            0.90 
_reflns_shell.pdbx_redundancy             18.2 
_reflns_shell.percent_possible_obs        99.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.7 
_reflns_shell.pdbx_Rrim_I_all             4.736 
_reflns_shell.pdbx_Rpim_I_all             1.097 
_reflns_shell.pdbx_CC_half                0.334 
_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                                 7HP1 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     17161 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             42.36 
_refine.ls_d_res_high                            1.84 
_refine.ls_percent_reflns_obs                    99.92 
_refine.ls_R_factor_obs                          0.22434 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.22201 
_refine.ls_R_factor_R_free                       0.26882 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_number_reflns_R_free                  892 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.946 
_refine.B_iso_mean                               47.359 
_refine.aniso_B[1][1]                            0.40 
_refine.aniso_B[2][2]                            0.40 
_refine.aniso_B[3][3]                            -0.81 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            -0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.186 
_refine.pdbx_overall_ESU_R_Free                  0.168 
_refine.overall_SU_ML                            0.195 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             14.739 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.number_atoms_solvent             98 
_refine_hist.number_atoms_total               1614 
_refine_hist.d_res_high                       1.84 
_refine_hist.d_res_low                        42.36 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.013  0.013  ? 2042 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.002  0.015  ? 1671 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.778  1.642  ? 2503 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.318  1.588  ? 3855 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.600  5.000  ? 238  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       30.763 22.410 ? 83   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       15.458 15.000 ? 283  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       15.922 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.073  0.200  ? 219  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 2157 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 425  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  1.791  2.675  ? 1001 'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.828  2.523  ? 958  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 3.164  3.742  ? 1152 'X-RAY DIFFRACTION' ? 
r_mcangle_other              3.163  3.747  ? 1153 'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.066  3.070  ? 1041 'X-RAY DIFFRACTION' ? 
r_scbond_other               2.054  3.002  ? 1027 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              3.581  4.206  ? 1340 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       12.722 29.236 ? 2055 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         12.725 28.893 ? 2039 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.840 
_refine_ls_shell.d_res_low                        1.888 
_refine_ls_shell.number_reflns_R_work             1196 
_refine_ls_shell.R_factor_R_work                  0.413 
_refine_ls_shell.percent_reflns_obs               99.69 
_refine_ls_shell.R_factor_R_free                  0.451 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             76 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HP1 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0014738-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HP1 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, XChemExplorer, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 7 ? 
J N N 7 ? 
# 
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 7HP1 A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HP1 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 7HP1 SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HP1 MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HP1 MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HP1 LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            134 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            134 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             143 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             143 
_struct_conn.ptnr2_symmetry                8_444 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.474 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       134 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      134 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        143 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       143 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          8_444 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA2 5 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 4 5 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O LYS B 98  ? O LYS B 107 N ALA B 90  ? N ALA B 99  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N VAL A 33  ? N VAL A 76  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                   7HP1 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD2 B ASP 90 ? ? OG B SER 93  ? ? 1.87 
2 1 OE1 B GLU 17 ? ? O  B HOH 301 ? ? 2.17 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 C A THR 60 ? A O A THR 60 ? A 1.367 1.229 0.138 0.019 N 
2 1 C A THR 60 ? B O A THR 60 ? B 1.344 1.229 0.115 0.019 N 
3 1 C A THR 60 ? C O A THR 60 ? C 1.367 1.229 0.138 0.019 N 
4 1 C A THR 60 ? D O A THR 60 ? D 1.344 1.229 0.115 0.019 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP B 20  ? ? -48.46  154.60  
2 1 LEU B 30  ? ? -116.73 -165.48 
3 1 CYS B 80  ? ? 79.32   -9.40   
4 1 LEU B 92  ? ? -134.28 -52.17  
5 1 ALA B 127 ? ? -105.78 70.20   
6 1 ALA B 127 ? ? -103.01 70.20   
7 1 ALA B 127 ? ? -105.84 70.20   
8 1 ALA B 127 ? ? -103.24 70.20   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 337 ? J HOH . 
2 1 B HOH 371 ? J HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined -13.4210 -1.8355 -19.2174 0.2572 0.3060 0.0302 0.2263 0.0575 0.0540  1.4258 1.8058 0.4922 -0.5034 
-0.1594 0.1913  0.3768 0.2906 0.1883 -0.2642 -0.3506 -0.1596 -0.0234 0.1814 -0.0263 
'X-RAY DIFFRACTION' 2 ? refined -18.2036 0.7762  -15.8102 0.3133 0.3340 0.0872 0.1576 0.0668 -0.0104 0.7946 0.4428 0.8085 -0.3971 
0.4963  -0.0971 0.3317 0.1969 0.0958 -0.1581 -0.3173 0.0110  0.1648  0.0838 -0.0144 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 A 50 ? ? A 88  ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 16 ? ? B 302 ? ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 1 Y 1 B GLU 177 ? B GLU 168 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BG8 N1   N  Y N 1   
A1BG8 N3   N  Y N 2   
A1BG8 C4   C  Y N 3   
A1BG8 C5   C  Y N 4   
A1BG8 C6   C  Y N 5   
A1BG8 C7   C  Y N 6   
A1BG8 C8   C  Y N 7   
A1BG8 C10  C  Y N 8   
A1BG8 C13  C  Y N 9   
A1BG8 C15  C  Y N 10  
A1BG8 C1   C  N N 11  
A1BG8 C2   C  Y N 12  
A1BG8 C3   C  Y N 13  
A1BG8 C9   C  Y N 14  
A1BG8 C11  C  N N 15  
A1BG8 O1   O  N N 16  
A1BG8 N2   N  N N 17  
A1BG8 C12  C  Y N 18  
A1BG8 N4   N  Y N 19  
A1BG8 C14  C  N N 20  
A1BG8 C16  C  Y N 21  
A1BG8 N5   N  Y N 22  
A1BG8 H5   H  N N 23  
A1BG8 H6   H  N N 24  
A1BG8 H7   H  N N 25  
A1BG8 H10  H  N N 26  
A1BG8 H14  H  N N 27  
A1BG8 H3   H  N N 28  
A1BG8 H2   H  N N 29  
A1BG8 H1   H  N N 30  
A1BG8 H4   H  N N 31  
A1BG8 H8   H  N N 32  
A1BG8 H9   H  N N 33  
A1BG8 H11  H  N N 34  
A1BG8 H13  H  N N 35  
A1BG8 H12  H  N N 36  
A1BG8 H15  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CL    CL   CL N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
DMS   S    S  N N 126 
DMS   O    O  N N 127 
DMS   C1   C  N N 128 
DMS   C2   C  N N 129 
DMS   H11  H  N N 130 
DMS   H12  H  N N 131 
DMS   H13  H  N N 132 
DMS   H21  H  N N 133 
DMS   H22  H  N N 134 
DMS   H23  H  N N 135 
GLN   N    N  N N 136 
GLN   CA   C  N S 137 
GLN   C    C  N N 138 
GLN   O    O  N N 139 
GLN   CB   C  N N 140 
GLN   CG   C  N N 141 
GLN   CD   C  N N 142 
GLN   OE1  O  N N 143 
GLN   NE2  N  N N 144 
GLN   OXT  O  N N 145 
GLN   H    H  N N 146 
GLN   H2   H  N N 147 
GLN   HA   H  N N 148 
GLN   HB2  H  N N 149 
GLN   HB3  H  N N 150 
GLN   HG2  H  N N 151 
GLN   HG3  H  N N 152 
GLN   HE21 H  N N 153 
GLN   HE22 H  N N 154 
GLN   HXT  H  N N 155 
GLU   N    N  N N 156 
GLU   CA   C  N S 157 
GLU   C    C  N N 158 
GLU   O    O  N N 159 
GLU   CB   C  N N 160 
GLU   CG   C  N N 161 
GLU   CD   C  N N 162 
GLU   OE1  O  N N 163 
GLU   OE2  O  N N 164 
GLU   OXT  O  N N 165 
GLU   H    H  N N 166 
GLU   H2   H  N N 167 
GLU   HA   H  N N 168 
GLU   HB2  H  N N 169 
GLU   HB3  H  N N 170 
GLU   HG2  H  N N 171 
GLU   HG3  H  N N 172 
GLU   HE2  H  N N 173 
GLU   HXT  H  N N 174 
GLY   N    N  N N 175 
GLY   CA   C  N N 176 
GLY   C    C  N N 177 
GLY   O    O  N N 178 
GLY   OXT  O  N N 179 
GLY   H    H  N N 180 
GLY   H2   H  N N 181 
GLY   HA2  H  N N 182 
GLY   HA3  H  N N 183 
GLY   HXT  H  N N 184 
HIS   N    N  N N 185 
HIS   CA   C  N S 186 
HIS   C    C  N N 187 
HIS   O    O  N N 188 
HIS   CB   C  N N 189 
HIS   CG   C  Y N 190 
HIS   ND1  N  Y N 191 
HIS   CD2  C  Y N 192 
HIS   CE1  C  Y N 193 
HIS   NE2  N  Y N 194 
HIS   OXT  O  N N 195 
HIS   H    H  N N 196 
HIS   H2   H  N N 197 
HIS   HA   H  N N 198 
HIS   HB2  H  N N 199 
HIS   HB3  H  N N 200 
HIS   HD1  H  N N 201 
HIS   HD2  H  N N 202 
HIS   HE1  H  N N 203 
HIS   HE2  H  N N 204 
HIS   HXT  H  N N 205 
HOH   O    O  N N 206 
HOH   H1   H  N N 207 
HOH   H2   H  N N 208 
ILE   N    N  N N 209 
ILE   CA   C  N S 210 
ILE   C    C  N N 211 
ILE   O    O  N N 212 
ILE   CB   C  N S 213 
ILE   CG1  C  N N 214 
ILE   CG2  C  N N 215 
ILE   CD1  C  N N 216 
ILE   OXT  O  N N 217 
ILE   H    H  N N 218 
ILE   H2   H  N N 219 
ILE   HA   H  N N 220 
ILE   HB   H  N N 221 
ILE   HG12 H  N N 222 
ILE   HG13 H  N N 223 
ILE   HG21 H  N N 224 
ILE   HG22 H  N N 225 
ILE   HG23 H  N N 226 
ILE   HD11 H  N N 227 
ILE   HD12 H  N N 228 
ILE   HD13 H  N N 229 
ILE   HXT  H  N N 230 
LEU   N    N  N N 231 
LEU   CA   C  N S 232 
LEU   C    C  N N 233 
LEU   O    O  N N 234 
LEU   CB   C  N N 235 
LEU   CG   C  N N 236 
LEU   CD1  C  N N 237 
LEU   CD2  C  N N 238 
LEU   OXT  O  N N 239 
LEU   H    H  N N 240 
LEU   H2   H  N N 241 
LEU   HA   H  N N 242 
LEU   HB2  H  N N 243 
LEU   HB3  H  N N 244 
LEU   HG   H  N N 245 
LEU   HD11 H  N N 246 
LEU   HD12 H  N N 247 
LEU   HD13 H  N N 248 
LEU   HD21 H  N N 249 
LEU   HD22 H  N N 250 
LEU   HD23 H  N N 251 
LEU   HXT  H  N N 252 
LYS   N    N  N N 253 
LYS   CA   C  N S 254 
LYS   C    C  N N 255 
LYS   O    O  N N 256 
LYS   CB   C  N N 257 
LYS   CG   C  N N 258 
LYS   CD   C  N N 259 
LYS   CE   C  N N 260 
LYS   NZ   N  N N 261 
LYS   OXT  O  N N 262 
LYS   H    H  N N 263 
LYS   H2   H  N N 264 
LYS   HA   H  N N 265 
LYS   HB2  H  N N 266 
LYS   HB3  H  N N 267 
LYS   HG2  H  N N 268 
LYS   HG3  H  N N 269 
LYS   HD2  H  N N 270 
LYS   HD3  H  N N 271 
LYS   HE2  H  N N 272 
LYS   HE3  H  N N 273 
LYS   HZ1  H  N N 274 
LYS   HZ2  H  N N 275 
LYS   HZ3  H  N N 276 
LYS   HXT  H  N N 277 
MET   N    N  N N 278 
MET   CA   C  N S 279 
MET   C    C  N N 280 
MET   O    O  N N 281 
MET   CB   C  N N 282 
MET   CG   C  N N 283 
MET   SD   S  N N 284 
MET   CE   C  N N 285 
MET   OXT  O  N N 286 
MET   H    H  N N 287 
MET   H2   H  N N 288 
MET   HA   H  N N 289 
MET   HB2  H  N N 290 
MET   HB3  H  N N 291 
MET   HG2  H  N N 292 
MET   HG3  H  N N 293 
MET   HE1  H  N N 294 
MET   HE2  H  N N 295 
MET   HE3  H  N N 296 
MET   HXT  H  N N 297 
PHE   N    N  N N 298 
PHE   CA   C  N S 299 
PHE   C    C  N N 300 
PHE   O    O  N N 301 
PHE   CB   C  N N 302 
PHE   CG   C  Y N 303 
PHE   CD1  C  Y N 304 
PHE   CD2  C  Y N 305 
PHE   CE1  C  Y N 306 
PHE   CE2  C  Y N 307 
PHE   CZ   C  Y N 308 
PHE   OXT  O  N N 309 
PHE   H    H  N N 310 
PHE   H2   H  N N 311 
PHE   HA   H  N N 312 
PHE   HB2  H  N N 313 
PHE   HB3  H  N N 314 
PHE   HD1  H  N N 315 
PHE   HD2  H  N N 316 
PHE   HE1  H  N N 317 
PHE   HE2  H  N N 318 
PHE   HZ   H  N N 319 
PHE   HXT  H  N N 320 
PRO   N    N  N N 321 
PRO   CA   C  N S 322 
PRO   C    C  N N 323 
PRO   O    O  N N 324 
PRO   CB   C  N N 325 
PRO   CG   C  N N 326 
PRO   CD   C  N N 327 
PRO   OXT  O  N N 328 
PRO   H    H  N N 329 
PRO   HA   H  N N 330 
PRO   HB2  H  N N 331 
PRO   HB3  H  N N 332 
PRO   HG2  H  N N 333 
PRO   HG3  H  N N 334 
PRO   HD2  H  N N 335 
PRO   HD3  H  N N 336 
PRO   HXT  H  N N 337 
SER   N    N  N N 338 
SER   CA   C  N S 339 
SER   C    C  N N 340 
SER   O    O  N N 341 
SER   CB   C  N N 342 
SER   OG   O  N N 343 
SER   OXT  O  N N 344 
SER   H    H  N N 345 
SER   H2   H  N N 346 
SER   HA   H  N N 347 
SER   HB2  H  N N 348 
SER   HB3  H  N N 349 
SER   HG   H  N N 350 
SER   HXT  H  N N 351 
SO4   S    S  N N 352 
SO4   O1   O  N N 353 
SO4   O2   O  N N 354 
SO4   O3   O  N N 355 
SO4   O4   O  N N 356 
THR   N    N  N N 357 
THR   CA   C  N S 358 
THR   C    C  N N 359 
THR   O    O  N N 360 
THR   CB   C  N R 361 
THR   OG1  O  N N 362 
THR   CG2  C  N N 363 
THR   OXT  O  N N 364 
THR   H    H  N N 365 
THR   H2   H  N N 366 
THR   HA   H  N N 367 
THR   HB   H  N N 368 
THR   HG1  H  N N 369 
THR   HG21 H  N N 370 
THR   HG22 H  N N 371 
THR   HG23 H  N N 372 
THR   HXT  H  N N 373 
TRP   N    N  N N 374 
TRP   CA   C  N S 375 
TRP   C    C  N N 376 
TRP   O    O  N N 377 
TRP   CB   C  N N 378 
TRP   CG   C  Y N 379 
TRP   CD1  C  Y N 380 
TRP   CD2  C  Y N 381 
TRP   NE1  N  Y N 382 
TRP   CE2  C  Y N 383 
TRP   CE3  C  Y N 384 
TRP   CZ2  C  Y N 385 
TRP   CZ3  C  Y N 386 
TRP   CH2  C  Y N 387 
TRP   OXT  O  N N 388 
TRP   H    H  N N 389 
TRP   H2   H  N N 390 
TRP   HA   H  N N 391 
TRP   HB2  H  N N 392 
TRP   HB3  H  N N 393 
TRP   HD1  H  N N 394 
TRP   HE1  H  N N 395 
TRP   HE3  H  N N 396 
TRP   HZ2  H  N N 397 
TRP   HZ3  H  N N 398 
TRP   HH2  H  N N 399 
TRP   HXT  H  N N 400 
TYR   N    N  N N 401 
TYR   CA   C  N S 402 
TYR   C    C  N N 403 
TYR   O    O  N N 404 
TYR   CB   C  N N 405 
TYR   CG   C  Y N 406 
TYR   CD1  C  Y N 407 
TYR   CD2  C  Y N 408 
TYR   CE1  C  Y N 409 
TYR   CE2  C  Y N 410 
TYR   CZ   C  Y N 411 
TYR   OH   O  N N 412 
TYR   OXT  O  N N 413 
TYR   H    H  N N 414 
TYR   H2   H  N N 415 
TYR   HA   H  N N 416 
TYR   HB2  H  N N 417 
TYR   HB3  H  N N 418 
TYR   HD1  H  N N 419 
TYR   HD2  H  N N 420 
TYR   HE1  H  N N 421 
TYR   HE2  H  N N 422 
TYR   HH   H  N N 423 
TYR   HXT  H  N N 424 
VAL   N    N  N N 425 
VAL   CA   C  N S 426 
VAL   C    C  N N 427 
VAL   O    O  N N 428 
VAL   CB   C  N N 429 
VAL   CG1  C  N N 430 
VAL   CG2  C  N N 431 
VAL   OXT  O  N N 432 
VAL   H    H  N N 433 
VAL   H2   H  N N 434 
VAL   HA   H  N N 435 
VAL   HB   H  N N 436 
VAL   HG11 H  N N 437 
VAL   HG12 H  N N 438 
VAL   HG13 H  N N 439 
VAL   HG21 H  N N 440 
VAL   HG22 H  N N 441 
VAL   HG23 H  N N 442 
VAL   HXT  H  N N 443 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1BG8 C1  C2   sing N N 1   
A1BG8 C2  N1   doub Y N 2   
A1BG8 N1  C3   sing Y N 3   
A1BG8 C3  C4   doub Y N 4   
A1BG8 C4  C5   sing N N 5   
A1BG8 C5  C6   doub Y N 6   
A1BG8 C6  C7   sing Y N 7   
A1BG8 C7  C8   doub Y N 8   
A1BG8 C8  C9   sing Y N 9   
A1BG8 C9  C10  doub Y N 10  
A1BG8 C10 C11  sing N N 11  
A1BG8 C11 O1   doub N N 12  
A1BG8 C11 N2   sing N N 13  
A1BG8 N2  C12  sing N N 14  
A1BG8 C12 C13  sing Y N 15  
A1BG8 C13 N3   doub Y N 16  
A1BG8 N3  N4   sing Y N 17  
A1BG8 N4  C14  sing N N 18  
A1BG8 N4  C15  sing Y N 19  
A1BG8 C4  C16  sing Y N 20  
A1BG8 C16 N5   doub Y N 21  
A1BG8 C2  N5   sing Y N 22  
A1BG8 C5  C10  sing Y N 23  
A1BG8 C12 C15  doub Y N 24  
A1BG8 C6  H5   sing N N 25  
A1BG8 C7  H6   sing N N 26  
A1BG8 C8  H7   sing N N 27  
A1BG8 C13 H10  sing N N 28  
A1BG8 C15 H14  sing N N 29  
A1BG8 C1  H3   sing N N 30  
A1BG8 C1  H2   sing N N 31  
A1BG8 C1  H1   sing N N 32  
A1BG8 C3  H4   sing N N 33  
A1BG8 C9  H8   sing N N 34  
A1BG8 N2  H9   sing N N 35  
A1BG8 C14 H11  sing N N 36  
A1BG8 C14 H13  sing N N 37  
A1BG8 C14 H12  sing N N 38  
A1BG8 C16 H15  sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
DMS   S   O    doub N N 122 
DMS   S   C1   sing N N 123 
DMS   S   C2   sing N N 124 
DMS   C1  H11  sing N N 125 
DMS   C1  H12  sing N N 126 
DMS   C1  H13  sing N N 127 
DMS   C2  H21  sing N N 128 
DMS   C2  H22  sing N N 129 
DMS   C2  H23  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
HIS   N   CA   sing N N 177 
HIS   N   H    sing N N 178 
HIS   N   H2   sing N N 179 
HIS   CA  C    sing N N 180 
HIS   CA  CB   sing N N 181 
HIS   CA  HA   sing N N 182 
HIS   C   O    doub N N 183 
HIS   C   OXT  sing N N 184 
HIS   CB  CG   sing N N 185 
HIS   CB  HB2  sing N N 186 
HIS   CB  HB3  sing N N 187 
HIS   CG  ND1  sing Y N 188 
HIS   CG  CD2  doub Y N 189 
HIS   ND1 CE1  doub Y N 190 
HIS   ND1 HD1  sing N N 191 
HIS   CD2 NE2  sing Y N 192 
HIS   CD2 HD2  sing N N 193 
HIS   CE1 NE2  sing Y N 194 
HIS   CE1 HE1  sing N N 195 
HIS   NE2 HE2  sing N N 196 
HIS   OXT HXT  sing N N 197 
HOH   O   H1   sing N N 198 
HOH   O   H2   sing N N 199 
ILE   N   CA   sing N N 200 
ILE   N   H    sing N N 201 
ILE   N   H2   sing N N 202 
ILE   CA  C    sing N N 203 
ILE   CA  CB   sing N N 204 
ILE   CA  HA   sing N N 205 
ILE   C   O    doub N N 206 
ILE   C   OXT  sing N N 207 
ILE   CB  CG1  sing N N 208 
ILE   CB  CG2  sing N N 209 
ILE   CB  HB   sing N N 210 
ILE   CG1 CD1  sing N N 211 
ILE   CG1 HG12 sing N N 212 
ILE   CG1 HG13 sing N N 213 
ILE   CG2 HG21 sing N N 214 
ILE   CG2 HG22 sing N N 215 
ILE   CG2 HG23 sing N N 216 
ILE   CD1 HD11 sing N N 217 
ILE   CD1 HD12 sing N N 218 
ILE   CD1 HD13 sing N N 219 
ILE   OXT HXT  sing N N 220 
LEU   N   CA   sing N N 221 
LEU   N   H    sing N N 222 
LEU   N   H2   sing N N 223 
LEU   CA  C    sing N N 224 
LEU   CA  CB   sing N N 225 
LEU   CA  HA   sing N N 226 
LEU   C   O    doub N N 227 
LEU   C   OXT  sing N N 228 
LEU   CB  CG   sing N N 229 
LEU   CB  HB2  sing N N 230 
LEU   CB  HB3  sing N N 231 
LEU   CG  CD1  sing N N 232 
LEU   CG  CD2  sing N N 233 
LEU   CG  HG   sing N N 234 
LEU   CD1 HD11 sing N N 235 
LEU   CD1 HD12 sing N N 236 
LEU   CD1 HD13 sing N N 237 
LEU   CD2 HD21 sing N N 238 
LEU   CD2 HD22 sing N N 239 
LEU   CD2 HD23 sing N N 240 
LEU   OXT HXT  sing N N 241 
LYS   N   CA   sing N N 242 
LYS   N   H    sing N N 243 
LYS   N   H2   sing N N 244 
LYS   CA  C    sing N N 245 
LYS   CA  CB   sing N N 246 
LYS   CA  HA   sing N N 247 
LYS   C   O    doub N N 248 
LYS   C   OXT  sing N N 249 
LYS   CB  CG   sing N N 250 
LYS   CB  HB2  sing N N 251 
LYS   CB  HB3  sing N N 252 
LYS   CG  CD   sing N N 253 
LYS   CG  HG2  sing N N 254 
LYS   CG  HG3  sing N N 255 
LYS   CD  CE   sing N N 256 
LYS   CD  HD2  sing N N 257 
LYS   CD  HD3  sing N N 258 
LYS   CE  NZ   sing N N 259 
LYS   CE  HE2  sing N N 260 
LYS   CE  HE3  sing N N 261 
LYS   NZ  HZ1  sing N N 262 
LYS   NZ  HZ2  sing N N 263 
LYS   NZ  HZ3  sing N N 264 
LYS   OXT HXT  sing N N 265 
MET   N   CA   sing N N 266 
MET   N   H    sing N N 267 
MET   N   H2   sing N N 268 
MET   CA  C    sing N N 269 
MET   CA  CB   sing N N 270 
MET   CA  HA   sing N N 271 
MET   C   O    doub N N 272 
MET   C   OXT  sing N N 273 
MET   CB  CG   sing N N 274 
MET   CB  HB2  sing N N 275 
MET   CB  HB3  sing N N 276 
MET   CG  SD   sing N N 277 
MET   CG  HG2  sing N N 278 
MET   CG  HG3  sing N N 279 
MET   SD  CE   sing N N 280 
MET   CE  HE1  sing N N 281 
MET   CE  HE2  sing N N 282 
MET   CE  HE3  sing N N 283 
MET   OXT HXT  sing N N 284 
PHE   N   CA   sing N N 285 
PHE   N   H    sing N N 286 
PHE   N   H2   sing N N 287 
PHE   CA  C    sing N N 288 
PHE   CA  CB   sing N N 289 
PHE   CA  HA   sing N N 290 
PHE   C   O    doub N N 291 
PHE   C   OXT  sing N N 292 
PHE   CB  CG   sing N N 293 
PHE   CB  HB2  sing N N 294 
PHE   CB  HB3  sing N N 295 
PHE   CG  CD1  doub Y N 296 
PHE   CG  CD2  sing Y N 297 
PHE   CD1 CE1  sing Y N 298 
PHE   CD1 HD1  sing N N 299 
PHE   CD2 CE2  doub Y N 300 
PHE   CD2 HD2  sing N N 301 
PHE   CE1 CZ   doub Y N 302 
PHE   CE1 HE1  sing N N 303 
PHE   CE2 CZ   sing Y N 304 
PHE   CE2 HE2  sing N N 305 
PHE   CZ  HZ   sing N N 306 
PHE   OXT HXT  sing N N 307 
PRO   N   CA   sing N N 308 
PRO   N   CD   sing N N 309 
PRO   N   H    sing N N 310 
PRO   CA  C    sing N N 311 
PRO   CA  CB   sing N N 312 
PRO   CA  HA   sing N N 313 
PRO   C   O    doub N N 314 
PRO   C   OXT  sing N N 315 
PRO   CB  CG   sing N N 316 
PRO   CB  HB2  sing N N 317 
PRO   CB  HB3  sing N N 318 
PRO   CG  CD   sing N N 319 
PRO   CG  HG2  sing N N 320 
PRO   CG  HG3  sing N N 321 
PRO   CD  HD2  sing N N 322 
PRO   CD  HD3  sing N N 323 
PRO   OXT HXT  sing N N 324 
SER   N   CA   sing N N 325 
SER   N   H    sing N N 326 
SER   N   H2   sing N N 327 
SER   CA  C    sing N N 328 
SER   CA  CB   sing N N 329 
SER   CA  HA   sing N N 330 
SER   C   O    doub N N 331 
SER   C   OXT  sing N N 332 
SER   CB  OG   sing N N 333 
SER   CB  HB2  sing N N 334 
SER   CB  HB3  sing N N 335 
SER   OG  HG   sing N N 336 
SER   OXT HXT  sing N N 337 
SO4   S   O1   doub N N 338 
SO4   S   O2   doub N N 339 
SO4   S   O3   sing N N 340 
SO4   S   O4   sing N N 341 
THR   N   CA   sing N N 342 
THR   N   H    sing N N 343 
THR   N   H2   sing N N 344 
THR   CA  C    sing N N 345 
THR   CA  CB   sing N N 346 
THR   CA  HA   sing N N 347 
THR   C   O    doub N N 348 
THR   C   OXT  sing N N 349 
THR   CB  OG1  sing N N 350 
THR   CB  CG2  sing N N 351 
THR   CB  HB   sing N N 352 
THR   OG1 HG1  sing N N 353 
THR   CG2 HG21 sing N N 354 
THR   CG2 HG22 sing N N 355 
THR   CG2 HG23 sing N N 356 
THR   OXT HXT  sing N N 357 
TRP   N   CA   sing N N 358 
TRP   N   H    sing N N 359 
TRP   N   H2   sing N N 360 
TRP   CA  C    sing N N 361 
TRP   CA  CB   sing N N 362 
TRP   CA  HA   sing N N 363 
TRP   C   O    doub N N 364 
TRP   C   OXT  sing N N 365 
TRP   CB  CG   sing N N 366 
TRP   CB  HB2  sing N N 367 
TRP   CB  HB3  sing N N 368 
TRP   CG  CD1  doub Y N 369 
TRP   CG  CD2  sing Y N 370 
TRP   CD1 NE1  sing Y N 371 
TRP   CD1 HD1  sing N N 372 
TRP   CD2 CE2  doub Y N 373 
TRP   CD2 CE3  sing Y N 374 
TRP   NE1 CE2  sing Y N 375 
TRP   NE1 HE1  sing N N 376 
TRP   CE2 CZ2  sing Y N 377 
TRP   CE3 CZ3  doub Y N 378 
TRP   CE3 HE3  sing N N 379 
TRP   CZ2 CH2  doub Y N 380 
TRP   CZ2 HZ2  sing N N 381 
TRP   CZ3 CH2  sing Y N 382 
TRP   CZ3 HZ3  sing N N 383 
TRP   CH2 HH2  sing N N 384 
TRP   OXT HXT  sing N N 385 
TYR   N   CA   sing N N 386 
TYR   N   H    sing N N 387 
TYR   N   H2   sing N N 388 
TYR   CA  C    sing N N 389 
TYR   CA  CB   sing N N 390 
TYR   CA  HA   sing N N 391 
TYR   C   O    doub N N 392 
TYR   C   OXT  sing N N 393 
TYR   CB  CG   sing N N 394 
TYR   CB  HB2  sing N N 395 
TYR   CB  HB3  sing N N 396 
TYR   CG  CD1  doub Y N 397 
TYR   CG  CD2  sing Y N 398 
TYR   CD1 CE1  sing Y N 399 
TYR   CD1 HD1  sing N N 400 
TYR   CD2 CE2  doub Y N 401 
TYR   CD2 HD2  sing N N 402 
TYR   CE1 CZ   doub Y N 403 
TYR   CE1 HE1  sing N N 404 
TYR   CE2 CZ   sing Y N 405 
TYR   CE2 HE2  sing N N 406 
TYR   CZ  OH   sing N N 407 
TYR   OH  HH   sing N N 408 
TYR   OXT HXT  sing N N 409 
VAL   N   CA   sing N N 410 
VAL   N   H    sing N N 411 
VAL   N   H2   sing N N 412 
VAL   CA  C    sing N N 413 
VAL   CA  CB   sing N N 414 
VAL   CA  HA   sing N N 415 
VAL   C   O    doub N N 416 
VAL   C   OXT  sing N N 417 
VAL   CB  CG1  sing N N 418 
VAL   CB  CG2  sing N N 419 
VAL   CB  HB   sing N N 420 
VAL   CG1 HG11 sing N N 421 
VAL   CG1 HG12 sing N N 422 
VAL   CG1 HG13 sing N N 423 
VAL   CG2 HG21 sing N N 424 
VAL   CG2 HG22 sing N N 425 
VAL   CG2 HG23 sing N N 426 
VAL   OXT HXT  sing N N 427 
# 
_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                    7HP1 
_atom_sites.fract_transf_matrix[1][1]   0.023629 
_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]   0.023629 
_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]   0.004645 
_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  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASP   A 1 7   ? -21.543 19.156  -7.284  1.00 59.40  ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -22.634 18.150  -7.365  1.00 59.06  ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -22.483 17.497  -8.754  1.00 56.19  ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -22.321 18.193  -9.796  1.00 57.25  ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -24.026 18.733  -7.053  1.00 59.11  ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -24.918 17.939  -6.085  1.00 66.98  ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -25.438 18.561  -5.106  1.00 71.02  ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -25.176 16.713  -6.326  1.00 71.25  ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -22.409 16.183  -8.749  1.00 49.55  ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -22.277 15.371  -9.965  1.00 46.65  ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -23.689 15.076  -10.473 1.00 43.47  ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -24.596 14.898  -9.647  1.00 43.18  ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -21.527 14.062  -9.688  1.00 46.12  ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -20.102 14.283  -9.381  1.00 47.75  ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -19.248 12.709  -9.156  1.00 49.19  ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -17.554 13.294  -9.124  1.00 50.90  ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -23.846 15.043  -11.793 1.00 39.56  ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -25.144 14.837  -12.464 1.00 38.05  ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -24.949 13.858  -13.596 1.00 36.40  ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -23.854 13.671  -14.051 1.00 35.21  ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -25.756 16.186  -12.862 1.00 37.96  ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -24.983 16.941  -13.906 1.00 38.82  ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -23.966 17.799  -13.523 1.00 39.69  ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -25.250 16.802  -15.265 1.00 40.43  ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -23.251 18.541  -14.446 1.00 41.31  ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -24.506 17.504  -16.215 1.00 41.48  ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -23.517 18.396  -15.795 1.00 42.24  ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -22.711 19.081  -16.670 1.00 44.63  ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -26.017 13.164  -13.970 1.00 37.70  ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -25.957 12.189  -15.094 1.00 37.42  ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -26.783 12.671  -16.300 1.00 38.46  ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -27.769 13.443  -16.111 1.00 38.87  ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -26.374 10.786  -14.623 1.00 36.80  ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -27.788 10.722  -14.076 1.00 37.98  ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -25.379 10.231  -13.627 1.00 37.25  ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -28.249 9.294   -13.947 1.00 39.21  ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -26.377 12.230  -17.492 1.00 39.09  ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -27.013 12.547  -18.818 1.00 40.71  ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -27.037 11.271  -19.666 1.00 38.80  ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -25.965 10.587  -19.746 1.00 35.47  ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -26.210 13.550  -19.648 1.00 43.53  ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -26.234 14.990  -19.192 1.00 46.96  ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -25.285 15.872  -20.007 1.00 50.52  ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -24.390 15.348  -20.739 1.00 51.67  ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -25.403 17.083  -19.888 1.00 52.92  ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -28.207 10.898  -20.206 1.00 39.11  ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -28.349 9.662   -21.010 1.00 39.64  ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -27.452 9.820   -22.229 1.00 40.64  ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -27.366 10.967  -22.741 1.00 41.67  ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -29.812 9.411   -21.338 1.00 42.48  ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -30.089 7.998   -21.835 1.00 44.57  ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -31.520 7.540   -21.536 1.00 47.73  ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -31.600 6.148   -21.909 1.00 49.38  ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -31.669 5.744   -23.178 1.00 50.57  ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -31.763 6.635   -24.137 1.00 56.50  ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -31.627 4.466   -23.494 1.00 48.81  ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -26.705 8.769   -22.593 1.00 39.73  ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -25.765 8.735   -23.746 1.00 40.17  ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -26.140 7.655   -24.765 1.00 40.36  ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -25.472 7.633   -25.815 1.00 41.09  ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -24.326 8.536   -23.334 1.00 41.68  ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -27.063 6.749   -24.473 1.00 38.98  ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -27.424 5.712   -25.441 1.00 40.25  ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -28.158 4.560   -24.819 1.00 41.42  ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -28.179 4.479   -23.523 1.00 39.33  ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -28.677 3.682   -25.699 1.00 42.89  ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -29.177 2.323   -25.375 1.00 44.60  ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -27.982 1.366   -25.256 1.00 46.55  ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -26.920 1.639   -25.837 1.00 48.63  ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -30.126 1.740   -26.423 1.00 45.73  ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -31.481 2.401   -26.502 1.00 48.89  ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -31.643 3.474   -25.912 1.00 45.91  ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -32.360 1.859   -27.228 1.00 51.98  ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -28.146 0.305   -24.474 1.00 45.24  ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -27.121 -0.753  -24.308 1.00 45.47  ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -27.532 -1.854  -25.274 1.00 46.65  ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -28.489 -2.608  -25.005 1.00 45.68  ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -26.969 -1.182  -22.853 1.00 44.68  ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -26.427 0.005   -22.050 1.00 43.70  ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -26.073 -2.415  -22.708 1.00 44.17  ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -26.581 -0.179  -20.606 1.00 43.98  ? 59  ILE   A CD1 1 
ATOM   82   N  N   A THR   A 1 17  ? -26.821 -1.883  -26.407 0.25 47.43  ? 60  THR   A N   1 
ATOM   83   N  N   B THR   A 1 17  ? -26.815 -1.945  -26.395 0.25 47.11  ? 60  THR   A N   1 
ATOM   84   N  N   C THR   A 1 17  ? -26.821 -1.883  -26.407 0.25 47.43  ? 60  THR   A N   1 
ATOM   85   N  N   D THR   A 1 17  ? -26.815 -1.945  -26.395 0.25 47.11  ? 60  THR   A N   1 
ATOM   86   C  CA  A THR   A 1 17  ? -27.024 -2.776  -27.577 0.25 48.46  ? 60  THR   A CA  1 
ATOM   87   C  CA  B THR   A 1 17  ? -27.120 -2.869  -27.517 0.25 47.93  ? 60  THR   A CA  1 
ATOM   88   C  CA  C THR   A 1 17  ? -27.024 -2.776  -27.577 0.25 48.46  ? 60  THR   A CA  1 
ATOM   89   C  CA  D THR   A 1 17  ? -27.120 -2.869  -27.517 0.25 47.93  ? 60  THR   A CA  1 
ATOM   90   C  C   A THR   A 1 17  ? -25.654 -3.296  -28.107 0.25 48.87  ? 60  THR   A C   1 
ATOM   91   C  C   B THR   A 1 17  ? -25.824 -3.245  -28.312 0.25 48.58  ? 60  THR   A C   1 
ATOM   92   C  C   C THR   A 1 17  ? -25.654 -3.296  -28.107 0.25 48.87  ? 60  THR   A C   1 
ATOM   93   C  C   D THR   A 1 17  ? -25.824 -3.245  -28.312 0.25 48.58  ? 60  THR   A C   1 
ATOM   94   O  O   A THR   A 1 17  ? -24.617 -2.431  -28.322 0.25 49.35  ? 60  THR   A O   1 
ATOM   95   O  O   B THR   A 1 17  ? -25.019 -2.236  -28.688 0.25 48.74  ? 60  THR   A O   1 
ATOM   96   O  O   C THR   A 1 17  ? -24.617 -2.431  -28.322 0.25 49.35  ? 60  THR   A O   1 
ATOM   97   O  O   D THR   A 1 17  ? -25.019 -2.236  -28.688 0.25 48.74  ? 60  THR   A O   1 
ATOM   98   C  CB  A THR   A 1 17  ? -27.701 -2.035  -28.737 0.25 49.60  ? 60  THR   A CB  1 
ATOM   99   C  CB  B THR   A 1 17  ? -28.136 -2.224  -28.466 0.25 48.71  ? 60  THR   A CB  1 
ATOM   100  C  CB  C THR   A 1 17  ? -27.701 -2.035  -28.737 0.25 49.60  ? 60  THR   A CB  1 
ATOM   101  C  CB  D THR   A 1 17  ? -28.136 -2.224  -28.466 0.25 48.71  ? 60  THR   A CB  1 
ATOM   102  O  OG1 A THR   A 1 17  ? -26.787 -1.101  -29.312 0.25 49.96  ? 60  THR   A OG1 1 
ATOM   103  O  OG1 B THR   A 1 17  ? -29.349 -2.008  -27.737 0.25 47.83  ? 60  THR   A OG1 1 
ATOM   104  O  OG1 C THR   A 1 17  ? -26.787 -1.101  -29.312 0.25 49.96  ? 60  THR   A OG1 1 
ATOM   105  O  OG1 D THR   A 1 17  ? -29.349 -2.008  -27.737 0.25 47.83  ? 60  THR   A OG1 1 
ATOM   106  C  CG2 A THR   A 1 17  ? -28.923 -1.267  -28.302 0.25 50.01  ? 60  THR   A CG2 1 
ATOM   107  C  CG2 B THR   A 1 17  ? -28.402 -3.078  -29.678 0.25 49.93  ? 60  THR   A CG2 1 
ATOM   108  C  CG2 C THR   A 1 17  ? -28.923 -1.267  -28.302 0.25 50.01  ? 60  THR   A CG2 1 
ATOM   109  C  CG2 D THR   A 1 17  ? -28.402 -3.078  -29.678 0.25 49.93  ? 60  THR   A CG2 1 
ATOM   110  N  N   . TRP   A 1 18  ? -25.719 -4.637  -28.464 1.00 49.38  ? 61  TRP   A N   1 
ATOM   111  C  CA  . TRP   A 1 18  ? -24.657 -5.208  -29.319 1.00 53.65  ? 61  TRP   A CA  1 
ATOM   112  C  C   . TRP   A 1 18  ? -24.877 -4.584  -30.708 1.00 56.40  ? 61  TRP   A C   1 
ATOM   113  O  O   . TRP   A 1 18  ? -26.026 -4.502  -31.127 1.00 60.06  ? 61  TRP   A O   1 
ATOM   114  C  CB  . TRP   A 1 18  ? -24.755 -6.723  -29.331 1.00 52.96  ? 61  TRP   A CB  1 
ATOM   115  C  CG  . TRP   A 1 18  ? -23.639 -7.326  -30.106 1.00 56.24  ? 61  TRP   A CG  1 
ATOM   116  C  CD1 . TRP   A 1 18  ? -23.583 -7.489  -31.459 1.00 59.35  ? 61  TRP   A CD1 1 
ATOM   117  C  CD2 . TRP   A 1 18  ? -22.423 -7.883  -29.580 1.00 57.31  ? 61  TRP   A CD2 1 
ATOM   118  N  NE1 . TRP   A 1 18  ? -22.399 -8.076  -31.802 1.00 60.03  ? 61  TRP   A NE1 1 
ATOM   119  C  CE2 . TRP   A 1 18  ? -21.680 -8.359  -30.679 1.00 58.89  ? 61  TRP   A CE2 1 
ATOM   120  C  CE3 . TRP   A 1 18  ? -21.885 -8.027  -28.305 1.00 54.73  ? 61  TRP   A CE3 1 
ATOM   121  C  CZ2 . TRP   A 1 18  ? -20.431 -8.961  -30.541 1.00 59.73  ? 61  TRP   A CZ2 1 
ATOM   122  C  CZ3 . TRP   A 1 18  ? -20.657 -8.630  -28.164 1.00 57.16  ? 61  TRP   A CZ3 1 
ATOM   123  C  CH2 . TRP   A 1 18  ? -19.940 -9.088  -29.261 1.00 58.21  ? 61  TRP   A CH2 1 
ATOM   124  N  N   A GLU   A 1 19  ? -23.802 -4.173  -31.387 0.25 58.89  ? 62  GLU   A N   1 
ATOM   125  N  N   B GLU   A 1 19  ? -23.802 -4.173  -31.387 0.25 58.89  ? 62  GLU   A N   1 
ATOM   126  N  N   C GLU   A 1 19  ? -23.800 -4.089  -31.340 0.25 57.51  ? 62  GLU   A N   1 
ATOM   127  N  N   D GLU   A 1 19  ? -23.800 -4.089  -31.340 0.25 57.51  ? 62  GLU   A N   1 
ATOM   128  C  CA  A GLU   A 1 19  ? -23.853 -3.569  -32.747 0.25 61.72  ? 62  GLU   A CA  1 
ATOM   129  C  CA  B GLU   A 1 19  ? -23.853 -3.569  -32.747 0.25 61.72  ? 62  GLU   A CA  1 
ATOM   130  C  CA  C GLU   A 1 19  ? -23.777 -3.568  -32.739 0.25 59.61  ? 62  GLU   A CA  1 
ATOM   131  C  CA  D GLU   A 1 19  ? -23.777 -3.568  -32.739 0.25 59.61  ? 62  GLU   A CA  1 
ATOM   132  C  C   A GLU   A 1 19  ? -22.972 -4.379  -33.707 0.25 63.90  ? 62  GLU   A C   1 
ATOM   133  C  C   B GLU   A 1 19  ? -22.972 -4.379  -33.707 0.25 63.90  ? 62  GLU   A C   1 
ATOM   134  C  C   C GLU   A 1 19  ? -22.978 -4.524  -33.628 0.25 62.48  ? 62  GLU   A C   1 
ATOM   135  C  C   D GLU   A 1 19  ? -22.978 -4.524  -33.628 0.25 62.48  ? 62  GLU   A C   1 
ATOM   136  O  O   A GLU   A 1 19  ? -21.739 -4.359  -33.535 0.25 63.63  ? 62  GLU   A O   1 
ATOM   137  O  O   B GLU   A 1 19  ? -21.739 -4.359  -33.535 0.25 63.63  ? 62  GLU   A O   1 
ATOM   138  O  O   C GLU   A 1 19  ? -21.798 -4.769  -33.318 0.25 62.10  ? 62  GLU   A O   1 
ATOM   139  O  O   D GLU   A 1 19  ? -21.798 -4.769  -33.318 0.25 62.10  ? 62  GLU   A O   1 
ATOM   140  C  CB  A GLU   A 1 19  ? -23.406 -2.107  -32.689 0.25 62.23  ? 62  GLU   A CB  1 
ATOM   141  C  CB  B GLU   A 1 19  ? -23.406 -2.107  -32.689 0.25 62.23  ? 62  GLU   A CB  1 
ATOM   142  C  CB  C GLU   A 1 19  ? -23.120 -2.187  -32.841 0.25 58.73  ? 62  GLU   A CB  1 
ATOM   143  C  CB  D GLU   A 1 19  ? -23.120 -2.187  -32.841 0.25 58.73  ? 62  GLU   A CB  1 
ATOM   144  C  CG  A GLU   A 1 19  ? -24.167 -1.278  -31.664 0.25 61.70  ? 62  GLU   A CG  1 
ATOM   145  C  CG  B GLU   A 1 19  ? -24.167 -1.278  -31.664 0.25 61.70  ? 62  GLU   A CG  1 
ATOM   146  C  CG  C GLU   A 1 19  ? -23.080 -1.644  -34.269 0.25 59.90  ? 62  GLU   A CG  1 
ATOM   147  C  CG  D GLU   A 1 19  ? -23.080 -1.644  -34.269 0.25 59.90  ? 62  GLU   A CG  1 
ATOM   148  C  CD  A GLU   A 1 19  ? -25.600 -0.917  -32.021 0.25 62.50  ? 62  GLU   A CD  1 
ATOM   149  C  CD  B GLU   A 1 19  ? -25.600 -0.917  -32.021 0.25 62.50  ? 62  GLU   A CD  1 
ATOM   150  C  CD  C GLU   A 1 19  ? -22.046 -0.560  -34.547 0.25 59.57  ? 62  GLU   A CD  1 
ATOM   151  C  CD  D GLU   A 1 19  ? -22.046 -0.560  -34.547 0.25 59.57  ? 62  GLU   A CD  1 
ATOM   152  O  OE1 A GLU   A 1 19  ? -26.059 -1.309  -33.118 0.25 65.98  ? 62  GLU   A OE1 1 
ATOM   153  O  OE1 B GLU   A 1 19  ? -26.059 -1.309  -33.118 0.25 65.98  ? 62  GLU   A OE1 1 
ATOM   154  O  OE1 C GLU   A 1 19  ? -21.461 -0.037  -33.549 0.25 60.12  ? 62  GLU   A OE1 1 
ATOM   155  O  OE1 D GLU   A 1 19  ? -21.461 -0.037  -33.549 0.25 60.12  ? 62  GLU   A OE1 1 
ATOM   156  O  OE2 A GLU   A 1 19  ? -26.250 -0.241  -31.199 0.25 61.22  ? 62  GLU   A OE2 1 
ATOM   157  O  OE2 B GLU   A 1 19  ? -26.250 -0.241  -31.199 0.25 61.22  ? 62  GLU   A OE2 1 
ATOM   158  O  OE2 C GLU   A 1 19  ? -21.811 -0.253  -35.764 0.25 61.06  ? 62  GLU   A OE2 1 
ATOM   159  O  OE2 D GLU   A 1 19  ? -21.811 -0.253  -35.764 0.25 61.06  ? 62  GLU   A OE2 1 
ATOM   160  N  N   . LYS   A 1 20  ? -23.584 -5.027  -34.706 1.00 66.65  ? 63  LYS   A N   1 
ATOM   161  C  CA  . LYS   A 1 20  ? -22.852 -5.870  -35.702 1.00 70.94  ? 63  LYS   A CA  1 
ATOM   162  C  C   . LYS   A 1 20  ? -21.945 -4.963  -36.527 1.00 70.51  ? 63  LYS   A C   1 
ATOM   163  O  O   . LYS   A 1 20  ? -22.349 -3.831  -36.811 1.00 66.27  ? 63  LYS   A O   1 
ATOM   164  C  CB  . LYS   A 1 20  ? -23.803 -6.635  -36.618 1.00 77.39  ? 63  LYS   A CB  1 
ATOM   165  C  CG  . LYS   A 1 20  ? -24.576 -7.751  -35.938 1.00 81.31  ? 63  LYS   A CG  1 
ATOM   166  C  CD  . LYS   A 1 20  ? -25.950 -7.919  -36.539 1.00 85.77  ? 63  LYS   A CD  1 
ATOM   167  C  CE  . LYS   A 1 20  ? -26.848 -8.860  -35.768 1.00 88.53  ? 63  LYS   A CE  1 
ATOM   168  N  NZ  . LYS   A 1 20  ? -28.271 -8.632  -36.117 1.00 89.07  ? 63  LYS   A NZ  1 
ATOM   169  N  N   . ASP   A 1 21  ? -20.744 -5.424  -36.861 1.00 73.14  ? 64  ASP   A N   1 
ATOM   170  C  CA  . ASP   A 1 21  ? -19.778 -4.593  -37.634 1.00 78.81  ? 64  ASP   A CA  1 
ATOM   171  C  C   . ASP   A 1 21  ? -19.507 -3.312  -36.813 1.00 77.56  ? 64  ASP   A C   1 
ATOM   172  O  O   . ASP   A 1 21  ? -19.432 -2.203  -37.392 1.00 77.01  ? 64  ASP   A O   1 
ATOM   173  C  CB  . ASP   A 1 21  ? -20.263 -4.335  -39.076 1.00 87.09  ? 64  ASP   A CB  1 
ATOM   174  C  CG  . ASP   A 1 21  ? -20.400 -5.581  -39.947 1.00 92.30  ? 64  ASP   A CG  1 
ATOM   175  O  OD1 . ASP   A 1 21  ? -19.346 -6.117  -40.407 1.00 99.71  ? 64  ASP   A OD1 1 
ATOM   176  O  OD2 . ASP   A 1 21  ? -21.559 -6.019  -40.151 1.00 95.10  ? 64  ASP   A OD2 1 
ATOM   177  N  N   . ALA   A 1 22  ? -19.363 -3.454  -35.481 1.00 74.09  ? 65  ALA   A N   1 
ATOM   178  C  CA  . ALA   A 1 22  ? -18.546 -2.519  -34.671 1.00 67.23  ? 65  ALA   A CA  1 
ATOM   179  C  C   . ALA   A 1 22  ? -17.012 -2.806  -35.056 1.00 64.46  ? 65  ALA   A C   1 
ATOM   180  O  O   . ALA   A 1 22  ? -16.593 -3.998  -35.435 1.00 64.86  ? 65  ALA   A O   1 
ATOM   181  C  CB  . ALA   A 1 22  ? -18.755 -2.729  -33.187 1.00 67.46  ? 65  ALA   A CB  1 
ATOM   182  N  N   . GLU   A 1 23  ? -16.293 -1.645  -34.931 1.00 62.85  ? 66  GLU   A N   1 
ATOM   183  C  CA  . GLU   A 1 23  ? -14.816 -1.566  -35.108 1.00 64.89  ? 66  GLU   A CA  1 
ATOM   184  C  C   . GLU   A 1 23  ? -14.223 -2.659  -34.212 1.00 63.53  ? 66  GLU   A C   1 
ATOM   185  O  O   . GLU   A 1 23  ? -14.520 -2.669  -32.981 1.00 57.17  ? 66  GLU   A O   1 
ATOM   186  C  CB  . GLU   A 1 23  ? -14.346 -0.166  -34.726 1.00 68.42  ? 66  GLU   A CB  1 
ATOM   187  C  CG  . GLU   A 1 23  ? -12.833 -0.008  -34.667 1.00 74.68  ? 66  GLU   A CG  1 
ATOM   188  C  CD  . GLU   A 1 23  ? -12.468 1.468   -34.583 1.00 82.83  ? 66  GLU   A CD  1 
ATOM   189  O  OE1 . GLU   A 1 23  ? -12.689 2.200   -35.594 1.00 87.74  ? 66  GLU   A OE1 1 
ATOM   190  O  OE2 . GLU   A 1 23  ? -12.016 1.902   -33.502 1.00 85.62  ? 66  GLU   A OE2 1 
ATOM   191  N  N   . VAL   A 1 24  ? -13.530 -3.633  -34.794 1.00 62.96  ? 67  VAL   A N   1 
ATOM   192  C  CA  . VAL   A 1 24  ? -13.039 -4.802  -34.013 1.00 62.46  ? 67  VAL   A CA  1 
ATOM   193  C  C   . VAL   A 1 24  ? -11.555 -4.548  -33.800 1.00 62.63  ? 67  VAL   A C   1 
ATOM   194  O  O   . VAL   A 1 24  ? -10.835 -4.598  -34.774 1.00 64.95  ? 67  VAL   A O   1 
ATOM   195  C  CB  . VAL   A 1 24  ? -13.330 -6.134  -34.727 1.00 64.06  ? 67  VAL   A CB  1 
ATOM   196  C  CG1 . VAL   A 1 24  ? -12.812 -7.302  -33.929 1.00 61.41  ? 67  VAL   A CG1 1 
ATOM   197  C  CG2 . VAL   A 1 24  ? -14.814 -6.310  -35.038 1.00 65.32  ? 67  VAL   A CG2 1 
ATOM   198  N  N   . THR   A 1 25  ? -11.122 -4.264  -32.567 1.00 61.82  ? 68  THR   A N   1 
ATOM   199  C  CA  . THR   A 1 25  ? -9.709  -3.913  -32.275 1.00 59.69  ? 68  THR   A CA  1 
ATOM   200  C  C   . THR   A 1 25  ? -9.333  -4.419  -30.887 1.00 58.23  ? 68  THR   A C   1 
ATOM   201  O  O   . THR   A 1 25  ? -10.149 -5.118  -30.268 1.00 57.23  ? 68  THR   A O   1 
ATOM   202  C  CB  . THR   A 1 25  ? -9.470  -2.408  -32.457 1.00 60.55  ? 68  THR   A CB  1 
ATOM   203  O  OG1 . THR   A 1 25  ? -8.085  -2.125  -32.316 1.00 62.39  ? 68  THR   A OG1 1 
ATOM   204  C  CG2 . THR   A 1 25  ? -10.197 -1.536  -31.470 1.00 59.52  ? 68  THR   A CG2 1 
ATOM   205  N  N   . GLY   A 1 26  ? -8.129  -4.070  -30.438 1.00 57.76  ? 69  GLY   A N   1 
ATOM   206  C  CA  . GLY   A 1 26  ? -7.577  -4.488  -29.146 1.00 56.60  ? 69  GLY   A CA  1 
ATOM   207  C  C   . GLY   A 1 26  ? -6.946  -5.864  -29.210 1.00 57.01  ? 69  GLY   A C   1 
ATOM   208  O  O   . GLY   A 1 26  ? -7.439  -6.727  -29.949 1.00 59.34  ? 69  GLY   A O   1 
ATOM   209  N  N   . ASN   A 1 27  ? -5.936  -6.078  -28.380 1.00 56.82  ? 70  ASN   A N   1 
ATOM   210  C  CA  . ASN   A 1 27  ? -5.302  -7.405  -28.167 1.00 57.01  ? 70  ASN   A CA  1 
ATOM   211  C  C   . ASN   A 1 27  ? -5.896  -8.061  -26.890 1.00 51.80  ? 70  ASN   A C   1 
ATOM   212  O  O   . ASN   A 1 27  ? -6.905  -7.506  -26.351 1.00 45.94  ? 70  ASN   A O   1 
ATOM   213  C  CB  . ASN   A 1 27  ? -3.786  -7.222  -28.261 1.00 60.44  ? 70  ASN   A CB  1 
ATOM   214  C  CG  . ASN   A 1 27  ? -3.191  -6.587  -27.021 1.00 61.73  ? 70  ASN   A CG  1 
ATOM   215  O  OD1 . ASN   A 1 27  ? -3.595  -5.510  -26.595 1.00 63.62  ? 70  ASN   A OD1 1 
ATOM   216  N  ND2 . ASN   A 1 27  ? -2.209  -7.249  -26.442 1.00 64.45  ? 70  ASN   A ND2 1 
ATOM   217  N  N   . SER   A 1 28  ? -5.399  -9.254  -26.515 1.00 49.17  ? 71  SER   A N   1 
ATOM   218  C  CA  . SER   A 1 28  ? -5.931  -10.173 -25.467 1.00 50.77  ? 71  SER   A CA  1 
ATOM   219  C  C   . SER   A 1 28  ? -4.788  -10.629 -24.585 1.00 52.02  ? 71  SER   A C   1 
ATOM   220  O  O   . SER   A 1 28  ? -4.499  -11.805 -24.561 1.00 54.77  ? 71  SER   A O   1 
ATOM   221  C  CB  . SER   A 1 28  ? -6.649  -11.388 -26.020 1.00 51.15  ? 71  SER   A CB  1 
ATOM   222  O  OG  . SER   A 1 28  ? -7.445  -11.046 -27.135 1.00 55.41  ? 71  SER   A OG  1 
ATOM   223  N  N   . PRO   A 1 29  ? -4.145  -9.725  -23.821 1.00 53.49  ? 72  PRO   A N   1 
ATOM   224  C  CA  . PRO   A 1 29  ? -2.957  -10.063 -23.049 1.00 53.89  ? 72  PRO   A CA  1 
ATOM   225  C  C   . PRO   A 1 29  ? -3.320  -10.890 -21.810 1.00 51.88  ? 72  PRO   A C   1 
