data_7HPB
# 
_entry.id   7HPB 
# 
_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   7HPB         pdb_00007hpb 10.2210/pdb7hpb/pdb 
WWPDB D_1001407761 ?            ?                   
# 
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                        7HPB 
_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    1  ?                           ?    ? ? 
4 non-polymer syn 
'N-{3-chloro-5-[(1-hydroxy-2-methylpropan-2-yl)carbamoyl]phenyl}-2-methyl-3-oxo-2,3-dihydro-1,2-oxazole-5-carboxamide' 367.784   1 
?                           ?    ? ? 
5 water       nat water 18.015    65 ?                           ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                                                                                   DMS   
4 'N-{3-chloro-5-[(1-hydroxy-2-methylpropan-2-yl)carbamoyl]phenyl}-2-methyl-3-oxo-2,3-dihydro-1,2-oxazole-5-carboxamide' A1BGR 
5 water                                                                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BGR non-polymer         . 
'N-{3-chloro-5-[(1-hydroxy-2-methylpropan-2-yl)carbamoyl]phenyl}-2-methyl-3-oxo-2,3-dihydro-1,2-oxazole-5-carboxamide' ? 
'C16 H18 Cl N3 O5' 367.784 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'     121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S'        78.133  
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'       75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER ? 'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BGR 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BGR 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS   1  201 202 DMS   DMS B . 
D 4 A1BGR 1  202 203 A1BGR LIG B . 
E 5 HOH   1  101 65  HOH   HOH A . 
E 5 HOH   2  102 28  HOH   HOH A . 
E 5 HOH   3  103 121 HOH   HOH A . 
E 5 HOH   4  104 34  HOH   HOH A . 
E 5 HOH   5  105 105 HOH   HOH A . 
E 5 HOH   6  106 50  HOH   HOH A . 
E 5 HOH   7  107 49  HOH   HOH A . 
E 5 HOH   8  108 29  HOH   HOH A . 
E 5 HOH   9  109 119 HOH   HOH A . 
E 5 HOH   10 110 48  HOH   HOH A . 
E 5 HOH   11 111 20  HOH   HOH A . 
E 5 HOH   12 112 118 HOH   HOH A . 
F 5 HOH   1  301 5   HOH   HOH B . 
F 5 HOH   2  302 90  HOH   HOH B . 
F 5 HOH   3  303 108 HOH   HOH B . 
F 5 HOH   4  304 9   HOH   HOH B . 
F 5 HOH   5  305 58  HOH   HOH B . 
F 5 HOH   6  306 79  HOH   HOH B . 
F 5 HOH   7  307 11  HOH   HOH B . 
F 5 HOH   8  308 39  HOH   HOH B . 
F 5 HOH   9  309 123 HOH   HOH B . 
F 5 HOH   10 310 4   HOH   HOH B . 
F 5 HOH   11 311 31  HOH   HOH B . 
F 5 HOH   12 312 24  HOH   HOH B . 
F 5 HOH   13 313 81  HOH   HOH B . 
F 5 HOH   14 314 125 HOH   HOH B . 
F 5 HOH   15 315 77  HOH   HOH B . 
F 5 HOH   16 316 32  HOH   HOH B . 
F 5 HOH   17 317 126 HOH   HOH B . 
F 5 HOH   18 318 46  HOH   HOH B . 
F 5 HOH   19 319 10  HOH   HOH B . 
F 5 HOH   20 320 2   HOH   HOH B . 
F 5 HOH   21 321 1   HOH   HOH B . 
F 5 HOH   22 322 63  HOH   HOH B . 
F 5 HOH   23 323 64  HOH   HOH B . 
F 5 HOH   24 324 124 HOH   HOH B . 
F 5 HOH   25 325 23  HOH   HOH B . 
F 5 HOH   26 326 102 HOH   HOH B . 
F 5 HOH   27 327 73  HOH   HOH B . 
F 5 HOH   28 328 13  HOH   HOH B . 
F 5 HOH   29 329 3   HOH   HOH B . 
F 5 HOH   30 330 69  HOH   HOH B . 
F 5 HOH   31 331 100 HOH   HOH B . 
F 5 HOH   32 332 61  HOH   HOH B . 
F 5 HOH   33 333 12  HOH   HOH B . 
F 5 HOH   34 334 27  HOH   HOH B . 
F 5 HOH   35 335 116 HOH   HOH B . 
F 5 HOH   36 336 30  HOH   HOH B . 
F 5 HOH   37 337 130 HOH   HOH B . 
F 5 HOH   38 338 103 HOH   HOH B . 
F 5 HOH   39 339 60  HOH   HOH B . 
F 5 HOH   40 340 56  HOH   HOH B . 
F 5 HOH   41 341 62  HOH   HOH B . 
F 5 HOH   42 342 67  HOH   HOH B . 
F 5 HOH   43 343 94  HOH   HOH B . 
F 5 HOH   44 344 26  HOH   HOH B . 
F 5 HOH   45 345 122 HOH   HOH B . 
F 5 HOH   46 346 127 HOH   HOH B . 
F 5 HOH   47 347 109 HOH   HOH B . 
F 5 HOH   48 348 128 HOH   HOH B . 
F 5 HOH   49 349 87  HOH   HOH B . 
F 5 HOH   50 350 107 HOH   HOH B . 
F 5 HOH   51 351 129 HOH   HOH B . 
F 5 HOH   52 352 59  HOH   HOH B . 
F 5 HOH   53 353 57  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (20-OCT-2021)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
'data reduction' XDS     .                      ? 5 
'data reduction' XDS     .                      ? 6 
'data reduction' XDS     .                      ? 7 
'data reduction' XDS     .                      ? 8 
# 
_cell.entry_id           7HPB 
_cell.length_a           42.553 
_cell.length_b           42.553 
_cell.length_c           215.874 
_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                         7HPB 
_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          7HPB 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.11 
_exptl_crystal.density_percent_sol   41.64 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-11-20 
_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                     7HPB 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             53.97 
_reflns.d_resolution_high            2.16 
_reflns.number_obs                   11648 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.299 
_reflns.pdbx_netI_over_sigmaI        7.9 
_reflns.pdbx_redundancy              22.9 
_reflns.pdbx_Rrim_I_all              0.306 
_reflns.pdbx_Rpim_I_all              0.063 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     267313 
_reflns.pdbx_chi_squared             0.88 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  2.16 
_reflns_shell.d_res_low                   2.27 
_reflns_shell.number_measured_all         38466 
_reflns_shell.number_unique_obs           1622 
_reflns_shell.Rmerge_I_obs                4.707 
_reflns_shell.pdbx_chi_squared            0.80 
_reflns_shell.pdbx_redundancy             23.7 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             4.809 
_reflns_shell.pdbx_Rpim_I_all             0.975 
_reflns_shell.pdbx_CC_half                0.810 
_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                                 7HPB 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     11549 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             53.97 
_refine.ls_d_res_high                            2.156 
_refine.ls_percent_reflns_obs                    99.8 
_refine.ls_R_factor_obs                          0.2327 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2302 
_refine.ls_R_factor_R_free                       0.2802 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.810 
_refine.ls_number_reflns_R_free                  555 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.942 
_refine.correlation_coeff_Fo_to_Fc_free          0.921 
_refine.B_iso_mean                               63.48 
_refine.aniso_B[1][1]                            -4.60820 
_refine.aniso_B[2][2]                            -4.60820 
_refine.aniso_B[3][3]                            9.21640 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.277 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.225 
_refine.pdbx_overall_SU_R_Blow_DPI               0.309 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.233 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HPB 
_refine_analyze.Luzzati_coordinate_error_obs    0.36 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             65 
_refine_hist.number_atoms_total               1570 
_refine_hist.d_res_high                       2.156 
_refine_hist.d_res_low                        53.97 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.008 ? 2.00  1572 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.98  ? 2.00  2143 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  537  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  272  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1572 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.25  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           17.35 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  196  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  1144 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   28 
_refine_ls_shell.d_res_high                       2.16 
_refine_ls_shell.d_res_low                        2.19 
_refine_ls_shell.number_reflns_R_work             404 
_refine_ls_shell.R_factor_R_work                  0.3646 
_refine_ls_shell.percent_reflns_obs               94.77 
_refine_ls_shell.R_factor_R_free                  0.3581 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.61 
_refine_ls_shell.number_reflns_R_free             24 
_refine_ls_shell.number_reflns_all                428 
_refine_ls_shell.R_factor_all                     0.3641 
# 
_struct.entry_id                  7HPB 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0015080-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HPB 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, XChemExplorer, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
# 
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 7HPB A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HPB 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 7HPB SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HPB MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HPB MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HPB LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4230 ? 
1 MORE         -27  ? 
1 'SSA (A^2)'  9720 ? 
# 
_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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 SER B 128 ? LEU B 131 ? SER B 137 LEU B 140 
AA2 5 VAL B 137 ? TYR B 141 ? VAL B 146 TYR B 150 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? 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 SER B 151 ? ALA B 155 ? SER B 160 ALA B 164 
AA3 6 GLY B 144 ? ILE B 147 ? GLY B 153 ILE B 156 
# 
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 TRP B 60  ? N TRP B 69  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N LEU B 89  ? N LEU B 98  O PRO B 129 ? O PRO B 138 
AA2 4 5 N SER B 128 ? N SER B 137 O TYR B 141 ? O TYR B 150 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7HPB 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 CYS B 80  ? ? 77.18 -7.45  
2 1 LYS B 157 ? ? -2.72 -63.27 
# 
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 -13.3205 -2.3012 -19.3366 -0.0226 -0.1258 -0.3331 0.2874 0.1977 0.1672 5.9469 5.0565 6.4199 
-2.4028 0.2643 0.2505  0.6074 0.5581 0.2622 -0.5334 -0.4811 -0.3369 0.1888 0.4793 -0.1263 
'X-RAY DIFFRACTION' 2 ? refined -18.0367 0.2178  -15.6598 0.1648  0.0810  -0.0986 0.3023 0.1103 0.0893 1.7925 2.0726 2.4957 
-1.4049 0.5551 -0.5467 0.5707 0.2549 0.3114 -0.1810 -0.5066 0.0097  0.2009 0.2135 -0.0640 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ B|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 1 Y 1 B GLU 177 ? B GLU 168 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BGR N1   N  N N 1   
A1BGR N3   N  N N 2   
A1BGR C4   C  Y N 3   
A1BGR C5   C  Y N 4   
A1BGR C6   C  Y N 5   
A1BGR C7   C  Y N 6   
A1BGR C8   C  Y N 7   
A1BGR C10  C  N N 8   
A1BGR C13  C  N N 9   
A1BGR C15  C  N N 10  
A1BGR C1   C  N N 11  
A1BGR O1   O  N N 12  
A1BGR C2   C  N N 13  
A1BGR C3   C  N N 14  
A1BGR O2   O  N N 15  
A1BGR N2   N  N N 16  
A1BGR CL1  CL N N 17  
A1BGR C9   C  N N 18  
A1BGR O3   O  N N 19  
A1BGR C11  C  N N 20  
A1BGR C12  C  N N 21  
A1BGR O4   O  N N 22  
A1BGR C14  C  Y N 23  
A1BGR C16  C  N N 24  
A1BGR O5   O  N N 25  
A1BGR H7   H  N N 26  
A1BGR H5   H  N N 27  
A1BGR H6   H  N N 28  
A1BGR H14  H  N N 29  
A1BGR H15  H  N N 30  
A1BGR H18  H  N N 31  
A1BGR H3   H  N N 32  
A1BGR H1   H  N N 33  
A1BGR H2   H  N N 34  
A1BGR H4   H  N N 35  
A1BGR H8   H  N N 36  
A1BGR H9   H  N N 37  
A1BGR H10  H  N N 38  
A1BGR H12  H  N N 39  
A1BGR H13  H  N N 40  
A1BGR H11  H  N N 41  
A1BGR H16  H  N N 42  
A1BGR H17  H  N N 43  
ALA   N    N  N N 44  
ALA   CA   C  N S 45  
ALA   C    C  N N 46  
ALA   O    O  N N 47  
ALA   CB   C  N N 48  
ALA   OXT  O  N N 49  
ALA   H    H  N N 50  
ALA   H2   H  N N 51  
ALA   HA   H  N N 52  
ALA   HB1  H  N N 53  
ALA   HB2  H  N N 54  
ALA   HB3  H  N N 55  
ALA   HXT  H  N N 56  
ARG   N    N  N N 57  
ARG   CA   C  N S 58  
ARG   C    C  N N 59  
ARG   O    O  N N 60  
ARG   CB   C  N N 61  
ARG   CG   C  N N 62  
ARG   CD   C  N N 63  
ARG   NE   N  N N 64  
ARG   CZ   C  N N 65  
ARG   NH1  N  N N 66  
ARG   NH2  N  N N 67  
ARG   OXT  O  N N 68  
ARG   H    H  N N 69  
ARG   H2   H  N N 70  
ARG   HA   H  N N 71  
ARG   HB2  H  N N 72  
ARG   HB3  H  N N 73  
ARG   HG2  H  N N 74  
ARG   HG3  H  N N 75  
ARG   HD2  H  N N 76  
ARG   HD3  H  N N 77  
ARG   HE   H  N N 78  
ARG   HH11 H  N N 79  
ARG   HH12 H  N N 80  
ARG   HH21 H  N N 81  
ARG   HH22 H  N N 82  
ARG   HXT  H  N N 83  
ASN   N    N  N N 84  
ASN   CA   C  N S 85  
ASN   C    C  N N 86  
ASN   O    O  N N 87  
ASN   CB   C  N N 88  
ASN   CG   C  N N 89  
ASN   OD1  O  N N 90  
ASN   ND2  N  N N 91  
ASN   OXT  O  N N 92  
ASN   H    H  N N 93  
ASN   H2   H  N N 94  
ASN   HA   H  N N 95  
ASN   HB2  H  N N 96  
ASN   HB3  H  N N 97  
ASN   HD21 H  N N 98  
ASN   HD22 H  N N 99  
ASN   HXT  H  N N 100 
ASP   N    N  N N 101 
ASP   CA   C  N S 102 
ASP   C    C  N N 103 
ASP   O    O  N N 104 
ASP   CB   C  N N 105 
ASP   CG   C  N N 106 
ASP   OD1  O  N N 107 
ASP   OD2  O  N N 108 
ASP   OXT  O  N N 109 
ASP   H    H  N N 110 
ASP   H2   H  N N 111 
ASP   HA   H  N N 112 
ASP   HB2  H  N N 113 
ASP   HB3  H  N N 114 
ASP   HD2  H  N N 115 
ASP   HXT  H  N N 116 
CYS   N    N  N N 117 
CYS   CA   C  N R 118 
CYS   C    C  N N 119 
CYS   O    O  N N 120 
CYS   CB   C  N N 121 
CYS   SG   S  N N 122 
CYS   OXT  O  N N 123 
CYS   H    H  N N 124 
CYS   H2   H  N N 125 
CYS   HA   H  N N 126 
CYS   HB2  H  N N 127 
CYS   HB3  H  N N 128 
CYS   HG   H  N N 129 
CYS   HXT  H  N N 130 
DMS   S    S  N N 131 
DMS   O    O  N N 132 
DMS   C1   C  N N 133 
DMS   C2   C  N N 134 
DMS   H11  H  N N 135 
DMS   H12  H  N N 136 
DMS   H13  H  N N 137 
DMS   H21  H  N N 138 
DMS   H22  H  N N 139 
DMS   H23  H  N N 140 
GLN   N    N  N N 141 
GLN   CA   C  N S 142 
GLN   C    C  N N 143 
GLN   O    O  N N 144 
GLN   CB   C  N N 145 
GLN   CG   C  N N 146 
GLN   CD   C  N N 147 
GLN   OE1  O  N N 148 
GLN   NE2  N  N N 149 
GLN   OXT  O  N N 150 
GLN   H    H  N N 151 
GLN   H2   H  N N 152 
GLN   HA   H  N N 153 
GLN   HB2  H  N N 154 
GLN   HB3  H  N N 155 
GLN   HG2  H  N N 156 
GLN   HG3  H  N N 157 
GLN   HE21 H  N N 158 
GLN   HE22 H  N N 159 
GLN   HXT  H  N N 160 
GLU   N    N  N N 161 
GLU   CA   C  N S 162 
GLU   C    C  N N 163 
GLU   O    O  N N 164 
GLU   CB   C  N N 165 
GLU   CG   C  N N 166 
GLU   CD   C  N N 167 
GLU   OE1  O  N N 168 
GLU   OE2  O  N N 169 
GLU   OXT  O  N N 170 
GLU   H    H  N N 171 
GLU   H2   H  N N 172 
GLU   HA   H  N N 173 
GLU   HB2  H  N N 174 
GLU   HB3  H  N N 175 
GLU   HG2  H  N N 176 
GLU   HG3  H  N N 177 
GLU   HE2  H  N N 178 
GLU   HXT  H  N N 179 
GLY   N    N  N N 180 
GLY   CA   C  N N 181 
GLY   C    C  N N 182 
GLY   O    O  N N 183 
GLY   OXT  O  N N 184 
GLY   H    H  N N 185 
GLY   H2   H  N N 186 
GLY   HA2  H  N N 187 
GLY   HA3  H  N N 188 
GLY   HXT  H  N N 189 
HIS   N    N  N N 190 
HIS   CA   C  N S 191 
HIS   C    C  N N 192 
HIS   O    O  N N 193 
HIS   CB   C  N N 194 
HIS   CG   C  Y N 195 
HIS   ND1  N  Y N 196 
HIS   CD2  C  Y N 197 
HIS   CE1  C  Y N 198 
HIS   NE2  N  Y N 199 
HIS   OXT  O  N N 200 
HIS   H    H  N N 201 
HIS   H2   H  N N 202 
HIS   HA   H  N N 203 
HIS   HB2  H  N N 204 
HIS   HB3  H  N N 205 
HIS   HD1  H  N N 206 
HIS   HD2  H  N N 207 
HIS   HE1  H  N N 208 
HIS   HE2  H  N N 209 
HIS   HXT  H  N N 210 
HOH   O    O  N N 211 
HOH   H1   H  N N 212 
HOH   H2   H  N N 213 
ILE   N    N  N N 214 
ILE   CA   C  N S 215 
ILE   C    C  N N 216 
ILE   O    O  N N 217 
ILE   CB   C  N S 218 
ILE   CG1  C  N N 219 
ILE   CG2  C  N N 220 
ILE   CD1  C  N N 221 
ILE   OXT  O  N N 222 
ILE   H    H  N N 223 
ILE   H2   H  N N 224 
ILE   HA   H  N N 225 
ILE   HB   H  N N 226 
ILE   HG12 H  N N 227 
ILE   HG13 H  N N 228 
ILE   HG21 H  N N 229 
ILE   HG22 H  N N 230 
ILE   HG23 H  N N 231 
ILE   HD11 H  N N 232 
ILE   HD12 H  N N 233 
ILE   HD13 H  N N 234 
ILE   HXT  H  N N 235 
LEU   N    N  N N 236 
LEU   CA   C  N S 237 
LEU   C    C  N N 238 
LEU   O    O  N N 239 
LEU   CB   C  N N 240 
LEU   CG   C  N N 241 
LEU   CD1  C  N N 242 
LEU   CD2  C  N N 243 
LEU   OXT  O  N N 244 
LEU   H    H  N N 245 
LEU   H2   H  N N 246 
LEU   HA   H  N N 247 
LEU   HB2  H  N N 248 
LEU   HB3  H  N N 249 
LEU   HG   H  N N 250 
LEU   HD11 H  N N 251 
LEU   HD12 H  N N 252 
LEU   HD13 H  N N 253 
LEU   HD21 H  N N 254 
LEU   HD22 H  N N 255 
LEU   HD23 H  N N 256 
LEU   HXT  H  N N 257 
LYS   N    N  N N 258 
LYS   CA   C  N S 259 
LYS   C    C  N N 260 
LYS   O    O  N N 261 
LYS   CB   C  N N 262 
LYS   CG   C  N N 263 
LYS   CD   C  N N 264 
LYS   CE   C  N N 265 
LYS   NZ   N  N N 266 
LYS   OXT  O  N N 267 
LYS   H    H  N N 268 
LYS   H2   H  N N 269 
LYS   HA   H  N N 270 
LYS   HB2  H  N N 271 
LYS   HB3  H  N N 272 
LYS   HG2  H  N N 273 
LYS   HG3  H  N N 274 
LYS   HD2  H  N N 275 
LYS   HD3  H  N N 276 
LYS   HE2  H  N N 277 
LYS   HE3  H  N N 278 
LYS   HZ1  H  N N 279 
LYS   HZ2  H  N N 280 
LYS   HZ3  H  N N 281 
LYS   HXT  H  N N 282 
MET   N    N  N N 283 
MET   CA   C  N S 284 
MET   C    C  N N 285 
MET   O    O  N N 286 
MET   CB   C  N N 287 
MET   CG   C  N N 288 
MET   SD   S  N N 289 
MET   CE   C  N N 290 
MET   OXT  O  N N 291 
MET   H    H  N N 292 
MET   H2   H  N N 293 
MET   HA   H  N N 294 
MET   HB2  H  N N 295 
MET   HB3  H  N N 296 
MET   HG2  H  N N 297 
MET   HG3  H  N N 298 
MET   HE1  H  N N 299 
MET   HE2  H  N N 300 
MET   HE3  H  N N 301 
MET   HXT  H  N N 302 
PHE   N    N  N N 303 
PHE   CA   C  N S 304 
PHE   C    C  N N 305 
PHE   O    O  N N 306 
PHE   CB   C  N N 307 
PHE   CG   C  Y N 308 
PHE   CD1  C  Y N 309 
PHE   CD2  C  Y N 310 
PHE   CE1  C  Y N 311 
PHE   CE2  C  Y N 312 
PHE   CZ   C  Y N 313 
PHE   OXT  O  N N 314 
PHE   H    H  N N 315 
PHE   H2   H  N N 316 
PHE   HA   H  N N 317 
PHE   HB2  H  N N 318 
PHE   HB3  H  N N 319 
PHE   HD1  H  N N 320 
PHE   HD2  H  N N 321 
PHE   HE1  H  N N 322 
PHE   HE2  H  N N 323 
PHE   HZ   H  N N 324 
PHE   HXT  H  N N 325 
PRO   N    N  N N 326 
PRO   CA   C  N S 327 
PRO   C    C  N N 328 
PRO   O    O  N N 329 
PRO   CB   C  N N 330 
PRO   CG   C  N N 331 
PRO   CD   C  N N 332 
PRO   OXT  O  N N 333 
PRO   H    H  N N 334 
PRO   HA   H  N N 335 
PRO   HB2  H  N N 336 
PRO   HB3  H  N N 337 
PRO   HG2  H  N N 338 
PRO   HG3  H  N N 339 
PRO   HD2  H  N N 340 
PRO   HD3  H  N N 341 
PRO   HXT  H  N N 342 
SER   N    N  N N 343 
SER   CA   C  N S 344 
SER   C    C  N N 345 
SER   O    O  N N 346 
SER   CB   C  N N 347 
SER   OG   O  N N 348 
SER   OXT  O  N N 349 
SER   H    H  N N 350 
SER   H2   H  N N 351 
SER   HA   H  N N 352 
SER   HB2  H  N N 353 
SER   HB3  H  N N 354 
SER   HG   H  N N 355 
SER   HXT  H  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 
A1BGR C1  N1   sing N N 1   
A1BGR N1  O1   sing N N 2   
A1BGR O1  C2   sing N N 3   
A1BGR C2  C3   sing N N 4   
A1BGR C3  O2   doub N N 5   
A1BGR C3  N2   sing N N 6   
A1BGR N2  C4   sing N N 7   
A1BGR C4  C5   doub Y N 8   
A1BGR C5  C6   sing Y N 9   
A1BGR C6  CL1  sing N N 10  
A1BGR C6  C7   doub Y N 11  
A1BGR C7  C8   sing Y N 12  
A1BGR C8  C9   sing N N 13  
A1BGR C9  O3   doub N N 14  
A1BGR C9  N3   sing N N 15  
A1BGR N3  C10  sing N N 16  
A1BGR C10 C11  sing N N 17  
A1BGR C10 C12  sing N N 18  
A1BGR C10 C13  sing N N 19  
A1BGR C13 O4   sing N N 20  
A1BGR C8  C14  doub Y N 21  
A1BGR C2  C15  doub N N 22  
A1BGR C15 C16  sing N N 23  
A1BGR C16 O5   doub N N 24  
A1BGR N1  C16  sing N N 25  
A1BGR C4  C14  sing Y N 26  
A1BGR N3  H7   sing N N 27  
A1BGR C5  H5   sing N N 28  
A1BGR C7  H6   sing N N 29  
A1BGR C13 H14  sing N N 30  
A1BGR C13 H15  sing N N 31  
A1BGR C15 H18  sing N N 32  
A1BGR C1  H3   sing N N 33  
A1BGR C1  H1   sing N N 34  
A1BGR C1  H2   sing N N 35  
A1BGR N2  H4   sing N N 36  
A1BGR C11 H8   sing N N 37  
A1BGR C11 H9   sing N N 38  
A1BGR C11 H10  sing N N 39  
A1BGR C12 H12  sing N N 40  
A1BGR C12 H13  sing N N 41  
A1BGR C12 H11  sing N N 42  
A1BGR O4  H16  sing N N 43  
A1BGR C14 H17  sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ARG   N   CA   sing N N 57  
ARG   N   H    sing N N 58  
ARG   N   H2   sing N N 59  
ARG   CA  C    sing N N 60  
ARG   CA  CB   sing N N 61  
ARG   CA  HA   sing N N 62  
ARG   C   O    doub N N 63  
ARG   C   OXT  sing N N 64  
ARG   CB  CG   sing N N 65  
ARG   CB  HB2  sing N N 66  
ARG   CB  HB3  sing N N 67  
ARG   CG  CD   sing N N 68  
ARG   CG  HG2  sing N N 69  
ARG   CG  HG3  sing N N 70  
ARG   CD  NE   sing N N 71  
ARG   CD  HD2  sing N N 72  
ARG   CD  HD3  sing N N 73  
ARG   NE  CZ   sing N N 74  
ARG   NE  HE   sing N N 75  
ARG   CZ  NH1  sing N N 76  
ARG   CZ  NH2  doub N N 77  
ARG   NH1 HH11 sing N N 78  
ARG   NH1 HH12 sing N N 79  
ARG   NH2 HH21 sing N N 80  
ARG   NH2 HH22 sing N N 81  
ARG   OXT HXT  sing N N 82  
ASN   N   CA   sing N N 83  
ASN   N   H    sing N N 84  
ASN   N   H2   sing N N 85  
ASN   CA  C    sing N N 86  
ASN   CA  CB   sing N N 87  
ASN   CA  HA   sing N N 88  
ASN   C   O    doub N N 89  
ASN   C   OXT  sing N N 90  
ASN   CB  CG   sing N N 91  
ASN   CB  HB2  sing N N 92  
ASN   CB  HB3  sing N N 93  
ASN   CG  OD1  doub N N 94  
ASN   CG  ND2  sing N N 95  
ASN   ND2 HD21 sing N N 96  
ASN   ND2 HD22 sing N N 97  
ASN   OXT HXT  sing N N 98  
ASP   N   CA   sing N N 99  
ASP   N   H    sing N N 100 
ASP   N   H2   sing N N 101 
ASP   CA  C    sing N N 102 
ASP   CA  CB   sing N N 103 
ASP   CA  HA   sing N N 104 
ASP   C   O    doub N N 105 
ASP   C   OXT  sing N N 106 
ASP   CB  CG   sing N N 107 
ASP   CB  HB2  sing N N 108 
ASP   CB  HB3  sing N N 109 
ASP   CG  OD1  doub N N 110 
ASP   CG  OD2  sing N N 111 
ASP   OD2 HD2  sing N N 112 
ASP   OXT HXT  sing N N 113 
CYS   N   CA   sing N N 114 
CYS   N   H    sing N N 115 