ATOM   226  O  O   . PRO   A 1 29  ? -4.363  -10.645 -21.202 1.00 48.18  ? 72  PRO   A O   1 
ATOM   227  C  CB  . PRO   A 1 29  ? -2.374  -8.689  -22.672 1.00 55.55  ? 72  PRO   A CB  1 
ATOM   228  C  CG  . PRO   A 1 29  ? -3.619  -7.798  -22.531 1.00 54.36  ? 72  PRO   A CG  1 
ATOM   229  C  CD  . PRO   A 1 29  ? -4.600  -8.344  -23.557 1.00 54.34  ? 72  PRO   A CD  1 
ATOM   230  N  N   . ARG   A 1 30  ? -2.471  -11.860 -21.482 1.00 54.42  ? 73  ARG   A N   1 
ATOM   231  C  CA  . ARG   A 1 30  ? -2.565  -12.646 -20.214 1.00 59.30  ? 73  ARG   A CA  1 
ATOM   232  C  C   . ARG   A 1 30  ? -1.587  -12.045 -19.195 1.00 55.25  ? 73  ARG   A C   1 
ATOM   233  O  O   . ARG   A 1 30  ? -0.424  -12.053 -19.450 1.00 50.83  ? 73  ARG   A O   1 
ATOM   234  C  CB  . ARG   A 1 30  ? -2.332  -14.136 -20.472 1.00 66.49  ? 73  ARG   A CB  1 
ATOM   235  C  CG  . ARG   A 1 30  ? -3.383  -14.755 -21.391 1.00 74.11  ? 73  ARG   A CG  1 
ATOM   236  C  CD  . ARG   A 1 30  ? -2.913  -15.993 -22.168 1.00 84.49  ? 73  ARG   A CD  1 
ATOM   237  N  NE  . ARG   A 1 30  ? -3.990  -16.670 -22.915 1.00 87.82  ? 73  ARG   A NE  1 
ATOM   238  C  CZ  . ARG   A 1 30  ? -4.886  -17.518 -22.391 1.00 85.03  ? 73  ARG   A CZ  1 
ATOM   239  N  NH1 . ARG   A 1 30  ? -4.847  -17.814 -21.098 1.00 88.67  ? 73  ARG   A NH1 1 
ATOM   240  N  NH2 . ARG   A 1 30  ? -5.828  -18.053 -23.157 1.00 74.58  ? 73  ARG   A NH2 1 
ATOM   241  N  N   . LEU   A 1 31  ? -2.084  -11.480 -18.096 1.00 53.31  ? 74  LEU   A N   1 
ATOM   242  C  CA  . LEU   A 1 31  ? -1.286  -10.630 -17.183 1.00 52.72  ? 74  LEU   A CA  1 
ATOM   243  C  C   . LEU   A 1 31  ? -1.470  -11.141 -15.745 1.00 49.58  ? 74  LEU   A C   1 
ATOM   244  O  O   . LEU   A 1 31  ? -2.620  -11.321 -15.312 1.00 50.12  ? 74  LEU   A O   1 
ATOM   245  C  CB  . LEU   A 1 31  ? -1.756  -9.180  -17.339 1.00 54.20  ? 74  LEU   A CB  1 
ATOM   246  C  CG  . LEU   A 1 31  ? -1.442  -8.504  -18.679 1.00 54.69  ? 74  LEU   A CG  1 
ATOM   247  C  CD1 . LEU   A 1 31  ? -2.009  -7.099  -18.682 1.00 54.20  ? 74  LEU   A CD1 1 
ATOM   248  C  CD2 . LEU   A 1 31  ? 0.059   -8.454  -18.941 1.00 56.80  ? 74  LEU   A CD2 1 
ATOM   249  N  N   . ASP   A 1 32  ? -0.369  -11.410 -15.066 1.00 49.73  ? 75  ASP   A N   1 
ATOM   250  C  CA  . ASP   A 1 32  ? -0.324  -11.661 -13.604 1.00 50.87  ? 75  ASP   A CA  1 
ATOM   251  C  C   . ASP   A 1 32  ? -0.510  -10.370 -12.832 1.00 45.91  ? 75  ASP   A C   1 
ATOM   252  O  O   . ASP   A 1 32  ? 0.388   -9.479  -12.918 1.00 45.46  ? 75  ASP   A O   1 
ATOM   253  C  CB  . ASP   A 1 32  ? 1.039   -12.199 -13.190 1.00 54.96  ? 75  ASP   A CB  1 
ATOM   254  C  CG  . ASP   A 1 32  ? 1.242   -13.601 -13.706 1.00 58.54  ? 75  ASP   A CG  1 
ATOM   255  O  OD1 . ASP   A 1 32  ? 0.230   -14.375 -13.742 1.00 59.58  ? 75  ASP   A OD1 1 
ATOM   256  O  OD2 . ASP   A 1 32  ? 2.388   -13.895 -14.062 1.00 64.24  ? 75  ASP   A OD2 1 
ATOM   257  N  N   . VAL   A 1 33  ? -1.594  -10.286 -12.068 1.00 45.23  ? 76  VAL   A N   1 
ATOM   258  C  CA  . VAL   A 1 33  ? -1.916  -9.015  -11.372 1.00 44.84  ? 76  VAL   A CA  1 
ATOM   259  C  C   . VAL   A 1 33  ? -2.211  -9.321  -9.884  1.00 45.40  ? 76  VAL   A C   1 
ATOM   260  O  O   . VAL   A 1 33  ? -2.604  -10.485 -9.538  1.00 44.00  ? 76  VAL   A O   1 
ATOM   261  C  CB  . VAL   A 1 33  ? -3.067  -8.258  -12.071 1.00 44.47  ? 76  VAL   A CB  1 
ATOM   262  C  CG1 . VAL   A 1 33  ? -2.855  -8.105  -13.556 1.00 45.69  ? 76  VAL   A CG1 1 
ATOM   263  C  CG2 . VAL   A 1 33  ? -4.410  -8.915  -11.832 1.00 44.18  ? 76  VAL   A CG2 1 
ATOM   264  N  N   . ALA   A 1 34  ? -2.063  -8.288  -9.048  1.00 43.63  ? 77  ALA   A N   1 
ATOM   265  C  CA  . ALA   A 1 34  ? -2.492  -8.250  -7.634  1.00 42.48  ? 77  ALA   A CA  1 
ATOM   266  C  C   . ALA   A 1 34  ? -3.495  -7.101  -7.474  1.00 40.33  ? 77  ALA   A C   1 
ATOM   267  O  O   . ALA   A 1 34  ? -3.415  -6.168  -8.258  1.00 39.12  ? 77  ALA   A O   1 
ATOM   268  C  CB  . ALA   A 1 34  ? -1.304  -8.102  -6.746  1.00 43.81  ? 77  ALA   A CB  1 
ATOM   269  N  N   . LEU   A 1 35  ? -4.454  -7.279  -6.582  1.00 39.22  ? 78  LEU   A N   1 
ATOM   270  C  CA  . LEU   A 1 35  ? -5.519  -6.320  -6.224  1.00 40.09  ? 78  LEU   A CA  1 
ATOM   271  C  C   . LEU   A 1 35  ? -5.380  -6.005  -4.717  1.00 42.45  ? 78  LEU   A C   1 
ATOM   272  O  O   . LEU   A 1 35  ? -5.448  -6.969  -3.851  1.00 43.98  ? 78  LEU   A O   1 
ATOM   273  C  CB  . LEU   A 1 35  ? -6.862  -6.961  -6.574  1.00 38.94  ? 78  LEU   A CB  1 
ATOM   274  C  CG  . LEU   A 1 35  ? -8.097  -6.145  -6.185  1.00 38.58  ? 78  LEU   A CG  1 
ATOM   275  C  CD1 . LEU   A 1 35  ? -8.102  -4.808  -6.885  1.00 37.30  ? 78  LEU   A CD1 1 
ATOM   276  C  CD2 . LEU   A 1 35  ? -9.366  -6.911  -6.483  1.00 38.09  ? 78  LEU   A CD2 1 
ATOM   277  N  N   . ASP   A 1 36  ? -5.059  -4.752  -4.417  1.00 40.27  ? 79  ASP   A N   1 
ATOM   278  C  CA  . ASP   A 1 36  ? -4.776  -4.298  -3.043  1.00 41.13  ? 79  ASP   A CA  1 
ATOM   279  C  C   . ASP   A 1 36  ? -6.099  -3.850  -2.394  1.00 40.91  ? 79  ASP   A C   1 
ATOM   280  O  O   . ASP   A 1 36  ? -7.146  -3.799  -3.089  1.00 36.80  ? 79  ASP   A O   1 
ATOM   281  C  CB  . ASP   A 1 36  ? -3.670  -3.249  -3.052  1.00 42.19  ? 79  ASP   A CB  1 
ATOM   282  C  CG  . ASP   A 1 36  ? -4.094  -1.856  -3.480  1.00 43.48  ? 79  ASP   A CG  1 
ATOM   283  O  OD1 . ASP   A 1 36  ? -5.288  -1.650  -3.695  1.00 44.42  ? 79  ASP   A OD1 1 
ATOM   284  O  OD2 . ASP   A 1 36  ? -3.202  -0.984  -3.601  1.00 47.10  ? 79  ASP   A OD2 1 
ATOM   285  N  N   . GLU   A 1 37  ? -6.043  -3.534  -1.087  1.00 40.76  ? 80  GLU   A N   1 
ATOM   286  C  CA  . GLU   A 1 37  ? -7.243  -3.230  -0.304  1.00 41.47  ? 80  GLU   A CA  1 
ATOM   287  C  C   . GLU   A 1 37  ? -7.906  -1.949  -0.843  1.00 39.74  ? 80  GLU   A C   1 
ATOM   288  O  O   . GLU   A 1 37  ? -9.107  -1.802  -0.606  1.00 40.49  ? 80  GLU   A O   1 
ATOM   289  C  CB  . GLU   A 1 37  ? -6.806  -3.196  1.159   1.00 45.37  ? 80  GLU   A CB  1 
ATOM   290  C  CG  . GLU   A 1 37  ? -7.980  -3.220  2.100   1.00 47.99  ? 80  GLU   A CG  1 
ATOM   291  C  CD  . GLU   A 1 37  ? -7.589  -3.072  3.561   1.00 50.52  ? 80  GLU   A CD  1 
ATOM   292  O  OE1 . GLU   A 1 37  ? -7.348  -1.927  4.004   1.00 51.24  ? 80  GLU   A OE1 1 
ATOM   293  O  OE2 . GLU   A 1 37  ? -7.516  -4.109  4.233   1.00 52.00  ? 80  GLU   A OE2 1 
ATOM   294  N  N   . SER   A 1 38  ? -7.150  -1.058  -1.505  1.00 39.92  ? 81  SER   A N   1 
ATOM   295  C  CA  . SER   A 1 38  ? -7.622  0.222   -2.089  1.00 40.31  ? 81  SER   A CA  1 
ATOM   296  C  C   . SER   A 1 38  ? -8.252  -0.021  -3.451  1.00 38.83  ? 81  SER   A C   1 
ATOM   297  O  O   . SER   A 1 38  ? -8.683  0.974   -4.003  1.00 39.21  ? 81  SER   A O   1 
ATOM   298  C  CB  . SER   A 1 38  ? -6.534  1.235   -2.257  1.00 43.83  ? 81  SER   A CB  1 
ATOM   299  O  OG  . SER   A 1 38  ? -5.806  1.406   -1.053  1.00 48.82  ? 81  SER   A OG  1 
ATOM   300  N  N   . GLY   A 1 39  ? -8.330  -1.266  -3.958  1.00 37.57  ? 82  GLY   A N   1 
ATOM   301  C  CA  . GLY   A 1 39  ? -8.986  -1.559  -5.258  1.00 37.93  ? 82  GLY   A CA  1 
ATOM   302  C  C   . GLY   A 1 39  ? -8.120  -1.167  -6.454  1.00 37.60  ? 82  GLY   A C   1 
ATOM   303  O  O   . GLY   A 1 39  ? -8.653  -1.017  -7.533  1.00 36.68  ? 82  GLY   A O   1 
ATOM   304  N  N   . ASP   A 1 40  ? -6.813  -1.075  -6.256  1.00 40.21  ? 83  ASP   A N   1 
ATOM   305  C  CA  . ASP   A 1 40  ? -5.796  -0.802  -7.294  1.00 41.20  ? 83  ASP   A CA  1 
ATOM   306  C  C   . ASP   A 1 40  ? -5.179  -2.132  -7.702  1.00 41.66  ? 83  ASP   A C   1 
ATOM   307  O  O   . ASP   A 1 40  ? -4.590  -2.834  -6.845  1.00 39.49  ? 83  ASP   A O   1 
ATOM   308  C  CB  . ASP   A 1 40  ? -4.750  0.207   -6.805  1.00 43.99  ? 83  ASP   A CB  1 
ATOM   309  C  CG  . ASP   A 1 40  ? -5.348  1.592   -6.625  1.00 47.39  ? 83  ASP   A CG  1 
ATOM   310  O  OD1 . ASP   A 1 40  ? -6.290  1.925   -7.361  1.00 48.62  ? 83  ASP   A OD1 1 
ATOM   311  O  OD2 . ASP   A 1 40  ? -4.887  2.317   -5.746  1.00 51.05  ? 83  ASP   A OD2 1 
ATOM   312  N  N   . PHE   A 1 41  ? -5.276  -2.441  -8.985  1.00 40.94  ? 84  PHE   A N   1 
ATOM   313  C  CA  . PHE   A 1 41  ? -4.527  -3.561  -9.594  1.00 40.70  ? 84  PHE   A CA  1 
ATOM   314  C  C   . PHE   A 1 41  ? -3.077  -3.170  -9.791  1.00 43.49  ? 84  PHE   A C   1 
ATOM   315  O  O   . PHE   A 1 41  ? -2.823  -1.992  -10.017 1.00 46.32  ? 84  PHE   A O   1 
ATOM   316  C  CB  . PHE   A 1 41  ? -5.162  -3.928  -10.916 1.00 38.25  ? 84  PHE   A CB  1 
ATOM   317  C  CG  . PHE   A 1 41  ? -6.463  -4.667  -10.782 1.00 36.93  ? 84  PHE   A CG  1 
ATOM   318  C  CD1 . PHE   A 1 41  ? -6.452  -5.977  -10.363 1.00 35.42  ? 84  PHE   A CD1 1 
ATOM   319  C  CD2 . PHE   A 1 41  ? -7.691  -4.080  -11.128 1.00 35.16  ? 84  PHE   A CD2 1 
ATOM   320  C  CE1 . PHE   A 1 41  ? -7.636  -6.692  -10.292 1.00 35.19  ? 84  PHE   A CE1 1 
ATOM   321  C  CE2 . PHE   A 1 41  ? -8.868  -4.812  -11.064 1.00 33.90  ? 84  PHE   A CE2 1 
ATOM   322  C  CZ  . PHE   A 1 41  ? -8.833  -6.125  -10.679 1.00 33.11  ? 84  PHE   A CZ  1 
ATOM   323  N  N   . SER   A 1 42  ? -2.178  -4.147  -9.739  1.00 43.61  ? 85  SER   A N   1 
ATOM   324  C  CA  . SER   A 1 42  ? -0.740  -3.986  -10.037 1.00 46.45  ? 85  SER   A CA  1 
ATOM   325  C  C   . SER   A 1 42  ? -0.249  -5.227  -10.786 1.00 46.84  ? 85  SER   A C   1 
ATOM   326  O  O   . SER   A 1 42  ? -0.809  -6.357  -10.570 1.00 42.34  ? 85  SER   A O   1 
ATOM   327  C  CB  . SER   A 1 42  ? 0.035   -3.809  -8.765  1.00 50.41  ? 85  SER   A CB  1 
ATOM   328  O  OG  . SER   A 1 42  ? -0.230  -4.894  -7.874  1.00 50.34  ? 85  SER   A OG  1 
ATOM   329  N  N   . LEU   A 1 43  ? 0.748   -5.033  -11.639 1.00 50.88  ? 86  LEU   A N   1 
ATOM   330  C  CA  . LEU   A 1 43  ? 1.448   -6.155  -12.310 1.00 55.06  ? 86  LEU   A CA  1 
ATOM   331  C  C   . LEU   A 1 43  ? 2.347   -6.849  -11.299 1.00 57.50  ? 86  LEU   A C   1 
ATOM   332  O  O   . LEU   A 1 43  ? 3.194   -6.179  -10.685 1.00 57.72  ? 86  LEU   A O   1 
ATOM   333  C  CB  . LEU   A 1 43  ? 2.221   -5.600  -13.502 1.00 57.35  ? 86  LEU   A CB  1 
ATOM   334  C  CG  . LEU   A 1 43  ? 1.270   -5.093  -14.579 1.00 58.29  ? 86  LEU   A CG  1 
ATOM   335  C  CD1 . LEU   A 1 43  ? 1.840   -3.898  -15.324 1.00 61.25  ? 86  LEU   A CD1 1 
ATOM   336  C  CD2 . LEU   A 1 43  ? 0.891   -6.224  -15.522 1.00 59.90  ? 86  LEU   A CD2 1 
ATOM   337  N  N   . VAL   A 1 44  ? 2.120   -8.141  -11.114 1.00 61.51  ? 87  VAL   A N   1 
ATOM   338  C  CA  . VAL   A 1 44  ? 3.033   -9.058  -10.373 1.00 63.81  ? 87  VAL   A CA  1 
ATOM   339  C  C   . VAL   A 1 44  ? 4.098   -9.508  -11.374 1.00 69.69  ? 87  VAL   A C   1 
ATOM   340  O  O   . VAL   A 1 44  ? 3.735   -9.941  -12.493 1.00 73.26  ? 87  VAL   A O   1 
ATOM   341  C  CB  . VAL   A 1 44  ? 2.248   -10.262 -9.827  1.00 62.59  ? 87  VAL   A CB  1 
ATOM   342  C  CG1 . VAL   A 1 44  ? 3.171   -11.397 -9.385  1.00 62.72  ? 87  VAL   A CG1 1 
ATOM   343  C  CG2 . VAL   A 1 44  ? 1.280   -9.830  -8.730  1.00 61.50  ? 87  VAL   A CG2 1 
ATOM   344  N  N   . GLU   A 1 45  ? 5.365   -9.383  -11.036 1.00 75.84  ? 88  GLU   A N   1 
ATOM   345  C  CA  . GLU   A 1 45  ? 6.431   -9.866  -11.950 1.00 85.88  ? 88  GLU   A CA  1 
ATOM   346  C  C   . GLU   A 1 45  ? 7.406   -10.753 -11.166 1.00 86.68  ? 88  GLU   A C   1 
ATOM   347  O  O   . GLU   A 1 45  ? 7.042   -11.878 -10.822 1.00 86.98  ? 88  GLU   A O   1 
ATOM   348  C  CB  . GLU   A 1 45  ? 7.048   -8.648  -12.629 1.00 90.17  ? 88  GLU   A CB  1 
ATOM   349  C  CG  . GLU   A 1 45  ? 6.114   -7.987  -13.636 1.00 91.60  ? 88  GLU   A CG  1 
ATOM   350  C  CD  . GLU   A 1 45  ? 6.276   -8.504  -15.052 1.00 90.01  ? 88  GLU   A CD  1 
ATOM   351  O  OE1 . GLU   A 1 45  ? 6.415   -9.730  -15.222 1.00 89.41  ? 88  GLU   A OE1 1 
ATOM   352  O  OE2 . GLU   A 1 45  ? 6.325   -7.668  -15.966 1.00 90.47  ? 88  GLU   A OE2 1 
ATOM   353  N  N   . GLY   B 2 7   ? -35.758 12.286  -11.557 1.00 67.93  ? 16  GLY   B N   1 
ATOM   354  C  CA  . GLY   B 2 7   ? -35.455 12.536  -13.011 1.00 68.24  ? 16  GLY   B CA  1 
ATOM   355  C  C   . GLY   B 2 7   ? -35.462 11.261  -13.866 1.00 65.59  ? 16  GLY   B C   1 
ATOM   356  O  O   . GLY   B 2 7   ? -36.347 10.382  -13.672 1.00 65.80  ? 16  GLY   B O   1 
ATOM   357  N  N   . GLU   B 2 8   ? -34.515 11.149  -14.799 1.00 58.82  ? 17  GLU   B N   1 
ATOM   358  C  CA  . GLU   B 2 8   ? -34.560 10.160  -15.907 1.00 55.71  ? 17  GLU   B CA  1 
ATOM   359  C  C   . GLU   B 2 8   ? -34.183 8.762   -15.388 1.00 53.38  ? 17  GLU   B C   1 
ATOM   360  O  O   . GLU   B 2 8   ? -33.100 8.586   -14.859 1.00 51.85  ? 17  GLU   B O   1 
ATOM   361  C  CB  . GLU   B 2 8   ? -33.619 10.599  -17.024 1.00 55.55  ? 17  GLU   B CB  1 
ATOM   362  C  CG  . GLU   B 2 8   ? -33.806 9.789   -18.283 1.00 55.69  ? 17  GLU   B CG  1 
ATOM   363  C  CD  . GLU   B 2 8   ? -33.051 10.350  -19.475 1.00 58.25  ? 17  GLU   B CD  1 
ATOM   364  O  OE1 . GLU   B 2 8   ? -32.070 11.139  -19.243 1.00 55.77  ? 17  GLU   B OE1 1 
ATOM   365  O  OE2 . GLU   B 2 8   ? -33.486 10.038  -20.638 1.00 61.10  ? 17  GLU   B OE2 1 
ATOM   366  N  N   A THR   B 2 9   ? -35.065 7.777   -15.561 0.25 52.90  ? 18  THR   B N   1 
ATOM   367  N  N   B THR   B 2 9   ? -35.097 7.805   -15.567 0.25 52.57  ? 18  THR   B N   1 
ATOM   368  N  N   C THR   B 2 9   ? -35.065 7.777   -15.561 0.25 52.90  ? 18  THR   B N   1 
ATOM   369  N  N   D THR   B 2 9   ? -35.097 7.805   -15.567 0.25 52.57  ? 18  THR   B N   1 
ATOM   370  C  CA  A THR   B 2 9   ? -34.897 6.418   -14.984 0.25 52.65  ? 18  THR   B CA  1 
ATOM   371  C  CA  B THR   B 2 9   ? -35.047 6.442   -14.980 0.25 52.05  ? 18  THR   B CA  1 
ATOM   372  C  CA  C THR   B 2 9   ? -34.897 6.418   -14.984 0.25 52.65  ? 18  THR   B CA  1 
ATOM   373  C  CA  D THR   B 2 9   ? -35.047 6.442   -14.980 0.25 52.05  ? 18  THR   B CA  1 
ATOM   374  C  C   A THR   B 2 9   ? -34.911 5.351   -16.078 0.25 52.20  ? 18  THR   B C   1 
ATOM   375  C  C   B THR   B 2 9   ? -34.811 5.393   -16.073 0.25 51.86  ? 18  THR   B C   1 
ATOM   376  C  C   C THR   B 2 9   ? -34.911 5.351   -16.078 0.25 52.20  ? 18  THR   B C   1 
ATOM   377  C  C   D THR   B 2 9   ? -34.811 5.393   -16.073 0.25 51.86  ? 18  THR   B C   1 
ATOM   378  O  O   A THR   B 2 9   ? -34.812 4.163   -15.714 0.25 52.70  ? 18  THR   B O   1 
ATOM   379  O  O   B THR   B 2 9   ? -34.399 4.273   -15.707 0.25 52.19  ? 18  THR   B O   1 
ATOM   380  O  O   C THR   B 2 9   ? -34.812 4.163   -15.714 0.25 52.70  ? 18  THR   B O   1 
ATOM   381  O  O   D THR   B 2 9   ? -34.399 4.273   -15.707 0.25 52.19  ? 18  THR   B O   1 
ATOM   382  C  CB  A THR   B 2 9   ? -35.978 6.143   -13.933 0.25 53.46  ? 18  THR   B CB  1 
ATOM   383  C  CB  B THR   B 2 9   ? -36.324 6.155   -14.174 0.25 52.33  ? 18  THR   B CB  1 
ATOM   384  C  CB  C THR   B 2 9   ? -35.978 6.143   -13.933 0.25 53.46  ? 18  THR   B CB  1 
ATOM   385  C  CB  D THR   B 2 9   ? -36.324 6.155   -14.174 0.25 52.33  ? 18  THR   B CB  1 
ATOM   386  O  OG1 A THR   B 2 9   ? -36.182 7.382   -13.257 0.25 53.94  ? 18  THR   B OG1 1 
ATOM   387  O  OG1 B THR   B 2 9   ? -37.462 6.536   -14.946 0.25 52.32  ? 18  THR   B OG1 1 
ATOM   388  O  OG1 C THR   B 2 9   ? -36.182 7.382   -13.257 0.25 53.94  ? 18  THR   B OG1 1 
ATOM   389  O  OG1 D THR   B 2 9   ? -37.462 6.536   -14.946 0.25 52.32  ? 18  THR   B OG1 1 
ATOM   390  C  CG2 A THR   B 2 9   ? -35.596 5.044   -12.962 0.25 53.74  ? 18  THR   B CG2 1 
ATOM   391  C  CG2 B THR   B 2 9   ? -36.364 6.886   -12.851 0.25 52.80  ? 18  THR   B CG2 1 
ATOM   392  C  CG2 C THR   B 2 9   ? -35.596 5.044   -12.962 0.25 53.74  ? 18  THR   B CG2 1 
ATOM   393  C  CG2 D THR   B 2 9   ? -36.364 6.886   -12.851 0.25 52.80  ? 18  THR   B CG2 1 
ATOM   394  N  N   . THR   B 2 10  ? -35.016 5.748   -17.351 1.00 51.10  ? 19  THR   B N   1 
ATOM   395  C  CA  . THR   B 2 10  ? -34.922 4.817   -18.493 1.00 49.15  ? 19  THR   B CA  1 
ATOM   396  C  C   . THR   B 2 10  ? -33.591 4.045   -18.439 1.00 44.68  ? 19  THR   B C   1 
ATOM   397  O  O   . THR   B 2 10  ? -32.509 4.645   -18.299 1.00 43.30  ? 19  THR   B O   1 
ATOM   398  C  CB  . THR   B 2 10  ? -35.097 5.538   -19.846 1.00 51.18  ? 19  THR   B CB  1 
ATOM   399  O  OG1 . THR   B 2 10  ? -36.012 6.632   -19.742 1.00 56.41  ? 19  THR   B OG1 1 
ATOM   400  C  CG2 . THR   B 2 10  ? -35.653 4.620   -20.906 1.00 52.64  ? 19  THR   B CG2 1 
ATOM   401  N  N   . ASP   B 2 11  ? -33.666 2.753   -18.650 1.00 42.03  ? 20  ASP   B N   1 
ATOM   402  C  CA  . ASP   B 2 11  ? -32.468 1.927   -18.882 1.00 42.66  ? 20  ASP   B CA  1 
ATOM   403  C  C   . ASP   B 2 11  ? -31.550 2.560   -19.935 1.00 44.31  ? 20  ASP   B C   1 
ATOM   404  O  O   . ASP   B 2 11  ? -32.050 3.283   -20.835 1.00 43.73  ? 20  ASP   B O   1 
ATOM   405  C  CB  . ASP   B 2 11  ? -32.870 0.532   -19.310 1.00 44.18  ? 20  ASP   B CB  1 
ATOM   406  C  CG  . ASP   B 2 11  ? -33.478 -0.352  -18.231 1.00 45.88  ? 20  ASP   B CG  1 
ATOM   407  O  OD1 . ASP   B 2 11  ? -33.715 0.123   -17.134 1.00 43.03  ? 20  ASP   B OD1 1 
ATOM   408  O  OD2 . ASP   B 2 11  ? -33.699 -1.554  -18.543 1.00 50.54  ? 20  ASP   B OD2 1 
ATOM   409  N  N   . GLY   B 2 12  ? -30.257 2.234   -19.863 1.00 41.90  ? 21  GLY   B N   1 
ATOM   410  C  CA  . GLY   B 2 12  ? -29.227 2.602   -20.842 1.00 40.47  ? 21  GLY   B CA  1 
ATOM   411  C  C   . GLY   B 2 12  ? -27.993 3.139   -20.168 1.00 38.81  ? 21  GLY   B C   1 
ATOM   412  O  O   . GLY   B 2 12  ? -27.855 2.984   -18.952 1.00 35.15  ? 21  GLY   B O   1 
ATOM   413  N  N   . VAL   B 2 13  ? -27.117 3.747   -20.951 1.00 38.63  ? 22  VAL   B N   1 
ATOM   414  C  CA  . VAL   B 2 13  ? -25.777 4.231   -20.515 1.00 37.65  ? 22  VAL   B CA  1 
ATOM   415  C  C   . VAL   B 2 13  ? -25.846 5.742   -20.331 1.00 38.18  ? 22  VAL   B C   1 
ATOM   416  O  O   . VAL   B 2 13  ? -26.566 6.448   -21.124 1.00 40.01  ? 22  VAL   B O   1 
ATOM   417  C  CB  . VAL   B 2 13  ? -24.673 3.753   -21.463 1.00 37.62  ? 22  VAL   B CB  1 
ATOM   418  C  CG1 . VAL   B 2 13  ? -24.769 4.263   -22.933 1.00 37.93  ? 22  VAL   B CG1 1 
ATOM   419  C  CG2 . VAL   B 2 13  ? -23.289 4.028   -20.910 1.00 38.35  ? 22  VAL   B CG2 1 
ATOM   420  N  N   . TYR   B 2 14  ? -25.182 6.241   -19.294 1.00 36.86  ? 23  TYR   B N   1 
ATOM   421  C  CA  . TYR   B 2 14  ? -25.239 7.665   -18.914 1.00 36.94  ? 23  TYR   B CA  1 
ATOM   422  C  C   . TYR   B 2 14  ? -23.831 8.167   -18.680 1.00 37.70  ? 23  TYR   B C   1 
ATOM   423  O  O   . TYR   B 2 14  ? -22.935 7.382   -18.226 1.00 38.72  ? 23  TYR   B O   1 
ATOM   424  C  CB  . TYR   B 2 14  ? -26.064 7.893   -17.662 1.00 36.25  ? 23  TYR   B CB  1 
ATOM   425  C  CG  . TYR   B 2 14  ? -27.529 7.654   -17.814 1.00 35.72  ? 23  TYR   B CG  1 
ATOM   426  C  CD1 . TYR   B 2 14  ? -28.018 6.409   -18.137 1.00 35.12  ? 23  TYR   B CD1 1 
ATOM   427  C  CD2 . TYR   B 2 14  ? -28.412 8.711   -17.653 1.00 36.74  ? 23  TYR   B CD2 1 
ATOM   428  C  CE1 . TYR   B 2 14  ? -29.372 6.185   -18.258 1.00 35.99  ? 23  TYR   B CE1 1 
ATOM   429  C  CE2 . TYR   B 2 14  ? -29.781 8.511   -17.753 1.00 37.27  ? 23  TYR   B CE2 1 
ATOM   430  C  CZ  . TYR   B 2 14  ? -30.253 7.252   -18.073 1.00 38.06  ? 23  TYR   B CZ  1 
ATOM   431  O  OH  . TYR   B 2 14  ? -31.596 7.093   -18.173 1.00 40.87  ? 23  TYR   B OH  1 
ATOM   432  N  N   . ARG   B 2 15  ? -23.640 9.450   -18.957 1.00 37.35  ? 24  ARG   B N   1 
ATOM   433  C  CA  . ARG   B 2 15  ? -22.390 10.169  -18.605 1.00 37.41  ? 24  ARG   B CA  1 
ATOM   434  C  C   . ARG   B 2 15  ? -22.503 10.600  -17.147 1.00 36.98  ? 24  ARG   B C   1 
ATOM   435  O  O   . ARG   B 2 15  ? -23.612 11.000  -16.748 1.00 35.41  ? 24  ARG   B O   1 
ATOM   436  C  CB  . ARG   B 2 15  ? -22.149 11.379  -19.520 1.00 38.85  ? 24  ARG   B CB  1 
ATOM   437  C  CG  . ARG   B 2 15  ? -22.161 11.060  -21.014 1.00 39.89  ? 24  ARG   B CG  1 
ATOM   438  C  CD  . ARG   B 2 15  ? -21.998 12.315  -21.863 1.00 41.68  ? 24  ARG   B CD  1 
ATOM   439  N  NE  . ARG   B 2 15  ? -22.196 11.998  -23.286 1.00 41.56  ? 24  ARG   B NE  1 
ATOM   440  C  CZ  . ARG   B 2 15  ? -21.252 11.631  -24.145 1.00 43.83  ? 24  ARG   B CZ  1 
ATOM   441  N  NH1 . ARG   B 2 15  ? -19.981 11.603  -23.789 1.00 43.48  ? 24  ARG   B NH1 1 
ATOM   442  N  NH2 . ARG   B 2 15  ? -21.581 11.291  -25.386 1.00 45.82  ? 24  ARG   B NH2 1 
ATOM   443  N  N   . VAL   B 2 16  ? -21.382 10.623  -16.440 1.00 36.56  ? 25  VAL   B N   1 
ATOM   444  C  CA  . VAL   B 2 16  ? -21.307 11.231  -15.095 1.00 38.03  ? 25  VAL   B CA  1 
ATOM   445  C  C   . VAL   B 2 16  ? -20.443 12.478  -15.208 1.00 37.55  ? 25  VAL   B C   1 
ATOM   446  O  O   . VAL   B 2 16  ? -19.310 12.359  -15.562 1.00 38.13  ? 25  VAL   B O   1 
ATOM   447  C  CB  . VAL   B 2 16  ? -20.755 10.213  -14.058 1.00 38.99  ? 25  VAL   B CB  1 
ATOM   448  C  CG1 . VAL   B 2 16  ? -20.736 10.823  -12.660 1.00 39.37  ? 25  VAL   B CG1 1 
ATOM   449  C  CG2 . VAL   B 2 16  ? -21.561 8.913   -14.094 1.00 38.74  ? 25  VAL   B CG2 1 
ATOM   450  N  N   . MET   B 2 17  ? -21.031 13.622  -14.916 1.00 39.78  ? 26  MET   B N   1 
ATOM   451  C  CA  . MET   B 2 17  ? -20.464 14.971  -15.118 1.00 42.21  ? 26  MET   B CA  1 
ATOM   452  C  C   . MET   B 2 17  ? -20.316 15.667  -13.762 1.00 43.69  ? 26  MET   B C   1 
ATOM   453  O  O   . MET   B 2 17  ? -21.127 15.380  -12.832 1.00 41.91  ? 26  MET   B O   1 
ATOM   454  C  CB  . MET   B 2 17  ? -21.418 15.825  -15.951 1.00 43.21  ? 26  MET   B CB  1 
ATOM   455  C  CG  . MET   B 2 17  ? -21.901 15.162  -17.236 1.00 44.70  ? 26  MET   B CG  1 
ATOM   456  S  SD  . MET   B 2 17  ? -20.622 14.834  -18.483 1.00 45.78  ? 26  MET   B SD  1 
ATOM   457  C  CE  . MET   B 2 17  ? -20.110 16.518  -18.837 1.00 48.51  ? 26  MET   B CE  1 
ATOM   458  N  N   . THR   B 2 18  ? -19.399 16.626  -13.725 1.00 45.36  ? 27  THR   B N   1 
ATOM   459  C  CA  . THR   B 2 18  ? -19.214 17.597  -12.635 1.00 49.97  ? 27  THR   B CA  1 
ATOM   460  C  C   . THR   B 2 18  ? -19.046 19.018  -13.215 1.00 52.98  ? 27  THR   B C   1 
ATOM   461  O  O   . THR   B 2 18  ? -18.441 19.166  -14.324 1.00 47.93  ? 27  THR   B O   1 
ATOM   462  C  CB  . THR   B 2 18  ? -18.042 17.153  -11.754 1.00 48.26  ? 27  THR   B CB  1 
ATOM   463  O  OG1 . THR   B 2 18  ? -18.019 18.100  -10.677 1.00 48.97  ? 27  THR   B OG1 1 
ATOM   464  C  CG2 . THR   B 2 18  ? -16.732 17.063  -12.509 1.00 49.23  ? 27  THR   B CG2 1 
ATOM   465  N  N   . ARG   B 2 19  ? -19.469 20.017  -12.435 1.00 57.83  ? 28  ARG   B N   1 
ATOM   466  C  CA  . ARG   B 2 19  ? -19.210 21.460  -12.705 1.00 66.64  ? 28  ARG   B CA  1 
ATOM   467  C  C   . ARG   B 2 19  ? -18.202 22.055  -11.702 1.00 66.24  ? 28  ARG   B C   1 
ATOM   468  O  O   . ARG   B 2 19  ? -17.902 23.260  -11.802 1.00 65.96  ? 28  ARG   B O   1 
ATOM   469  C  CB  . ARG   B 2 19  ? -20.544 22.212  -12.729 1.00 69.73  ? 28  ARG   B CB  1 
ATOM   470  C  CG  . ARG   B 2 19  ? -21.370 21.861  -13.960 1.00 74.97  ? 28  ARG   B CG  1 
ATOM   471  C  CD  . ARG   B 2 19  ? -22.023 23.032  -14.667 1.00 76.96  ? 28  ARG   B CD  1 
ATOM   472  N  NE  . ARG   B 2 19  ? -23.137 22.589  -15.497 1.00 78.91  ? 28  ARG   B NE  1 
ATOM   473  C  CZ  . ARG   B 2 19  ? -24.330 22.215  -15.039 1.00 82.40  ? 28  ARG   B CZ  1 
ATOM   474  N  NH1 . ARG   B 2 19  ? -24.584 22.219  -13.736 1.00 85.36  ? 28  ARG   B NH1 1 
ATOM   475  N  NH2 . ARG   B 2 19  ? -25.269 21.833  -15.889 1.00 82.95  ? 28  ARG   B NH2 1 
ATOM   476  N  N   . ARG   B 2 20  ? -17.619 21.233  -10.840 1.00 67.95  ? 29  ARG   B N   1 
ATOM   477  C  CA  . ARG   B 2 20  ? -16.723 21.675  -9.735  1.00 74.04  ? 29  ARG   B CA  1 
ATOM   478  C  C   . ARG   B 2 20  ? -15.352 22.069  -10.313 1.00 71.93  ? 29  ARG   B C   1 
ATOM   479  O  O   . ARG   B 2 20  ? -14.496 22.593  -9.569  1.00 70.60  ? 29  ARG   B O   1 
ATOM   480  C  CB  . ARG   B 2 20  ? -16.637 20.545  -8.701  1.00 77.74  ? 29  ARG   B CB  1 
ATOM   481  C  CG  . ARG   B 2 20  ? -16.477 20.993  -7.257  1.00 84.53  ? 29  ARG   B CG  1 
ATOM   482  C  CD  . ARG   B 2 20  ? -16.189 19.768  -6.402  1.00 94.29  ? 29  ARG   B CD  1 
ATOM   483  N  NE  . ARG   B 2 20  ? -15.171 18.928  -7.047  1.00 100.74 ? 29  ARG   B NE  1 
ATOM   484  C  CZ  . ARG   B 2 20  ? -13.850 18.985  -6.830  1.00 103.69 ? 29  ARG   B CZ  1 
ATOM   485  N  NH1 . ARG   B 2 20  ? -13.338 19.828  -5.946  1.00 105.94 ? 29  ARG   B NH1 1 
ATOM   486  N  NH2 . ARG   B 2 20  ? -13.035 18.187  -7.503  1.00 103.29 ? 29  ARG   B NH2 1 
ATOM   487  N  N   . LEU   B 2 21  ? -15.124 21.791  -11.595 1.00 69.38  ? 30  LEU   B N   1 
ATOM   488  C  CA  . LEU   B 2 21  ? -13.878 22.156  -12.311 1.00 66.37  ? 30  LEU   B CA  1 
ATOM   489  C  C   . LEU   B 2 21  ? -14.241 23.133  -13.423 1.00 62.22  ? 30  LEU   B C   1 
ATOM   490  O  O   . LEU   B 2 21  ? -15.340 23.716  -13.355 1.00 60.24  ? 30  LEU   B O   1 
ATOM   491  C  CB  . LEU   B 2 21  ? -13.226 20.879  -12.830 1.00 68.12  ? 30  LEU   B CB  1 
ATOM   492  C  CG  . LEU   B 2 21  ? -12.204 20.225  -11.909 1.00 70.55  ? 30  LEU   B CG  1 
ATOM   493  C  CD1 . LEU   B 2 21  ? -12.457 20.521  -10.440 1.00 73.12  ? 30  LEU   B CD1 1 
ATOM   494  C  CD2 . LEU   B 2 21  ? -12.180 18.727  -12.153 1.00 70.62  ? 30  LEU   B CD2 1 
ATOM   495  N  N   . LEU   B 2 22  ? -13.327 23.357  -14.367 1.00 61.80  ? 31  LEU   B N   1 
ATOM   496  C  CA  . LEU   B 2 22  ? -13.568 24.259  -15.519 1.00 59.98  ? 31  LEU   B CA  1 
ATOM   497  C  C   . LEU   B 2 22  ? -14.695 23.681  -16.365 1.00 58.16  ? 31  LEU   B C   1 
ATOM   498  O  O   . LEU   B 2 22  ? -14.720 22.448  -16.519 1.00 61.42  ? 31  LEU   B O   1 
ATOM   499  C  CB  . LEU   B 2 22  ? -12.287 24.365  -16.329 1.00 59.76  ? 31  LEU   B CB  1 
ATOM   500  C  CG  . LEU   B 2 22  ? -12.292 25.490  -17.347 1.00 59.22  ? 31  LEU   B CG  1 
ATOM   501  C  CD1 . LEU   B 2 22  ? -12.122 26.849  -16.677 1.00 58.59  ? 31  LEU   B CD1 1 
ATOM   502  C  CD2 . LEU   B 2 22  ? -11.213 25.232  -18.395 1.00 58.62  ? 31  LEU   B CD2 1 
ATOM   503  N  N   . GLY   B 2 23  ? -15.587 24.528  -16.879 1.00 56.61  ? 32  GLY   B N   1 
ATOM   504  C  CA  . GLY   B 2 23  ? -16.782 24.086  -17.624 1.00 52.98  ? 32  GLY   B CA  1 
ATOM   505  C  C   . GLY   B 2 23  ? -17.481 22.896  -16.949 1.00 51.63  ? 32  GLY   B C   1 
ATOM   506  O  O   . GLY   B 2 23  ? -17.558 22.827  -15.700 1.00 50.12  ? 32  GLY   B O   1 
ATOM   507  N  N   . SER   B 2 24  ? -18.040 22.015  -17.767 1.00 49.69  ? 33  SER   B N   1 
ATOM   508  C  CA  . SER   B 2 24  ? -18.695 20.746  -17.373 1.00 48.03  ? 33  SER   B CA  1 
ATOM   509  C  C   . SER   B 2 24  ? -17.729 19.630  -17.750 1.00 46.68  ? 33  SER   B C   1 
ATOM   510  O  O   . SER   B 2 24  ? -17.447 19.569  -18.909 1.00 44.55  ? 33  SER   B O   1 
ATOM   511  C  CB  . SER   B 2 24  ? -19.984 20.603  -18.090 1.00 47.22  ? 33  SER   B CB  1 
ATOM   512  O  OG  . SER   B 2 24  ? -20.929 21.531  -17.569 1.00 48.35  ? 33  SER   B OG  1 
ATOM   513  N  N   . THR   B 2 25  ? -17.274 18.810  -16.805 1.00 45.24  ? 34  THR   B N   1 
ATOM   514  C  CA  . THR   B 2 25  ? -16.212 17.793  -17.011 1.00 46.07  ? 34  THR   B CA  1 
ATOM   515  C  C   . THR   B 2 25  ? -16.802 16.400  -16.799 1.00 45.56  ? 34  THR   B C   1 
ATOM   516  O  O   . THR   B 2 25  ? -17.577 16.212  -15.811 1.00 43.51  ? 34  THR   B O   1 
ATOM   517  C  CB  . THR   B 2 25  ? -15.002 18.049  -16.103 1.00 47.07  ? 34  THR   B CB  1 
ATOM   518  O  OG1 . THR   B 2 25  ? -14.534 19.393  -16.301 1.00 48.05  ? 34  THR   B OG1 1 
ATOM   519  C  CG2 . THR   B 2 25  ? -13.877 17.067  -16.364 1.00 46.17  ? 34  THR   B CG2 1 
ATOM   520  N  N   . GLN   B 2 26  ? -16.513 15.483  -17.724 1.00 44.66  ? 35  GLN   B N   1 
ATOM   521  C  CA  . GLN   B 2 26  ? -17.052 14.106  -17.626 1.00 43.86  ? 35  GLN   B CA  1 
ATOM   522  C  C   . GLN   B 2 26  ? -16.048 13.331  -16.771 1.00 44.93  ? 35  GLN   B C   1 
ATOM   523  O  O   . GLN   B 2 26  ? -14.895 13.158  -17.223 1.00 45.05  ? 35  GLN   B O   1 
ATOM   524  C  CB  . GLN   B 2 26  ? -17.228 13.403  -18.970 1.00 42.24  ? 35  GLN   B CB  1 
ATOM   525  C  CG  . GLN   B 2 26  ? -17.829 11.999  -18.846 1.00 41.17  ? 35  GLN   B CG  1 
ATOM   526  C  CD  . GLN   B 2 26  ? -18.133 11.344  -20.174 1.00 40.76  ? 35  GLN   B CD  1 
ATOM   527  O  OE1 . GLN   B 2 26  ? -18.810 11.929  -20.999 1.00 39.43  ? 35  GLN   B OE1 1 
ATOM   528  N  NE2 . GLN   B 2 26  ? -17.650 10.127  -20.409 1.00 38.75  ? 35  GLN   B NE2 1 
ATOM   529  N  N   . VAL   B 2 27  ? -16.468 12.877  -15.599 1.00 42.99  ? 36  VAL   B N   1 
ATOM   530  C  CA  . VAL   B 2 27  ? -15.565 12.130  -14.680 1.00 41.81  ? 36  VAL   B CA  1 
ATOM   531  C  C   . VAL   B 2 27  ? -15.781 10.629  -14.913 1.00 39.39  ? 36  VAL   B C   1 
ATOM   532  O  O   . VAL   B 2 27  ? -14.895 9.842   -14.611 1.00 38.60  ? 36  VAL   B O   1 
ATOM   533  C  CB  . VAL   B 2 27  ? -15.801 12.553  -13.220 1.00 43.38  ? 36  VAL   B CB  1 
ATOM   534  C  CG1 . VAL   B 2 27  ? -15.354 13.977  -12.963 1.00 45.52  ? 36  VAL   B CG1 1 
ATOM   535  C  CG2 . VAL   B 2 27  ? -17.231 12.369  -12.770 1.00 42.35  ? 36  VAL   B CG2 1 
ATOM   536  N  N   . GLY   B 2 28  ? -16.923 10.212  -15.449 1.00 38.33  ? 37  GLY   B N   1 
ATOM   537  C  CA  . GLY   B 2 28  ? -17.076 8.809   -15.896 1.00 35.54  ? 37  GLY   B CA  1 
ATOM   538  C  C   . GLY   B 2 28  ? -18.435 8.550   -16.512 1.00 35.77  ? 37  GLY   B C   1 
ATOM   539  O  O   . GLY   B 2 28  ? -19.074 9.506   -17.003 1.00 37.03  ? 37  GLY   B O   1 
ATOM   540  N  N   . VAL   B 2 29  ? -18.885 7.295   -16.451 1.00 34.62  ? 38  VAL   B N   1 
ATOM   541  C  CA  . VAL   B 2 29  ? -20.034 6.691   -17.172 1.00 33.97  ? 38  VAL   B CA  1 
ATOM   542  C  C   . VAL   B 2 29  ? -20.691 5.691   -16.235 1.00 33.88  ? 38  VAL   B C   1 
ATOM   543  O  O   . VAL   B 2 29  ? -19.997 5.234   -15.318 1.00 32.12  ? 38  VAL   B O   1 
ATOM   544  C  CB  . VAL   B 2 29  ? -19.543 5.985   -18.446 1.00 36.02  ? 38  VAL   B CB  1 
ATOM   545  C  CG1 . VAL   B 2 29  ? -20.640 5.250   -19.200 1.00 36.50  ? 38  VAL   B CG1 1 
ATOM   546  C  CG2 . VAL   B 2 29  ? -18.794 6.912   -19.359 1.00 36.19  ? 38  VAL   B CG2 1 
ATOM   547  N  N   . GLY   B 2 30  ? -21.957 5.354   -16.475 1.00 32.75  ? 39  GLY   B N   1 
ATOM   548  C  CA  . GLY   B 2 30  ? -22.694 4.353   -15.710 1.00 31.87  ? 39  GLY   B CA  1 
ATOM   549  C  C   . GLY   B 2 30  ? -23.803 3.730   -16.487 1.00 31.77  ? 39  GLY   B C   1 
ATOM   550  O  O   . GLY   B 2 30  ? -24.084 4.195   -17.624 1.00 33.14  ? 39  GLY   B O   1 
ATOM   551  N  N   . VAL   B 2 31  ? -24.428 2.742   -15.877 1.00 31.40  ? 40  VAL   B N   1 
ATOM   552  C  CA  . VAL   B 2 31  ? -25.501 1.891   -16.437 1.00 32.46  ? 40  VAL   B CA  1 
ATOM   553  C  C   . VAL   B 2 31  ? -26.717 1.994   -15.569 1.00 33.54  ? 40  VAL   B C   1 
ATOM   554  O  O   . VAL   B 2 31  ? -26.610 1.795   -14.319 1.00 32.74  ? 40  VAL   B O   1 
ATOM   555  C  CB  . VAL   B 2 31  ? -25.124 0.416   -16.529 1.00 33.94  ? 40  VAL   B CB  1 
ATOM   556  C  CG1 . VAL   B 2 31  ? -26.290 -0.415  -17.036 1.00 35.36  ? 40  VAL   B CG1 1 
ATOM   557  C  CG2 . VAL   B 2 31  ? -23.908 0.247   -17.378 1.00 34.21  ? 40  VAL   B CG2 1 
ATOM   558  N  N   . MET   B 2 32  ? -27.822 2.372   -16.193 1.00 33.58  ? 41  MET   B N   1 
ATOM   559  C  CA  . MET   B 2 32  ? -29.130 2.405   -15.541 1.00 34.85  ? 41  MET   B CA  1 
ATOM   560  C  C   . MET   B 2 32  ? -29.852 1.125   -15.966 1.00 35.27  ? 41  MET   B C   1 
ATOM   561  O  O   . MET   B 2 32  ? -30.007 0.871   -17.167 1.00 34.61  ? 41  MET   B O   1 
ATOM   562  C  CB  . MET   B 2 32  ? -29.909 3.653   -15.969 1.00 36.28  ? 41  MET   B CB  1 
ATOM   563  C  CG  . MET   B 2 32  ? -31.194 3.882   -15.144 1.00 37.09  ? 41  MET   B CG  1 
ATOM   564  S  SD  . MET   B 2 32  ? -30.917 4.460   -13.414 1.00 38.52  ? 41  MET   B SD  1 
ATOM   565  C  CE  . MET   B 2 32  ? -30.165 6.049   -13.758 1.00 41.82  ? 41  MET   B CE  1 
ATOM   566  N  N   . GLN   B 2 33  ? -30.222 0.298   -15.006 1.00 36.70  ? 42  GLN   B N   1 
ATOM   567  C  CA  . GLN   B 2 33  ? -30.944 -0.957  -15.265 1.00 38.35  ? 42  GLN   B CA  1 
ATOM   568  C  C   . GLN   B 2 33  ? -31.843 -1.206  -14.084 1.00 39.46  ? 42  GLN   B C   1 
ATOM   569  O  O   . GLN   B 2 33  ? -31.373 -1.044  -12.949 1.00 39.37  ? 42  GLN   B O   1 
ATOM   570  C  CB  . GLN   B 2 33  ? -30.004 -2.145  -15.506 1.00 38.76  ? 42  GLN   B CB  1 
ATOM   571  C  CG  . GLN   B 2 33  ? -30.805 -3.358  -15.937 1.00 41.53  ? 42  GLN   B CG  1 
ATOM   572  C  CD  . GLN   B 2 33  ? -29.943 -4.492  -16.435 1.00 44.10  ? 42  GLN   B CD  1 
ATOM   573  O  OE1 . GLN   B 2 33  ? -30.022 -5.620  -15.931 1.00 50.29  ? 42  GLN   B OE1 1 
ATOM   574  N  NE2 . GLN   B 2 33  ? -29.015 -4.185  -17.324 1.00 43.56  ? 42  GLN   B NE2 1 
ATOM   575  N  N   . GLU   B 2 34  ? -33.081 -1.569  -14.351 1.00 41.96  ? 43  GLU   B N   1 
ATOM   576  C  CA  . GLU   B 2 34  ? -34.109 -1.852  -13.322 1.00 43.01  ? 43  GLU   B CA  1 
ATOM   577  C  C   . GLU   B 2 34  ? -34.131 -0.741  -12.265 1.00 43.22  ? 43  GLU   B C   1 
ATOM   578  O  O   . GLU   B 2 34  ? -34.275 -1.067  -11.072 1.00 42.65  ? 43  GLU   B O   1 
ATOM   579  C  CB  . GLU   B 2 34  ? -33.789 -3.220  -12.717 1.00 46.33  ? 43  GLU   B CB  1 
ATOM   580  C  CG  . GLU   B 2 34  ? -34.022 -4.385  -13.680 1.00 48.02  ? 43  GLU   B CG  1 
ATOM   581  C  CD  . GLU   B 2 34  ? -33.291 -5.682  -13.380 1.00 50.36  ? 43  GLU   B CD  1 
ATOM   582  O  OE1 . GLU   B 2 34  ? -33.620 -6.281  -12.395 1.00 54.81  ? 43  GLU   B OE1 1 
ATOM   583  O  OE2 . GLU   B 2 34  ? -32.361 -6.070  -14.134 1.00 54.80  ? 43  GLU   B OE2 1 
ATOM   584  N  N   . GLY   B 2 35  ? -34.006 0.542   -12.644 1.00 40.73  ? 44  GLY   B N   1 
ATOM   585  C  CA  . GLY   B 2 35  ? -34.160 1.667   -11.696 1.00 37.94  ? 44  GLY   B CA  1 
ATOM   586  C  C   . GLY   B 2 35  ? -32.933 1.849   -10.830 1.00 36.00  ? 44  GLY   B C   1 
ATOM   587  O  O   . GLY   B 2 35  ? -32.926 2.738   -9.959  1.00 34.77  ? 44  GLY   B O   1 
ATOM   588  N  N   . VAL   B 2 36  ? -31.872 1.111   -11.094 1.00 34.03  ? 45  VAL   B N   1 
ATOM   589  C  CA  . VAL   B 2 36  ? -30.604 1.209   -10.328 1.00 32.81  ? 45  VAL   B CA  1 
ATOM   590  C  C   . VAL   B 2 36  ? -29.508 1.770   -11.221 1.00 31.53  ? 45  VAL   B C   1 
ATOM   591  O  O   . VAL   B 2 36  ? -29.372 1.284   -12.379 1.00 32.05  ? 45  VAL   B O   1 
ATOM   592  C  CB  . VAL   B 2 36  ? -30.240 -0.141  -9.662  1.00 33.76  ? 45  VAL   B CB  1 
ATOM   593  C  CG1 . VAL   B 2 36  ? -28.838 -0.097  -9.058  1.00 33.63  ? 45  VAL   B CG1 1 
ATOM   594  C  CG2 . VAL   B 2 36  ? -31.238 -0.441  -8.549  1.00 34.71  ? 45  VAL   B CG2 1 
ATOM   595  N  N   . PHE   B 2 37  ? -28.758 2.745   -10.702 1.00 30.28  ? 46  PHE   B N   1 
ATOM   596  C  CA  . PHE   B 2 37  ? -27.616 3.316   -11.432 1.00 30.87  ? 46  PHE   B CA  1 
ATOM   597  C  C   . PHE   B 2 37  ? -26.341 2.613   -10.951 1.00 30.35  ? 46  PHE   B C   1 
ATOM   598  O  O   . PHE   B 2 37  ? -26.064 2.584   -9.769  1.00 30.33  ? 46  PHE   B O   1 
ATOM   599  C  CB  . PHE   B 2 37  ? -27.468 4.815   -11.252 1.00 30.38  ? 46  PHE   B CB  1 
ATOM   600  C  CG  . PHE   B 2 37  ? -26.485 5.372   -12.230 1.00 30.71  ? 46  PHE   B CG  1 
ATOM   601  C  CD1 . PHE   B 2 37  ? -26.700 5.224   -13.576 1.00 31.00  ? 46  PHE   B CD1 1 
ATOM   602  C  CD2 . PHE   B 2 37  ? -25.391 6.087   -11.808 1.00 30.43  ? 46  PHE   B CD2 1 
ATOM   603  C  CE1 . PHE   B 2 37  ? -25.808 5.712   -14.514 1.00 31.72  ? 46  PHE   B CE1 1 
ATOM   604  C  CE2 . PHE   B 2 37  ? -24.499 6.594   -12.735 1.00 31.22  ? 46  PHE   B CE2 1 
ATOM   605  C  CZ  . PHE   B 2 37  ? -24.728 6.438   -14.091 1.00 31.91  ? 46  PHE   B CZ  1 
ATOM   606  N  N   . HIS   B 2 38  ? -25.559 2.159   -11.887 1.00 29.66  ? 47  HIS   B N   1 
ATOM   607  C  CA  . HIS   B 2 38  ? -24.363 1.293   -11.639 1.00 29.91  ? 47  HIS   B CA  1 
ATOM   608  C  C   . HIS   B 2 38  ? -23.139 2.029   -12.138 1.00 30.16  ? 47  HIS   B C   1 
ATOM   609  O  O   . HIS   B 2 38  ? -23.105 2.334   -13.324 1.00 30.13  ? 47  HIS   B O   1 
ATOM   610  C  CB  . HIS   B 2 38  ? -24.518 -0.018  -12.343 1.00 30.00  ? 47  HIS   B CB  1 
ATOM   611  C  CG  . HIS   B 2 38  ? -25.706 -0.821  -11.986 1.00 30.55  ? 47  HIS   B CG  1 
ATOM   612  N  ND1 . HIS   B 2 38  ? -26.921 -0.544  -12.504 1.00 31.87  ? 47  HIS   B ND1 1 
ATOM   613  C  CD2 . HIS   B 2 38  ? -25.860 -1.914  -11.201 1.00 31.32  ? 47  HIS   B CD2 1 
ATOM   614  C  CE1 . HIS   B 2 38  ? -27.835 -1.368  -12.005 1.00 32.49  ? 47  HIS   B CE1 1 
ATOM   615  N  NE2 . HIS   B 2 38  ? -27.194 -2.245  -11.186 1.00 32.38  ? 47  HIS   B NE2 1 
ATOM   616  N  N   . THR   B 2 39  ? -22.172 2.350   -11.289 1.00 30.53  ? 48  THR   B N   1 
ATOM   617  C  CA  . THR   B 2 39  ? -20.901 2.904   -11.818 1.00 31.03  ? 48  THR   B CA  1 
ATOM   618  C  C   . THR   B 2 39  ? -19.700 2.289   -11.080 1.00 31.79  ? 48  THR   B C   1 
ATOM   619  O  O   . THR   B 2 39  ? -19.910 1.416   -10.187 1.00 31.03  ? 48  THR   B O   1 
ATOM   620  C  CB  . THR   B 2 39  ? -20.984 4.432   -11.838 1.00 31.24  ? 48  THR   B CB  1 
ATOM   621  O  OG1 . THR   B 2 39  ? -19.942 5.007   -12.625 1.00 31.86  ? 48  THR   B OG1 1 
ATOM   622  C  CG2 . THR   B 2 39  ? -20.945 5.057   -10.468 1.00 31.98  ? 48  THR   B CG2 1 
ATOM   623  N  N   . MET   B 2 40  ? -18.514 2.845   -11.320 1.00 32.49  ? 49  MET   B N   1 
ATOM   624  C  CA  . MET   B 2 40  ? -17.295 2.501   -10.556 1.00 33.11  ? 49  MET   B CA  1 
ATOM   625  C  C   . MET   B 2 40  ? -17.108 3.493   -9.407  1.00 33.05  ? 49  MET   B C   1 
ATOM   626  O  O   . MET   B 2 40  ? -17.371 4.740   -9.559  1.00 32.93  ? 49  MET   B O   1 
ATOM   627  C  CB  . MET   B 2 40  ? -16.050 2.467   -11.425 1.00 33.98  ? 49  MET   B CB  1 
ATOM   628  C  CG  . MET   B 2 40  ? -16.285 1.797   -12.790 1.00 35.41  ? 49  MET   B CG  1 
ATOM   629  S  SD  . MET   B 2 40  ? -14.846 0.871   -13.361 1.00 39.01  ? 49  MET   B SD  1 
ATOM   630  C  CE  . MET   B 2 40  ? -14.915 -0.550  -12.260 1.00 39.71  ? 49  MET   B CE  1 
ATOM   631  N  N   A TRP   B 2 41  ? -16.645 2.979   -8.263  0.25 32.80  ? 50  TRP   B N   1 
ATOM   632  N  N   B TRP   B 2 41  ? -16.650 2.980   -8.265  0.16 32.42  ? 50  TRP   B N   1 
ATOM   633  N  N   C TRP   B 2 41  ? -16.646 2.980   -8.263  0.25 32.80  ? 50  TRP   B N   1 
ATOM   634  N  N   D TRP   B 2 41  ? -16.649 2.980   -8.265  0.25 32.34  ? 50  TRP   B N   1 
ATOM   635  C  CA  A TRP   B 2 41  ? -16.475 3.764   -7.015  0.25 33.04  ? 50  TRP   B CA  1 
ATOM   636  C  CA  B TRP   B 2 41  ? -16.500 3.773   -7.022  0.16 32.29  ? 50  TRP   B CA  1 
ATOM   637  C  CA  C TRP   B 2 41  ? -16.475 3.764   -7.014  0.25 33.04  ? 50  TRP   B CA  1 
ATOM   638  C  CA  D TRP   B 2 41  ? -16.500 3.773   -7.023  0.25 32.26  ? 50  TRP   B CA  1 
ATOM   639  C  C   A TRP   B 2 41  ? -15.551 4.960   -7.275  0.25 33.13  ? 50  TRP   B C   1 
ATOM   640  C  C   B TRP   B 2 41  ? -15.551 4.956   -7.263  0.16 32.69  ? 50  TRP   B C   1 
ATOM   641  C  C   C TRP   B 2 41  ? -15.550 4.960   -7.273  0.25 33.13  ? 50  TRP   B C   1 
ATOM   642  C  C   D TRP   B 2 41  ? -15.551 4.957   -7.268  0.25 32.68  ? 50  TRP   B C   1 
ATOM   643  O  O   A TRP   B 2 41  ? -15.828 6.061   -6.755  0.25 32.79  ? 50  TRP   B O   1 
ATOM   644  O  O   B TRP   B 2 41  ? -15.820 6.051   -6.727  0.16 32.47  ? 50  TRP   B O   1 
ATOM   645  O  O   C TRP   B 2 41  ? -15.827 6.061   -6.752  0.25 32.79  ? 50  TRP   B O   1 
ATOM   646  O  O   D TRP   B 2 41  ? -15.819 6.055   -6.738  0.25 32.42  ? 50  TRP   B O   1 
ATOM   647  C  CB  A TRP   B 2 41  ? -15.947 2.890   -5.864  0.25 33.35  ? 50  TRP   B CB  1 
ATOM   648  C  CB  B TRP   B 2 41  ? -16.029 2.902   -5.850  0.16 31.96  ? 50  TRP   B CB  1 
ATOM   649  C  CB  C TRP   B 2 41  ? -15.948 2.890   -5.865  0.25 33.36  ? 50  TRP   B CB  1 
ATOM   650  C  CB  D TRP   B 2 41  ? -16.029 2.901   -5.850  0.25 31.94  ? 50  TRP   B CB  1 
ATOM   651  C  CG  A TRP   B 2 41  ? -16.056 3.585   -4.542  0.25 33.58  ? 50  TRP   B CG  1 
ATOM   652  C  CG  B TRP   B 2 41  ? -15.841 3.737   -4.625  0.16 31.64  ? 50  TRP   B CG  1 
ATOM   653  C  CG  C TRP   B 2 41  ? -16.056 3.585   -4.543  0.25 33.58  ? 50  TRP   B CG  1 
ATOM   654  C  CG  D TRP   B 2 41  ? -15.842 3.735   -4.624  0.25 31.60  ? 50  TRP   B CG  1 
ATOM   655  C  CD1 A TRP   B 2 41  ? -17.117 3.548   -3.692  0.25 33.80  ? 50  TRP   B CD1 1 
ATOM   656  C  CD1 B TRP   B 2 41  ? -14.775 4.538   -4.348  0.16 31.61  ? 50  TRP   B CD1 1 
ATOM   657  C  CD1 C TRP   B 2 41  ? -17.117 3.548   -3.692  0.25 33.80  ? 50  TRP   B CD1 1 
ATOM   658  C  CD1 D TRP   B 2 41  ? -14.778 4.538   -4.349  0.25 31.56  ? 50  TRP   B CD1 1 
ATOM   659  C  CD2 A TRP   B 2 41  ? -15.110 4.502   -3.964  0.25 34.01  ? 50  TRP   B CD2 1 
ATOM   660  C  CD2 B TRP   B 2 41  ? -16.794 3.957   -3.575  0.16 31.54  ? 50  TRP   B CD2 1 
ATOM   661  C  CD2 C TRP   B 2 41  ? -15.110 4.502   -3.965  0.25 34.01  ? 50  TRP   B CD2 1 
ATOM   662  C  CD2 D TRP   B 2 41  ? -16.795 3.958   -3.577  0.25 31.54  ? 50  TRP   B CD2 1 
ATOM   663  N  NE1 A TRP   B 2 41  ? -16.881 4.348   -2.603  0.25 34.16  ? 50  TRP   B NE1 1 
ATOM   664  N  NE1 B TRP   B 2 41  ? -14.977 5.210   -3.178  0.16 31.39  ? 50  TRP   B NE1 1 
ATOM   665  N  NE1 C TRP   B 2 41  ? -16.880 4.348   -2.604  0.25 34.16  ? 50  TRP   B NE1 1 
ATOM   666  N  NE1 D TRP   B 2 41  ? -14.980 5.213   -3.182  0.25 31.30  ? 50  TRP   B NE1 1 
ATOM   667  C  CE2 A TRP   B 2 41  ? -15.659 4.951   -2.747  0.25 34.26  ? 50  TRP   B CE2 1 
ATOM   668  C  CE2 B TRP   B 2 41  ? -16.205 4.872   -2.678  0.16 31.47  ? 50  TRP   B CE2 1 
ATOM   669  C  CE2 C TRP   B 2 41  ? -15.658 4.951   -2.748  0.25 34.26  ? 50  TRP   B CE2 1 
ATOM   670  C  CE2 D TRP   B 2 41  ? -16.207 4.876   -2.682  0.25 31.46  ? 50  TRP   B CE2 1 
ATOM   671  C  CE3 A TRP   B 2 41  ? -13.844 4.968   -4.340  0.25 34.92  ? 50  TRP   B CE3 1 
ATOM   672  C  CE3 B TRP   B 2 41  ? -18.066 3.454   -3.284  0.16 31.66  ? 50  TRP   B CE3 1 
ATOM   673  C  CE3 C TRP   B 2 41  ? -13.845 4.968   -4.341  0.25 34.92  ? 50  TRP   B CE3 1 
ATOM   674  C  CE3 D TRP   B 2 41  ? -18.066 3.454   -3.284  0.25 31.72  ? 50  TRP   B CE3 1 
ATOM   675  C  CZ2 A TRP   B 2 41  ? -14.978 5.829   -1.900  0.25 34.87  ? 50  TRP   B CZ2 1 
ATOM   676  C  CZ2 B TRP   B 2 41  ? -16.845 5.285   -1.512  0.16 31.44  ? 50  TRP   B CZ2 1 
ATOM   677  C  CZ2 C TRP   B 2 41  ? -14.978 5.828   -1.901  0.25 34.87  ? 50  TRP   B CZ2 1 
ATOM   678  C  CZ2 D TRP   B 2 41  ? -16.847 5.288   -1.515  0.25 31.43  ? 50  TRP   B CZ2 1 
ATOM   679  C  CZ3 A TRP   B 2 41  ? -13.179 5.849   -3.513  0.25 35.02  ? 50  TRP   B CZ3 1 
ATOM   680  C  CZ3 B TRP   B 2 41  ? -18.696 3.861   -2.126  0.16 31.44  ? 50  TRP   B CZ3 1 
ATOM   681  C  CZ3 C TRP   B 2 41  ? -13.181 5.849   -3.514  0.25 35.02  ? 50  TRP   B CZ3 1 
ATOM   682  C  CZ3 D TRP   B 2 41  ? -18.695 3.860   -2.124  0.25 31.44  ? 50  TRP   B CZ3 1 
ATOM   683  C  CH2 A TRP   B 2 41  ? -13.738 6.268   -2.305  0.25 35.18  ? 50  TRP   B CH2 1 
ATOM   684  C  CH2 B TRP   B 2 41  ? -18.093 4.764   -1.254  0.16 31.42  ? 50  TRP   B CH2 1 
ATOM   685  C  CH2 C TRP   B 2 41  ? -13.738 6.267   -2.306  0.25 35.18  ? 50  TRP   B CH2 1 
ATOM   686  C  CH2 D TRP   B 2 41  ? -18.094 4.765   -1.255  0.25 31.42  ? 50  TRP   B CH2 1 
ATOM   687  N  N   . HIS   B 2 42  ? -14.481 4.760   -8.035  1.00 32.97  ? 51  HIS   B N   1 
ATOM   688  C  CA  . HIS   B 2 42  ? -13.475 5.847   -8.265  1.00 34.40  ? 51  HIS   B CA  1 
ATOM   689  C  C   . HIS   B 2 42  ? -14.076 7.015   -9.101  1.00 35.26  ? 51  HIS   B C   1 
ATOM   690  O  O   . HIS   B 2 42  ? -13.510 8.110   -9.036  1.00 35.81  ? 51  HIS   B O   1 
ATOM   691  C  CB  . HIS   B 2 42  ? -12.175 5.338   -8.863  1.00 34.46  ? 51  HIS   B CB  1 
ATOM   692  C  CG  . HIS   B 2 42  ? -12.229 5.055   -10.310 1.00 35.82  ? 51  HIS   B CG  1 
ATOM   693  N  ND1 . HIS   B 2 42  ? -12.461 3.781   -10.792 1.00 35.77  ? 51  HIS   B ND1 1 
ATOM   694  C  CD2 . HIS   B 2 42  ? -11.959 5.830   -11.398 1.00 36.99  ? 51  HIS   B CD2 1 
ATOM   695  C  CE1 . HIS   B 2 42  ? -12.411 3.810   -12.104 1.00 36.26  ? 51  HIS   B CE1 1 
ATOM   696  N  NE2 . HIS   B 2 42  ? -12.102 5.045   -12.498 1.00 36.35  ? 51  HIS   B NE2 1 
ATOM   697  N  N   . VAL   B 2 43  ? -15.226 6.838   -9.746  1.00 34.83  ? 52  VAL   B N   1 
ATOM   698  C  CA  . VAL   B 2 43  ? -15.888 7.926   -10.509 1.00 35.43  ? 52  VAL   B CA  1 
ATOM   699  C  C   . VAL   B 2 43  ? -16.578 8.861   -9.516  1.00 35.58  ? 52  VAL   B C   1 
ATOM   700  O  O   . VAL   B 2 43  ? -16.278 10.063  -9.579  1.00 36.99  ? 52  VAL   B O   1 
ATOM   701  C  CB  . VAL   B 2 43  ? -16.843 7.339   -11.567 1.00 36.71  ? 52  VAL   B CB  1 
ATOM   702  C  CG1 . VAL   B 2 43  ? -17.785 8.367   -12.194 1.00 38.51  ? 52  VAL   B CG1 1 
ATOM   703  C  CG2 . VAL   B 2 43  ? -16.068 6.628   -12.639 1.00 36.87  ? 52  VAL   B CG2 1 
ATOM   704  N  N   . THR   B 2 44  ? -17.403 8.357   -8.589  1.00 32.70  ? 53  THR   B N   1 
ATOM   705  C  CA  . THR   B 2 44  ? -18.271 9.211   -7.733  1.00 34.31  ? 53  THR   B CA  1 
ATOM   706  C  C   . THR   B 2 44  ? -17.689 9.368   -6.329  1.00 35.97  ? 53  THR   B C   1 
ATOM   707  O  O   . THR   B 2 44  ? -18.080 10.332  -5.673  1.00 37.24  ? 53  THR   B O   1 
ATOM   708  C  CB  . THR   B 2 44  ? -19.702 8.673   -7.672  1.00 33.14  ? 53  THR   B CB  1 
ATOM   709  O  OG1 . THR   B 2 44  ? -19.710 7.426   -6.969  1.00 32.62  ? 53  THR   B OG1 1 
ATOM   710  C  CG2 . THR   B 2 44  ? -20.261 8.501   -9.071  1.00 32.47  ? 53  THR   B CG2 1 
ATOM   711  N  N   . LYS   B 2 45  ? -16.748 8.506   -5.937  1.00 37.97  ? 54  LYS   B N   1 
ATOM   712  C  CA  . LYS   B 2 45  ? -16.263 8.334   -4.537  1.00 41.71  ? 54  LYS   B CA  1 
ATOM   713  C  C   . LYS   B 2 45  ? -17.454 8.136   -3.583  1.00 40.49  ? 54  LYS   B C   1 
ATOM   714  O  O   . LYS   B 2 45  ? -17.344 8.513   -2.399  1.00 40.21  ? 54  LYS   B O   1 
ATOM   715  C  CB  . LYS   B 2 45  ? -15.430 9.524   -4.052  1.00 46.59  ? 54  LYS   B CB  1 
ATOM   716  C  CG  . LYS   B 2 45  ? -14.341 10.019  -4.980  1.00 51.89  ? 54  LYS   B CG  1 
ATOM   717  C  CD  . LYS   B 2 45  ? -13.294 9.004   -5.270  1.00 57.73  ? 54  LYS   B CD  1 
ATOM   718  C  CE  . LYS   B 2 45  ? -12.193 9.597   -6.135  1.00 62.85  ? 54  LYS   B CE  1 
ATOM   719  N  NZ  . LYS   B 2 45  ? -11.482 8.554   -6.921  1.00 66.36  ? 54  LYS   B NZ  1 
ATOM   720  N  N   . GLY   B 2 46  ? -18.565 7.576   -4.053  1.00 39.76  ? 55  GLY   B N   1 
ATOM   721  C  CA  . GLY   B 2 46  ? -19.730 7.322   -3.196  1.00 39.01  ? 55  GLY   B CA  1 
ATOM   722  C  C   . GLY   B 2 46  ? -20.616 8.538   -2.998  1.00 40.20  ? 55  GLY   B C   1 
ATOM   723  O  O   . GLY   B 2 46  ? -21.575 8.409   -2.284  1.00 41.51  ? 55  GLY   B O   1 
ATOM   724  N  N   . ALA   B 2 47  ? -20.386 9.670   -3.661  1.00 41.08  ? 56  ALA   B N   1 
ATOM   725  C  CA  . ALA   B 2 47  ? -21.245 10.876  -3.519  1.00 41.23  ? 56  ALA   B CA  1 
ATOM   726  C  C   . ALA   B 2 47  ? -22.618 10.651  -4.168  1.00 39.91  ? 56  ALA   B C   1 
ATOM   727  O  O   . ALA   B 2 47  ? -22.736 9.902   -5.136  1.00 39.39  ? 56  ALA   B O   1 
ATOM   728  C  CB  . ALA   B 2 47  ? -20.547 12.083  -4.130  1.00 42.90  ? 56  ALA   B CB  1 
ATOM   729  N  N   . ALA   B 2 48  ? -23.607 11.423  -3.762  1.00 38.30  ? 57  ALA   B N   1 
ATOM   730  C  CA  . ALA   B 2 48  ? -24.920 11.485  -4.428  1.00 39.54  ? 57  ALA   B CA  1 
ATOM   731  C  C   . ALA   B 2 48  ? -24.789 12.141  -5.799  1.00 39.75  ? 57  ALA   B C   1 
ATOM   732  O  O   . ALA   B 2 48  ? -23.818 12.844  -6.060  1.00 40.04  ? 57  ALA   B O   1 
ATOM   733  C  CB  . ALA   B 2 48  ? -25.935 12.198  -3.561  1.00 41.61  ? 57  ALA   B CB  1 
ATOM   734  N  N   . LEU   B 2 49  ? -25.776 11.875  -6.646  1.00 38.72  ? 58  LEU   B N   1 
ATOM   735  C  CA  . LEU   B 2 49  ? -25.861 12.323  -8.044  1.00 38.97  ? 58  LEU   B CA  1 
ATOM   736  C  C   . LEU   B 2 49  ? -27.205 13.003  -8.269  1.00 41.97  ? 58  LEU   B C   1 
ATOM   737  O  O   . LEU   B 2 49  ? -28.195 12.658  -7.597  1.00 44.87  ? 58  LEU   B O   1 
ATOM   738  C  CB  . LEU   B 2 49  ? -25.792 11.111  -8.977  1.00 37.86  ? 58  LEU   B CB  1 
ATOM   739  C  CG  . LEU   B 2 49  ? -24.559 10.232  -8.828  1.00 36.39  ? 58  LEU   B CG  1 
ATOM   740  C  CD1 . LEU   B 2 49  ? -24.696 8.994   -9.670  1.00 36.07  ? 58  LEU   B CD1 1 
ATOM   741  C  CD2 . LEU   B 2 49  ? -23.305 11.004  -9.203  1.00 37.51  ? 58  LEU   B CD2 1 
ATOM   742  N  N   . ARG   B 2 50  ? -27.233 13.900  -9.230  1.00 43.49  ? 59  ARG   B N   1 
ATOM   743  C  CA  . ARG   B 2 50  ? -28.465 14.550  -9.699  1.00 46.67  ? 59  ARG   B CA  1 
ATOM   744  C  C   . ARG   B 2 50  ? -28.812 13.941  -11.059 1.00 45.86  ? 59  ARG   B C   1 
ATOM   745  O  O   . ARG   B 2 50  ? -27.891 13.585  -11.803 1.00 44.25  ? 59  ARG   B O   1 
ATOM   746  C  CB  . ARG   B 2 50  ? -28.161 16.041  -9.722  1.00 51.47  ? 59  ARG   B CB  1 
ATOM   747  C  CG  . ARG   B 2 50  ? -29.320 16.901  -10.197 1.00 59.36  ? 59  ARG   B CG  1 
ATOM   748  C  CD  . ARG   B 2 50  ? -29.085 18.332  -9.754  1.00 62.58  ? 59  ARG   B CD  1 
ATOM   749  N  NE  . ARG   B 2 50  ? -27.666 18.673  -9.883  1.00 65.23  ? 59  ARG   B NE  1 
ATOM   750  C  CZ  . ARG   B 2 50  ? -27.078 19.047  -11.020 1.00 67.23  ? 59  ARG   B CZ  1 
ATOM   751  N  NH1 . ARG   B 2 50  ? -27.771 19.107  -12.152 1.00 65.99  ? 59  ARG   B NH1 1 
ATOM   752  N  NH2 . ARG   B 2 50  ? -25.784 19.341  -11.019 1.00 72.16  ? 59  ARG   B NH2 1 
ATOM   753  N  N   . SER   B 2 51  ? -30.091 13.684  -11.289 1.00 46.44  ? 60  SER   B N   1 
ATOM   754  C  CA  . SER   B 2 51  ? -30.710 13.457  -12.616 1.00 48.72  ? 60  SER   B CA  1 
ATOM   755  C  C   . SER   B 2 51  ? -31.891 14.434  -12.801 1.00 52.74  ? 60  SER   B C   1 
ATOM   756  O  O   . SER   B 2 51  ? -32.916 14.227  -12.139 1.00 53.16  ? 60  SER   B O   1 
ATOM   757  C  CB  . SER   B 2 51  ? -31.193 12.059  -12.664 1.00 46.85  ? 60  SER   B CB  1 
ATOM   758  O  OG  . SER   B 2 51  ? -31.749 11.804  -13.921 1.00 46.34  ? 60  SER   B OG  1 
ATOM   759  N  N   . GLY   B 2 52  ? -31.771 15.467  -13.632 1.00 57.34  ? 61  GLY   B N   1 
ATOM   760  C  CA  . GLY   B 2 52  ? -32.800 16.528  -13.669 1.00 60.78  ? 61  GLY   B CA  1 
ATOM   761  C  C   . GLY   B 2 52  ? -32.917 17.180  -12.305 1.00 63.62  ? 61  GLY   B C   1 
ATOM   762  O  O   . GLY   B 2 52  ? -31.884 17.602  -11.766 1.00 67.04  ? 61  GLY   B O   1 
ATOM   763  N  N   . GLU   B 2 53  ? -34.112 17.202  -11.731 1.00 66.55  ? 62  GLU   B N   1 
ATOM   764  C  CA  . GLU   B 2 53  ? -34.348 17.739  -10.372 1.00 69.55  ? 62  GLU   B CA  1 
ATOM   765  C  C   . GLU   B 2 53  ? -34.222 16.622  -9.331  1.00 67.36  ? 62  GLU   B C   1 
ATOM   766  O  O   . GLU   B 2 53  ? -34.194 16.953  -8.144  1.00 64.28  ? 62  GLU   B O   1 
ATOM   767  C  CB  . GLU   B 2 53  ? -35.742 18.345  -10.281 1.00 75.22  ? 62  GLU   B CB  1 
ATOM   768  C  CG  . GLU   B 2 53  ? -35.758 19.857  -10.371 1.00 81.59  ? 62  GLU   B CG  1 
ATOM   769  C  CD  . GLU   B 2 53  ? -37.173 20.407  -10.250 1.00 88.80  ? 62  GLU   B CD  1 
ATOM   770  O  OE1 . GLU   B 2 53  ? -38.067 19.908  -10.987 1.00 87.78  ? 62  GLU   B OE1 1 
ATOM   771  O  OE2 . GLU   B 2 53  ? -37.392 21.303  -9.393  1.00 95.73  ? 62  GLU   B OE2 1 
ATOM   772  N  N   . GLY   B 2 54  ? -34.142 15.361  -9.763  1.00 63.23  ? 63  GLY   B N   1 
ATOM   773  C  CA  . GLY   B 2 54  ? -34.117 14.181  -8.878  1.00 61.24  ? 63  GLY   B CA  1 
ATOM   774  C  C   . GLY   B 2 54  ? -32.736 13.928  -8.297  1.00 60.06  ? 63  GLY   B C   1 
ATOM   775  O  O   . GLY   B 2 54  ? -31.742 14.343  -8.914  1.00 58.16  ? 63  GLY   B O   1 
ATOM   776  N  N   . ARG   B 2 55  ? -32.678 13.328  -7.106  1.00 57.49  ? 64  ARG   B N   1 
ATOM   777  C  CA  . ARG   B 2 55  ? -31.412 12.947  -6.430  1.00 54.00  ? 64  ARG   B CA  1 
ATOM   778  C  C   . ARG   B 2 55  ? -31.261 11.411  -6.490  1.00 51.26  ? 64  ARG   B C   1 
ATOM   779  O  O   . ARG   B 2 55  ? -32.247 10.660  -6.399  1.00 51.60  ? 64  ARG   B O   1 
ATOM   780  C  CB  . ARG   B 2 55  ? -31.391 13.546  -5.023  1.00 55.01  ? 64  ARG   B CB  1 
ATOM   781  C  CG  . ARG   B 2 55  ? -30.046 13.460  -4.314  1.00 57.68  ? 64  ARG   B CG  1 
ATOM   782  C  CD  . ARG   B 2 55  ? -30.220 13.607  -2.800  1.00 60.51  ? 64  ARG   B CD  1 
ATOM   783  N  NE  . ARG   B 2 55  ? -29.020 13.369  -1.991  1.00 63.72  ? 64  ARG   B NE  1 
ATOM   784  C  CZ  . ARG   B 2 55  ? -28.265 14.294  -1.369  1.00 65.60  ? 64  ARG   B CZ  1 
ATOM   785  N  NH1 . ARG   B 2 55  ? -28.548 15.584  -1.454  1.00 65.46  ? 64  ARG   B NH1 1 
ATOM   786  N  NH2 . ARG   B 2 55  ? -27.217 13.914  -0.649  1.00 65.01  ? 64  ARG   B NH2 1 
ATOM   787  N  N   . LEU   B 2 56  ? -30.053 10.942  -6.736  1.00 45.59  ? 65  LEU   B N   1 
ATOM   788  C  CA  . LEU   B 2 56  ? -29.763 9.495   -6.701  1.00 44.05  ? 65  LEU   B CA  1 
ATOM   789  C  C   . LEU   B 2 56  ? -28.874 9.306   -5.482  1.00 41.32  ? 65  LEU   B C   1 
ATOM   790  O  O   . LEU   B 2 56  ? -27.774 9.921   -5.471  1.00 40.41  ? 65  LEU   B O   1 
ATOM   791  C  CB  . LEU   B 2 56  ? -29.028 9.073   -7.983  1.00 44.30  ? 65  LEU   B CB  1 
ATOM   792  C  CG  . LEU   B 2 56  ? -29.741 9.218   -9.319  1.00 46.32  ? 65  LEU   B CG  1 
ATOM   793  C  CD1 . LEU   B 2 56  ? -29.093 8.281   -10.332 1.00 47.56  ? 65  LEU   B CD1 1 
ATOM   794  C  CD2 . LEU   B 2 56  ? -31.219 8.892   -9.229  1.00 48.85  ? 65  LEU   B CD2 1 
ATOM   795  N  N   . ASP   B 2 57  ? -29.318 8.536   -4.493  1.00 38.99  ? 66  ASP   B N   1 
ATOM   796  C  CA  . ASP   B 2 57  ? -28.479 8.253   -3.304  1.00 38.41  ? 66  ASP   B CA  1 
ATOM   797  C  C   . ASP   B 2 57  ? -27.732 6.927   -3.460  1.00 35.46  ? 66  ASP   B C   1 
ATOM   798  O  O   . ASP   B 2 57  ? -28.299 5.923   -3.878  1.00 33.78  ? 66  ASP   B O   1 
ATOM   799  C  CB  . ASP   B 2 57  ? -29.368 8.207   -2.075  1.00 43.32  ? 66  ASP   B CB  1 
ATOM   800  C  CG  . ASP   B 2 57  ? -29.979 9.574   -1.772  1.00 47.99  ? 66  ASP   B CG  1 
ATOM   801  O  OD1 . ASP   B 2 57  ? -29.265 10.579  -1.955  1.00 51.82  ? 66  ASP   B OD1 1 
ATOM   802  O  OD2 . ASP   B 2 57  ? -31.151 9.616   -1.407  1.00 49.64  ? 66  ASP   B OD2 1 
ATOM   803  N  N   . PRO   B 2 58  ? -26.469 6.839   -3.008  1.00 34.12  ? 67  PRO   B N   1 
ATOM   804  C  CA  . PRO   B 2 58  ? -25.743 5.563   -2.993  1.00 33.34  ? 67  PRO   B CA  1 
ATOM   805  C  C   . PRO   B 2 58  ? -26.541 4.524   -2.175  1.00 33.30  ? 67  PRO   B C   1 
ATOM   806  O  O   . PRO   B 2 58  ? -27.158 4.880   -1.209  1.00 33.93  ? 67  PRO   B O   1 
ATOM   807  C  CB  . PRO   B 2 58  ? -24.380 5.952   -2.378  1.00 33.33  ? 67  PRO   B CB  1 
ATOM   808  C  CG  . PRO   B 2 58  ? -24.670 7.181   -1.555  1.00 34.89  ? 67  PRO   B CG  1 
ATOM   809  C  CD  . PRO   B 2 58  ? -25.724 7.924   -2.335  1.00 34.71  ? 67  PRO   B CD  1 
ATOM   810  N  N   . TYR   B 2 59  ? -26.596 3.265   -2.590  1.00 31.59  ? 68  TYR   B N   1 
ATOM   811  C  CA  . TYR   B 2 59  ? -27.269 2.180   -1.858  1.00 31.24  ? 68  TYR   B CA  1 
ATOM   812  C  C   . TYR   B 2 59  ? -26.239 1.142   -1.375  1.00 31.19  ? 68  TYR   B C   1 
ATOM   813  O  O   . TYR   B 2 59  ? -26.439 0.563   -0.306  1.00 32.86  ? 68  TYR   B O   1 
ATOM   814  C  CB  . TYR   B 2 59  ? -28.309 1.552   -2.771  1.00 31.71  ? 68  TYR   B CB  1 
ATOM   815  C  CG  . TYR   B 2 59  ? -29.143 0.457   -2.172  1.00 31.86  ? 68  TYR   B CG  1 
ATOM   816  C  CD1 . TYR   B 2 59  ? -28.652 -0.833  -2.143  1.00 32.20  ? 68  TYR   B CD1 1 
ATOM   817  C  CD2 . TYR   B 2 59  ? -30.432 0.688   -1.742  1.00 31.84  ? 68  TYR   B CD2 1 
ATOM   818  C  CE1 . TYR   B 2 59  ? -29.414 -1.869  -1.612  1.00 32.97  ? 68  TYR   B CE1 1 
ATOM   819  C  CE2 . TYR   B 2 59  ? -31.213 -0.344  -1.232  1.00 33.12  ? 68  TYR   B CE2 1 
ATOM   820  C  CZ  . TYR   B 2 59  ? -30.686 -1.629  -1.149  1.00 33.79  ? 68  TYR   B CZ  1 
ATOM   821  O  OH  . TYR   B 2 59  ? -31.387 -2.692  -0.639  1.00 34.61  ? 68  TYR   B OH  1 
ATOM   822  N  N   . TRP   B 2 60  ? -25.342 0.765   -2.240  1.00 30.15  ? 69  TRP   B N   1 
ATOM   823  C  CA  . TRP   B 2 60  ? -24.285 -0.271  -2.076  1.00 30.53  ? 69  TRP   B CA  1 
ATOM   824  C  C   . TRP   B 2 60  ? -22.975 0.211   -2.695  1.00 30.46  ? 69  TRP   B C   1 
ATOM   825  O  O   . TRP   B 2 60  ? -22.978 0.668   -3.833  1.00 31.01  ? 69  TRP   B O   1 
ATOM   826  C  CB  . TRP   B 2 60  ? -24.689 -1.621  -2.642  1.00 30.64  ? 69  TRP   B CB  1 
ATOM   827  C  CG  . TRP   B 2 60  ? -23.555 -2.597  -2.570  1.00 30.94  ? 69  TRP   B CG  1 
ATOM   828  C  CD1 . TRP   B 2 60  ? -23.131 -3.305  -1.471  1.00 31.54  ? 69  TRP   B CD1 1 
ATOM   829  C  CD2 . TRP   B 2 60  ? -22.617 -2.872  -3.606  1.00 30.20  ? 69  TRP   B CD2 1 
ATOM   830  N  NE1 . TRP   B 2 60  ? -22.016 -4.045  -1.804  1.00 31.34  ? 69  TRP   B NE1 1 
ATOM   831  C  CE2 . TRP   B 2 60  ? -21.675 -3.787  -3.099  1.00 30.75  ? 69  TRP   B CE2 1 
ATOM   832  C  CE3 . TRP   B 2 60  ? -22.513 -2.475  -4.948  1.00 30.94  ? 69  TRP   B CE3 1 
ATOM   833  C  CZ2 . TRP   B 2 60  ? -20.624 -4.275  -3.862  1.00 30.09  ? 69  TRP   B CZ2 1 
ATOM   834  C  CZ3 . TRP   B 2 60  ? -21.472 -2.946  -5.694  1.00 30.32  ? 69  TRP   B CZ3 1 
ATOM   835  C  CH2 . TRP   B 2 60  ? -20.546 -3.843  -5.166  1.00 30.92  ? 69  TRP   B CH2 1 
ATOM   836  N  N   . GLY   B 2 61  ? -21.854 -0.010  -2.028  1.00 30.80  ? 70  GLY   B N   1 
ATOM   837  C  CA  . GLY   B 2 61  ? -20.537 0.149   -2.674  1.00 31.33  ? 70  GLY   B CA  1 
ATOM   838  C  C   . GLY   B 2 61  ? -19.427 -0.576  -1.976  1.00 30.93  ? 70  GLY   B C   1 
ATOM   839  O  O   . GLY   B 2 61  ? -19.596 -0.933  -0.773  1.00 31.12  ? 70  GLY   B O   1 
ATOM   840  N  N   . ASP   B 2 62  ? -18.309 -0.703  -2.647  1.00 32.01  ? 71  ASP   B N   1 
ATOM   841  C  CA  . ASP   B 2 62  ? -17.114 -1.480  -2.188  1.00 32.79  ? 71  ASP   B CA  1 
ATOM   842  C  C   . ASP   B 2 62  ? -15.917 -0.902  -2.927  1.00 31.75  ? 71  ASP   B C   1 
ATOM   843  O  O   . ASP   B 2 62  ? -15.855 -1.074  -4.156  1.00 33.17  ? 71  ASP   B O   1 
ATOM   844  C  CB  . ASP   B 2 62  ? -17.284 -2.979  -2.387  1.00 34.43  ? 71  ASP   B CB  1 
ATOM   845  C  CG  . ASP   B 2 62  ? -16.163 -3.790  -1.746  1.00 37.17  ? 71  ASP   B CG  1 
ATOM   846  O  OD1 . ASP   B 2 62  ? -15.029 -3.650  -2.104  1.00 38.03  ? 71  ASP   B OD1 1 
ATOM   847  O  OD2 . ASP   B 2 62  ? -16.455 -4.478  -0.792  1.00 44.86  ? 71  ASP   B OD2 1 
ATOM   848  N  N   . VAL   B 2 63  ? -15.018 -0.237  -2.210  1.00 31.41  ? 72  VAL   B N   1 
ATOM   849  C  CA  . VAL   B 2 63  ? -13.784 0.381   -2.769  1.00 32.09  ? 72  VAL   B CA  1 
ATOM   850  C  C   . VAL   B 2 63  ? -12.919 -0.723  -3.368  1.00 32.77  ? 72  VAL   B C   1 
ATOM   851  O  O   . VAL   B 2 63  ? -12.250 -0.470  -4.393  1.00 32.67  ? 72  VAL   B O   1 
ATOM   852  C  CB  . VAL   B 2 63  ? -13.014 1.221   -1.732  1.00 32.31  ? 72  VAL   B CB  1 
ATOM   853  C  CG1 . VAL   B 2 63  ? -11.553 1.404   -2.077  1.00 33.29  ? 72  VAL   B CG1 1 
ATOM   854  C  CG2 . VAL   B 2 63  ? -13.635 2.587   -1.546  1.00 32.44  ? 72  VAL   B CG2 1 
ATOM   855  N  N   . LYS   B 2 64  ? -12.981 -1.957  -2.879  1.00 33.84  ? 73  LYS   B N   1 
ATOM   856  C  CA  . LYS   B 2 64  ? -11.971 -2.948  -3.388  1.00 34.55  ? 73  LYS   B CA  1 
ATOM   857  C  C   . LYS   B 2 64  ? -12.401 -3.495  -4.762  1.00 34.76  ? 73  LYS   B C   1 
ATOM   858  O  O   . LYS   B 2 64  ? -11.569 -3.663  -5.658  1.00 34.08  ? 73  LYS   B O   1 
ATOM   859  C  CB  . LYS   B 2 64  ? -11.760 -4.099  -2.406  1.00 34.44  ? 73  LYS   B CB  1 
ATOM   860  C  CG  . LYS   B 2 64  ? -10.735 -5.086  -2.964  1.00 35.69  ? 73  LYS   B CG  1 
ATOM   861  C  CD  . LYS   B 2 64  ? -10.230 -6.023  -1.949  1.00 36.64  ? 73  LYS   B CD  1 
ATOM   862  C  CE  . LYS   B 2 64  ? -9.210  -6.983  -2.537  1.00 37.99  ? 73  LYS   B CE  1 
ATOM   863  N  NZ  . LYS   B 2 64  ? -8.907  -8.009  -1.526  1.00 39.70  ? 73  LYS   B NZ  1 
ATOM   864  N  N   . GLN   B 2 65  ? -13.690 -3.803  -4.883  1.00 36.19  ? 74  GLN   B N   1 
ATOM   865  C  CA  . GLN   B 2 65  ? -14.380 -4.161  -6.129  1.00 36.49  ? 74  GLN   B CA  1 
ATOM   866  C  C   . GLN   B 2 65  ? -14.418 -2.964  -7.101  1.00 35.36  ? 74  GLN   B C   1 
ATOM   867  O  O   . GLN   B 2 65  ? -14.597 -3.240  -8.314  1.00 33.12  ? 74  GLN   B O   1 
ATOM   868  C  CB  . GLN   B 2 65  ? -15.810 -4.579  -5.836  1.00 38.11  ? 74  GLN   B CB  1 
ATOM   869  C  CG  . GLN   B 2 65  ? -15.929 -5.882  -5.051  1.00 40.22  ? 74  GLN   B CG  1 
ATOM   870  C  CD  . GLN   B 2 65  ? -17.359 -6.380  -5.014  1.00 42.53  ? 74  GLN   B CD  1 
ATOM   871  O  OE1 . GLN   B 2 65  ? -18.060 -6.516  -6.034  1.00 47.91  ? 74  GLN   B OE1 1 
ATOM   872  N  NE2 . GLN   B 2 65  ? -17.831 -6.653  -3.816  1.00 45.74  ? 74  GLN   B NE2 1 
ATOM   873  N  N   . ASP   B 2 66  ? -14.252 -1.749  -6.565  1.00 33.79  ? 75  ASP   B N   1 
ATOM   874  C  CA  . ASP   B 2 66  ? -14.357 -0.409  -7.204  1.00 33.86  ? 75  ASP   B CA  1 
ATOM   875  C  C   . ASP   B 2 66  ? -15.699 -0.275  -7.893  1.00 33.00  ? 75  ASP   B C   1 
ATOM   876  O  O   . ASP   B 2 66  ? -15.675 0.193   -9.036  1.00 32.71  ? 75  ASP   B O   1 
ATOM   877  C  CB  . ASP   B 2 66  ? -13.223 -0.135  -8.194  1.00 34.59  ? 75  ASP   B CB  1 
ATOM   878  C  CG  . ASP   B 2 66  ? -13.200 1.286   -8.734  1.00 34.14  ? 75  ASP   B CG  1 
ATOM   879  O  OD1 . ASP   B 2 66  ? -13.510 2.212   -7.984  1.00 32.13  ? 75  ASP   B OD1 1 
ATOM   880  O  OD2 . ASP   B 2 66  ? -12.783 1.424   -9.923  1.00 37.01  ? 75  ASP   B OD2 1 
ATOM   881  N  N   . LEU   B 2 67  ? -16.801 -0.648  -7.225  1.00 31.82  ? 76  LEU   B N   1 
ATOM   882  C  CA  . LEU   B 2 67  ? -18.191 -0.569  -7.747  1.00 31.15  ? 76  LEU   B CA  1 
ATOM   883  C  C   . LEU   B 2 67  ? -19.106 0.185   -6.782  1.00 31.83  ? 76  LEU   B C   1 
ATOM   884  O  O   . LEU   B 2 67  ? -18.915 0.110   -5.508  1.00 31.14  ? 76  LEU   B O   1 
ATOM   885  C  CB  . LEU   B 2 67  ? -18.723 -1.979  -7.962  1.00 31.50  ? 76  LEU   B CB  1 
ATOM   886  C  CG  . LEU   B 2 67  ? -18.060 -2.796  -9.068  1.00 31.63  ? 76  LEU   B CG  1 
ATOM   887  C  CD1 . LEU   B 2 67  ? -18.805 -4.105  -9.192  1.00 32.16  ? 76  LEU   B CD1 1 
ATOM   888  C  CD2 . LEU   B 2 67  ? -18.160 -2.086  -10.443 1.00 32.70  ? 76  LEU   B CD2 1 
ATOM   889  N  N   . VAL   B 2 68  ? -20.169 0.769   -7.341  1.00 30.97  ? 77  VAL   B N   1 
ATOM   890  C  CA  . VAL   B 2 68  ? -21.224 1.430   -6.526  1.00 29.99  ? 77  VAL   B CA  1 
ATOM   891  C  C   . VAL   B 2 68  ? -22.564 1.410   -7.258  1.00 29.42  ? 77  VAL   B C   1 
ATOM   892  O  O   . VAL   B 2 68  ? -22.594 1.534   -8.500  1.00 29.23  ? 77  VAL   B O   1 
ATOM   893  C  CB  . VAL   B 2 68  ? -20.756 2.835   -6.137  1.00 30.22  ? 77  VAL   B CB  1 
ATOM   894  C  CG1 . VAL   B 2 68  ? -20.448 3.686   -7.372  1.00 30.86  ? 77  VAL   B CG1 1 
ATOM   895  C  CG2 . VAL   B 2 68  ? -21.753 3.529   -5.205  1.00 29.93  ? 77  VAL   B CG2 1 
ATOM   896  N  N   . SER   B 2 69  ? -23.634 1.202   -6.524  1.00 28.85  ? 78  SER   B N   1 
ATOM   897  C  CA  . SER   B 2 69  ? -25.013 1.183   -7.040  1.00 29.42  ? 78  SER   B CA  1 
ATOM   898  C  C   . SER   B 2 69  ? -25.781 2.310   -6.357  1.00 29.18  ? 78  SER   B C   1 
ATOM   899  O  O   . SER   B 2 69  ? -25.515 2.635   -5.157  1.00 29.00  ? 78  SER   B O   1 
ATOM   900  C  CB  . SER   B 2 69  ? -25.698 -0.219  -6.934  1.00 29.91  ? 78  SER   B CB  1 
ATOM   901  O  OG  . SER   B 2 69  ? -26.077 -0.537  -5.590  1.00 30.28  ? 78  SER   B OG  1 
ATOM   902  N  N   . TYR   B 2 70  ? -26.701 2.905   -7.089  1.00 29.30  ? 79  TYR   B N   1 
ATOM   903  C  CA  . TYR   B 2 70  ? -27.580 4.015   -6.618  1.00 29.40  ? 79  TYR   B CA  1 
ATOM   904  C  C   . TYR   B 2 70  ? -29.033 3.574   -6.740  1.00 30.28  ? 79  TYR   B C   1 
ATOM   905  O  O   . TYR   B 2 70  ? -29.349 2.985   -7.785  1.00 29.20  ? 79  TYR   B O   1 
ATOM   906  C  CB  . TYR   B 2 70  ? -27.342 5.280   -7.445  1.00 29.81  ? 79  TYR   B CB  1 
ATOM   907  C  CG  . TYR   B 2 70  ? -26.010 5.921   -7.178  1.00 29.83  ? 79  TYR   B CG  1 
ATOM   908  C  CD1 . TYR   B 2 70  ? -24.851 5.437   -7.743  1.00 30.29  ? 79  TYR   B CD1 1 
ATOM   909  C  CD2 . TYR   B 2 70  ? -25.894 6.981   -6.299  1.00 31.00  ? 79  TYR   B CD2 1 
ATOM   910  C  CE1 . TYR   B 2 70  ? -23.613 5.994   -7.451  1.00 30.31  ? 79  TYR   B CE1 1 
ATOM   911  C  CE2 . TYR   B 2 70  ? -24.668 7.577   -6.018  1.00 31.08  ? 79  TYR   B CE2 1 
ATOM   912  C  CZ  . TYR   B 2 70  ? -23.524 7.053   -6.579  1.00 29.83  ? 79  TYR   B CZ  1 
ATOM   913  O  OH  . TYR   B 2 70  ? -22.303 7.595   -6.304  1.00 31.87  ? 79  TYR   B OH  1 
ATOM   914  N  N   . CYS   B 2 71  ? -29.848 3.880   -5.721  1.00 31.52  ? 80  CYS   B N   1 
ATOM   915  C  CA  . CYS   B 2 71  ? -31.319 3.711   -5.649  1.00 34.47  ? 80  CYS   B CA  1 
ATOM   916  C  C   . CYS   B 2 71  ? -31.679 2.267   -5.343  1.00 34.70  ? 80  CYS   B C   1 
ATOM   917  O  O   . CYS   B 2 71  ? -32.831 2.000   -5.080  1.00 36.21  ? 80  CYS   B O   1 
ATOM   918  C  CB  . CYS   B 2 71  ? -32.027 4.152   -6.928  1.00 38.27  ? 80  CYS   B CB  1 
ATOM   919  S  SG  . CYS   B 2 71  ? -31.558 5.846   -7.401  1.00 43.51  ? 80  CYS   B SG  1 
ATOM   920  N  N   . GLY   B 2 72  ? -30.730 1.338   -5.369  1.00 33.48  ? 81  GLY   B N   1 
ATOM   921  C  CA  . GLY   B 2 72  ? -31.146 -0.054  -5.142  1.00 33.28  ? 81  GLY   B CA  1 
ATOM   922  C  C   . GLY   B 2 72  ? -29.911 -0.919  -5.217  1.00 32.02  ? 81  GLY   B C   1 
ATOM   923  O  O   . GLY   B 2 72  ? -28.824 -0.399  -5.476  1.00 31.08  ? 81  GLY   B O   1 
ATOM   924  N  N   . PRO   B 2 73  ? -30.053 -2.226  -4.974  1.00 32.90  ? 82  PRO   B N   1 
ATOM   925  C  CA  . PRO   B 2 73  ? -28.902 -3.124  -5.036  1.00 33.93  ? 82  PRO   B CA  1 
ATOM   926  C  C   . PRO   B 2 73  ? -28.376 -3.350  -6.468  1.00 34.00  ? 82  PRO   B C   1 
ATOM   927  O  O   . PRO   B 2 73  ? -29.154 -3.206  -7.390  1.00 35.33  ? 82  PRO   B O   1 
ATOM   928  C  CB  . PRO   B 2 73  ? -29.459 -4.424  -4.418  1.00 35.01  ? 82  PRO   B CB  1 
ATOM   929  C  CG  . PRO   B 2 73  ? -30.964 -4.376  -4.682  1.00 35.26  ? 82  PRO   B CG  1 
ATOM   930  C  CD  . PRO   B 2 73  ? -31.329 -2.907  -4.677  1.00 34.34  ? 82  PRO   B CD  1 
ATOM   931  N  N   . TRP   B 2 74  ? -27.105 -3.768  -6.594  1.00 34.32  ? 83  TRP   B N   1 
ATOM   932  C  CA  . TRP   B 2 74  ? -26.451 -4.168  -7.857  1.00 34.29  ? 83  TRP   B CA  1 
ATOM   933  C  C   . TRP   B 2 74  ? -27.348 -5.166  -8.594  1.00 36.62  ? 83  TRP   B C   1 
ATOM   934  O  O   . TRP   B 2 74  ? -27.693 -6.200  -8.001  1.00 37.93  ? 83  TRP   B O   1 
ATOM   935  C  CB  . TRP   B 2 74  ? -25.058 -4.741  -7.609  1.00 34.01  ? 83  TRP   B CB  1 
ATOM   936  C  CG  . TRP   B 2 74  ? -24.253 -4.904  -8.862  1.00 32.77  ? 83  TRP   B CG  1 
ATOM   937  C  CD1 . TRP   B 2 74  ? -24.219 -5.997  -9.656  1.00 32.69  ? 83  TRP   B CD1 1 
ATOM   938  C  CD2 . TRP   B 2 74  ? -23.402 -3.911  -9.490  1.00 32.37  ? 83  TRP   B CD2 1 
ATOM   939  N  NE1 . TRP   B 2 74  ? -23.366 -5.770  -10.706 1.00 33.20  ? 83  TRP   B NE1 1 
ATOM   940  C  CE2 . TRP   B 2 74  ? -22.835 -4.514  -10.623 1.00 32.10  ? 83  TRP   B CE2 1 
ATOM   941  C  CE3 . TRP   B 2 74  ? -23.028 -2.588  -9.180  1.00 32.16  ? 83  TRP   B CE3 1 
ATOM   942  C  CZ2 . TRP   B 2 74  ? -22.041 -3.813  -11.535 1.00 32.37  ? 83  TRP   B CZ2 1 
ATOM   943  C  CZ3 . TRP   B 2 74  ? -22.176 -1.916  -10.036 1.00 31.98  ? 83  TRP   B CZ3 1 
ATOM   944  C  CH2 . TRP   B 2 74  ? -21.700 -2.527  -11.211 1.00 31.96  ? 83  TRP   B CH2 1 
ATOM   945  N  N   . LYS   B 2 75  ? -27.667 -4.875  -9.869  1.00 36.89  ? 84  LYS   B N   1 
ATOM   946  C  CA  . LYS   B 2 75  ? -28.623 -5.653  -10.701 1.00 37.90  ? 84  LYS   B CA  1 
ATOM   947  C  C   . LYS   B 2 75  ? -27.900 -6.490  -11.756 1.00 37.77  ? 84  LYS   B C   1 
ATOM   948  O  O   . LYS   B 2 75  ? -28.541 -7.413  -12.249 1.00 38.85  ? 84  LYS   B O   1 
ATOM   949  C  CB  . LYS   B 2 75  ? -29.591 -4.708  -11.401 1.00 38.97  ? 84  LYS   B CB  1 
ATOM   950  C  CG  . LYS   B 2 75  ? -30.457 -3.874  -10.471 1.00 39.51  ? 84  LYS   B CG  1 
ATOM   951  C  CD  . LYS   B 2 75  ? -31.494 -4.709  -9.789  1.00 41.88  ? 84  LYS   B CD  1 
ATOM   952  C  CE  . LYS   B 2 75  ? -32.198 -3.912  -8.710  1.00 44.19  ? 84  LYS   B CE  1 
ATOM   953  N  NZ  . LYS   B 2 75  ? -33.487 -4.543  -8.374  1.00 46.91  ? 84  LYS   B NZ  1 
ATOM   954  N  N   . LEU   B 2 76  ? -26.656 -6.182  -12.106 1.00 37.56  ? 85  LEU   B N   1 
ATOM   955  C  CA  . LEU   B 2 76  ? -25.970 -6.743  -13.308 1.00 39.85  ? 85  LEU   B CA  1 
ATOM   956  C  C   . LEU   B 2 76  ? -25.266 -8.051  -12.921 1.00 42.68  ? 85  LEU   B C   1 
ATOM   957  O  O   . LEU   B 2 76  ? -24.332 -8.008  -12.087 1.00 42.29  ? 85  LEU   B O   1 
ATOM   958  C  CB  . LEU   B 2 76  ? -24.975 -5.710  -13.854 1.00 39.34  ? 85  LEU   B CB  1 
ATOM   959  C  CG  . LEU   B 2 76  ? -25.534 -4.279  -13.982 1.00 39.15  ? 85  LEU   B CG  1 
ATOM   960  C  CD1 . LEU   B 2 76  ? -24.567 -3.329  -14.651 1.00 39.03  ? 85  LEU   B CD1 1 
ATOM   961  C  CD2 . LEU   B 2 76  ? -26.849 -4.247  -14.723 1.00 40.89  ? 85  LEU   B CD2 1 
ATOM   962  N  N   . ASP   B 2 77  ? -25.685 -9.176  -13.500 1.00 45.93  ? 86  ASP   B N   1 
ATOM   963  C  CA  . ASP   B 2 77  ? -25.175 -10.499 -13.070 1.00 50.66  ? 86  ASP   B CA  1 
ATOM   964  C  C   . ASP   B 2 77  ? -24.578 -11.276 -14.247 1.00 48.74  ? 86  ASP   B C   1 
ATOM   965  O  O   . ASP   B 2 77  ? -24.070 -12.337 -14.008 1.00 47.90  ? 86  ASP   B O   1 
ATOM   966  C  CB  . ASP   B 2 77  ? -26.256 -11.315 -12.357 1.00 56.65  ? 86  ASP   B CB  1 
ATOM   967  C  CG  . ASP   B 2 77  ? -27.564 -11.396 -13.105 1.00 64.07  ? 86  ASP   B CG  1 
ATOM   968  O  OD1 . ASP   B 2 77  ? -27.608 -10.934 -14.264 1.00 70.12  ? 86  ASP   B OD1 1 
ATOM   969  O  OD2 . ASP   B 2 77  ? -28.538 -11.896 -12.513 1.00 71.95  ? 86  ASP   B OD2 1 
ATOM   970  N  N   . ALA   B 2 78  ? -24.590 -10.763 -15.474 1.00 45.73  ? 87  ALA   B N   1 
ATOM   971  C  CA  . ALA   B 2 78  ? -24.047 -11.527 -16.600 1.00 44.45  ? 87  ALA   B CA  1 
ATOM   972  C  C   . ALA   B 2 78  ? -22.520 -11.574 -16.466 1.00 43.31  ? 87  ALA   B C   1 
ATOM   973  O  O   . ALA   B 2 78  ? -21.866 -10.634 -15.857 1.00 42.08  ? 87  ALA   B O   1 
ATOM   974  C  CB  . ALA   B 2 78  ? -24.536 -10.967 -17.921 1.00 44.82  ? 87  ALA   B CB  1 
ATOM   975  N  N   . ALA   B 2 79  ? -21.954 -12.621 -17.058 1.00 44.06  ? 88  ALA   B N   1 
ATOM   976  C  CA  . ALA   B 2 79  ? -20.545 -13.019 -16.909 1.00 44.52  ? 88  ALA   B CA  1 
ATOM   977  C  C   . ALA   B 2 79  ? -19.950 -13.273 -18.295 1.00 43.40  ? 88  ALA   B C   1 
ATOM   978  O  O   . ALA   B 2 79  ? -20.663 -13.857 -19.107 1.00 42.43  ? 88  ALA   B O   1 
ATOM   979  C  CB  . ALA   B 2 79  ? -20.503 -14.244 -16.017 1.00 46.16  ? 88  ALA   B CB  1 
ATOM   980  N  N   . TRP   B 2 80  ? -18.739 -12.763 -18.574 1.00 43.23  ? 89  TRP   B N   1 
ATOM   981  C  CA  . TRP   B 2 80  ? -17.912 -13.135 -19.754 1.00 46.35  ? 89  TRP   B CA  1 
ATOM   982  C  C   . TRP   B 2 80  ? -17.861 -14.652 -19.822 1.00 47.19  ? 89  TRP   B C   1 
ATOM   983  O  O   . TRP   B 2 80  ? -17.699 -15.218 -18.707 1.00 44.20  ? 89  TRP   B O   1 
ATOM   984  C  CB  . TRP   B 2 80  ? -16.477 -12.592 -19.690 1.00 46.16  ? 89  TRP   B CB  1 
ATOM   985  C  CG  . TRP   B 2 80  ? -15.689 -12.948 -20.914 1.00 46.47  ? 89  TRP   B CG  1 
ATOM   986  C  CD1 . TRP   B 2 80  ? -16.152 -13.005 -22.203 1.00 48.10  ? 89  TRP   B CD1 1 
ATOM   987  C  CD2 . TRP   B 2 80  ? -14.297 -13.303 -20.978 1.00 47.59  ? 89  TRP   B CD2 1 
ATOM   988  N  NE1 . TRP   B 2 80  ? -15.147 -13.353 -23.054 1.00 47.87  ? 89  TRP   B NE1 1 
ATOM   989  C  CE2 . TRP   B 2 80  ? -13.999 -13.570 -22.330 1.00 47.50  ? 89  TRP   B CE2 1 
ATOM   990  C  CE3 . TRP   B 2 80  ? -13.288 -13.482 -20.021 1.00 47.54  ? 89  TRP   B CE3 1 
ATOM   991  C  CZ2 . TRP   B 2 80  ? -12.726 -13.949 -22.756 1.00 47.46  ? 89  TRP   B CZ2 1 
ATOM   992  C  CZ3 . TRP   B 2 80  ? -12.027 -13.852 -20.452 1.00 47.16  ? 89  TRP   B CZ3 1 
ATOM   993  C  CH2 . TRP   B 2 80  ? -11.754 -14.075 -21.796 1.00 46.64  ? 89  TRP   B CH2 1 
ATOM   994  N  N   . ASP   B 2 81  ? -18.028 -15.245 -21.021 1.00 48.65  ? 90  ASP   B N   1 
ATOM   995  C  CA  . ASP   B 2 81  ? -18.095 -16.729 -21.213 1.00 51.92  ? 90  ASP   B CA  1 
ATOM   996  C  C   . ASP   B 2 81  ? -16.667 -17.290 -21.123 1.00 54.02  ? 90  ASP   B C   1 
ATOM   997  O  O   . ASP   B 2 81  ? -16.567 -18.499 -21.020 1.00 57.53  ? 90  ASP   B O   1 
ATOM   998  C  CB  . ASP   B 2 81  ? -18.835 -17.185 -22.495 1.00 49.59  ? 90  ASP   B CB  1 
ATOM   999  C  CG  . ASP   B 2 81  ? -18.224 -16.670 -23.771 1.00 51.73  ? 90  ASP   B CG  1 
ATOM   1000 O  OD1 . ASP   B 2 81  ? -17.164 -16.062 -23.658 1.00 55.15  ? 90  ASP   B OD1 1 
ATOM   1001 O  OD2 . ASP   B 2 81  ? -18.840 -16.796 -24.868 1.00 52.47  ? 90  ASP   B OD2 1 
ATOM   1002 N  N   . GLY   B 2 82  ? -15.635 -16.435 -21.182 1.00 55.13  ? 91  GLY   B N   1 
ATOM   1003 C  CA  . GLY   B 2 82  ? -14.210 -16.809 -21.208 1.00 54.51  ? 91  GLY   B CA  1 
ATOM   1004 C  C   . GLY   B 2 82  ? -13.696 -17.158 -22.604 1.00 57.27  ? 91  GLY   B C   1 
ATOM   1005 O  O   . GLY   B 2 82  ? -12.535 -17.632 -22.695 1.00 56.37  ? 91  GLY   B O   1 
ATOM   1006 N  N   . LEU   B 2 83  ? -14.514 -16.980 -23.649 1.00 58.16  ? 92  LEU   B N   1 
ATOM   1007 C  CA  . LEU   B 2 83  ? -14.243 -17.427 -25.047 1.00 60.99  ? 92  LEU   B CA  1 
ATOM   1008 C  C   . LEU   B 2 83  ? -14.563 -16.335 -26.076 1.00 61.89  ? 92  LEU   B C   1 
ATOM   1009 O  O   . LEU   B 2 83  ? -13.747 -16.098 -27.010 1.00 61.68  ? 92  LEU   B O   1 
ATOM   1010 C  CB  . LEU   B 2 83  ? -15.146 -18.620 -25.341 1.00 63.99  ? 92  LEU   B CB  1 
ATOM   1011 C  CG  . LEU   B 2 83  ? -14.731 -19.966 -24.758 1.00 67.09  ? 92  LEU   B CG  1 
ATOM   1012 C  CD1 . LEU   B 2 83  ? -15.716 -21.022 -25.228 1.00 69.14  ? 92  LEU   B CD1 1 
ATOM   1013 C  CD2 . LEU   B 2 83  ? -13.317 -20.369 -25.180 1.00 67.84  ? 92  LEU   B CD2 1 
ATOM   1014 N  N   . SER   B 2 84  ? -15.771 -15.784 -26.007 1.00 60.22  ? 93  SER   B N   1 
ATOM   1015 C  CA  . SER   B 2 84  ? -16.371 -14.961 -27.089 1.00 59.20  ? 93  SER   B CA  1 
ATOM   1016 C  C   . SER   B 2 84  ? -15.798 -13.551 -27.029 1.00 56.88  ? 93  SER   B C   1 
ATOM   1017 O  O   . SER   B 2 84  ? -15.295 -13.138 -25.966 1.00 52.41  ? 93  SER   B O   1 
ATOM   1018 C  CB  . SER   B 2 84  ? -17.858 -14.927 -26.977 1.00 59.38  ? 93  SER   B CB  1 
ATOM   1019 O  OG  . SER   B 2 84  ? -18.305 -16.211 -26.563 1.00 60.60  ? 93  SER   B OG  1 
ATOM   1020 N  N   . GLU   B 2 85  ? -15.825 -12.869 -28.163 1.00 55.21  ? 94  GLU   B N   1 
ATOM   1021 C  CA  . GLU   B 2 85  ? -15.530 -11.422 -28.189 1.00 54.03  ? 94  GLU   B CA  1 
ATOM   1022 C  C   . GLU   B 2 85  ? -16.649 -10.807 -27.281 1.00 50.25  ? 94  GLU   B C   1 
ATOM   1023 O  O   . GLU   B 2 85  ? -17.697 -11.498 -26.960 1.00 50.44  ? 94  GLU   B O   1 
ATOM   1024 C  CB  . GLU   B 2 85  ? -15.314 -10.943 -29.650 1.00 56.05  ? 94  GLU   B CB  1 
ATOM   1025 C  CG  . GLU   B 2 85  ? -13.927 -11.339 -30.225 1.00 56.75  ? 94  GLU   B CG  1 
ATOM   1026 C  CD  . GLU   B 2 85  ? -13.429 -10.624 -31.491 1.00 60.78  ? 94  GLU   B CD  1 
ATOM   1027 O  OE1 . GLU   B 2 85  ? -14.202 -9.819  -32.077 1.00 57.67  ? 94  GLU   B OE1 1 
ATOM   1028 O  OE2 . GLU   B 2 85  ? -12.251 -10.884 -31.906 1.00 61.47  ? 94  GLU   B OE2 1 
ATOM   1029 N  N   . VAL   B 2 86  ? -16.359 -9.554  -26.949 1.00 47.73  ? 95  VAL   B N   1 
ATOM   1030 C  CA  . VAL   B 2 86  ? -17.308 -8.664  -26.242 1.00 43.96  ? 95  VAL   B CA  1 
ATOM   1031 C  C   . VAL   B 2 86  ? -17.265 -7.300  -26.896 1.00 43.58  ? 95  VAL   B C   1 
ATOM   1032 O  O   . VAL   B 2 86  ? -16.315 -7.048  -27.649 1.00 46.13  ? 95  VAL   B O   1 
ATOM   1033 C  CB  . VAL   B 2 86  ? -16.908 -8.552  -24.752 1.00 41.79  ? 95  VAL   B CB  1 
ATOM   1034 C  CG1 . VAL   B 2 86  ? -16.745 -9.907  -24.132 1.00 41.72  ? 95  VAL   B CG1 1 
ATOM   1035 C  CG2 . VAL   B 2 86  ? -15.601 -7.775  -24.592 1.00 41.59  ? 95  VAL   B CG2 1 
ATOM   1036 N  N   . GLN   B 2 87  ? -18.181 -6.404  -26.491 1.00 42.72  ? 96  GLN   B N   1 
ATOM   1037 C  CA  . GLN   B 2 87  ? -18.148 -4.993  -26.950 1.00 42.58  ? 96  GLN   B CA  1 
ATOM   1038 C  C   . GLN   B 2 87  ? -18.070 -4.062  -25.746 1.00 39.13  ? 96  GLN   B C   1 
ATOM   1039 O  O   . GLN   B 2 87  ? -18.875 -4.212  -24.873 1.00 39.28  ? 96  GLN   B O   1 
ATOM   1040 C  CB  . GLN   B 2 87  ? -19.343 -4.663  -27.855 1.00 43.52  ? 96  GLN   B CB  1 
ATOM   1041 C  CG  . GLN   B 2 87  ? -19.401 -5.527  -29.098 1.00 45.18  ? 96  GLN   B CG  1 
ATOM   1042 C  CD  . GLN   B 2 87  ? -20.248 -4.923  -30.204 1.00 46.51  ? 96  GLN   B CD  1 
ATOM   1043 O  OE1 . GLN   B 2 87  ? -21.035 -4.007  -29.988 1.00 46.85  ? 96  GLN   B OE1 1 
ATOM   1044 N  NE2 . GLN   B 2 87  ? -20.087 -5.437  -31.405 1.00 47.77  ? 96  GLN   B NE2 1 
ATOM   1045 N  N   . LEU   B 2 88  ? -17.060 -3.196  -25.745 1.00 38.02  ? 97  LEU   B N   1 
ATOM   1046 C  CA  . LEU   B 2 88  ? -16.985 -1.986  -24.913 1.00 37.58  ? 97  LEU   B CA  1 
ATOM   1047 C  C   . LEU   B 2 88  ? -17.902 -0.953  -25.574 1.00 37.73  ? 97  LEU   B C   1 
ATOM   1048 O  O   . LEU   B 2 88  ? -17.643 -0.556  -26.719 1.00 38.79  ? 97  LEU   B O   1 
ATOM   1049 C  CB  . LEU   B 2 88  ? -15.528 -1.489  -24.780 1.00 38.09  ? 97  LEU   B CB  1 
ATOM   1050 C  CG  . LEU   B 2 88  ? -15.366 -0.204  -23.969 1.00 37.91  ? 97  LEU   B CG  1 
ATOM   1051 C  CD1 . LEU   B 2 88  ? -15.764 -0.376  -22.498 1.00 38.01  ? 97  LEU   B CD1 1 
ATOM   1052 C  CD2 . LEU   B 2 88  ? -13.975 0.391   -24.073 1.00 38.10  ? 97  LEU   B CD2 1 
ATOM   1053 N  N   . LEU   B 2 89  ? -18.983 -0.607  -24.921 1.00 37.54  ? 98  LEU   B N   1 
ATOM   1054 C  CA  . LEU   B 2 89  ? -19.783 0.596   -25.285 1.00 37.80  ? 98  LEU   B CA  1 
ATOM   1055 C  C   . LEU   B 2 89  ? -19.051 1.788   -24.684 1.00 37.76  ? 98  LEU   B C   1 
ATOM   1056 O  O   . LEU   B 2 89  ? -19.462 2.277   -23.586 1.00 38.13  ? 98  LEU   B O   1 
ATOM   1057 C  CB  . LEU   B 2 89  ? -21.187 0.353   -24.751 1.00 38.28  ? 98  LEU   B CB  1 
ATOM   1058 C  CG  . LEU   B 2 89  ? -22.259 1.442   -24.965 1.00 39.87  ? 98  LEU   B CG  1 
ATOM   1059 C  CD1 . LEU   B 2 89  ? -21.961 2.340   -26.124 1.00 41.23  ? 98  LEU   B CD1 1 
ATOM   1060 C  CD2 . LEU   B 2 89  ? -23.643 0.820   -25.119 1.00 40.81  ? 98  LEU   B CD2 1 
ATOM   1061 N  N   . ALA   B 2 90  ? -17.961 2.226   -25.337 1.00 38.55  ? 99  ALA   B N   1 
ATOM   1062 C  CA  . ALA   B 2 90  ? -17.180 3.406   -24.879 1.00 38.87  ? 99  ALA   B CA  1 
ATOM   1063 C  C   . ALA   B 2 90  ? -18.070 4.640   -24.982 1.00 38.91  ? 99  ALA   B C   1 
ATOM   1064 O  O   . ALA   B 2 90  ? -18.712 4.805   -26.052 1.00 40.00  ? 99  ALA   B O   1 
ATOM   1065 C  CB  . ALA   B 2 90  ? -15.912 3.652   -25.663 1.00 39.34  ? 99  ALA   B CB  1 
ATOM   1066 N  N   . VAL   B 2 91  ? -18.080 5.449   -23.915 1.00 38.56  ? 100 VAL   B N   1 
ATOM   1067 C  CA  . VAL   B 2 91  ? -18.686 6.799   -23.896 1.00 38.11  ? 100 VAL   B CA  1 
ATOM   1068 C  C   . VAL   B 2 91  ? -17.596 7.794   -23.503 1.00 38.72  ? 100 VAL   B C   1 
ATOM   1069 O  O   . VAL   B 2 91  ? -17.480 8.214   -22.368 1.00 37.69  ? 100 VAL   B O   1 
ATOM   1070 C  CB  . VAL   B 2 91  ? -19.890 6.788   -22.975 1.00 37.10  ? 100 VAL   B CB  1 
ATOM   1071 C  CG1 . VAL   B 2 91  ? -20.570 8.148   -22.934 1.00 37.85  ? 100 VAL   B CG1 1 
ATOM   1072 C  CG2 . VAL   B 2 91  ? -20.858 5.693   -23.403 1.00 37.15  ? 100 VAL   B CG2 1 
ATOM   1073 N  N   . PRO   B 2 92  ? -16.741 8.207   -24.454 1.00 39.82  ? 101 PRO   B N   1 
ATOM   1074 C  CA  . PRO   B 2 92  ? -15.634 9.105   -24.138 1.00 39.94  ? 101 PRO   B CA  1 
ATOM   1075 C  C   . PRO   B 2 92  ? -16.120 10.517  -23.911 1.00 40.15  ? 101 PRO   B C   1 
ATOM   1076 O  O   . PRO   B 2 92  ? -17.210 10.838  -24.352 1.00 39.48  ? 101 PRO   B O   1 
ATOM   1077 C  CB  . PRO   B 2 92  ? -14.686 9.006   -25.333 1.00 41.61  ? 101 PRO   B CB  1 
ATOM   1078 C  CG  . PRO   B 2 92  ? -15.306 7.993   -26.278 1.00 41.59  ? 101 PRO   B CG  1 
ATOM   1079 C  CD  . PRO   B 2 92  ? -16.710 7.701   -25.826 1.00 40.61  ? 101 PRO   B CD  1 
ATOM   1080 N  N   . PRO   B 2 93  ? -15.345 11.358  -23.191 1.00 41.52  ? 102 PRO   B N   1 
ATOM   1081 C  CA  . PRO   B 2 93  ? -15.756 12.719  -22.889 1.00 43.34  ? 102 PRO   B CA  1 
ATOM   1082 C  C   . PRO   B 2 93  ? -15.916 13.537  -24.185 1.00 45.09  ? 102 PRO   B C   1 
ATOM   1083 O  O   . PRO   B 2 93  ? -15.072 13.482  -25.040 1.00 46.96  ? 102 PRO   B O   1 
ATOM   1084 C  CB  . PRO   B 2 93  ? -14.637 13.235  -21.965 1.00 43.14  ? 102 PRO   B CB  1 
ATOM   1085 C  CG  . PRO   B 2 93  ? -14.086 11.952  -21.354 1.00 43.42  ? 102 PRO   B CG  1 
ATOM   1086 C  CD  . PRO   B 2 93  ? -14.050 11.031  -22.557 1.00 43.13  ? 102 PRO   B CD  1 
ATOM   1087 N  N   . GLY   B 2 94  ? -17.052 14.214  -24.314 1.00 45.48  ? 103 GLY   B N   1 
ATOM   1088 C  CA  . GLY   B 2 94  ? -17.413 15.046  -25.473 1.00 46.52  ? 103 GLY   B CA  1 
ATOM   1089 C  C   . GLY   B 2 94  ? -17.674 14.270  -26.762 1.00 47.35  ? 103 GLY   B C   1 
ATOM   1090 O  O   . GLY   B 2 94  ? -17.877 14.917  -27.787 1.00 49.14  ? 103 GLY   B O   1 
ATOM   1091 N  N   . GLU   B 2 95  ? -17.677 12.948  -26.763 1.00 46.41  ? 104 GLU   B N   1 
ATOM   1092 C  CA  . GLU   B 2 95  ? -17.752 12.152  -28.013 1.00 47.09  ? 104 GLU   B CA  1 
ATOM   1093 C  C   . GLU   B 2 95  ? -18.948 11.222  -27.900 1.00 47.24  ? 104 GLU   B C   1 
ATOM   1094 O  O   . GLU   B 2 95  ? -19.397 10.972  -26.762 1.00 47.00  ? 104 GLU   B O   1 
ATOM   1095 C  CB  . GLU   B 2 95  ? -16.438 11.379  -28.240 1.00 48.00  ? 104 GLU   B CB  1 
ATOM   1096 C  CG  . GLU   B 2 95  ? -15.214 12.298  -28.362 1.00 50.18  ? 104 GLU   B CG  1 
ATOM   1097 C  CD  . GLU   B 2 95  ? -13.822 11.662  -28.468 1.00 52.72  ? 104 GLU   B CD  1 
ATOM   1098 O  OE1 . GLU   B 2 95  ? -13.716 10.436  -28.249 1.00 53.46  ? 104 GLU   B OE1 1 
ATOM   1099 O  OE2 . GLU   B 2 95  ? -12.813 12.405  -28.751 1.00 53.85  ? 104 GLU   B OE2 1 
ATOM   1100 N  N   . ARG   B 2 96  ? -19.478 10.752  -29.012 1.00 47.87  ? 105 ARG   B N   1 
ATOM   1101 C  CA  . ARG   B 2 96  ? -20.689 9.897   -29.033 1.00 50.73  ? 105 ARG   B CA  1 
ATOM   1102 C  C   . ARG   B 2 96  ? -20.362 8.529   -28.460 1.00 49.23  ? 105 ARG   B C   1 
ATOM   1103 O  O   . ARG   B 2 96  ? -19.264 7.988   -28.778 1.00 47.85  ? 105 ARG   B O   1 
ATOM   1104 C  CB  . ARG   B 2 96  ? -21.176 9.717   -30.475 1.00 57.33  ? 105 ARG   B CB  1 
ATOM   1105 C  CG  . ARG   B 2 96  ? -22.560 9.094   -30.613 1.00 61.73  ? 105 ARG   B CG  1 
ATOM   1106 C  CD  . ARG   B 2 96  ? -23.381 9.717   -31.752 1.00 64.75  ? 105 ARG   B CD  1 
ATOM   1107 N  NE  . ARG   B 2 96  ? -22.737 9.762   -33.065 1.00 67.62  ? 105 ARG   B NE  1 
ATOM   1108 C  CZ  . ARG   B 2 96  ? -22.260 10.860  -33.690 1.00 71.39  ? 105 ARG   B CZ  1 
ATOM   1109 N  NH1 . ARG   B 2 96  ? -22.326 12.067  -33.145 1.00 69.84  ? 105 ARG   B NH1 1 
ATOM   1110 N  NH2 . ARG   B 2 96  ? -21.715 10.743  -34.893 1.00 72.90  ? 105 ARG   B NH2 1 
ATOM   1111 N  N   . ALA   B 2 97  ? -21.320 7.913   -27.783 1.00 47.60  ? 106 ALA   B N   1 
ATOM   1112 C  CA  . ALA   B 2 97  ? -21.278 6.462   -27.500 1.00 47.86  ? 106 ALA   B CA  1 
ATOM   1113 C  C   . ALA   B 2 97  ? -20.777 5.738   -28.756 1.00 49.37  ? 106 ALA   B C   1 
ATOM   1114 O  O   . ALA   B 2 97  ? -21.313 5.982   -29.819 1.00 46.03  ? 106 ALA   B O   1 
ATOM   1115 C  CB  . ALA   B 2 97  ? -22.634 5.964   -27.090 1.00 47.34  ? 106 ALA   B CB  1 
ATOM   1116 N  N   . LYS   B 2 98  ? -19.802 4.838   -28.616 1.00 49.99  ? 107 LYS   B N   1 
ATOM   1117 C  CA  . LYS   B 2 98  ? -19.259 4.015   -29.728 1.00 52.61  ? 107 LYS   B CA  1 
ATOM   1118 C  C   . LYS   B 2 98  ? -18.960 2.593   -29.230 1.00 51.61  ? 107 LYS   B C   1 
ATOM   1119 O  O   . LYS   B 2 98  ? -18.276 2.486   -28.186 1.00 51.14  ? 107 LYS   B O   1 
ATOM   1120 C  CB  . LYS   B 2 98  ? -17.990 4.696   -30.239 1.00 58.25  ? 107 LYS   B CB  1 
ATOM   1121 C  CG  . LYS   B 2 98  ? -17.362 4.108   -31.505 1.00 65.88  ? 107 LYS   B CG  1 
ATOM   1122 C  CD  . LYS   B 2 98  ? -15.888 4.533   -31.703 1.00 71.79  ? 107 LYS   B CD  1 
ATOM   1123 C  CE  . LYS   B 2 98  ? -15.201 4.920   -30.396 1.00 73.74  ? 107 LYS   B CE  1 
ATOM   1124 N  NZ  . LYS   B 2 98  ? -13.774 5.262   -30.599 1.00 78.47  ? 107 LYS   B NZ  1 
ATOM   1125 N  N   . ASN   B 2 99  ? -19.515 1.568   -29.887 1.00 48.08  ? 108 ASN   B N   1 
ATOM   1126 C  CA  . ASN   B 2 99  ? -19.177 0.142   -29.659 1.00 48.38  ? 108 ASN   B CA  1 
ATOM   1127 C  C   . ASN   B 2 99  ? -17.780 -0.148  -30.207 1.00 49.00  ? 108 ASN   B C   1 
ATOM   1128 O  O   . ASN   B 2 99  ? -17.502 0.198   -31.348 1.00 50.48  ? 108 ASN   B O   1 
ATOM   1129 C  CB  . ASN   B 2 99  ? -20.194 -0.840  -30.246 1.00 47.96  ? 108 ASN   B CB  1 
ATOM   1130 C  CG  . ASN   B 2 99  ? -21.550 -0.691  -29.593 1.00 50.34  ? 108 ASN   B CG  1 
ATOM   1131 O  OD1 . ASN   B 2 99  ? -22.095 0.415   -29.558 1.00 51.32  ? 108 ASN   B OD1 1 
ATOM   1132 N  ND2 . ASN   B 2 99  ? -22.126 -1.778  -29.102 1.00 49.71  ? 108 ASN   B ND2 1 
ATOM   1133 N  N   . ILE   B 2 100 ? -16.935 -0.812  -29.436 1.00 46.92  ? 109 ILE   B N   1 
ATOM   1134 C  CA  . ILE   B 2 100 ? -15.623 -1.301  -29.897 1.00 47.16  ? 109 ILE   B CA  1 
ATOM   1135 C  C   . ILE   B 2 100 ? -15.578 -2.771  -29.541 1.00 46.92  ? 109 ILE   B C   1 
ATOM   1136 O  O   . ILE   B 2 100 ? -15.735 -3.113  -28.323 1.00 46.94  ? 109 ILE   B O   1 
ATOM   1137 C  CB  . ILE   B 2 100 ? -14.493 -0.534  -29.211 1.00 49.04  ? 109 ILE   B CB  1 
ATOM   1138 C  CG1 . ILE   B 2 100 ? -14.654 0.977   -29.355 1.00 50.63  ? 109 ILE   B CG1 1 
ATOM   1139 C  CG2 . ILE   B 2 100 ? -13.150 -1.041  -29.689 1.00 50.90  ? 109 ILE   B CG2 1 
ATOM   1140 C  CD1 . ILE   B 2 100 ? -14.270 1.481   -30.721 1.00 52.34  ? 109 ILE   B CD1 1 
ATOM   1141 N  N   . GLN   B 2 101 ? -15.384 -3.638  -30.506 1.00 47.43  ? 110 GLN   B N   1 
ATOM   1142 C  CA  . GLN   B 2 101 ? -15.500 -5.080  -30.225 1.00 49.35  ? 110 GLN   B CA  1 
ATOM   1143 C  C   . GLN   B 2 101 ? -14.089 -5.611  -30.055 1.00 50.21  ? 110 GLN   B C   1 
ATOM   1144 O  O   . GLN   B 2 101 ? -13.216 -5.127  -30.778 1.00 50.50  ? 110 GLN   B O   1 
ATOM   1145 C  CB  . GLN   B 2 101 ? -16.261 -5.797  -31.318 1.00 51.71  ? 110 GLN   B CB  1 
ATOM   1146 C  CG  . GLN   B 2 101 ? -16.188 -7.309  -31.185 1.00 51.07  ? 110 GLN   B CG  1 
ATOM   1147 C  CD  . GLN   B 2 101 ? -17.164 -7.928  -32.155 1.00 53.12  ? 110 GLN   B CD  1 
ATOM   1148 O  OE1 . GLN   B 2 101 ? -18.257 -7.399  -32.427 1.00 49.74  ? 110 GLN   B OE1 1 
ATOM   1149 N  NE2 . GLN   B 2 101 ? -16.737 -9.032  -32.728 1.00 54.13  ? 110 GLN   B NE2 1 
ATOM   1150 N  N   . THR   B 2 102 ? -13.877 -6.541  -29.096 1.00 51.13  ? 111 THR   B N   1 
ATOM   1151 C  CA  . THR   B 2 102 ? -12.528 -7.055  -28.748 1.00 49.69  ? 111 THR   B CA  1 
ATOM   1152 C  C   . THR   B 2 102 ? -12.656 -8.409  -28.066 1.00 48.36  ? 111 THR   B C   1 
ATOM   1153 O  O   . THR   B 2 102 ? -13.746 -8.711  -27.594 1.00 49.12  ? 111 THR   B O   1 
ATOM   1154 C  CB  . THR   B 2 102 ? -11.770 -6.017  -27.916 1.00 48.74  ? 111 THR   B CB  1 
ATOM   1155 O  OG1 . THR   B 2 102 ? -10.402 -6.393  -27.796 1.00 47.92  ? 111 THR   B OG1 1 
ATOM   1156 C  CG2 . THR   B 2 102 ? -12.325 -5.824  -26.526 1.00 49.26  ? 111 THR   B CG2 1 
ATOM   1157 N  N   . LEU   B 2 103 ? -11.619 -9.246  -28.193 1.00 48.08  ? 112 LEU   B N   1 
ATOM   1158 C  CA  . LEU   B 2 103 ? -11.456 -10.499 -27.416 1.00 47.48  ? 112 LEU   B CA  1 
ATOM   1159 C  C   . LEU   B 2 103 ? -10.657 -10.158 -26.158 1.00 47.38  ? 112 LEU   B C   1 
ATOM   1160 O  O   . LEU   B 2 103 ? -9.469  -9.777  -26.240 1.00 47.82  ? 112 LEU   B O   1 
ATOM   1161 C  CB  . LEU   B 2 103 ? -10.700 -11.571 -28.231 1.00 49.34  ? 112 LEU   B CB  1 
ATOM   1162 C  CG  . LEU   B 2 103 ? -10.505 -12.865 -27.432 1.00 49.53  ? 112 LEU   B CG  1 
ATOM   1163 C  CD1 . LEU   B 2 103 ? -11.813 -13.642 -27.415 1.00 50.07  ? 112 LEU   B CD1 1 
ATOM   1164 C  CD2 . LEU   B 2 103 ? -9.360  -13.729 -27.962 1.00 51.93  ? 112 LEU   B CD2 1 
ATOM   1165 N  N   . PRO   B 2 104 ? -11.254 -10.309 -24.951 1.00 45.44  ? 113 PRO   B N   1 
ATOM   1166 C  CA  . PRO   B 2 104 ? -10.562 -9.960  -23.728 1.00 45.46  ? 113 PRO   B CA  1 
ATOM   1167 C  C   . PRO   B 2 104 ? -9.396  -10.929 -23.505 1.00 47.24  ? 113 PRO   B C   1 
ATOM   1168 O  O   . PRO   B 2 104 ? -9.474  -12.100 -23.896 1.00 46.34  ? 113 PRO   B O   1 
ATOM   1169 C  CB  . PRO   B 2 104 ? -11.574 -10.169 -22.586 1.00 44.94  ? 113 PRO   B CB  1 
ATOM   1170 C  CG  . PRO   B 2 104 ? -12.911 -10.304 -23.297 1.00 45.37  ? 113 PRO   B CG  1 
ATOM   1171 C  CD  . PRO   B 2 104 ? -12.595 -10.858 -24.687 1.00 45.57  ? 113 PRO   B CD  1 
ATOM   1172 N  N   . GLY   B 2 105 ? -8.364  -10.376 -22.877 1.00 48.67  ? 114 GLY   B N   1 
ATOM   1173 C  CA  . GLY   B 2 105 ? -7.306  -11.129 -22.198 1.00 49.97  ? 114 GLY   B CA  1 
ATOM   1174 C  C   . GLY   B 2 105 ? -7.766  -11.512 -20.814 1.00 49.78  ? 114 GLY   B C   1 
ATOM   1175 O  O   . GLY   B 2 105 ? -8.987  -11.483 -20.548 1.00 48.12  ? 114 GLY   B O   1 
ATOM   1176 N  N   . ILE   B 2 106 ? -6.798  -11.859 -19.977 1.00 51.26  ? 115 ILE   B N   1 
ATOM   1177 C  CA  . ILE   B 2 106 ? -6.990  -12.476 -18.637 1.00 50.25  ? 115 ILE   B CA  1 
ATOM   1178 C  C   . ILE   B 2 106 ? -6.094  -11.749 -17.636 1.00 48.69  ? 115 ILE   B C   1 
ATOM   1179 O  O   . ILE   B 2 106 ? -4.894  -11.601 -17.856 1.00 48.76  ? 115 ILE   B O   1 
ATOM   1180 C  CB  . ILE   B 2 106 ? -6.634  -13.963 -18.681 1.00 53.72  ? 115 ILE   B CB  1 
ATOM   1181 C  CG1 . ILE   B 2 106 ? -7.445  -14.721 -19.733 1.00 58.44  ? 115 ILE   B CG1 1 
ATOM   1182 C  CG2 . ILE   B 2 106 ? -6.817  -14.570 -17.322 1.00 55.11  ? 115 ILE   B CG2 1 
ATOM   1183 C  CD1 . ILE   B 2 106 ? -8.805  -15.137 -19.260 1.00 57.82  ? 115 ILE   B CD1 1 
ATOM   1184 N  N   . PHE   B 2 107 ? -6.678  -11.310 -16.546 1.00 46.39  ? 116 PHE   B N   1 
ATOM   1185 C  CA  . PHE   B 2 107 ? -5.958  -10.968 -15.305 1.00 45.56  ? 116 PHE   B CA  1 
ATOM   1186 C  C   . PHE   B 2 107 ? -5.918  -12.250 -14.488 1.00 47.20  ? 116 PHE   B C   1 