CYS   N   H2   sing N N 116 
CYS   CA  C    sing N N 117 
CYS   CA  CB   sing N N 118 
CYS   CA  HA   sing N N 119 
CYS   C   O    doub N N 120 
CYS   C   OXT  sing N N 121 
CYS   CB  SG   sing N N 122 
CYS   CB  HB2  sing N N 123 
CYS   CB  HB3  sing N N 124 
CYS   SG  HG   sing N N 125 
CYS   OXT HXT  sing N N 126 
DMS   S   O    doub N N 127 
DMS   S   C1   sing N N 128 
DMS   S   C2   sing N N 129 
DMS   C1  H11  sing N N 130 
DMS   C1  H12  sing N N 131 
DMS   C1  H13  sing N N 132 
DMS   C2  H21  sing N N 133 
DMS   C2  H22  sing N N 134 
DMS   C2  H23  sing N N 135 
GLN   N   CA   sing N N 136 
GLN   N   H    sing N N 137 
GLN   N   H2   sing N N 138 
GLN   CA  C    sing N N 139 
GLN   CA  CB   sing N N 140 
GLN   CA  HA   sing N N 141 
GLN   C   O    doub N N 142 
GLN   C   OXT  sing N N 143 
GLN   CB  CG   sing N N 144 
GLN   CB  HB2  sing N N 145 
GLN   CB  HB3  sing N N 146 
GLN   CG  CD   sing N N 147 
GLN   CG  HG2  sing N N 148 
GLN   CG  HG3  sing N N 149 
GLN   CD  OE1  doub N N 150 
GLN   CD  NE2  sing N N 151 
GLN   NE2 HE21 sing N N 152 
GLN   NE2 HE22 sing N N 153 
GLN   OXT HXT  sing N N 154 
GLU   N   CA   sing N N 155 
GLU   N   H    sing N N 156 
GLU   N   H2   sing N N 157 
GLU   CA  C    sing N N 158 
GLU   CA  CB   sing N N 159 
GLU   CA  HA   sing N N 160 
GLU   C   O    doub N N 161 
GLU   C   OXT  sing N N 162 
GLU   CB  CG   sing N N 163 
GLU   CB  HB2  sing N N 164 
GLU   CB  HB3  sing N N 165 
GLU   CG  CD   sing N N 166 
GLU   CG  HG2  sing N N 167 
GLU   CG  HG3  sing N N 168 
GLU   CD  OE1  doub N N 169 
GLU   CD  OE2  sing N N 170 
GLU   OE2 HE2  sing N N 171 
GLU   OXT HXT  sing N N 172 
GLY   N   CA   sing N N 173 
GLY   N   H    sing N N 174 
GLY   N   H2   sing N N 175 
GLY   CA  C    sing N N 176 
GLY   CA  HA2  sing N N 177 
GLY   CA  HA3  sing N N 178 
GLY   C   O    doub N N 179 
GLY   C   OXT  sing N N 180 
GLY   OXT HXT  sing N N 181 
HIS   N   CA   sing N N 182 
HIS   N   H    sing N N 183 
HIS   N   H2   sing N N 184 
HIS   CA  C    sing N N 185 
HIS   CA  CB   sing N N 186 
HIS   CA  HA   sing N N 187 
HIS   C   O    doub N N 188 
HIS   C   OXT  sing N N 189 
HIS   CB  CG   sing N N 190 
HIS   CB  HB2  sing N N 191 
HIS   CB  HB3  sing N N 192 
HIS   CG  ND1  sing Y N 193 
HIS   CG  CD2  doub Y N 194 
HIS   ND1 CE1  doub Y N 195 
HIS   ND1 HD1  sing N N 196 
HIS   CD2 NE2  sing Y N 197 
HIS   CD2 HD2  sing N N 198 
HIS   CE1 NE2  sing Y N 199 
HIS   CE1 HE1  sing N N 200 
HIS   NE2 HE2  sing N N 201 
HIS   OXT HXT  sing N N 202 
HOH   O   H1   sing N N 203 
HOH   O   H2   sing N N 204 
ILE   N   CA   sing N N 205 
ILE   N   H    sing N N 206 
ILE   N   H2   sing N N 207 
ILE   CA  C    sing N N 208 
ILE   CA  CB   sing N N 209 
ILE   CA  HA   sing N N 210 
ILE   C   O    doub N N 211 
ILE   C   OXT  sing N N 212 
ILE   CB  CG1  sing N N 213 
ILE   CB  CG2  sing N N 214 
ILE   CB  HB   sing N N 215 
ILE   CG1 CD1  sing N N 216 
ILE   CG1 HG12 sing N N 217 
ILE   CG1 HG13 sing N N 218 
ILE   CG2 HG21 sing N N 219 
ILE   CG2 HG22 sing N N 220 
ILE   CG2 HG23 sing N N 221 
ILE   CD1 HD11 sing N N 222 
ILE   CD1 HD12 sing N N 223 
ILE   CD1 HD13 sing N N 224 
ILE   OXT HXT  sing N N 225 
LEU   N   CA   sing N N 226 
LEU   N   H    sing N N 227 
LEU   N   H2   sing N N 228 
LEU   CA  C    sing N N 229 
LEU   CA  CB   sing N N 230 
LEU   CA  HA   sing N N 231 
LEU   C   O    doub N N 232 
LEU   C   OXT  sing N N 233 
LEU   CB  CG   sing N N 234 
LEU   CB  HB2  sing N N 235 
LEU   CB  HB3  sing N N 236 
LEU   CG  CD1  sing N N 237 
LEU   CG  CD2  sing N N 238 
LEU   CG  HG   sing N N 239 
LEU   CD1 HD11 sing N N 240 
LEU   CD1 HD12 sing N N 241 
LEU   CD1 HD13 sing N N 242 
LEU   CD2 HD21 sing N N 243 
LEU   CD2 HD22 sing N N 244 
LEU   CD2 HD23 sing N N 245 
LEU   OXT HXT  sing N N 246 
LYS   N   CA   sing N N 247 
LYS   N   H    sing N N 248 
LYS   N   H2   sing N N 249 
LYS   CA  C    sing N N 250 
LYS   CA  CB   sing N N 251 
LYS   CA  HA   sing N N 252 
LYS   C   O    doub N N 253 
LYS   C   OXT  sing N N 254 
LYS   CB  CG   sing N N 255 
LYS   CB  HB2  sing N N 256 
LYS   CB  HB3  sing N N 257 
LYS   CG  CD   sing N N 258 
LYS   CG  HG2  sing N N 259 
LYS   CG  HG3  sing N N 260 
LYS   CD  CE   sing N N 261 
LYS   CD  HD2  sing N N 262 
LYS   CD  HD3  sing N N 263 
LYS   CE  NZ   sing N N 264 
LYS   CE  HE2  sing N N 265 
LYS   CE  HE3  sing N N 266 
LYS   NZ  HZ1  sing N N 267 
LYS   NZ  HZ2  sing N N 268 
LYS   NZ  HZ3  sing N N 269 
LYS   OXT HXT  sing N N 270 
MET   N   CA   sing N N 271 
MET   N   H    sing N N 272 
MET   N   H2   sing N N 273 
MET   CA  C    sing N N 274 
MET   CA  CB   sing N N 275 
MET   CA  HA   sing N N 276 
MET   C   O    doub N N 277 
MET   C   OXT  sing N N 278 
MET   CB  CG   sing N N 279 
MET   CB  HB2  sing N N 280 
MET   CB  HB3  sing N N 281 
MET   CG  SD   sing N N 282 
MET   CG  HG2  sing N N 283 
MET   CG  HG3  sing N N 284 
MET   SD  CE   sing N N 285 
MET   CE  HE1  sing N N 286 
MET   CE  HE2  sing N N 287 
MET   CE  HE3  sing N N 288 
MET   OXT HXT  sing N N 289 
PHE   N   CA   sing N N 290 
PHE   N   H    sing N N 291 
PHE   N   H2   sing N N 292 
PHE   CA  C    sing N N 293 
PHE   CA  CB   sing N N 294 
PHE   CA  HA   sing N N 295 
PHE   C   O    doub N N 296 
PHE   C   OXT  sing N N 297 
PHE   CB  CG   sing N N 298 
PHE   CB  HB2  sing N N 299 
PHE   CB  HB3  sing N N 300 
PHE   CG  CD1  doub Y N 301 
PHE   CG  CD2  sing Y N 302 
PHE   CD1 CE1  sing Y N 303 
PHE   CD1 HD1  sing N N 304 
PHE   CD2 CE2  doub Y N 305 
PHE   CD2 HD2  sing N N 306 
PHE   CE1 CZ   doub Y N 307 
PHE   CE1 HE1  sing N N 308 
PHE   CE2 CZ   sing Y N 309 
PHE   CE2 HE2  sing N N 310 
PHE   CZ  HZ   sing N N 311 
PHE   OXT HXT  sing N N 312 
PRO   N   CA   sing N N 313 
PRO   N   CD   sing N N 314 
PRO   N   H    sing N N 315 
PRO   CA  C    sing N N 316 
PRO   CA  CB   sing N N 317 
PRO   CA  HA   sing N N 318 
PRO   C   O    doub N N 319 
PRO   C   OXT  sing N N 320 
PRO   CB  CG   sing N N 321 
PRO   CB  HB2  sing N N 322 
PRO   CB  HB3  sing N N 323 
PRO   CG  CD   sing N N 324 
PRO   CG  HG2  sing N N 325 
PRO   CG  HG3  sing N N 326 
PRO   CD  HD2  sing N N 327 
PRO   CD  HD3  sing N N 328 
PRO   OXT HXT  sing N N 329 
SER   N   CA   sing N N 330 
SER   N   H    sing N N 331 
SER   N   H2   sing N N 332 
SER   CA  C    sing N N 333 
SER   CA  CB   sing N N 334 
SER   CA  HA   sing N N 335 
SER   C   O    doub N N 336 
SER   C   OXT  sing N N 337 
SER   CB  OG   sing N N 338 
SER   CB  HB2  sing N N 339 
SER   CB  HB3  sing N N 340 
SER   OG  HG   sing N N 341 
SER   OXT HXT  sing N N 342 
THR   N   CA   sing N N 343 
THR   N   H    sing N N 344 
THR   N   H2   sing N N 345 
THR   CA  C    sing N N 346 
THR   CA  CB   sing N N 347 
THR   CA  HA   sing N N 348 
THR   C   O    doub N N 349 
THR   C   OXT  sing N N 350 
THR   CB  OG1  sing N N 351 
THR   CB  CG2  sing N N 352 
THR   CB  HB   sing N N 353 
THR   OG1 HG1  sing N N 354 
THR   CG2 HG21 sing N N 355 
THR   CG2 HG22 sing N N 356 
THR   CG2 HG23 sing N N 357 
THR   OXT HXT  sing N N 358 
TRP   N   CA   sing N N 359 
TRP   N   H    sing N N 360 
TRP   N   H2   sing N N 361 
TRP   CA  C    sing N N 362 
TRP   CA  CB   sing N N 363 
TRP   CA  HA   sing N N 364 
TRP   C   O    doub N N 365 
TRP   C   OXT  sing N N 366 
TRP   CB  CG   sing N N 367 
TRP   CB  HB2  sing N N 368 
TRP   CB  HB3  sing N N 369 
TRP   CG  CD1  doub Y N 370 
TRP   CG  CD2  sing Y N 371 
TRP   CD1 NE1  sing Y N 372 
TRP   CD1 HD1  sing N N 373 
TRP   CD2 CE2  doub Y N 374 
TRP   CD2 CE3  sing Y N 375 
TRP   NE1 CE2  sing Y N 376 
TRP   NE1 HE1  sing N N 377 
TRP   CE2 CZ2  sing Y N 378 
TRP   CE3 CZ3  doub Y N 379 
TRP   CE3 HE3  sing N N 380 
TRP   CZ2 CH2  doub Y N 381 
TRP   CZ2 HZ2  sing N N 382 
TRP   CZ3 CH2  sing Y N 383 
TRP   CZ3 HZ3  sing N N 384 
TRP   CH2 HH2  sing N N 385 
TRP   OXT HXT  sing N N 386 
TYR   N   CA   sing N N 387 
TYR   N   H    sing N N 388 
TYR   N   H2   sing N N 389 
TYR   CA  C    sing N N 390 
TYR   CA  CB   sing N N 391 
TYR   CA  HA   sing N N 392 
TYR   C   O    doub N N 393 
TYR   C   OXT  sing N N 394 
TYR   CB  CG   sing N N 395 
TYR   CB  HB2  sing N N 396 
TYR   CB  HB3  sing N N 397 
TYR   CG  CD1  doub Y N 398 
TYR   CG  CD2  sing Y N 399 
TYR   CD1 CE1  sing Y N 400 
TYR   CD1 HD1  sing N N 401 
TYR   CD2 CE2  doub Y N 402 
TYR   CD2 HD2  sing N N 403 
TYR   CE1 CZ   doub Y N 404 
TYR   CE1 HE1  sing N N 405 
TYR   CE2 CZ   sing Y N 406 
TYR   CE2 HE2  sing N N 407 
TYR   CZ  OH   sing N N 408 
TYR   OH  HH   sing N N 409 
TYR   OXT HXT  sing N N 410 
VAL   N   CA   sing N N 411 
VAL   N   H    sing N N 412 
VAL   N   H2   sing N N 413 
VAL   CA  C    sing N N 414 
VAL   CA  CB   sing N N 415 
VAL   CA  HA   sing N N 416 
VAL   C   O    doub N N 417 
VAL   C   OXT  sing N N 418 
VAL   CB  CG1  sing N N 419 
VAL   CB  CG2  sing N N 420 
VAL   CB  HB   sing N N 421 
VAL   CG1 HG11 sing N N 422 
VAL   CG1 HG12 sing N N 423 
VAL   CG1 HG13 sing N N 424 
VAL   CG2 HG21 sing N N 425 
VAL   CG2 HG22 sing N N 426 
VAL   CG2 HG23 sing N N 427 
VAL   OXT HXT  sing N N 428 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002322 
_pdbx_deposit_group.group_description   
'Crystallographic fragment screen of ZIKV NS2B-NS3 protease at the XChem facility of Diamond Light Source beamline I04-1' 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HPB 
_atom_sites.fract_transf_matrix[1][1]   0.023500 
_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]   0.023500 
_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]   0.004632 
_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   ? -21.159 18.932  -7.627  1.00 71.58  ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -22.190 17.893  -7.644  1.00 71.30  ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -22.095 17.102  -8.943  1.00 69.58  ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -21.873 17.682  -10.005 1.00 70.30  ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -23.595 18.518  -7.471  1.00 73.82  ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -24.431 17.855  -6.387  1.00 81.23  ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -25.003 18.592  -5.537  1.00 82.83  ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -24.510 16.599  -6.378  1.00 84.34  ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -22.215 15.780  -8.856  1.00 67.48  ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -22.138 14.924  -10.026 1.00 65.31  ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -23.522 14.642  -10.617 1.00 63.37  ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -24.523 14.629  -9.890  1.00 63.47  ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -21.395 13.629  -9.705  1.00 65.56  ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -19.977 13.859  -9.252  1.00 66.77  ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -19.091 12.305  -9.014  1.00 67.16  ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -17.399 12.863  -9.215  1.00 69.53  ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -23.587 14.460  -11.946 1.00 61.28  ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -24.857 14.196  -12.622 1.00 59.98  ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -24.689 13.221  -13.798 1.00 58.51  ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -23.577 13.044  -14.293 1.00 58.29  ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -25.572 15.496  -13.045 1.00 59.71  ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -24.853 16.259  -14.139 1.00 60.57  ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -23.837 17.153  -13.835 1.00 61.16  ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -25.165 16.058  -15.481 1.00 61.29  ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -23.135 17.809  -14.835 1.00 62.22  ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -24.489 16.732  -16.487 1.00 62.06  ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -23.479 17.615  -16.160 1.00 63.43  ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -22.805 18.299  -17.142 1.00 66.29  ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -25.792 12.584  -14.243 1.00 57.23  ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -25.714 11.620  -15.336 1.00 56.91  ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -26.461 12.088  -16.599 1.00 56.95  ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -27.475 12.795  -16.518 1.00 57.85  ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -26.135 10.177  -14.903 1.00 56.78  ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -27.625 10.088  -14.483 1.00 58.17  ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -25.220 9.636   -13.818 1.00 56.83  ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -28.131 8.636   -14.265 1.00 59.00  ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -25.933 11.708  -17.769 1.00 56.53  ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -26.527 12.012  -19.080 1.00 57.15  ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -26.567 10.704  -19.897 1.00 57.42  ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -25.551 10.025  -19.979 1.00 56.26  ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -25.659 13.022  -19.851 1.00 59.70  ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -25.738 14.477  -19.403 1.00 65.75  ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -24.808 15.407  -20.169 1.00 73.55  ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -23.899 14.894  -20.862 1.00 75.53  ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -24.972 16.646  -20.065 1.00 75.63  ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -27.700 10.381  -20.536 1.00 58.34  ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -27.785 9.166   -21.348 1.00 59.32  ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -26.844 9.239   -22.542 1.00 60.13  ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -26.761 10.272  -23.225 1.00 59.89  ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -29.221 8.881   -21.805 1.00 60.38  ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -29.481 7.386   -21.959 1.00 62.46  ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -30.952 7.071   -22.165 1.00 64.16  ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -31.144 5.658   -22.467 1.00 65.47  ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -31.097 5.141   -23.687 1.00 66.89  ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -30.892 5.924   -24.740 1.00 67.88  ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -31.220 3.831   -23.865 1.00 65.65  ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -26.107 8.150   -22.767 1.00 60.14  ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -25.145 8.072   -23.855 1.00 60.76  ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -25.492 7.041   -24.937 1.00 61.02  ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -24.854 7.052   -25.972 1.00 61.66  ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -23.759 7.807   -23.303 1.00 60.90  ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -26.475 6.173   -24.703 1.00 60.37  ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -26.872 5.192   -25.705 1.00 60.03  ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -27.512 3.929   -25.171 1.00 59.86  ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -27.731 3.808   -23.968 1.00 59.50  ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -27.860 2.997   -26.079 1.00 59.89  ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -28.465 1.711   -25.735 1.00 60.86  ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -27.387 0.655   -25.568 1.00 61.90  ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -26.337 0.735   -26.205 1.00 61.88  ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -29.422 1.220   -26.832 1.00 62.65  ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -30.697 2.008   -26.975 1.00 70.54  ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -30.775 3.112   -26.412 1.00 71.79  ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -31.613 1.540   -27.693 1.00 73.94  ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -27.663 -0.365  -24.749 1.00 62.25  ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -26.728 -1.463  -24.569 1.00 62.40  ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -27.096 -2.575  -25.539 1.00 63.72  ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -28.016 -3.358  -25.290 1.00 63.42  ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -26.679 -1.914  -23.110 1.00 61.58  ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -26.303 -0.739  -22.210 1.00 61.87  ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -25.703 -3.050  -22.953 1.00 61.53  ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -26.591 -0.991  -20.791 1.00 62.20  ? 59  ILE   A CD1 1 
ATOM   82   N  N   A THR   A 1 17  ? -26.410 -2.605  -26.686 0.50 64.40  ? 60  THR   A N   1 
ATOM   83   N  N   B THR   A 1 17  ? -26.396 -2.619  -26.671 0.50 64.62  ? 60  THR   A N   1 
ATOM   84   C  CA  A THR   A 1 17  ? -26.621 -3.610  -27.730 0.50 65.53  ? 60  THR   A CA  1 
ATOM   85   C  CA  B THR   A 1 17  ? -26.657 -3.584  -27.737 0.50 65.99  ? 60  THR   A CA  1 
ATOM   86   C  C   A THR   A 1 17  ? -25.287 -4.078  -28.303 0.50 67.35  ? 60  THR   A C   1 
ATOM   87   C  C   B THR   A 1 17  ? -25.334 -4.034  -28.386 0.50 67.66  ? 60  THR   A C   1 
ATOM   88   O  O   A THR   A 1 17  ? -24.307 -3.331  -28.299 0.50 67.37  ? 60  THR   A O   1 
ATOM   89   O  O   B THR   A 1 17  ? -24.373 -3.265  -28.428 0.50 67.83  ? 60  THR   A O   1 
ATOM   90   C  CB  A THR   A 1 17  ? -27.460 -3.049  -28.913 0.50 65.85  ? 60  THR   A CB  1 
ATOM   91   C  CB  B THR   A 1 17  ? -27.653 -2.943  -28.748 0.50 66.75  ? 60  THR   A CB  1 
ATOM   92   O  OG1 A THR   A 1 17  ? -26.754 -1.979  -29.543 0.50 66.08  ? 60  THR   A OG1 1 
ATOM   93   O  OG1 B THR   A 1 17  ? -28.863 -2.593  -28.069 0.50 67.48  ? 60  THR   A OG1 1 
ATOM   94   C  CG2 A THR   A 1 17  ? -28.876 -2.642  -28.523 0.50 66.13  ? 60  THR   A CG2 1 
ATOM   95   C  CG2 B THR   A 1 17  ? -28.004 -3.846  -29.904 0.50 66.94  ? 60  THR   A CG2 1 
ATOM   96   N  N   . TRP   A 1 18  ? -25.272 -5.281  -28.866 1.00 68.77  ? 61  TRP   A N   1 
ATOM   97   C  CA  . TRP   A 1 18  ? -24.094 -5.779  -29.560 1.00 72.27  ? 61  TRP   A CA  1 
ATOM   98   C  C   . TRP   A 1 18  ? -24.271 -5.282  -31.036 1.00 75.97  ? 61  TRP   A C   1 
ATOM   99   O  O   . TRP   A 1 18  ? -25.383 -5.332  -31.571 1.00 75.78  ? 61  TRP   A O   1 
ATOM   100  C  CB  . TRP   A 1 18  ? -24.058 -7.314  -29.484 1.00 72.18  ? 61  TRP   A CB  1 
ATOM   101  C  CG  . TRP   A 1 18  ? -22.977 -7.987  -30.286 1.00 72.89  ? 61  TRP   A CG  1 
ATOM   102  C  CD1 . TRP   A 1 18  ? -23.048 -8.369  -31.594 1.00 73.42  ? 61  TRP   A CD1 1 
ATOM   103  C  CD2 . TRP   A 1 18  ? -21.755 -8.541  -29.774 1.00 73.08  ? 61  TRP   A CD2 1 
ATOM   104  N  NE1 . TRP   A 1 18  ? -21.906 -9.041  -31.952 1.00 73.68  ? 61  TRP   A NE1 1 
ATOM   105  C  CE2 . TRP   A 1 18  ? -21.103 -9.179  -30.849 1.00 73.86  ? 61  TRP   A CE2 1 
ATOM   106  C  CE3 . TRP   A 1 18  ? -21.129 -8.523  -28.524 1.00 73.47  ? 61  TRP   A CE3 1 
ATOM   107  C  CZ2 . TRP   A 1 18  ? -19.860 -9.797  -30.705 1.00 74.58  ? 61  TRP   A CZ2 1 
ATOM   108  C  CZ3 . TRP   A 1 18  ? -19.910 -9.154  -28.382 1.00 74.26  ? 61  TRP   A CZ3 1 
ATOM   109  C  CH2 . TRP   A 1 18  ? -19.277 -9.758  -29.465 1.00 74.34  ? 61  TRP   A CH2 1 
ATOM   110  N  N   . GLU   A 1 19  ? -23.197 -4.776  -31.674 1.00 78.82  ? 62  GLU   A N   1 
ATOM   111  C  CA  . GLU   A 1 19  ? -23.280 -4.316  -33.063 1.00 81.88  ? 62  GLU   A CA  1 
ATOM   112  C  C   . GLU   A 1 19  ? -22.526 -5.260  -33.959 1.00 85.22  ? 62  GLU   A C   1 
ATOM   113  O  O   . GLU   A 1 19  ? -21.325 -5.450  -33.761 1.00 85.13  ? 62  GLU   A O   1 
ATOM   114  C  CB  . GLU   A 1 19  ? -22.720 -2.894  -33.237 1.00 84.44  ? 62  GLU   A CB  1 
ATOM   115  C  CG  . GLU   A 1 19  ? -23.587 -1.811  -32.605 1.00 91.19  ? 62  GLU   A CG  1 
ATOM   116  C  CD  . GLU   A 1 19  ? -24.972 -1.603  -33.200 1.00 98.65  ? 62  GLU   A CD  1 
ATOM   117  O  OE1 . GLU   A 1 19  ? -25.065 -1.342  -34.425 1.00 101.96 ? 62  GLU   A OE1 1 
ATOM   118  O  OE2 . GLU   A 1 19  ? -25.963 -1.682  -32.436 1.00 98.69  ? 62  GLU   A OE2 1 
ATOM   119  N  N   . LYS   A 1 20  ? -23.213 -5.848  -34.955 1.00 87.85  ? 63  LYS   A N   1 
ATOM   120  C  CA  . LYS   A 1 20  ? -22.550 -6.751  -35.900 1.00 90.99  ? 63  LYS   A CA  1 
ATOM   121  C  C   . LYS   A 1 20  ? -21.631 -5.907  -36.770 1.00 93.86  ? 63  LYS   A C   1 
ATOM   122  O  O   . LYS   A 1 20  ? -22.019 -4.811  -37.177 1.00 94.49  ? 63  LYS   A O   1 
ATOM   123  C  CB  . LYS   A 1 20  ? -23.561 -7.473  -36.822 1.00 93.24  ? 63  LYS   A CB  1 
ATOM   124  C  CG  . LYS   A 1 20  ? -24.886 -7.885  -36.181 1.00 97.61  ? 63  LYS   A CG  1 
ATOM   125  C  CD  . LYS   A 1 20  ? -25.715 -8.713  -37.168 1.00 101.87 ? 63  LYS   A CD  1 
ATOM   126  C  CE  . LYS   A 1 20  ? -27.208 -8.531  -37.016 1.00 106.10 ? 63  LYS   A CE  1 
ATOM   127  N  NZ  . LYS   A 1 20  ? -27.937 -8.761  -38.308 1.00 108.85 ? 63  LYS   A NZ  1 
ATOM   128  N  N   . ASP   A 1 21  ? -20.429 -6.405  -37.056 1.00 95.53  ? 64  ASP   A N   1 
ATOM   129  C  CA  . ASP   A 1 21  ? -19.463 -5.680  -37.883 1.00 97.35  ? 64  ASP   A CA  1 
ATOM   130  C  C   . ASP   A 1 21  ? -19.000 -4.383  -37.211 1.00 97.60  ? 64  ASP   A C   1 
ATOM   131  O  O   . ASP   A 1 21  ? -19.091 -3.296  -37.796 1.00 97.89  ? 64  ASP   A O   1 
ATOM   132  C  CB  . ASP   A 1 21  ? -19.990 -5.412  -39.304 1.00 100.93 ? 64  ASP   A CB  1 
ATOM   133  C  CG  . ASP   A 1 21  ? -20.410 -6.663  -40.048 1.00 108.26 ? 64  ASP   A CG  1 
ATOM   134  O  OD1 . ASP   A 1 21  ? -19.805 -7.741  -39.795 1.00 110.20 ? 64  ASP   A OD1 1 
ATOM   135  O  OD2 . ASP   A 1 21  ? -21.339 -6.569  -40.881 1.00 110.00 ? 64  ASP   A OD2 1 
ATOM   136  N  N   . ALA   A 1 22  ? -18.526 -4.512  -35.964 1.00 96.85  ? 65  ALA   A N   1 
ATOM   137  C  CA  . ALA   A 1 22  ? -17.936 -3.409  -35.210 1.00 96.20  ? 65  ALA   A CA  1 
ATOM   138  C  C   . ALA   A 1 22  ? -16.390 -3.473  -35.415 1.00 95.41  ? 65  ALA   A C   1 