ATOM   1187 O  O   . PHE   B 2 107 ? -7.007  -12.738 -14.148 1.00 45.52  ? 116 PHE   B O   1 
ATOM   1188 C  CB  . PHE   B 2 107 ? -6.735  -9.895  -14.567 1.00 45.99  ? 116 PHE   B CB  1 
ATOM   1189 C  CG  . PHE   B 2 107 ? -6.495  -8.464  -14.951 1.00 45.91  ? 116 PHE   B CG  1 
ATOM   1190 C  CD1 . PHE   B 2 107 ? -5.721  -8.114  -16.039 1.00 46.89  ? 116 PHE   B CD1 1 
ATOM   1191 C  CD2 . PHE   B 2 107 ? -7.054  -7.463  -14.170 1.00 46.56  ? 116 PHE   B CD2 1 
ATOM   1192 C  CE1 . PHE   B 2 107 ? -5.499  -6.785  -16.350 1.00 48.57  ? 116 PHE   B CE1 1 
ATOM   1193 C  CE2 . PHE   B 2 107 ? -6.843  -6.129  -14.494 1.00 47.01  ? 116 PHE   B CE2 1 
ATOM   1194 C  CZ  . PHE   B 2 107 ? -6.085  -5.791  -15.587 1.00 48.25  ? 116 PHE   B CZ  1 
ATOM   1195 N  N   . LYS   B 2 108 ? -4.718  -12.813 -14.293 1.00 48.42  ? 117 LYS   B N   1 
ATOM   1196 C  CA  . LYS   B 2 108 ? -4.443  -13.939 -13.361 1.00 50.77  ? 117 LYS   B CA  1 
ATOM   1197 C  C   . LYS   B 2 108 ? -4.133  -13.348 -11.980 1.00 46.96  ? 117 LYS   B C   1 
ATOM   1198 O  O   . LYS   B 2 108 ? -3.187  -12.521 -11.872 1.00 44.81  ? 117 LYS   B O   1 
ATOM   1199 C  CB  . LYS   B 2 108 ? -3.275  -14.788 -13.887 1.00 56.37  ? 117 LYS   B CB  1 
ATOM   1200 C  CG  . LYS   B 2 108 ? -3.669  -15.951 -14.783 1.00 64.31  ? 117 LYS   B CG  1 
ATOM   1201 C  CD  . LYS   B 2 108 ? -2.614  -16.373 -15.810 1.00 70.73  ? 117 LYS   B CD  1 
ATOM   1202 C  CE  . LYS   B 2 108 ? -3.151  -17.384 -16.818 1.00 79.23  ? 117 LYS   B CE  1 
ATOM   1203 N  NZ  . LYS   B 2 108 ? -2.194  -17.754 -17.911 1.00 82.26  ? 117 LYS   B NZ  1 
ATOM   1204 N  N   . THR   B 2 109 ? -4.946  -13.699 -10.984 1.00 45.42  ? 118 THR   B N   1 
ATOM   1205 C  CA  . THR   B 2 109 ? -4.767  -13.290 -9.565  1.00 45.88  ? 118 THR   B CA  1 
ATOM   1206 C  C   . THR   B 2 109 ? -4.813  -14.516 -8.651  1.00 46.18  ? 118 THR   B C   1 
ATOM   1207 O  O   . THR   B 2 109 ? -5.330  -15.584 -9.032  1.00 44.17  ? 118 THR   B O   1 
ATOM   1208 C  CB  . THR   B 2 109 ? -5.823  -12.303 -9.051  1.00 44.49  ? 118 THR   B CB  1 
ATOM   1209 O  OG1 . THR   B 2 109 ? -6.993  -13.026 -8.668  1.00 43.66  ? 118 THR   B OG1 1 
ATOM   1210 C  CG2 . THR   B 2 109 ? -6.129  -11.218 -10.055 1.00 45.19  ? 118 THR   B CG2 1 
ATOM   1211 N  N   . LYS   B 2 110 ? -4.358  -14.309 -7.432  1.00 49.44  ? 119 LYS   B N   1 
ATOM   1212 C  CA  . LYS   B 2 110 ? -4.295  -15.364 -6.384  1.00 51.43  ? 119 LYS   B CA  1 
ATOM   1213 C  C   . LYS   B 2 110 ? -5.720  -15.875 -6.109  1.00 53.34  ? 119 LYS   B C   1 
ATOM   1214 O  O   . LYS   B 2 110 ? -5.836  -17.046 -5.694  1.00 55.53  ? 119 LYS   B O   1 
ATOM   1215 C  CB  . LYS   B 2 110 ? -3.592  -14.775 -5.155  1.00 52.68  ? 119 LYS   B CB  1 
ATOM   1216 C  CG  . LYS   B 2 110 ? -4.309  -13.618 -4.481  1.00 55.52  ? 119 LYS   B CG  1 
ATOM   1217 C  CD  . LYS   B 2 110 ? -3.553  -13.033 -3.286  1.00 56.75  ? 119 LYS   B CD  1 
ATOM   1218 C  CE  . LYS   B 2 110 ? -4.279  -13.173 -1.973  1.00 59.38  ? 119 LYS   B CE  1 
ATOM   1219 N  NZ  . LYS   B 2 110 ? -5.424  -12.246 -1.879  1.00 59.82  ? 119 LYS   B NZ  1 
ATOM   1220 N  N   . ASP   B 2 111 ? -6.760  -15.055 -6.350  1.00 51.93  ? 120 ASP   B N   1 
ATOM   1221 C  CA  . ASP   B 2 111 ? -8.183  -15.388 -6.064  1.00 51.97  ? 120 ASP   B CA  1 
ATOM   1222 C  C   . ASP   B 2 111 ? -8.941  -15.771 -7.330  1.00 52.88  ? 120 ASP   B C   1 
ATOM   1223 O  O   . ASP   B 2 111 ? -10.169 -15.928 -7.232  1.00 55.81  ? 120 ASP   B O   1 
ATOM   1224 C  CB  . ASP   B 2 111 ? -8.899  -14.205 -5.421  1.00 53.45  ? 120 ASP   B CB  1 
ATOM   1225 C  CG  . ASP   B 2 111 ? -8.292  -13.853 -4.081  1.00 54.42  ? 120 ASP   B CG  1 
ATOM   1226 O  OD1 . ASP   B 2 111 ? -7.938  -14.777 -3.345  1.00 52.84  ? 120 ASP   B OD1 1 
ATOM   1227 O  OD2 . ASP   B 2 111 ? -8.145  -12.676 -3.819  1.00 60.22  ? 120 ASP   B OD2 1 
ATOM   1228 N  N   . GLY   B 2 112 ? -8.268  -15.861 -8.475  1.00 51.48  ? 121 GLY   B N   1 
ATOM   1229 C  CA  . GLY   B 2 112 ? -8.909  -16.319 -9.709  1.00 52.20  ? 121 GLY   B CA  1 
ATOM   1230 C  C   . GLY   B 2 112 ? -8.617  -15.433 -10.914 1.00 50.54  ? 121 GLY   B C   1 
ATOM   1231 O  O   . GLY   B 2 112 ? -8.049  -14.352 -10.738 1.00 50.20  ? 121 GLY   B O   1 
ATOM   1232 N  N   . ASP   B 2 113 ? -8.986  -15.920 -12.095 1.00 50.89  ? 122 ASP   B N   1 
ATOM   1233 C  CA  . ASP   B 2 113 ? -8.796  -15.226 -13.397 1.00 50.53  ? 122 ASP   B CA  1 
ATOM   1234 C  C   . ASP   B 2 113 ? -9.975  -14.262 -13.618 1.00 50.88  ? 122 ASP   B C   1 
ATOM   1235 O  O   . ASP   B 2 113 ? -11.097 -14.552 -13.151 1.00 46.82  ? 122 ASP   B O   1 
ATOM   1236 C  CB  . ASP   B 2 113 ? -8.678  -16.220 -14.539 1.00 54.62  ? 122 ASP   B CB  1 
ATOM   1237 C  CG  . ASP   B 2 113 ? -7.377  -17.006 -14.589 1.00 57.04  ? 122 ASP   B CG  1 
ATOM   1238 O  OD1 . ASP   B 2 113 ? -6.491  -16.732 -13.774 1.00 58.30  ? 122 ASP   B OD1 1 
ATOM   1239 O  OD2 . ASP   B 2 113 ? -7.264  -17.855 -15.497 1.00 62.17  ? 122 ASP   B OD2 1 
ATOM   1240 N  N   . ILE   B 2 114 ? -9.715  -13.127 -14.267 1.00 49.26  ? 123 ILE   B N   1 
ATOM   1241 C  CA  . ILE   B 2 114 ? -10.747 -12.107 -14.575 1.00 49.51  ? 123 ILE   B CA  1 
ATOM   1242 C  C   . ILE   B 2 114 ? -10.523 -11.684 -16.031 1.00 46.38  ? 123 ILE   B C   1 
ATOM   1243 O  O   . ILE   B 2 114 ? -9.379  -11.377 -16.357 1.00 44.72  ? 123 ILE   B O   1 
ATOM   1244 C  CB  . ILE   B 2 114 ? -10.653 -10.875 -13.644 1.00 48.85  ? 123 ILE   B CB  1 
ATOM   1245 C  CG1 . ILE   B 2 114 ? -10.330 -11.201 -12.196 1.00 53.31  ? 123 ILE   B CG1 1 
ATOM   1246 C  CG2 . ILE   B 2 114 ? -11.907 -10.043 -13.719 1.00 50.63  ? 123 ILE   B CG2 1 
ATOM   1247 C  CD1 . ILE   B 2 114 ? -9.973  -9.963  -11.392 1.00 52.97  ? 123 ILE   B CD1 1 
ATOM   1248 N  N   . GLY   B 2 115 ? -11.596 -11.527 -16.812 1.00 45.36  ? 124 GLY   B N   1 
ATOM   1249 C  CA  . GLY   B 2 115 ? -11.507 -10.906 -18.152 1.00 43.68  ? 124 GLY   B CA  1 
ATOM   1250 C  C   . GLY   B 2 115 ? -10.838 -9.542  -18.072 1.00 42.84  ? 124 GLY   B C   1 
ATOM   1251 O  O   . GLY   B 2 115 ? -10.931 -8.849  -17.007 1.00 38.91  ? 124 GLY   B O   1 
ATOM   1252 N  N   . ALA   B 2 116 ? -10.137 -9.163  -19.132 1.00 42.55  ? 125 ALA   B N   1 
ATOM   1253 C  CA  . ALA   B 2 116 ? -9.452  -7.858  -19.233 1.00 44.61  ? 125 ALA   B CA  1 
ATOM   1254 C  C   . ALA   B 2 116 ? -9.599  -7.371  -20.662 1.00 45.29  ? 125 ALA   B C   1 
ATOM   1255 O  O   . ALA   B 2 116 ? -9.481  -8.208  -21.575 1.00 47.29  ? 125 ALA   B O   1 
ATOM   1256 C  CB  . ALA   B 2 116 ? -7.993  -7.957  -18.862 1.00 46.01  ? 125 ALA   B CB  1 
ATOM   1257 N  N   A VAL   B 2 117 ? -9.880  -6.077  -20.864 0.25 45.13  ? 126 VAL   B N   1 
ATOM   1258 N  N   B VAL   B 2 117 ? -9.763  -6.054  -20.832 0.01 45.02  ? 126 VAL   B N   1 
ATOM   1259 N  N   C VAL   B 2 117 ? -9.883  -6.078  -20.863 0.33 45.08  ? 126 VAL   B N   1 
ATOM   1260 N  N   D VAL   B 2 117 ? -9.771  -6.054  -20.829 0.40 44.74  ? 126 VAL   B N   1 
ATOM   1261 C  CA  A VAL   B 2 117 ? -9.912  -5.451  -22.221 0.25 45.95  ? 126 VAL   B CA  1 
ATOM   1262 C  CA  B VAL   B 2 117 ? -9.945  -5.350  -22.138 0.01 45.41  ? 126 VAL   B CA  1 
ATOM   1263 C  CA  C VAL   B 2 117 ? -9.911  -5.451  -22.219 0.33 45.93  ? 126 VAL   B CA  1 
ATOM   1264 C  CA  D VAL   B 2 117 ? -9.944  -5.349  -22.133 0.40 45.18  ? 126 VAL   B CA  1 
ATOM   1265 C  C   A VAL   B 2 117 ? -8.755  -4.451  -22.355 0.25 46.22  ? 126 VAL   B C   1 
ATOM   1266 C  C   B VAL   B 2 117 ? -8.767  -4.387  -22.361 0.01 45.76  ? 126 VAL   B C   1 
ATOM   1267 C  C   C VAL   B 2 117 ? -8.754  -4.452  -22.355 0.33 46.25  ? 126 VAL   B C   1 
ATOM   1268 C  C   D VAL   B 2 117 ? -8.764  -4.389  -22.358 0.40 45.90  ? 126 VAL   B C   1 
ATOM   1269 O  O   A VAL   B 2 117 ? -8.542  -3.648  -21.424 0.25 45.65  ? 126 VAL   B O   1 
ATOM   1270 O  O   B VAL   B 2 117 ? -8.553  -3.524  -21.484 0.01 45.19  ? 126 VAL   B O   1 
ATOM   1271 O  O   C VAL   B 2 117 ? -8.542  -3.646  -21.425 0.33 45.68  ? 126 VAL   B O   1 
ATOM   1272 O  O   D VAL   B 2 117 ? -8.552  -3.519  -21.487 0.40 45.32  ? 126 VAL   B O   1 
ATOM   1273 C  CB  A VAL   B 2 117 ? -11.273 -4.804  -22.546 0.25 46.24  ? 126 VAL   B CB  1 
ATOM   1274 C  CB  B VAL   B 2 117 ? -11.298 -4.611  -22.140 0.01 44.95  ? 126 VAL   B CB  1 
ATOM   1275 C  CB  C VAL   B 2 117 ? -11.272 -4.805  -22.547 0.33 46.30  ? 126 VAL   B CB  1 
ATOM   1276 C  CB  D VAL   B 2 117 ? -11.295 -4.608  -22.138 0.40 44.89  ? 126 VAL   B CB  1 
ATOM   1277 C  CG1 A VAL   B 2 117 ? -12.401 -5.822  -22.458 0.25 46.45  ? 126 VAL   B CG1 1 
ATOM   1278 C  CG1 B VAL   B 2 117 ? -11.437 -3.653  -23.311 0.01 45.30  ? 126 VAL   B CG1 1 
ATOM   1279 C  CG1 C VAL   B 2 117 ? -12.399 -5.823  -22.459 0.33 46.54  ? 126 VAL   B CG1 1 
ATOM   1280 C  CG1 D VAL   B 2 117 ? -11.439 -3.648  -23.302 0.40 45.04  ? 126 VAL   B CG1 1 
ATOM   1281 C  CG2 A VAL   B 2 117 ? -11.572 -3.587  -21.686 0.25 45.65  ? 126 VAL   B CG2 1 
ATOM   1282 C  CG2 B VAL   B 2 117 ? -12.464 -5.587  -22.105 0.01 44.91  ? 126 VAL   B CG2 1 
ATOM   1283 C  CG2 C VAL   B 2 117 ? -11.572 -3.586  -21.689 0.33 45.72  ? 126 VAL   B CG2 1 
ATOM   1284 C  CG2 D VAL   B 2 117 ? -12.461 -5.584  -22.104 0.40 45.03  ? 126 VAL   B CG2 1 
ATOM   1285 N  N   . ALA   B 2 118 ? -8.058  -4.495  -23.497 1.00 46.10  ? 127 ALA   B N   1 
ATOM   1286 C  CA  . ALA   B 2 118 ? -6.864  -3.644  -23.795 1.00 48.07  ? 127 ALA   B CA  1 
ATOM   1287 C  C   . ALA   B 2 118 ? -7.236  -2.544  -24.792 1.00 50.20  ? 127 ALA   B C   1 
ATOM   1288 O  O   . ALA   B 2 118 ? -6.944  -2.675  -25.996 1.00 52.35  ? 127 ALA   B O   1 
ATOM   1289 C  CB  . ALA   B 2 118 ? -5.709  -4.477  -24.324 1.00 49.23  ? 127 ALA   B CB  1 
ATOM   1290 N  N   . LEU   B 2 119 ? -8.026  -1.576  -24.355 1.00 49.70  ? 128 LEU   B N   1 
ATOM   1291 C  CA  . LEU   B 2 119 ? -8.491  -0.475  -25.205 1.00 50.74  ? 128 LEU   B CA  1 
ATOM   1292 C  C   . LEU   B 2 119 ? -8.154  0.828   -24.484 1.00 54.34  ? 128 LEU   B C   1 
ATOM   1293 O  O   . LEU   B 2 119 ? -8.345  0.909   -23.264 1.00 59.54  ? 128 LEU   B O   1 
ATOM   1294 C  CB  . LEU   B 2 119 ? -9.986  -0.674  -25.453 1.00 49.93  ? 128 LEU   B CB  1 
ATOM   1295 C  CG  . LEU   B 2 119 ? -10.401 -1.980  -26.136 1.00 48.15  ? 128 LEU   B CG  1 
ATOM   1296 C  CD1 . LEU   B 2 119 ? -11.917 -2.187  -26.075 1.00 45.59  ? 128 LEU   B CD1 1 
ATOM   1297 C  CD2 . LEU   B 2 119 ? -9.945  -1.992  -27.576 1.00 50.06  ? 128 LEU   B CD2 1 
ATOM   1298 N  N   . ASP   B 2 120 ? -7.632  1.809   -25.203 1.00 59.76  ? 129 ASP   B N   1 
ATOM   1299 C  CA  . ASP   B 2 120 ? -7.063  3.021   -24.572 1.00 62.87  ? 129 ASP   B CA  1 
ATOM   1300 C  C   . ASP   B 2 120 ? -8.098  4.142   -24.664 1.00 58.96  ? 129 ASP   B C   1 
ATOM   1301 O  O   . ASP   B 2 120 ? -8.355  4.606   -25.771 1.00 65.34  ? 129 ASP   B O   1 
ATOM   1302 C  CB  . ASP   B 2 120 ? -5.714  3.375   -25.209 1.00 68.69  ? 129 ASP   B CB  1 
ATOM   1303 C  CG  . ASP   B 2 120 ? -4.594  3.443   -24.176 1.00 73.45  ? 129 ASP   B CG  1 
ATOM   1304 O  OD1 . ASP   B 2 120 ? -4.839  3.941   -23.027 1.00 71.02  ? 129 ASP   B OD1 1 
ATOM   1305 O  OD2 . ASP   B 2 120 ? -3.508  2.948   -24.492 1.00 80.30  ? 129 ASP   B OD2 1 
ATOM   1306 N  N   . TYR   B 2 121 ? -8.676  4.579   -23.556 1.00 55.35  ? 130 TYR   B N   1 
ATOM   1307 C  CA  . TYR   B 2 121 ? -9.580  5.748   -23.575 1.00 54.12  ? 130 TYR   B CA  1 
ATOM   1308 C  C   . TYR   B 2 121 ? -9.236  6.660   -22.420 1.00 51.24  ? 130 TYR   B C   1 
ATOM   1309 O  O   . TYR   B 2 121 ? -8.568  6.243   -21.485 1.00 49.85  ? 130 TYR   B O   1 
ATOM   1310 C  CB  . TYR   B 2 121 ? -11.034 5.308   -23.503 1.00 55.25  ? 130 TYR   B CB  1 
ATOM   1311 C  CG  . TYR   B 2 121 ? -11.553 4.717   -24.781 1.00 58.40  ? 130 TYR   B CG  1 
ATOM   1312 C  CD1 . TYR   B 2 121 ? -12.065 5.537   -25.772 1.00 61.45  ? 130 TYR   B CD1 1 
ATOM   1313 C  CD2 . TYR   B 2 121 ? -11.541 3.350   -25.011 1.00 60.46  ? 130 TYR   B CD2 1 
ATOM   1314 C  CE1 . TYR   B 2 121 ? -12.559 5.014   -26.953 1.00 63.51  ? 130 TYR   B CE1 1 
ATOM   1315 C  CE2 . TYR   B 2 121 ? -12.026 2.811   -26.198 1.00 63.59  ? 130 TYR   B CE2 1 
ATOM   1316 C  CZ  . TYR   B 2 121 ? -12.530 3.650   -27.175 1.00 64.49  ? 130 TYR   B CZ  1 
ATOM   1317 O  OH  . TYR   B 2 121 ? -13.014 3.170   -28.358 1.00 70.30  ? 130 TYR   B OH  1 
ATOM   1318 N  N   . PRO   B 2 122 ? -9.705  7.916   -22.407 1.00 49.87  ? 131 PRO   B N   1 
ATOM   1319 C  CA  . PRO   B 2 122 ? -9.395  8.783   -21.291 1.00 49.76  ? 131 PRO   B CA  1 
ATOM   1320 C  C   . PRO   B 2 122 ? -10.095 8.179   -20.061 1.00 46.21  ? 131 PRO   B C   1 
ATOM   1321 O  O   . PRO   B 2 122 ? -10.995 7.301   -20.178 1.00 42.75  ? 131 PRO   B O   1 
ATOM   1322 C  CB  . PRO   B 2 122 ? -9.908  10.167  -21.723 1.00 51.84  ? 131 PRO   B CB  1 
ATOM   1323 C  CG  . PRO   B 2 122 ? -10.245 10.034  -23.195 1.00 52.80  ? 131 PRO   B CG  1 
ATOM   1324 C  CD  . PRO   B 2 122 ? -10.579 8.571   -23.395 1.00 52.92  ? 131 PRO   B CD  1 
ATOM   1325 N  N   . ALA   B 2 123 ? -9.652  8.652   -18.909 1.00 45.93  ? 132 ALA   B N   1 
ATOM   1326 C  CA  . ALA   B 2 123 ? -10.092 8.171   -17.589 1.00 43.57  ? 132 ALA   B CA  1 
ATOM   1327 C  C   . ALA   B 2 123 ? -11.567 8.505   -17.412 1.00 43.52  ? 132 ALA   B C   1 
ATOM   1328 O  O   . ALA   B 2 123 ? -12.311 7.660   -16.773 1.00 40.36  ? 132 ALA   B O   1 
ATOM   1329 C  CB  . ALA   B 2 123 ? -9.197  8.748   -16.537 1.00 44.19  ? 132 ALA   B CB  1 
ATOM   1330 N  N   . GLY   B 2 124 ? -12.018 9.612   -18.039 1.00 41.18  ? 133 GLY   B N   1 
ATOM   1331 C  CA  . GLY   B 2 124 ? -13.437 9.996   -18.015 1.00 39.41  ? 133 GLY   B CA  1 
ATOM   1332 C  C   . GLY   B 2 124 ? -14.334 8.934   -18.649 1.00 37.61  ? 133 GLY   B C   1 
ATOM   1333 O  O   . GLY   B 2 124 ? -15.553 9.085   -18.493 1.00 35.85  ? 133 GLY   B O   1 
ATOM   1334 N  N   . THR   B 2 125 ? -13.788 7.899   -19.296 1.00 36.60  ? 134 THR   B N   1 
ATOM   1335 C  CA  . THR   B 2 125 ? -14.589 6.775   -19.879 1.00 38.06  ? 134 THR   B CA  1 
ATOM   1336 C  C   . THR   B 2 125 ? -14.911 5.677   -18.835 1.00 37.80  ? 134 THR   B C   1 
ATOM   1337 O  O   . THR   B 2 125 ? -15.717 4.702   -19.152 1.00 36.94  ? 134 THR   B O   1 
ATOM   1338 C  CB  . THR   B 2 125 ? -13.880 6.236   -21.122 1.00 41.60  ? 134 THR   B CB  1 
ATOM   1339 O  OG1 . THR   B 2 125 ? -13.515 7.337   -21.958 1.00 43.30  ? 134 THR   B OG1 1 
ATOM   1340 C  CG2 . THR   B 2 125 ? -14.725 5.333   -21.992 1.00 42.48  ? 134 THR   B CG2 1 
ATOM   1341 N  N   . SER   B 2 126 ? -14.307 5.787   -17.646 1.00 36.64  ? 135 SER   B N   1 
ATOM   1342 C  CA  . SER   B 2 126 ? -14.503 4.842   -16.506 1.00 35.77  ? 135 SER   B CA  1 
ATOM   1343 C  C   . SER   B 2 126 ? -15.989 4.591   -16.265 1.00 34.33  ? 135 SER   B C   1 
ATOM   1344 O  O   . SER   B 2 126 ? -16.780 5.591   -16.062 1.00 34.44  ? 135 SER   B O   1 
ATOM   1345 C  CB  . SER   B 2 126 ? -13.872 5.382   -15.283 1.00 35.99  ? 135 SER   B CB  1 
ATOM   1346 O  OG  . SER   B 2 126 ? -12.475 5.281   -15.365 1.00 36.93  ? 135 SER   B OG  1 
ATOM   1347 N  N   . GLY   B 2 127 ? -16.412 3.338   -16.293 1.00 33.48  ? 136 GLY   B N   1 
ATOM   1348 C  CA  . GLY   B 2 127 ? -17.822 3.012   -16.004 1.00 34.27  ? 136 GLY   B CA  1 
ATOM   1349 C  C   . GLY   B 2 127 ? -18.592 2.618   -17.237 1.00 34.38  ? 136 GLY   B C   1 
ATOM   1350 O  O   . GLY   B 2 127 ? -19.676 2.006   -17.085 1.00 33.72  ? 136 GLY   B O   1 
ATOM   1351 N  N   . SER   B 2 128 ? -17.994 2.816   -18.415 1.00 34.66  ? 137 SER   B N   1 
ATOM   1352 C  CA  . SER   B 2 128 ? -18.592 2.335   -19.667 1.00 35.11  ? 137 SER   B CA  1 
ATOM   1353 C  C   . SER   B 2 128 ? -18.777 0.842   -19.548 1.00 34.11  ? 137 SER   B C   1 
ATOM   1354 O  O   . SER   B 2 128 ? -17.850 0.120   -19.181 1.00 34.38  ? 137 SER   B O   1 
ATOM   1355 C  CB  . SER   B 2 128 ? -17.803 2.711   -20.902 1.00 35.62  ? 137 SER   B CB  1 
ATOM   1356 O  OG  . SER   B 2 128 ? -17.451 4.085   -20.937 1.00 36.52  ? 137 SER   B OG  1 
ATOM   1357 N  N   . PRO   B 2 129 ? -19.957 0.353   -19.984 1.00 34.29  ? 138 PRO   B N   1 
ATOM   1358 C  CA  . PRO   B 2 129 ? -20.292 -1.059  -19.919 1.00 33.79  ? 138 PRO   B CA  1 
ATOM   1359 C  C   . PRO   B 2 129 ? -19.671 -1.928  -21.002 1.00 35.33  ? 138 PRO   B C   1 
ATOM   1360 O  O   . PRO   B 2 129 ? -19.484 -1.532  -22.208 1.00 34.67  ? 138 PRO   B O   1 
ATOM   1361 C  CB  . PRO   B 2 129 ? -21.814 -1.112  -20.116 1.00 34.00  ? 138 PRO   B CB  1 
ATOM   1362 C  CG  . PRO   B 2 129 ? -22.137 0.163   -20.925 1.00 33.99  ? 138 PRO   B CG  1 
ATOM   1363 C  CD  . PRO   B 2 129 ? -21.088 1.174   -20.494 1.00 33.97  ? 138 PRO   B CD  1 
ATOM   1364 N  N   . ILE   B 2 130 ? -19.419 -3.158  -20.591 1.00 35.73  ? 139 ILE   B N   1 
ATOM   1365 C  CA  . ILE   B 2 130 ? -18.878 -4.212  -21.475 1.00 36.93  ? 139 ILE   B CA  1 
ATOM   1366 C  C   . ILE   B 2 130 ? -20.017 -5.180  -21.700 1.00 37.56  ? 139 ILE   B C   1 
ATOM   1367 O  O   . ILE   B 2 130 ? -20.639 -5.537  -20.716 1.00 35.89  ? 139 ILE   B O   1 
ATOM   1368 C  CB  . ILE   B 2 130 ? -17.655 -4.879  -20.856 1.00 37.68  ? 139 ILE   B CB  1 
ATOM   1369 C  CG1 . ILE   B 2 130 ? -16.511 -3.883  -20.649 1.00 38.68  ? 139 ILE   B CG1 1 
ATOM   1370 C  CG2 . ILE   B 2 130 ? -17.231 -6.050  -21.718 1.00 37.79  ? 139 ILE   B CG2 1 
ATOM   1371 C  CD1 . ILE   B 2 130 ? -15.611 -4.286  -19.514 1.00 39.10  ? 139 ILE   B CD1 1 
ATOM   1372 N  N   . LEU   B 2 131 ? -20.280 -5.545  -22.968 1.00 40.34  ? 140 LEU   B N   1 
ATOM   1373 C  CA  . LEU   B 2 131 ? -21.470 -6.349  -23.335 1.00 42.69  ? 140 LEU   B CA  1 
ATOM   1374 C  C   . LEU   B 2 131 ? -21.090 -7.705  -23.911 1.00 43.30  ? 140 LEU   B C   1 
ATOM   1375 O  O   . LEU   B 2 131 ? -20.105 -7.766  -24.628 1.00 45.36  ? 140 LEU   B O   1 
ATOM   1376 C  CB  . LEU   B 2 131 ? -22.237 -5.613  -24.420 1.00 45.29  ? 140 LEU   B CB  1 
ATOM   1377 C  CG  . LEU   B 2 131 ? -22.570 -4.155  -24.149 1.00 45.84  ? 140 LEU   B CG  1 
ATOM   1378 C  CD1 . LEU   B 2 131 ? -23.488 -3.626  -25.269 1.00 46.80  ? 140 LEU   B CD1 1 
ATOM   1379 C  CD2 . LEU   B 2 131 ? -23.191 -3.983  -22.761 1.00 45.28  ? 140 LEU   B CD2 1 
ATOM   1380 N  N   . ASP   B 2 132 ? -21.958 -8.688  -23.700 1.00 44.36  ? 141 ASP   B N   1 
ATOM   1381 C  CA  . ASP   B 2 132 ? -21.966 -9.965  -24.444 1.00 48.21  ? 141 ASP   B CA  1 
ATOM   1382 C  C   . ASP   B 2 132 ? -22.861 -9.809  -25.675 1.00 51.20  ? 141 ASP   B C   1 
ATOM   1383 O  O   . ASP   B 2 132 ? -23.417 -8.712  -25.868 1.00 49.40  ? 141 ASP   B O   1 
ATOM   1384 C  CB  . ASP   B 2 132 ? -22.418 -11.127 -23.557 1.00 48.71  ? 141 ASP   B CB  1 
ATOM   1385 C  CG  . ASP   B 2 132 ? -23.887 -11.155 -23.197 1.00 49.26  ? 141 ASP   B CG  1 
ATOM   1386 O  OD1 . ASP   B 2 132 ? -24.649 -10.358 -23.715 1.00 47.80  ? 141 ASP   B OD1 1 
ATOM   1387 O  OD2 . ASP   B 2 132 ? -24.237 -11.975 -22.327 1.00 53.97  ? 141 ASP   B OD2 1 
ATOM   1388 N  N   . LYS   B 2 133 ? -23.039 -10.912 -26.409 1.00 54.72  ? 142 LYS   B N   1 
ATOM   1389 C  CA  . LYS   B 2 133 ? -23.615 -10.938 -27.777 1.00 59.69  ? 142 LYS   B CA  1 
ATOM   1390 C  C   . LYS   B 2 133 ? -25.110 -10.689 -27.687 1.00 58.27  ? 142 LYS   B C   1 
ATOM   1391 O  O   . LYS   B 2 133 ? -25.684 -10.437 -28.721 1.00 57.22  ? 142 LYS   B O   1 
ATOM   1392 C  CB  . LYS   B 2 133 ? -23.348 -12.283 -28.478 1.00 62.64  ? 142 LYS   B CB  1 
ATOM   1393 C  CG  . LYS   B 2 133 ? -22.063 -12.317 -29.297 1.00 67.99  ? 142 LYS   B CG  1 
ATOM   1394 C  CD  . LYS   B 2 133 ? -21.245 -13.609 -29.168 1.00 72.84  ? 142 LYS   B CD  1 
ATOM   1395 C  CE  . LYS   B 2 133 ? -19.860 -13.455 -29.768 1.00 76.92  ? 142 LYS   B CE  1 
ATOM   1396 N  NZ  . LYS   B 2 133 ? -19.288 -14.731 -30.279 1.00 78.01  ? 142 LYS   B NZ  1 
ATOM   1397 N  N   . CYS   B 2 134 ? -25.700 -10.838 -26.501 1.00 57.49  ? 143 CYS   B N   1 
ATOM   1398 C  CA  . CYS   B 2 134 ? -27.149 -10.643 -26.285 1.00 56.47  ? 143 CYS   B CA  1 
ATOM   1399 C  C   . CYS   B 2 134 ? -27.390 -9.238  -25.719 1.00 52.23  ? 143 CYS   B C   1 
ATOM   1400 O  O   . CYS   B 2 134 ? -28.503 -8.960  -25.359 1.00 49.30  ? 143 CYS   B O   1 
ATOM   1401 C  CB  . CYS   B 2 134 ? -27.699 -11.704 -25.347 1.00 60.32  ? 143 CYS   B CB  1 
ATOM   1402 S  SG  . CYS   B 2 134 ? -27.705 -13.375 -26.040 1.00 65.16  ? 143 CYS   B SG  1 
ATOM   1403 N  N   . GLY   B 2 135 ? -26.363 -8.393  -25.663 1.00 50.74  ? 144 GLY   B N   1 
ATOM   1404 C  CA  . GLY   B 2 135 ? -26.444 -7.036  -25.098 1.00 49.36  ? 144 GLY   B CA  1 
ATOM   1405 C  C   . GLY   B 2 135 ? -26.466 -7.001  -23.566 1.00 47.51  ? 144 GLY   B C   1 
ATOM   1406 O  O   . GLY   B 2 135 ? -26.804 -5.959  -23.030 1.00 46.08  ? 144 GLY   B O   1 
ATOM   1407 N  N   . ARG   B 2 136 ? -26.105 -8.082  -22.864 1.00 47.71  ? 145 ARG   B N   1 
ATOM   1408 C  CA  . ARG   B 2 136 ? -26.127 -8.094  -21.371 1.00 48.13  ? 145 ARG   B CA  1 
ATOM   1409 C  C   . ARG   B 2 136 ? -24.852 -7.462  -20.834 1.00 44.16  ? 145 ARG   B C   1 
ATOM   1410 O  O   . ARG   B 2 136 ? -23.762 -7.674  -21.438 1.00 41.86  ? 145 ARG   B O   1 
ATOM   1411 C  CB  . ARG   B 2 136 ? -26.389 -9.499  -20.867 1.00 51.37  ? 145 ARG   B CB  1 
ATOM   1412 C  CG  . ARG   B 2 136 ? -27.859 -9.847  -21.012 1.00 55.34  ? 145 ARG   B CG  1 
ATOM   1413 C  CD  . ARG   B 2 136 ? -28.062 -11.263 -20.597 1.00 59.56  ? 145 ARG   B CD  1 
ATOM   1414 N  NE  . ARG   B 2 136 ? -27.242 -12.030 -21.509 1.00 67.30  ? 145 ARG   B NE  1 
ATOM   1415 C  CZ  . ARG   B 2 136 ? -26.681 -13.201 -21.257 1.00 68.54  ? 145 ARG   B CZ  1 
ATOM   1416 N  NH1 . ARG   B 2 136 ? -26.821 -13.793 -20.075 1.00 69.91  ? 145 ARG   B NH1 1 
ATOM   1417 N  NH2 . ARG   B 2 136 ? -25.991 -13.774 -22.227 1.00 72.40  ? 145 ARG   B NH2 1 
ATOM   1418 N  N   . VAL   B 2 137 ? -24.962 -6.676  -19.764 1.00 39.79  ? 146 VAL   B N   1 
ATOM   1419 C  CA  . VAL   B 2 137 ? -23.743 -6.024  -19.206 1.00 38.66  ? 146 VAL   B CA  1 
ATOM   1420 C  C   . VAL   B 2 137 ? -23.027 -7.103  -18.380 1.00 39.11  ? 146 VAL   B C   1 
ATOM   1421 O  O   . VAL   B 2 137 ? -23.610 -7.537  -17.350 1.00 40.94  ? 146 VAL   B O   1 
ATOM   1422 C  CB  . VAL   B 2 137 ? -23.998 -4.751  -18.395 1.00 37.13  ? 146 VAL   B CB  1 
ATOM   1423 C  CG1 . VAL   B 2 137 ? -22.696 -4.177  -17.875 1.00 36.99  ? 146 VAL   B CG1 1 
ATOM   1424 C  CG2 . VAL   B 2 137 ? -24.717 -3.701  -19.234 1.00 37.92  ? 146 VAL   B CG2 1 
ATOM   1425 N  N   . ILE   B 2 138 ? -21.844 -7.497  -18.841 1.00 38.77  ? 147 ILE   B N   1 
ATOM   1426 C  CA  . ILE   B 2 138 ? -20.953 -8.496  -18.171 1.00 38.99  ? 147 ILE   B CA  1 
ATOM   1427 C  C   . ILE   B 2 138 ? -19.928 -7.800  -17.253 1.00 38.36  ? 147 ILE   B C   1 
ATOM   1428 O  O   . ILE   B 2 138 ? -19.205 -8.532  -16.532 1.00 36.83  ? 147 ILE   B O   1 
ATOM   1429 C  CB  . ILE   B 2 138 ? -20.276 -9.406  -19.221 1.00 38.68  ? 147 ILE   B CB  1 
ATOM   1430 C  CG1 . ILE   B 2 138 ? -19.451 -8.615  -20.235 1.00 39.14  ? 147 ILE   B CG1 1 
ATOM   1431 C  CG2 . ILE   B 2 138 ? -21.311 -10.280 -19.879 1.00 38.49  ? 147 ILE   B CG2 1 
ATOM   1432 C  CD1 . ILE   B 2 138 ? -18.507 -9.470  -21.055 1.00 41.31  ? 147 ILE   B CD1 1 
ATOM   1433 N  N   . GLY   B 2 139 ? -19.919 -6.464  -17.202 1.00 38.12  ? 148 GLY   B N   1 
ATOM   1434 C  CA  . GLY   B 2 139 ? -19.085 -5.681  -16.265 1.00 37.31  ? 148 GLY   B CA  1 
ATOM   1435 C  C   . GLY   B 2 139 ? -18.823 -4.258  -16.743 1.00 37.76  ? 148 GLY   B C   1 
ATOM   1436 O  O   . GLY   B 2 139 ? -19.303 -3.890  -17.863 1.00 36.10  ? 148 GLY   B O   1 
ATOM   1437 N  N   . LEU   B 2 140 ? -18.010 -3.513  -16.000 1.00 36.30  ? 149 LEU   B N   1 
ATOM   1438 C  CA  . LEU   B 2 140 ? -17.675 -2.102  -16.288 1.00 35.93  ? 149 LEU   B CA  1 
ATOM   1439 C  C   . LEU   B 2 140 ? -16.182 -1.963  -16.537 1.00 36.81  ? 149 LEU   B C   1 
ATOM   1440 O  O   . LEU   B 2 140 ? -15.395 -2.681  -15.849 1.00 35.16  ? 149 LEU   B O   1 
ATOM   1441 C  CB  . LEU   B 2 140 ? -18.049 -1.186  -15.128 1.00 35.62  ? 149 LEU   B CB  1 
ATOM   1442 C  CG  . LEU   B 2 140 ? -19.508 -1.204  -14.702 1.00 34.97  ? 149 LEU   B CG  1 
ATOM   1443 C  CD1 . LEU   B 2 140 ? -19.788 -0.120  -13.672 1.00 34.67  ? 149 LEU   B CD1 1 
ATOM   1444 C  CD2 . LEU   B 2 140 ? -20.441 -1.137  -15.884 1.00 35.92  ? 149 LEU   B CD2 1 
ATOM   1445 N  N   . TYR   B 2 141 ? -15.858 -1.068  -17.476 1.00 34.72  ? 150 TYR   B N   1 
ATOM   1446 C  CA  . TYR   B 2 141 ? -14.501 -0.676  -17.920 1.00 35.68  ? 150 TYR   B CA  1 
ATOM   1447 C  C   . TYR   B 2 141 ? -13.966 0.424   -17.040 1.00 35.20  ? 150 TYR   B C   1 
ATOM   1448 O  O   . TYR   B 2 141 ? -14.692 1.373   -16.786 1.00 35.64  ? 150 TYR   B O   1 
ATOM   1449 C  CB  . TYR   B 2 141 ? -14.591 -0.151  -19.377 1.00 37.60  ? 150 TYR   B CB  1 
ATOM   1450 C  CG  . TYR   B 2 141 ? -13.339 0.451   -19.968 1.00 38.64  ? 150 TYR   B CG  1 
ATOM   1451 C  CD1 . TYR   B 2 141 ? -13.124 1.824   -19.954 1.00 39.17  ? 150 TYR   B CD1 1 
ATOM   1452 C  CD2 . TYR   B 2 141 ? -12.347 -0.364  -20.502 1.00 39.71  ? 150 TYR   B CD2 1 
ATOM   1453 C  CE1 . TYR   B 2 141 ? -11.953 2.362   -20.481 1.00 41.58  ? 150 TYR   B CE1 1 
ATOM   1454 C  CE2 . TYR   B 2 141 ? -11.194 0.163   -21.077 1.00 40.70  ? 150 TYR   B CE2 1 
ATOM   1455 C  CZ  . TYR   B 2 141 ? -10.988 1.535   -21.061 1.00 42.15  ? 150 TYR   B CZ  1 
ATOM   1456 O  OH  . TYR   B 2 141 ? -9.850  2.082   -21.622 1.00 45.95  ? 150 TYR   B OH  1 
ATOM   1457 N  N   . GLY   B 2 142 ? -12.709 0.376   -16.649 1.00 36.05  ? 151 GLY   B N   1 
ATOM   1458 C  CA  . GLY   B 2 142 ? -12.121 1.544   -15.963 1.00 37.88  ? 151 GLY   B CA  1 
ATOM   1459 C  C   . GLY   B 2 142 ? -11.241 1.227   -14.762 1.00 38.16  ? 151 GLY   B C   1 
ATOM   1460 O  O   . GLY   B 2 142 ? -10.609 2.218   -14.242 1.00 40.11  ? 151 GLY   B O   1 
ATOM   1461 N  N   . ASN   B 2 143 ? -11.118 -0.057  -14.366 1.00 37.26  ? 152 ASN   B N   1 
ATOM   1462 C  CA  . ASN   B 2 143 ? -10.198 -0.415  -13.269 1.00 36.40  ? 152 ASN   B CA  1 
ATOM   1463 C  C   . ASN   B 2 143 ? -9.233  -1.484  -13.785 1.00 36.11  ? 152 ASN   B C   1 
ATOM   1464 O  O   . ASN   B 2 143 ? -9.650  -2.569  -14.101 1.00 35.85  ? 152 ASN   B O   1 
ATOM   1465 C  CB  . ASN   B 2 143 ? -10.916 -0.892  -12.015 1.00 36.47  ? 152 ASN   B CB  1 
ATOM   1466 C  CG  . ASN   B 2 143 ? -10.018 -0.792  -10.787 1.00 37.55  ? 152 ASN   B CG  1 
ATOM   1467 O  OD1 . ASN   B 2 143 ? -9.123  0.076   -10.681 1.00 38.94  ? 152 ASN   B OD1 1 
ATOM   1468 N  ND2 . ASN   B 2 143 ? -10.219 -1.719  -9.876  1.00 36.62  ? 152 ASN   B ND2 1 
ATOM   1469 N  N   . GLY   B 2 144 ? -7.983  -1.132  -13.864 1.00 36.00  ? 153 GLY   B N   1 
ATOM   1470 C  CA  . GLY   B 2 144 ? -6.971  -2.092  -14.307 1.00 38.33  ? 153 GLY   B CA  1 
ATOM   1471 C  C   . GLY   B 2 144 ? -5.600  -1.516  -14.115 1.00 40.46  ? 153 GLY   B C   1 
ATOM   1472 O  O   . GLY   B 2 144 ? -5.334  -0.948  -13.009 1.00 40.42  ? 153 GLY   B O   1 
ATOM   1473 N  N   . VAL   B 2 145 ? -4.747  -1.707  -15.120 1.00 43.96  ? 154 VAL   B N   1 
ATOM   1474 C  CA  . VAL   B 2 145 ? -3.293  -1.541  -14.971 1.00 45.84  ? 154 VAL   B CA  1 
ATOM   1475 C  C   . VAL   B 2 145 ? -2.697  -0.847  -16.217 1.00 50.02  ? 154 VAL   B C   1 
ATOM   1476 O  O   . VAL   B 2 145 ? -3.205  -1.038  -17.333 1.00 48.46  ? 154 VAL   B O   1 
ATOM   1477 C  CB  . VAL   B 2 145 ? -2.771  -2.956  -14.662 1.00 48.05  ? 154 VAL   B CB  1 
ATOM   1478 C  CG1 . VAL   B 2 145 ? -2.482  -3.810  -15.865 1.00 45.34  ? 154 VAL   B CG1 1 
ATOM   1479 C  CG2 . VAL   B 2 145 ? -1.627  -2.910  -13.697 1.00 52.50  ? 154 VAL   B CG2 1 
ATOM   1480 N  N   . VAL   B 2 146 ? -1.643  -0.054  -16.008 1.00 52.55  ? 155 VAL   B N   1 
ATOM   1481 C  CA  . VAL   B 2 146 ? -0.800  0.547   -17.079 1.00 56.74  ? 155 VAL   B CA  1 
ATOM   1482 C  C   . VAL   B 2 146 ? 0.252   -0.490  -17.429 1.00 57.84  ? 155 VAL   B C   1 
ATOM   1483 O  O   . VAL   B 2 146 ? 0.762   -1.088  -16.489 1.00 57.62  ? 155 VAL   B O   1 
ATOM   1484 C  CB  . VAL   B 2 146 ? -0.211  1.877   -16.582 1.00 57.77  ? 155 VAL   B CB  1 
ATOM   1485 C  CG1 . VAL   B 2 146 ? 0.805   2.444   -17.530 1.00 60.98  ? 155 VAL   B CG1 1 
ATOM   1486 C  CG2 . VAL   B 2 146 ? -1.328  2.885   -16.319 1.00 60.08  ? 155 VAL   B CG2 1 
ATOM   1487 N  N   . ILE   B 2 147 ? 0.507   -0.777  -18.714 1.00 62.68  ? 156 ILE   B N   1 
ATOM   1488 C  CA  . ILE   B 2 147 ? 1.391   -1.924  -19.084 1.00 65.55  ? 156 ILE   B CA  1 
ATOM   1489 C  C   . ILE   B 2 147 ? 2.712   -1.361  -19.600 1.00 71.69  ? 156 ILE   B C   1 
ATOM   1490 O  O   . ILE   B 2 147 ? 2.888   -0.145  -19.487 1.00 71.57  ? 156 ILE   B O   1 
ATOM   1491 C  CB  . ILE   B 2 147 ? 0.702   -2.911  -20.052 1.00 68.68  ? 156 ILE   B CB  1 
ATOM   1492 C  CG1 . ILE   B 2 147 ? 0.081   -2.240  -21.287 1.00 69.43  ? 156 ILE   B CG1 1 
ATOM   1493 C  CG2 . ILE   B 2 147 ? -0.316  -3.753  -19.295 1.00 65.31  ? 156 ILE   B CG2 1 
ATOM   1494 C  CD1 . ILE   B 2 147 ? -0.304  -3.214  -22.373 1.00 68.26  ? 156 ILE   B CD1 1 
ATOM   1495 N  N   . LYS   B 2 148 ? 3.634   -2.225  -20.033 1.00 79.97  ? 157 LYS   B N   1 
ATOM   1496 C  CA  . LYS   B 2 148 ? 4.982   -1.831  -20.522 1.00 87.58  ? 157 LYS   B CA  1 
ATOM   1497 C  C   . LYS   B 2 148 ? 4.832   -0.661  -21.502 1.00 92.62  ? 157 LYS   B C   1 
ATOM   1498 O  O   . LYS   B 2 148 ? 5.526   0.356   -21.319 1.00 96.95  ? 157 LYS   B O   1 
ATOM   1499 C  CB  . LYS   B 2 148 ? 5.668   -3.042  -21.161 1.00 92.35  ? 157 LYS   B CB  1 
ATOM   1500 C  CG  . LYS   B 2 148 ? 5.846   -4.234  -20.222 1.00 96.51  ? 157 LYS   B CG  1 
ATOM   1501 C  CD  . LYS   B 2 148 ? 6.009   -5.565  -20.932 1.00 99.76  ? 157 LYS   B CD  1 
ATOM   1502 C  CE  . LYS   B 2 148 ? 7.323   -5.694  -21.677 1.00 104.15 ? 157 LYS   B CE  1 
ATOM   1503 N  NZ  . LYS   B 2 148 ? 8.433   -6.099  -20.779 1.00 106.06 ? 157 LYS   B NZ  1 
ATOM   1504 N  N   . ASN   B 2 149 ? 3.882   -0.773  -22.438 1.00 92.39  ? 158 ASN   B N   1 
ATOM   1505 C  CA  . ASN   B 2 149 ? 3.675   0.136   -23.601 1.00 92.56  ? 158 ASN   B CA  1 
ATOM   1506 C  C   . ASN   B 2 149 ? 3.216   1.529   -23.164 1.00 88.12  ? 158 ASN   B C   1 
ATOM   1507 O  O   . ASN   B 2 149 ? 3.060   2.386   -24.045 1.00 90.54  ? 158 ASN   B O   1 
ATOM   1508 C  CB  . ASN   B 2 149 ? 2.598   -0.374  -24.571 1.00 96.98  ? 158 ASN   B CB  1 
ATOM   1509 C  CG  . ASN   B 2 149 ? 2.389   -1.877  -24.532 1.00 96.45  ? 158 ASN   B CG  1 
ATOM   1510 O  OD1 . ASN   B 2 149 ? 3.221   -2.609  -24.003 1.00 90.32  ? 158 ASN   B OD1 1 
ATOM   1511 N  ND2 . ASN   B 2 149 ? 1.277   -2.345  -25.077 1.00 97.90  ? 158 ASN   B ND2 1 
ATOM   1512 N  N   . GLY   B 2 150 ? 2.888   1.710   -21.884 1.00 80.94  ? 159 GLY   B N   1 
ATOM   1513 C  CA  . GLY   B 2 150 ? 2.234   2.927   -21.357 1.00 73.10  ? 159 GLY   B CA  1 
ATOM   1514 C  C   . GLY   B 2 150 ? 0.712   2.909   -21.508 1.00 68.34  ? 159 GLY   B C   1 
ATOM   1515 O  O   . GLY   B 2 150 ? 0.050   3.783   -20.944 1.00 64.52  ? 159 GLY   B O   1 
ATOM   1516 N  N   A SER   B 2 151 ? 0.196   1.923   -22.256 0.25 68.43  ? 160 SER   B N   1 
ATOM   1517 N  N   B SER   B 2 151 ? 0.188   1.941   -22.269 0.01 67.12  ? 160 SER   B N   1 
ATOM   1518 N  N   C SER   B 2 151 ? 0.191   1.923   -22.254 0.33 68.62  ? 160 SER   B N   1 
ATOM   1519 N  N   D SER   B 2 151 ? 0.181   1.942   -22.270 0.40 68.21  ? 160 SER   B N   1 
ATOM   1520 C  CA  A SER   B 2 151 ? -1.243  1.688   -22.551 0.25 65.78  ? 160 SER   B CA  1 
ATOM   1521 C  CA  B SER   B 2 151 ? -1.258  1.738   -22.549 0.01 65.12  ? 160 SER   B CA  1 
ATOM   1522 C  CA  C SER   B 2 151 ? -1.252  1.686   -22.545 0.33 65.62  ? 160 SER   B CA  1 
ATOM   1523 C  CA  D SER   B 2 151 ? -1.269  1.736   -22.545 0.40 64.82  ? 160 SER   B CA  1 
ATOM   1524 C  C   A SER   B 2 151 ? -1.970  1.171   -21.301 0.25 63.48  ? 160 SER   B C   1 
ATOM   1525 C  C   B SER   B 2 151 ? -1.970  1.208   -21.299 0.01 62.82  ? 160 SER   B C   1 
ATOM   1526 C  C   C SER   B 2 151 ? -1.979  1.169   -21.285 0.33 63.18  ? 160 SER   B C   1 
ATOM   1527 C  C   D SER   B 2 151 ? -1.984  1.199   -21.288 0.40 62.73  ? 160 SER   B C   1 
ATOM   1528 O  O   A SER   B 2 151 ? -1.291  0.732   -20.337 0.25 62.13  ? 160 SER   B O   1 
ATOM   1529 O  O   B SER   B 2 151 ? -1.279  0.794   -20.339 0.01 62.15  ? 160 SER   B O   1 
ATOM   1530 O  O   C SER   B 2 151 ? -1.283  0.721   -20.337 0.33 61.84  ? 160 SER   B O   1 
ATOM   1531 O  O   D SER   B 2 151 ? -1.281  0.754   -20.344 0.40 61.46  ? 160 SER   B O   1 
ATOM   1532 C  CB  A SER   B 2 151 ? -1.382  0.722   -23.704 0.25 66.70  ? 160 SER   B CB  1 
ATOM   1533 C  CB  B SER   B 2 151 ? -1.439  0.805   -23.718 0.01 65.66  ? 160 SER   B CB  1 
ATOM   1534 C  CB  C SER   B 2 151 ? -1.384  0.720   -23.700 0.33 66.64  ? 160 SER   B CB  1 
ATOM   1535 C  CB  D SER   B 2 151 ? -1.441  0.803   -23.715 0.40 65.45  ? 160 SER   B CB  1 
ATOM   1536 O  OG  A SER   B 2 151 ? -2.740  0.563   -24.080 0.25 66.72  ? 160 SER   B OG  1 
ATOM   1537 O  OG  B SER   B 2 151 ? -0.653  -0.363  -23.546 0.01 65.81  ? 160 SER   B OG  1 
ATOM   1538 O  OG  C SER   B 2 151 ? -2.739  0.561   -24.083 0.33 66.74  ? 160 SER   B OG  1 
ATOM   1539 O  OG  D SER   B 2 151 ? -0.650  -0.363  -23.535 0.40 65.30  ? 160 SER   B OG  1 
ATOM   1540 N  N   A TYR   B 2 152 ? -3.303  1.189   -21.349 0.25 61.01  ? 161 TYR   B N   1 
ATOM   1541 N  N   B TYR   B 2 152 ? -3.303  1.191   -21.348 0.01 60.91  ? 161 TYR   B N   1 
ATOM   1542 N  N   C TYR   B 2 152 ? -3.322  1.235   -21.252 0.33 60.01  ? 161 TYR   B N   1 
ATOM   1543 N  N   D TYR   B 2 152 ? -3.327  1.242   -21.253 0.40 59.81  ? 161 TYR   B N   1 
ATOM   1544 C  CA  A TYR   B 2 152 ? -4.203  0.808   -20.233 0.25 59.45  ? 161 TYR   B CA  1 
ATOM   1545 C  CA  B TYR   B 2 152 ? -4.199  0.808   -20.229 0.01 58.91  ? 161 TYR   B CA  1 
ATOM   1546 C  CA  C TYR   B 2 152 ? -4.162  0.806   -20.092 0.33 58.35  ? 161 TYR   B CA  1 
ATOM   1547 C  CA  D TYR   B 2 152 ? -4.164  0.807   -20.092 0.40 58.38  ? 161 TYR   B CA  1 
ATOM   1548 C  C   A TYR   B 2 152 ? -4.890  -0.526  -20.548 0.25 56.93  ? 161 TYR   B C   1 
ATOM   1549 C  C   B TYR   B 2 152 ? -4.888  -0.524  -20.547 0.01 56.74  ? 161 TYR   B C   1 
ATOM   1550 C  C   C TYR   B 2 152 ? -4.991  -0.435  -20.460 0.33 56.28  ? 161 TYR   B C   1 
ATOM   1551 C  C   D TYR   B 2 152 ? -4.991  -0.435  -20.460 0.40 56.29  ? 161 TYR   B C   1 
ATOM   1552 O  O   A TYR   B 2 152 ? -5.294  -0.738  -21.698 0.25 56.56  ? 161 TYR   B O   1 
ATOM   1553 O  O   B TYR   B 2 152 ? -5.294  -0.728  -21.708 0.01 56.98  ? 161 TYR   B O   1 
ATOM   1554 O  O   C TYR   B 2 152 ? -5.630  -0.480  -21.517 0.33 55.64  ? 161 TYR   B O   1 
ATOM   1555 O  O   D TYR   B 2 152 ? -5.632  -0.481  -21.514 0.40 55.55  ? 161 TYR   B O   1 
ATOM   1556 C  CB  A TYR   B 2 152 ? -5.228  1.913   -19.984 0.25 59.75  ? 161 TYR   B CB  1 
ATOM   1557 C  CB  B TYR   B 2 152 ? -5.225  1.914   -19.982 0.01 59.26  ? 161 TYR   B CB  1 
ATOM   1558 C  CB  C TYR   B 2 152 ? -5.061  1.939   -19.578 0.33 57.40  ? 161 TYR   B CB  1 
ATOM   1559 C  CB  D TYR   B 2 152 ? -5.063  1.939   -19.576 0.40 57.41  ? 161 TYR   B CB  1 
ATOM   1560 C  CG  A TYR   B 2 152 ? -6.011  1.726   -18.713 0.25 59.80  ? 161 TYR   B CG  1 
ATOM   1561 C  CG  B TYR   B 2 152 ? -6.009  1.726   -18.712 0.01 59.12  ? 161 TYR   B CG  1 
ATOM   1562 C  CG  C TYR   B 2 152 ? -5.596  1.783   -18.168 0.33 56.57  ? 161 TYR   B CG  1 
ATOM   1563 C  CG  D TYR   B 2 152 ? -5.598  1.783   -18.166 0.40 56.63  ? 161 TYR   B CG  1 
ATOM   1564 C  CD1 A TYR   B 2 152 ? -5.452  2.040   -17.487 0.25 59.37  ? 161 TYR   B CD1 1 
ATOM   1565 C  CD1 B TYR   B 2 152 ? -5.449  2.037   -17.485 0.01 59.03  ? 161 TYR   B CD1 1 
ATOM   1566 C  CD1 C TYR   B 2 152 ? -4.782  1.962   -17.059 0.33 56.33  ? 161 TYR   B CD1 1 
ATOM   1567 C  CD1 D TYR   B 2 152 ? -4.785  1.963   -17.056 0.40 56.42  ? 161 TYR   B CD1 1 
ATOM   1568 C  CD2 A TYR   B 2 152 ? -7.296  1.208   -18.730 0.25 59.71  ? 161 TYR   B CD2 1 
ATOM   1569 C  CD2 B TYR   B 2 152 ? -7.294  1.210   -18.730 0.01 59.08  ? 161 TYR   B CD2 1 
ATOM   1570 C  CD2 C TYR   B 2 152 ? -6.932  1.495   -17.927 0.33 55.32  ? 161 TYR   B CD2 1 
ATOM   1571 C  CD2 D TYR   B 2 152 ? -6.934  1.493   -17.924 0.40 55.33  ? 161 TYR   B CD2 1 
ATOM   1572 C  CE1 A TYR   B 2 152 ? -6.152  1.855   -16.308 0.25 58.99  ? 161 TYR   B CE1 1 
ATOM   1573 C  CE1 B TYR   B 2 152 ? -6.150  1.856   -16.307 0.01 58.52  ? 161 TYR   B CE1 1 
ATOM   1574 C  CE1 C TYR   B 2 152 ? -5.264  1.830   -15.762 0.33 54.75  ? 161 TYR   B CE1 1 
ATOM   1575 C  CE1 D TYR   B 2 152 ? -5.267  1.830   -15.759 0.40 54.77  ? 161 TYR   B CE1 1 
ATOM   1576 C  CE2 A TYR   B 2 152 ? -8.010  1.020   -17.559 0.25 59.02  ? 161 TYR   B CE2 1 
ATOM   1577 C  CE2 B TYR   B 2 152 ? -8.010  1.023   -17.559 0.01 58.48  ? 161 TYR   B CE2 1 
ATOM   1578 C  CE2 C TYR   B 2 152 ? -7.433  1.366   -16.638 0.33 53.85  ? 161 TYR   B CE2 1 
ATOM   1579 C  CE2 D TYR   B 2 152 ? -7.435  1.363   -16.636 0.40 53.81  ? 161 TYR   B CE2 1 
ATOM   1580 C  CZ  A TYR   B 2 152 ? -7.438  1.346   -16.342 0.25 58.47  ? 161 TYR   B CZ  1 
ATOM   1581 C  CZ  B TYR   B 2 152 ? -7.437  1.349   -16.343 0.01 58.17  ? 161 TYR   B CZ  1 
ATOM   1582 C  CZ  C TYR   B 2 152 ? -6.600  1.536   -15.544 0.33 53.80  ? 161 TYR   B CZ  1 
ATOM   1583 C  CZ  D TYR   B 2 152 ? -6.603  1.534   -15.541 0.40 53.81  ? 161 TYR   B CZ  1 
ATOM   1584 O  OH  A TYR   B 2 152 ? -8.135  1.171   -15.180 0.25 58.22  ? 161 TYR   B OH  1 
ATOM   1585 O  OH  B TYR   B 2 152 ? -8.137  1.172   -15.185 0.01 57.63  ? 161 TYR   B OH  1 
ATOM   1586 O  OH  C TYR   B 2 152 ? -7.090  1.424   -14.266 0.33 49.84  ? 161 TYR   B OH  1 
ATOM   1587 O  OH  D TYR   B 2 152 ? -7.095  1.423   -14.263 0.40 49.53  ? 161 TYR   B OH  1 
ATOM   1588 N  N   . VAL   B 2 153 ? -4.995  -1.405  -19.546 1.00 54.42  ? 162 VAL   B N   1 
ATOM   1589 C  CA  . VAL   B 2 153 ? -5.731  -2.688  -19.664 1.00 50.19  ? 162 VAL   B CA  1 
ATOM   1590 C  C   . VAL   B 2 153 ? -6.675  -2.767  -18.463 1.00 45.19  ? 162 VAL   B C   1 
ATOM   1591 O  O   . VAL   B 2 153 ? -6.194  -2.742  -17.325 1.00 42.87  ? 162 VAL   B O   1 
ATOM   1592 C  CB  . VAL   B 2 153 ? -4.735  -3.861  -19.683 1.00 49.08  ? 162 VAL   B CB  1 
ATOM   1593 C  CG1 . VAL   B 2 153 ? -5.442  -5.200  -19.843 1.00 47.56  ? 162 VAL   B CG1 1 
ATOM   1594 C  CG2 . VAL   B 2 153 ? -3.652  -3.642  -20.739 1.00 51.95  ? 162 VAL   B CG2 1 
ATOM   1595 N  N   . SER   B 2 154 ? -7.970  -2.796  -18.720 1.00 43.64  ? 163 SER   B N   1 
ATOM   1596 C  CA  . SER   B 2 154 ? -9.046  -2.744  -17.707 1.00 40.54  ? 163 SER   B CA  1 
ATOM   1597 C  C   . SER   B 2 154 ? -9.516  -4.176  -17.446 1.00 39.72  ? 163 SER   B C   1 
ATOM   1598 O  O   . SER   B 2 154 ? -9.703  -4.928  -18.396 1.00 39.96  ? 163 SER   B O   1 
ATOM   1599 C  CB  . SER   B 2 154 ? -10.201 -1.895  -18.180 1.00 39.43  ? 163 SER   B CB  1 
ATOM   1600 O  OG  . SER   B 2 154 ? -11.350 -2.070  -17.339 1.00 36.52  ? 163 SER   B OG  1 
ATOM   1601 N  N   . ALA   B 2 155 ? -9.770  -4.502  -16.195 1.00 38.63  ? 164 ALA   B N   1 
ATOM   1602 C  CA  . ALA   B 2 155 ? -10.579 -5.660  -15.794 1.00 37.54  ? 164 ALA   B CA  1 
ATOM   1603 C  C   . ALA   B 2 155 ? -11.947 -5.460  -16.418 1.00 38.07  ? 164 ALA   B C   1 
ATOM   1604 O  O   . ALA   B 2 155 ? -12.382 -4.287  -16.600 1.00 39.87  ? 164 ALA   B O   1 
ATOM   1605 C  CB  . ALA   B 2 155 ? -10.684 -5.735  -14.271 1.00 37.56  ? 164 ALA   B CB  1 
ATOM   1606 N  N   . ILE   B 2 156 ? -12.610 -6.565  -16.709 1.00 38.46  ? 165 ILE   B N   1 
ATOM   1607 C  CA  . ILE   B 2 156 ? -14.090 -6.646  -16.748 1.00 39.64  ? 165 ILE   B CA  1 
ATOM   1608 C  C   . ILE   B 2 156 ? -14.620 -6.767  -15.310 1.00 38.42  ? 165 ILE   B C   1 
ATOM   1609 O  O   . ILE   B 2 156 ? -14.752 -7.899  -14.815 1.00 38.25  ? 165 ILE   B O   1 
ATOM   1610 C  CB  . ILE   B 2 156 ? -14.523 -7.835  -17.619 1.00 40.87  ? 165 ILE   B CB  1 
ATOM   1611 C  CG1 . ILE   B 2 156 ? -13.780 -7.811  -18.958 1.00 42.25  ? 165 ILE   B CG1 1 
ATOM   1612 C  CG2 . ILE   B 2 156 ? -16.048 -7.820  -17.786 1.00 40.81  ? 165 ILE   B CG2 1 
ATOM   1613 C  CD1 . ILE   B 2 156 ? -14.135 -8.950  -19.868 1.00 43.56  ? 165 ILE   B CD1 1 
ATOM   1614 N  N   . THR   B 2 157 ? -14.931 -5.639  -14.665 1.00 38.04  ? 166 THR   B N   1 
ATOM   1615 C  CA  . THR   B 2 157 ? -15.368 -5.597  -13.247 1.00 36.22  ? 166 THR   B CA  1 
ATOM   1616 C  C   . THR   B 2 157 ? -16.897 -5.800  -13.174 1.00 36.84  ? 166 THR   B C   1 
ATOM   1617 O  O   . THR   B 2 157 ? -17.675 -4.869  -13.625 1.00 34.82  ? 166 THR   B O   1 
ATOM   1618 C  CB  . THR   B 2 157 ? -14.933 -4.287  -12.614 1.00 36.26  ? 166 THR   B CB  1 
ATOM   1619 O  OG1 . THR   B 2 157 ? -13.515 -4.140  -12.693 1.00 35.07  ? 166 THR   B OG1 1 
ATOM   1620 C  CG2 . THR   B 2 157 ? -15.419 -4.196  -11.186 1.00 35.29  ? 166 THR   B CG2 1 
ATOM   1621 N  N   . GLN   B 2 158 ? -17.332 -6.910  -12.567 1.00 34.85  ? 167 GLN   B N   1 
ATOM   1622 C  CA  . GLN   B 2 158 ? -18.745 -7.282  -12.392 1.00 35.41  ? 167 GLN   B CA  1 
ATOM   1623 C  C   . GLN   B 2 158 ? -19.045 -7.347  -10.891 1.00 38.08  ? 167 GLN   B C   1 
ATOM   1624 O  O   . GLN   B 2 158 ? -18.187 -7.787  -10.140 1.00 36.02  ? 167 GLN   B O   1 
ATOM   1625 C  CB  . GLN   B 2 158 ? -19.047 -8.587  -13.098 1.00 35.61  ? 167 GLN   B CB  1 
ATOM   1626 C  CG  . GLN   B 2 158 ? -20.513 -8.952  -13.139 1.00 36.02  ? 167 GLN   B CG  1 
ATOM   1627 C  CD  . GLN   B 2 158 ? -21.421 -7.827  -13.636 1.00 36.21  ? 167 GLN   B CD  1 
ATOM   1628 O  OE1 . GLN   B 2 158 ? -21.493 -6.737  -13.059 1.00 35.32  ? 167 GLN   B OE1 1 
ATOM   1629 N  NE2 . GLN   B 2 158 ? -22.215 -8.136  -14.640 1.00 36.51  ? 167 GLN   B NE2 1 
ATOM   1630 N  N   . GLY   B 2 159 ? -20.204 -6.848  -10.478 1.00 40.86  ? 168 GLY   B N   1 
ATOM   1631 C  CA  . GLY   B 2 159 ? -20.699 -7.009  -9.104  1.00 45.02  ? 168 GLY   B CA  1 
ATOM   1632 C  C   . GLY   B 2 159 ? -21.452 -8.315  -8.941  1.00 49.77  ? 168 GLY   B C   1 
ATOM   1633 O  O   . GLY   B 2 159 ? -21.568 -9.079  -9.873  1.00 52.19  ? 168 GLY   B O   1 
ATOM   1634 N  N   A LYS   B 2 160 ? -21.916 -8.579  -7.718  0.25 51.63  ? 169 LYS   B N   1 
ATOM   1635 N  N   B LYS   B 2 160 ? -21.916 -8.579  -7.718  0.25 51.63  ? 169 LYS   B N   1 
ATOM   1636 N  N   C LYS   B 2 160 ? -21.981 -8.532  -7.739  0.25 52.46  ? 169 LYS   B N   1 
ATOM   1637 N  N   D LYS   B 2 160 ? -21.981 -8.532  -7.739  0.25 52.46  ? 169 LYS   B N   1 
ATOM   1638 C  CA  A LYS   B 2 160 ? -22.786 -9.735  -7.369  0.25 53.34  ? 169 LYS   B CA  1 
ATOM   1639 C  CA  B LYS   B 2 160 ? -22.786 -9.735  -7.369  0.25 53.34  ? 169 LYS   B CA  1 
ATOM   1640 C  CA  C LYS   B 2 160 ? -22.774 -9.726  -7.346  0.25 54.77  ? 169 LYS   B CA  1 
ATOM   1641 C  CA  D LYS   B 2 160 ? -22.774 -9.726  -7.346  0.25 54.77  ? 169 LYS   B CA  1 
ATOM   1642 C  C   A LYS   B 2 160 ? -24.222 -9.227  -7.199  0.25 54.86  ? 169 LYS   B C   1 
ATOM   1643 C  C   B LYS   B 2 160 ? -24.222 -9.227  -7.199  0.25 54.86  ? 169 LYS   B C   1 
ATOM   1644 C  C   C LYS   B 2 160 ? -24.224 -9.278  -7.112  0.25 55.83  ? 169 LYS   B C   1 
ATOM   1645 C  C   D LYS   B 2 160 ? -24.224 -9.278  -7.112  0.25 55.83  ? 169 LYS   B C   1 
ATOM   1646 O  O   A LYS   B 2 160 ? -24.398 -8.126  -6.645  0.25 53.29  ? 169 LYS   B O   1 
ATOM   1647 O  O   B LYS   B 2 160 ? -24.398 -8.126  -6.645  0.25 53.29  ? 169 LYS   B O   1 
ATOM   1648 O  O   C LYS   B 2 160 ? -24.417 -8.257  -6.424  0.25 54.49  ? 169 LYS   B O   1 
ATOM   1649 O  O   D LYS   B 2 160 ? -24.417 -8.257  -6.424  0.25 54.49  ? 169 LYS   B O   1 
ATOM   1650 C  CB  A LYS   B 2 160 ? -22.311 -10.432 -6.090  0.25 53.76  ? 169 LYS   B CB  1 
ATOM   1651 C  CB  B LYS   B 2 160 ? -22.311 -10.432 -6.090  0.25 53.76  ? 169 LYS   B CB  1 
ATOM   1652 C  CB  C LYS   B 2 160 ? -22.127 -10.363 -6.113  0.25 56.23  ? 169 LYS   B CB  1 
ATOM   1653 C  CB  D LYS   B 2 160 ? -22.127 -10.363 -6.113  0.25 56.23  ? 169 LYS   B CB  1 
ATOM   1654 C  CG  A LYS   B 2 160 ? -23.000 -11.763 -5.811  0.25 54.18  ? 169 LYS   B CG  1 
ATOM   1655 C  CG  B LYS   B 2 160 ? -23.000 -11.763 -5.811  0.25 54.18  ? 169 LYS   B CG  1 
ATOM   1656 C  CG  C LYS   B 2 160 ? -20.656 -10.731 -6.286  0.25 56.94  ? 169 LYS   B CG  1 
ATOM   1657 C  CG  D LYS   B 2 160 ? -20.656 -10.731 -6.286  0.25 56.94  ? 169 LYS   B CG  1 
ATOM   1658 C  CD  A LYS   B 2 160 ? -22.649 -12.377 -4.475  0.25 53.94  ? 169 LYS   B CD  1 
ATOM   1659 C  CD  B LYS   B 2 160 ? -22.649 -12.377 -4.475  0.25 53.94  ? 169 LYS   B CD  1 
ATOM   1660 C  CD  C LYS   B 2 160 ? -20.014 -11.246 -5.018  0.25 57.76  ? 169 LYS   B CD  1 
ATOM   1661 C  CD  D LYS   B 2 160 ? -20.014 -11.246 -5.018  0.25 57.76  ? 169 LYS   B CD  1 
ATOM   1662 C  CE  A LYS   B 2 160 ? -23.489 -13.593 -4.155  0.25 54.04  ? 169 LYS   B CE  1 
ATOM   1663 C  CE  B LYS   B 2 160 ? -23.489 -13.593 -4.155  0.25 54.04  ? 169 LYS   B CE  1 
ATOM   1664 C  CE  C LYS   B 2 160 ? -18.919 -12.260 -5.277  0.25 58.79  ? 169 LYS   B CE  1 
ATOM   1665 C  CE  D LYS   B 2 160 ? -18.919 -12.260 -5.277  0.25 58.79  ? 169 LYS   B CE  1 
ATOM   1666 N  NZ  A LYS   B 2 160 ? -23.362 -13.969 -2.729  0.25 54.34  ? 169 LYS   B NZ  1 