ATOM   139  O  O   . ALA   A 1 22  ? -15.876 -4.471  -35.933 1.00 94.90  ? 65  ALA   A O   1 
ATOM   140  C  CB  . ALA   A 1 22  ? -18.290 -3.548  -33.732 1.00 96.04  ? 65  ALA   A CB  1 
ATOM   141  N  N   . GLU   A 1 23  ? -15.658 -2.407  -35.051 1.00 95.06  ? 66  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 23  ? -14.198 -2.399  -35.174 1.00 95.16  ? 66  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 23  ? -13.604 -3.454  -34.224 1.00 93.61  ? 66  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 23  ? -13.781 -3.340  -33.015 1.00 93.35  ? 66  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 23  ? -13.643 -1.005  -34.820 1.00 99.32  ? 66  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 23  ? -12.124 -0.943  -34.726 1.00 106.88 ? 66  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 23  ? -11.539 0.429   -34.450 1.00 115.69 ? 66  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 23  ? -12.315 1.410   -34.371 1.00 116.93 ? 66  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 23  ? -10.296 0.520   -34.316 1.00 118.30 ? 66  GLU   A OE2 1 
ATOM   150  N  N   . VAL   A 1 24  ? -12.933 -4.487  -34.778 1.00 92.32  ? 67  VAL   A N   1 
ATOM   151  C  CA  . VAL   A 1 24  ? -12.312 -5.568  -34.004 1.00 91.26  ? 67  VAL   A CA  1 
ATOM   152  C  C   . VAL   A 1 24  ? -10.815 -5.274  -33.827 1.00 89.87  ? 67  VAL   A C   1 
ATOM   153  O  O   . VAL   A 1 24  ? -10.078 -5.270  -34.817 1.00 90.15  ? 67  VAL   A O   1 
ATOM   154  C  CB  . VAL   A 1 24  ? -12.511 -6.988  -34.611 1.00 92.09  ? 67  VAL   A CB  1 
ATOM   155  C  CG1 . VAL   A 1 24  ? -12.372 -8.047  -33.533 1.00 92.24  ? 67  VAL   A CG1 1 
ATOM   156  C  CG2 . VAL   A 1 24  ? -13.852 -7.137  -35.325 1.00 92.80  ? 67  VAL   A CG2 1 
ATOM   157  N  N   . THR   A 1 25  ? -10.368 -5.031  -32.575 1.00 88.04  ? 68  THR   A N   1 
ATOM   158  C  CA  . THR   A 1 25  ? -8.971  -4.703  -32.250 1.00 86.93  ? 68  THR   A CA  1 
ATOM   159  C  C   . THR   A 1 25  ? -8.578  -5.148  -30.797 1.00 85.82  ? 68  THR   A C   1 
ATOM   160  O  O   . THR   A 1 25  ? -9.413  -5.659  -30.066 1.00 85.82  ? 68  THR   A O   1 
ATOM   161  C  CB  . THR   A 1 25  ? -8.716  -3.200  -32.519 1.00 87.89  ? 68  THR   A CB  1 
ATOM   162  O  OG1 . THR   A 1 25  ? -7.306  -2.962  -32.509 1.00 88.93  ? 68  THR   A OG1 1 
ATOM   163  C  CG2 . THR   A 1 25  ? -9.408  -2.303  -31.511 1.00 87.99  ? 68  THR   A CG2 1 
ATOM   164  N  N   . GLY   A 1 26  ? -7.314  -4.984  -30.414 1.00 84.60  ? 69  GLY   A N   1 
ATOM   165  C  CA  . GLY   A 1 26  ? -6.843  -5.356  -29.091 1.00 84.03  ? 69  GLY   A CA  1 
ATOM   166  C  C   . GLY   A 1 26  ? -6.340  -6.782  -28.978 1.00 83.41  ? 69  GLY   A C   1 
ATOM   167  O  O   . GLY   A 1 26  ? -6.876  -7.695  -29.610 1.00 83.73  ? 69  GLY   A O   1 
ATOM   168  N  N   . ASN   A 1 27  ? -5.316  -6.987  -28.153 1.00 82.19  ? 70  ASN   A N   1 
ATOM   169  C  CA  . ASN   A 1 27  ? -4.781  -8.320  -27.906 1.00 81.20  ? 70  ASN   A CA  1 
ATOM   170  C  C   . ASN   A 1 27  ? -5.408  -8.963  -26.621 1.00 78.99  ? 70  ASN   A C   1 
ATOM   171  O  O   . ASN   A 1 27  ? -6.308  -8.373  -26.028 1.00 78.72  ? 70  ASN   A O   1 
ATOM   172  C  CB  . ASN   A 1 27  ? -3.236  -8.302  -27.908 1.00 83.12  ? 70  ASN   A CB  1 
ATOM   173  C  CG  . ASN   A 1 27  ? -2.614  -7.566  -26.748 1.00 86.73  ? 70  ASN   A CG  1 
ATOM   174  O  OD1 . ASN   A 1 27  ? -3.122  -6.535  -26.294 1.00 87.32  ? 70  ASN   A OD1 1 
ATOM   175  N  ND2 . ASN   A 1 27  ? -1.486  -8.093  -26.243 1.00 87.80  ? 70  ASN   A ND2 1 
ATOM   176  N  N   . SER   A 1 28  ? -4.981  -10.196 -26.246 1.00 77.24  ? 71  SER   A N   1 
ATOM   177  C  CA  . SER   A 1 28  ? -5.459  -10.985 -25.097 1.00 75.96  ? 71  SER   A CA  1 
ATOM   178  C  C   . SER   A 1 28  ? -4.268  -11.408 -24.201 1.00 74.98  ? 71  SER   A C   1 
ATOM   179  O  O   . SER   A 1 28  ? -3.894  -12.588 -24.163 1.00 74.64  ? 71  SER   A O   1 
ATOM   180  C  CB  . SER   A 1 28  ? -6.190  -12.240 -25.580 1.00 76.94  ? 71  SER   A CB  1 
ATOM   181  O  OG  . SER   A 1 28  ? -6.876  -12.098 -26.811 1.00 78.89  ? 71  SER   A OG  1 
ATOM   182  N  N   . PRO   A 1 29  ? -3.638  -10.463 -23.480 1.00 74.29  ? 72  PRO   A N   1 
ATOM   183  C  CA  . PRO   A 1 29  ? -2.474  -10.834 -22.670 1.00 73.81  ? 72  PRO   A CA  1 
ATOM   184  C  C   . PRO   A 1 29  ? -2.851  -11.575 -21.391 1.00 73.21  ? 72  PRO   A C   1 
ATOM   185  O  O   . PRO   A 1 29  ? -3.924  -11.337 -20.855 1.00 73.02  ? 72  PRO   A O   1 
ATOM   186  C  CB  . PRO   A 1 29  ? -1.817  -9.483  -22.380 1.00 74.56  ? 72  PRO   A CB  1 
ATOM   187  C  CG  . PRO   A 1 29  ? -2.948  -8.531  -22.337 1.00 74.87  ? 72  PRO   A CG  1 
ATOM   188  C  CD  . PRO   A 1 29  ? -3.938  -9.020  -23.364 1.00 73.64  ? 72  PRO   A CD  1 
ATOM   189  N  N   . ARG   A 1 30  ? -1.979  -12.496 -20.924 1.00 72.69  ? 73  ARG   A N   1 
ATOM   190  C  CA  . ARG   A 1 30  ? -2.179  -13.231 -19.676 1.00 72.87  ? 73  ARG   A CA  1 
ATOM   191  C  C   . ARG   A 1 30  ? -1.187  -12.653 -18.693 1.00 71.61  ? 73  ARG   A C   1 
ATOM   192  O  O   . ARG   A 1 30  ? -0.002  -12.696 -18.942 1.00 71.92  ? 73  ARG   A O   1 
ATOM   193  C  CB  . ARG   A 1 30  ? -1.995  -14.743 -19.872 1.00 75.52  ? 73  ARG   A CB  1 
ATOM   194  C  CG  . ARG   A 1 30  ? -3.051  -15.304 -20.820 1.00 81.11  ? 73  ARG   A CG  1 
ATOM   195  C  CD  . ARG   A 1 30  ? -3.135  -16.820 -20.834 1.00 86.94  ? 73  ARG   A CD  1 
ATOM   196  N  NE  . ARG   A 1 30  ? -4.024  -17.266 -21.911 1.00 92.42  ? 73  ARG   A NE  1 
ATOM   197  C  CZ  . ARG   A 1 30  ? -4.210  -18.536 -22.259 1.00 95.69  ? 73  ARG   A CZ  1 
ATOM   198  N  NH1 . ARG   A 1 30  ? -3.587  -19.512 -21.603 1.00 96.80  ? 73  ARG   A NH1 1 
ATOM   199  N  NH2 . ARG   A 1 30  ? -5.033  -18.842 -23.256 1.00 94.39  ? 73  ARG   A NH2 1 
ATOM   200  N  N   . LEU   A 1 31  ? -1.669  -11.987 -17.657 1.00 70.56  ? 74  LEU   A N   1 
ATOM   201  C  CA  . LEU   A 1 31  ? -0.805  -11.282 -16.715 1.00 69.68  ? 74  LEU   A CA  1 
ATOM   202  C  C   . LEU   A 1 31  ? -0.950  -11.789 -15.311 1.00 67.99  ? 74  LEU   A C   1 
ATOM   203  O  O   . LEU   A 1 31  ? -2.068  -12.013 -14.880 1.00 67.43  ? 74  LEU   A O   1 
ATOM   204  C  CB  . LEU   A 1 31  ? -1.169  -9.785  -16.735 1.00 69.73  ? 74  LEU   A CB  1 
ATOM   205  C  CG  . LEU   A 1 31  ? -1.092  -9.120  -18.110 1.00 71.03  ? 74  LEU   A CG  1 
ATOM   206  C  CD1 . LEU   A 1 31  ? -1.672  -7.725  -18.078 1.00 71.04  ? 74  LEU   A CD1 1 
ATOM   207  C  CD2 . LEU   A 1 31  ? 0.351   -9.138  -18.637 1.00 71.63  ? 74  LEU   A CD2 1 
ATOM   208  N  N   . ASP   A 1 32  ? 0.161   -11.914 -14.576 1.00 67.28  ? 75  ASP   A N   1 
ATOM   209  C  CA  . ASP   A 1 32  ? 0.106   -12.286 -13.162 1.00 67.21  ? 75  ASP   A CA  1 
ATOM   210  C  C   . ASP   A 1 32  ? -0.093  -10.957 -12.416 1.00 65.30  ? 75  ASP   A C   1 
ATOM   211  O  O   . ASP   A 1 32  ? 0.755   -10.072 -12.546 1.00 65.28  ? 75  ASP   A O   1 
ATOM   212  C  CB  . ASP   A 1 32  ? 1.428   -12.913 -12.711 1.00 71.62  ? 75  ASP   A CB  1 
ATOM   213  C  CG  . ASP   A 1 32  ? 1.649   -14.356 -13.110 1.00 80.13  ? 75  ASP   A CG  1 
ATOM   214  O  OD1 . ASP   A 1 32  ? 0.696   -14.982 -13.620 1.00 81.98  ? 75  ASP   A OD1 1 
ATOM   215  O  OD2 . ASP   A 1 32  ? 2.776   -14.864 -12.898 1.00 83.92  ? 75  ASP   A OD2 1 
ATOM   216  N  N   . VAL   A 1 33  ? -1.211  -10.782 -11.701 1.00 63.49  ? 76  VAL   A N   1 
ATOM   217  C  CA  . VAL   A 1 33  ? -1.472  -9.508  -11.014 1.00 63.14  ? 76  VAL   A CA  1 
ATOM   218  C  C   . VAL   A 1 33  ? -1.776  -9.674  -9.511  1.00 62.94  ? 76  VAL   A C   1 
ATOM   219  O  O   . VAL   A 1 33  ? -2.015  -10.792 -9.046  1.00 62.92  ? 76  VAL   A O   1 
ATOM   220  C  CB  . VAL   A 1 33  ? -2.592  -8.677  -11.719 1.00 62.85  ? 76  VAL   A CB  1 
ATOM   221  C  CG1 . VAL   A 1 33  ? -2.221  -8.301  -13.155 1.00 63.01  ? 76  VAL   A CG1 1 
ATOM   222  C  CG2 . VAL   A 1 33  ? -3.924  -9.400  -11.657 1.00 62.70  ? 76  VAL   A CG2 1 
ATOM   223  N  N   . ALA   A 1 34  ? -1.762  -8.550  -8.755  1.00 62.47  ? 77  ALA   A N   1 
ATOM   224  C  CA  . ALA   A 1 34  ? -2.106  -8.530  -7.341  1.00 62.28  ? 77  ALA   A CA  1 
ATOM   225  C  C   . ALA   A 1 34  ? -3.107  -7.400  -7.078  1.00 61.42  ? 77  ALA   A C   1 
ATOM   226  O  O   . ALA   A 1 34  ? -2.917  -6.278  -7.540  1.00 60.92  ? 77  ALA   A O   1 
ATOM   227  C  CB  . ALA   A 1 34  ? -0.864  -8.370  -6.467  1.00 62.33  ? 77  ALA   A CB  1 
ATOM   228  N  N   . LEU   A 1 35  ? -4.183  -7.712  -6.338  1.00 60.70  ? 78  LEU   A N   1 
ATOM   229  C  CA  . LEU   A 1 35  ? -5.217  -6.754  -5.969  1.00 59.43  ? 78  LEU   A CA  1 
ATOM   230  C  C   . LEU   A 1 35  ? -4.987  -6.393  -4.503  1.00 60.23  ? 78  LEU   A C   1 
ATOM   231  O  O   . LEU   A 1 35  ? -5.033  -7.271  -3.634  1.00 60.33  ? 78  LEU   A O   1 
ATOM   232  C  CB  . LEU   A 1 35  ? -6.599  -7.402  -6.133  1.00 58.03  ? 78  LEU   A CB  1 
ATOM   233  C  CG  . LEU   A 1 35  ? -7.800  -6.491  -5.879  1.00 57.28  ? 78  LEU   A CG  1 
ATOM   234  C  CD1 . LEU   A 1 35  ? -7.823  -5.333  -6.859  1.00 57.27  ? 78  LEU   A CD1 1 
ATOM   235  C  CD2 . LEU   A 1 35  ? -9.096  -7.265  -5.980  1.00 56.88  ? 78  LEU   A CD2 1 
ATOM   236  N  N   . ASP   A 1 36  ? -4.710  -5.114  -4.223  1.00 60.31  ? 79  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 36  ? -4.500  -4.671  -2.855  1.00 60.71  ? 79  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 36  ? -5.849  -4.358  -2.169  1.00 60.55  ? 79  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 36  ? -6.903  -4.435  -2.805  1.00 60.37  ? 79  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 36  ? -3.462  -3.518  -2.776  1.00 63.02  ? 79  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 36  ? -3.941  -2.154  -3.234  1.00 68.38  ? 79  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 36  ? -5.082  -2.056  -3.703  1.00 69.37  ? 79  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 36  ? -3.175  -1.178  -3.097  1.00 71.25  ? 79  ASP   A OD2 1 
ATOM   244  N  N   . GLU   A 1 37  ? -5.815  -4.018  -0.881  1.00 60.45  ? 80  GLU   A N   1 
ATOM   245  C  CA  . GLU   A 1 37  ? -7.014  -3.707  -0.118  1.00 60.99  ? 80  GLU   A CA  1 
ATOM   246  C  C   . GLU   A 1 37  ? -7.743  -2.433  -0.594  1.00 61.09  ? 80  GLU   A C   1 
ATOM   247  O  O   . GLU   A 1 37  ? -8.931  -2.283  -0.344  1.00 61.36  ? 80  GLU   A O   1 
ATOM   248  C  CB  . GLU   A 1 37  ? -6.685  -3.643  1.373   1.00 63.07  ? 80  GLU   A CB  1 
ATOM   249  C  CG  . GLU   A 1 37  ? -7.929  -3.579  2.233   1.00 68.36  ? 80  GLU   A CG  1 
ATOM   250  C  CD  . GLU   A 1 37  ? -7.666  -3.326  3.697   1.00 73.32  ? 80  GLU   A CD  1 
ATOM   251  O  OE1 . GLU   A 1 37  ? -7.639  -2.143  4.107   1.00 73.65  ? 80  GLU   A OE1 1 
ATOM   252  O  OE2 . GLU   A 1 37  ? -7.478  -4.320  4.434   1.00 75.97  ? 80  GLU   A OE2 1 
ATOM   253  N  N   . SER   A 1 38  ? -7.057  -1.555  -1.338  1.00 60.41  ? 81  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 38  ? -7.676  -0.353  -1.884  1.00 59.73  ? 81  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 38  ? -8.318  -0.568  -3.263  1.00 59.05  ? 81  SER   A C   1 