ATOM   1667 N  NZ  B LYS   B 2 160 ? -23.362 -13.969 -2.729  0.25 54.34  ? 169 LYS   B NZ  1 
ATOM   1668 N  NZ  C LYS   B 2 160 ? -18.615 -13.061 -4.063  0.25 58.82  ? 169 LYS   B NZ  1 
ATOM   1669 N  NZ  D LYS   B 2 160 ? -18.615 -13.061 -4.063  0.25 58.82  ? 169 LYS   B NZ  1 
ATOM   1670 N  N   . ARG   B 2 161 ? -25.200 -9.995  -7.686  1.00 56.99  ? 170 ARG   B N   1 
ATOM   1671 C  CA  . ARG   B 2 161 ? -26.653 -9.711  -7.480  1.00 62.16  ? 170 ARG   B CA  1 
ATOM   1672 C  C   . ARG   B 2 161 ? -27.176 -10.646 -6.372  1.00 69.90  ? 170 ARG   B C   1 
ATOM   1673 O  O   . ARG   B 2 161 ? -26.893 -11.856 -6.467  1.00 73.19  ? 170 ARG   B O   1 
ATOM   1674 C  CB  . ARG   B 2 161 ? -27.364 -9.895  -8.829  1.00 63.95  ? 170 ARG   B CB  1 
ATOM   1675 C  CG  . ARG   B 2 161 ? -28.844 -9.551  -8.839  1.00 64.06  ? 170 ARG   B CG  1 
ATOM   1676 C  CD  . ARG   B 2 161 ? -29.546 -10.000 -10.117 1.00 64.58  ? 170 ARG   B CD  1 
ATOM   1677 N  NE  . ARG   B 2 161 ? -30.962 -9.679  -9.975  1.00 66.16  ? 170 ARG   B NE  1 
ATOM   1678 C  CZ  . ARG   B 2 161 ? -31.654 -8.781  -10.685 1.00 66.02  ? 170 ARG   B CZ  1 
ATOM   1679 N  NH1 . ARG   B 2 161 ? -31.099 -8.080  -11.662 1.00 60.73  ? 170 ARG   B NH1 1 
ATOM   1680 N  NH2 . ARG   B 2 161 ? -32.930 -8.593  -10.391 1.00 69.48  ? 170 ARG   B NH2 1 
ATOM   1681 N  N   . GLU   B 2 162 ? -27.893 -10.127 -5.365  1.00 75.87  ? 171 GLU   B N   1 
ATOM   1682 C  CA  . GLU   B 2 162 ? -28.506 -10.930 -4.265  1.00 80.18  ? 171 GLU   B CA  1 
ATOM   1683 C  C   . GLU   B 2 162 ? -30.005 -11.121 -4.541  1.00 79.78  ? 171 GLU   B C   1 
ATOM   1684 O  O   . GLU   B 2 162 ? -30.679 -11.947 -3.907  1.00 83.38  ? 171 GLU   B O   1 
ATOM   1685 C  CB  . GLU   B 2 162 ? -28.270 -10.239 -2.922  1.00 87.00  ? 171 GLU   B CB  1 
ATOM   1686 C  CG  . GLU   B 2 162 ? -26.802 -9.938  -2.613  1.00 91.43  ? 171 GLU   B CG  1 
ATOM   1687 C  CD  . GLU   B 2 162 ? -26.017 -11.041 -1.907  1.00 97.33  ? 171 GLU   B CD  1 
ATOM   1688 O  OE1 . GLU   B 2 162 ? -25.594 -10.816 -0.754  1.00 94.42  ? 171 GLU   B OE1 1 
ATOM   1689 O  OE2 . GLU   B 2 162 ? -25.814 -12.120 -2.511  1.00 105.47 ? 171 GLU   B OE2 1 
HETATM 1690 S  S   A DMS   C 3 .   ? -7.911  5.683   -17.948 0.25 56.24  ? 201 DMS   B S   1 
HETATM 1691 S  S   B DMS   C 3 .   ? -7.906  5.676   -17.952 0.01 56.24  ? 201 DMS   B S   1 
HETATM 1692 O  O   A DMS   C 3 .   ? -6.515  5.229   -18.283 0.25 56.30  ? 201 DMS   B O   1 
HETATM 1693 O  O   B DMS   C 3 .   ? -6.515  5.212   -18.281 0.01 56.62  ? 201 DMS   B O   1 
HETATM 1694 C  C1  A DMS   C 3 .   ? -8.167  5.302   -16.238 0.25 55.87  ? 201 DMS   B C1  1 
HETATM 1695 C  C1  B DMS   C 3 .   ? -8.160  5.302   -16.238 0.01 55.51  ? 201 DMS   B C1  1 
HETATM 1696 C  C2  A DMS   C 3 .   ? -9.014  4.468   -18.626 0.25 56.33  ? 201 DMS   B C2  1 
HETATM 1697 C  C2  B DMS   C 3 .   ? -9.010  4.461   -18.626 0.01 56.13  ? 201 DMS   B C2  1 
HETATM 1698 S  S   A DMS   D 3 .   ? -18.296 11.952  -0.690  0.25 259.91 ? 202 DMS   B S   1 
HETATM 1699 S  S   B DMS   D 3 .   ? -18.296 11.952  -0.688  0.22 259.32 ? 202 DMS   B S   1 
HETATM 1700 O  O   A DMS   D 3 .   ? -19.161 10.818  -1.165  0.25 256.93 ? 202 DMS   B O   1 
HETATM 1701 O  O   B DMS   D 3 .   ? -19.161 10.818  -1.161  0.22 256.39 ? 202 DMS   B O   1 
HETATM 1702 C  C1  A DMS   D 3 .   ? -19.198 13.442  -1.034  0.25 257.71 ? 202 DMS   B C1  1 
HETATM 1703 C  C1  B DMS   D 3 .   ? -19.198 13.441  -1.033  0.22 257.37 ? 202 DMS   B C1  1 
HETATM 1704 C  C2  A DMS   D 3 .   ? -17.026 12.143  -1.912  0.25 256.73 ? 202 DMS   B C2  1 
HETATM 1705 C  C2  B DMS   D 3 .   ? -17.027 12.143  -1.911  0.22 256.47 ? 202 DMS   B C2  1 
HETATM 1706 S  S   A DMS   E 3 .   ? -6.568  2.607   -13.179 0.25 57.70  ? 203 DMS   B S   1 
HETATM 1707 S  S   B DMS   E 3 .   ? -6.570  2.619   -13.160 0.01 57.62  ? 203 DMS   B S   1 
HETATM 1708 O  O   A DMS   E 3 .   ? -5.585  1.941   -12.264 0.25 56.21  ? 203 DMS   B O   1 
HETATM 1709 O  O   B DMS   E 3 .   ? -5.593  1.944   -12.239 0.01 56.98  ? 203 DMS   B O   1 
HETATM 1710 C  C1  A DMS   E 3 .   ? -7.993  2.989   -12.181 0.25 57.41  ? 203 DMS   B C1  1 
HETATM 1711 C  C1  B DMS   E 3 .   ? -8.001  2.995   -12.178 0.01 57.04  ? 203 DMS   B C1  1 
HETATM 1712 C  C2  A DMS   E 3 .   ? -5.979  4.271   -13.371 0.25 58.29  ? 203 DMS   B C2  1 
HETATM 1713 C  C2  B DMS   E 3 .   ? -5.982  4.280   -13.360 0.01 58.07  ? 203 DMS   B C2  1 
HETATM 1714 N  N1  C A1BG8 F 4 .   ? -4.450  7.317   -17.150 0.33 56.94  ? 204 A1BG8 B N1  1 
HETATM 1715 N  N1  D A1BG8 F 4 .   ? -4.449  7.317   -17.151 0.40 57.03  ? 204 A1BG8 B N1  1 
HETATM 1716 N  N3  C A1BG8 F 4 .   ? -8.888  3.932   -10.214 0.33 45.27  ? 204 A1BG8 B N3  1 
HETATM 1717 N  N3  D A1BG8 F 4 .   ? -8.886  3.932   -10.212 0.40 45.16  ? 204 A1BG8 B N3  1 
HETATM 1718 C  C4  C A1BG8 F 4 .   ? -6.223  5.744   -16.781 0.33 54.48  ? 204 A1BG8 B C4  1 
HETATM 1719 C  C4  D A1BG8 F 4 .   ? -6.223  5.745   -16.782 0.40 54.53  ? 204 A1BG8 B C4  1 
HETATM 1720 C  C5  C A1BG8 F 4 .   ? -7.554  5.165   -17.135 0.33 52.61  ? 204 A1BG8 B C5  1 
HETATM 1721 C  C5  D A1BG8 F 4 .   ? -7.554  5.166   -17.136 0.40 52.61  ? 204 A1BG8 B C5  1 
HETATM 1722 C  C6  C A1BG8 F 4 .   ? -7.796  4.797   -18.461 0.33 53.06  ? 204 A1BG8 B C6  1 
HETATM 1723 C  C6  D A1BG8 F 4 .   ? -7.796  4.798   -18.462 0.40 53.09  ? 204 A1BG8 B C6  1 
HETATM 1724 C  C7  C A1BG8 F 4 .   ? -8.995  4.233   -18.847 0.33 52.60  ? 204 A1BG8 B C7  1 
HETATM 1725 C  C7  D A1BG8 F 4 .   ? -8.996  4.233   -18.847 0.40 52.64  ? 204 A1BG8 B C7  1 
HETATM 1726 C  C8  C A1BG8 F 4 .   ? -9.976  4.002   -17.909 0.33 51.07  ? 204 A1BG8 B C8  1 
HETATM 1727 C  C8  D A1BG8 F 4 .   ? -9.975  4.000   -17.909 0.40 51.02  ? 204 A1BG8 B C8  1 
HETATM 1728 C  C10 C A1BG8 F 4 .   ? -8.556  4.912   -16.176 0.33 50.97  ? 204 A1BG8 B C10 1 
HETATM 1729 C  C10 D A1BG8 F 4 .   ? -8.556  4.911   -16.176 0.40 50.97  ? 204 A1BG8 B C10 1 
HETATM 1730 C  C13 C A1BG8 F 4 .   ? -9.052  3.485   -11.449 0.33 46.03  ? 204 A1BG8 B C13 1 
HETATM 1731 C  C13 D A1BG8 F 4 .   ? -9.049  3.485   -11.448 0.40 45.96  ? 204 A1BG8 B C13 1 
HETATM 1732 C  C15 C A1BG8 F 4 .   ? -8.357  5.573   -11.672 0.33 47.29  ? 204 A1BG8 B C15 1 
HETATM 1733 C  C15 D A1BG8 F 4 .   ? -8.356  5.573   -11.672 0.40 47.33  ? 204 A1BG8 B C15 1 
HETATM 1734 C  C1  C A1BG8 F 4 .   ? -2.441  7.286   -15.773 0.33 57.71  ? 204 A1BG8 B C1  1 
HETATM 1735 C  C1  D A1BG8 F 4 .   ? -2.440  7.285   -15.772 0.40 57.80  ? 204 A1BG8 B C1  1 
HETATM 1736 C  C2  C A1BG8 F 4 .   ? -3.781  6.738   -16.143 0.33 57.13  ? 204 A1BG8 B C2  1 
HETATM 1737 C  C2  D A1BG8 F 4 .   ? -3.780  6.737   -16.144 0.40 57.24  ? 204 A1BG8 B C2  1 
HETATM 1738 C  C3  C A1BG8 F 4 .   ? -5.649  6.810   -17.463 0.33 55.42  ? 204 A1BG8 B C3  1 
HETATM 1739 C  C3  D A1BG8 F 4 .   ? -5.648  6.810   -17.465 0.40 55.42  ? 204 A1BG8 B C3  1 
HETATM 1740 C  C9  C A1BG8 F 4 .   ? -9.760  4.334   -16.589 0.33 50.17  ? 204 A1BG8 B C9  1 
HETATM 1741 C  C9  D A1BG8 F 4 .   ? -9.758  4.331   -16.589 0.40 50.09  ? 204 A1BG8 B C9  1 
HETATM 1742 C  C11 C A1BG8 F 4 .   ? -8.423  5.262   -14.717 0.33 49.22  ? 204 A1BG8 B C11 1 
HETATM 1743 C  C11 D A1BG8 F 4 .   ? -8.423  5.261   -14.716 0.40 49.17  ? 204 A1BG8 B C11 1 
HETATM 1744 O  O1  C A1BG8 F 4 .   ? -7.994  6.353   -14.372 0.33 49.60  ? 204 A1BG8 B O1  1 
HETATM 1745 O  O1  D A1BG8 F 4 .   ? -7.992  6.350   -14.369 0.40 49.60  ? 204 A1BG8 B O1  1 
HETATM 1746 N  N2  C A1BG8 F 4 .   ? -8.812  4.318   -13.810 0.33 47.77  ? 204 A1BG8 B N2  1 
HETATM 1747 N  N2  D A1BG8 F 4 .   ? -8.813  4.317   -13.809 0.40 47.70  ? 204 A1BG8 B N2  1 
HETATM 1748 C  C12 C A1BG8 F 4 .   ? -8.745  4.461   -12.412 0.33 47.01  ? 204 A1BG8 B C12 1 
HETATM 1749 C  C12 D A1BG8 F 4 .   ? -8.744  4.460   -12.412 0.40 46.98  ? 204 A1BG8 B C12 1 
HETATM 1750 N  N4  C A1BG8 F 4 .   ? -8.458  5.222   -10.367 0.33 46.35  ? 204 A1BG8 B N4  1 
HETATM 1751 N  N4  D A1BG8 F 4 .   ? -8.457  5.222   -10.367 0.40 46.34  ? 204 A1BG8 B N4  1 
HETATM 1752 C  C14 C A1BG8 F 4 .   ? -8.172  6.047   -9.195  0.33 46.11  ? 204 A1BG8 B C14 1 
HETATM 1753 C  C14 D A1BG8 F 4 .   ? -8.172  6.048   -9.196  0.40 46.09  ? 204 A1BG8 B C14 1 
HETATM 1754 C  C16 C A1BG8 F 4 .   ? -5.436  5.216   -15.765 0.33 54.91  ? 204 A1BG8 B C16 1 
HETATM 1755 C  C16 D A1BG8 F 4 .   ? -5.437  5.216   -15.766 0.40 54.96  ? 204 A1BG8 B C16 1 
HETATM 1756 N  N5  C A1BG8 F 4 .   ? -4.237  5.703   -15.432 0.33 56.09  ? 204 A1BG8 B N5  1 
HETATM 1757 N  N5  D A1BG8 F 4 .   ? -4.237  5.703   -15.433 0.40 56.18  ? 204 A1BG8 B N5  1 
HETATM 1758 S  S   C SO4   G 5 .   ? -18.628 11.656  -0.426  0.50 97.14  ? 205 SO4   B S   1 
HETATM 1759 S  S   D SO4   G 5 .   ? -18.628 11.656  -0.426  0.50 97.14  ? 205 SO4   B S   1 
HETATM 1760 O  O1  C SO4   G 5 .   ? -17.418 11.697  -1.214  0.50 97.32  ? 205 SO4   B O1  1 
HETATM 1761 O  O1  D SO4   G 5 .   ? -17.418 11.697  -1.214  0.50 97.32  ? 205 SO4   B O1  1 
HETATM 1762 O  O2  C SO4   G 5 .   ? -18.376 12.203  0.876   0.50 101.00 ? 205 SO4   B O2  1 
HETATM 1763 O  O2  D SO4   G 5 .   ? -18.376 12.203  0.876   0.50 101.00 ? 205 SO4   B O2  1 
HETATM 1764 O  O3  C SO4   G 5 .   ? -19.639 12.450  -1.069  0.50 102.93 ? 205 SO4   B O3  1 
HETATM 1765 O  O3  D SO4   G 5 .   ? -19.639 12.450  -1.069  0.50 102.93 ? 205 SO4   B O3  1 
HETATM 1766 O  O4  C SO4   G 5 .   ? -19.083 10.293  -0.287  0.50 93.45  ? 205 SO4   B O4  1 
HETATM 1767 O  O4  D SO4   G 5 .   ? -19.083 10.293  -0.287  0.50 93.45  ? 205 SO4   B O4  1 
HETATM 1768 CL CL  C CL    H 6 .   ? -1.257  -15.048 -9.868  0.50 80.39  ? 206 CL    B CL  1 
HETATM 1769 CL CL  D CL    H 6 .   ? -1.257  -15.048 -9.868  0.50 80.39  ? 206 CL    B CL  1 
HETATM 1770 O  O   . HOH   I 7 .   ? -27.747 -5.899  -28.019 1.00 46.60  ? 101 HOH   A O   1 
HETATM 1771 O  O   . HOH   I 7 .   ? -7.923  0.501   3.358   1.00 45.70  ? 102 HOH   A O   1 
HETATM 1772 O  O   A HOH   I 7 .   ? -23.443 18.667  -19.340 0.50 51.89  ? 103 HOH   A O   1 
HETATM 1773 O  O   B HOH   I 7 .   ? -23.443 18.667  -19.340 0.50 51.89  ? 103 HOH   A O   1 
HETATM 1774 O  O   . HOH   I 7 .   ? -3.910  -14.250 -25.264 1.00 40.62  ? 104 HOH   A O   1 
HETATM 1775 O  O   . HOH   I 7 .   ? -8.970  -6.318  -25.264 1.00 47.80  ? 105 HOH   A O   1 
HETATM 1776 O  O   . HOH   I 7 .   ? -23.930 9.053   -27.393 1.00 32.79  ? 106 HOH   A O   1 
HETATM 1777 O  O   . HOH   I 7 .   ? -2.277  -3.980  -6.373  1.00 48.41  ? 107 HOH   A O   1 
HETATM 1778 O  O   A HOH   I 7 .   ? -9.680  1.386   -8.166  0.25 21.83  ? 108 HOH   A O   1 
HETATM 1779 O  O   B HOH   I 7 .   ? -10.025 2.633   -8.742  0.01 5.01   ? 108 HOH   A O   1 
HETATM 1780 O  O   C HOH   I 7 .   ? -8.645  2.110   -8.690  0.33 38.49  ? 108 HOH   A O   1 
HETATM 1781 O  O   D HOH   I 7 .   ? -8.645  2.114   -8.697  0.40 38.42  ? 108 HOH   A O   1 
HETATM 1782 O  O   . HOH   I 7 .   ? -3.817  -4.402  0.332   1.00 43.24  ? 109 HOH   A O   1 
HETATM 1783 O  O   . HOH   I 7 .   ? -28.763 15.712  -14.806 1.00 48.99  ? 110 HOH   A O   1 
HETATM 1784 O  O   . HOH   I 7 .   ? -2.921  -11.769 -7.062  1.00 41.73  ? 111 HOH   A O   1 
HETATM 1785 O  O   A HOH   I 7 .   ? 6.634   -5.113  -17.159 0.50 68.87  ? 112 HOH   A O   1 
HETATM 1786 O  O   B HOH   I 7 .   ? 6.634   -5.113  -17.159 0.50 68.87  ? 112 HOH   A O   1 
HETATM 1787 O  O   . HOH   I 7 .   ? -8.083  -1.932  6.766   1.00 46.01  ? 113 HOH   A O   1 
HETATM 1788 O  O   A HOH   I 7 .   ? -26.144 -3.694  -34.960 0.50 54.24  ? 114 HOH   A O   1 
HETATM 1789 O  O   B HOH   I 7 .   ? -26.144 -3.694  -34.960 0.50 54.24  ? 114 HOH   A O   1 
HETATM 1790 O  O   . HOH   I 7 .   ? -22.054 -9.235  -34.501 1.00 52.47  ? 115 HOH   A O   1 
HETATM 1791 O  O   A HOH   I 7 .   ? -0.557  -12.407 -23.691 0.50 62.67  ? 116 HOH   A O   1 
HETATM 1792 O  O   B HOH   I 7 .   ? -0.557  -12.407 -23.691 0.50 62.67  ? 116 HOH   A O   1 
HETATM 1793 O  O   . HOH   I 7 .   ? -30.795 0.241   -22.903 1.00 43.89  ? 117 HOH   A O   1 
HETATM 1794 O  O   . HOH   I 7 .   ? -3.889  -0.881  -0.274  1.00 46.01  ? 118 HOH   A O   1 
HETATM 1795 O  O   . HOH   I 7 .   ? -4.561  -10.187 -5.539  1.00 41.61  ? 119 HOH   A O   1 
HETATM 1796 O  O   . HOH   I 7 .   ? -2.996  -9.006  -3.377  1.00 48.02  ? 120 HOH   A O   1 
HETATM 1797 O  O   A HOH   I 7 .   ? -0.251  -13.098 -9.780  0.50 69.71  ? 121 HOH   A O   1 
HETATM 1798 O  O   B HOH   I 7 .   ? -0.251  -13.098 -9.780  0.50 69.71  ? 121 HOH   A O   1 
HETATM 1799 O  O   C HOH   I 7 .   ? -21.301 15.755  -22.609 0.50 50.01  ? 122 HOH   A O   1 
HETATM 1800 O  O   D HOH   I 7 .   ? -21.301 15.755  -22.609 0.50 50.01  ? 122 HOH   A O   1 
HETATM 1801 O  O   . HOH   J 7 .   ? -30.473 12.591  -19.471 1.00 48.33  ? 301 HOH   B O   1 
HETATM 1802 O  O   . HOH   J 7 .   ? -19.306 -12.178 -25.570 1.00 55.78  ? 302 HOH   B O   1 
HETATM 1803 O  O   . HOH   J 7 .   ? -33.507 1.544   -15.357 1.00 43.10  ? 303 HOH   B O   1 
HETATM 1804 O  O   A HOH   J 7 .   ? -5.260  2.314   -10.010 0.25 27.15  ? 304 HOH   B O   1 
HETATM 1805 O  O   B HOH   J 7 .   ? -4.589  4.001   -10.626 0.01 8.25   ? 304 HOH   B O   1 
HETATM 1806 O  O   A HOH   J 7 .   ? -16.545 25.504  -12.531 0.50 70.79  ? 305 HOH   B O   1 
HETATM 1807 O  O   B HOH   J 7 .   ? -16.545 25.504  -12.531 0.50 70.79  ? 305 HOH   B O   1 
HETATM 1808 O  O   A HOH   J 7 .   ? -15.528 -10.154 -15.021 0.50 43.73  ? 306 HOH   B O   1 
HETATM 1809 O  O   B HOH   J 7 .   ? -15.528 -10.154 -15.021 0.50 43.73  ? 306 HOH   B O   1 
HETATM 1810 O  O   . HOH   J 7 .   ? -25.805 -8.142  -16.606 1.00 40.05  ? 307 HOH   B O   1 
HETATM 1811 O  O   A HOH   J 7 .   ? -19.642 -16.532 -18.140 0.50 80.03  ? 308 HOH   B O   1 
HETATM 1812 O  O   B HOH   J 7 .   ? -19.642 -16.532 -18.140 0.50 80.03  ? 308 HOH   B O   1 
HETATM 1813 O  O   . HOH   J 7 .   ? -17.983 -10.696 -16.449 1.00 37.62  ? 309 HOH   B O   1 
HETATM 1814 O  O   . HOH   J 7 .   ? -6.343  -0.537  -10.772 1.00 37.33  ? 310 HOH   B O   1 
HETATM 1815 O  O   . HOH   J 7 .   ? -17.106 12.674  -5.472  1.00 39.12  ? 311 HOH   B O   1 
HETATM 1816 O  O   C HOH   J 7 .   ? -20.364 13.631  1.576   0.50 57.50  ? 312 HOH   B O   1 
HETATM 1817 O  O   D HOH   J 7 .   ? -20.364 13.631  1.576   0.50 57.50  ? 312 HOH   B O   1 
HETATM 1818 O  O   . HOH   J 7 .   ? -15.129 -4.677  1.397   1.00 39.63  ? 313 HOH   B O   1 
HETATM 1819 O  O   A HOH   J 7 .   ? -28.500 -4.205  -22.214 0.50 61.23  ? 314 HOH   B O   1 
HETATM 1820 O  O   B HOH   J 7 .   ? -28.500 -4.205  -22.214 0.50 61.23  ? 314 HOH   B O   1 
HETATM 1821 O  O   . HOH   J 7 .   ? -35.236 -5.239  -10.145 1.00 50.02  ? 315 HOH   B O   1 
HETATM 1822 O  O   A HOH   J 7 .   ? -19.757 -7.928  -2.630  0.50 57.68  ? 316 HOH   B O   1 
HETATM 1823 O  O   B HOH   J 7 .   ? -19.757 -7.928  -2.630  0.50 57.68  ? 316 HOH   B O   1 
HETATM 1824 O  O   . HOH   J 7 .   ? -31.367 6.920   -4.401  1.00 60.69  ? 317 HOH   B O   1 
HETATM 1825 O  O   . HOH   J 7 .   ? -6.871  -10.903 -5.256  1.00 43.63  ? 318 HOH   B O   1 
HETATM 1826 O  O   . HOH   J 7 .   ? -27.588 -7.139  -5.558  1.00 54.58  ? 319 HOH   B O   1 
HETATM 1827 O  O   C HOH   J 7 .   ? -22.200 14.904  -6.126  0.50 46.46  ? 320 HOH   B O   1 
HETATM 1828 O  O   D HOH   J 7 .   ? -22.200 14.904  -6.126  0.50 46.46  ? 320 HOH   B O   1 
HETATM 1829 O  O   . HOH   J 7 .   ? -12.064 1.994   -5.788  1.00 45.54  ? 321 HOH   B O   1 
HETATM 1830 O  O   . HOH   J 7 .   ? -23.510 -14.580 -17.904 1.00 59.06  ? 322 HOH   B O   1 
HETATM 1831 O  O   . HOH   J 7 .   ? -13.014 -2.373  -14.747 1.00 35.70  ? 323 HOH   B O   1 
HETATM 1832 O  O   . HOH   J 7 .   ? -35.045 4.096   -9.155  1.00 52.76  ? 324 HOH   B O   1 
HETATM 1833 O  O   C HOH   J 7 .   ? -17.914 1.003   -33.839 0.50 49.48  ? 325 HOH   B O   1 
HETATM 1834 O  O   D HOH   J 7 .   ? -17.914 1.003   -33.839 0.50 49.48  ? 325 HOH   B O   1 
HETATM 1835 O  O   . HOH   J 7 .   ? -7.062  -9.145  -3.090  1.00 39.86  ? 326 HOH   B O   1 
HETATM 1836 O  O   . HOH   J 7 .   ? -15.739 -13.954 -30.611 1.00 50.40  ? 327 HOH   B O   1 
HETATM 1837 O  O   A HOH   J 7 .   ? -18.508 19.234  -21.348 0.50 54.80  ? 328 HOH   B O   1 
HETATM 1838 O  O   B HOH   J 7 .   ? -18.508 19.234  -21.348 0.50 54.80  ? 328 HOH   B O   1 
HETATM 1839 O  O   A HOH   J 7 .   ? -11.617 -17.619 -27.634 0.50 64.90  ? 329 HOH   B O   1 
HETATM 1840 O  O   B HOH   J 7 .   ? -11.617 -17.619 -27.634 0.50 64.90  ? 329 HOH   B O   1 
HETATM 1841 O  O   . HOH   J 7 .   ? -21.533 -12.352 -13.103 1.00 49.11  ? 330 HOH   B O   1 
HETATM 1842 O  O   . HOH   J 7 .   ? -10.890 11.844  -19.080 1.00 47.52  ? 331 HOH   B O   1 
HETATM 1843 O  O   . HOH   J 7 .   ? -16.394 -7.355  -8.148  1.00 55.54  ? 332 HOH   B O   1 
HETATM 1844 O  O   . HOH   J 7 .   ? -16.075 20.520  -14.190 1.00 52.72  ? 333 HOH   B O   1 
HETATM 1845 O  O   . HOH   J 7 .   ? -15.431 9.235   -0.574  1.00 44.78  ? 334 HOH   B O   1 
HETATM 1846 O  O   . HOH   J 7 .   ? -30.594 12.376  -16.350 1.00 49.81  ? 335 HOH   B O   1 
HETATM 1847 O  O   A HOH   J 7 .   ? -21.644 5.243   -32.466 0.25 42.54  ? 336 HOH   B O   1 
HETATM 1848 O  O   B HOH   J 7 .   ? -21.644 5.243   -32.466 0.25 42.54  ? 336 HOH   B O   1 
HETATM 1849 O  O   A HOH   J 7 .   ? -21.160 6.901   -0.000  0.25 43.84  ? 337 HOH   B O   1 
HETATM 1850 O  O   B HOH   J 7 .   ? -21.160 6.899   -0.000  0.22 43.83  ? 337 HOH   B O   1 
HETATM 1851 O  O   . HOH   J 7 .   ? -15.107 16.381  -19.942 1.00 47.34  ? 338 HOH   B O   1 
HETATM 1852 O  O   . HOH   J 7 .   ? -27.693 -6.267  -18.597 1.00 51.11  ? 339 HOH   B O   1 
HETATM 1853 O  O   . HOH   J 7 .   ? -12.361 -3.539  -10.032 1.00 35.35  ? 340 HOH   B O   1 
HETATM 1854 O  O   A HOH   J 7 .   ? -8.330  -10.874 -7.420  0.50 60.15  ? 341 HOH   B O   1 
HETATM 1855 O  O   B HOH   J 7 .   ? -8.330  -10.874 -7.420  0.50 60.15  ? 341 HOH   B O   1 
HETATM 1856 O  O   . HOH   J 7 .   ? -14.256 -12.433 -16.431 1.00 43.25  ? 342 HOH   B O   1 
HETATM 1857 O  O   A HOH   J 7 .   ? -14.284 -6.352  -1.602  0.50 55.93  ? 343 HOH   B O   1 
HETATM 1858 O  O   B HOH   J 7 .   ? -14.284 -6.352  -1.602  0.50 55.93  ? 343 HOH   B O   1 
HETATM 1859 O  O   A HOH   J 7 .   ? -0.880  0.272   -13.245 0.50 58.27  ? 344 HOH   B O   1 
HETATM 1860 O  O   B HOH   J 7 .   ? -0.880  0.272   -13.245 0.50 58.27  ? 344 HOH   B O   1 
HETATM 1861 O  O   . HOH   J 7 .   ? -21.522 -13.735 -21.859 1.00 59.18  ? 345 HOH   B O   1 
HETATM 1862 O  O   . HOH   J 7 .   ? -18.671 14.836  -22.001 1.00 37.70  ? 346 HOH   B O   1 
HETATM 1863 O  O   . HOH   J 7 .   ? -11.375 -5.135  -8.173  1.00 44.04  ? 347 HOH   B O   1 
HETATM 1864 O  O   A HOH   J 7 .   ? -7.273  -6.454  0.337   0.50 53.23  ? 348 HOH   B O   1 
HETATM 1865 O  O   B HOH   J 7 .   ? -7.273  -6.454  0.337   0.50 53.23  ? 348 HOH   B O   1 
HETATM 1866 O  O   . HOH   J 7 .   ? -29.444 -1.409  -18.917 1.00 48.54  ? 349 HOH   B O   1 
HETATM 1867 O  O   C HOH   J 7 .   ? -5.478  10.026  -16.626 0.33 51.27  ? 350 HOH   B O   1 
HETATM 1868 O  O   D HOH   J 7 .   ? -5.474  10.026  -16.626 0.40 51.20  ? 350 HOH   B O   1 
HETATM 1869 O  O   . HOH   J 7 .   ? -15.790 -14.578 -16.554 1.00 43.78  ? 351 HOH   B O   1 
HETATM 1870 O  O   . HOH   J 7 .   ? -25.917 -4.651  -4.038  1.00 37.12  ? 352 HOH   B O   1 
HETATM 1871 O  O   A HOH   J 7 .   ? -20.645 2.559   -32.449 0.50 55.95  ? 353 HOH   B O   1 
HETATM 1872 O  O   B HOH   J 7 .   ? -20.645 2.559   -32.449 0.50 55.95  ? 353 HOH   B O   1 
HETATM 1873 O  O   . HOH   J 7 .   ? -17.109 14.660  -30.646 1.00 50.10  ? 354 HOH   B O   1 
HETATM 1874 O  O   C HOH   J 7 .   ? -7.280  10.484  -19.057 0.33 48.86  ? 355 HOH   B O   1 
HETATM 1875 O  O   D HOH   J 7 .   ? -7.284  10.483  -19.057 0.40 48.82  ? 355 HOH   B O   1 
HETATM 1876 O  O   . HOH   J 7 .   ? -30.429 4.319   -2.498  1.00 51.90  ? 356 HOH   B O   1 
HETATM 1877 O  O   A HOH   J 7 .   ? -19.422 -13.374 -22.938 0.50 44.16  ? 357 HOH   B O   1 
HETATM 1878 O  O   B HOH   J 7 .   ? -19.422 -13.374 -22.938 0.50 44.16  ? 357 HOH   B O   1 
HETATM 1879 O  O   A HOH   J 7 .   ? -19.051 25.103  -14.313 0.50 58.57  ? 358 HOH   B O   1 
HETATM 1880 O  O   B HOH   J 7 .   ? -19.051 25.103  -14.313 0.50 58.57  ? 358 HOH   B O   1 
HETATM 1881 O  O   . HOH   J 7 .   ? -10.788 7.640   -13.717 1.00 48.02  ? 359 HOH   B O   1 
HETATM 1882 O  O   A HOH   J 7 .   ? -10.383 -18.812 -12.182 0.50 69.49  ? 360 HOH   B O   1 
HETATM 1883 O  O   B HOH   J 7 .   ? -10.383 -18.812 -12.182 0.50 69.49  ? 360 HOH   B O   1 
HETATM 1884 O  O   A HOH   J 7 .   ? -30.081 -7.780  -5.124  0.50 61.99  ? 361 HOH   B O   1 
HETATM 1885 O  O   B HOH   J 7 .   ? -30.081 -7.780  -5.124  0.50 61.99  ? 361 HOH   B O   1 
HETATM 1886 O  O   C HOH   J 7 .   ? -21.788 -13.805 -25.679 0.50 46.72  ? 362 HOH   B O   1 
HETATM 1887 O  O   D HOH   J 7 .   ? -21.788 -13.805 -25.679 0.50 46.72  ? 362 HOH   B O   1 
HETATM 1888 O  O   A HOH   J 7 .   ? -19.469 -5.822  -0.830  0.50 48.78  ? 363 HOH   B O   1 
HETATM 1889 O  O   B HOH   J 7 .   ? -19.469 -5.822  -0.830  0.50 48.78  ? 363 HOH   B O   1 
HETATM 1890 O  O   A HOH   J 7 .   ? -17.119 16.365  -21.652 0.50 52.25  ? 364 HOH   B O   1 
HETATM 1891 O  O   B HOH   J 7 .   ? -17.119 16.365  -21.652 0.50 52.25  ? 364 HOH   B O   1 
HETATM 1892 O  O   A HOH   J 7 .   ? -31.720 -7.188  -6.981  0.50 58.85  ? 365 HOH   B O   1 
HETATM 1893 O  O   B HOH   J 7 .   ? -31.720 -7.188  -6.981  0.50 58.85  ? 365 HOH   B O   1 
HETATM 1894 O  O   A HOH   J 7 .   ? -11.174 11.713  -15.361 0.50 66.89  ? 366 HOH   B O   1 
HETATM 1895 O  O   B HOH   J 7 .   ? -11.174 11.713  -15.361 0.50 66.89  ? 366 HOH   B O   1 
HETATM 1896 O  O   . HOH   J 7 .   ? -23.334 -7.323  -2.239  1.00 61.19  ? 367 HOH   B O   1 
HETATM 1897 O  O   C HOH   J 7 .   ? -12.121 -9.313  -0.216  0.50 60.33  ? 368 HOH   B O   1 
HETATM 1898 O  O   D HOH   J 7 .   ? -12.121 -9.313  -0.216  0.50 60.33  ? 368 HOH   B O   1 
HETATM 1899 O  O   . HOH   J 7 .   ? -29.212 -5.734  -1.022  1.00 44.81  ? 369 HOH   B O   1 
HETATM 1900 O  O   C HOH   J 7 .   ? -5.303  2.851   -11.266 0.33 37.64  ? 370 HOH   B O   1 
HETATM 1901 O  O   D HOH   J 7 .   ? -5.301  2.849   -11.267 0.40 37.53  ? 370 HOH   B O   1 
HETATM 1902 O  O   A HOH   J 7 .   ? -30.450 -11.870 -26.912 0.25 120.93 ? 371 HOH   B O   1 
HETATM 1903 O  O   B HOH   J 7 .   ? -30.450 -11.870 -26.912 0.25 120.93 ? 371 HOH   B O   1 
HETATM 1904 O  O   A HOH   J 7 .   ? -19.095 -12.140 -13.585 0.50 52.47  ? 372 HOH   B O   1 
HETATM 1905 O  O   B HOH   J 7 .   ? -19.095 -12.140 -13.585 0.50 52.47  ? 372 HOH   B O   1 
HETATM 1906 O  O   A HOH   J 7 .   ? -10.541 3.880   -6.095  0.25 18.99  ? 373 HOH   B O   1 
HETATM 1907 O  O   B HOH   J 7 .   ? -11.711 4.752   -4.780  0.16 12.10  ? 373 HOH   B O   1 
HETATM 1908 O  O   A HOH   J 7 .   ? -19.759 3.417   -0.075  0.25 23.51  ? 374 HOH   B O   1 
HETATM 1909 O  O   B HOH   J 7 .   ? -20.950 4.629   0.777   0.16 11.07  ? 374 HOH   B O   1 
HETATM 1910 O  O   A HOH   J 7 .   ? -8.641  5.933   -10.648 0.25 30.34  ? 375 HOH   B O   1 
HETATM 1911 O  O   B HOH   J 7 .   ? -9.030  5.314   -9.726  0.01 27.08  ? 375 HOH   B O   1 
HETATM 1912 O  O   . HOH   J 7 .   ? -11.387 -7.539  1.883   1.00 52.70  ? 376 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP   A 7   ? 0.7738 0.6902 0.7927 0.0412  0.1608  -0.0142 50  ASP   A N   
2    C CA  . ASP   A 7   ? 0.7756 0.6924 0.7758 0.0476  0.1550  -0.0178 50  ASP   A CA  
3    C C   . ASP   A 7   ? 0.7398 0.6638 0.7312 0.0636  0.1516  -0.0032 50  ASP   A C   
4    O O   . ASP   A 7   ? 0.7502 0.6729 0.7519 0.0732  0.1573  0.0092  50  ASP   A O   
5    C CB  . ASP   A 7   ? 0.7772 0.6837 0.7847 0.0468  0.1598  -0.0265 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 0.8823 0.7868 0.8758 0.0407  0.1559  -0.0402 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 0.9340 0.8303 0.9342 0.0309  0.1613  -0.0524 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 0.9400 0.8504 0.9167 0.0464  0.1485  -0.0388 50  ASP   A OD2 
9    N N   . MET   A 8   ? 0.6598 0.5909 0.6319 0.0664  0.1428  -0.0042 51  MET   A N   
10   C CA  . MET   A 8   ? 0.6246 0.5628 0.5847 0.0814  0.1380  0.0070  51  MET   A CA  
11   C C   . MET   A 8   ? 0.5873 0.5218 0.5423 0.0912  0.1352  0.0047  51  MET   A C   
12   O O   . MET   A 8   ? 0.5853 0.5153 0.5399 0.0844  0.1340  -0.0071 51  MET   A O   
13   C CB  . MET   A 8   ? 0.6205 0.5678 0.5640 0.0796  0.1294  0.0059  51  MET   A CB  
14   C CG  . MET   A 8   ? 0.6371 0.5900 0.5870 0.0725  0.1308  0.0094  51  MET   A CG  
15   S SD  . MET   A 8   ? 0.6579 0.6217 0.5892 0.0726  0.1200  0.0093  51  MET   A SD  
16   C CE  . MET   A 8   ? 0.6719 0.6430 0.6191 0.0670  0.1237  0.0163  51  MET   A CE  
17   N N   . TYR   A 9   ? 0.5382 0.4747 0.4899 0.1071  0.1344  0.0158  52  TYR   A N   
18   C CA  . TYR   A 9   ? 0.5210 0.4548 0.4697 0.1187  0.1303  0.0147  52  TYR   A CA  
19   C C   . TYR   A 9   ? 0.5034 0.4445 0.4349 0.1338  0.1226  0.0225  52  TYR   A C   
20   O O   . TYR   A 9   ? 0.4886 0.4352 0.4137 0.1371  0.1237  0.0316  52  TYR   A O   
21   C CB  . TYR   A 9   ? 0.5171 0.4424 0.4828 0.1229  0.1380  0.0189  52  TYR   A CB  
22   C CG  . TYR   A 9   ? 0.5270 0.4519 0.4960 0.1326  0.1444  0.0352  52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 0.5342 0.4572 0.5165 0.1232  0.1536  0.0394  52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 0.5503 0.4765 0.5093 0.1510  0.1415  0.0463  52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 0.5532 0.4750 0.5413 0.1313  0.1616  0.0551  52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 0.5635 0.4884 0.5238 0.1602  0.1491  0.0626  52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 0.5687 0.4911 0.5449 0.1499  0.1601  0.0674  52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 0.5981 0.5191 0.5782 0.1576  0.1694  0.0840  52  TYR   A OH  
29   N N   . ILE   A 10  ? 0.5219 0.4635 0.4468 0.1422  0.1145  0.0174  53  ILE   A N   
30   C CA  . ILE   A 10  ? 0.5219 0.4699 0.4297 0.1578  0.1057  0.0228  53  ILE   A CA  
31   C C   . ILE   A 10  ? 0.5361 0.4811 0.4439 0.1748  0.1036  0.0289  53  ILE   A C   
32   O O   . ILE   A 10  ? 0.5386 0.4772 0.4609 0.1738  0.1059  0.0249  53  ILE   A O   
33   C CB  . ILE   A 10  ? 0.5158 0.4679 0.4143 0.1547  0.0958  0.0117  53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 0.5289 0.4763 0.4376 0.1508  0.0931  -0.0004 53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 0.5220 0.4774 0.4159 0.1412  0.0967  0.0087  53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 0.5461 0.4975 0.4463 0.1518  0.0831  -0.0090 53  ILE   A CD1 
37   N N   . GLU   A 11  ? 0.5480 0.4975 0.4396 0.1904  0.0994  0.0383  54  GLU   A N   
38   C CA  . GLU   A 11  ? 0.5714 0.5189 0.4563 0.2099  0.0956  0.0457  54  GLU   A CA  
39   C C   . GLU   A 11  ? 0.5521 0.5063 0.4158 0.2234  0.0836  0.0443  54  GLU   A C   
40   O O   . GLU   A 11  ? 0.5120 0.4720 0.3635 0.2229  0.0843  0.0479  54  GLU   A O   
41   C CB  . GLU   A 11  ? 0.6090 0.5534 0.4914 0.2184  0.1059  0.0631  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 0.6482 0.5843 0.5517 0.2102  0.1180  0.0675  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 0.6948 0.6280 0.5966 0.2179  0.1295  0.0859  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 0.7131 0.6519 0.5979 0.2265  0.1302  0.0950  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 0.7223 0.6475 0.6408 0.2149  0.1389  0.0912  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 0.5568 0.5108 0.4182 0.2344  0.0724  0.0377  55  ARG   A N   
47   C CA  . ARG   A 12  ? 0.5677 0.5277 0.4106 0.2475  0.0594  0.0339  55  ARG   A CA  
48   C C   . ARG   A 12  ? 0.5869 0.5483 0.4088 0.2634  0.0623  0.0488  55  ARG   A C   
49   O O   . ARG   A 12  ? 0.6014 0.5573 0.4246 0.2699  0.0705  0.0609  55  ARG   A O   
50   C CB  . ARG   A 12  ? 0.6019 0.5611 0.4508 0.2558  0.0468  0.0235  55  ARG   A CB  
51   C CG  . ARG   A 12  ? 0.6308 0.5960 0.4667 0.2646  0.0322  0.0144  55  ARG   A CG  
52   C CD  . ARG   A 12  ? 0.6652 0.6307 0.5176 0.2632  0.0210  -0.0010 55  ARG   A CD  
53   N NE  . ARG   A 12  ? 0.6877 0.6588 0.5295 0.2693  0.0083  -0.0099 55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 0.7080 0.6817 0.5314 0.2888  -0.0027 -0.0085 55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 0.7872 0.7582 0.6010 0.3037  -0.0025 0.0015  55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 0.6874 0.6658 0.5011 0.2939  -0.0136 -0.0169 55  ARG   A NH2 
57   N N   . ALA   A 13  ? 0.5792 0.5467 0.3835 0.2682  0.0583  0.0489  56  ALA   A N   
58   C CA  . ALA   A 13  ? 0.5914 0.5612 0.3735 0.2836  0.0619  0.0623  56  ALA   A CA  
59   C C   . ALA   A 13  ? 0.5998 0.5734 0.3600 0.3013  0.0476  0.0568  56  ALA   A C   
60   O O   . ALA   A 13  ? 0.6159 0.5905 0.3547 0.3164  0.0504  0.0675  56  ALA   A O   
61   C CB  . ALA   A 13  ? 0.6095 0.5837 0.3905 0.2744  0.0721  0.0686  56  ALA   A CB  
62   N N   . GLY   A 14  ? 0.5801 0.5557 0.3450 0.2995  0.0338  0.0410  57  GLY   A N   
63   C CA  . GLY   A 14  ? 0.6014 0.5805 0.3474 0.3162  0.0192  0.0342  57  GLY   A CA  
64   C C   . GLY   A 14  ? 0.6116 0.5936 0.3684 0.3086  0.0067  0.0162  57  GLY   A C   
65   O O   . GLY   A 14  ? 0.5786 0.5603 0.3553 0.2888  0.0116  0.0105  57  GLY   A O   
66   N N   . ASP   A 15  ? 0.6338 0.6184 0.3774 0.3239  -0.0083 0.0078  58  ASP   A N   
67   C CA  . ASP   A 15  ? 0.6522 0.6402 0.4021 0.3202  -0.0211 -0.0088 58  ASP   A CA  
68   C C   . ASP   A 15  ? 0.6797 0.6715 0.4172 0.3174  -0.0179 -0.0074 58  ASP   A C   
69   O O   . ASP   A 15  ? 0.7118 0.7048 0.4311 0.3249  -0.0096 0.0049  58  ASP   A O   
70   C CB  . ASP   A 15  ? 0.6689 0.6582 0.4102 0.3384  -0.0394 -0.0193 58  ASP   A CB  
71   C CG  . ASP   A 15  ? 0.7042 0.6911 0.4621 0.3415  -0.0468 -0.0248 58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 0.6627 0.6461 0.4353 0.3321  -0.0364 -0.0181 58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 0.7434 0.7322 0.4993 0.3546  -0.0638 -0.0360 58  ASP   A OD2 
74   N N   . ILE   A 16  ? 0.6587 0.6522 0.4080 0.3062  -0.0231 -0.0192 59  ILE   A N   
75   C CA  . ILE   A 16  ? 0.6634 0.6604 0.4036 0.3036  -0.0221 -0.0198 59  ILE   A CA  
76   C C   . ILE   A 16  ? 0.6818 0.6807 0.4097 0.3195  -0.0378 -0.0308 59  ILE   A C   
77   O O   . ILE   A 16  ? 0.6650 0.6634 0.4070 0.3166  -0.0492 -0.0452 59  ILE   A O   
78   C CB  . ILE   A 16  ? 0.6476 0.6439 0.4062 0.2822  -0.0174 -0.0241 59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 0.6330 0.6275 0.3997 0.2689  -0.0023 -0.0130 59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 0.6426 0.6420 0.3935 0.2808  -0.0193 -0.0263 59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 0.6314 0.6237 0.4159 0.2487  0.0015  -0.0183 59  ILE   A CD1 
82   N N   A THR   A 17  ? 0.6995 0.7005 0.4019 0.3366  -0.0375 -0.0238 60  THR   A N   
83   N N   B THR   A 17  ? 0.6954 0.6965 0.3979 0.3364  -0.0379 -0.0243 60  THR   A N   
84   N N   C THR   A 17  ? 0.6995 0.7005 0.4019 0.3366  -0.0375 -0.0238 60  THR   A N   
85   N N   D THR   A 17  ? 0.6954 0.6965 0.3979 0.3364  -0.0379 -0.0243 60  THR   A N   
86   C CA  A THR   A 17  ? 0.7184 0.7210 0.4016 0.3560  -0.0515 -0.0325 60  THR   A CA  
87   C CA  B THR   A 17  ? 0.7111 0.7137 0.3963 0.3551  -0.0527 -0.0342 60  THR   A CA  
88   C CA  C THR   A 17  ? 0.7184 0.7210 0.4016 0.3560  -0.0515 -0.0325 60  THR   A CA  
89   C CA  D THR   A 17  ? 0.7111 0.7137 0.3963 0.3551  -0.0527 -0.0342 60  THR   A CA  
90   C C   A THR   A 17  ? 0.7300 0.7358 0.3909 0.3639  -0.0450 -0.0253 60  THR   A C   
91   C C   B THR   A 17  ? 0.7273 0.7328 0.3858 0.3673  -0.0471 -0.0261 60  THR   A C   
92   C C   C THR   A 17  ? 0.7300 0.7358 0.3909 0.3639  -0.0450 -0.0253 60  THR   A C   
93   C C   D THR   A 17  ? 0.7273 0.7328 0.3858 0.3673  -0.0471 -0.0261 60  THR   A C   
94   O O   A THR   A 17  ? 0.7397 0.7462 0.3891 0.3657  -0.0294 -0.0080 60  THR   A O   
95   O O   B THR   A 17  ? 0.7336 0.7389 0.3790 0.3718  -0.0331 -0.0090 60  THR   A O   
96   O O   C THR   A 17  ? 0.7397 0.7462 0.3891 0.3657  -0.0294 -0.0080 60  THR   A O   
97   O O   D THR   A 17  ? 0.7336 0.7389 0.3790 0.3718  -0.0331 -0.0090 60  THR   A O   
98   C CB  A THR   A 17  ? 0.7385 0.7393 0.4065 0.3749  -0.0581 -0.0302 60  THR   A CB  
99   C CB  B THR   A 17  ? 0.7241 0.7247 0.4019 0.3709  -0.0623 -0.0361 60  THR   A CB  
100  C CB  C THR   A 17  ? 0.7385 0.7393 0.4065 0.3749  -0.0581 -0.0302 60  THR   A CB  
101  C CB  D THR   A 17  ? 0.7241 0.7247 0.4019 0.3709  -0.0623 -0.0361 60  THR   A CB  
102  O OG1 A THR   A 17  ? 0.7499 0.7500 0.3981 0.3829  -0.0444 -0.0121 60  THR   A OG1 
103  O OG1 B THR   A 17  ? 0.7042 0.7032 0.4096 0.3600  -0.0681 -0.0453 60  THR   A OG1 
104  O OG1 C THR   A 17  ? 0.7499 0.7500 0.3981 0.3829  -0.0444 -0.0121 60  THR   A OG1 
105  O OG1 D THR   A 17  ? 0.7042 0.7032 0.4096 0.3600  -0.0681 -0.0453 60  THR   A OG1 
106  C CG2 A THR   A 17  ? 0.7375 0.7355 0.4272 0.3686  -0.0618 -0.0339 60  THR   A CG2 
107  C CG2 B THR   A 17  ? 0.7459 0.7480 0.4028 0.3916  -0.0782 -0.0463 60  THR   A CG2 
108  C CG2 C THR   A 17  ? 0.7375 0.7355 0.4272 0.3686  -0.0618 -0.0339 60  THR   A CG2 
109  C CG2 D THR   A 17  ? 0.7459 0.7480 0.4028 0.3916  -0.0782 -0.0463 60  THR   A CG2 
110  N N   . TRP   A 18  ? 0.7378 0.7452 0.3929 0.3708  -0.0572 -0.0385 61  TRP   A N   
111  C CA  . TRP   A 18  ? 0.7994 0.8096 0.4294 0.3847  -0.0547 -0.0348 61  TRP   A CA  
112  C C   . TRP   A 18  ? 0.8438 0.8527 0.4463 0.4072  -0.0576 -0.0300 61  TRP   A C   
113  O O   . TRP   A 18  ? 0.8907 0.8974 0.4937 0.4150  -0.0713 -0.0394 61  TRP   A O   
114  C CB  . TRP   A 18  ? 0.7895 0.8006 0.4220 0.3864  -0.0672 -0.0508 61  TRP   A CB  
115  C CG  . TRP   A 18  ? 0.8380 0.8518 0.4471 0.3994  -0.0635 -0.0477 61  TRP   A CG  
116  C CD1 . TRP   A 18  ? 0.8870 0.9008 0.4671 0.4220  -0.0691 -0.0498 61  TRP   A CD1 
117  C CD2 . TRP   A 18  ? 0.8493 0.8663 0.4618 0.3913  -0.0536 -0.0424 61  TRP   A CD2 
118  N NE1 . TRP   A 18  ? 0.8994 0.9161 0.4651 0.4281  -0.0617 -0.0459 61  TRP   A NE1 
119  C CE2 . TRP   A 18  ? 0.8773 0.8963 0.4637 0.4097  -0.0528 -0.0417 61  TRP   A CE2 
120  C CE3 . TRP   A 18  ? 0.8091 0.8272 0.4431 0.3712  -0.0457 -0.0383 61  TRP   A CE3 
121  C CZ2 . TRP   A 18  ? 0.8874 0.9101 0.4717 0.4083  -0.0440 -0.0370 61  TRP   A CZ2 
122  C CZ3 . TRP   A 18  ? 0.8396 0.8614 0.4708 0.3700  -0.0385 -0.0337 61  TRP   A CZ3 
123  C CH2 . TRP   A 18  ? 0.8596 0.8840 0.4679 0.3880  -0.0374 -0.0330 61  TRP   A CH2 
124  N N   A GLU   A 19  ? 0.8826 0.8926 0.4623 0.4174  -0.0450 -0.0157 62  GLU   A N   
125  N N   B GLU   A 19  ? 0.8826 0.8926 0.4623 0.4174  -0.0450 -0.0157 62  GLU   A N   
126  N N   C GLU   A 19  ? 0.8648 0.8747 0.4455 0.4166  -0.0442 -0.0148 62  GLU   A N   
127  N N   D GLU   A 19  ? 0.8648 0.8747 0.4455 0.4166  -0.0442 -0.0148 62  GLU   A N   
128  C CA  A GLU   A 19  ? 0.9295 0.9373 0.4780 0.4402  -0.0451 -0.0083 62  GLU   A CA  
129  C CA  B GLU   A 19  ? 0.9295 0.9373 0.4780 0.4402  -0.0451 -0.0083 62  GLU   A CA  
130  C CA  C GLU   A 19  ? 0.9029 0.9108 0.4511 0.4400  -0.0441 -0.0077 62  GLU   A CA  
131  C CA  D GLU   A 19  ? 0.9029 0.9108 0.4511 0.4400  -0.0441 -0.0077 62  GLU   A CA  
132  C C   A GLU   A 19  ? 0.9659 0.9758 0.4858 0.4570  -0.0441 -0.0090 62  GLU   A C   
133  C C   B GLU   A 19  ? 0.9659 0.9758 0.4858 0.4570  -0.0441 -0.0090 62  GLU   A C   
134  C C   C GLU   A 19  ? 0.9472 0.9575 0.4691 0.4558  -0.0451 -0.0108 62  GLU   A C   
135  C C   D GLU   A 19  ? 0.9472 0.9575 0.4691 0.4558  -0.0451 -0.0108 62  GLU   A C   
136  O O   A GLU   A 19  ? 0.9622 0.9751 0.4801 0.4529  -0.0282 0.0022  62  GLU   A O   
137  O O   B GLU   A 19  ? 0.9622 0.9751 0.4801 0.4529  -0.0282 0.0022  62  GLU   A O   
138  O O   C GLU   A 19  ? 0.9408 0.9544 0.4643 0.4497  -0.0319 -0.0032 62  GLU   A O   
139  O O   D GLU   A 19  ? 0.9408 0.9544 0.4643 0.4497  -0.0319 -0.0032 62  GLU   A O   
140  C CB  A GLU   A 19  ? 0.9369 0.9425 0.4848 0.4373  -0.0273 0.0122  62  GLU   A CB  
141  C CB  B GLU   A 19  ? 0.9369 0.9425 0.4848 0.4373  -0.0273 0.0122  62  GLU   A CB  
142  C CB  C GLU   A 19  ? 0.8942 0.9004 0.4368 0.4397  -0.0249 0.0141  62  GLU   A CB  
143  C CB  D GLU   A 19  ? 0.8942 0.9004 0.4368 0.4397  -0.0249 0.0141  62  GLU   A CB  
144  C CG  A GLU   A 19  ? 0.9211 0.9244 0.4985 0.4197  -0.0262 0.0130  62  GLU   A CG  
145  C CG  B GLU   A 19  ? 0.9211 0.9244 0.4985 0.4197  -0.0262 0.0130  62  GLU   A CG  
146  C CG  C GLU   A 19  ? 0.9219 0.9248 0.4292 0.4643  -0.0233 0.0234  62  GLU   A CG  
147  C CG  D GLU   A 19  ? 0.9219 0.9248 0.4292 0.4643  -0.0233 0.0234  62  GLU   A CG  
148  C CD  A GLU   A 19  ? 0.9319 0.9315 0.5111 0.4273  -0.0410 0.0049  62  GLU   A CD  
149  C CD  B GLU   A 19  ? 0.9319 0.9315 0.5111 0.4273  -0.0410 0.0049  62  GLU   A CD  
150  C CD  C GLU   A 19  ? 0.9214 0.9230 0.4189 0.4667  -0.0008 0.0464  62  GLU   A CD  
151  C CD  D GLU   A 19  ? 0.9214 0.9230 0.4189 0.4667  -0.0008 0.0464  62  GLU   A CD  
152  O OE1 A GLU   A 19  ? 0.9839 0.9828 0.5401 0.4474  -0.0542 -0.0019 62  GLU   A OE1 
153  O OE1 B GLU   A 19  ? 0.9839 0.9828 0.5401 0.4474  -0.0542 -0.0019 62  GLU   A OE1 
154  O OE1 C GLU   A 19  ? 0.9194 0.9227 0.4419 0.4474  0.0129  0.0552  62  GLU   A OE1 
155  O OE1 D GLU   A 19  ? 0.9194 0.9227 0.4419 0.4474  0.0129  0.0552  62  GLU   A OE1 
156  O OE2 A GLU   A 19  ? 0.9081 0.9057 0.5121 0.4135  -0.0397 0.0050  62  GLU   A OE2 
157  O OE2 B GLU   A 19  ? 0.9081 0.9057 0.5121 0.4135  -0.0397 0.0050  62  GLU   A OE2 
158  O OE2 C GLU   A 19  ? 0.9522 0.9508 0.4167 0.4881  0.0030  0.0555  62  GLU   A OE2 
159  O OE2 D GLU   A 19  ? 0.9522 0.9508 0.4167 0.4881  0.0030  0.0555  62  GLU   A OE2 
160  N N   . LYS   A 20  ? 1.0083 1.0169 0.5070 0.4758  -0.0604 -0.0219 63  LYS   A N   
161  C CA  . LYS   A 20  ? 1.0722 1.0821 0.5410 0.4940  -0.0611 -0.0253 63  LYS   A CA  
162  C C   . LYS   A 20  ? 1.0766 1.0854 0.5170 0.5073  -0.0430 -0.0048 63  LYS   A C   
163  O O   . LYS   A 20  ? 1.0263 1.0313 0.4601 0.5118  -0.0392 0.0063  63  LYS   A O   
164  C CB  . LYS   A 20  ? 1.1603 1.1683 0.6117 0.5120  -0.0837 -0.0445 63  LYS   A CB  
165  C CG  . LYS   A 20  ? 1.2004 1.2095 0.6794 0.5009  -0.1011 -0.0661 63  LYS   A CG  
166  C CD  . LYS   A 20  ? 1.2585 1.2656 0.7345 0.5126  -0.1241 -0.0827 63  LYS   A CD  
167  C CE  . LYS   A 20  ? 1.2818 1.2897 0.7920 0.4993  -0.1398 -0.1028 63  LYS   A CE  
168  N NZ  . LYS   A 20  ? 1.2868 1.2936 0.8038 0.5061  -0.1592 -0.1150 63  LYS   A NZ  
169  N N   . ASP   A 21  ? 1.1136 1.1252 0.5399 0.5129  -0.0309 0.0006  64  ASP   A N   
170  C CA  . ASP   A 21  ? 1.1942 1.2049 0.5953 0.5251  -0.0106 0.0213  64  ASP   A CA  
171  C C   . ASP   A 21  ? 1.1705 1.1810 0.5953 0.5079  0.0058  0.0396  64  ASP   A C   
172  O O   . ASP   A 21  ? 1.1700 1.1764 0.5796 0.5170  0.0168  0.0560  64  ASP   A O   
173  C CB  . ASP   A 21  ? 1.3149 1.3201 0.6739 0.5525  -0.0173 0.0219  64  ASP   A CB  
174  C CG  . ASP   A 21  ? 1.3896 1.3949 0.7225 0.5708  -0.0325 0.0036  64  ASP   A CG  
175  O OD1 . ASP   A 21  ? 1.4883 1.4959 0.8042 0.5792  -0.0214 0.0064  64  ASP   A OD1 
176  O OD2 . ASP   A 21  ? 1.4261 1.4294 0.7577 0.5764  -0.0554 -0.0141 64  ASP   A OD2 
177  N N   . ALA   A 22  ? 1.1131 1.1274 0.5745 0.4838  0.0075  0.0368  65  ALA   A N   
178  C CA  . ALA   A 22  ? 1.0181 1.0344 0.5017 0.4669  0.0271  0.0539  65  ALA   A CA  
179  C C   . ALA   A 22  ? 0.9846 1.0061 0.4582 0.4724  0.0448  0.0645  65  ALA   A C   
180  O O   . ALA   A 22  ? 0.9925 1.0174 0.4543 0.4809  0.0397  0.0543  65  ALA   A O   
181  C CB  . ALA   A 22  ? 1.0078 1.0267 0.5286 0.4416  0.0229  0.0464  65  ALA   A CB  
182  N N   . GLU   A 23  ? 0.9616 0.9832 0.4430 0.4670  0.0649  0.0843  66  GLU   A N   
183  C CA  . GLU   A 23  ? 0.9855 1.0126 0.4674 0.4680  0.0856  0.0980  66  GLU   A CA  
184  C C   . GLU   A 23  ? 0.9582 0.9930 0.4623 0.4540  0.0813  0.0873  66  GLU   A C   
185  O O   . GLU   A 23  ? 0.8674 0.9036 0.4009 0.4333  0.0749  0.0813  66  GLU   A O   
186  C CB  . GLU   A 23  ? 1.0245 1.0506 0.5245 0.4574  0.1043  0.1172  66  GLU   A CB  
187  C CG  . GLU   A 23  ? 1.0976 1.1307 0.6089 0.4536  0.1256  0.1309  66  GLU   A CG  
188  C CD  . GLU   A 23  ? 1.1975 1.2276 0.7220 0.4478  0.1445  0.1507  66  GLU   A CD  
189  O OE1 . GLU   A 23  ? 1.2702 1.2932 0.7702 0.4643  0.1525  0.1628  66  GLU   A OE1 
190  O OE2 . GLU   A 23  ? 1.2199 1.2541 0.7788 0.4271  0.1502  0.1537  66  GLU   A OE2 
191  N N   . VAL   A 24  ? 0.9546 0.9934 0.4439 0.4656  0.0826  0.0830  67  VAL   A N   
192  C CA  . VAL   A 24  ? 0.9398 0.9850 0.4484 0.4546  0.0763  0.0716  67  VAL   A CA  
193  C C   . VAL   A 24  ? 0.9343 0.9874 0.4578 0.4491  0.0966  0.0858  67  VAL   A C   
194  O O   . VAL   A 24  ? 0.9697 1.0244 0.4734 0.4652  0.1088  0.0932  67  VAL   A O   
195  C CB  . VAL   A 24  ? 0.9678 1.0120 0.4542 0.4703  0.0623  0.0549  67  VAL   A CB  
196  C CG1 . VAL   A 24  ? 0.9254 0.9751 0.4327 0.4593  0.0566  0.0446  67  VAL   A CG1 
197  C CG2 . VAL   A 24  ? 0.9907 1.0276 0.4636 0.4771  0.0420  0.0409  67  VAL   A CG2 
198  N N   . THR   A 25  ? 0.9112 0.9689 0.4686 0.4273  0.1000  0.0891  68  THR   A N   
199  C CA  . THR   A 25  ? 0.8748 0.9410 0.4520 0.4202  0.1186  0.1026  68  THR   A CA  
200  C C   . THR   A 25  ? 0.8435 0.9157 0.4533 0.3991  0.1120  0.0961  68  THR   A C   
201  O O   . THR   A 25  ? 0.8307 0.8996 0.4439 0.3921  0.0945  0.0819  68  THR   A O   
202  C CB  . THR   A 25  ? 0.8846 0.9489 0.4668 0.4183  0.1360  0.1209  68  THR   A CB  
203  O OG1 . THR   A 25  ? 0.8986 0.9716 0.5002 0.4136  0.1543  0.1332  68  THR   A OG1 
204  C CG2 . THR   A 25  ? 0.8662 0.9263 0.4690 0.4003  0.1309  0.1210  68  THR   A CG2 
205  N N   . GLY   A 26  ? 0.8269 0.9074 0.4600 0.3900  0.1258  0.1066  69  GLY   A N   
206  C CA  . GLY   A 26  ? 0.7998 0.8870 0.4635 0.3711  0.1207  0.1025  69  GLY   A CA  
207  C C   . GLY   A 26  ? 0.8033 0.8963 0.4665 0.3767  0.1155  0.0943  69  GLY   A C   
208  O O   . GLY   A 26  ? 0.8420 0.9309 0.4815 0.3913  0.1072  0.0847  69  GLY   A O   
209  N N   . ASN   A 27  ? 0.7888 0.8907 0.4792 0.3647  0.1184  0.0968  70  ASN   A N   
210  C CA  . ASN   A 27  ? 0.7872 0.8949 0.4838 0.3666  0.1118  0.0889  70  ASN   A CA  
211  C C   . ASN   A 27  ? 0.7181 0.8225 0.4275 0.3507  0.0933  0.0773  70  ASN   A C   
212  O O   . ASN   A 27  ? 0.6465 0.7436 0.3553 0.3408  0.0862  0.0744  70  ASN   A O   
213  C CB  . ASN   A 27  ? 0.8200 0.9399 0.5365 0.3671  0.1280  0.1002  70  ASN   A CB  
214  C CG  . ASN   A 27  ? 0.8228 0.9492 0.5734 0.3464  0.1294  0.1058  70  ASN   A CG  
215  O OD1 . ASN   A 27  ? 0.8455 0.9686 0.6032 0.3357  0.1317  0.1107  70  ASN   A OD1 
216  N ND2 . ASN   A 27  ? 0.8467 0.9827 0.6192 0.3410  0.1276  0.1048  70  ASN   A ND2 
217  N N   . SER   A 28  ? 0.6807 0.7889 0.3983 0.3501  0.0857  0.0703  71  SER   A N   
218  C CA  . SER   A 28  ? 0.6999 0.8037 0.4252 0.3390  0.0682  0.0589  71  SER   A CA  
219  C C   . SER   A 28  ? 0.7043 0.8172 0.4548 0.3295  0.0679  0.0618  71  SER   A C   
220  O O   . SER   A 28  ? 0.7386 0.8523 0.4900 0.3343  0.0610  0.0553  71  SER   A O   
221  C CB  . SER   A 28  ? 0.7133 0.8100 0.4199 0.3510  0.0565  0.0455  71  SER   A CB  
222  O OG  . SER   A 28  ? 0.7777 0.8685 0.4590 0.3650  0.0580  0.0433  71  SER   A OG  
223  N N   . PRO   A 29  ? 0.7135 0.8330 0.4856 0.3158  0.0742  0.0709  72  PRO   A N   
224  C CA  . PRO   A 29  ? 0.7068 0.8365 0.5042 0.3079  0.0740  0.0743  72  PRO   A CA  
225  C C   . PRO   A 29  ? 0.6807 0.8057 0.4845 0.2958  0.0570  0.0661  72  PRO   A C   
226  O O   . PRO   A 29  ? 0.6392 0.7549 0.4364 0.2863  0.0491  0.0613  72  PRO   A O   
227  C CB  . PRO   A 29  ? 0.7190 0.8555 0.5358 0.2971  0.0850  0.0852  72  PRO   A CB  
228  C CG  . PRO   A 29  ? 0.7118 0.8376 0.5159 0.2908  0.0831  0.0837  72  PRO   A CG  
229  C CD  . PRO   A 29  ? 0.7243 0.8410 0.4992 0.3062  0.0799  0.0770  72  PRO   A CD  
230  N N   . ARG   A 30  ? 0.7068 0.8378 0.5230 0.2969  0.0524  0.0648  73  ARG   A N   
231  C CA  . ARG   A 30  ? 0.7669 0.8944 0.5918 0.2853  0.0374  0.0597  73  ARG   A CA  
232  C C   . ARG   A 30  ? 0.7039 0.8413 0.5539 0.2716  0.0380  0.0669  73  ARG   A C   
233  O O   . ARG   A 30  ? 0.6385 0.7878 0.5051 0.2758  0.0448  0.0725  73  ARG   A O   
234  C CB  . ARG   A 30  ? 0.8592 0.9855 0.6815 0.2957  0.0302  0.0534  73  ARG   A CB  
235  C CG  . ARG   A 30  ? 0.9672 1.0828 0.7655 0.3082  0.0271  0.0440  73  ARG   A CG  
236  C CD  . ARG   A 30  ? 1.0994 1.2163 0.8945 0.3240  0.0262  0.0388  73  ARG   A CD  
237  N NE  . ARG   A 30  ? 1.1524 1.2582 0.9260 0.3347  0.0202  0.0274  73  ARG   A NE  
238  C CZ  . ARG   A 30  ? 1.1219 1.2165 0.8922 0.3303  0.0067  0.0180  73  ARG   A CZ  
239  N NH1 . ARG   A 30  ? 1.1642 1.2564 0.9483 0.3159  -0.0014 0.0195  73  ARG   A NH1 
240  N NH2 . ARG   A 30  ? 0.9981 1.0839 0.7515 0.3405  0.0016  0.0071  73  ARG   A NH2 
241  N N   . LEU   A 31  ? 0.6800 0.8126 0.5327 0.2557  0.0316  0.0661  74  LEU   A N   
242  C CA  . LEU   A 31  ? 0.6624 0.8037 0.5371 0.2422  0.0326  0.0720  74  LEU   A CA  
243  C C   . LEU   A 31  ? 0.6236 0.7597 0.5003 0.2292  0.0173  0.0678  74  LEU   A C   
244  O O   . LEU   A 31  ? 0.6402 0.7635 0.5005 0.2242  0.0105  0.0620  74  LEU   A O   
245  C CB  . LEU   A 31  ? 0.6821 0.8215 0.5556 0.2362  0.0420  0.0754  74  LEU   A CB  