ATOM   256  O  O   . SER   A 1 38  ? -8.761  0.399   -3.882  1.00 59.06  ? 81  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 38  ? -6.660  0.777   -1.961  1.00 61.38  ? 81  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 38  ? -6.072  1.012   -0.690  1.00 65.28  ? 81  SER   A OG  1 
ATOM   259  N  N   . GLY   A 1 39  ? -8.379  -1.809  -3.738  1.00 58.17  ? 82  GLY   A N   1 
ATOM   260  C  CA  . GLY   A 1 39  ? -8.967  -2.106  -5.035  1.00 58.00  ? 82  GLY   A CA  1 
ATOM   261  C  C   . GLY   A 1 39  ? -8.058  -1.821  -6.214  1.00 57.95  ? 82  GLY   A C   1 
ATOM   262  O  O   . GLY   A 1 39  ? -8.526  -1.796  -7.355  1.00 58.12  ? 82  GLY   A O   1 
ATOM   263  N  N   . ASP   A 1 40  ? -6.751  -1.620  -5.965  1.00 57.77  ? 83  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 40  ? -5.788  -1.351  -7.042  1.00 58.51  ? 83  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 40  ? -5.064  -2.625  -7.536  1.00 58.25  ? 83  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 40  ? -4.616  -3.450  -6.738  1.00 57.73  ? 83  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 40  ? -4.745  -0.283  -6.620  1.00 60.12  ? 83  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 40  ? -5.338  1.053   -6.212  1.00 64.02  ? 83  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 40  ? -6.201  1.563   -6.942  1.00 63.82  ? 83  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 40  ? -4.932  1.584   -5.161  1.00 67.02  ? 83  ASP   A OD2 1 
ATOM   271  N  N   . PHE   A 1 41  ? -4.964  -2.773  -8.854  1.00 58.41  ? 84  PHE   A N   1 
ATOM   272  C  CA  . PHE   A 1 41  ? -4.256  -3.891  -9.458  1.00 59.26  ? 84  PHE   A CA  1 
ATOM   273  C  C   . PHE   A 1 41  ? -2.808  -3.494  -9.703  1.00 62.25  ? 84  PHE   A C   1 
ATOM   274  O  O   . PHE   A 1 41  ? -2.506  -2.332  -9.969  1.00 62.62  ? 84  PHE   A O   1 
ATOM   275  C  CB  . PHE   A 1 41  ? -4.907  -4.308  -10.787 1.00 57.56  ? 84  PHE   A CB  1 
ATOM   276  C  CG  . PHE   A 1 41  ? -6.164  -5.135  -10.651 1.00 56.60  ? 84  PHE   A CG  1 
ATOM   277  C  CD1 . PHE   A 1 41  ? -6.099  -6.475  -10.299 1.00 56.40  ? 84  PHE   A CD1 1 
ATOM   278  C  CD2 . PHE   A 1 41  ? -7.412  -4.575  -10.880 1.00 56.32  ? 84  PHE   A CD2 1 
ATOM   279  C  CE1 . PHE   A 1 41  ? -7.260  -7.236  -10.178 1.00 56.38  ? 84  PHE   A CE1 1 
ATOM   280  C  CE2 . PHE   A 1 41  ? -8.568  -5.336  -10.748 1.00 56.24  ? 84  PHE   A CE2 1 
ATOM   281  C  CZ  . PHE   A 1 41  ? -8.485  -6.663  -10.406 1.00 55.80  ? 84  PHE   A CZ  1 
ATOM   282  N  N   . SER   A 1 42  ? -1.912  -4.454  -9.623  1.00 64.54  ? 85  SER   A N   1 
ATOM   283  C  CA  . SER   A 1 42  ? -0.491  -4.225  -9.884  1.00 67.40  ? 85  SER   A CA  1 
ATOM   284  C  C   . SER   A 1 42  ? 0.129   -5.457  -10.537 1.00 69.91  ? 85  SER   A C   1 
ATOM   285  O  O   . SER   A 1 42  ? -0.377  -6.561  -10.340 1.00 69.87  ? 85  SER   A O   1 
ATOM   286  C  CB  . SER   A 1 42  ? 0.250   -3.876  -8.599  1.00 69.50  ? 85  SER   A CB  1 
ATOM   287  O  OG  . SER   A 1 42  ? 0.389   -4.997  -7.741  1.00 72.63  ? 85  SER   A OG  1 
ATOM   288  N  N   . LEU   A 1 43  ? 1.212   -5.280  -11.323 1.00 71.89  ? 86  LEU   A N   1 
ATOM   289  C  CA  . LEU   A 1 43  ? 1.850   -6.419  -11.974 1.00 74.24  ? 86  LEU   A CA  1 
ATOM   290  C  C   . LEU   A 1 43  ? 2.768   -7.183  -11.038 1.00 76.34  ? 86  LEU   A C   1 
ATOM   291  O  O   . LEU   A 1 43  ? 3.608   -6.591  -10.359 1.00 76.59  ? 86  LEU   A O   1 
ATOM   292  C  CB  . LEU   A 1 43  ? 2.631   -6.020  -13.239 1.00 74.81  ? 86  LEU   A CB  1 
ATOM   293  C  CG  . LEU   A 1 43  ? 1.864   -5.831  -14.555 1.00 76.80  ? 86  LEU   A CG  1 
ATOM   294  C  CD1 . LEU   A 1 43  ? 2.834   -5.781  -15.710 1.00 77.61  ? 86  LEU   A CD1 1 
ATOM   295  C  CD2 . LEU   A 1 43  ? 0.869   -6.962  -14.814 1.00 77.51  ? 86  LEU   A CD2 1 
ATOM   296  N  N   . VAL   A 1 44  ? 2.630   -8.511  -11.043 1.00 77.76  ? 87  VAL   A N   1 
ATOM   297  C  CA  . VAL   A 1 44  ? 3.446   -9.435  -10.263 1.00 79.60  ? 87  VAL   A CA  1 
ATOM   298  C  C   . VAL   A 1 44  ? 4.324   -10.168 -11.249 1.00 82.28  ? 87  VAL   A C   1 
ATOM   299  O  O   . VAL   A 1 44  ? 3.803   -10.775 -12.186 1.00 82.74  ? 87  VAL   A O   1 
ATOM   300  C  CB  . VAL   A 1 44  ? 2.554   -10.425 -9.479  1.00 79.90  ? 87  VAL   A CB  1 
ATOM   301  C  CG1 . VAL   A 1 44  ? 3.355   -11.629 -8.974  1.00 80.81  ? 87  VAL   A CG1 1 
ATOM   302  C  CG2 . VAL   A 1 44  ? 1.863   -9.719  -8.327  1.00 79.98  ? 87  VAL   A CG2 1 
ATOM   303  N  N   . GLU   A 1 45  ? 5.646   -10.069 -11.100 1.00 83.85  ? 88  GLU   A N   1 
ATOM   304  C  CA  . GLU   A 1 45  ? 6.551   -10.780 -12.014 1.00 85.96  ? 88  GLU   A CA  1 
ATOM   305  C  C   . GLU   A 1 45  ? 7.705   -11.453 -11.265 1.00 86.26  ? 88  GLU   A C   1 
ATOM   306  O  O   . GLU   A 1 45  ? 7.653   -11.634 -10.042 1.00 86.35  ? 88  GLU   A O   1 
ATOM   307  C  CB  . GLU   A 1 45  ? 7.048   -9.883  -13.184 1.00 89.69  ? 88  GLU   A CB  1 
ATOM   308  C  CG  . GLU   A 1 45  ? 6.038   -8.851  -13.699 1.00 94.44  ? 88  GLU   A CG  1 
ATOM   309  C  CD  . GLU   A 1 45  ? 5.168   -9.241  -14.880 1.00 100.45 ? 88  GLU   A CD  1 
ATOM   310  O  OE1 . GLU   A 1 45  ? 3.958   -9.497  -14.674 1.00 100.69 ? 88  GLU   A OE1 1 
ATOM   311  O  OE2 . GLU   A 1 45  ? 5.693   -9.266  -16.018 1.00 103.11 ? 88  GLU   A OE2 1 
ATOM   312  N  N   . GLY   B 2 7   ? -35.822 11.254  -12.133 1.00 71.59  ? 16  GLY   B N   1 
ATOM   313  C  CA  . GLY   B 2 7   ? -35.718 11.878  -13.445 1.00 71.78  ? 16  GLY   B CA  1 
ATOM   314  C  C   . GLY   B 2 7   ? -35.570 10.881  -14.582 1.00 71.59  ? 16  GLY   B C   1 
ATOM   315  O  O   . GLY   B 2 7   ? -36.573 10.435  -15.143 1.00 72.43  ? 16  GLY   B O   1 
ATOM   316  N  N   . GLU   B 2 8   ? -34.324 10.516  -14.939 1.00 70.13  ? 17  GLU   B N   1 
ATOM   317  C  CA  . GLU   B 2 8   ? -34.103 9.555   -16.016 1.00 69.25  ? 17  GLU   B CA  1 
ATOM   318  C  C   . GLU   B 2 8   ? -33.772 8.144   -15.490 1.00 68.39  ? 17  GLU   B C   1 
ATOM   319  O  O   . GLU   B 2 8   ? -32.659 7.884   -15.022 1.00 68.85  ? 17  GLU   B O   1 
ATOM   320  C  CB  . GLU   B 2 8   ? -33.061 10.049  -17.040 1.00 69.89  ? 17  GLU   B CB  1 
ATOM   321  C  CG  . GLU   B 2 8   ? -33.275 9.418   -18.403 1.00 72.39  ? 17  GLU   B CG  1 
ATOM   322  C  CD  . GLU   B 2 8   ? -32.397 9.928   -19.529 1.00 77.59  ? 17  GLU   B CD  1 
ATOM   323  O  OE1 . GLU   B 2 8   ? -31.500 10.767  -19.274 1.00 77.06  ? 17  GLU   B OE1 1 
ATOM   324  O  OE2 . GLU   B 2 8   ? -32.642 9.511   -20.686 1.00 80.65  ? 17  GLU   B OE2 1 
ATOM   325  N  N   A THR   B 2 9   ? -34.752 7.239   -15.561 0.50 67.37  ? 18  THR   B N   1 
ATOM   326  N  N   B THR   B 2 9   ? -34.750 7.239   -15.561 0.50 67.50  ? 18  THR   B N   1 
ATOM   327  C  CA  A THR   B 2 9   ? -34.580 5.862   -15.092 0.50 66.61  ? 18  THR   B CA  1 
ATOM   328  C  CA  B THR   B 2 9   ? -34.556 5.864   -15.114 0.50 66.86  ? 18  THR   B CA  1 
ATOM   329  C  C   A THR   B 2 9   ? -34.569 4.845   -16.263 0.50 65.38  ? 18  THR   B C   1 
ATOM   330  C  C   B THR   B 2 9   ? -34.556 4.851   -16.262 0.50 65.50  ? 18  THR   B C   1 
ATOM   331  O  O   A THR   B 2 9   ? -34.632 3.643   -16.025 0.50 65.50  ? 18  THR   B O   1 
ATOM   332  O  O   B THR   B 2 9   ? -34.623 3.653   -16.004 0.50 65.62  ? 18  THR   B O   1 
ATOM   333  C  CB  A THR   B 2 9   ? -35.625 5.514   -13.990 0.50 68.17  ? 18  THR   B CB  1 
ATOM   334  C  CB  B THR   B 2 9   ? -35.575 5.504   -14.030 0.50 68.69  ? 18  THR   B CB  1 
ATOM   335  O  OG1 A THR   B 2 9   ? -35.916 6.655   -13.169 0.50 69.25  ? 18  THR   B OG1 1 
ATOM   336  O  OG1 B THR   B 2 9   ? -36.892 5.771   -14.520 0.50 70.03  ? 18  THR   B OG1 1 
ATOM   337  C  CG2 A THR   B 2 9   ? -35.179 4.364   -13.097 0.50 68.53  ? 18  THR   B CG2 1 
ATOM   338  C  CG2 B THR   B 2 9   ? -35.335 6.267   -12.735 0.50 69.13  ? 18  THR   B CG2 1 
ATOM   339  N  N   . THR   B 2 10  ? -34.462 5.318   -17.521 1.00 64.11  ? 19  THR   B N   1 
ATOM   340  C  CA  . THR   B 2 10  ? -34.442 4.453   -18.700 1.00 61.50  ? 19  THR   B CA  1 
ATOM   341  C  C   . THR   B 2 10  ? -33.196 3.553   -18.745 1.00 58.71  ? 19  THR   B C   1 
ATOM   342  O  O   . THR   B 2 10  ? -32.086 4.038   -18.529 1.00 58.10  ? 19  THR   B O   1 
ATOM   343  C  CB  . THR   B 2 10  ? -34.518 5.341   -19.973 1.00 62.31  ? 19  THR   B CB  1 
ATOM   344  O  OG1 . THR   B 2 10  ? -35.783 6.001   -20.000 1.00 64.43  ? 19  THR   B OG1 1 
ATOM   345  C  CG2 . THR   B 2 10  ? -34.351 4.560   -21.253 1.00 61.54  ? 19  THR   B CG2 1 
ATOM   346  N  N   . ASP   B 2 11  ? -33.370 2.253   -19.079 1.00 56.88  ? 20  ASP   B N   1 
ATOM   347  C  CA  . ASP   B 2 11  ? -32.257 1.324   -19.277 1.00 56.53  ? 20  ASP   B CA  1 
ATOM   348  C  C   . ASP   B 2 11  ? -31.310 1.891   -20.371 1.00 55.22  ? 20  ASP   B C   1 
ATOM   349  O  O   . ASP   B 2 11  ? -31.783 2.522   -21.321 1.00 55.71  ? 20  ASP   B O   1 
ATOM   350  C  CB  . ASP   B 2 11  ? -32.781 -0.061  -19.735 1.00 58.93  ? 20  ASP   B CB  1 
ATOM   351  C  CG  . ASP   B 2 11  ? -33.151 -1.045  -18.637 1.00 64.42  ? 20  ASP   B CG  1 
ATOM   352  O  OD1 . ASP   B 2 11  ? -33.569 -0.598  -17.547 1.00 64.68  ? 20  ASP   B OD1 1 
ATOM   353  O  OD2 . ASP   B 2 11  ? -33.037 -2.262  -18.875 1.00 67.41  ? 20  ASP   B OD2 1 
ATOM   354  N  N   . GLY   B 2 12  ? -30.007 1.685   -20.218 1.00 53.18  ? 21  GLY   B N   1 
ATOM   355  C  CA  . GLY   B 2 12  ? -29.026 2.198   -21.166 1.00 51.47  ? 21  GLY   B CA  1 
ATOM   356  C  C   . GLY   B 2 12  ? -27.705 2.562   -20.517 1.00 49.88  ? 21  GLY   B C   1 
ATOM   357  O  O   . GLY   B 2 12  ? -27.519 2.326   -19.318 1.00 48.66  ? 21  GLY   B O   1 
ATOM   358  N  N   . VAL   B 2 13  ? -26.757 3.114   -21.323 1.00 49.07  ? 22  VAL   B N   1 
ATOM   359  C  CA  . VAL   B 2 13  ? -25.420 3.543   -20.851 1.00 48.78  ? 22  VAL   B CA  1 
ATOM   360  C  C   . VAL   B 2 13  ? -25.421 5.075   -20.656 1.00 49.29  ? 22  VAL   B C   1 
ATOM   361  O  O   . VAL   B 2 13  ? -26.148 5.767   -21.350 1.00 49.52  ? 22  VAL   B O   1 
ATOM   362  C  CB  . VAL   B 2 13  ? -24.242 2.996   -21.712 1.00 48.54  ? 22  VAL   B CB  1 
ATOM   363  C  CG1 . VAL   B 2 13  ? -24.245 3.558   -23.142 1.00 47.72  ? 22  VAL   B CG1 1 
ATOM   364  C  CG2 . VAL   B 2 13  ? -22.902 3.217   -21.030 1.00 48.46  ? 22  VAL   B CG2 1 
ATOM   365  N  N   . TYR   B 2 14  ? -24.799 5.570   -19.576 1.00 49.78  ? 23  TYR   B N   1 
ATOM   366  C  CA  . TYR   B 2 14  ? -24.843 6.983   -19.214 1.00 49.33  ? 23  TYR   B CA  1 
ATOM   367  C  C   . TYR   B 2 14  ? -23.452 7.523   -18.915 1.00 49.44  ? 23  TYR   B C   1 
ATOM   368  O  O   . TYR   B 2 14  ? -22.618 6.799   -18.401 1.00 50.36  ? 23  TYR   B O   1 
ATOM   369  C  CB  . TYR   B 2 14  ? -25.689 7.169   -17.934 1.00 48.97  ? 23  TYR   B CB  1 
ATOM   370  C  CG  . TYR   B 2 14  ? -27.182 6.990   -18.109 1.00 49.35  ? 23  TYR   B CG  1 
ATOM   371  C  CD1 . TYR   B 2 14  ? -27.730 5.739   -18.356 1.00 50.10  ? 23  TYR   B CD1 1 