246  C CG  . LEU   A 31  ? 0.6868 0.8315 0.5597 0.2482  0.0588  0.0823  74  LEU   A CG  
247  C CD1 . LEU   A 31  ? 0.6822 0.8227 0.5541 0.2410  0.0665  0.0857  74  LEU   A CD1 
248  C CD2 . LEU   A 31  ? 0.7001 0.8602 0.5975 0.2519  0.0674  0.0898  74  LEU   A CD2 
249  N N   . ASP   A 32  ? 0.6157 0.7616 0.5120 0.2250  0.0122  0.0707  75  ASP   A N   
250  C CA  . ASP   A 32  ? 0.6300 0.7729 0.5298 0.2118  -0.0016 0.0688  75  ASP   A CA  
251  C C   . ASP   A 32  ? 0.5657 0.7084 0.4703 0.1971  -0.0006 0.0694  75  ASP   A C   
252  O O   . ASP   A 32  ? 0.5488 0.7036 0.4746 0.1941  0.0060  0.0743  75  ASP   A O   
253  C CB  . ASP   A 32  ? 0.6702 0.8257 0.5921 0.2128  -0.0074 0.0723  75  ASP   A CB  
254  C CG  . ASP   A 32  ? 0.7171 0.8715 0.6354 0.2259  -0.0108 0.0708  75  ASP   A CG  
255  O OD1 . ASP   A 32  ? 0.7418 0.8824 0.6395 0.2288  -0.0159 0.0655  75  ASP   A OD1 
256  O OD2 . ASP   A 32  ? 0.7785 0.9458 0.7163 0.2329  -0.0081 0.0746  75  ASP   A OD2 
257  N N   . VAL   A 33  ? 0.5670 0.6966 0.4547 0.1881  -0.0069 0.0645  76  VAL   A N   
258  C CA  . VAL   A 33  ? 0.5621 0.6896 0.4520 0.1745  -0.0051 0.0638  76  VAL   A CA  
259  C C   . VAL   A 33  ? 0.5745 0.6941 0.4562 0.1623  -0.0184 0.0598  76  VAL   A C   
260  O O   . VAL   A 33  ? 0.5640 0.6753 0.4324 0.1649  -0.0270 0.0576  76  VAL   A O   
261  C CB  . VAL   A 33  ? 0.5647 0.6835 0.4412 0.1760  0.0046  0.0621  76  VAL   A CB  
262  C CG1 . VAL   A 33  ? 0.5776 0.7020 0.4562 0.1899  0.0169  0.0663  76  VAL   A CG1 
263  C CG2 . VAL   A 33  ? 0.5736 0.6772 0.4275 0.1756  -0.0012 0.0557  76  VAL   A CG2 
264  N N   . ALA   A 34  ? 0.5491 0.6705 0.4379 0.1497  -0.0195 0.0589  77  ALA   A N   
265  C CA  . ALA   A 34  ? 0.5414 0.6538 0.4187 0.1371  -0.0298 0.0545  77  ALA   A CA  
266  C C   . ALA   A 34  ? 0.5197 0.6236 0.3890 0.1285  -0.0228 0.0506  77  ALA   A C   
267  O O   . ALA   A 34  ? 0.4989 0.6079 0.3793 0.1303  -0.0120 0.0527  77  ALA   A O   
268  C CB  . ALA   A 34  ? 0.5494 0.6722 0.4429 0.1306  -0.0391 0.0557  77  ALA   A CB  
269  N N   . LEU   A 35  ? 0.5165 0.6070 0.3666 0.1211  -0.0278 0.0458  78  LEU   A N   
270  C CA  . LEU   A 35  ? 0.5340 0.6145 0.3747 0.1123  -0.0224 0.0409  78  LEU   A CA  
271  C C   . LEU   A 35  ? 0.5670 0.6438 0.4021 0.0991  -0.0311 0.0369  78  LEU   A C   
272  O O   . LEU   A 35  ? 0.5934 0.6636 0.4138 0.0975  -0.0410 0.0363  78  LEU   A O   
273  C CB  . LEU   A 35  ? 0.5300 0.5974 0.3520 0.1168  -0.0199 0.0381  78  LEU   A CB  
274  C CG  . LEU   A 35  ? 0.5326 0.5886 0.3445 0.1085  -0.0145 0.0326  78  LEU   A CG  
275  C CD1 . LEU   A 35  ? 0.5105 0.5714 0.3351 0.1082  -0.0042 0.0335  78  LEU   A CD1 
276  C CD2 . LEU   A 35  ? 0.5352 0.5794 0.3324 0.1131  -0.0134 0.0295  78  LEU   A CD2 
277  N N   . ASP   A 36  ? 0.5338 0.6152 0.3811 0.0907  -0.0281 0.0348  79  ASP   A N   
278  C CA  . ASP   A 36  ? 0.5463 0.6259 0.3903 0.0785  -0.0367 0.0298  79  ASP   A CA  
279  C C   . ASP   A 36  ? 0.5554 0.6194 0.3793 0.0705  -0.0330 0.0233  79  ASP   A C   
280  O O   . ASP   A 36  ? 0.5079 0.5646 0.3256 0.0743  -0.0236 0.0231  79  ASP   A O   
281  C CB  . ASP   A 36  ? 0.5464 0.6395 0.4169 0.0739  -0.0364 0.0297  79  ASP   A CB  
282  C CG  . ASP   A 36  ? 0.5595 0.6515 0.4410 0.0693  -0.0241 0.0275  79  ASP   A CG  
283  O OD1 . ASP   A 36  ? 0.5800 0.6605 0.4473 0.0692  -0.0167 0.0254  79  ASP   A OD1 
284  O OD2 . ASP   A 36  ? 0.5933 0.6961 0.5000 0.0659  -0.0221 0.0281  79  ASP   A OD2 
285  N N   . GLU   A 37  ? 0.5584 0.6177 0.3725 0.0600  -0.0403 0.0178  80  GLU   A N   
286  C CA  . GLU   A 37  ? 0.5796 0.6235 0.3725 0.0522  -0.0371 0.0114  80  GLU   A CA  
287  C C   . GLU   A 37  ? 0.5548 0.5968 0.3580 0.0489  -0.0245 0.0079  80  GLU   A C   
288  O O   . GLU   A 37  ? 0.5733 0.6028 0.3621 0.0458  -0.0184 0.0037  80  GLU   A O   
289  C CB  . GLU   A 37  ? 0.6341 0.6752 0.4143 0.0434  -0.0486 0.0068  80  GLU   A CB  
290  C CG  . GLU   A 37  ? 0.6820 0.7062 0.4351 0.0368  -0.0461 0.0014  80  GLU   A CG  
291  C CD  . GLU   A 37  ? 0.7209 0.7411 0.4576 0.0283  -0.0568 -0.0038 80  GLU   A CD  
292  O OE1 . GLU   A 37  ? 0.7268 0.7493 0.4705 0.0203  -0.0571 -0.0112 80  GLU   A OE1 
293  O OE2 . GLU   A 37  ? 0.7481 0.7626 0.4650 0.0303  -0.0651 -0.0006 80  GLU   A OE2 
294  N N   . SER   A 38  ? 0.5450 0.5985 0.3732 0.0495  -0.0203 0.0097  81  SER   A N   
295  C CA  . SER   A 38  ? 0.5459 0.5982 0.3872 0.0472  -0.0081 0.0079  81  SER   A CA  
296  C C   . SER   A 38  ? 0.5269 0.5785 0.3698 0.0583  0.0016  0.0137  81  SER   A C   
297  O O   . SER   A 38  ? 0.5291 0.5790 0.3814 0.0579  0.0116  0.0135  81  SER   A O   
298  C CB  . SER   A 38  ? 0.5775 0.6416 0.4461 0.0436  -0.0069 0.0085  81  SER   A CB  
299  O OG  . SER   A 38  ? 0.6394 0.7063 0.5089 0.0344  -0.0183 0.0025  81  SER   A OG  
300  N N   . GLY   A 39  ? 0.5140 0.5659 0.3476 0.0680  -0.0014 0.0182  82  GLY   A N   
301  C CA  . GLY   A 39  ? 0.5193 0.5700 0.3519 0.0794  0.0064  0.0222  82  GLY   A CA  
302  C C   . GLY   A 39  ? 0.5045 0.5674 0.3567 0.0879  0.0127  0.0295  82  GLY   A C   
303  O O   . GLY   A 39  ? 0.4933 0.5549 0.3453 0.0965  0.0208  0.0325  82  GLY   A O   
304  N N   . ASP   A 40  ? 0.5283 0.6029 0.3966 0.0861  0.0089  0.0324  83  ASP   A N   
305  C CA  . ASP   A 40  ? 0.5295 0.6171 0.4188 0.0938  0.0153  0.0401  83  ASP   A CA  
306  C C   . ASP   A 40  ? 0.5339 0.6282 0.4207 0.1040  0.0095  0.0444  83  ASP   A C   
307  O O   . ASP   A 40  ? 0.5059 0.6030 0.3913 0.1005  -0.0019 0.0427  83  ASP   A O   
308  C CB  . ASP   A 40  ? 0.5536 0.6504 0.4674 0.0847  0.0154  0.0399  83  ASP   A CB  
309  C CG  . ASP   A 40  ? 0.5970 0.6871 0.5164 0.0762  0.0234  0.0362  83  ASP   A CG  
310  O OD1 . ASP   A 40  ? 0.6176 0.7002 0.5294 0.0812  0.0327  0.0378  83  ASP   A OD1 
311  O OD2 . ASP   A 40  ? 0.6388 0.7308 0.5701 0.0651  0.0196  0.0312  83  ASP   A OD2 
312  N N   . PHE   A 41  ? 0.5242 0.6208 0.4103 0.1169  0.0171  0.0497  84  PHE   A N   
313  C CA  . PHE   A 41  ? 0.5177 0.6225 0.4059 0.1282  0.0142  0.0542  84  PHE   A CA  
314  C C   . PHE   A 41  ? 0.5391 0.6593 0.4539 0.1285  0.0171  0.0597  84  PHE   A C   
315  O O   . PHE   A 41  ? 0.5685 0.6924 0.4991 0.1246  0.0261  0.0621  84  PHE   A O   
316  C CB  . PHE   A 41  ? 0.4915 0.5929 0.3686 0.1421  0.0218  0.0567  84  PHE   A CB  
317  C CG  . PHE   A 41  ? 0.4869 0.5751 0.3412 0.1437  0.0167  0.0508  84  PHE   A CG  
318  C CD1 . PHE   A 41  ? 0.4717 0.5572 0.3167 0.1458  0.0066  0.0484  84  PHE   A CD1 
319  C CD2 . PHE   A 41  ? 0.4710 0.5495 0.3152 0.1438  0.0223  0.0479  84  PHE   A CD2 
320  C CE1 . PHE   A 41  ? 0.4787 0.5521 0.3060 0.1475  0.0028  0.0431  84  PHE   A CE1 
321  C CE2 . PHE   A 41  ? 0.4646 0.5320 0.2914 0.1459  0.0177  0.0422  84  PHE   A CE2 
322  C CZ  . PHE   A 41  ? 0.4580 0.5230 0.2771 0.1477  0.0084  0.0398  84  PHE   A CZ  
323  N N   . SER   A 42  ? 0.5357 0.6645 0.4567 0.1336  0.0101  0.0618  85  SER   A N   
324  C CA  . SER   A 42  ? 0.5570 0.7021 0.5058 0.1361  0.0128  0.0673  85  SER   A CA  
325  C C   . SER   A 42  ? 0.5605 0.7112 0.5078 0.1500  0.0121  0.0711  85  SER   A C   
326  O O   . SER   A 42  ? 0.5130 0.6555 0.4402 0.1539  0.0034  0.0678  85  SER   A O   
327  C CB  . SER   A 42  ? 0.6003 0.7514 0.5634 0.1242  0.0009  0.0639  85  SER   A CB  
328  O OG  . SER   A 42  ? 0.6078 0.7524 0.5525 0.1227  -0.0136 0.0598  85  SER   A OG  
329  N N   . LEU   A 43  ? 0.6002 0.7639 0.5688 0.1574  0.0217  0.0776  86  LEU   A N   
330  C CA  . LEU   A 43  ? 0.6494 0.8209 0.6217 0.1705  0.0216  0.0810  86  LEU   A CA  
331  C C   . LEU   A 43  ? 0.6733 0.8525 0.6589 0.1658  0.0068  0.0792  86  LEU   A C   
332  O O   . LEU   A 43  ? 0.6646 0.8538 0.6746 0.1569  0.0041  0.0797  86  LEU   A O   
333  C CB  . LEU   A 43  ? 0.6684 0.8510 0.6597 0.1793  0.0385  0.0889  86  LEU   A CB  
334  C CG  . LEU   A 43  ? 0.6896 0.8630 0.6621 0.1868  0.0519  0.0912  86  LEU   A CG  
335  C CD1 . LEU   A 43  ? 0.7179 0.8988 0.7104 0.1880  0.0694  0.0994  86  LEU   A CD1 
336  C CD2 . LEU   A 43  ? 0.7186 0.8877 0.6697 0.2027  0.0529  0.0906  86  LEU   A CD2 
337  N N   . VAL   A 44  ? 0.7310 0.9048 0.7011 0.1716  -0.0029 0.0769  87  VAL   A N   
338  C CA  . VAL   A 44  ? 0.7539 0.9350 0.7355 0.1715  -0.0167 0.0768  87  VAL   A CA  
339  C C   . VAL   A 44  ? 0.8168 1.0120 0.8191 0.1843  -0.0088 0.0822  87  VAL   A C   
340  O O   . VAL   A 44  ? 0.8670 1.0588 0.8577 0.1967  0.0008  0.0835  87  VAL   A O   
341  C CB  . VAL   A 44  ? 0.7518 0.9190 0.7072 0.1730  -0.0287 0.0730  87  VAL   A CB  
342  C CG1 . VAL   A 44  ? 0.7477 0.9216 0.7135 0.1776  -0.0407 0.0746  87  VAL   A CG1 
343  C CG2 . VAL   A 44  ? 0.7487 0.9027 0.6851 0.1599  -0.0358 0.0681  87  VAL   A CG2 
344  N N   . GLU   A 45  ? 0.8793 1.0901 0.9119 0.1821  -0.0123 0.0847  88  GLU   A N   
345  C CA  . GLU   A 45  ? 0.9943 1.2192 1.0492 0.1945  -0.0042 0.0897  88  GLU   A CA  
346  C C   . GLU   A 45  ? 0.9957 1.2298 1.0679 0.1948  -0.0198 0.0894  88  GLU   A C   
347  O O   . GLU   A 45  ? 1.0084 1.2336 1.0625 0.1988  -0.0308 0.0871  88  GLU   A O   
348  C CB  . GLU   A 45  ? 1.0363 1.2729 1.1168 0.1934  0.0124  0.0948  88  GLU   A CB  
349  C CG  . GLU   A 45  ? 1.0642 1.2912 1.1249 0.1977  0.0288  0.0968  88  GLU   A CG  
350  C CD  . GLU   A 45  ? 1.0449 1.2742 1.1007 0.2149  0.0434  0.1012  88  GLU   A CD  
351  O OE1 . GLU   A 45  ? 1.0398 1.2688 1.0885 0.2245  0.0374  0.0993  88  GLU   A OE1 
352  O OE2 . GLU   A 45  ? 1.0484 1.2802 1.1087 0.2189  0.0609  0.1067  88  GLU   A OE2 
353  N N   . GLY   B 7   ? 0.8635 0.9582 0.7591 0.1036  0.0788  -0.0949 16  GLY   B N   
354  C CA  . GLY   B 7   ? 0.8717 0.9586 0.7622 0.1164  0.0784  -0.0898 16  GLY   B CA  
355  C C   . GLY   B 7   ? 0.8425 0.9261 0.7234 0.1197  0.0737  -0.0882 16  GLY   B C   
356  O O   . GLY   B 7   ? 0.8435 0.9329 0.7236 0.1149  0.0691  -0.0937 16  GLY   B O   
357  N N   . GLU   B 8   ? 0.7620 0.8368 0.6358 0.1279  0.0743  -0.0808 17  GLU   B N   
358  C CA  . GLU   B 8   ? 0.7273 0.7981 0.5910 0.1355  0.0694  -0.0796 17  GLU   B CA  
359  C C   . GLU   B 8   ? 0.7005 0.7689 0.5586 0.1273  0.0656  -0.0798 17  GLU   B C   
360  O O   . GLU   B 8   ? 0.6829 0.7473 0.5398 0.1228  0.0683  -0.0749 17  GLU   B O   
361  C CB  . GLU   B 8   ? 0.7296 0.7933 0.5876 0.1477  0.0722  -0.0712 17  GLU   B CB  
362  C CG  . GLU   B 8   ? 0.7360 0.7965 0.5832 0.1584  0.0671  -0.0710 17  GLU   B CG  
363  C CD  . GLU   B 8   ? 0.7718 0.8279 0.6135 0.1721  0.0702  -0.0628 17  GLU   B CD  
364  O OE1 . GLU   B 8   ? 0.7396 0.7939 0.5854 0.1714  0.0764  -0.0554 17  GLU   B OE1 
365  O OE2 . GLU   B 8   ? 0.8108 0.8659 0.6446 0.1835  0.0663  -0.0638 17  GLU   B OE2 
366  N N   A THR   B 9   ? 0.6948 0.7653 0.5497 0.1255  0.0590  -0.0851 18  THR   B N   
367  N N   B THR   B 9   ? 0.6904 0.7611 0.5456 0.1256  0.0591  -0.0853 18  THR   B N   
368  N N   C THR   B 9   ? 0.6948 0.7653 0.5497 0.1255  0.0590  -0.0851 18  THR   B N   
369  N N   D THR   B 9   ? 0.6904 0.7611 0.5456 0.1256  0.0591  -0.0853 18  THR   B N   
370  C CA  A THR   B 9   ? 0.6939 0.7619 0.5444 0.1163  0.0542  -0.0860 18  THR   B CA  
371  C CA  B THR   B 9   ? 0.6858 0.7547 0.5370 0.1161  0.0540  -0.0867 18  THR   B CA  
372  C CA  C THR   B 9   ? 0.6939 0.7619 0.5444 0.1163  0.0542  -0.0860 18  THR   B CA  
373  C CA  D THR   B 9   ? 0.6858 0.7547 0.5370 0.1161  0.0540  -0.0867 18  THR   B CA  
374  C C   A THR   B 9   ? 0.6943 0.7551 0.5339 0.1244  0.0469  -0.0860 18  THR   B C   
375  C C   B THR   B 9   ? 0.6901 0.7506 0.5296 0.1246  0.0474  -0.0855 18  THR   B C   
376  C C   C THR   B 9   ? 0.6943 0.7551 0.5339 0.1244  0.0469  -0.0860 18  THR   B C   
377  C C   D THR   B 9   ? 0.6901 0.7506 0.5296 0.1246  0.0474  -0.0855 18  THR   B C   
378  O O   A THR   B 9   ? 0.7033 0.7604 0.5385 0.1177  0.0415  -0.0868 18  THR   B O   
379  O O   B THR   B 9   ? 0.6978 0.7532 0.5319 0.1188  0.0432  -0.0848 18  THR   B O   
380  O O   C THR   B 9   ? 0.7033 0.7604 0.5385 0.1177  0.0415  -0.0868 18  THR   B O   
381  O O   D THR   B 9   ? 0.6978 0.7532 0.5319 0.1188  0.0432  -0.0848 18  THR   B O   
382  C CB  A THR   B 9   ? 0.6983 0.7760 0.5566 0.1038  0.0523  -0.0924 18  THR   B CB  
383  C CB  B THR   B 9   ? 0.6835 0.7625 0.5421 0.1056  0.0510  -0.0939 18  THR   B CB  
384  C CB  C THR   B 9   ? 0.6983 0.7760 0.5566 0.1038  0.0523  -0.0924 18  THR   B CB  
385  C CB  D THR   B 9   ? 0.6835 0.7625 0.5421 0.1056  0.0510  -0.0939 18  THR   B CB  
386  O OG1 A THR   B 9   ? 0.6988 0.7839 0.5666 0.1012  0.0586  -0.0938 18  THR   B OG1 
387  O OG1 B THR   B 9   ? 0.6807 0.7651 0.5418 0.1126  0.0485  -0.0987 18  THR   B OG1 
388  O OG1 C THR   B 9   ? 0.6988 0.7839 0.5666 0.1012  0.0586  -0.0938 18  THR   B OG1 
389  O OG1 D THR   B 9   ? 0.6807 0.7651 0.5418 0.1126  0.0485  -0.0987 18  THR   B OG1 
390  C CG2 A THR   B 9   ? 0.7033 0.7790 0.5594 0.0916  0.0498  -0.0916 18  THR   B CG2 
391  C CG2 B THR   B 9   ? 0.6836 0.7705 0.5517 0.0956  0.0568  -0.0951 18  THR   B CG2 
392  C CG2 C THR   B 9   ? 0.7033 0.7790 0.5594 0.0916  0.0498  -0.0916 18  THR   B CG2 
393  C CG2 D THR   B 9   ? 0.6836 0.7705 0.5517 0.0956  0.0568  -0.0951 18  THR   B CG2 
394  N N   . THR   B 10  ? 0.6826 0.7412 0.5176 0.1383  0.0463  -0.0851 19  THR   B N   
395  C CA  . THR   B 10  ? 0.6643 0.7157 0.4875 0.1485  0.0393  -0.0851 19  THR   B CA  
396  C C   . THR   B 10  ? 0.6135 0.6563 0.4279 0.1490  0.0390  -0.0794 19  THR   B C   
397  O O   . THR   B 10  ? 0.5962 0.6379 0.4110 0.1508  0.0459  -0.0728 19  THR   B O   
398  C CB  . THR   B 10  ? 0.6913 0.7425 0.5106 0.1646  0.0402  -0.0838 19  THR   B CB  
399  O OG1 . THR   B 10  ? 0.7516 0.8108 0.5806 0.1643  0.0435  -0.0870 19  THR   B OG1 
400  C CG2 . THR   B 10  ? 0.7143 0.7614 0.5242 0.1736  0.0310  -0.0880 19  THR   B CG2 
401  N N   . ASP   B 11  ? 0.5847 0.6213 0.3910 0.1487  0.0306  -0.0820 20  ASP   B N   
402  C CA  . ASP   B 11  ? 0.5993 0.6269 0.3947 0.1530  0.0286  -0.0775 20  ASP   B CA  
403  C C   . ASP   B 11  ? 0.6227 0.6489 0.4116 0.1685  0.0336  -0.0710 20  ASP   B C   
404  O O   . ASP   B 11  ? 0.6142 0.6437 0.4033 0.1786  0.0350  -0.0714 20  ASP   B O   
405  C CB  . ASP   B 11  ? 0.6241 0.6440 0.4103 0.1546  0.0170  -0.0823 20  ASP   B CB  
406  C CG  . ASP   B 11  ? 0.6444 0.6637 0.4352 0.1385  0.0113  -0.0865 20  ASP   B CG  
407  O OD1 . ASP   B 11  ? 0.6024 0.6289 0.4037 0.1261  0.0165  -0.0864 20  ASP   B OD1 
408  O OD2 . ASP   B 11  ? 0.7086 0.7197 0.4919 0.1391  0.0011  -0.0898 20  ASP   B OD2 
409  N N   . GLY   B 12  ? 0.5956 0.6176 0.3785 0.1706  0.0359  -0.0651 21  GLY   B N   
410  C CA  . GLY   B 12  ? 0.5801 0.6015 0.3557 0.1852  0.0401  -0.0578 21  GLY   B CA  
411  C C   . GLY   B 12  ? 0.5568 0.5804 0.3373 0.1805  0.0485  -0.0500 21  GLY   B C   
412  O O   . GLY   B 12  ? 0.5084 0.5319 0.2952 0.1667  0.0495  -0.0509 21  GLY   B O   
413  N N   . VAL   B 13  ? 0.5546 0.5806 0.3322 0.1919  0.0543  -0.0421 22  VAL   B N   
414  C CA  . VAL   B 13  ? 0.5401 0.5687 0.3217 0.1896  0.0620  -0.0332 22  VAL   B CA  
415  C C   . VAL   B 13  ? 0.5407 0.5751 0.3349 0.1869  0.0703  -0.0288 22  VAL   B C   
416  O O   . VAL   B 13  ? 0.5627 0.5994 0.3579 0.1946  0.0711  -0.0293 22  VAL   B O   
417  C CB  . VAL   B 13  ? 0.5437 0.5718 0.3136 0.2036  0.0622  -0.0268 22  VAL   B CB  
418  C CG1 . VAL   B 13  ? 0.5486 0.5802 0.3123 0.2209  0.0639  -0.0230 22  VAL   B CG1 
419  C CG2 . VAL   B 13  ? 0.5505 0.5817 0.3247 0.1999  0.0688  -0.0183 22  VAL   B CG2 
420  N N   . TYR   B 14  ? 0.5201 0.5563 0.3239 0.1762  0.0755  -0.0253 23  TYR   B N   
421  C CA  . TYR   B 14  ? 0.5155 0.5556 0.3323 0.1716  0.0823  -0.0220 23  TYR   B CA  
422  C C   . TYR   B 14  ? 0.5228 0.5651 0.3444 0.1706  0.0887  -0.0120 23  TYR   B C   
423  O O   . TYR   B 14  ? 0.5374 0.5784 0.3553 0.1673  0.0879  -0.0102 23  TYR   B O   
424  C CB  . TYR   B 14  ? 0.5034 0.5441 0.3298 0.1573  0.0813  -0.0295 23  TYR   B CB  
425  C CG  . TYR   B 14  ? 0.4969 0.5380 0.3222 0.1570  0.0761  -0.0387 23  TYR   B CG  
426  C CD1 . TYR   B 14  ? 0.4935 0.5315 0.3092 0.1591  0.0686  -0.0440 23  TYR   B CD1 
427  C CD2 . TYR   B 14  ? 0.5055 0.5502 0.3400 0.1551  0.0783  -0.0418 23  TYR   B CD2 
428  C CE1 . TYR   B 14  ? 0.5041 0.5432 0.3200 0.1581  0.0634  -0.0522 23  TYR   B CE1 
429  C CE2 . TYR   B 14  ? 0.5115 0.5583 0.3460 0.1545  0.0736  -0.0503 23  TYR   B CE2 
430  C CZ  . TYR   B 14  ? 0.5252 0.5696 0.3509 0.1559  0.0663  -0.0552 23  TYR   B CZ  
431  O OH  . TYR   B 14  ? 0.5594 0.6068 0.3866 0.1549  0.0615  -0.0631 23  TYR   B OH  
432  N N   . ARG   B 15  ? 0.5145 0.5597 0.3446 0.1731  0.0946  -0.0057 24  ARG   B N   
433  C CA  . ARG   B 15  ? 0.5116 0.5594 0.3501 0.1698  0.1008  0.0039  24  ARG   B CA  
434  C C   . ARG   B 15  ? 0.5028 0.5493 0.3528 0.1544  0.1015  -0.0004 24  ARG   B C   
435  O O   . ARG   B 15  ? 0.4818 0.5274 0.3362 0.1498  0.0997  -0.0080 24  ARG   B O   
436  C CB  . ARG   B 15  ? 0.5273 0.5780 0.3707 0.1783  0.1062  0.0133  24  ARG   B CB  
437  C CG  . ARG   B 15  ? 0.5437 0.5967 0.3753 0.1947  0.1059  0.0175  24  ARG   B CG  
438  C CD  . ARG   B 15  ? 0.5635 0.6196 0.4005 0.2023  0.1114  0.0272  24  ARG   B CD  
439  N NE  . ARG   B 15  ? 0.5653 0.6238 0.3898 0.2186  0.1105  0.0300  24  ARG   B NE  
440  C CZ  . ARG   B 15  ? 0.5949 0.6589 0.4115 0.2295  0.1130  0.0388  24  ARG   B CZ  
441  N NH1 . ARG   B 15  ? 0.5877 0.6558 0.4085 0.2260  0.1171  0.0471  24  ARG   B NH1 
442  N NH2 . ARG   B 15  ? 0.6236 0.6894 0.4276 0.2446  0.1113  0.0393  24  ARG   B NH2 
443  N N   . VAL   B 16  ? 0.4956 0.5429 0.3505 0.1479  0.1041  0.0045  25  VAL   B N   
444  C CA  . VAL   B 16  ? 0.5105 0.5570 0.3771 0.1345  0.1053  0.0018  25  VAL   B CA  
445  C C   . VAL   B 16  ? 0.5002 0.5484 0.3780 0.1348  0.1108  0.0116  25  VAL   B C   
446  O O   . VAL   B 16  ? 0.5068 0.5578 0.3842 0.1382  0.1135  0.0206  25  VAL   B O   
447  C CB  . VAL   B 16  ? 0.5240 0.5695 0.3877 0.1255  0.1029  -0.0012 25  VAL   B CB  
448  C CG1 . VAL   B 16  ? 0.5253 0.5705 0.4001 0.1124  0.1038  -0.0048 25  VAL   B CG1 
449  C CG2 . VAL   B 16  ? 0.5255 0.5686 0.3776 0.1259  0.0969  -0.0094 25  VAL   B CG2 
450  N N   . MET   B 17  ? 0.5257 0.5723 0.4133 0.1314  0.1118  0.0096  26  MET   B N   
451  C CA  . MET   B 17  ? 0.5526 0.5990 0.4518 0.1320  0.1159  0.0184  26  MET   B CA  
452  C C   . MET   B 17  ? 0.5683 0.6122 0.4795 0.1195  0.1156  0.0147  26  MET   B C   
453  O O   . MET   B 17  ? 0.5464 0.5891 0.4568 0.1125  0.1124  0.0037  26  MET   B O   
454  C CB  . MET   B 17  ? 0.5656 0.6104 0.4657 0.1395  0.1162  0.0180  26  MET   B CB  
455  C CG  . MET   B 17  ? 0.5880 0.6348 0.4754 0.1521  0.1153  0.0186  26  MET   B CG  
456  S SD  . MET   B 17  ? 0.6022 0.6541 0.4831 0.1637  0.1193  0.0329  26  MET   B SD  
457  C CE  . MET   B 17  ? 0.6321 0.6838 0.5270 0.1645  0.1244  0.0451  26  MET   B CE  
458  N N   . THR   B 18  ? 0.5860 0.6293 0.5081 0.1176  0.1185  0.0237  27  THR   B N   
459  C CA  . THR   B 18  ? 0.6412 0.6808 0.5763 0.1077  0.1179  0.0217  27  THR   B CA  
460  C C   . THR   B 18  ? 0.6769 0.7133 0.6226 0.1109  0.1199  0.0300  27  THR   B C   
461  O O   . THR   B 18  ? 0.6123 0.6515 0.5574 0.1186  0.1232  0.0418  27  THR   B O   
462  C CB  . THR   B 18  ? 0.6178 0.6592 0.5563 0.0995  0.1182  0.0242  27  THR   B CB  
463  O OG1 . THR   B 18  ? 0.6242 0.6616 0.5747 0.0904  0.1166  0.0204  27  THR   B OG1 
464  C CG2 . THR   B 18  ? 0.6281 0.6740 0.5681 0.1040  0.1219  0.0379  27  THR   B CG2 
465  N N   . ARG   B 19  ? 0.7369 0.7679 0.6923 0.1049  0.1176  0.0245  28  ARG   B N   
466  C CA  . ARG   B 19  ? 0.8461 0.8717 0.8139 0.1054  0.1181  0.0319  28  ARG   B CA  
467  C C   . ARG   B 19  ? 0.8378 0.8604 0.8186 0.0952  0.1171  0.0347  28  ARG   B C   
468  O O   . ARG   B 19  ? 0.8322 0.8493 0.8247 0.0940  0.1165  0.0408  28  ARG   B O   
469  C CB  . ARG   B 19  ? 0.8869 0.9073 0.8551 0.1083  0.1154  0.0232  28  ARG   B CB  
470  C CG  . ARG   B 19  ? 0.9558 0.9789 0.9135 0.1196  0.1166  0.0237  28  ARG   B CG  
471  C CD  . ARG   B 19  ? 0.9816 0.9991 0.9433 0.1262  0.1160  0.0259  28  ARG   B CD  
472  N NE  . ARG   B 19  ? 1.0090 1.0292 0.9597 0.1355  0.1156  0.0209  28  ARG   B NE  
473  C CZ  . ARG   B 19  ? 1.0544 1.0761 1.0003 0.1349  0.1126  0.0074  28  ARG   B CZ  
474  N NH1 . ARG   B 19  ? 1.0906 1.1118 1.0407 0.1257  0.1100  -0.0025 28  ARG   B NH1 
475  N NH2 . ARG   B 19  ? 1.0635 1.0878 1.0002 0.1437  0.1120  0.0041  28  ARG   B NH2 
476  N N   . ARG   B 20  ? 0.8589 0.8850 0.8379 0.0884  0.1166  0.0315  29  ARG   B N   
477  C CA  . ARG   B 20  ? 0.9330 0.9567 0.9234 0.0782  0.1148  0.0320  29  ARG   B CA  
478  C C   . ARG   B 20  ? 0.9024 0.9284 0.9022 0.0783  0.1177  0.0478  29  ARG   B C   
479  O O   . ARG   B 20  ? 0.8823 0.9062 0.8938 0.0703  0.1160  0.0506  29  ARG   B O   
480  C CB  . ARG   B 20  ? 0.9809 1.0084 0.9643 0.0721  0.1134  0.0233  29  ARG   B CB  
481  C CG  . ARG   B 20  ? 1.0656 1.0892 1.0569 0.0621  0.1096  0.0156  29  ARG   B CG  
482  C CD  . ARG   B 20  ? 1.1902 1.2186 1.1737 0.0568  0.1090  0.0101  29  ARG   B CD  
483  N NE  . ARG   B 20  ? 1.2713 1.3053 1.2509 0.0595  0.1122  0.0202  29  ARG   B NE  
484  C CZ  . ARG   B 20  ? 1.3054 1.3416 1.2926 0.0556  0.1130  0.0284  29  ARG   B CZ  
485  N NH1 . ARG   B 20  ? 1.3311 1.3635 1.3307 0.0479  0.1104  0.0277  29  ARG   B NH1 
486  N NH2 . ARG   B 20  ? 1.2998 1.3423 1.2822 0.0597  0.1160  0.0370  29  ARG   B NH2 
487  N N   . LEU   B 21  ? 0.8700 0.9012 0.8646 0.0872  0.1219  0.0581  30  LEU   B N   
488  C CA  . LEU   B 21  ? 0.8275 0.8635 0.8305 0.0887  0.1256  0.0747  30  LEU   B CA  
489  C C   . LEU   B 21  ? 0.7749 0.8079 0.7813 0.0959  0.1273  0.0832  30  LEU   B C   
490  O O   . LEU   B 21  ? 0.7526 0.7779 0.7582 0.0973  0.1245  0.0751  30  LEU   B O   
491  C CB  . LEU   B 21  ? 0.8498 0.8961 0.8422 0.0938  0.1292  0.0796  30  LEU   B CB  
492  C CG  . LEU   B 21  ? 0.8783 0.9289 0.8733 0.0861  0.1286  0.0791  30  LEU   B CG  
493  C CD1 . LEU   B 21  ? 0.9112 0.9546 0.9122 0.0751  0.1236  0.0676  30  LEU   B CD1 
494  C CD2 . LEU   B 21  ? 0.8823 0.9393 0.8613 0.0915  0.1297  0.0759  30  LEU   B CD2 
495  N N   . LEU   B 22  ? 0.7659 0.8053 0.7768 0.1001  0.1317  0.0992  31  LEU   B N   
496  C CA  . LEU   B 22  ? 0.7425 0.7801 0.7563 0.1075  0.1339  0.1096  31  LEU   B CA  
497  C C   . LEU   B 22  ? 0.7245 0.7632 0.7220 0.1188  0.1348  0.1036  31  LEU   B C   
498  O O   . LEU   B 22  ? 0.7678 0.8134 0.7524 0.1231  0.1361  0.0994  31  LEU   B O   
499  C CB  . LEU   B 22  ? 0.7343 0.7819 0.7544 0.1099  0.1391  0.1283  31  LEU   B CB  
500  C CG  . LEU   B 22  ? 0.7256 0.7712 0.7530 0.1147  0.1412  0.1418  31  LEU   B CG  
501  C CD1 . LEU   B 22  ? 0.7153 0.7497 0.7610 0.1045  0.1369  0.1440  31  LEU   B CD1 
502  C CD2 . LEU   B 22  ? 0.7132 0.7732 0.7409 0.1209  0.1479  0.1597  31  LEU   B CD2 
503  N N   . GLY   B 23  ? 0.7070 0.7386 0.7050 0.1236  0.1336  0.1029  32  GLY   B N   
504  C CA  . GLY   B 23  ? 0.6659 0.6977 0.6494 0.1340  0.1335  0.0959  32  GLY   B CA  
505  C C   . GLY   B 23  ? 0.6523 0.6854 0.6240 0.1326  0.1309  0.0800  32  GLY   B C   
506  O O   . GLY   B 23  ? 0.6328 0.6623 0.6090 0.1228  0.1275  0.0702  32  GLY   B O   
507  N N   . SER   B 24  ? 0.6310 0.6689 0.5881 0.1425  0.1319  0.0773  33  SER   B N   
508  C CA  . SER   B 24  ? 0.6133 0.6533 0.5580 0.1426  0.1294  0.0642  33  SER   B CA  
509  C C   . SER   B 24  ? 0.5960 0.6445 0.5329 0.1461  0.1321  0.0705  33  SER   B C   
510  O O   . SER   B 24  ? 0.5691 0.6226 0.5007 0.1563  0.1353  0.0799  33  SER   B O   
511  C CB  . SER   B 24  ? 0.6070 0.6456 0.5415 0.1516  0.1277  0.0573  33  SER   B CB  
512  O OG  . SER   B 24  ? 0.6215 0.6528 0.5628 0.1479  0.1246  0.0494  33  SER   B OG  
513  N N   . THR   B 25  ? 0.5776 0.6276 0.5134 0.1384  0.1307  0.0652  34  THR   B N   
514  C CA  . THR   B 25  ? 0.5876 0.6454 0.5174 0.1408  0.1328  0.0711  34  THR   B CA  
515  C C   . THR   B 25  ? 0.5860 0.6438 0.5013 0.1424  0.1293  0.0596  34  THR   B C   
516  O O   . THR   B 25  ? 0.5616 0.6144 0.4771 0.1344  0.1254  0.0474  34  THR   B O   
517  C CB  . THR   B 25  ? 0.5957 0.6551 0.5376 0.1305  0.1339  0.0764  34  THR   B CB  
518  O OG1 . THR   B 25  ? 0.6036 0.6619 0.5601 0.1283  0.1362  0.0869  34  THR   B OG1 
519  C CG2 . THR   B 25  ? 0.5832 0.6515 0.5195 0.1338  0.1362  0.0830  34  THR   B CG2 
520  N N   . GLN   B 26  ? 0.5768 0.6401 0.4799 0.1528  0.1303  0.0633  35  GLN   B N   
521  C CA  . GLN   B 26  ? 0.5718 0.6340 0.4606 0.1550  0.1260  0.0530  35  GLN   B CA  
522  C C   . GLN   B 26  ? 0.5846 0.6489 0.4737 0.1480  0.1255  0.0531  35  GLN   B C   
523  O O   . GLN   B 26  ? 0.5839 0.6550 0.4728 0.1526  0.1288  0.0633  35  GLN   B O   
524  C CB  . GLN   B 26  ? 0.5548 0.6206 0.4292 0.1699  0.1259  0.0553  35  GLN   B CB  
525  C CG  . GLN   B 26  ? 0.5470 0.6098 0.4073 0.1716  0.1201  0.0442  35  GLN   B CG  
526  C CD  . GLN   B 26  ? 0.5459 0.6109 0.3918 0.1869  0.1187  0.0449  35  GLN   B CD  
527  O OE1 . GLN   B 26  ? 0.5295 0.5944 0.3741 0.1944  0.1194  0.0460  35  GLN   B OE1 
528  N NE2 . GLN   B 26  ? 0.5239 0.5904 0.3579 0.1924  0.1161  0.0438  35  GLN   B NE2 
529  N N   . VAL   B 27  ? 0.5616 0.6211 0.4507 0.1377  0.1216  0.0426  36  VAL   B N   
530  C CA  . VAL   B 27  ? 0.5463 0.6069 0.4354 0.1304  0.1205  0.0419  36  VAL   B CA  
531  C C   . VAL   B 27  ? 0.5212 0.5809 0.3943 0.1355  0.1164  0.0361  36  VAL   B C   
532  O O   . VAL   B 27  ? 0.5119 0.5736 0.3811 0.1346  0.1157  0.0380  36  VAL   B O   
533  C CB  . VAL   B 27  ? 0.5643 0.6206 0.4631 0.1162  0.1187  0.0347  36  VAL   B CB  
534  C CG1 . VAL   B 27  ? 0.5861 0.6425 0.5009 0.1114  0.1218  0.0411  36  VAL   B CG1 
535  C CG2 . VAL   B 27  ? 0.5544 0.6056 0.4491 0.1126  0.1148  0.0223  36  VAL   B CG2 
536  N N   . GLY   B 28  ? 0.5120 0.5684 0.3758 0.1409  0.1131  0.0292  37  GLY   B N   
537  C CA  . GLY   B 28  ? 0.4823 0.5372 0.3305 0.1477  0.1085  0.0249  37  GLY   B CA  
538  C C   . GLY   B 28  ? 0.4892 0.5403 0.3296 0.1532  0.1045  0.0173  37  GLY   B C   
539  O O   . GLY   B 28  ? 0.5032 0.5551 0.3487 0.1562  0.1067  0.0183  37  GLY   B O   
540  N N   . VAL   B 29  ? 0.4798 0.5267 0.3087 0.1538  0.0983  0.0098  38  VAL   B N   
541  C CA  . VAL   B 29  ? 0.4761 0.5195 0.2949 0.1607  0.0929  0.0026  38  VAL   B CA  
542  C C   . VAL   B 29  ? 0.4781 0.5158 0.2932 0.1507  0.0863  -0.0071 38  VAL   B C   
543  O O   . VAL   B 29  ? 0.4559 0.4924 0.2720 0.1427  0.0859  -0.0068 38  VAL   B O   
544  C CB  . VAL   B 29  ? 0.5061 0.5506 0.3116 0.1763  0.0913  0.0067  38  VAL   B CB  
545  C CG1 . VAL   B 29  ? 0.5175 0.5576 0.3117 0.1839  0.0844  -0.0009 38  VAL   B CG1 
546  C CG2 . VAL   B 29  ? 0.5047 0.5567 0.3137 0.1862  0.0983  0.0180  38  VAL   B CG2 
547  N N   . GLY   B 30  ? 0.4661 0.5008 0.2772 0.1514  0.0813  -0.0151 39  GLY   B N   
548  C CA  . GLY   B 30  ? 0.4577 0.4877 0.2652 0.1423  0.0746  -0.0238 39  GLY   B CA  
549  C C   . GLY   B 30  ? 0.4602 0.4871 0.2597 0.1485  0.0679  -0.0302 39  GLY   B C   
550  O O   . GLY   B 30  ? 0.4778 0.5066 0.2747 0.1603  0.0690  -0.0284 39  GLY   B O   
551  N N   . VAL   B 31  ? 0.4581 0.4805 0.2542 0.1405  0.0612  -0.0371 40  VAL   B N   
552  C CA  . VAL   B 31  ? 0.4755 0.4937 0.2641 0.1439  0.0528  -0.0440 40  VAL   B CA  
553  C C   . VAL   B 31  ? 0.4855 0.5061 0.2824 0.1312  0.0510  -0.0508 40  VAL   B C   
554  O O   . VAL   B 31  ? 0.4737 0.4948 0.2754 0.1180  0.0516  -0.0518 40  VAL   B O   
555  C CB  . VAL   B 31  ? 0.5011 0.5108 0.2775 0.1457  0.0446  -0.0458 40  VAL   B CB  
556  C CG1 . VAL   B 31  ? 0.5229 0.5276 0.2931 0.1477  0.0350  -0.0533 40  VAL   B CG1 
557  C CG2 . VAL   B 31  ? 0.5079 0.5165 0.2753 0.1591  0.0461  -0.0395 40  VAL   B CG2 
558  N N   . MET   B 32  ? 0.4845 0.5079 0.2833 0.1355  0.0495  -0.0549 41  MET   B N   
559  C CA  . MET   B 32  ? 0.4969 0.5243 0.3030 0.1253  0.0470  -0.0618 41  MET   B CA  
560  C C   . MET   B 32  ? 0.5067 0.5284 0.3047 0.1263  0.0366  -0.0672 41  MET   B C   
561  O O   . MET   B 32  ? 0.5021 0.5204 0.2922 0.1388  0.0324  -0.0681 41  MET   B O   
562  C CB  . MET   B 32  ? 0.5100 0.5444 0.3240 0.1297  0.0514  -0.0632 41  MET   B CB  
563  C CG  . MET   B 32  ? 0.5147 0.5562 0.3383 0.1187  0.0505  -0.0700 41  MET   B CG  
564  S SD  . MET   B 32  ? 0.5272 0.5744 0.3618 0.1029  0.0568  -0.0696 41  MET   B SD  
565  C CE  . MET   B 32  ? 0.5665 0.6154 0.4070 0.1106  0.0657  -0.0638 41  MET   B CE  
566  N N   . GLN   B 33  ? 0.5249 0.5452 0.3243 0.1135  0.0320  -0.0704 42  GLN   B N   
567  C CA  . GLN   B 33  ? 0.5498 0.5640 0.3431 0.1119  0.0212  -0.0753 42  GLN   B CA  
568  C C   . GLN   B 33  ? 0.5592 0.5788 0.3613 0.0956  0.0197  -0.0788 42  GLN   B C   
569  O O   . GLN   B 33  ? 0.5557 0.5780 0.3622 0.0854  0.0245  -0.0764 42  GLN   B O   
570  C CB  . GLN   B 33  ? 0.5632 0.5655 0.3438 0.1160  0.0149  -0.0733 42  GLN   B CB  
571  C CG  . GLN   B 33  ? 0.6029 0.5976 0.3773 0.1160  0.0026  -0.0787 42  GLN   B CG  
572  C CD  . GLN   B 33  ? 0.6445 0.6262 0.4047 0.1237  -0.0049 -0.0777 42  GLN   B CD  
573  O OE1 . GLN   B 33  ? 0.7269 0.7003 0.4834 0.1158  -0.0131 -0.0794 42  GLN   B OE1 
574  N NE2 . GLN   B 33  ? 0.6408 0.6210 0.3932 0.1386  -0.0016 -0.0742 42  GLN   B NE2 
575  N N   . GLU   B 34  ? 0.5892 0.6111 0.3938 0.0935  0.0133  -0.0842 43  GLU   B N   
576  C CA  . GLU   B 34  ? 0.5971 0.6264 0.4107 0.0781  0.0113  -0.0874 43  GLU   B CA  
577  C C   . GLU   B 34  ? 0.5921 0.6334 0.4166 0.0702  0.0216  -0.0864 43  GLU   B C   
578  O O   . GLU   B 34  ? 0.5820 0.6274 0.4109 0.0567  0.0222  -0.0861 43  GLU   B O   
579  C CB  . GLU   B 34  ? 0.6441 0.6643 0.4519 0.0689  0.0040  -0.0862 43  GLU   B CB  
580  C CG  . GLU   B 34  ? 0.6726 0.6809 0.4709 0.0753  -0.0081 -0.0887 43  GLU   B CG  
581  C CD  . GLU   B 34  ? 0.7100 0.7046 0.4986 0.0715  -0.0156 -0.0866 43  GLU   B CD  
582  O OE1 . GLU   B 34  ? 0.7649 0.7602 0.5574 0.0574  -0.0184 -0.0861 43  GLU   B OE1 
583  O OE2 . GLU   B 34  ? 0.7738 0.7575 0.5507 0.0833  -0.0186 -0.0852 43  GLU   B OE2 
584  N N   . GLY   B 35  ? 0.5574 0.6040 0.3860 0.0783  0.0291  -0.0858 44  GLY   B N   
585  C CA  . GLY   B 35  ? 0.5148 0.5724 0.3541 0.0718  0.0376  -0.0860 44  GLY   B CA  
586  C C   . GLY   B 35  ? 0.4914 0.5462 0.3300 0.0671  0.0431  -0.0812 44  GLY   B C   
587  O O   . GLY   B 35  ? 0.4705 0.5330 0.3172 0.0616  0.0496  -0.0815 44  GLY   B O   
588  N N   . VAL   B 36  ? 0.4731 0.5172 0.3024 0.0703  0.0406  -0.0770 45  VAL   B N   
589  C CA  . VAL   B 36  ? 0.4592 0.5002 0.2873 0.0665  0.0452  -0.0722 45  VAL   B CA  
590  C C   . VAL   B 36  ? 0.4460 0.4820 0.2700 0.0792  0.0491  -0.0671 45  VAL   B C   
591  O O   . VAL   B 36  ? 0.4574 0.4872 0.2729 0.0901  0.0448  -0.0663 45  VAL   B O   
592  C CB  . VAL   B 36  ? 0.4757 0.5098 0.2972 0.0578  0.0394  -0.0711 45  VAL   B CB  
593  C CG1 . VAL   B 36  ? 0.4761 0.5062 0.2951 0.0562  0.0435  -0.0660 45  VAL   B CG1 
594  C CG2 . VAL   B 36  ? 0.4828 0.5249 0.3109 0.0435  0.0380  -0.0745 45  VAL   B CG2 
595  N N   . PHE   B 37  ? 0.4270 0.4662 0.2569 0.0779  0.0566  -0.0636 46  PHE   B N   
596  C CA  . PHE   B 37  ? 0.4363 0.4723 0.2640 0.0883  0.0609  -0.0574 46  PHE   B CA  
597  C C   . PHE   B 37  ? 0.4336 0.4639 0.2557 0.0855  0.0605  -0.0528 46  PHE   B C   
598  O O   . PHE   B 37  ? 0.4314 0.4634 0.2574 0.0749  0.0622  -0.0530 46  PHE   B O   
599  C CB  . PHE   B 37  ? 0.4248 0.4665 0.2628 0.0892  0.0686  -0.0555 46  PHE   B CB  
600  C CG  . PHE   B 37  ? 0.4305 0.4696 0.2664 0.1008  0.0723  -0.0484 46  PHE   B CG  
601  C CD1 . PHE   B 37  ? 0.4372 0.4742 0.2664 0.1133  0.0701  -0.0474 46  PHE   B CD1 
602  C CD2 . PHE   B 37  ? 0.4251 0.4648 0.2663 0.0992  0.0780  -0.0427 46  PHE   B CD2 
603  C CE1 . PHE   B 37  ? 0.4473 0.4834 0.2742 0.1245  0.0738  -0.0400 46  PHE   B CE1 
604  C CE2 . PHE   B 37  ? 0.4356 0.4745 0.2759 0.1096  0.0816  -0.0351 46  PHE   B CE2 
605  C CZ  . PHE   B 37  ? 0.4472 0.4848 0.2803 0.1223  0.0799  -0.0335 46  PHE   B CZ  
606  N N   . HIS   B 38  ? 0.4296 0.4544 0.2430 0.0960  0.0588  -0.0488 47  HIS   B N   
607  C CA  . HIS   B 38  ? 0.4373 0.4561 0.2431 0.0958  0.0570  -0.0448 47  HIS   B CA  
608  C C   . HIS   B 38  ? 0.4393 0.4601 0.2465 0.1043  0.0633  -0.0374 47  HIS   B C   
609  O O   . HIS   B 38  ? 0.4398 0.4612 0.2438 0.1166  0.0642  -0.0349 47  HIS   B O   
610  C CB  . HIS   B 38  ? 0.4452 0.4559 0.2385 0.1017  0.0483  -0.0470 47  HIS   B CB  
611  C CG  . HIS   B 38  ? 0.4534 0.4616 0.2456 0.0937  0.0410  -0.0534 47  HIS   B CG  
612  N ND1 . HIS   B 38  ? 0.4679 0.4795 0.2632 0.0957  0.0392  -0.0579 47  HIS   B ND1 
613  C CD2 . HIS   B 38  ? 0.4661 0.4691 0.2547 0.0839  0.0348  -0.0556 47  HIS   B CD2 
614  C CE1 . HIS   B 38  ? 0.4765 0.4864 0.2716 0.0864  0.0326  -0.0627 47  HIS   B CE1 
615  N NE2 . HIS   B 38  ? 0.4784 0.4826 0.2692 0.0788  0.0297  -0.0610 47  HIS   B NE2 
616  N N   . THR   B 39  ? 0.4417 0.4642 0.2538 0.0983  0.0676  -0.0335 48  THR   B N   
617  C CA  . THR   B 39  ? 0.4469 0.4717 0.2602 0.1064  0.0729  -0.0253 48  THR   B CA  
618  C C   . THR   B 39  ? 0.4581 0.4808 0.2687 0.1020  0.0725  -0.0221 48  THR   B C   
619  O O   . THR   B 39  ? 0.4511 0.4696 0.2582 0.0930  0.0678  -0.0263 48  THR   B O   
620  C CB  . THR   B 39  ? 0.4433 0.4743 0.2690 0.1062  0.0800  -0.0226 48  THR   B CB  
621  O OG1 . THR   B 39  ? 0.4498 0.4837 0.2768 0.1155  0.0848  -0.0139 48  THR   B OG1 
622  C CG2 . THR   B 39  ? 0.4484 0.4820 0.2847 0.0932  0.0829  -0.0243 48  THR   B CG2 
623  N N   . MET   B 40  ? 0.4645 0.4912 0.2787 0.1068  0.0777  -0.0145 49  MET   B N   
624  C CA  . MET   B 40  ? 0.4722 0.4988 0.2867 0.1023  0.0785  -0.0109 49  MET   B CA  
625  C C   . MET   B 40  ? 0.4658 0.4964 0.2936 0.0909  0.0832  -0.0105 49  MET   B C   
626  O O   . MET   B 40  ? 0.4593 0.4942 0.2975 0.0909  0.0880  -0.0089 49  MET   B O   
627  C CB  . MET   B 40  ? 0.4833 0.5133 0.2944 0.1139  0.0811  -0.0027 49  MET   B CB  
628  C CG  . MET   B 40  ? 0.5063 0.5341 0.3050 0.1283  0.0774  -0.0028 49  MET   B CG  
629  S SD  . MET   B 40  ? 0.5552 0.5839 0.3430 0.1398  0.0759  0.0029  49  MET   B SD  
630  C CE  . MET   B 40  ? 0.5705 0.5887 0.3496 0.1303  0.0674  -0.0040 49  MET   B CE  
631  N N   A TRP   B 41  ? 0.4633 0.4920 0.2908 0.0816  0.0814  -0.0120 50  TRP   B N   
632  N N   B TRP   B 41  ? 0.4585 0.4872 0.2860 0.0816  0.0814  -0.0120 50  TRP   B N   
633  N N   C TRP   B 41  ? 0.4634 0.4920 0.2908 0.0816  0.0814  -0.0120 50  TRP   B N   
634  N N   D TRP   B 41  ? 0.4575 0.4862 0.2850 0.0816  0.0814  -0.0120 50  TRP   B N   
635  C CA  A TRP   B 41  ? 0.4617 0.4934 0.3003 0.0702  0.0846  -0.0130 50  TRP   B CA  
636  C CA  B TRP   B 41  ? 0.4522 0.4839 0.2908 0.0702  0.0846  -0.0130 50  TRP   B CA  
637  C CA  C TRP   B 41  ? 0.4617 0.4934 0.3003 0.0702  0.0846  -0.0130 50  TRP   B CA  
638  C CA  D TRP   B 41  ? 0.4518 0.4835 0.2904 0.0702  0.0846  -0.0130 50  TRP   B CA  
639  C C   A TRP   B 41  ? 0.4572 0.4945 0.3069 0.0732  0.0907  -0.0057 50  TRP   B C   
640  C C   B TRP   B 41  ? 0.4517 0.4889 0.3014 0.0731  0.0906  -0.0057 50  TRP   B C   
641  C C   C TRP   B 41  ? 0.4572 0.4945 0.3069 0.0732  0.0907  -0.0057 50  TRP   B C   
642  C C   D TRP   B 41  ? 0.4516 0.4888 0.3012 0.0732  0.0906  -0.0057 50  TRP   B C   
643  O O   A TRP   B 41  ? 0.4484 0.4882 0.3092 0.0675  0.0937  -0.0069 50  TRP   B O   
644  O O   B TRP   B 41  ? 0.4444 0.4841 0.3052 0.0673  0.0937  -0.0069 50  TRP   B O   
645  O O   C TRP   B 41  ? 0.4484 0.4882 0.3092 0.0675  0.0937  -0.0069 50  TRP   B O   
646  O O   D TRP   B 41  ? 0.4437 0.4834 0.3045 0.0674  0.0937  -0.0069 50  TRP   B O   
647  C CB  A TRP   B 41  ? 0.4680 0.4967 0.3024 0.0616  0.0813  -0.0147 50  TRP   B CB  
648  C CB  B TRP   B 41  ? 0.4503 0.4790 0.2848 0.0613  0.0812  -0.0151 50  TRP   B CB  
649  C CB  C TRP   B 41  ? 0.4680 0.4968 0.3024 0.0616  0.0813  -0.0147 50  TRP   B CB  
650  C CB  D TRP   B 41  ? 0.4501 0.4788 0.2846 0.0613  0.0812  -0.0151 50  TRP   B CB  
651  C CG  A TRP   B 41  ? 0.4668 0.4983 0.3107 0.0500  0.0834  -0.0177 50  TRP   B CG  
652  C CG  B TRP   B 41  ? 0.4415 0.4737 0.2867 0.0510  0.0842  -0.0164 50  TRP   B CG  
653  C CG  C TRP   B 41  ? 0.4668 0.4983 0.3107 0.0500  0.0834  -0.0177 50  TRP   B CG  
654  C CG  D TRP   B 41  ? 0.4410 0.4732 0.2862 0.0510  0.0842  -0.0164 50  TRP   B CG  
655  C CD1 A TRP   B 41  ? 0.4692 0.5008 0.3139 0.0411  0.0818  -0.0245 50  TRP   B CD1 
656  C CD1 B TRP   B 41  ? 0.4368 0.4727 0.2912 0.0502  0.0881  -0.0113 50  TRP   B CD1 
657  C CD1 C TRP   B 41  ? 0.4693 0.5008 0.3139 0.0411  0.0818  -0.0245 50  TRP   B CD1 
658  C CD1 D TRP   B 41  ? 0.4362 0.4721 0.2906 0.0502  0.0881  -0.0113 50  TRP   B CD1 
659  C CD2 A TRP   B 41  ? 0.4674 0.5028 0.3218 0.0466  0.0874  -0.0141 50  TRP   B CD2 
660  C CD2 B TRP   B 41  ? 0.4389 0.4720 0.2875 0.0408  0.0835  -0.0232 50  TRP   B CD2 
661  C CD2 C TRP   B 41  ? 0.4674 0.5028 0.3219 0.0466  0.0874  -0.0141 50  TRP   B CD2 
662  C CD2 D TRP   B 41  ? 0.4389 0.4720 0.2875 0.0408  0.0835  -0.0232 50  TRP   B CD2 
663  N NE1 A TRP   B 41  ? 0.4697 0.5048 0.3234 0.0331  0.0844  -0.0259 50  TRP   B NE1 
664  N NE1 B TRP   B 41  ? 0.4307 0.4684 0.2933 0.0403  0.0892  -0.0152 50  TRP   B NE1 
665  N NE1 C TRP   B 41  ? 0.4697 0.5048 0.3234 0.0331  0.0844  -0.0259 50  TRP   B NE1 
666  N NE1 D TRP   B 41  ? 0.4296 0.4673 0.2922 0.0404  0.0892  -0.0152 50  TRP   B NE1 
667  C CE2 A TRP   B 41  ? 0.4682 0.5050 0.3284 0.0361  0.0875  -0.0198 50  TRP   B CE2 
668  C CE2 B TRP   B 41  ? 0.4334 0.4699 0.2922 0.0348  0.0867  -0.0225 50  TRP   B CE2 
669  C CE2 C TRP   B 41  ? 0.4682 0.5050 0.3283 0.0361  0.0875  -0.0198 50  TRP   B CE2 
670  C CE2 D TRP   B 41  ? 0.4332 0.4698 0.2921 0.0348  0.0867  -0.0225 50  TRP   B CE2 
671  C CE3 A TRP   B 41  ? 0.4761 0.5146 0.3360 0.0513  0.0906  -0.0064 50  TRP   B CE3 
672  C CE3 B TRP   B 41  ? 0.4421 0.4742 0.2864 0.0361  0.0804  -0.0296 50  TRP   B CE3 
673  C CE3 C TRP   B 41  ? 0.4760 0.5145 0.3360 0.0513  0.0906  -0.0064 50  TRP   B CE3 
674  C CE3 D TRP   B 41  ? 0.4429 0.4750 0.2871 0.0361  0.0804  -0.0296 50  TRP   B CE3 
675  C CZ2 A TRP   B 41  ? 0.4716 0.5113 0.3420 0.0306  0.0900  -0.0188 50  TRP   B CZ2 
676  C CZ2 B TRP   B 41  ? 0.4306 0.4696 0.2942 0.0253  0.0868  -0.0285 50  TRP   B CZ2 
677  C CZ2 C TRP   B 41  ? 0.4716 0.5112 0.3419 0.0306  0.0900  -0.0188 50  TRP   B CZ2 
678  C CZ2 D TRP   B 41  ? 0.4306 0.4695 0.2941 0.0254  0.0869  -0.0285 50  TRP   B CZ2 
679  C CZ3 A TRP   B 41  ? 0.4725 0.5142 0.3439 0.0449  0.0931  -0.0049 50  TRP   B CZ3 
680  C CZ3 B TRP   B 41  ? 0.4364 0.4722 0.2859 0.0263  0.0811  -0.0348 50  TRP   B CZ3 
681  C CZ3 C TRP   B 41  ? 0.4725 0.5141 0.3438 0.0449  0.0931  -0.0049 50  TRP   B CZ3 
682  C CZ3 D TRP   B 41  ? 0.4363 0.4721 0.2859 0.0262  0.0811  -0.0348 50  TRP   B CZ3 
683  C CH2 A TRP   B 41  ? 0.4730 0.5144 0.3491 0.0349  0.0925  -0.0114 50  TRP   B CH2 
684  C CH2 B TRP   B 41  ? 0.4320 0.4712 0.2905 0.0214  0.0843  -0.0346 50  TRP   B CH2 
685  C CH2 C TRP   B 41  ? 0.4729 0.5144 0.3491 0.0349  0.0925  -0.0114 50  TRP   B CH2 
686  C CH2 D TRP   B 41  ? 0.4320 0.4711 0.2905 0.0214  0.0843  -0.0346 50  TRP   B CH2 
687  N N   . HIS   B 42  ? 0.4554 0.4948 0.3024 0.0819  0.0921  0.0016  51  HIS   B N   
688  C CA  . HIS   B 42  ? 0.4675 0.5132 0.3261 0.0840  0.0979  0.0101  51  HIS   B CA  
689  C C   . HIS   B 42  ? 0.4752 0.5233 0.3411 0.0889  0.1017  0.0125  51  HIS   B C   
690  O O   . HIS   B 42  ? 0.4768 0.5288 0.3549 0.0873  0.1059  0.0182  51  HIS   B O   
691  C CB  . HIS   B 42  ? 0.4684 0.5180 0.3229 0.0922  0.0989  0.0180  51  HIS   B CB  
692  C CG  . HIS   B 42  ? 0.4876 0.5392 0.3340 0.1061  0.0994  0.0219  51  HIS   B CG  
693  N ND1 . HIS   B 42  ? 0.4936 0.5406 0.3246 0.1131  0.0942  0.0183  51  HIS   B ND1 
694  C CD2 . HIS   B 42  ? 0.4990 0.5568 0.3496 0.1153  0.1042  0.0298  51  HIS   B CD2 
695  C CE1 . HIS   B 42  ? 0.5005 0.5508 0.3264 0.1262  0.0956  0.0228  51  HIS   B CE1 
696  N NE2 . HIS   B 42  ? 0.4952 0.5528 0.3328 0.1278  0.1021  0.0301  51  HIS   B NE2 
697  N N   . VAL   B 43  ? 0.4727 0.5182 0.3323 0.0936  0.0998  0.0079  52  VAL   B N   
698  C CA  . VAL   B 43  ? 0.4777 0.5249 0.3434 0.0984  0.1029  0.0095  52  VAL   B CA  
699  C C   . VAL   B 43  ? 0.4764 0.5225 0.3529 0.0881  0.1035  0.0039  52  VAL   B C   
700  O O   . VAL   B 43  ? 0.4898 0.5379 0.3776 0.0876  0.1072  0.0086  52  VAL   B O   
701  C CB  . VAL   B 43  ? 0.4983 0.5434 0.3529 0.1078  0.1001  0.0062  52  VAL   B CB  
702  C CG1 . VAL   B 43  ? 0.5191 0.5650 0.3790 0.1116  0.1022  0.0055  52  VAL   B CG1 
703  C CG2 . VAL   B 43  ? 0.5030 0.5499 0.3478 0.1200  0.0999  0.0124  52  VAL   B CG2 
704  N N   . THR   B 44  ? 0.4418 0.4853 0.3152 0.0799  0.0999  -0.0051 53  THR   B N   
705  C CA  . THR   B 44  ? 0.4593 0.5030 0.3413 0.0719  0.1002  -0.0117 53  THR   B CA  
706  C C   . THR   B 44  ? 0.4782 0.5222 0.3662 0.0611  0.1001  -0.0136 53  THR   B C   
707  O O   . THR   B 44  ? 0.4911 0.5358 0.3881 0.0559  0.1011  -0.0172 53  THR   B O   
708  C CB  . THR   B 44  ? 0.4469 0.4898 0.3225 0.0705  0.0967  -0.0205 53  THR   B CB  
709  O OG1 . THR   B 44  ? 0.4435 0.4847 0.3110 0.0646  0.0928  -0.0243 53  THR   B OG1 
710  C CG2 . THR   B 44  ? 0.4405 0.4829 0.3100 0.0817  0.0961  -0.0191 53  THR   B CG2 
711  N N   . LYS   B 45  ? 0.5053 0.5487 0.3885 0.0588  0.0988  -0.0110 54  LYS   B N   
712  C CA  . LYS   B 45  ? 0.5519 0.5953 0.4376 0.0484  0.0976  -0.0139 54  LYS   B CA  
713  C C   . LYS   B 45  ? 0.5370 0.5804 0.4207 0.0405  0.0952  -0.0235 54  LYS   B C   
714  O O   . LYS   B 45  ? 0.5313 0.5760 0.4204 0.0323  0.0951  -0.0271 54  LYS   B O   
715  C CB  . LYS   B 45  ? 0.6086 0.6537 0.5077 0.0449  0.1004  -0.0102 54  LYS   B CB  
716  C CG  . LYS   B 45  ? 0.6732 0.7203 0.5780 0.0518  0.1036  0.0002  54  LYS   B CG  
717  C CD  . LYS   B 45  ? 0.7491 0.7976 0.6468 0.0553  0.1032  0.0058  54  LYS   B CD  
718  C CE  . LYS   B 45  ? 0.8099 0.8630 0.7148 0.0618  0.1070  0.0169  54  LYS   B CE  
719  N NZ  . LYS   B 45  ? 0.8569 0.9125 0.7517 0.0702  0.1069  0.0223  54  LYS   B NZ  
720  N N   . GLY   B 46  ? 0.5304 0.5732 0.4070 0.0430  0.0931  -0.0277 55  GLY   B N   
721  C CA  . GLY   B 46  ? 0.5208 0.5656 0.3958 0.0355  0.0910  -0.0361 55  GLY   B CA  
722  C C   . GLY   B 46  ? 0.5316 0.5802 0.4157 0.0346  0.0931  -0.0408 55  GLY   B C   
723  O O   . GLY   B 46  ? 0.5472 0.5993 0.4307 0.0289  0.0918  -0.0476 55  GLY   B O   
724  N N   . ALA   B 47  ? 0.5402 0.5884 0.4322 0.0404  0.0959  -0.0373 56  ALA   B N   
725  C CA  . ALA   B 47  ? 0.5384 0.5890 0.4389 0.0406  0.0973  -0.0421 56  ALA   B CA  
726  C C   . ALA   B 47  ? 0.5223 0.5752 0.4186 0.0446  0.0961  -0.0468 56  ALA   B C   
727  O O   . ALA   B 47  ? 0.5189 0.5700 0.4077 0.0504  0.0948  -0.0441 56  ALA   B O   
728  C CB  . ALA   B 47  ? 0.5573 0.6054 0.4670 0.0458  0.1000  -0.0359 56  ALA   B CB  
729  N N   . ALA   B 48  ? 0.4988 0.5556 0.4005 0.0430  0.0963  -0.0534 57  ALA   B N   
730  C CA  . ALA   B 48  ? 0.5140 0.5739 0.4142 0.0477  0.0955  -0.0578 57  ALA   B CA  
731  C C   . ALA   B 48  ? 0.5174 0.5735 0.4194 0.0583  0.0970  -0.0524 57  ALA   B C   
732  O O   . ALA   B 48  ? 0.5207 0.5729 0.4278 0.0609  0.0992  -0.0460 57  ALA   B O   
733  C CB  . ALA   B 48  ? 0.5361 0.6024 0.4421 0.0437  0.0955  -0.0664 57  ALA   B CB  
734  N N   . LEU   B 49  ? 0.5051 0.5629 0.4030 0.0641  0.0956  -0.0548 58  LEU   B N   
735  C CA  . LEU   B 49  ? 0.5094 0.5644 0.4067 0.0751  0.0965  -0.0502 58  LEU   B CA  
736  C C   . LEU   B 49  ? 0.5450 0.6038 0.4457 0.0783  0.0959  -0.0568 58  LEU   B C   
737  O O   . LEU   B 49  ? 0.5798 0.6446 0.4803 0.0730  0.0940  -0.0647 58  LEU   B O   
738  C CB  . LEU   B 49  ? 0.4997 0.5528 0.3861 0.0804  0.0942  -0.0473 58  LEU   B CB  
739  C CG  . LEU   B 49  ? 0.4839 0.5336 0.3649 0.0784  0.0940  -0.0416 58  LEU   B CG  
740  C CD1 . LEU   B 49  ? 0.4845 0.5320 0.3540 0.0838  0.0903  -0.0409 58  LEU   B CD1 
741  C CD2 . LEU   B 49  ? 0.4974 0.5446 0.3833 0.0824  0.0979  -0.0326 58  LEU   B CD2 
742  N N   . ARG   B 50  ? 0.5641 0.6202 0.4679 0.0871  0.0974  -0.0532 59  ARG   B N   
743  C CA  . ARG   B 50  ? 0.6028 0.6616 0.5088 0.0926  0.0966  -0.0585 59  ARG   B CA  
744  C C   . ARG   B 50  ? 0.5955 0.6535 0.4934 0.1021  0.0951  -0.0559 59  ARG   B C   
745  O O   . ARG   B 50  ? 0.5781 0.6319 0.4711 0.1070  0.0961  -0.0479 59  ARG   B O   
746  C CB  . ARG   B 50  ? 0.6617 0.7167 0.5770 0.0954  0.0989  -0.0559 59  ARG   B CB  
747  C CG  . ARG   B 50  ? 0.7601 0.8167 0.6785 0.1019  0.0980  -0.0609 59  ARG   B CG  
748  C CD  . ARG   B 50  ? 0.7989 0.8514 0.7274 0.1015  0.0990  -0.0608 59  ARG   B CD  
749  N NE  . ARG   B 50  ? 0.8337 0.8792 0.7655 0.1007  0.1012  -0.0506 59  ARG   B NE  
750  C CZ  . ARG   B 50  ? 0.8606 0.9013 0.7923 0.1083  0.1031  -0.0407 59  ARG   B CZ  
751  N NH1 . ARG   B 50  ? 0.8463 0.8874 0.7736 0.1178  0.1028  -0.0398 59  ARG   B NH1 
752  N NH2 . ARG   B 50  ? 0.9230 0.9593 0.8591 0.1063  0.1051  -0.0313 59  ARG   B NH2 
753  N N   . SER   B 51  ? 0.6018 0.6647 0.4977 0.1040  0.0924  -0.0630 60  SER   B N   
754  C CA  . SER   B 51  ? 0.6328 0.6953 0.5228 0.1145  0.0904  -0.0625 60  SER   B CA  
755  C C   . SER   B 51  ? 0.6806 0.7470 0.5762 0.1187  0.0900  -0.0684 60  SER   B C   
756  O O   . SER   B 51  ? 0.6827 0.7564 0.5807 0.1134  0.0880  -0.0769 60  SER   B O   
757  C CB  . SER   B 51  ? 0.6109 0.6758 0.4932 0.1119  0.0860  -0.0663 60  SER   B CB  
758  O OG  . SER   B 51  ? 0.6067 0.6708 0.4830 0.1222  0.0833  -0.0663 60  SER   B OG  
759  N N   . GLY   B 52  ? 0.7394 0.8018 0.6374 0.1278  0.0919  -0.0640 61  GLY   B N   
760  C CA  . GLY   B 52  ? 0.7800 0.8450 0.6841 0.1315  0.0915  -0.0698 61  GLY   B CA  
761  C C   . GLY   B 52  ? 0.8122 0.8801 0.7249 0.1227  0.0924  -0.0753 61  GLY   B C   
762  O O   . GLY   B 52  ? 0.8559 0.9187 0.7726 0.1184  0.0947  -0.0706 61  GLY   B O   
763  N N   . GLU   B 53  ? 0.8455 0.9219 0.7610 0.1200  0.0905  -0.0852 62  GLU   B N   
764  C CA  . GLU   B 53  ? 0.8795 0.9608 0.8022 0.1123  0.0910  -0.0918 62  GLU   B CA  
765  C C   . GLU   B 53  ? 0.8505 0.9379 0.7709 0.1011  0.0907  -0.0944 62  GLU   B C   
766  O O   . GLU   B 53  ? 0.8086 0.8998 0.7337 0.0943  0.0915  -0.0988 62  GLU   B O   
767  C CB  . GLU   B 53  ? 0.9472 1.0368 0.8739 0.1160  0.0894  -0.1011 62  GLU   B CB  
768  C CG  . GLU   B 53  ? 1.0277 1.1116 0.9608 0.1222  0.0898  -0.1017 62  GLU   B CG  
769  C CD  . GLU   B 53  ? 1.1147 1.2078 1.0514 0.1264  0.0879  -0.1117 62  GLU   B CD  
770  O OE1 . GLU   B 53  ? 1.1008 1.2000 1.0342 0.1310  0.0861  -0.1142 62  GLU   B OE1 
771  O OE2 . GLU   B 53  ? 1.2000 1.2947 1.1426 0.1252  0.0877  -0.1176 62  GLU   B OE2 
772  N N   . GLY   B 54  ? 0.8005 0.8884 0.7136 0.0998  0.0891  -0.0919 63  GLY   B N   
773  C CA  . GLY   B 54  ? 0.7745 0.8675 0.6845 0.0893  0.0880  -0.0939 63  GLY   B CA  
774  C C   . GLY   B 54  ? 0.7624 0.8487 0.6710 0.0835  0.0898  -0.0879 63  GLY   B C   
775  O O   . GLY   B 54  ? 0.7413 0.8187 0.6495 0.0886  0.0916  -0.0805 63  GLY   B O   
776  N N   . ARG   B 55  ? 0.7280 0.8194 0.6367 0.0732  0.0897  -0.0907 64  ARG   B N   
777  C CA  . ARG   B 55  ? 0.6862 0.7723 0.5931 0.0667  0.0909  -0.0858 64  ARG   B CA  
778  C C   . ARG   B 55  ? 0.6546 0.7400 0.5530 0.0622  0.0882  -0.0836 64  ARG   B C   
779  O O   . ARG   B 55  ? 0.6574 0.7496 0.5537 0.0590  0.0855  -0.0880 64  ARG   B O   
780  C CB  . ARG   B 55  ? 0.6954 0.7864 0.6083 0.0594  0.0925  -0.0906 64  ARG   B CB  
781  C CG  . ARG   B 55  ? 0.7312 0.8163 0.6439 0.0538  0.0938  -0.0859 64  ARG   B CG  
782  C CD  . ARG   B 55  ? 0.7636 0.8559 0.6794 0.0452  0.0942  -0.0920 64  ARG   B CD  
783  N NE  . ARG   B 55  ? 0.8060 0.8939 0.7210 0.0389  0.0948  -0.0885 64  ARG   B NE  
784  C CZ  . ARG   B 55  ? 0.8291 0.9133 0.7499 0.0378  0.0958  -0.0884 64  ARG   B CZ  
785  N NH1 . ARG   B 55  ? 0.8253 0.9083 0.7532 0.0428  0.0961  -0.0916 64  ARG   B NH1 
786  N NH2 . ARG   B 55  ? 0.8232 0.9043 0.7425 0.0318  0.0959  -0.0853 64  ARG   B NH2 
787  N N   . LEU   B 56  ? 0.5870 0.6643 0.4808 0.0626  0.0885  -0.0766 65  LEU   B N   
788  C CA  . LEU   B 56  ? 0.5711 0.6460 0.4564 0.0584  0.0854  -0.0745 65  LEU   B CA  
789  C C   . LEU   B 56  ? 0.5366 0.6108 0.4226 0.0493  0.0868  -0.0731 65  LEU   B C   
790  O O   . LEU   B 56  ? 0.5258 0.5949 0.4145 0.0513  0.0895  -0.0682 65  LEU   B O   
791  C CB  . LEU   B 56  ? 0.5794 0.6459 0.4578 0.0675  0.0844  -0.0677 65  LEU   B CB  
792  C CG  . LEU   B 56  ? 0.6059 0.6718 0.4821 0.0781  0.0828  -0.0681 65  LEU   B CG  
793  C CD1 . LEU   B 56  ? 0.6273 0.6861 0.4934 0.0850  0.0801  -0.0628 65  LEU   B CD1 
794  C CD2 . LEU   B 56  ? 0.6352 0.7085 0.5123 0.0756  0.0794  -0.0757 65  LEU   B CD2 
795  N N   . ASP   B 57  ? 0.5058 0.5855 0.3901 0.0398  0.0850  -0.0767 66  ASP   B N   
796  C CA  . ASP   B 57  ? 0.4988 0.5779 0.3825 0.0312  0.0858  -0.0754 66  ASP   B CA  
797  C C   . ASP   B 57  ? 0.4669 0.5389 0.3414 0.0291  0.0827  -0.0705 66  ASP   B C   
798  O O   . ASP   B 57  ? 0.4478 0.5190 0.3164 0.0287  0.0787  -0.0711 66  ASP   B O   
799  C CB  . ASP   B 57  ? 0.5564 0.6463 0.4430 0.0222  0.0859  -0.0818 66  ASP   B CB  
800  C CG  . ASP   B 57  ? 0.6104 0.7071 0.5057 0.0248  0.0889  -0.0873 66  ASP   B CG  
801  O OD1 . ASP   B 57  ? 0.6593 0.7506 0.5590 0.0295  0.0911  -0.0854 66  ASP   B OD1 
802  O OD2 . ASP   B 57  ? 0.6269 0.7342 0.5248 0.0223  0.0885  -0.0931 66  ASP   B OD2 
803  N N   . PRO   B 58  ? 0.4522 0.5190 0.3253 0.0270  0.0839  -0.0661 67  PRO   B N   
804  C CA  . PRO   B 58  ? 0.4473 0.5077 0.3115 0.0246  0.0806  -0.0621 67  PRO   B CA  
805  C C   . PRO   B 58  ? 0.4469 0.5113 0.3070 0.0149  0.0770  -0.0656 67  PRO   B C   
806  O O   . PRO   B 58  ? 0.4504 0.5232 0.3152 0.0082  0.0786  -0.0698 67  PRO   B O   
807  C CB  . PRO   B 58  ? 0.4475 0.5048 0.3138 0.0228  0.0833  -0.0581 67  PRO   B CB  
808  C CG  . PRO   B 58  ? 0.4619 0.5257 0.3378 0.0195  0.0868  -0.0623 67  PRO   B CG  
809  C CD  . PRO   B 58  ? 0.4570 0.5243 0.3374 0.0256  0.0877  -0.0655 67  PRO   B CD  
810  N N   . TYR   B 59  ? 0.4299 0.4887 0.2816 0.0146  0.0719  -0.0638 68  TYR   B N   
811  C CA  . TYR   B 59  ? 0.4260 0.4871 0.2737 0.0048  0.0677  -0.0657 68  TYR   B CA  
812  C C   . TYR   B 59  ? 0.4308 0.4836 0.2704 0.0006  0.0647  -0.0615 68  TYR   B C   
813  O O   . TYR   B 59  ? 0.4516 0.5073 0.2896 -0.0094 0.0633  -0.0620 68  TYR   B O   
814  C CB  . TYR   B 59  ? 0.4330 0.4934 0.2781 0.0076  0.0628  -0.0675 68  TYR   B CB  
815  C CG  . TYR   B 59  ? 0.4349 0.4981 0.2775 -0.0024 0.0578  -0.0689 68  TYR   B CG  
816  C CD1 . TYR   B 59  ? 0.4455 0.4986 0.2791 -0.0055 0.0519  -0.0656 68  TYR   B CD1 
817  C CD2 . TYR   B 59  ? 0.4282 0.5038 0.2775 -0.0081 0.0585  -0.0731 68  TYR   B CD2 
818  C CE1 . TYR   B 59  ? 0.4554 0.5101 0.2870 -0.0154 0.0467  -0.0659 68  TYR   B CE1 
819  C CE2 . TYR   B 59  ? 0.4439 0.5228 0.2917 -0.0180 0.0539  -0.0732 68  TYR   B CE2 
820  C CZ  . TYR   B 59  ? 0.4589 0.5268 0.2980 -0.0221 0.0478  -0.0693 68  TYR   B CZ  
821  O OH  . TYR   B 59  ? 0.4691 0.5389 0.3068 -0.0325 0.0425  -0.0683 68  TYR   B OH  
822  N N   . TRP   B 60  ? 0.4230 0.4660 0.2565 0.0085  0.0627  -0.0575 69  TRP   B N   
823  C CA  . TRP   B 60  ? 0.4340 0.4675 0.2584 0.0076  0.0590  -0.0534 69  TRP   B CA  
824  C C   . TRP   B 60  ? 0.4348 0.4639 0.2587 0.0170  0.0619  -0.0490 69  TRP   B C   
825  O O   . TRP   B 60  ? 0.4417 0.4700 0.2665 0.0271  0.0631  -0.0480 69  TRP   B O   
826  C CB  . TRP   B 60  ? 0.4412 0.4665 0.2563 0.0082  0.0509  -0.0533 69  TRP   B CB  
827  C CG  . TRP   B 60  ? 0.4517 0.4665 0.2572 0.0093  0.0469  -0.0494 69  TRP   B CG  
828  C CD1 . TRP   B 60  ? 0.4615 0.4736 0.2631 0.0001  0.0448  -0.0479 69  TRP   B CD1 
829  C CD2 . TRP   B 60  ? 0.4473 0.4539 0.2460 0.0209  0.0451  -0.0463 69  TRP   B CD2 
830  N NE1 . TRP   B 60  ? 0.4654 0.4672 0.2580 0.0056  0.0411  -0.0444 69  TRP   B NE1 
831  C CE2 . TRP   B 60  ? 0.4595 0.4585 0.2503 0.0185  0.0414  -0.0435 69  TRP   B CE2 
832  C CE3 . TRP   B 60  ? 0.4573 0.4629 0.2553 0.0338  0.0459  -0.0456 69  TRP   B CE3 
833  C CZ2 . TRP   B 60  ? 0.4564 0.4475 0.2391 0.0286  0.0389  -0.0403 69  TRP   B CZ2 
834  C CZ3 . TRP   B 60  ? 0.4545 0.4530 0.2444 0.0437  0.0438  -0.0420 69  TRP   B CZ3 
835  C CH2 . TRP   B 60  ? 0.4669 0.4584 0.2493 0.0414  0.0402  -0.0397 69  TRP   B CH2 
836  N N   . GLY   B 61  ? 0.4407 0.4669 0.2625 0.0142  0.0625  -0.0458 70  GLY   B N   
837  C CA  . GLY   B 61  ? 0.4495 0.4715 0.2693 0.0232  0.0641  -0.0407 70  GLY   B CA  
838  C C   . GLY   B 61  ? 0.4479 0.4651 0.2622 0.0198  0.0621  -0.0377 70  GLY   B C   
839  O O   . GLY   B 61  ? 0.4500 0.4683 0.2638 0.0092  0.0609  -0.0395 70  GLY   B O   
840  N N   . ASP   B 62  ? 0.4638 0.4775 0.2748 0.0284  0.0623  -0.0331 71  ASP   B N   
841  C CA  . ASP   B 62  ? 0.4776 0.4863 0.2820 0.0277  0.0598  -0.0298 71  ASP   B CA  
842  C C   . ASP   B 62  ? 0.4626 0.4736 0.2701 0.0376  0.0638  -0.0243 71  ASP   B C   
843  O O   . ASP   B 62  ? 0.4826 0.4919 0.2857 0.0485  0.0629  -0.0223 71  ASP   B O   
844  C CB  . ASP   B 62  ? 0.5059 0.5048 0.2972 0.0283  0.0516  -0.0306 71  ASP   B CB  
845  C CG  . ASP   B 62  ? 0.5446 0.5382 0.3292 0.0265  0.0486  -0.0280 71  ASP   B CG  
846  O OD1 . ASP   B 62  ? 0.5555 0.5497 0.3396 0.0337  0.0504  -0.0241 71  ASP   B OD1 
847  O OD2 . ASP   B 62  ? 0.6446 0.6347 0.4252 0.0170  0.0449  -0.0296 71  ASP   B OD2 
848  N N   . VAL   B 63  ? 0.4543 0.4698 0.2692 0.0340  0.0678  -0.0218 72  VAL   B N   
849  C CA  . VAL   B 63  ? 0.4598 0.4794 0.2800 0.0417  0.0720  -0.0155 72  VAL   B CA  
850  C C   . VAL   B 63  ? 0.4738 0.4886 0.2827 0.0499  0.0680  -0.0122 72  VAL   B C   
851  O O   . VAL   B 63  ? 0.4711 0.4892 0.2806 0.0606  0.0704  -0.0071 72  VAL   B O   
852  C CB  . VAL   B 63  ? 0.4573 0.4821 0.2880 0.0346  0.0758  -0.0141 72  VAL   B CB  
853  C CG1 . VAL   B 63  ? 0.4676 0.4957 0.3015 0.0406  0.0780  -0.0072 72  VAL   B CG1 
854  C CG2 . VAL   B 63  ? 0.4531 0.4831 0.2962 0.0311  0.0804  -0.0161 72  VAL   B CG2 
855  N N   . LYS   B 64  ? 0.4935 0.5007 0.2916 0.0465  0.0616  -0.0147 73  LYS   B N   
856  C CA  . LYS   B 64  ? 0.5074 0.5101 0.2951 0.0553  0.0576  -0.0115 73  LYS   B CA  
857  C C   . LYS   B 64  ? 0.5145 0.5129 0.2930 0.0672  0.0541  -0.0119 73  LYS   B C   
858  O O   . LYS   B 64  ? 0.5067 0.5068 0.2812 0.0791  0.0545  -0.0079 73  LYS   B O   
859  C CB  . LYS   B 64  ? 0.5117 0.5064 0.2902 0.0484  0.0513  -0.0136 73  LYS   B CB  
860  C CG  . LYS   B 64  ? 0.5329 0.5227 0.3004 0.0586  0.0467  -0.0108 73  LYS   B CG  
861  C CD  . LYS   B 64  ? 0.5494 0.5326 0.3098 0.0525  0.0415  -0.0116 73  LYS   B CD  
862  C CE  . LYS   B 64  ? 0.5719 0.5503 0.3211 0.0638  0.0366  -0.0093 73  LYS   B CE  
863  N NZ  . LYS   B 64  ? 0.5994 0.5688 0.3401 0.0573  0.0301  -0.0107 73  LYS   B NZ  
864  N N   . GLN   B 65  ? 0.5354 0.5289 0.3107 0.0640  0.0505  -0.0168 74  GLN   B N   
865  C CA  . GLN   B 65  ? 0.5427 0.5324 0.3112 0.0738  0.0470  -0.0186 74  GLN   B CA  
866  C C   . GLN   B 65  ? 0.5228 0.5214 0.2994 0.0820  0.0541  -0.0155 74  GLN   B C   
867  O O   . GLN   B 65  ? 0.4972 0.4941 0.2670 0.0939  0.0519  -0.0154 74  GLN   B O   
868  C CB  . GLN   B 65  ? 0.5656 0.5500 0.3322 0.0657  0.0422  -0.0245 74  GLN   B CB  
869  C CG  . GLN   B 65  ? 0.5989 0.5730 0.3562 0.0582  0.0340  -0.0269 74  GLN   B CG  
870  C CD  . GLN   B 65  ? 0.6305 0.5997 0.3858 0.0518  0.0285  -0.0318 74  GLN   B CD  
871  O OE1 . GLN   B 65  ? 0.7003 0.6672 0.4526 0.0589  0.0254  -0.0340 74  GLN   B OE1 
872  N NE2 . GLN   B 65  ? 0.6707 0.6393 0.4280 0.0381  0.0272  -0.0333 74  GLN   B NE2 
873  N N   . ASP   B 66  ? 0.4956 0.5025 0.2855 0.0761  0.0614  -0.0134 75  ASP   B N   
874  C CA  . ASP   B 66  ? 0.4902 0.5055 0.2908 0.0804  0.0686  -0.0102 75  ASP   B CA  
875  C C   . ASP   B 66  ? 0.4802 0.4939 0.2795 0.0830  0.0671  -0.0145 75  ASP   B C   
876  O O   . ASP   B 66  ? 0.4753 0.4924 0.2749 0.0938  0.0697  -0.0114 75  ASP   B O   
877  C CB  . ASP   B 66  ? 0.4976 0.5183 0.2981 0.0929  0.0722  -0.0027 75  ASP   B CB  
878  C CG  . ASP   B 66  ? 0.4850 0.5143 0.2977 0.0960  0.0797  0.0019  75  ASP   B CG  
879  O OD1 . ASP   B 66  ? 0.4549 0.4867 0.2789 0.0867  0.0831  0.0007  75  ASP   B OD1 
880  O OD2 . ASP   B 66  ? 0.5209 0.5541 0.3310 0.1085  0.0818  0.0072  75  ASP   B OD2 
881  N N   . LEU   B 67  ? 0.4668 0.4768 0.2651 0.0737  0.0633  -0.0209 76  LEU   B N   
882  C CA  . LEU   B 67  ? 0.4587 0.4679 0.2567 0.0745  0.0613  -0.0257 76  LEU   B CA  
883  C C   . LEU   B 67  ? 0.4623 0.4764 0.2705 0.0627  0.0641  -0.0298 76  LEU   B C   
884  O O   . LEU   B 67  ? 0.4523 0.4672 0.2636 0.0517  0.0645  -0.0310 76  LEU   B O   
885  C CB  . LEU   B 67  ? 0.4704 0.4704 0.2560 0.0752  0.0522  -0.0297 76  LEU   B CB  
886  C CG  . LEU   B 67  ? 0.4779 0.4722 0.2516 0.0888  0.0478  -0.0275 76  LEU   B CG  
887  C CD1 . LEU   B 67  ? 0.4916 0.4756 0.2545 0.0878  0.0377  -0.0326 76  LEU   B CD1 
888  C CD2 . LEU   B 67  ? 0.4897 0.4887 0.2641 0.1023  0.0512  -0.0252 76  LEU   B CD2 
889  N N   . VAL   B 68  ? 0.4491 0.4663 0.2613 0.0652  0.0652  -0.0327 77  VAL   B N   
890  C CA  . VAL   B 68  ? 0.4320 0.4545 0.2530 0.0554  0.0672  -0.0377 77  VAL   B CA  
891  C C   . VAL   B 68  ? 0.4247 0.4481 0.2449 0.0587  0.0646  -0.0421 77  VAL   B C   
892  O O   . VAL   B 68  ? 0.4238 0.4458 0.2409 0.0701  0.0643  -0.0405 77  VAL   B O   
893  C CB  . VAL   B 68  ? 0.4288 0.4577 0.2616 0.0540  0.0745  -0.0353 77  VAL   B CB  
894  C CG1 . VAL   B 68  ? 0.4354 0.4659 0.2712 0.0658  0.0783  -0.0308 77  VAL   B CG1 
895  C CG2 . VAL   B 68  ? 0.4204 0.4551 0.2616 0.0448  0.0763  -0.0410 77  VAL   B CG2 
896  N N   . SER   B 69  ? 0.4157 0.4419 0.2384 0.0492  0.0625  -0.0474 78  SER   B N   
897  C CA  . SER   B 69  ? 0.4217 0.4505 0.2453 0.0503  0.0598  -0.0523 78  SER   B CA  
898  C C   . SER   B 69  ? 0.4117 0.4502 0.2466 0.0444  0.0649  -0.0558 78  SER   B C   
899  O O   . SER   B 69  ? 0.4065 0.4490 0.2463 0.0355  0.0679  -0.0562 78  SER   B O   
900  C CB  . SER   B 69  ? 0.4322 0.4559 0.2482 0.0453  0.0515  -0.0552 78  SER   B CB  
901  O OG  . SER   B 69  ? 0.4347 0.4621 0.2536 0.0315  0.0510  -0.0572 78  SER   B OG  
902  N N   . TYR   B 70  ? 0.4107 0.4531 0.2493 0.0499  0.0655  -0.0586 79  TYR   B N   
903  C CA  . TYR   B 70  ? 0.4053 0.4572 0.2543 0.0465  0.0696  -0.0629 79  TYR   B CA  
904  C C   . TYR   B 70  ? 0.4147 0.4716 0.2642 0.0438  0.0654  -0.0685 79  TYR   B C   
905  O O   . TYR   B 70  ? 0.4045 0.4567 0.2481 0.0506  0.0608  -0.0686 79  TYR   B O   
906  C CB  . TYR   B 70  ? 0.4087 0.4612 0.2628 0.0565  0.0743  -0.0608 79  TYR   B CB  
907  C CG  . TYR   B 70  ? 0.4088 0.4588 0.2658 0.0574  0.0789  -0.0552 79  TYR   B CG  
908  C CD1 . TYR   B 70  ? 0.4187 0.4624 0.2695 0.0630  0.0785  -0.0489 79  TYR   B CD1 
909  C CD2 . TYR   B 70  ? 0.4190 0.4735 0.2854 0.0524  0.0832  -0.0564 79  TYR   B CD2 
910  C CE1 . TYR   B 70  ? 0.4181 0.4608 0.2727 0.0630  0.0825  -0.0434 79  TYR   B CE1 
911  C CE2 . TYR   B 70  ? 0.4194 0.4715 0.2897 0.0525  0.0867  -0.0514 79  TYR   B CE2 
912  C CZ  . TYR   B 70  ? 0.4073 0.4539 0.2719 0.0573  0.0864  -0.0446 79  TYR   B CZ  
913  O OH  . TYR   B 70  ? 0.4320 0.4774 0.3012 0.0569  0.0897  -0.0392 79  TYR   B OH  
914  N N   . CYS   B 71  ? 0.4250 0.4914 0.2812 0.0347  0.0670  -0.0729 80  CYS   B N   
915  C CA  . CYS   B 71  ? 0.4581 0.5335 0.3180 0.0309  0.0645  -0.0784 80  CYS   B CA  
916  C C   . CYS   B 71  ? 0.4635 0.5369 0.3178 0.0228  0.0580  -0.0783 80  CYS   B C   
917  O O   . CYS   B 71  ? 0.4786 0.5604 0.3367 0.0171  0.0558  -0.0819 80  CYS   B O   
918  C CB  . CYS   B 71  ? 0.5057 0.5814 0.3667 0.0415  0.0633  -0.0804 80  CYS   B CB  
919  S SG  . CYS   B 71  ? 0.5699 0.6460 0.4370 0.0515  0.0703  -0.0792 80  CYS   B SG  
920  N N   . GLY   B 72  ? 0.4544 0.5171 0.3003 0.0221  0.0547  -0.0741 81  GLY   B N   
921  C CA  . GLY   B 72  ? 0.4548 0.5140 0.2954 0.0146  0.0474  -0.0740 81  GLY   B CA  
922  C C   . GLY   B 72  ? 0.4466 0.4927 0.2773 0.0160  0.0442  -0.0693 81  GLY   B C   
923  O O   . GLY   B 72  ? 0.4368 0.4785 0.2656 0.0229  0.0481  -0.0663 81  GLY   B O   
924  N N   . PRO   B 73  ? 0.4618 0.5017 0.2864 0.0095  0.0369  -0.0684 82  PRO   B N   
925  C CA  . PRO   B 73  ? 0.4827 0.5094 0.2970 0.0113  0.0329  -0.0645 82  PRO   B CA  
926  C C   . PRO   B 73  ? 0.4897 0.5059 0.2961 0.0257  0.0293  -0.0637 82  PRO   B C   
927  O O   . PRO   B 73  ? 0.5058 0.5233 0.3132 0.0320  0.0269  -0.0666 82  PRO   B O   
928  C CB  . PRO   B 73  ? 0.4987 0.5218 0.3096 0.0000  0.0251  -0.0643 82  PRO   B CB  
929  C CG  . PRO   B 73  ? 0.4966 0.5285 0.3144 -0.0032 0.0227  -0.0683 82  PRO   B CG  
930  C CD  . PRO   B 73  ? 0.4774 0.5225 0.3049 0.0003  0.0316  -0.0710 82  PRO   B CD  
931  N N   . TRP   B 74  ? 0.4995 0.5064 0.2978 0.0306  0.0284  -0.0599 83  TRP   B N   
932  C CA  . TRP   B 74  ? 0.5057 0.5028 0.2944 0.0446  0.0244  -0.0586 83  TRP   B CA  
933  C C   . TRP   B 74  ? 0.5394 0.5294 0.3224 0.0466  0.0142  -0.0621 83  TRP   B C   
934  O O   . TRP   B 74  ? 0.5587 0.5433 0.3388 0.0371  0.0072  -0.0627 83  TRP   B O   
935  C CB  . TRP   B 74  ? 0.5075 0.4963 0.2881 0.0467  0.0235  -0.0544 83  TRP   B CB  
936  C CG  . TRP   B 74  ? 0.4970 0.4792 0.2688 0.0624  0.0217  -0.0525 83  TRP   B CG  
937  C CD1 . TRP   B 74  ? 0.5034 0.4746 0.2639 0.0698  0.0123  -0.0539 83  TRP   B CD1 
938  C CD2 . TRP   B 74  ? 0.4895 0.4767 0.2635 0.0732  0.0293  -0.0488 83  TRP   B CD2 
939  N NE1 . TRP   B 74  ? 0.5123 0.4821 0.2669 0.0850  0.0141  -0.0515 83  TRP   B NE1 
940  C CE2 . TRP   B 74  ? 0.4923 0.4721 0.2551 0.0870  0.0246  -0.0478 83  TRP   B CE2 
941  C CE3 . TRP   B 74  ? 0.4802 0.4771 0.2643 0.0724  0.0392  -0.0461 83  TRP   B CE3 
942  C CZ2 . TRP   B 74  ? 0.4946 0.4785 0.2567 0.1002  0.0302  -0.0437 83  TRP   B CZ2 
943  C CZ3 . TRP   B 74  ? 0.4773 0.4766 0.2612 0.0844  0.0442  -0.0416 83  TRP   B CZ3 
944  C CH2 . TRP   B 74  ? 0.4826 0.4762 0.2556 0.0981  0.0401  -0.0401 83  TRP   B CH2 
945  N N   . LYS   B 75  ? 0.5437 0.5332 0.3247 0.0590  0.0129  -0.0640 84  LYS   B N   
946  C CA  . LYS   B 75  ? 0.5598 0.5435 0.3365 0.0624  0.0031  -0.0683 84  LYS   B CA  
947  C C   . LYS   B 75  ? 0.5671 0.5377 0.3301 0.0757  -0.0042 -0.0680 84  LYS   B C   
948  O O   . LYS   B 75  ? 0.5852 0.5478 0.3429 0.0768  -0.0146 -0.0716 84  LYS   B O   
949  C CB  . LYS   B 75  ? 0.5678 0.5610 0.3518 0.0677  0.0064  -0.0715 84  LYS   B CB  
950  C CG  . LYS   B 75  ? 0.5656 0.5725 0.3630 0.0562  0.0128  -0.0730 84  LYS   B CG  
951  C CD  . LYS   B 75  ? 0.5940 0.6023 0.3948 0.0430  0.0062  -0.0756 84  LYS   B CD  
952  C CE  . LYS   B 75  ? 0.6141 0.6375 0.4273 0.0316  0.0134  -0.0765 84  LYS   B CE  
953  N NZ  . LYS   B 75  ? 0.6451 0.6736 0.4635 0.0212  0.0073  -0.0793 84  LYS   B NZ  
954  N N   . LEU   B 76  ? 0.5667 0.5358 0.3243 0.0857  0.0004  -0.0641 85  LEU   B N   
955  C CA  . LEU   B 76  ? 0.6032 0.5631 0.3478 0.1020  -0.0049 -0.0639 85  LEU   B CA  
956  C C   . LEU   B 76  ? 0.6468 0.5938 0.3809 0.0998  -0.0132 -0.0633 85  LEU   B C   
957  O O   . LEU   B 76  ? 0.6414 0.5892 0.3762 0.0948  -0.0086 -0.0592 85  LEU   B O   
958  C CB  . LEU   B 76  ? 0.5941 0.5611 0.3392 0.1135  0.0050  -0.0590 85  LEU   B CB  
959  C CG  . LEU   B 76  ? 0.5835 0.5632 0.3406 0.1134  0.0143  -0.0584 85  LEU   B CG  
960  C CD1 . LEU   B 76  ? 0.5801 0.5655 0.3373 0.1254  0.0229  -0.0528 85  LEU   B CD1 
961  C CD2 . LEU   B 76  ? 0.6049 0.5854 0.3630 0.1166  0.0096  -0.0639 85  LEU   B CD2 
962  N N   . ASP   B 77  ? 0.6951 0.6301 0.4199 0.1038  -0.0255 -0.0674 86  ASP   B N   
963  C CA  . ASP   B 77  ? 0.7630 0.6838 0.4780 0.1004  -0.0352 -0.0674 86  ASP   B CA  
964  C C   . ASP   B 77  ? 0.7477 0.6569 0.4473 0.1180  -0.0438 -0.0695 86  ASP   B C   
965  O O   . ASP   B 77  ? 0.7443 0.6410 0.4346 0.1176  -0.0522 -0.0698 86  ASP   B O   
966  C CB  . ASP   B 77  ? 0.8395 0.7546 0.5581 0.0850  -0.0439 -0.0701 86  ASP   B CB  
967  C CG  . ASP   B 77  ? 0.9326 0.8477 0.6540 0.0864  -0.0503 -0.0753 86  ASP   B CG  
968  O OD1 . ASP   B 77  ? 1.0095 0.9270 0.7277 0.1010  -0.0493 -0.0774 86  ASP   B OD1 
969  O OD2 . ASP   B 77  ? 1.0308 0.9447 0.7580 0.0728  -0.0561 -0.0768 86  ASP   B OD2 
970  N N   . ALA   B 78  ? 0.7093 0.6226 0.4055 0.1336  -0.0419 -0.0707 87  ALA   B N   
971  C CA  . ALA   B 78  ? 0.7017 0.6048 0.3822 0.1514  -0.0505 -0.0732 87  ALA   B CA  
972  C C   . ALA   B 78  ? 0.6893 0.5930 0.3632 0.1587  -0.0458 -0.0682 87  ALA   B C   
973  O O   . ALA   B 78  ? 0.6668 0.5824 0.3494 0.1540  -0.0332 -0.0622 87  ALA   B O   
974  C CB  . ALA   B 78  ? 0.7052 0.6136 0.3838 0.1660  -0.0498 -0.0758 87  ALA   B CB  
975  N N   . ALA   B 79  ? 0.7079 0.5993 0.3666 0.1707  -0.0559 -0.0707 88  ALA   B N   
976  C CA  . ALA   B 79  ? 0.7175 0.6064 0.3674 0.1779  -0.0550 -0.0672 88  ALA   B CA  
977  C C   . ALA   B 79  ? 0.7085 0.5961 0.3442 0.2011  -0.0587 -0.0688 88  ALA   B C   
978  O O   . ALA   B 79  ? 0.7019 0.5803 0.3297 0.2087  -0.0693 -0.0751 88  ALA   B O   
979  C CB  . ALA   B 79  ? 0.7452 0.6185 0.3901 0.1672  -0.0658 -0.0692 88  ALA   B CB  
980  N N   . TRP   B 80  ? 0.7036 0.6018 0.3371 0.2119  -0.0496 -0.0632 89  TRP   B N   
981  C CA  . TRP   B 80  ? 0.7482 0.6463 0.3666 0.2346  -0.0527 -0.0637 89  TRP   B CA  
982  C C   . TRP   B 80  ? 0.7704 0.6487 0.3736 0.2392  -0.0693 -0.0704 89  TRP   B C   
983  O O   . TRP   B 80  ? 0.7348 0.6045 0.3401 0.2253  -0.0727 -0.0700 89  TRP   B O   
984  C CB  . TRP   B 80  ? 0.7411 0.6525 0.3603 0.2416  -0.0416 -0.0558 89  TRP   B CB  
985  C CG  . TRP   B 80  ? 0.7493 0.6630 0.3532 0.2653  -0.0443 -0.0561 89  TRP   B CG  
986  C CD1 . TRP   B 80  ? 0.7731 0.6866 0.3678 0.2816  -0.0487 -0.0600 89  TRP   B CD1 
987  C CD2 . TRP   B 80  ? 0.7648 0.6825 0.3606 0.2763  -0.0428 -0.0524 89  TRP   B CD2 
988  N NE1 . TRP   B 80  ? 0.7733 0.6909 0.3544 0.3022  -0.0497 -0.0589 89  TRP   B NE1 
989  C CE2 . TRP   B 80  ? 0.7676 0.6879 0.3491 0.2994  -0.0464 -0.0544 89  TRP   B CE2 
990  C CE3 . TRP   B 80  ? 0.7627 0.6820 0.3613 0.2693  -0.0396 -0.0482 89  TRP   B CE3 
991  C CZ2 . TRP   B 80  ? 0.7688 0.6948 0.3394 0.3158  -0.0459 -0.0518 89  TRP   B CZ2 
992  C CZ3 . TRP   B 80  ? 0.7596 0.6842 0.3479 0.2853  -0.0394 -0.0457 89  TRP   B CZ3 
993  C CH2 . TRP   B 80  ? 0.7562 0.6847 0.3310 0.3081  -0.0422 -0.0473 89  TRP   B CH2 
994  N N   . ASP   B 81  ? 0.7961 0.6672 0.3850 0.2571  -0.0791 -0.0762 90  ASP   B N   
995  C CA  . ASP   B 81  ? 0.8497 0.6996 0.4232 0.2630  -0.0972 -0.0840 90  ASP   B CA  
996  C C   . ASP   B 81  ? 0.8805 0.7290 0.4429 0.2736  -0.0981 -0.0818 90  ASP   B C   
997  O O   . ASP   B 81  ? 0.9349 0.7653 0.4856 0.2759  -0.1123 -0.0872 90  ASP   B O   
998  C CB  . ASP   B 81  ? 0.8267 0.6684 0.3889 0.2784  -0.1089 -0.0920 90  ASP   B CB  
999  C CG  . ASP   B 81  ? 0.8525 0.7071 0.4058 0.3017  -0.1029 -0.0906 90  ASP   B CG  
1000 O OD1 . ASP   B 81  ? 0.8902 0.7594 0.4458 0.3060  -0.0907 -0.0832 90  ASP   B OD1 
1001 O OD2 . ASP   B 81  ? 0.8655 0.7173 0.4108 0.3151  -0.1098 -0.0964 90  ASP   B OD2 
1002 N N   . GLY   B 82  ? 0.8870 0.7540 0.4533 0.2797  -0.0838 -0.0741 91  GLY   B N   
1003 C CA  . GLY   B 82  ? 0.8812 0.7516 0.4381 0.2917  -0.0826 -0.0711 91  GLY   B CA  
1004 C C   . GLY   B 82  ? 0.9210 0.7938 0.4609 0.3185  -0.0872 -0.0742 91  GLY   B C   
1005 O O   . GLY   B 82  ? 0.9123 0.7869 0.4424 0.3305  -0.0882 -0.0729 91  GLY   B O   
1006 N N   . LEU   B 83  ? 0.9337 0.8065 0.4695 0.3284  -0.0904 -0.0784 92  LEU   B N   
1007 C CA  . LEU   B 83  ? 0.9756 0.8482 0.4932 0.3548  -0.0973 -0.0832 92  LEU   B CA  
1008 C C   . LEU   B 83  ? 0.9800 0.8702 0.5011 0.3651  -0.0870 -0.0797 92  LEU   B C   
1009 O O   . LEU   B 83  ? 0.9758 0.8798 0.4878 0.3856  -0.0819 -0.0765 92  LEU   B O   
1010 C CB  . LEU   B 83  ? 1.0256 0.8739 0.5315 0.3571  -0.1172 -0.0948 92  LEU   B CB  
1011 C CG  . LEU   B 83  ? 1.0754 0.9031 0.5705 0.3556  -0.1317 -0.1000 92  LEU   B CG  
1012 C CD1 . LEU   B 83  ? 1.1128 0.9171 0.5971 0.3591  -0.1517 -0.1112 92  LEU   B CD1 
1013 C CD2 . LEU   B 83  ? 1.0877 0.9211 0.5685 0.3760  -0.1315 -0.0988 92  LEU   B CD2 
1014 N N   . SER   B 84  ? 0.9557 0.8447 0.4876 0.3530  -0.0858 -0.0811 93  SER   B N   
1015 C CA  . SER   B 84  ? 0.9389 0.8389 0.4715 0.3635  -0.0806 -0.0806 93  SER   B CA  
1016 C C   . SER   B 84  ? 0.8972 0.8208 0.4431 0.3613  -0.0610 -0.0688 93  SER   B C   
1017 O O   . SER   B 84  ? 0.8346 0.7635 0.3930 0.3460  -0.0523 -0.0623 93  SER   B O   
1018 C CB  . SER   B 84  ? 0.9421 0.8321 0.4819 0.3510  -0.0870 -0.0866 93  SER   B CB  
1019 O OG  . SER   B 84  ? 0.9673 0.8348 0.5002 0.3450  -0.1040 -0.0953 93  SER   B OG  
1020 N N   . GLU   B 85  ? 0.8728 0.8095 0.4151 0.3771  -0.0550 -0.0660 94  GLU   B N   
1021 C CA  . GLU   B 85  ? 0.8462 0.8040 0.4026 0.3737  -0.0371 -0.0547 94  GLU   B CA  
1022 C C   . GLU   B 85  ? 0.7938 0.7471 0.3682 0.3499  -0.0344 -0.0554 94  GLU   B C   
1023 O O   . GLU   B 85  ? 0.8021 0.7387 0.3757 0.3407  -0.0464 -0.0645 94  GLU   B O   
1024 C CB  . GLU   B 85  ? 0.8703 0.8421 0.4170 0.3970  -0.0326 -0.0515 94  GLU   B CB  
1025 C CG  . GLU   B 85  ? 0.8802 0.8622 0.4137 0.4170  -0.0307 -0.0473 94  GLU   B CG  
1026 C CD  . GLU   B 85  ? 0.9264 0.9288 0.4539 0.4379  -0.0214 -0.0398 94  GLU   B CD  
1027 O OE1 . GLU   B 85  ? 0.8838 0.8915 0.4156 0.4392  -0.0170 -0.0381 94  GLU   B OE1 
1028 O OE2 . GLU   B 85  ? 0.9345 0.9483 0.4526 0.4537  -0.0185 -0.0353 94  GLU   B OE2 
1029 N N   . VAL   B 86  ? 0.7515 0.7206 0.3412 0.3418  -0.0193 -0.0456 95  VAL   B N   
1030 C CA  . VAL   B 86  ? 0.6976 0.6677 0.3049 0.3225  -0.0136 -0.0445 95  VAL   B CA  
1031 C C   . VAL   B 86  ? 0.6845 0.6717 0.2995 0.3282  -0.0005 -0.0361 95  VAL   B C   
1032 O O   . VAL   B 86  ? 0.7147 0.7141 0.3236 0.3438  0.0054  -0.0293 95  VAL   B O   
1033 C CB  . VAL   B 86  ? 0.6661 0.6352 0.2865 0.3018  -0.0089 -0.0411 95  VAL   B CB  
1034 C CG1 . VAL   B 86  ? 0.6735 0.6265 0.2851 0.2976  -0.0211 -0.0477 95  VAL   B CG1 
1035 C CG2 . VAL   B 86  ? 0.6559 0.6413 0.2829 0.3038  0.0042  -0.0298 95  VAL   B CG2 
1036 N N   . GLN   B 87  ? 0.6682 0.6572 0.2976 0.3145  0.0044  -0.0356 96  GLN   B N   
1037 C CA  . GLN   B 87  ? 0.6580 0.6623 0.2972 0.3171  0.0172  -0.0267 96  GLN   B CA  
1038 C C   . GLN   B 87  ? 0.6063 0.6154 0.2649 0.2970  0.0269  -0.0212 96  GLN   B C   
1039 O O   . GLN   B 87  ? 0.6086 0.6093 0.2744 0.2813  0.0229  -0.0270 96  GLN   B O   
1040 C CB  . GLN   B 87  ? 0.6713 0.6743 0.3078 0.3242  0.0140  -0.0314 96  GLN   B CB  
1041 C CG  . GLN   B 87  ? 0.7003 0.6990 0.3171 0.3455  0.0043  -0.0371 96  GLN   B CG  
1042 C CD  . GLN   B 87  ? 0.7167 0.7196 0.3306 0.3568  0.0048  -0.0382 96  GLN   B CD  
1043 O OE1 . GLN   B 87  ? 0.7159 0.7218 0.3423 0.3470  0.0099  -0.0370 96  GLN   B OE1 
1044 N NE2 . GLN   B 87  ? 0.7383 0.7417 0.3350 0.3782  -0.0007 -0.0407 96  GLN   B NE2 
1045 N N   . LEU   B 88  ? 0.5852 0.6080 0.2511 0.2985  0.0385  -0.0101 97  LEU   B N   
1046 C CA  . LEU   B 88  ? 0.5710 0.6010 0.2558 0.2832  0.0491  -0.0034 97  LEU   B CA  
1047 C C   . LEU   B 88  ? 0.5696 0.6039 0.2598 0.2858  0.0532  -0.0021 97  LEU   B C   
1048 O O   . LEU   B 88  ? 0.5822 0.6251 0.2665 0.3016  0.0570  0.0033  97  LEU   B O   
1049 C CB  . LEU   B 88  ? 0.5714 0.6142 0.2616 0.2852  0.0589  0.0082  97  LEU   B CB  
1050 C CG  . LEU   B 88  ? 0.5602 0.6100 0.2700 0.2702  0.0692  0.0155  97  LEU   B CG  
1051 C CD1 . LEU   B 88  ? 0.5614 0.6021 0.2806 0.2498  0.0664  0.0096  97  LEU   B CD1 
1052 C CD2 . LEU   B 88  ? 0.5559 0.6200 0.2717 0.2740  0.0789  0.0282  97  LEU   B CD2 
1053 N N   . LEU   B 89  ? 0.5660 0.5945 0.2657 0.2720  0.0517  -0.0077 98  LEU   B N   
1054 C CA  . LEU   B 89  ? 0.5646 0.5981 0.2734 0.2712  0.0573  -0.0055 98  LEU   B CA  
1055 C C   . LEU   B 89  ? 0.5558 0.5985 0.2801 0.2623  0.0688  0.0046  98  LEU   B C   
1056 O O   . LEU   B 89  ? 0.5570 0.5972 0.2944 0.2455  0.0707  0.0025  98  LEU   B O   
1057 C CB  . LEU   B 89  ? 0.5726 0.5967 0.2850 0.2600  0.0501  -0.0163 98  LEU   B CB  
1058 C CG  . LEU   B 89  ? 0.5887 0.6158 0.3103 0.2574  0.0536  -0.0171 98  LEU   B CG  
1059 C CD1 . LEU   B 89  ? 0.6034 0.6396 0.3232 0.2720  0.0604  -0.0088 98  LEU   B CD1 
1060 C CD2 . LEU   B 89  ? 0.6047 0.6237 0.3220 0.2563  0.0435  -0.0285 98  LEU   B CD2 
1061 N N   . ALA   B 90  ? 0.5627 0.6161 0.2857 0.2729  0.0760  0.0155  99  ALA   B N   
1062 C CA  . ALA   B 90  ? 0.5586 0.6213 0.2970 0.2653  0.0868  0.0265  99  ALA   B CA  
1063 C C   . ALA   B 90  ? 0.5551 0.6187 0.3043 0.2609  0.0909  0.0277  99  ALA   B C   
1064 O O   . ALA   B 90  ? 0.5710 0.6355 0.3130 0.2730  0.0896  0.0269  99  ALA   B O   
1065 C CB  . ALA   B 90  ? 0.5611 0.6366 0.2967 0.2781  0.0936  0.0388  99  ALA   B CB  
1066 N N   . VAL   B 91  ? 0.5456 0.6088 0.3107 0.2450  0.0952  0.0292  100 VAL   B N   
1067 C CA  . VAL   B 91  ? 0.5352 0.5999 0.3127 0.2401  0.1002  0.0321  100 VAL   B CA  
1068 C C   . VAL   B 91  ? 0.5359 0.6081 0.3270 0.2343  0.1090  0.0441  100 VAL   B C   
1069 O O   . VAL   B 91  ? 0.5196 0.5895 0.3229 0.2197  0.1105  0.0431  100 VAL   B O   
1070 C CB  . VAL   B 91  ? 0.5234 0.5796 0.3065 0.2269  0.0955  0.0208  100 VAL   B CB  
1071 C CG1 . VAL   B 91  ? 0.5286 0.5859 0.3237 0.2227  0.0998  0.0225  100 VAL   B CG1 
1072 C CG2 . VAL   B 91  ? 0.5307 0.5803 0.3005 0.2327  0.0862  0.0100  100 VAL   B CG2 
1073 N N   . PRO   B 92  ? 0.5470 0.6290 0.3367 0.2458  0.1148  0.0561  101 PRO   B N   
1074 C CA  . PRO   B 92  ? 0.5414 0.6314 0.3447 0.2404  0.1227  0.0685  101 PRO   B CA  
1075 C C   . PRO   B 92  ? 0.5397 0.6280 0.3577 0.2326  0.1267  0.0720  101 PRO   B C   
1076 O O   . PRO   B 92  ? 0.5336 0.6175 0.3489 0.2361  0.1246  0.0671  101 PRO   B O   
1077 C CB  . PRO   B 92  ? 0.5611 0.6632 0.3567 0.2565  0.1273  0.0802  101 PRO   B CB  
1078 C CG  . PRO   B 92  ? 0.5681 0.6676 0.3445 0.2715  0.1211  0.0726  101 PRO   B CG  
1079 C CD  . PRO   B 92  ? 0.5607 0.6473 0.3349 0.2647  0.1137  0.0583  101 PRO   B CD  
1080 N N   . PRO   B 93  ? 0.5509 0.6421 0.3845 0.2219  0.1316  0.0797  102 PRO   B N   
1081 C CA  . PRO   B 93  ? 0.5701 0.6582 0.4182 0.2139  0.1344  0.0826  102 PRO   B CA  
1082 C C   . PRO   B 93  ? 0.5911 0.6841 0.4379 0.2260  0.1386  0.0923  102 PRO   B C   
1083 O O   . PRO   B 93  ? 0.6127 0.7157 0.4558 0.2362  0.1429  0.1034  102 PRO   B O   
1084 C CB  . PRO   B 93  ? 0.5616 0.6528 0.4247 0.2020  0.1381  0.0899  102 PRO   B CB  
1085 C CG  . PRO   B 93  ? 0.5673 0.6591 0.4231 0.1996  0.1349  0.0842  102 PRO   B CG  
1086 C CD  . PRO   B 93  ? 0.5678 0.6646 0.4063 0.2163  0.1339  0.0852  102 PRO   B CD  
1087 N N   . GLY   B 94  ? 0.5976 0.6839 0.4466 0.2255  0.1369  0.0873  103 GLY   B N   
1088 C CA  . GLY   B 94  ? 0.6104 0.6991 0.4580 0.2363  0.1399  0.0950  103 GLY   B CA  
1089 C C   . GLY   B 94  ? 0.6254 0.7187 0.4550 0.2540  0.1386  0.0946  103 GLY   B C   
1090 O O   . GLY   B 94  ? 0.6477 0.7443 0.4750 0.2642  0.1414  0.1021  103 GLY   B O   
1091 N N   . GLU   B 95  ? 0.6177 0.7109 0.4344 0.2583  0.1340  0.0865  104 GLU   B N   
1092 C CA  . GLU   B 95  ? 0.6308 0.7288 0.4295 0.2764  0.1322  0.0865  104 GLU   B CA  
1093 C C   . GLU   B 95  ? 0.6394 0.7281 0.4274 0.2773  0.1233  0.0701  104 GLU   B C   
1094 O O   . GLU   B 95  ? 0.6369 0.7179 0.4309 0.2635  0.1194  0.0603  104 GLU   B O   
1095 C CB  . GLU   B 95  ? 0.6411 0.7489 0.4337 0.2827  0.1347  0.0936  104 GLU   B CB  
1096 C CG  . GLU   B 95  ? 0.6609 0.7800 0.4655 0.2813  0.1437  0.1110  104 GLU   B CG  
1097 C CD  . GLU   B 95  ? 0.6902 0.8211 0.4918 0.2861  0.1470  0.1192  104 GLU   B CD  
1098 O OE1 . GLU   B 95  ? 0.7039 0.8327 0.4944 0.2888  0.1418  0.1103  104 GLU   B OE1 
1099 O OE2 . GLU   B 95  ? 0.6974 0.8401 0.5085 0.2868  0.1547  0.1349  104 GLU   B OE2 
1100 N N   . ARG   B 96  ? 0.6519 0.7414 0.4252 0.2927  0.1200  0.0672  105 ARG   B N   
1101 C CA  . ARG   B 96  ? 0.6944 0.7752 0.4578 0.2944  0.1107  0.0519  105 ARG   B CA  
1102 C C   . ARG   B 96  ? 0.6791 0.7563 0.4351 0.2911  0.1048  0.0440  105 ARG   B C   
1103 O O   . ARG   B 96  ? 0.6618 0.7453 0.4111 0.2985  0.1067  0.0503  105 ARG   B O   
1104 C CB  . ARG   B 96  ? 0.7821 0.8655 0.5307 0.3135  0.1084  0.0518  105 ARG   B CB  
1105 C CG  . ARG   B 96  ? 0.8433 0.9181 0.5841 0.3154  0.0990  0.0370  105 ARG   B CG  
1106 C CD  . ARG   B 96  ? 0.8827 0.9590 0.6182 0.3283  0.0988  0.0379  105 ARG   B CD  
1107 N NE  . ARG   B 96  ? 0.9201 1.0052 0.6438 0.3471  0.1024  0.0479  105 ARG   B NE  
1108 C CZ  . ARG   B 96  ? 0.9638 1.0569 0.6918 0.3530  0.1109  0.0619  105 ARG   B CZ  
1109 N NH1 . ARG   B 96  ? 0.9391 1.0311 0.6831 0.3416  0.1164  0.0678  105 ARG   B NH1 
1110 N NH2 . ARG   B 96  ? 0.9839 1.0862 0.6995 0.3710  0.1136  0.0702  105 ARG   B NH2 
1111 N N   . ALA   B 97  ? 0.6617 0.7296 0.4171 0.2826  0.0972  0.0308  106 ALA   B N   
1112 C CA  . ALA   B 97  ? 0.6704 0.7328 0.4151 0.2825  0.0892  0.0218  106 ALA   B CA  
1113 C C   . ALA   B 97  ? 0.6939 0.7604 0.4214 0.3022  0.0871  0.0245  106 ALA   B C   
1114 O O   . ALA   B 97  ? 0.6533 0.7217 0.3736 0.3151  0.0863  0.0247  106 ALA   B O   
1115 C CB  . ALA   B 97  ? 0.6672 0.7202 0.4110 0.2757  0.0807  0.0081  106 ALA   B CB  
1116 N N   . LYS   B 98  ? 0.7036 0.7714 0.4241 0.3050  0.0857  0.0257  107 LYS   B N   
1117 C CA  . LYS   B 98  ? 0.7414 0.8132 0.4442 0.3245  0.0827  0.0271  107 LYS   B CA  
1118 C C   . LYS   B 98  ? 0.7343 0.7985 0.4279 0.3229  0.0742  0.0188  107 LYS   B C   
1119 O O   . LYS   B 98  ? 0.7258 0.7896 0.4276 0.3104  0.0765  0.0208  107 LYS   B O   
1120 C CB  . LYS   B 98  ? 0.8072 0.8935 0.5125 0.3324  0.0932  0.0425  107 LYS   B CB  
1121 C CG  . LYS   B 98  ? 0.9069 1.0014 0.5948 0.3545  0.0926  0.0464  107 LYS   B CG  
1122 C CD  . LYS   B 98  ? 0.9752 1.0854 0.6669 0.3592  0.1026  0.0617  107 LYS   B CD  
1123 C CE  . LYS   B 98  ? 0.9939 1.1047 0.7029 0.3402  0.1075  0.0662  107 LYS   B CE  
1124 N NZ  . LYS   B 98  ? 1.0471 1.1737 0.7603 0.3447  0.1165  0.0807  107 LYS   B NZ  
1125 N N   . ASN   B 99  ? 0.6972 0.7543 0.3750 0.3341  0.0640  0.0093  108 ASN   B N   
1126 C CA  . ASN   B 99  ? 0.7077 0.7568 0.3737 0.3365  0.0546  0.0018  108 ASN   B CA  
1127 C C   . ASN   B 99  ? 0.7151 0.7744 0.3722 0.3506  0.0587  0.0102  108 ASN   B C   
1128 O O   . ASN   B 99  ? 0.7331 0.8023 0.3826 0.3674  0.0626  0.0164  108 ASN   B O   
1129 C CB  . ASN   B 99  ? 0.7108 0.7485 0.3629 0.3448  0.0416  -0.0108 108 ASN   B CB  
1130 C CG  . ASN   B 99  ? 0.7408 0.7694 0.4025 0.3297  0.0369  -0.0194 108 ASN   B CG  
1131 O OD1 . ASN   B 99  ? 0.7479 0.7813 0.4208 0.3243  0.0433  -0.0161 108 ASN   B OD1 
1132 N ND2 . ASN   B 99  ? 0.7384 0.7544 0.3959 0.3231  0.0255  -0.0301 108 ASN   B ND2 
1133 N N   . ILE   B 100 ? 0.6893 0.7467 0.3465 0.3446  0.0574  0.0102  109 ILE   B N   
1134 C CA  . ILE   B 100 ? 0.6926 0.7591 0.3399 0.3584  0.0595  0.0164  109 ILE   B CA  
1135 C C   . ILE   B 100 ? 0.6981 0.7515 0.3332 0.3593  0.0473  0.0056  109 ILE   B C   
1136 O O   . ILE   B 100 ? 0.6989 0.7424 0.3419 0.3416  0.0440  0.0009  109 ILE   B O   
1137 C CB  . ILE   B 100 ? 0.7076 0.7860 0.3696 0.3490  0.0710  0.0285  109 ILE   B CB  
1138 C CG1 . ILE   B 100 ? 0.7196 0.8076 0.3965 0.3439  0.0820  0.0386  109 ILE   B CG1 
1139 C CG2 . ILE   B 100 ? 0.7305 0.8202 0.3831 0.3634  0.0733  0.0350  109 ILE   B CG2 
1140 C CD1 . ILE   B 100 ? 0.7388 0.8411 0.4087 0.3631  0.0880  0.0483  109 ILE   B CD1 
1141 N N   . GLN   B 101 ? 0.7110 0.7635 0.3276 0.3788  0.0402  0.0016  110 GLN   B N   
1142 C CA  . GLN   B 101 ? 0.7447 0.7816 0.3487 0.3801  0.0264  -0.0099 110 GLN   B CA  
1143 C C   . GLN   B 101 ? 0.7551 0.7986 0.3537 0.3866  0.0283  -0.0051 110 GLN   B C   
1144 O O   . GLN   B 101 ? 0.7539 0.8144 0.3502 0.4000  0.0370  0.0046  110 GLN   B O   
1145 C CB  . GLN   B 101 ? 0.7831 0.8118 0.3696 0.3969  0.0150  -0.0195 110 GLN   B CB  
1146 C CG  . GLN   B 101 ? 0.7850 0.7982 0.3569 0.4016  0.0003  -0.0304 110 GLN   B CG  
1147 C CD  . GLN   B 101 ? 0.8194 0.8222 0.3767 0.4150  -0.0121 -0.0411 110 GLN   B CD  
1148 O OE1 . GLN   B 101 ? 0.7755 0.7764 0.3379 0.4114  -0.0125 -0.0438 110 GLN   B OE1 
1149 N NE2 . GLN   B 101 ? 0.8404 0.8371 0.3792 0.4317  -0.0224 -0.0472 110 GLN   B NE2 
1150 N N   . THR   B 102 ? 0.7713 0.8025 0.3687 0.3767  0.0208  -0.0112 111 THR   B N   
1151 C CA  . THR   B 102 ? 0.7524 0.7892 0.3462 0.3806  0.0223  -0.0070 111 THR   B CA  
1152 C C   . THR   B 102 ? 0.7449 0.7624 0.3300 0.3755  0.0085  -0.0179 111 THR   B C   
1153 O O   . THR   B 102 ? 0.7589 0.7609 0.3464 0.3634  0.0007  -0.0262 111 THR   B O   
1154 C CB  . THR   B 102 ? 0.7295 0.7796 0.3425 0.3663  0.0360  0.0046  111 THR   B CB  
1155 O OG1 . THR   B 102 ? 0.7172 0.7767 0.3268 0.3731  0.0388  0.0101  111 THR   B OG1 
1156 C CG2 . THR   B 102 ? 0.7348 0.7742 0.3626 0.3415  0.0356  0.0016  111 THR   B CG2 
1157 N N   . LEU   B 103 ? 0.7448 0.7636 0.3181 0.3874  0.0048  -0.0181 112 LEU   B N   
1158 C CA  . LEU   B 103 ? 0.7455 0.7471 0.3114 0.3820  -0.0071 -0.0263 112 LEU   B CA  
1159 C C   . LEU   B 103 ? 0.7375 0.7444 0.3180 0.3651  0.0008  -0.0194 112 LEU   B C   
1160 O O   . LEU   B 103 ? 0.7366 0.7603 0.3199 0.3714  0.0100  -0.0103 112 LEU   B O   
1161 C CB  . LEU   B 103 ? 0.7765 0.7769 0.3213 0.4053  -0.0157 -0.0305 112 LEU   B CB  
1162 C CG  . LEU   B 103 ? 0.7878 0.7692 0.3247 0.4001  -0.0287 -0.0387 112 LEU   B CG  
1163 C CD1 . LEU   B 103 ? 0.8046 0.7626 0.3351 0.3949  -0.0438 -0.0509 112 LEU   B CD1 
1164 C CD2 . LEU   B 103 ? 0.8228 0.8077 0.3425 0.4211  -0.0335 -0.0398 112 LEU   B CD2 
1165 N N   . PRO   B 104 ? 0.7143 0.7078 0.3043 0.3436  -0.0027 -0.0235 113 PRO   B N   
1166 C CA  . PRO   B 104 ? 0.7085 0.7065 0.3122 0.3273  0.0044  -0.0175 113 PRO   B CA  
1167 C C   . PRO   B 104 ? 0.7351 0.7315 0.3283 0.3353  -0.0004 -0.0180 113 PRO   B C   
1168 O O   . PRO   B 104 ? 0.7337 0.7169 0.3099 0.3465  -0.0132 -0.0263 113 PRO   B O   
1169 C CB  . PRO   B 104 ? 0.7046 0.6864 0.3163 0.3053  -0.0011 -0.0237 113 PRO   B CB  
1170 C CG  . PRO   B 104 ? 0.7150 0.6873 0.3213 0.3087  -0.0084 -0.0312 113 PRO   B CG  
1171 C CD  . PRO   B 104 ? 0.7231 0.6971 0.3112 0.3339  -0.0139 -0.0337 113 PRO   B CD  
1172 N N   . GLY   B 105 ? 0.7450 0.7548 0.3492 0.3292  0.0095  -0.0092 114 GLY   B N   
1173 C CA  . GLY   B 105 ? 0.7634 0.7714 0.3636 0.3291  0.0063  -0.0090 114 GLY   B CA  
1174 C C   . GLY   B 105 ? 0.7644 0.7562 0.3708 0.3077  0.0010  -0.0137 114 GLY   B C   
1175 O O   . GLY   B 105 ? 0.7463 0.7259 0.3560 0.2963  -0.0032 -0.0192 114 GLY   B O   
1176 N N   . ILE   B 106 ? 0.7822 0.7751 0.3903 0.3030  0.0013  -0.0114 115 ILE   B N   
1177 C CA  . ILE   B 106 ? 0.7738 0.7509 0.3842 0.2854  -0.0052 -0.0158 115 ILE   B CA  
1178 C C   . ILE   B 106 ? 0.7448 0.7345 0.3706 0.2733  0.0052  -0.0078 115 ILE   B C   
1179 O O   . ILE   B 106 ? 0.7407 0.7450 0.3669 0.2828  0.0107  -0.0016 115 ILE   B O   
1180 C CB  . ILE   B 106 ? 0.8292 0.7908 0.4210 0.2953  -0.0192 -0.0231 115 ILE   B CB  
1181 C CG1 . ILE   B 106 ? 0.8987 0.8473 0.4745 0.3089  -0.0308 -0.0315 115 ILE   B CG1 
1182 C CG2 . ILE   B 106 ? 0.8513 0.7971 0.4454 0.2772  -0.0256 -0.0265 115 ILE   B CG2 
1183 C CD1 . ILE   B 106 ? 0.8973 0.8259 0.4736 0.2945  -0.0401 -0.0389 115 ILE   B CD1 
1184 N N   . PHE   B 107 ? 0.7131 0.6979 0.3516 0.2527  0.0075  -0.0080 116 PHE   B N   
1185 C CA  . PHE   B 107 ? 0.6970 0.6867 0.3473 0.2386  0.0130  -0.0034 116 PHE   B CA  
1186 C C   . PHE   B 107 ? 0.7273 0.6989 0.3670 0.2335  0.0012  -0.0099 116 PHE   B C   
1187 O O   . PHE   B 107 ? 0.7125 0.6679 0.3488 0.2243  -0.0065 -0.0163 116 PHE   B O   
1188 C CB  . PHE   B 107 ? 0.6959 0.6881 0.3634 0.2200  0.0203  -0.0016 116 PHE   B CB  
1189 C CG  . PHE   B 107 ? 0.6837 0.6946 0.3661 0.2202  0.0333  0.0067  116 PHE   B CG  
1190 C CD1 . PHE   B 107 ? 0.6916 0.7176 0.3722 0.2368  0.0389  0.0131  116 PHE   B CD1 
1191 C CD2 . PHE   B 107 ? 0.6858 0.6990 0.3842 0.2035  0.0397  0.0083  116 PHE   B CD2 
1192 C CE1 . PHE   B 107 ? 0.7024 0.7451 0.3977 0.2358  0.0507  0.0217  116 PHE   B CE1 
1193 C CE2 . PHE   B 107 ? 0.6817 0.7103 0.3942 0.2031  0.0509  0.0160  116 PHE   B CE2 
1194 C CZ  . PHE   B 107 ? 0.6930 0.7359 0.4042 0.2188  0.0562  0.0230  116 PHE   B CZ  
1195 N N   . LYS   B 108 ? 0.7438 0.7183 0.3775 0.2407  -0.0005 -0.0081 117 LYS   B N   
1196 C CA  . LYS   B 108 ? 0.7816 0.7405 0.4068 0.2351  -0.0105 -0.0126 117 LYS   B CA  
1197 C C   . LYS   B 108 ? 0.7268 0.6904 0.3670 0.2162  -0.0039 -0.0085 117 LYS   B C   
1198 O O   . LYS   B 108 ? 0.6898 0.6715 0.3411 0.2170  0.0062  -0.0012 117 LYS   B O   
1199 C CB  . LYS   B 108 ? 0.8565 0.8175 0.4678 0.2538  -0.0156 -0.0129 117 LYS   B CB  
1200 C CG  . LYS   B 108 ? 0.9689 0.9143 0.5601 0.2692  -0.0289 -0.0209 117 LYS   B CG  
1201 C CD  . LYS   B 108 ? 1.0511 1.0062 0.6299 0.2933  -0.0303 -0.0201 117 LYS   B CD  
1202 C CE  . LYS   B 108 ? 1.1704 1.1102 0.7295 0.3095  -0.0434 -0.0287 117 LYS   B CE  
1203 N NZ  . LYS   B 108 ? 1.2095 1.1602 0.7556 0.3350  -0.0446 -0.0285 117 LYS   B NZ  
1204 N N   . THR   B 109 ? 0.7119 0.6606 0.3530 0.1998  -0.0092 -0.0127 118 THR   B N   
1205 C CA  . THR   B 109 ? 0.7133 0.6636 0.3662 0.1815  -0.0048 -0.0102 118 THR   B CA  
1206 C C   . THR   B 109 ? 0.7268 0.6585 0.3691 0.1746  -0.0162 -0.0148 118 THR   B C   
1207 O O   . THR   B 109 ? 0.7117 0.6268 0.3398 0.1798  -0.0277 -0.0205 118 THR   B O   
1208 C CB  . THR   B 109 ? 0.6900 0.6429 0.3573 0.1653  0.0016  -0.0098 118 THR   B CB  
1209 O OG1 . THR   B 109 ? 0.6873 0.6229 0.3484 0.1561  -0.0073 -0.0159 118 THR   B OG1 
1210 C CG2 . THR   B 109 ? 0.6916 0.6579 0.3671 0.1718  0.0103  -0.0066 118 THR   B CG2 
1211 N N   . LYS   B 110 ? 0.7648 0.6990 0.4147 0.1619  -0.0130 -0.0123 119 LYS   B N   
1212 C CA  . LYS   B 110 ? 0.7982 0.7163 0.4396 0.1536  -0.0224 -0.0153 119 LYS   B CA  
1213 C C   . LYS   B 110 ? 0.8292 0.7306 0.4668 0.1425  -0.0300 -0.0201 119 LYS   B C   
1214 O O   . LYS   B 110 ? 0.8667 0.7506 0.4924 0.1403  -0.0413 -0.0234 119 LYS   B O   
1215 C CB  . LYS   B 110 ? 0.8070 0.7345 0.4599 0.1417  -0.0155 -0.0111 119 LYS   B CB  
1216 C CG  . LYS   B 110 ? 0.8348 0.7703 0.5040 0.1257  -0.0065 -0.0094 119 LYS   B CG  
1217 C CD  . LYS   B 110 ? 0.8438 0.7884 0.5238 0.1153  -0.0004 -0.0059 119 LYS   B CD  
1218 C CE  . LYS   B 110 ? 0.8794 0.8153 0.5613 0.0974  -0.0026 -0.0080 119 LYS   B CE  
1219 N NZ  . LYS   B 110 ? 0.8798 0.8202 0.5728 0.0873  0.0033  -0.0088 119 LYS   B NZ  
1220 N N   . ASP   B 111 ? 0.8064 0.7129 0.4536 0.1361  -0.0244 -0.0204 120 ASP   B N   
1221 C CA  . ASP   B 111 ? 0.8112 0.7054 0.4577 0.1243  -0.0301 -0.0244 120 ASP   B CA  
1222 C C   . ASP   B 111 ? 0.8279 0.7150 0.4664 0.1353  -0.0364 -0.0286 120 ASP   B C   
1223 O O   . ASP   B 111 ? 0.8671 0.7463 0.5069 0.1262  -0.0404 -0.0316 120 ASP   B O   
1224 C CB  . ASP   B 111 ? 0.8209 0.7261 0.4839 0.1096  -0.0200 -0.0225 120 ASP   B CB  
1225 C CG  . ASP   B 111 ? 0.8286 0.7395 0.4992 0.0976  -0.0149 -0.0194 120 ASP   B CG  
1226 O OD1 . ASP   B 111 ? 0.8150 0.7152 0.4773 0.0937  -0.0220 -0.0199 120 ASP   B OD1 
1227 O OD2 . ASP   B 111 ? 0.8928 0.8182 0.5769 0.0931  -0.0044 -0.0164 120 ASP   B OD2 
1228 N N   . GLY   B 112 ? 0.8111 0.7024 0.4425 0.1540  -0.0368 -0.0286 121 GLY   B N   
1229 C CA  . GLY   B 112 ? 0.8260 0.7096 0.4476 0.1664  -0.0441 -0.0332 121 GLY   B CA  
1230 C C   . GLY   B 112 ? 0.7984 0.6983 0.4234 0.1812  -0.0355 -0.0308 121 GLY   B C   
1231 O O   . GLY   B 112 ? 0.7843 0.7016 0.4215 0.1793  -0.0232 -0.0249 121 GLY   B O   
1232 N N   . ASP   B 113 ? 0.8087 0.7023 0.4225 0.1956  -0.0425 -0.0351 122 ASP   B N   
1233 C CA  . ASP   B 113 ? 0.7994 0.7071 0.4133 0.2119  -0.0360 -0.0332 122 ASP   B CA  
1234 C C   . ASP   B 113 ? 0.7981 0.7114 0.4236 0.2039  -0.0298 -0.0331 122 ASP   B C   
1235 O O   . ASP   B 113 ? 0.7499 0.6517 0.3772 0.1912  -0.0355 -0.0373 122 ASP   B O   
1236 C CB  . ASP   B 113 ? 0.8605 0.7585 0.4560 0.2319  -0.0472 -0.0385 122 ASP   B CB  
1237 C CG  . ASP   B 113 ? 0.8955 0.7924 0.4792 0.2448  -0.0517 -0.0382 122 ASP   B CG  
1238 O OD1 . ASP   B 113 ? 0.9064 0.8116 0.4969 0.2387  -0.0454 -0.0332 122 ASP   B OD1 
1239 O OD2 . ASP   B 113 ? 0.9687 0.8571 0.5363 0.2619  -0.0616 -0.0433 122 ASP   B OD2 
1240 N N   . ILE   B 114 ? 0.7688 0.7000 0.4028 0.2105  -0.0183 -0.0279 123 ILE   B N   
1241 C CA  . ILE   B 114 ? 0.7661 0.7040 0.4110 0.2050  -0.0117 -0.0274 123 ILE   B CA  
1242 C C   . ILE   B 114 ? 0.7245 0.6729 0.3648 0.2244  -0.0080 -0.0254 123 ILE   B C   
1243 O O   . ILE   B 114 ? 0.6991 0.6603 0.3395 0.2345  -0.0016 -0.0195 123 ILE   B O   
1244 C CB  . ILE   B 114 ? 0.7472 0.6977 0.4108 0.1897  0.0006  -0.0216 123 ILE   B CB  
1245 C CG1 . ILE   B 114 ? 0.8041 0.7494 0.4717 0.1742  -0.0006 -0.0213 123 ILE   B CG1 
1246 C CG2 . ILE   B 114 ? 0.7657 0.7185 0.4394 0.1813  0.0045  -0.0230 123 ILE   B CG2 
1247 C CD1 . ILE   B 114 ? 0.7895 0.7487 0.4743 0.1628  0.0115  -0.0154 123 ILE   B CD1 
1248 N N   . GLY   B 115 ? 0.7130 0.6585 0.3517 0.2281  -0.0105 -0.0292 124 GLY   B N   
1249 C CA  . GLY   B 115 ? 0.6886 0.6460 0.3249 0.2450  -0.0052 -0.0264 124 GLY   B CA  
1250 C C   . GLY   B 115 ? 0.6664 0.6437 0.3175 0.2428  0.0099  -0.0166 124 GLY   B C   
1251 O O   . GLY   B 115 ? 0.6106 0.5911 0.2764 0.2255  0.0163  -0.0137 124 GLY   B O   
1252 N N   . ALA   B 116 ? 0.6594 0.6501 0.3070 0.2598  0.0154  -0.0112 125 ALA   B N   
1253 C CA  . ALA   B 116 ? 0.6743 0.6847 0.3359 0.2595  0.0295  -0.0007 125 ALA   B CA  
1254 C C   . ALA   B 116 ? 0.6811 0.7014 0.3381 0.2765  0.0333  0.0023  125 ALA   B C   
1255 O O   . ALA   B 116 ? 0.7131 0.7300 0.3535 0.2937  0.0261  -0.0015 125 ALA   B O   
1256 C CB  . ALA   B 116 ? 0.6883 0.7085 0.3513 0.2623  0.0337  0.0056  125 ALA   B CB  
1257 N N   A VAL   B 117 ? 0.6710 0.7024 0.3413 0.2724  0.0434  0.0086  126 VAL   B N   
1258 N N   B VAL   B 117 ? 0.6691 0.7015 0.3399 0.2724  0.0441  0.0093  126 VAL   B N   
1259 N N   C VAL   B 117 ? 0.6703 0.7016 0.3406 0.2723  0.0434  0.0086  126 VAL   B N   
1260 N N   D VAL   B 117 ? 0.6655 0.6979 0.3364 0.2723  0.0440  0.0093  126 VAL   B N   