ATOM   372  C  CD2 . TYR   B 2 14  ? -28.055 8.057   -17.941 1.00 50.21  ? 23  TYR   B CD2 1 
ATOM   373  C  CE1 . TYR   B 2 14  ? -29.088 5.577   -18.570 1.00 50.92  ? 23  TYR   B CE1 1 
ATOM   374  C  CE2 . TYR   B 2 14  ? -29.421 7.905   -18.139 1.00 51.29  ? 23  TYR   B CE2 1 
ATOM   375  C  CZ  . TYR   B 2 14  ? -29.936 6.658   -18.443 1.00 52.09  ? 23  TYR   B CZ  1 
ATOM   376  O  OH  . TYR   B 2 14  ? -31.292 6.464   -18.544 1.00 53.48  ? 23  TYR   B OH  1 
ATOM   377  N  N   . ARG   B 2 15  ? -23.228 8.808   -19.146 1.00 48.45  ? 24  ARG   B N   1 
ATOM   378  C  CA  . ARG   B 2 15  ? -21.983 9.472   -18.771 1.00 48.30  ? 24  ARG   B CA  1 
ATOM   379  C  C   . ARG   B 2 15  ? -22.126 9.983   -17.340 1.00 48.16  ? 24  ARG   B C   1 
ATOM   380  O  O   . ARG   B 2 15  ? -23.221 10.367  -16.943 1.00 47.62  ? 24  ARG   B O   1 
ATOM   381  C  CB  . ARG   B 2 15  ? -21.740 10.701  -19.659 1.00 49.34  ? 24  ARG   B CB  1 
ATOM   382  C  CG  . ARG   B 2 15  ? -21.618 10.397  -21.122 1.00 51.38  ? 24  ARG   B CG  1 
ATOM   383  C  CD  . ARG   B 2 15  ? -21.455 11.687  -21.874 1.00 55.09  ? 24  ARG   B CD  1 
ATOM   384  N  NE  . ARG   B 2 15  ? -21.745 11.497  -23.292 1.00 57.06  ? 24  ARG   B NE  1 
ATOM   385  C  CZ  . ARG   B 2 15  ? -20.839 11.222  -24.215 1.00 58.19  ? 24  ARG   B CZ  1 
ATOM   386  N  NH1 . ARG   B 2 15  ? -19.556 11.103  -23.884 1.00 58.92  ? 24  ARG   B NH1 1 
ATOM   387  N  NH2 . ARG   B 2 15  ? -21.205 11.035  -25.471 1.00 57.73  ? 24  ARG   B NH2 1 
ATOM   388  N  N   . VAL   B 2 16  ? -21.027 10.041  -16.586 1.00 48.38  ? 25  VAL   B N   1 
ATOM   389  C  CA  . VAL   B 2 16  ? -20.998 10.597  -15.227 1.00 49.22  ? 25  VAL   B CA  1 
ATOM   390  C  C   . VAL   B 2 16  ? -20.184 11.881  -15.330 1.00 50.29  ? 25  VAL   B C   1 
ATOM   391  O  O   . VAL   B 2 16  ? -19.009 11.839  -15.689 1.00 50.46  ? 25  VAL   B O   1 
ATOM   392  C  CB  . VAL   B 2 16  ? -20.417 9.633   -14.152 1.00 49.92  ? 25  VAL   B CB  1 
ATOM   393  C  CG1 . VAL   B 2 16  ? -20.476 10.273  -12.766 1.00 50.44  ? 25  VAL   B CG1 1 
ATOM   394  C  CG2 . VAL   B 2 16  ? -21.155 8.299   -14.150 1.00 49.99  ? 25  VAL   B CG2 1 
ATOM   395  N  N   . MET   B 2 17  ? -20.817 13.014  -15.071 1.00 51.21  ? 26  MET   B N   1 
ATOM   396  C  CA  . MET   B 2 17  ? -20.226 14.335  -15.219 1.00 53.16  ? 26  MET   B CA  1 
ATOM   397  C  C   . MET   B 2 17  ? -20.127 15.090  -13.892 1.00 55.89  ? 26  MET   B C   1 
ATOM   398  O  O   . MET   B 2 17  ? -20.872 14.811  -12.966 1.00 56.09  ? 26  MET   B O   1 
ATOM   399  C  CB  . MET   B 2 17  ? -21.118 15.188  -16.157 1.00 52.98  ? 26  MET   B CB  1 
ATOM   400  C  CG  . MET   B 2 17  ? -21.537 14.516  -17.443 1.00 54.03  ? 26  MET   B CG  1 
ATOM   401  S  SD  . MET   B 2 17  ? -20.134 14.155  -18.501 1.00 57.00  ? 26  MET   B SD  1 
ATOM   402  C  CE  . MET   B 2 17  ? -19.735 15.779  -19.081 1.00 48.65  ? 26  MET   B CE  1 
ATOM   403  N  N   . THR   B 2 18  ? -19.242 16.094  -13.837 1.00 57.95  ? 27  THR   B N   1 
ATOM   404  C  CA  . THR   B 2 18  ? -19.066 16.990  -12.701 1.00 60.36  ? 27  THR   B CA  1 
ATOM   405  C  C   . THR   B 2 18  ? -18.874 18.424  -13.174 1.00 62.81  ? 27  THR   B C   1 
ATOM   406  O  O   . THR   B 2 18  ? -18.339 18.669  -14.251 1.00 62.40  ? 27  THR   B O   1 
ATOM   407  C  CB  . THR   B 2 18  ? -17.924 16.553  -11.745 1.00 61.51  ? 27  THR   B CB  1 
ATOM   408  O  OG1 . THR   B 2 18  ? -17.852 17.502  -10.668 1.00 62.98  ? 27  THR   B OG1 1 
ATOM   409  C  CG2 . THR   B 2 18  ? -16.569 16.479  -12.432 1.00 61.14  ? 27  THR   B CG2 1 
ATOM   410  N  N   . ARG   B 2 19  ? -19.299 19.376  -12.350 1.00 65.51  ? 28  ARG   B N   1 
ATOM   411  C  CA  . ARG   B 2 19  ? -19.119 20.792  -12.662 1.00 68.62  ? 28  ARG   B CA  1 
ATOM   412  C  C   . ARG   B 2 19  ? -18.104 21.489  -11.712 1.00 71.05  ? 28  ARG   B C   1 
ATOM   413  O  O   . ARG   B 2 19  ? -17.824 22.675  -11.888 1.00 71.41  ? 28  ARG   B O   1 
ATOM   414  C  CB  . ARG   B 2 19  ? -20.475 21.518  -12.724 1.00 70.95  ? 28  ARG   B CB  1 
ATOM   415  C  CG  . ARG   B 2 19  ? -21.361 21.026  -13.881 1.00 76.33  ? 28  ARG   B CG  1 
ATOM   416  C  CD  . ARG   B 2 19  ? -22.292 22.127  -14.367 1.00 81.73  ? 28  ARG   B CD  1 
ATOM   417  N  NE  . ARG   B 2 19  ? -22.668 22.018  -15.782 1.00 85.71  ? 28  ARG   B NE  1 
ATOM   418  C  CZ  . ARG   B 2 19  ? -23.913 21.806  -16.214 1.00 88.82  ? 28  ARG   B CZ  1 
ATOM   419  N  NH1 . ARG   B 2 19  ? -24.908 21.646  -15.347 1.00 88.82  ? 28  ARG   B NH1 1 
ATOM   420  N  NH2 . ARG   B 2 19  ? -24.169 21.741  -17.517 1.00 88.80  ? 28  ARG   B NH2 1 
ATOM   421  N  N   . ARG   B 2 20  ? -17.512 20.726  -10.754 1.00 72.61  ? 29  ARG   B N   1 
ATOM   422  C  CA  . ARG   B 2 20  ? -16.540 21.174  -9.753  1.00 74.46  ? 29  ARG   B CA  1 
ATOM   423  C  C   . ARG   B 2 20  ? -15.255 21.741  -10.369 1.00 74.61  ? 29  ARG   B C   1 
ATOM   424  O  O   . ARG   B 2 20  ? -14.797 22.808  -9.959  1.00 74.83  ? 29  ARG   B O   1 
ATOM   425  C  CB  . ARG   B 2 20  ? -16.223 20.025  -8.788  1.00 77.53  ? 29  ARG   B CB  1 
ATOM   426  C  CG  . ARG   B 2 20  ? -15.292 20.413  -7.647  1.00 83.48  ? 29  ARG   B CG  1 
ATOM   427  C  CD  . ARG   B 2 20  ? -15.001 19.237  -6.727  1.00 89.00  ? 29  ARG   B CD  1 
ATOM   428  N  NE  . ARG   B 2 20  ? -14.600 18.036  -7.467  1.00 93.71  ? 29  ARG   B NE  1 
ATOM   429  C  CZ  . ARG   B 2 20  ? -13.345 17.719  -7.770  1.00 96.69  ? 29  ARG   B CZ  1 
ATOM   430  N  NH1 . ARG   B 2 20  ? -12.343 18.503  -7.387  1.00 96.12  ? 29  ARG   B NH1 1 
ATOM   431  N  NH2 . ARG   B 2 20  ? -13.079 16.606  -8.443  1.00 97.43  ? 29  ARG   B NH2 1 
ATOM   432  N  N   . LEU   B 2 21  ? -14.698 21.059  -11.380 1.00 74.29  ? 30  LEU   B N   1 
ATOM   433  C  CA  . LEU   B 2 21  ? -13.510 21.564  -12.068 1.00 74.12  ? 30  LEU   B CA  1 
ATOM   434  C  C   . LEU   B 2 21  ? -13.941 22.630  -13.123 1.00 73.63  ? 30  LEU   B C   1 
ATOM   435  O  O   . LEU   B 2 21  ? -15.047 23.180  -13.034 1.00 74.05  ? 30  LEU   B O   1 
ATOM   436  C  CB  . LEU   B 2 21  ? -12.719 20.395  -12.718 1.00 74.31  ? 30  LEU   B CB  1 
ATOM   437  C  CG  . LEU   B 2 21  ? -12.004 19.363  -11.840 1.00 76.40  ? 30  LEU   B CG  1 
ATOM   438  C  CD1 . LEU   B 2 21  ? -11.446 19.959  -10.550 1.00 77.00  ? 30  LEU   B CD1 1 
ATOM   439  C  CD2 . LEU   B 2 21  ? -12.880 18.158  -11.579 1.00 77.39  ? 30  LEU   B CD2 1 
ATOM   440  N  N   . LEU   B 2 22  ? -13.069 22.943  -14.100 1.00 72.66  ? 31  LEU   B N   1 
ATOM   441  C  CA  . LEU   B 2 22  ? -13.384 23.876  -15.179 1.00 71.92  ? 31  LEU   B CA  1 
ATOM   442  C  C   . LEU   B 2 22  ? -14.437 23.213  -16.083 1.00 70.54  ? 31  LEU   B C   1 
ATOM   443  O  O   . LEU   B 2 22  ? -14.351 21.999  -16.322 1.00 70.79  ? 31  LEU   B O   1 
ATOM   444  C  CB  . LEU   B 2 22  ? -12.112 24.114  -15.988 1.00 72.12  ? 31  LEU   B CB  1 
ATOM   445  C  CG  . LEU   B 2 22  ? -12.229 25.098  -17.108 1.00 73.66  ? 31  LEU   B CG  1 
ATOM   446  C  CD1 . LEU   B 2 22  ? -11.982 26.503  -16.612 1.00 74.05  ? 31  LEU   B CD1 1 
ATOM   447  C  CD2 . LEU   B 2 22  ? -11.261 24.740  -18.219 1.00 74.63  ? 31  LEU   B CD2 1 
ATOM   448  N  N   . GLY   B 2 23  ? -15.428 23.988  -16.535 1.00 68.37  ? 32  GLY   B N   1 
ATOM   449  C  CA  . GLY   B 2 23  ? -16.498 23.493  -17.396 1.00 67.10  ? 32  GLY   B CA  1 
ATOM   450  C  C   . GLY   B 2 23  ? -17.189 22.226  -16.917 1.00 65.80  ? 32  GLY   B C   1 
ATOM   451  O  O   . GLY   B 2 23  ? -17.328 21.994  -15.711 1.00 65.75  ? 32  GLY   B O   1 
ATOM   452  N  N   . SER   B 2 24  ? -17.651 21.403  -17.862 1.00 64.65  ? 33  SER   B N   1 
ATOM   453  C  CA  . SER   B 2 24  ? -18.281 20.129  -17.525 1.00 63.89  ? 33  SER   B CA  1 
ATOM   454  C  C   . SER   B 2 24  ? -17.252 19.055  -17.846 1.00 62.69  ? 33  SER   B C   1 
ATOM   455  O  O   . SER   B 2 24  ? -16.761 18.984  -18.977 1.00 62.04  ? 33  SER   B O   1 
ATOM   456  C  CB  . SER   B 2 24  ? -19.544 19.910  -18.352 1.00 65.45  ? 33  SER   B CB  1 
ATOM   457  O  OG  . SER   B 2 24  ? -20.658 20.630  -17.848 1.00 67.74  ? 33  SER   B OG  1 
ATOM   458  N  N   . THR   B 2 25  ? -16.899 18.236  -16.844 1.00 61.83  ? 34  THR   B N   1 
ATOM   459  C  CA  . THR   B 2 25  ? -15.891 17.189  -17.003 1.00 60.60  ? 34  THR   B CA  1 
ATOM   460  C  C   . THR   B 2 25  ? -16.464 15.801  -16.787 1.00 59.08  ? 34  THR   B C   1 
ATOM   461  O  O   . THR   B 2 25  ? -17.152 15.560  -15.789 1.00 58.93  ? 34  THR   B O   1 
ATOM   462  C  CB  . THR   B 2 25  ? -14.747 17.435  -16.018 1.00 62.18  ? 34  THR   B CB  1 
ATOM   463  O  OG1 . THR   B 2 25  ? -14.255 18.766  -16.201 1.00 63.85  ? 34  THR   B OG1 1 
ATOM   464  C  CG2 . THR   B 2 25  ? -13.613 16.431  -16.170 1.00 62.29  ? 34  THR   B CG2 1 
ATOM   465  N  N   . GLN   B 2 26  ? -16.140 14.869  -17.699 1.00 57.68  ? 35  GLN   B N   1 
ATOM   466  C  CA  . GLN   B 2 26  ? -16.579 13.484  -17.585 1.00 56.65  ? 35  GLN   B CA  1 
ATOM   467  C  C   . GLN   B 2 26  ? -15.598 12.688  -16.710 1.00 55.68  ? 35  GLN   B C   1 
ATOM   468  O  O   . GLN   B 2 26  ? -14.436 12.480  -17.099 1.00 55.85  ? 35  GLN   B O   1 
ATOM   469  C  CB  . GLN   B 2 26  ? -16.718 12.841  -18.976 1.00 57.16  ? 35  GLN   B CB  1 
ATOM   470  C  CG  . GLN   B 2 26  ? -17.043 11.353  -18.927 1.00 58.08  ? 35  GLN   B CG  1 
ATOM   471  C  CD  . GLN   B 2 26  ? -17.549 10.840  -20.245 1.00 59.41  ? 35  GLN   B CD  1 
ATOM   472  O  OE1 . GLN   B 2 26  ? -18.300 11.519  -20.952 1.00 60.18  ? 35  GLN   B OE1 1 
ATOM   473  N  NE2 . GLN   B 2 26  ? -17.153 9.626   -20.599 1.00 58.77  ? 35  GLN   B NE2 1 
ATOM   474  N  N   . VAL   B 2 27  ? -16.067 12.256  -15.528 1.00 53.94  ? 36  VAL   B N   1 
ATOM   475  C  CA  . VAL   B 2 27  ? -15.261 11.463  -14.608 1.00 52.94  ? 36  VAL   B CA  1 
ATOM   476  C  C   . VAL   B 2 27  ? -15.382 9.936   -14.854 1.00 51.15  ? 36  VAL   B C   1 
ATOM   477  O  O   . VAL   B 2 27  ? -14.477 9.168   -14.508 1.00 51.41  ? 36  VAL   B O   1 
ATOM   478  C  CB  . VAL   B 2 27  ? -15.562 11.849  -13.140 1.00 54.46  ? 36  VAL   B CB  1 
ATOM   479  C  CG1 . VAL   B 2 27  ? -15.054 13.258  -12.846 1.00 55.40  ? 36  VAL   B CG1 1 
ATOM   480  C  CG2 . VAL   B 2 27  ? -17.060 11.752  -12.836 1.00 55.01  ? 36  VAL   B CG2 1 
ATOM   481  N  N   . GLY   B 2 28  ? -16.470 9.516   -15.477 1.00 49.23  ? 37  GLY   B N   1 
ATOM   482  C  CA  . GLY   B 2 28  ? -16.706 8.112   -15.754 1.00 48.68  ? 37  GLY   B CA  1 
ATOM   483  C  C   . GLY   B 2 28  ? -17.999 7.879   -16.500 1.00 47.84  ? 37  GLY   B C   1 
ATOM   484  O  O   . GLY   B 2 28  ? -18.582 8.816   -17.047 1.00 47.02  ? 37  GLY   B O   1 
ATOM   485  N  N   . VAL   B 2 29  ? -18.436 6.604   -16.539 1.00 47.13  ? 38  VAL   B N   1 
ATOM   486  C  CA  . VAL   B 2 29  ? -19.607 6.057   -17.249 1.00 46.33  ? 38  VAL   B CA  1 
ATOM   487  C  C   . VAL   B 2 29  ? -20.327 5.029   -16.328 1.00 45.44  ? 38  VAL   B C   1 
ATOM   488  O  O   . VAL   B 2 29  ? -19.731 4.521   -15.368 1.00 45.06  ? 38  VAL   B O   1 