1261 C CA  A VAL   B 117 ? 0.6783 0.7216 0.3457 0.2884  0.0488  0.0137  126 VAL   B CA  
1262 C CA  B VAL   B 117 ? 0.6708 0.7143 0.3400 0.2867  0.0495  0.0141  126 VAL   B CA  
1263 C CA  C VAL   B 117 ? 0.6781 0.7214 0.3455 0.2884  0.0488  0.0137  126 VAL   B CA  
1264 C CA  D VAL   B 117 ? 0.6680 0.7115 0.3372 0.2866  0.0495  0.0141  126 VAL   B CA  
1265 C C   A VAL   B 117 ? 0.6711 0.7348 0.3499 0.2909  0.0615  0.0269  126 VAL   B C   
1266 C C   B VAL   B 117 ? 0.6650 0.7291 0.3444 0.2906  0.0620  0.0272  126 VAL   B C   
1267 C C   C VAL   B 117 ? 0.6716 0.7353 0.3504 0.2909  0.0615  0.0269  126 VAL   B C   
1268 C C   D VAL   B 117 ? 0.6668 0.7309 0.3463 0.2906  0.0620  0.0272  126 VAL   B C   
1269 O O   A VAL   B 117 ? 0.6571 0.7247 0.3525 0.2751  0.0682  0.0317  126 VAL   B O   
1270 O O   B VAL   B 117 ? 0.6505 0.7193 0.3469 0.2753  0.0692  0.0325  126 VAL   B O   
1271 O O   C VAL   B 117 ? 0.6575 0.7252 0.3529 0.2751  0.0683  0.0317  126 VAL   B O   
1272 O O   D VAL   B 117 ? 0.6521 0.7210 0.3486 0.2753  0.0692  0.0326  126 VAL   B O   
1273 C CB  A VAL   B 117 ? 0.6820 0.7209 0.3540 0.2840  0.0491  0.0104  126 VAL   B CB  
1274 C CB  B VAL   B 117 ? 0.6640 0.7026 0.3411 0.2775  0.0506  0.0110  126 VAL   B CB  
1275 C CB  C VAL   B 117 ? 0.6827 0.7217 0.3547 0.2840  0.0491  0.0104  126 VAL   B CB  
1276 C CB  D VAL   B 117 ? 0.6632 0.7019 0.3405 0.2774  0.0506  0.0110  126 VAL   B CB  
1277 C CG1 A VAL   B 117 ? 0.6943 0.7144 0.3558 0.2817  0.0361  -0.0019 126 VAL   B CG1 
1278 C CG1 B VAL   B 117 ? 0.6637 0.7147 0.3426 0.2892  0.0580  0.0176  126 VAL   B CG1 
1279 C CG1 C VAL   B 117 ? 0.6956 0.7157 0.3570 0.2818  0.0361  -0.0019 126 VAL   B CG1 
1280 C CG1 D VAL   B 117 ? 0.6604 0.7114 0.3394 0.2890  0.0580  0.0176  126 VAL   B CG1 
1281 C CG2 A VAL   B 117 ? 0.6665 0.7096 0.3584 0.2659  0.0577  0.0149  126 VAL   B CG2 
1282 C CG2 B VAL   B 117 ? 0.6730 0.6933 0.3398 0.2756  0.0380  -0.0012 126 VAL   B CG2 
1283 C CG2 C VAL   B 117 ? 0.6673 0.7104 0.3592 0.2659  0.0577  0.0149  126 VAL   B CG2 
1284 C CG2 D VAL   B 117 ? 0.6746 0.6950 0.3414 0.2756  0.0380  -0.0012 126 VAL   B CG2 
1285 N N   . ALA   B 118 ? 0.6683 0.7448 0.3384 0.3103  0.0644  0.0325  127 ALA   B N   
1286 C CA  . ALA   B 118 ? 0.6828 0.7811 0.3625 0.3151  0.0763  0.0463  127 ALA   B CA  
1287 C C   . ALA   B 118 ? 0.7044 0.8138 0.3890 0.3218  0.0843  0.0539  127 ALA   B C   
1288 O O   . ALA   B 118 ? 0.7319 0.8515 0.4055 0.3412  0.0856  0.0575  127 ALA   B O   
1289 C CB  . ALA   B 118 ? 0.6986 0.8061 0.3656 0.3324  0.0746  0.0486  127 ALA   B CB  
1290 N N   . LEU   B 119 ? 0.6946 0.8002 0.3932 0.3074  0.0882  0.0547  128 LEU   B N   
1291 C CA  . LEU   B 119 ? 0.7033 0.8171 0.4074 0.3119  0.0952  0.0615  128 LEU   B CA  
1292 C C   . LEU   B 119 ? 0.7389 0.8604 0.4652 0.2961  0.1049  0.0711  128 LEU   B C   
1293 O O   . LEU   B 119 ? 0.8045 0.9171 0.5407 0.2786  0.1033  0.0668  128 LEU   B O   
1294 C CB  . LEU   B 119 ? 0.7004 0.7991 0.3976 0.3112  0.0879  0.0506  128 LEU   B CB  
1295 C CG  . LEU   B 119 ? 0.6882 0.7771 0.3639 0.3259  0.0766  0.0400  128 LEU   B CG  
1296 C CD1 . LEU   B 119 ? 0.6623 0.7349 0.3350 0.3201  0.0685  0.0286  128 LEU   B CD1 
1297 C CD2 . LEU   B 119 ? 0.7120 0.8141 0.3757 0.3488  0.0793  0.0458  128 LEU   B CD2 
1298 N N   . ASP   B 120 ? 0.7997 0.9373 0.5335 0.3023  0.1145  0.0840  129 ASP   B N   
1299 C CA  . ASP   B 120 ? 0.8291 0.9754 0.5843 0.2886  0.1234  0.0949  129 ASP   B CA  
1300 C C   . ASP   B 120 ? 0.7779 0.9191 0.5428 0.2812  0.1262  0.0956  129 ASP   B C   
1301 O O   . ASP   B 120 ? 0.8579 1.0057 0.6189 0.2930  0.1297  0.1011  129 ASP   B O   
1302 C CB  . ASP   B 120 ? 0.8941 1.0622 0.6534 0.2986  0.1319  0.1099  129 ASP   B CB  
1303 C CG  . ASP   B 120 ? 0.9480 1.1223 0.7204 0.2871  0.1347  0.1148  129 ASP   B CG  
1304 O OD1 . ASP   B 120 ? 0.9156 1.0810 0.7019 0.2684  0.1344  0.1120  129 ASP   B OD1 
1305 O OD2 . ASP   B 120 ? 1.0318 1.2195 0.7997 0.2972  0.1366  0.1205  129 ASP   B OD2 
1306 N N   . TYR   B 121 ? 0.7319 0.8622 0.5086 0.2632  0.1248  0.0902  130 TYR   B N   
1307 C CA  . TYR   B 121 ? 0.7142 0.8405 0.5016 0.2559  0.1278  0.0914  130 TYR   B CA  
1308 C C   . TYR   B 121 ? 0.6712 0.7971 0.4786 0.2378  0.1317  0.0952  130 TYR   B C   
1309 O O   . TYR   B 121 ? 0.6525 0.7778 0.4637 0.2294  0.1303  0.0936  130 TYR   B O   
1310 C CB  . TYR   B 121 ? 0.7365 0.8474 0.5152 0.2542  0.1200  0.0775  130 TYR   B CB  
1311 C CG  . TYR   B 121 ? 0.7822 0.8931 0.5434 0.2722  0.1164  0.0743  130 TYR   B CG  
1312 C CD1 . TYR   B 121 ? 0.8194 0.9345 0.5807 0.2805  0.1202  0.0795  130 TYR   B CD1 
1313 C CD2 . TYR   B 121 ? 0.8158 0.9215 0.5598 0.2814  0.1086  0.0661  130 TYR   B CD2 
1314 C CE1 . TYR   B 121 ? 0.8510 0.9662 0.5958 0.2977  0.1166  0.0762  130 TYR   B CE1 
1315 C CE2 . TYR   B 121 ? 0.8611 0.9663 0.5887 0.2987  0.1043  0.0625  130 TYR   B CE2 
1316 C CZ  . TYR   B 121 ? 0.8706 0.9810 0.5985 0.3070  0.1085  0.0676  130 TYR   B CZ  
1317 O OH  . TYR   B 121 ? 0.9498 1.0600 0.6613 0.3245  0.1043  0.0641  130 TYR   B OH  
1318 N N   . PRO   B 122 ? 0.6497 0.7749 0.4700 0.2311  0.1358  0.0996  131 PRO   B N   
1319 C CA  . PRO   B 122 ? 0.6427 0.7663 0.4816 0.2143  0.1384  0.1022  131 PRO   B CA  
1320 C C   . PRO   B 122 ? 0.6029 0.7126 0.4402 0.2019  0.1314  0.0878  131 PRO   B C   
1321 O O   . PRO   B 122 ? 0.5666 0.6674 0.3903 0.2056  0.1251  0.0768  131 PRO   B O   
1322 C CB  . PRO   B 122 ? 0.6652 0.7893 0.5151 0.2128  0.1429  0.1088  131 PRO   B CB  
1323 C CG  . PRO   B 122 ? 0.6799 0.8093 0.5169 0.2304  0.1443  0.1125  131 PRO   B CG  
1324 C CD  . PRO   B 122 ? 0.6894 0.8141 0.5072 0.2391  0.1374  0.1014  131 PRO   B CD  
1325 N N   . ALA   B 123 ? 0.5951 0.7035 0.4463 0.1874  0.1325  0.0885  132 ALA   B N   
1326 C CA  . ALA   B 123 ? 0.5687 0.6663 0.4204 0.1743  0.1270  0.0768  132 ALA   B CA  
1327 C C   . ALA   B 123 ? 0.5716 0.6587 0.4229 0.1696  0.1238  0.0672  132 ALA   B C   
1328 O O   . ALA   B 123 ? 0.5373 0.6152 0.3808 0.1646  0.1176  0.0554  132 ALA   B O   
1329 C CB  . ALA   B 123 ? 0.5704 0.6710 0.4376 0.1617  0.1295  0.0813  132 ALA   B CB  
1330 N N   . GLY   B 124 ? 0.5392 0.6279 0.3973 0.1723  0.1276  0.0722  133 GLY   B N   
1331 C CA  . GLY   B 124 ? 0.5197 0.6000 0.3774 0.1698  0.1249  0.0637  133 GLY   B CA  
1332 C C   . GLY   B 124 ? 0.5042 0.5799 0.3449 0.1789  0.1195  0.0550  133 GLY   B C   
1333 O O   . GLY   B 124 ? 0.4844 0.5533 0.3244 0.1757  0.1163  0.0464  133 GLY   B O   
1334 N N   . THR   B 125 ? 0.4946 0.5737 0.3222 0.1898  0.1178  0.0564  134 THR   B N   
1335 C CA  . THR   B 125 ? 0.5206 0.5939 0.3313 0.1987  0.1111  0.0475  134 THR   B CA  
1336 C C   . THR   B 125 ? 0.5221 0.5864 0.3275 0.1893  0.1039  0.0364  134 THR   B C   
1337 O O   . THR   B 125 ? 0.5178 0.5751 0.3104 0.1940  0.0968  0.0276  134 THR   B O   
1338 C CB  . THR   B 125 ? 0.5670 0.6479 0.3656 0.2161  0.1121  0.0540  134 THR   B CB  
1339 O OG1 . THR   B 125 ? 0.5831 0.6736 0.3885 0.2228  0.1195  0.0657  134 THR   B OG1 
1340 C CG2 . THR   B 125 ? 0.5855 0.6611 0.3673 0.2280  0.1054  0.0461  134 THR   B CG2 
1341 N N   . SER   B 126 ? 0.5044 0.5685 0.3190 0.1767  0.1051  0.0370  135 SER   B N   
1342 C CA  . SER   B 126 ? 0.4973 0.5534 0.3084 0.1661  0.0992  0.0280  135 SER   B CA  
1343 C C   . SER   B 126 ? 0.4828 0.5306 0.2907 0.1612  0.0937  0.0171  135 SER   B C   
1344 O O   . SER   B 126 ? 0.4809 0.5288 0.2986 0.1556  0.0962  0.0155  135 SER   B O   
1345 C CB  . SER   B 126 ? 0.4952 0.5529 0.3193 0.1527  0.1023  0.0301  135 SER   B CB  
1346 O OG  . SER   B 126 ? 0.5042 0.5692 0.3297 0.1563  0.1055  0.0387  135 SER   B OG  
1347 N N   . GLY   B 127 ? 0.4785 0.5194 0.2739 0.1632  0.0862  0.0099  136 GLY   B N   
1348 C CA  . GLY   B 127 ? 0.4916 0.5254 0.2848 0.1573  0.0806  0.0000  136 GLY   B CA  
1349 C C   . GLY   B 127 ? 0.4973 0.5289 0.2800 0.1699  0.0763  -0.0032 136 GLY   B C   
1350 O O   . GLY   B 127 ? 0.4925 0.5176 0.2709 0.1663  0.0697  -0.0118 136 GLY   B O   
1351 N N   . SER   B 128 ? 0.5009 0.5376 0.2783 0.1846  0.0793  0.0035  137 SER   B N   
1352 C CA  . SER   B 128 ? 0.5113 0.5460 0.2765 0.1988  0.0746  0.0005  137 SER   B CA  
1353 C C   . SER   B 128 ? 0.5060 0.5315 0.2583 0.1998  0.0646  -0.0071 137 SER   B C   
1354 O O   . SER   B 128 ? 0.5115 0.5355 0.2590 0.1995  0.0630  -0.0055 137 SER   B O   
1355 C CB  . SER   B 128 ? 0.5165 0.5596 0.2771 0.2151  0.0795  0.0096  137 SER   B CB  
1356 O OG  . SER   B 128 ? 0.5209 0.5722 0.2944 0.2131  0.0887  0.0185  137 SER   B OG  
1357 N N   . PRO   B 129 ? 0.5126 0.5317 0.2584 0.2024  0.0573  -0.0152 138 PRO   B N   
1358 C CA  . PRO   B 129 ? 0.5137 0.5223 0.2478 0.2028  0.0464  -0.0229 138 PRO   B CA  
1359 C C   . PRO   B 129 ? 0.5393 0.5457 0.2573 0.2203  0.0414  -0.0223 138 PRO   B C   
1360 O O   . PRO   B 129 ? 0.5307 0.5432 0.2433 0.2359  0.0443  -0.0184 138 PRO   B O   
1361 C CB  . PRO   B 129 ? 0.5176 0.5219 0.2524 0.2000  0.0408  -0.0311 138 PRO   B CB  
1362 C CG  . PRO   B 129 ? 0.5127 0.5255 0.2532 0.2075  0.0480  -0.0270 138 PRO   B CG  
1363 C CD  . PRO   B 129 ? 0.5061 0.5275 0.2569 0.2040  0.0587  -0.0175 138 PRO   B CD  
1364 N N   . ILE   B 130 ? 0.5503 0.5474 0.2596 0.2182  0.0332  -0.0268 139 ILE   B N   
1365 C CA  . ILE   B 130 ? 0.5728 0.5651 0.2651 0.2343  0.0259  -0.0283 139 ILE   B CA  
1366 C C   . ILE   B 130 ? 0.5878 0.5674 0.2718 0.2343  0.0133  -0.0386 139 ILE   B C   
1367 O O   . ILE   B 130 ? 0.5671 0.5398 0.2567 0.2188  0.0091  -0.0431 139 ILE   B O   
1368 C CB  . ILE   B 130 ? 0.5841 0.5748 0.2725 0.2328  0.0253  -0.0254 139 ILE   B CB  
1369 C CG1 . ILE   B 130 ? 0.5890 0.5934 0.2870 0.2325  0.0377  -0.0149 139 ILE   B CG1 
1370 C CG2 . ILE   B 130 ? 0.5939 0.5780 0.2639 0.2494  0.0161  -0.0288 139 ILE   B CG2 
1371 C CD1 . ILE   B 130 ? 0.5938 0.5966 0.2949 0.2224  0.0382  -0.0130 139 ILE   B CD1 
1372 N N   . LEU   B 131 ? 0.6277 0.6053 0.2994 0.2513  0.0076  -0.0417 140 LEU   B N   
1373 C CA  . LEU   B 131 ? 0.6637 0.6297 0.3285 0.2523  -0.0048 -0.0516 140 LEU   B CA  
1374 C C   . LEU   B 131 ? 0.6811 0.6358 0.3281 0.2650  -0.0169 -0.0567 140 LEU   B C   
1375 O O   . LEU   B 131 ? 0.7088 0.6685 0.3462 0.2808  -0.0146 -0.0527 140 LEU   B O   
1376 C CB  . LEU   B 131 ? 0.6947 0.6666 0.3595 0.2627  -0.0028 -0.0523 140 LEU   B CB  
1377 C CG  . LEU   B 131 ? 0.6924 0.6760 0.3730 0.2549  0.0091  -0.0469 140 LEU   B CG  
1378 C CD1 . LEU   B 131 ? 0.7042 0.6911 0.3827 0.2658  0.0084  -0.0493 140 LEU   B CD1 
1379 C CD2 . LEU   B 131 ? 0.6814 0.6629 0.3761 0.2329  0.0101  -0.0493 140 LEU   B CD2 
1380 N N   . ASP   B 132 ? 0.7005 0.6412 0.3435 0.2592  -0.0298 -0.0654 141 ASP   B N   
1381 C CA  . ASP   B 132 ? 0.7595 0.6869 0.3852 0.2724  -0.0443 -0.0725 141 ASP   B CA  
1382 C C   . ASP   B 132 ? 0.7992 0.7269 0.4192 0.2854  -0.0490 -0.0775 141 ASP   B C   
1383 O O   . ASP   B 132 ? 0.7694 0.7078 0.3995 0.2833  -0.0404 -0.0748 141 ASP   B O   
1384 C CB  . ASP   B 132 ? 0.7716 0.6826 0.3965 0.2585  -0.0566 -0.0787 141 ASP   B CB  
1385 C CG  . ASP   B 132 ? 0.7770 0.6833 0.4113 0.2443  -0.0622 -0.0842 141 ASP   B CG  
1386 O OD1 . ASP   B 132 ? 0.7538 0.6681 0.3941 0.2465  -0.0581 -0.0848 141 ASP   B OD1 
1387 O OD2 . ASP   B 132 ? 0.8396 0.7348 0.4760 0.2302  -0.0703 -0.0873 141 ASP   B OD2 
1388 N N   . LYS   B 133 ? 0.8530 0.7681 0.4578 0.2977  -0.0633 -0.0853 142 LYS   B N   
1389 C CA  . LYS   B 133 ? 0.9196 0.8342 0.5141 0.3157  -0.0694 -0.0905 142 LYS   B CA  
1390 C C   . LYS   B 133 ? 0.8990 0.8113 0.5037 0.3047  -0.0735 -0.0959 142 LYS   B C   
1391 O O   . LYS   B 133 ? 0.8865 0.8013 0.4863 0.3172  -0.0760 -0.0992 142 LYS   B O   
1392 C CB  . LYS   B 133 ? 0.9684 0.8683 0.5432 0.3313  -0.0852 -0.0982 142 LYS   B CB  
1393 C CG  . LYS   B 133 ? 1.0386 0.9457 0.5990 0.3531  -0.0813 -0.0941 142 LYS   B CG  
1394 C CD  . LYS   B 133 ? 1.1092 1.0031 0.6552 0.3598  -0.0923 -0.0980 142 LYS   B CD  
1395 C CE  . LYS   B 133 ? 1.1605 1.0664 0.6957 0.3788  -0.0848 -0.0919 142 LYS   B CE  
1396 N NZ  . LYS   B 133 ? 1.1852 1.0786 0.7003 0.3956  -0.0987 -0.0988 142 LYS   B NZ  
1397 N N   . CYS   B 134 ? 0.8864 0.7941 0.5038 0.2829  -0.0748 -0.0969 143 CYS   B N   
1398 C CA  . CYS   B 134 ? 0.8699 0.7769 0.4986 0.2706  -0.0786 -0.1018 143 CYS   B CA  
1399 C C   . CYS   B 134 ? 0.8053 0.7282 0.4510 0.2595  -0.0630 -0.0953 143 CYS   B C   
1400 O O   . CYS   B 134 ? 0.7637 0.6886 0.4207 0.2478  -0.0640 -0.0983 143 CYS   B O   
1401 C CB  . CYS   B 134 ? 0.9221 0.8154 0.5544 0.2536  -0.0902 -0.1066 143 CYS   B CB  
1402 S SG  . CYS   B 134 ? 0.9968 0.8684 0.6104 0.2653  -0.1117 -0.1159 143 CYS   B SG  
1403 N N   . GLY   B 135 ? 0.7821 0.7160 0.4296 0.2637  -0.0496 -0.0868 144 GLY   B N   
1404 C CA  . GLY   B 135 ? 0.7547 0.7025 0.4180 0.2538  -0.0351 -0.0803 144 GLY   B CA  
1405 C C   . GLY   B 135 ? 0.7270 0.6747 0.4033 0.2317  -0.0314 -0.0784 144 GLY   B C   
1406 O O   . GLY   B 135 ? 0.7011 0.6587 0.3911 0.2220  -0.0218 -0.0752 144 GLY   B O   
1407 N N   . ARG   B 136 ? 0.7345 0.6715 0.4065 0.2243  -0.0388 -0.0802 145 ARG   B N   
1408 C CA  . ARG   B 136 ? 0.7360 0.6732 0.4196 0.2033  -0.0355 -0.0782 145 ARG   B CA  
1409 C C   . ARG   B 136 ? 0.6820 0.6270 0.3688 0.2022  -0.0236 -0.0698 145 ARG   B C   
1410 O O   . ARG   B 136 ? 0.6565 0.6011 0.3327 0.2162  -0.0227 -0.0666 145 ARG   B O   
1411 C CB  . ARG   B 136 ? 0.7838 0.7060 0.4619 0.1953  -0.0491 -0.0833 145 ARG   B CB  
1412 C CG  . ARG   B 136 ? 0.8341 0.7522 0.5164 0.1891  -0.0585 -0.0903 145 ARG   B CG  
1413 C CD  . ARG   B 136 ? 0.8947 0.7969 0.5712 0.1819  -0.0727 -0.0946 145 ARG   B CD  
1414 N NE  . ARG   B 136 ? 1.0021 0.8938 0.6612 0.1998  -0.0805 -0.0965 145 ARG   B NE  
1415 C CZ  . ARG   B 136 ? 1.0259 0.9031 0.6749 0.1999  -0.0905 -0.0980 145 ARG   B CZ  
1416 N NH1 . ARG   B 136 ? 1.0436 0.9143 0.6981 0.1820  -0.0940 -0.0971 145 ARG   B NH1 
1417 N NH2 . ARG   B 136 ? 1.0828 0.9523 0.7155 0.2188  -0.0971 -0.1005 145 ARG   B NH2 
1418 N N   . VAL   B 137 ? 0.6193 0.5721 0.3204 0.1869  -0.0146 -0.0664 146 VAL   B N   
1419 C CA  . VAL   B 137 ? 0.6009 0.5612 0.3065 0.1851  -0.0036 -0.0585 146 VAL   B CA  
1420 C C   . VAL   B 137 ? 0.6117 0.5626 0.3115 0.1785  -0.0092 -0.0586 146 VAL   B C   
1421 O O   . VAL   B 137 ? 0.6345 0.5809 0.3398 0.1625  -0.0130 -0.0613 146 VAL   B O   
1422 C CB  . VAL   B 137 ? 0.5724 0.5439 0.2943 0.1729  0.0076  -0.0550 146 VAL   B CB  
1423 C CG1 . VAL   B 137 ? 0.5671 0.5450 0.2931 0.1716  0.0172  -0.0473 146 VAL   B CG1 
1424 C CG2 . VAL   B 137 ? 0.5780 0.5577 0.3050 0.1800  0.0124  -0.0551 146 VAL   B CG2 
1425 N N   . ILE   B 138 ? 0.6115 0.5606 0.3009 0.1907  -0.0095 -0.0554 147 ILE   B N   
1426 C CA  . ILE   B 138 ? 0.6195 0.5600 0.3018 0.1875  -0.0144 -0.0548 147 ILE   B CA  
1427 C C   . ILE   B 138 ? 0.6055 0.5552 0.2967 0.1799  -0.0033 -0.0475 147 ILE   B C   
1428 O O   . ILE   B 138 ? 0.5895 0.5331 0.2767 0.1752  -0.0065 -0.0467 147 ILE   B O   
1429 C CB  . ILE   B 138 ? 0.6237 0.5570 0.2886 0.2064  -0.0225 -0.0565 147 ILE   B CB  
1430 C CG1 . ILE   B 138 ? 0.6264 0.5721 0.2885 0.2234  -0.0136 -0.0507 147 ILE   B CG1 
1431 C CG2 . ILE   B 138 ? 0.6283 0.5494 0.2846 0.2108  -0.0359 -0.0649 147 ILE   B CG2 
1432 C CD1 . ILE   B 138 ? 0.6609 0.6024 0.3062 0.2417  -0.0195 -0.0511 147 ILE   B CD1 
1433 N N   . GLY   B 139 ? 0.5940 0.5567 0.2974 0.1776  0.0082  -0.0427 148 GLY   B N   
1434 C CA  . GLY   B 139 ? 0.5774 0.5486 0.2915 0.1687  0.0184  -0.0363 148 GLY   B CA  
1435 C C   . GLY   B 139 ? 0.5754 0.5601 0.2989 0.1737  0.0299  -0.0301 148 GLY   B C   
1436 O O   . GLY   B 139 ? 0.5544 0.5420 0.2751 0.1851  0.0303  -0.0305 148 GLY   B O   
1437 N N   . LEU   B 140 ? 0.5511 0.5435 0.2846 0.1669  0.0385  -0.0240 149 LEU   B N   
1438 C CA  . LEU   B 140 ? 0.5387 0.5431 0.2831 0.1693  0.0494  -0.0171 149 LEU   B CA  
1439 C C   . LEU   B 140 ? 0.5479 0.5593 0.2911 0.1774  0.0547  -0.0088 149 LEU   B C   
1440 O O   . LEU   B 140 ? 0.5293 0.5374 0.2691 0.1735  0.0521  -0.0085 149 LEU   B O   
1441 C CB  . LEU   B 140 ? 0.5285 0.5366 0.2881 0.1531  0.0551  -0.0171 149 LEU   B CB  
1442 C CG  . LEU   B 140 ? 0.5204 0.5246 0.2837 0.1434  0.0512  -0.0247 149 LEU   B CG  
1443 C CD1 . LEU   B 140 ? 0.5096 0.5197 0.2879 0.1301  0.0579  -0.0242 149 LEU   B CD1 
1444 C CD2 . LEU   B 140 ? 0.5341 0.5376 0.2927 0.1537  0.0483  -0.0279 149 LEU   B CD2 
1445 N N   . TYR   B 141 ? 0.5172 0.5383 0.2634 0.1879  0.0616  -0.0022 150 TYR   B N   
1446 C CA  . TYR   B 141 ? 0.5255 0.5571 0.2729 0.1968  0.0683  0.0075  150 TYR   B CA  
1447 C C   . TYR   B 141 ? 0.5114 0.5503 0.2755 0.1850  0.0768  0.0137  150 TYR   B C   
1448 O O   . TYR   B 141 ? 0.5132 0.5530 0.2878 0.1775  0.0803  0.0131  150 TYR   B O   
1449 C CB  . TYR   B 141 ? 0.5488 0.5876 0.2922 0.2130  0.0718  0.0121  150 TYR   B CB  
1450 C CG  . TYR   B 141 ? 0.5564 0.6088 0.3029 0.2224  0.0800  0.0237  150 TYR   B CG  
1451 C CD1 . TYR   B 141 ? 0.5550 0.6168 0.3163 0.2183  0.0894  0.0321  150 TYR   B CD1 
1452 C CD2 . TYR   B 141 ? 0.5725 0.6287 0.3076 0.2351  0.0782  0.0265  150 TYR   B CD2 
1453 C CE1 . TYR   B 141 ? 0.5798 0.6548 0.3451 0.2261  0.0969  0.0439  150 TYR   B CE1 
1454 C CE2 . TYR   B 141 ? 0.5792 0.6499 0.3174 0.2443  0.0861  0.0378  150 TYR   B CE2 
1455 C CZ  . TYR   B 141 ? 0.5890 0.6696 0.3429 0.2392  0.0956  0.0470  150 TYR   B CZ  
1456 O OH  . TYR   B 141 ? 0.6305 0.7265 0.3889 0.2472  0.1035  0.0594  150 TYR   B OH  
1457 N N   . GLY   B 142 ? 0.5194 0.5638 0.2863 0.1843  0.0800  0.0197  151 GLY   B N   
1458 C CA  . GLY   B 142 ? 0.5343 0.5867 0.3181 0.1745  0.0881  0.0266  151 GLY   B CA  
1459 C C   . GLY   B 142 ? 0.5366 0.5886 0.3248 0.1643  0.0877  0.0271  151 GLY   B C   
1460 O O   . GLY   B 142 ? 0.5540 0.6133 0.3567 0.1571  0.0942  0.0334  151 GLY   B O   
1461 N N   . ASN   B 143 ? 0.5317 0.5757 0.3084 0.1640  0.0804  0.0214  152 ASN   B N   
1462 C CA  . ASN   B 143 ? 0.5198 0.5638 0.2994 0.1556  0.0799  0.0223  152 ASN   B CA  
1463 C C   . ASN   B 143 ? 0.5201 0.5651 0.2868 0.1680  0.0762  0.0241  152 ASN   B C   
1464 O O   . ASN   B 143 ? 0.5247 0.5603 0.2771 0.1738  0.0684  0.0179  152 ASN   B O   
1465 C CB  . ASN   B 143 ? 0.5243 0.5575 0.3038 0.1409  0.0745  0.0139  152 ASN   B CB  
1466 C CG  . ASN   B 143 ? 0.5347 0.5702 0.3219 0.1303  0.0763  0.0160  152 ASN   B CG  
1467 O OD1 . ASN   B 143 ? 0.5451 0.5905 0.3437 0.1294  0.0829  0.0233  152 ASN   B OD1 
1468 N ND2 . ASN   B 143 ? 0.5281 0.5542 0.3088 0.1225  0.0699  0.0100  152 ASN   B ND2 
1469 N N   . GLY   B 144 ? 0.5130 0.5694 0.2854 0.1718  0.0816  0.0324  153 GLY   B N   
1470 C CA  . GLY   B 144 ? 0.5452 0.6047 0.3061 0.1841  0.0787  0.0344  153 GLY   B CA  
1471 C C   . GLY   B 144 ? 0.5638 0.6378 0.3356 0.1842  0.0857  0.0442  153 GLY   B C   
1472 O O   . GLY   B 144 ? 0.5586 0.6336 0.3435 0.1700  0.0883  0.0453  153 GLY   B O   
1473 N N   . VAL   B 145 ? 0.6062 0.6915 0.3725 0.1998  0.0880  0.0506  154 VAL   B N   
1474 C CA  . VAL   B 145 ? 0.6228 0.7225 0.3961 0.2023  0.0928  0.0593  154 VAL   B CA  
1475 C C   . VAL   B 145 ? 0.6685 0.7862 0.4457 0.2157  0.1008  0.0706  154 VAL   B C   
1476 O O   . VAL   B 145 ? 0.6523 0.7701 0.4188 0.2287  0.1000  0.0698  154 VAL   B O   
1477 C CB  . VAL   B 145 ? 0.6579 0.7510 0.4165 0.2076  0.0848  0.0536  154 VAL   B CB  
1478 C CG1 . VAL   B 145 ? 0.6282 0.7245 0.3698 0.2279  0.0815  0.0535  154 VAL   B CG1 
1479 C CG2 . VAL   B 145 ? 0.7090 0.8088 0.4768 0.2001  0.0866  0.0575  154 VAL   B CG2 
1480 N N   . VAL   B 146 ? 0.6903 0.8233 0.4829 0.2122  0.1081  0.0810  155 VAL   B N   
1481 C CA  . VAL   B 146 ? 0.7348 0.8883 0.5326 0.2242  0.1162  0.0939  155 VAL   B CA  
1482 C C   . VAL   B 146 ? 0.7497 0.9120 0.5358 0.2381  0.1140  0.0951  155 VAL   B C   
1483 O O   . VAL   B 146 ? 0.7485 0.9064 0.5342 0.2319  0.1098  0.0911  155 VAL   B O   
1484 C CB  . VAL   B 146 ? 0.7364 0.9008 0.5575 0.2119  0.1241  0.1042  155 VAL   B CB  
1485 C CG1 . VAL   B 146 ? 0.7671 0.9540 0.5956 0.2223  0.1324  0.1188  155 VAL   B CG1 
1486 C CG2 . VAL   B 146 ? 0.7658 0.9204 0.5966 0.2001  0.1255  0.1020  155 VAL   B CG2 
1487 N N   . ILE   B 147 ? 0.8110 0.9842 0.5864 0.2570  0.1157  0.0994  156 ILE   B N   
1488 C CA  . ILE   B 147 ? 0.8501 1.0297 0.6108 0.2725  0.1119  0.0983  156 ILE   B CA  
1489 C C   . ILE   B 147 ? 0.9153 1.1217 0.6866 0.2801  0.1212  0.1129  156 ILE   B C   
1490 O O   . ILE   B 147 ? 0.9042 1.1203 0.6946 0.2704  0.1292  0.1228  156 ILE   B O   
1491 C CB  . ILE   B 147 ? 0.9005 1.0709 0.6381 0.2894  0.1048  0.0899  156 ILE   B CB  
1492 C CG1 . ILE   B 147 ? 0.9084 1.0853 0.6443 0.2993  0.1097  0.0947  156 ILE   B CG1 
1493 C CG2 . ILE   B 147 ? 0.8697 1.0143 0.5972 0.2808  0.0939  0.0753  156 ILE   B CG2 
1494 C CD1 . ILE   B 147 ? 0.9026 1.0751 0.6156 0.3194  0.1032  0.0880  156 ILE   B CD1 
1495 N N   . LYS   B 148 ? 1.0203 1.2376 0.7804 0.2955  0.1196  0.1140  157 LYS   B N   
1496 C CA  . LYS   B 148 ? 1.1042 1.3495 0.8736 0.3041  0.1281  0.1281  157 LYS   B CA  
1497 C C   . LYS   B 148 ? 1.1599 1.4202 0.9391 0.3076  0.1379  0.1405  157 LYS   B C   
1498 O O   . LYS   B 148 ? 1.2024 1.4789 1.0023 0.2992  0.1463  0.1532  157 LYS   B O   
1499 C CB  . LYS   B 148 ? 1.1686 1.4216 0.9187 0.3252  0.1238  0.1252  157 LYS   B CB  
1500 C CG  . LYS   B 148 ? 1.2299 1.4673 0.9695 0.3225  0.1134  0.1132  157 LYS   B CG  
1501 C CD  . LYS   B 148 ? 1.2801 1.5150 0.9951 0.3440  0.1056  0.1056  157 LYS   B CD  
1502 C CE  . LYS   B 148 ? 1.3268 1.5898 1.0405 0.3619  0.1112  0.1153  157 LYS   B CE  
1503 N NZ  . LYS   B 148 ? 1.3469 1.6164 1.0664 0.3577  0.1098  0.1161  157 LYS   B NZ  
1504 N N   . ASN   B 149 ? 1.1637 1.4170 0.9294 0.3180  0.1362  0.1366  158 ASN   B N   
1505 C CA  . ASN   B 149 ? 1.1600 1.4271 0.9294 0.3262  0.1445  0.1475  158 ASN   B CA  
1506 C C   . ASN   B 149 ? 1.0977 1.3620 0.8885 0.3077  0.1504  0.1541  158 ASN   B C   
1507 O O   . ASN   B 149 ? 1.1231 1.3981 0.9189 0.3126  0.1574  0.1642  158 ASN   B O   
1508 C CB  . ASN   B 149 ? 1.2268 1.4826 0.9755 0.3404  0.1394  0.1390  158 ASN   B CB  
1509 C CG  . ASN   B 149 ? 1.2324 1.4737 0.9585 0.3509  0.1279  0.1243  158 ASN   B CG  
1510 O OD1 . ASN   B 149 ? 1.1548 1.3986 0.8780 0.3523  0.1246  0.1220  158 ASN   B OD1 
1511 N ND2 . ASN   B 149 ? 1.2614 1.4868 0.9714 0.3582  0.1211  0.1142  158 ASN   B ND2 
1512 N N   . GLY   B 150 ? 1.0086 1.2570 0.8095 0.2882  0.1467  0.1474  159 GLY   B N   
1513 C CA  . GLY   B 150 ? 0.9062 1.1466 0.7247 0.2705  0.1498  0.1499  159 GLY   B CA  
1514 C C   . GLY   B 150 ? 0.8560 1.0758 0.6649 0.2687  0.1449  0.1391  159 GLY   B C   
1515 O O   . GLY   B 150 ? 0.8065 1.0168 0.6279 0.2539  0.1458  0.1382  159 GLY   B O   
1516 N N   A SER   B 151 ? 0.8663 1.0800 0.6536 0.2840  0.1393  0.1309  160 SER   B N   
1517 N N   B SER   B 151 ? 0.8496 1.0634 0.6370 0.2840  0.1394  0.1310  160 SER   B N   
1518 N N   C SER   B 151 ? 0.8687 1.0823 0.6560 0.2840  0.1393  0.1308  160 SER   B N   
1519 N N   D SER   B 151 ? 0.8635 1.0772 0.6509 0.2840  0.1394  0.1310  160 SER   B N   
1520 C CA  A SER   B 151 ? 0.8429 1.0381 0.6182 0.2855  0.1334  0.1198  160 SER   B CA  
1521 C CA  B SER   B 151 ? 0.8343 1.0295 0.6102 0.2851  0.1336  0.1201  160 SER   B CA  
1522 C CA  C SER   B 151 ? 0.8410 1.0359 0.6162 0.2854  0.1333  0.1197  160 SER   B CA  
1523 C CA  D SER   B 151 ? 0.8306 1.0256 0.6064 0.2850  0.1336  0.1200  160 SER   B CA  
1524 C C   A SER   B 151 ? 0.8215 0.9946 0.5956 0.2702  0.1250  0.1060  160 SER   B C   
1525 C C   B SER   B 151 ? 0.8129 0.9862 0.5875 0.2700  0.1252  0.1063  160 SER   B C   
1526 C C   C SER   B 151 ? 0.8179 0.9907 0.5920 0.2700  0.1249  0.1059  160 SER   B C   
1527 C C   D SER   B 151 ? 0.8120 0.9849 0.5865 0.2698  0.1251  0.1061  160 SER   B C   
1528 O O   A SER   B 151 ? 0.8037 0.9755 0.5813 0.2625  0.1226  0.1040  160 SER   B O   
1529 O O   B SER   B 151 ? 0.8034 0.9758 0.5819 0.2622  0.1230  0.1045  160 SER   B O   
1530 O O   C SER   B 151 ? 0.8000 0.9719 0.5775 0.2626  0.1226  0.1039  160 SER   B O   
1531 O O   D SER   B 151 ? 0.7950 0.9672 0.5730 0.2625  0.1228  0.1042  160 SER   B O   
1532 C CB  A SER   B 151 ? 0.8615 1.0583 0.6144 0.3072  0.1292  0.1157  160 SER   B CB  
1533 C CB  B SER   B 151 ? 0.8481 1.0447 0.6017 0.3066  0.1296  0.1160  160 SER   B CB  
1534 C CB  C SER   B 151 ? 0.8608 1.0575 0.6137 0.3071  0.1292  0.1157  160 SER   B CB  
1535 C CB  D SER   B 151 ? 0.8455 1.0420 0.5991 0.3066  0.1295  0.1160  160 SER   B CB  
1536 O OG  A SER   B 151 ? 0.8705 1.0512 0.6130 0.3091  0.1237  0.1060  160 SER   B OG  
1537 O OG  B SER   B 151 ? 0.8533 1.0517 0.5955 0.3148  0.1245  0.1117  160 SER   B OG  
1538 O OG  C SER   B 151 ? 0.8709 1.0516 0.6133 0.3092  0.1237  0.1060  160 SER   B OG  
1539 O OG  D SER   B 151 ? 0.8468 1.0452 0.5891 0.3147  0.1245  0.1117  160 SER   B OG  
1540 N N   A TYR   B 152 ? 0.7974 0.9546 0.5662 0.2668  0.1205  0.0971  161 TYR   B N   
1541 N N   B TYR   B 152 ? 0.7961 0.9533 0.5649 0.2668  0.1205  0.0971  161 TYR   B N   
1542 N N   C TYR   B 152 ? 0.7845 0.9410 0.5545 0.2652  0.1206  0.0969  161 TYR   B N   
1543 N N   D TYR   B 152 ? 0.7819 0.9384 0.5519 0.2652  0.1206  0.0969  161 TYR   B N   
1544 C CA  A TYR   B 152 ? 0.7845 0.9214 0.5528 0.2519  0.1131  0.0845  161 TYR   B CA  
1545 C CA  B TYR   B 152 ? 0.7776 0.9146 0.5460 0.2519  0.1131  0.0845  161 TYR   B CA  
1546 C CA  C TYR   B 152 ? 0.7704 0.9068 0.5397 0.2503  0.1130  0.0843  161 TYR   B CA  
1547 C CA  D TYR   B 152 ? 0.7707 0.9071 0.5401 0.2503  0.1130  0.0843  161 TYR   B CA  
1548 C C   A TYR   B 152 ? 0.7643 0.8872 0.5114 0.2612  0.1027  0.0722  161 TYR   B C   
1549 C C   B TYR   B 152 ? 0.7619 0.8848 0.5090 0.2612  0.1028  0.0722  161 TYR   B C   
1550 C C   C TYR   B 152 ? 0.7560 0.8778 0.5045 0.2592  0.1029  0.0718  161 TYR   B C   
1551 C C   D TYR   B 152 ? 0.7561 0.8780 0.5046 0.2592  0.1029  0.0718  161 TYR   B C   
1552 O O   A TYR   B 152 ? 0.7631 0.8875 0.4983 0.2762  0.1015  0.0715  161 TYR   B O   
1553 O O   B TYR   B 152 ? 0.7684 0.8929 0.5036 0.2763  0.1016  0.0716  161 TYR   B O   
1554 O O   C TYR   B 152 ? 0.7513 0.8726 0.4902 0.2712  0.1018  0.0705  161 TYR   B O   
1555 O O   D TYR   B 152 ? 0.7501 0.8714 0.4890 0.2712  0.1018  0.0705  161 TYR   B O   
1556 C CB  A TYR   B 152 ? 0.7864 0.9169 0.5668 0.2398  0.1159  0.0840  161 TYR   B CB  
1557 C CB  B TYR   B 152 ? 0.7802 0.9108 0.5607 0.2398  0.1159  0.0840  161 TYR   B CB  
1558 C CB  C TYR   B 152 ? 0.7556 0.8855 0.5396 0.2351  0.1159  0.0838  161 TYR   B CB  
1559 C CB  D TYR   B 152 ? 0.7557 0.8856 0.5397 0.2351  0.1159  0.0838  161 TYR   B CB  
1560 C CG  A TYR   B 152 ? 0.7914 0.9053 0.5751 0.2229  0.1102  0.0732  161 TYR   B CG  
1561 C CG  B TYR   B 152 ? 0.7829 0.8968 0.5666 0.2229  0.1102  0.0733  161 TYR   B CG  
1562 C CG  C TYR   B 152 ? 0.7483 0.8635 0.5374 0.2171  0.1110  0.0744  161 TYR   B CG  
1563 C CG  D TYR   B 152 ? 0.7491 0.8642 0.5382 0.2171  0.1109  0.0744  161 TYR   B CG  
1564 C CD1 A TYR   B 152 ? 0.7816 0.8957 0.5784 0.2081  0.1117  0.0745  161 TYR   B CD1 
1565 C CD1 B TYR   B 152 ? 0.7772 0.8913 0.5740 0.2081  0.1117  0.0745  161 TYR   B CD1 
1566 C CD1 C TYR   B 152 ? 0.7406 0.8584 0.5412 0.2051  0.1125  0.0768  161 TYR   B CD1 
1567 C CD1 D TYR   B 152 ? 0.7417 0.8595 0.5424 0.2051  0.1125  0.0768  161 TYR   B CD1 
1568 C CD2 A TYR   B 152 ? 0.7987 0.8976 0.5723 0.2220  0.1032  0.0620  161 TYR   B CD2 
1569 C CD2 B TYR   B 152 ? 0.7907 0.8897 0.5644 0.2220  0.1032  0.0620  161 TYR   B CD2 
1570 C CD2 C TYR   B 152 ? 0.7397 0.8393 0.5227 0.2119  0.1049  0.0634  161 TYR   B CD2 
1571 C CD2 D TYR   B 152 ? 0.7398 0.8394 0.5228 0.2119  0.1049  0.0634  161 TYR   B CD2 
1572 C CE1 A TYR   B 152 ? 0.7806 0.8808 0.5797 0.1932  0.1068  0.0649  161 TYR   B CE1 
1573 C CE1 B TYR   B 152 ? 0.7747 0.8749 0.5737 0.1932  0.1068  0.0650  161 TYR   B CE1 
1574 C CE1 C TYR   B 152 ? 0.7233 0.8286 0.5280 0.1893  0.1082  0.0684  161 TYR   B CE1 
1575 C CE1 D TYR   B 152 ? 0.7236 0.8289 0.5283 0.1893  0.1082  0.0684  161 TYR   B CE1 
1576 C CE2 A TYR   B 152 ? 0.7934 0.8790 0.5701 0.2066  0.0984  0.0529  161 TYR   B CE2 
1577 C CE2 B TYR   B 152 ? 0.7865 0.8721 0.5633 0.2065  0.0984  0.0530  161 TYR   B CE2 
1578 C CE2 C TYR   B 152 ? 0.7234 0.8114 0.5111 0.1958  0.1009  0.0555  161 TYR   B CE2 
1579 C CE2 D TYR   B 152 ? 0.7229 0.8109 0.5106 0.1957  0.1009  0.0555  161 TYR   B CE2 
1580 C CZ  A TYR   B 152 ? 0.7819 0.8684 0.5710 0.1924  0.1004  0.0545  161 TYR   B CZ  
1581 C CZ  B TYR   B 152 ? 0.7781 0.8646 0.5673 0.1924  0.1004  0.0545  161 TYR   B CZ  
1582 C CZ  C TYR   B 152 ? 0.7184 0.8091 0.5165 0.1846  0.1026  0.0580  161 TYR   B CZ  
1583 C CZ  D TYR   B 152 ? 0.7186 0.8093 0.5167 0.1845  0.1026  0.0579  161 TYR   B CZ  
1584 O OH  A TYR   B 152 ? 0.7819 0.8565 0.5736 0.1777  0.0960  0.0459  161 TYR   B OH  
1585 O OH  B TYR   B 152 ? 0.7744 0.8490 0.5661 0.1778  0.0960  0.0459  161 TYR   B OH  
1586 O OH  C TYR   B 152 ? 0.6704 0.7506 0.4725 0.1692  0.0989  0.0504  161 TYR   B OH  
1587 O OH  D TYR   B 152 ? 0.6665 0.7466 0.4685 0.1692  0.0989  0.0504  161 TYR   B OH  
1588 N N   . VAL   B 153 ? 0.7385 0.8481 0.4810 0.2525  0.0951  0.0630  162 VAL   B N   
1589 C CA  . VAL   B 153 ? 0.6966 0.7898 0.4206 0.2580  0.0839  0.0507  162 VAL   B CA  
1590 C C   . VAL   B 153 ? 0.6371 0.7138 0.3662 0.2392  0.0790  0.0420  162 VAL   B C   
1591 O O   . VAL   B 153 ? 0.6052 0.6808 0.3427 0.2264  0.0796  0.0423  162 VAL   B O   
1592 C CB  . VAL   B 153 ? 0.6863 0.7807 0.3976 0.2684  0.0786  0.0492  162 VAL   B CB  
1593 C CG1 . VAL   B 153 ? 0.6795 0.7558 0.3716 0.2746  0.0660  0.0369  162 VAL   B CG1 
1594 C CG2 . VAL   B 153 ? 0.7165 0.8314 0.4258 0.2859  0.0853  0.0595  162 VAL   B CG2 
1595 N N   . SER   B 154 ? 0.6223 0.6883 0.3472 0.2377  0.0748  0.0349  163 SER   B N   
1596 C CA  . SER   B 154 ? 0.5857 0.6383 0.3161 0.2204  0.0710  0.0272  163 SER   B CA  
1597 C C   . SER   B 154 ? 0.5858 0.6223 0.3011 0.2209  0.0590  0.0167  163 SER   B C   
1598 O O   . SER   B 154 ? 0.5950 0.6275 0.2956 0.2353  0.0530  0.0131  163 SER   B O   
1599 C CB  . SER   B 154 ? 0.5701 0.6220 0.3058 0.2188  0.0736  0.0261  163 SER   B CB  
1600 O OG  . SER   B 154 ? 0.5367 0.5759 0.2747 0.2048  0.0684  0.0172  163 SER   B OG  
1601 N N   . ALA   B 155 ? 0.5738 0.6009 0.2929 0.2053  0.0554  0.0119  164 ALA   B N   
1602 C CA  . ALA   B 155 ? 0.5693 0.5794 0.2776 0.2008  0.0441  0.0021  164 ALA   B CA  
1603 C C   . ALA   B 155 ? 0.5782 0.5832 0.2850 0.2019  0.0416  -0.0029 164 ALA   B C   
1604 O O   . ALA   B 155 ? 0.5946 0.6075 0.3128 0.1987  0.0492  0.0004  164 ALA   B O   
1605 C CB  . ALA   B 155 ? 0.5689 0.5729 0.2850 0.1818  0.0432  -0.0002 164 ALA   B CB  
1606 N N   . ILE   B 156 ? 0.5919 0.5836 0.2855 0.2059  0.0306  -0.0107 165 ILE   B N   
1607 C CA  . ILE   B 156 ? 0.6098 0.5925 0.3035 0.1997  0.0254  -0.0178 165 ILE   B CA  
1608 C C   . ILE   B 156 ? 0.5940 0.5700 0.2958 0.1793  0.0236  -0.0211 165 ILE   B C   
1609 O O   . ILE   B 156 ? 0.5987 0.5622 0.2922 0.1750  0.0142  -0.0260 165 ILE   B O   
1610 C CB  . ILE   B 156 ? 0.6351 0.6060 0.3117 0.2120  0.0133  -0.0248 165 ILE   B CB  
1611 C CG1 . ILE   B 156 ? 0.6531 0.6320 0.3200 0.2335  0.0151  -0.0212 165 ILE   B CG1 
1612 C CG2 . ILE   B 156 ? 0.6361 0.6000 0.3144 0.2064  0.0083  -0.0314 165 ILE   B CG2 
1613 C CD1 . ILE   B 156 ? 0.6795 0.6469 0.3287 0.2476  0.0028  -0.0285 165 ILE   B CD1 
1614 N N   . THR   B 157 ? 0.5815 0.5652 0.2985 0.1675  0.0321  -0.0185 166 THR   B N   
1615 C CA  . THR   B 157 ? 0.5567 0.5370 0.2823 0.1486  0.0320  -0.0209 166 THR   B CA  
1616 C C   . THR   B 157 ? 0.5667 0.5403 0.2928 0.1413  0.0265  -0.0279 166 THR   B C   
1617 O O   . THR   B 157 ? 0.5365 0.5164 0.2701 0.1420  0.0312  -0.0282 166 THR   B O   
1618 C CB  . THR   B 157 ? 0.5482 0.5402 0.2893 0.1407  0.0430  -0.0153 166 THR   B CB  
1619 O OG1 . THR   B 157 ? 0.5306 0.5295 0.2721 0.1470  0.0475  -0.0085 166 THR   B OG1 
1620 C CG2 . THR   B 157 ? 0.5340 0.5236 0.2832 0.1226  0.0430  -0.0183 166 THR   B CG2 
1621 N N   . GLN   B 158 ? 0.5474 0.5094 0.2672 0.1337  0.0173  -0.0328 167 GLN   B N   
1622 C CA  . GLN   B 158 ? 0.5563 0.5120 0.2768 0.1253  0.0109  -0.0390 167 GLN   B CA  
1623 C C   . GLN   B 158 ? 0.5879 0.5429 0.3159 0.1066  0.0115  -0.0397 167 GLN   B C   
1624 O O   . GLN   B 158 ? 0.5637 0.5157 0.2892 0.1025  0.0110  -0.0374 167 GLN   B O   
1625 C CB  . GLN   B 158 ? 0.5681 0.5104 0.2743 0.1333  -0.0016 -0.0438 167 GLN   B CB  
1626 C CG  . GLN   B 158 ? 0.5748 0.5113 0.2821 0.1265  -0.0087 -0.0498 167 GLN   B CG  
1627 C CD  . GLN   B 158 ? 0.5705 0.5175 0.2877 0.1274  -0.0024 -0.0507 167 GLN   B CD  
1628 O OE1 . GLN   B 158 ? 0.5515 0.5092 0.2809 0.1199  0.0073  -0.0480 167 GLN   B OE1 
1629 N NE2 . GLN   B 158 ? 0.5776 0.5203 0.2893 0.1357  -0.0090 -0.0551 167 GLN   B NE2 
1630 N N   . GLY   B 159 ? 0.6186 0.5778 0.3559 0.0964  0.0133  -0.0425 168 GLY   B N   
1631 C CA  . GLY   B 159 ? 0.6693 0.6285 0.4127 0.0791  0.0130  -0.0437 168 GLY   B CA  
1632 C C   . GLY   B 159 ? 0.7359 0.6833 0.4718 0.0734  0.0014  -0.0476 168 GLY   B C   
1633 O O   . GLY   B 159 ? 0.7728 0.7111 0.4989 0.0829  -0.0067 -0.0500 168 GLY   B O   
1634 N N   A LYS   B 160 ? 0.7579 0.7054 0.4983 0.0577  0.0005  -0.0480 169 LYS   B N   
1635 N N   B LYS   B 160 ? 0.7579 0.7054 0.4983 0.0577  0.0005  -0.0480 169 LYS   B N   
1636 N N   C LYS   B 160 ? 0.7680 0.7160 0.5090 0.0577  0.0007  -0.0482 169 LYS   B N   
1637 N N   D LYS   B 160 ? 0.7680 0.7160 0.5090 0.0577  0.0007  -0.0482 169 LYS   B N   
1638 C CA  A LYS   B 160 ? 0.7841 0.7221 0.5204 0.0486  -0.0098 -0.0507 169 LYS   B CA  
1639 C CA  B LYS   B 160 ? 0.7841 0.7221 0.5204 0.0486  -0.0098 -0.0507 169 LYS   B CA  
1640 C CA  C LYS   B 160 ? 0.8022 0.7403 0.5386 0.0485  -0.0097 -0.0506 169 LYS   B CA  
1641 C CA  D LYS   B 160 ? 0.8022 0.7403 0.5386 0.0485  -0.0097 -0.0506 169 LYS   B CA  
1642 C C   A LYS   B 160 ? 0.7968 0.7437 0.5436 0.0400  -0.0080 -0.0536 169 LYS   B C   
1643 C C   B LYS   B 160 ? 0.7968 0.7437 0.5436 0.0400  -0.0080 -0.0536 169 LYS   B C   
1644 C C   C LYS   B 160 ? 0.8093 0.7559 0.5561 0.0390  -0.0082 -0.0535 169 LYS   B C   
1645 C C   D LYS   B 160 ? 0.8093 0.7559 0.5561 0.0390  -0.0082 -0.0535 169 LYS   B C   
1646 O O   A LYS   B 160 ? 0.7691 0.7290 0.5266 0.0349  0.0016  -0.0529 169 LYS   B O   
1647 O O   B LYS   B 160 ? 0.7691 0.7290 0.5266 0.0349  0.0016  -0.0529 169 LYS   B O   
1648 O O   C LYS   B 160 ? 0.7844 0.7438 0.5419 0.0323  0.0010  -0.0527 169 LYS   B O   
1649 O O   D LYS   B 160 ? 0.7844 0.7438 0.5419 0.0323  0.0010  -0.0527 169 LYS   B O   
1650 C CB  A LYS   B 160 ? 0.7919 0.7248 0.5256 0.0368  -0.0121 -0.0481 169 LYS   B CB  
1651 C CB  B LYS   B 160 ? 0.7919 0.7248 0.5256 0.0368  -0.0121 -0.0481 169 LYS   B CB  
1652 C CB  C LYS   B 160 ? 0.8232 0.7564 0.5566 0.0381  -0.0112 -0.0477 169 LYS   B CB  
1653 C CB  D LYS   B 160 ? 0.8232 0.7564 0.5566 0.0381  -0.0112 -0.0477 169 LYS   B CB  
1654 C CG  A LYS   B 160 ? 0.8034 0.7240 0.5312 0.0286  -0.0241 -0.0496 169 LYS   B CG  
1655 C CG  B LYS   B 160 ? 0.8034 0.7240 0.5312 0.0286  -0.0241 -0.0496 169 LYS   B CG  
1656 C CG  C LYS   B 160 ? 0.8376 0.7642 0.5616 0.0476  -0.0120 -0.0450 169 LYS   B CG  
1657 C CG  D LYS   B 160 ? 0.8376 0.7642 0.5616 0.0476  -0.0120 -0.0450 169 LYS   B CG  
1658 C CD  A LYS   B 160 ? 0.8021 0.7189 0.5282 0.0157  -0.0257 -0.0464 169 LYS   B CD  
1659 C CD  B LYS   B 160 ? 0.8021 0.7189 0.5282 0.0157  -0.0257 -0.0464 169 LYS   B CD  
1660 C CD  C LYS   B 160 ? 0.8499 0.7729 0.5718 0.0374  -0.0128 -0.0421 169 LYS   B CD  
1661 C CD  D LYS   B 160 ? 0.8499 0.7729 0.5718 0.0374  -0.0128 -0.0421 169 LYS   B CD  
1662 C CE  A LYS   B 160 ? 0.8083 0.7142 0.5307 0.0056  -0.0371 -0.0468 169 LYS   B CE  
1663 C CE  B LYS   B 160 ? 0.8083 0.7142 0.5307 0.0056  -0.0371 -0.0468 169 LYS   B CE  
1664 C CE  C LYS   B 160 ? 0.8717 0.7817 0.5802 0.0459  -0.0202 -0.0409 169 LYS   B CE  
1665 C CE  D LYS   B 160 ? 0.8717 0.7817 0.5802 0.0459  -0.0202 -0.0409 169 LYS   B CE  
1666 N NZ  A LYS   B 160 ? 0.8116 0.7178 0.5349 -0.0090 -0.0366 -0.0430 169 LYS   B NZ  
1667 N NZ  B LYS   B 160 ? 0.8116 0.7178 0.5349 -0.0090 -0.0366 -0.0430 169 LYS   B NZ  
1668 N NZ  C LYS   B 160 ? 0.8758 0.7786 0.5804 0.0344  -0.0244 -0.0389 169 LYS   B NZ  
1669 N NZ  D LYS   B 160 ? 0.8758 0.7786 0.5804 0.0344  -0.0244 -0.0389 169 LYS   B NZ  
1670 N N   . ARG   B 161 ? 0.8270 0.7672 0.5710 0.0390  -0.0174 -0.0570 170 ARG   B N   
1671 C CA  . ARG   B 161 ? 0.8863 0.8351 0.6404 0.0297  -0.0174 -0.0598 170 ARG   B CA  
1672 C C   . ARG   B 161 ? 0.9852 0.9304 0.7401 0.0133  -0.0233 -0.0586 170 ARG   B C   
1673 O O   . ARG   B 161 ? 1.0352 0.9654 0.7804 0.0133  -0.0337 -0.0581 170 ARG   B O   
1674 C CB  . ARG   B 161 ? 0.9113 0.8559 0.6625 0.0402  -0.0240 -0.0640 170 ARG   B CB  
1675 C CG  . ARG   B 161 ? 0.9060 0.8603 0.6677 0.0332  -0.0242 -0.0673 170 ARG   B CG  
1676 C CD  . ARG   B 161 ? 0.9162 0.8638 0.6735 0.0427  -0.0335 -0.0719 170 ARG   B CD  
1677 N NE  . ARG   B 161 ? 0.9289 0.8872 0.6975 0.0343  -0.0334 -0.0747 170 ARG   B NE  
1678 C CZ  . ARG   B 161 ? 0.9217 0.8898 0.6966 0.0410  -0.0294 -0.0778 170 ARG   B CZ  
1679 N NH1 . ARG   B 161 ? 0.8561 0.8244 0.6269 0.0564  -0.0250 -0.0783 170 ARG   B NH1 
1680 N NH2 . ARG   B 161 ? 0.9586 0.9371 0.7442 0.0318  -0.0297 -0.0802 170 ARG   B NH2 
1681 N N   . GLU   B 162 ? 1.0528 1.0111 0.8186 0.0003  -0.0174 -0.0579 171 GLU   B N   
1682 C CA  . GLU   B 162 ? 1.1067 1.0649 0.8747 -0.0161 -0.0219 -0.0558 171 GLU   B CA  
1683 C C   . GLU   B 162 ? 1.0973 1.0610 0.8727 -0.0221 -0.0268 -0.0585 171 GLU   B C   
1684 O O   . GLU   B 162 ? 1.1427 1.1051 0.9199 -0.0349 -0.0329 -0.0567 171 GLU   B O   
1685 C CB  . GLU   B 162 ? 1.1867 1.1576 0.9613 -0.0260 -0.0119 -0.0531 171 GLU   B CB  
1686 C CG  . GLU   B 162 ? 1.2458 1.2131 1.0150 -0.0205 -0.0067 -0.0506 171 GLU   B CG  
1687 C CD  . GLU   B 162 ? 1.3277 1.2827 1.0874 -0.0260 -0.0127 -0.0468 171 GLU   B CD  
1688 O OE1 . GLU   B 162 ? 1.2883 1.2490 1.0500 -0.0339 -0.0074 -0.0441 171 GLU   B OE1 
1689 O OE2 . GLU   B 162 ? 1.4393 1.3786 1.1894 -0.0217 -0.0231 -0.0468 171 GLU   B OE2 
1690 S S   A DMS   C .   ? 0.7325 0.8424 0.5617 0.1914  0.1235  0.0804  201 DMS   B S   
1691 S S   B DMS   C .   ? 0.7326 0.8425 0.5617 0.1915  0.1235  0.0804  201 DMS   B S   
1692 O O   A DMS   C .   ? 0.7297 0.8524 0.5568 0.1998  0.1261  0.0889  201 DMS   B O   
1693 O O   B DMS   C .   ? 0.7339 0.8565 0.5608 0.1998  0.1261  0.0888  201 DMS   B O   
1694 C C1  A DMS   C .   ? 0.7305 0.8283 0.5639 0.1733  0.1181  0.0697  201 DMS   B C1  
1695 C C1  B DMS   C .   ? 0.7259 0.8238 0.5594 0.1733  0.1181  0.0698  201 DMS   B C1  
1696 C C2  A DMS   C .   ? 0.7444 0.8438 0.5519 0.2023  0.1156  0.0688  201 DMS   B C2  
1697 C C2  B DMS   C .   ? 0.7419 0.8412 0.5493 0.2023  0.1156  0.0688  201 DMS   B C2  
1698 S S   A DMS   D .   ? 3.3032 3.3516 3.2206 0.0232  0.0978  -0.0386 202 DMS   B S   
1699 S S   B DMS   D .   ? 3.2956 3.3441 3.2131 0.0232  0.0978  -0.0386 202 DMS   B S   
1700 O O   A DMS   D .   ? 3.2687 3.3185 3.1749 0.0252  0.0968  -0.0407 202 DMS   B O   
1701 O O   B DMS   D .   ? 3.2618 3.3116 3.1680 0.0252  0.0968  -0.0407 202 DMS   B O   
1702 C C1  A DMS   D .   ? 3.2722 3.3203 3.1991 0.0271  0.0988  -0.0422 202 DMS   B C1  
1703 C C1  B DMS   D .   ? 3.2679 3.3161 3.1949 0.0271  0.0988  -0.0422 202 DMS   B C1  
1704 C C2  A DMS   D .   ? 3.2626 3.3082 3.1836 0.0304  0.1001  -0.0264 202 DMS   B C2  
1705 C C2  B DMS   D .   ? 3.2592 3.3049 3.1803 0.0304  0.1001  -0.0264 202 DMS   B C2  
1706 S S   A DMS   E .   ? 0.7613 0.8467 0.5841 0.1540  0.1046  0.0553  203 DMS   B S   
1707 S S   B DMS   E .   ? 0.7603 0.8456 0.5833 0.1537  0.1046  0.0553  203 DMS   B S   
1708 O O   A DMS   E .   ? 0.7424 0.8283 0.5647 0.1492  0.1021  0.0549  203 DMS   B O   
1709 O O   B DMS   E .   ? 0.7522 0.8380 0.5747 0.1489  0.1021  0.0548  203 DMS   B O   
1710 C C1  A DMS   E .   ? 0.7604 0.8330 0.5878 0.1387  0.1016  0.0452  203 DMS   B C1  
1711 C C1  B DMS   E .   ? 0.7557 0.8283 0.5832 0.1387  0.1016  0.0451  203 DMS   B C1  
1712 C C2  A DMS   E .   ? 0.7577 0.8558 0.6013 0.1506  0.1139  0.0673  203 DMS   B C2  
1713 C C2  B DMS   E .   ? 0.7548 0.8529 0.5985 0.1504  0.1139  0.0673  203 DMS   B C2  
1714 N N1  C A1BG8 F .   ? 0.7176 0.8603 0.5856 0.1800  0.1384  0.1105  204 A1BG8 B N1  
1715 N N1  D A1BG8 F .   ? 0.7186 0.8613 0.5867 0.1800  0.1384  0.1106  204 A1BG8 B N1  
1716 N N3  C A1BG8 F .   ? 0.6041 0.6681 0.4476 0.1140  0.1011  0.0367  204 A1BG8 B N3  
1717 N N3  D A1BG8 F .   ? 0.6027 0.6667 0.4462 0.1140  0.1011  0.0367  204 A1BG8 B N3  
1718 C C4  C A1BG8 F .   ? 0.7027 0.8215 0.5457 0.1808  0.1263  0.0874  204 A1BG8 B C4  
1719 C C4  D A1BG8 F .   ? 0.7033 0.8221 0.5463 0.1808  0.1263  0.0874  204 A1BG8 B C4  
1720 C C5  C A1BG8 F .   ? 0.6877 0.7946 0.5167 0.1850  0.1207  0.0767  204 A1BG8 B C5  
1721 C C5  D A1BG8 F .   ? 0.6876 0.7945 0.5166 0.1850  0.1207  0.0767  204 A1BG8 B C5  
1722 C C6  C A1BG8 F .   ? 0.6965 0.8068 0.5127 0.2014  0.1206  0.0783  204 A1BG8 B C6  
1723 C C6  D A1BG8 F .   ? 0.6968 0.8071 0.5130 0.2014  0.1206  0.0783  204 A1BG8 B C6  
1724 C C7  C A1BG8 F .   ? 0.6985 0.7981 0.5020 0.2059  0.1148  0.0685  204 A1BG8 B C7  
1725 C C7  D A1BG8 F .   ? 0.6989 0.7986 0.5024 0.2059  0.1148  0.0685  204 A1BG8 B C7  
1726 C C8  C A1BG8 F .   ? 0.6833 0.7697 0.4871 0.1938  0.1093  0.0574  204 A1BG8 B C8  
1727 C C8  D A1BG8 F .   ? 0.6827 0.7691 0.4865 0.1938  0.1093  0.0574  204 A1BG8 B C8  
1728 C C10 C A1BG8 F .   ? 0.6717 0.7648 0.4997 0.1735  0.1152  0.0650  204 A1BG8 B C10 
1729 C C10 D A1BG8 F .   ? 0.6718 0.7649 0.4998 0.1735  0.1152  0.0650  204 A1BG8 B C10 
1730 C C13 C A1BG8 F .   ? 0.6168 0.6820 0.4499 0.1273  0.1006  0.0385  204 A1BG8 B C13 
1731 C C13 D A1BG8 F .   ? 0.6160 0.6812 0.4491 0.1273  0.1006  0.0385  204 A1BG8 B C13 
1732 C C15 C A1BG8 F .   ? 0.6204 0.6984 0.4779 0.1242  0.1109  0.0515  204 A1BG8 B C15 
1733 C C15 D A1BG8 F .   ? 0.6209 0.6989 0.4784 0.1242  0.1109  0.0515  204 A1BG8 B C15 
1734 C C1  C A1BG8 F .   ? 0.7175 0.8723 0.6029 0.1677  0.1400  0.1179  204 A1BG8 B C1  
1735 C C1  D A1BG8 F .   ? 0.7186 0.8734 0.6040 0.1677  0.1400  0.1179  204 A1BG8 B C1  
1736 C C2  C A1BG8 F .   ? 0.7198 0.8615 0.5893 0.1728  0.1355  0.1071  204 A1BG8 B C2  
1737 C C2  D A1BG8 F .   ? 0.7212 0.8629 0.5907 0.1728  0.1355  0.1071  204 A1BG8 B C2  
1738 C C3  C A1BG8 F .   ? 0.7066 0.8380 0.5611 0.1843  0.1338  0.1005  204 A1BG8 B C3  
1739 C C3  D A1BG8 F .   ? 0.7066 0.8380 0.5611 0.1844  0.1338  0.1005  204 A1BG8 B C3  
1740 C C9  C A1BG8 F .   ? 0.6690 0.7526 0.4846 0.1779  0.1098  0.0559  204 A1BG8 B C9  
1741 C C9  D A1BG8 F .   ? 0.6679 0.7515 0.4835 0.1779  0.1098  0.0559  204 A1BG8 B C9  
1742 C C11 C A1BG8 F .   ? 0.6471 0.7359 0.4870 0.1565  0.1147  0.0618  204 A1BG8 B C11 
1743 C C11 D A1BG8 F .   ? 0.6464 0.7352 0.4863 0.1565  0.1147  0.0618  204 A1BG8 B C11 
1744 O O1  C A1BG8 F .   ? 0.6450 0.7390 0.5006 0.1495  0.1196  0.0683  204 A1BG8 B O1  
1745 O O1  D A1BG8 F .   ? 0.6449 0.7389 0.5005 0.1495  0.1196  0.0683  204 A1BG8 B O1  
1746 N N2  C A1BG8 F .   ? 0.6346 0.7134 0.4670 0.1495  0.1082  0.0517  204 A1BG8 B N2  
1747 N N2  D A1BG8 F .   ? 0.6337 0.7125 0.4661 0.1495  0.1082  0.0517  204 A1BG8 B N2  
1748 C C12 C A1BG8 F .   ? 0.6236 0.6981 0.4643 0.1347  0.1069  0.0476  204 A1BG8 B C12 
1749 C C12 D A1BG8 F .   ? 0.6232 0.6977 0.4639 0.1346  0.1069  0.0476  204 A1BG8 B C12 
1750 N N4  C A1BG8 F .   ? 0.6103 0.6819 0.4687 0.1124  0.1072  0.0444  204 A1BG8 B N4  
1751 N N4  D A1BG8 F .   ? 0.6101 0.6818 0.4686 0.1124  0.1072  0.0444  204 A1BG8 B N4  
1752 C C14 C A1BG8 F .   ? 0.6023 0.6742 0.4751 0.0994  0.1086  0.0442  204 A1BG8 B C14 
1753 C C14 D A1BG8 F .   ? 0.6021 0.6740 0.4749 0.0994  0.1086  0.0442  204 A1BG8 B C14 
1754 C C16 C A1BG8 F .   ? 0.7075 0.8261 0.5527 0.1733  0.1241  0.0855  204 A1BG8 B C16 
1755 C C16 D A1BG8 F .   ? 0.7081 0.8267 0.5533 0.1733  0.1241  0.0855  204 A1BG8 B C16 
1756 N N5  C A1BG8 F .   ? 0.7144 0.8441 0.5725 0.1694  0.1285  0.0948  204 A1BG8 B N5  
1757 N N5  D A1BG8 F .   ? 0.7155 0.8453 0.5737 0.1694  0.1285  0.0948  204 A1BG8 B N5  
1758 S S   C SO4   G .   ? 1.2422 1.2917 1.1567 0.0215  0.0972  -0.0413 205 SO4   B S   
1759 S S   D SO4   G .   ? 1.2422 1.2917 1.1567 0.0215  0.0972  -0.0413 205 SO4   B S   
1760 O O1  C SO4   G .   ? 1.2446 1.2914 1.1616 0.0260  0.0986  -0.0317 205 SO4   B O1  
1761 O O1  D SO4   G .   ? 1.2446 1.2914 1.1616 0.0260  0.0986  -0.0317 205 SO4   B O1  
1762 O O2  C SO4   G .   ? 1.2888 1.3394 1.2090 0.0145  0.0962  -0.0460 205 SO4   B O2  
1763 O O2  D SO4   G .   ? 1.2888 1.3394 1.2090 0.0145  0.0962  -0.0460 205 SO4   B O2  
1764 O O3  C SO4   G .   ? 1.3141 1.3642 1.2323 0.0265  0.0981  -0.0440 205 SO4   B O3  
1765 O O3  D SO4   G .   ? 1.3141 1.3642 1.2323 0.0265  0.0981  -0.0440 205 SO4   B O3  
1766 O O4  C SO4   G .   ? 1.1989 1.2499 1.1018 0.0193  0.0954  -0.0436 205 SO4   B O4  
1767 O O4  D SO4   G .   ? 1.1989 1.2499 1.1018 0.0193  0.0954  -0.0436 205 SO4   B O4  
# 