ATOM   489  C  CB  . VAL   B 2 29  ? -19.095 5.370   -18.576 1.00 45.93  ? 38  VAL   B CB  1 
ATOM   490  C  CG1 . VAL   B 2 29  ? -20.196 4.655   -19.336 1.00 45.78  ? 38  VAL   B CG1 1 
ATOM   491  C  CG2 . VAL   B 2 29  ? -18.417 6.369   -19.483 1.00 46.20  ? 38  VAL   B CG2 1 
ATOM   492  N  N   . GLY   B 2 30  ? -21.574 4.700   -16.654 1.00 44.49  ? 39  GLY   B N   1 
ATOM   493  C  CA  . GLY   B 2 30  ? -22.337 3.725   -15.890 1.00 44.55  ? 39  GLY   B CA  1 
ATOM   494  C  C   . GLY   B 2 30  ? -23.479 3.067   -16.642 1.00 45.09  ? 39  GLY   B C   1 
ATOM   495  O  O   . GLY   B 2 30  ? -23.848 3.495   -17.734 1.00 45.25  ? 39  GLY   B O   1 
ATOM   496  N  N   . VAL   B 2 31  ? -24.052 2.016   -16.054 1.00 45.60  ? 40  VAL   B N   1 
ATOM   497  C  CA  . VAL   B 2 31  ? -25.132 1.248   -16.654 1.00 46.99  ? 40  VAL   B CA  1 
ATOM   498  C  C   . VAL   B 2 31  ? -26.403 1.339   -15.851 1.00 47.41  ? 40  VAL   B C   1 
ATOM   499  O  O   . VAL   B 2 31  ? -26.405 0.993   -14.665 1.00 48.02  ? 40  VAL   B O   1 
ATOM   500  C  CB  . VAL   B 2 31  ? -24.721 -0.227  -16.786 1.00 49.23  ? 40  VAL   B CB  1 
ATOM   501  C  CG1 . VAL   B 2 31  ? -25.885 -1.086  -17.275 1.00 50.57  ? 40  VAL   B CG1 1 
ATOM   502  C  CG2 . VAL   B 2 31  ? -23.513 -0.369  -17.707 1.00 49.89  ? 40  VAL   B CG2 1 
ATOM   503  N  N   . MET   B 2 32  ? -27.499 1.749   -16.496 1.00 46.35  ? 41  MET   B N   1 
ATOM   504  C  CA  . MET   B 2 32  ? -28.792 1.764   -15.844 1.00 46.14  ? 41  MET   B CA  1 
ATOM   505  C  C   . MET   B 2 32  ? -29.513 0.509   -16.307 1.00 46.56  ? 41  MET   B C   1 
ATOM   506  O  O   . MET   B 2 32  ? -29.604 0.261   -17.513 1.00 46.84  ? 41  MET   B O   1 
ATOM   507  C  CB  . MET   B 2 32  ? -29.599 3.009   -16.250 1.00 46.31  ? 41  MET   B CB  1 
ATOM   508  C  CG  . MET   B 2 32  ? -30.891 3.166   -15.487 1.00 48.08  ? 41  MET   B CG  1 
ATOM   509  S  SD  . MET   B 2 32  ? -30.691 3.764   -13.779 1.00 49.65  ? 41  MET   B SD  1 
ATOM   510  C  CE  . MET   B 2 32  ? -30.210 5.457   -14.085 1.00 47.85  ? 41  MET   B CE  1 
ATOM   511  N  N   . GLN   B 2 33  ? -29.972 -0.309  -15.360 1.00 46.56  ? 42  GLN   B N   1 
ATOM   512  C  CA  . GLN   B 2 33  ? -30.715 -1.533  -15.643 1.00 47.29  ? 42  GLN   B CA  1 
ATOM   513  C  C   . GLN   B 2 33  ? -31.630 -1.824  -14.459 1.00 47.75  ? 42  GLN   B C   1 
ATOM   514  O  O   . GLN   B 2 33  ? -31.184 -1.742  -13.312 1.00 47.70  ? 42  GLN   B O   1 
ATOM   515  C  CB  . GLN   B 2 33  ? -29.773 -2.730  -15.866 1.00 49.53  ? 42  GLN   B CB  1 
ATOM   516  C  CG  . GLN   B 2 33  ? -30.508 -3.950  -16.420 1.00 54.85  ? 42  GLN   B CG  1 
ATOM   517  C  CD  . GLN   B 2 33  ? -29.574 -5.068  -16.819 1.00 62.51  ? 42  GLN   B CD  1 
ATOM   518  O  OE1 . GLN   B 2 33  ? -29.542 -6.142  -16.204 1.00 64.36  ? 42  GLN   B OE1 1 
ATOM   519  N  NE2 . GLN   B 2 33  ? -28.781 -4.840  -17.858 1.00 64.52  ? 42  GLN   B NE2 1 
ATOM   520  N  N   . GLU   B 2 34  ? -32.904 -2.132  -14.733 1.00 47.85  ? 43  GLU   B N   1 
ATOM   521  C  CA  . GLU   B 2 34  ? -33.906 -2.459  -13.726 1.00 49.13  ? 43  GLU   B CA  1 
ATOM   522  C  C   . GLU   B 2 34  ? -34.062 -1.375  -12.618 1.00 49.77  ? 43  GLU   B C   1 
ATOM   523  O  O   . GLU   B 2 34  ? -34.369 -1.678  -11.462 1.00 49.88  ? 43  GLU   B O   1 
ATOM   524  C  CB  . GLU   B 2 34  ? -33.635 -3.853  -13.137 1.00 51.80  ? 43  GLU   B CB  1 
ATOM   525  C  CG  . GLU   B 2 34  ? -33.539 -4.934  -14.205 1.00 56.68  ? 43  GLU   B CG  1 
ATOM   526  C  CD  . GLU   B 2 34  ? -33.257 -6.335  -13.691 1.00 64.91  ? 43  GLU   B CD  1 
ATOM   527  O  OE1 . GLU   B 2 34  ? -34.035 -6.814  -12.835 1.00 67.83  ? 43  GLU   B OE1 1 
ATOM   528  O  OE2 . GLU   B 2 34  ? -32.260 -6.954  -14.132 1.00 66.02  ? 43  GLU   B OE2 1 
ATOM   529  N  N   . GLY   B 2 35  ? -33.880 -0.120  -13.006 1.00 49.28  ? 44  GLY   B N   1 
ATOM   530  C  CA  . GLY   B 2 35  ? -34.011 0.994   -12.083 1.00 49.20  ? 44  GLY   B CA  1 
ATOM   531  C  C   . GLY   B 2 35  ? -32.820 1.202   -11.173 1.00 49.19  ? 44  GLY   B C   1 
ATOM   532  O  O   . GLY   B 2 35  ? -32.923 1.960   -10.211 1.00 50.07  ? 44  GLY   B O   1 
ATOM   533  N  N   . VAL   B 2 36  ? -31.670 0.559   -11.468 1.00 48.11  ? 45  VAL   B N   1 
ATOM   534  C  CA  . VAL   B 2 36  ? -30.449 0.667   -10.668 1.00 46.97  ? 45  VAL   B CA  1 
ATOM   535  C  C   . VAL   B 2 36  ? -29.273 1.209   -11.517 1.00 46.13  ? 45  VAL   B C   1 
ATOM   536  O  O   . VAL   B 2 36  ? -29.102 0.816   -12.683 1.00 45.51  ? 45  VAL   B O   1 
ATOM   537  C  CB  . VAL   B 2 36  ? -30.111 -0.704  -10.029 1.00 47.39  ? 45  VAL   B CB  1 
ATOM   538  C  CG1 . VAL   B 2 36  ? -28.738 -0.689  -9.354  1.00 48.27  ? 45  VAL   B CG1 1 
ATOM   539  C  CG2 . VAL   B 2 36  ? -31.184 -1.124  -9.045  1.00 47.11  ? 45  VAL   B CG2 1 
ATOM   540  N  N   . PHE   B 2 37  ? -28.495 2.152   -10.951 1.00 45.29  ? 46  PHE   B N   1 
ATOM   541  C  CA  . PHE   B 2 37  ? -27.336 2.684   -11.680 1.00 44.45  ? 46  PHE   B CA  1 
ATOM   542  C  C   . PHE   B 2 37  ? -26.079 1.976   -11.165 1.00 42.95  ? 46  PHE   B C   1 
ATOM   543  O  O   . PHE   B 2 37  ? -25.837 1.933   -9.967  1.00 42.02  ? 46  PHE   B O   1 
ATOM   544  C  CB  . PHE   B 2 37  ? -27.235 4.219   -11.547 1.00 44.25  ? 46  PHE   B CB  1 
ATOM   545  C  CG  . PHE   B 2 37  ? -26.290 4.833   -12.552 1.00 44.51  ? 46  PHE   B CG  1 
ATOM   546  C  CD1 . PHE   B 2 37  ? -26.569 4.790   -13.902 1.00 45.39  ? 46  PHE   B CD1 1 
ATOM   547  C  CD2 . PHE   B 2 37  ? -25.125 5.455   -12.141 1.00 45.12  ? 46  PHE   B CD2 1 
ATOM   548  C  CE1 . PHE   B 2 37  ? -25.683 5.322   -14.831 1.00 46.10  ? 46  PHE   B CE1 1 
ATOM   549  C  CE2 . PHE   B 2 37  ? -24.234 5.975   -13.066 1.00 45.70  ? 46  PHE   B CE2 1 
ATOM   550  C  CZ  . PHE   B 2 37  ? -24.527 5.919   -14.408 1.00 45.91  ? 46  PHE   B CZ  1 
ATOM   551  N  N   . HIS   B 2 38  ? -25.312 1.380   -12.072 1.00 42.36  ? 47  HIS   B N   1 
ATOM   552  C  CA  . HIS   B 2 38  ? -24.119 0.606   -11.761 1.00 41.66  ? 47  HIS   B CA  1 
ATOM   553  C  C   . HIS   B 2 38  ? -22.926 1.331   -12.308 1.00 41.70  ? 47  HIS   B C   1 
ATOM   554  O  O   . HIS   B 2 38  ? -22.889 1.581   -13.498 1.00 41.34  ? 47  HIS   B O   1 
ATOM   555  C  CB  . HIS   B 2 38  ? -24.192 -0.754  -12.483 1.00 40.99  ? 47  HIS   B CB  1 
ATOM   556  C  CG  . HIS   B 2 38  ? -25.444 -1.528  -12.212 1.00 42.11  ? 47  HIS   B CG  1 
ATOM   557  N  ND1 . HIS   B 2 38  ? -26.676 -1.097  -12.680 1.00 43.55  ? 47  HIS   B ND1 1 
ATOM   558  C  CD2 . HIS   B 2 38  ? -25.617 -2.697  -11.548 1.00 42.95  ? 47  HIS   B CD2 1 
ATOM   559  C  CE1 . HIS   B 2 38  ? -27.560 -1.985  -12.241 1.00 43.93  ? 47  HIS   B CE1 1 
ATOM   560  N  NE2 . HIS   B 2 38  ? -26.979 -2.952  -11.542 1.00 43.71  ? 47  HIS   B NE2 1 
ATOM   561  N  N   . THR   B 2 39  ? -21.930 1.643   -11.470 1.00 42.06  ? 48  THR   B N   1 
ATOM   562  C  CA  . THR   B 2 39  ? -20.696 2.278   -11.953 1.00 42.26  ? 48  THR   B CA  1 
ATOM   563  C  C   . THR   B 2 39  ? -19.474 1.787   -11.109 1.00 42.93  ? 48  THR   B C   1 
ATOM   564  O  O   . THR   B 2 39  ? -19.603 0.844   -10.336 1.00 42.76  ? 48  THR   B O   1 
ATOM   565  C  CB  . THR   B 2 39  ? -20.879 3.809   -12.030 1.00 43.32  ? 48  THR   B CB  1 
ATOM   566  O  OG1 . THR   B 2 39  ? -19.723 4.379   -12.643 1.00 44.06  ? 48  THR   B OG1 1 
ATOM   567  C  CG2 . THR   B 2 39  ? -21.085 4.426   -10.656 1.00 43.77  ? 48  THR   B CG2 1 
ATOM   568  N  N   . MET   B 2 40  ? -18.284 2.372   -11.310 1.00 43.30  ? 49  MET   B N   1 
ATOM   569  C  CA  . MET   B 2 40  ? -17.100 2.006   -10.574 1.00 43.68  ? 49  MET   B CA  1 
ATOM   570  C  C   . MET   B 2 40  ? -16.966 2.919   -9.359  1.00 44.26  ? 49  MET   B C   1 
ATOM   571  O  O   . MET   B 2 40  ? -17.196 4.120   -9.479  1.00 44.12  ? 49  MET   B O   1 
ATOM   572  C  CB  . MET   B 2 40  ? -15.881 2.072   -11.515 1.00 44.03  ? 49  MET   B CB  1 
ATOM   573  C  CG  . MET   B 2 40  ? -16.080 1.223   -12.762 1.00 46.51  ? 49  MET   B CG  1 
ATOM   574  S  SD  . MET   B 2 40  ? -14.686 0.155   -13.168 1.00 58.05  ? 49  MET   B SD  1 
ATOM   575  C  CE  . MET   B 2 40  ? -15.031 -1.279  -12.200 1.00 55.84  ? 49  MET   B CE  1 
ATOM   576  N  N   . TRP   B 2 41  ? -16.590 2.372   -8.178  1.00 44.67  ? 50  TRP   B N   1 
ATOM   577  C  CA  A TRP   B 2 41  ? -16.444 3.181   -6.959  0.50 45.50  ? 50  TRP   B CA  1 
ATOM   578  C  CA  B TRP   B 2 41  ? -16.465 3.192   -6.970  0.50 45.27  ? 50  TRP   B CA  1 
ATOM   579  C  C   . TRP   B 2 41  ? -15.523 4.378   -7.154  1.00 45.60  ? 50  TRP   B C   1 
ATOM   580  O  O   . TRP   B 2 41  ? -15.858 5.451   -6.707  1.00 46.06  ? 50  TRP   B O   1 
ATOM   581  C  CB  A TRP   B 2 41  ? -15.951 2.343   -5.762  0.50 45.70  ? 50  TRP   B CB  1 
ATOM   582  C  CB  B TRP   B 2 41  ? -16.084 2.361   -5.727  0.50 45.16  ? 50  TRP   B CB  1 
ATOM   583  C  CG  A TRP   B 2 41  ? -16.102 3.033   -4.428  0.50 46.69  ? 50  TRP   B CG  1 
ATOM   584  C  CG  B TRP   B 2 41  ? -15.977 3.178   -4.463  0.50 45.75  ? 50  TRP   B CG  1 
ATOM   585  C  CD1 A TRP   B 2 41  ? -17.139 2.895   -3.553  0.50 47.51  ? 50  TRP   B CD1 1 
ATOM   586  C  CD1 B TRP   B 2 41  ? -14.900 3.902   -4.042  0.50 46.51  ? 50  TRP   B CD1 1 
ATOM   587  C  CD2 A TRP   B 2 41  ? -15.167 3.931   -3.802  0.50 46.87  ? 50  TRP   B CD2 1 
ATOM   588  C  CD2 B TRP   B 2 41  ? -16.982 3.332   -3.450  0.50 45.65  ? 50  TRP   B CD2 1 
ATOM   589  N  NE1 A TRP   B 2 41  ? -16.925 3.672   -2.440  0.50 48.01  ? 50  TRP   B NE1 1 
ATOM   590  N  NE1 B TRP   B 2 41  ? -15.188 4.532   -2.856  0.50 46.83  ? 50  TRP   B NE1 1 
ATOM   591  C  CE2 A TRP   B 2 41  ? -15.725 4.324   -2.570  0.50 47.74  ? 50  TRP   B CE2 1 
ATOM   592  C  CE2 B TRP   B 2 41  ? -16.462 4.204   -2.473  0.50 46.49  ? 50  TRP   B CE2 1 
ATOM   593  C  CE3 A TRP   B 2 41  ? -13.921 4.456   -4.172  0.50 47.47  ? 50  TRP   B CE3 1 
ATOM   594  C  CE3 B TRP   B 2 41  ? -18.288 2.856   -3.298  0.50 46.20  ? 50  TRP   B CE3 1 
ATOM   595  C  CZ2 A TRP   B 2 41  ? -15.084 5.216   -1.709  0.50 48.35  ? 50  TRP   B CZ2 1 
ATOM   596  C  CZ2 B TRP   B 2 41  ? -17.189 4.578   -1.342  0.50 46.88  ? 50  TRP   B CZ2 1 
ATOM   597  C  CZ3 A TRP   B 2 41  ? -13.284 5.331   -3.314  0.50 48.43  ? 50  TRP   B CZ3 1 
ATOM   598  C  CZ3 B TRP   B 2 41  ? -19.011 3.240   -2.181  0.50 47.11  ? 50  TRP   B CZ3 1 
ATOM   599  C  CH2 A TRP   B 2 41  ? -13.853 5.683   -2.087  0.50 48.56  ? 50  TRP   B CH2 1 
ATOM   600  C  CH2 B TRP   B 2 41  ? -18.456 4.080   -1.214  0.50 47.01  ? 50  TRP   B CH2 1 
ATOM   601  N  N   . HIS   B 2 42  ? -14.348 4.196   -7.794  1.00 45.37  ? 51  HIS   B N   1 
ATOM   602  C  CA  . HIS   B 2 42  ? -13.416 5.327   -7.958  1.00 46.52  ? 51  HIS   B CA  1 
ATOM   603  C  C   . HIS   B 2 42  ? -13.967 6.502   -8.809  1.00 47.65  ? 51  HIS   B C   1 
ATOM   604  O  O   . HIS   B 2 42  ? -13.436 7.608   -8.717  1.00 48.77  ? 51  HIS   B O   1 
ATOM   605  C  CB  . HIS   B 2 42  ? -12.049 4.875   -8.477  1.00 47.38  ? 51  HIS   B CB  1 
ATOM   606  C  CG  . HIS   B 2 42  ? -12.018 4.588   -9.946  1.00 49.55  ? 51  HIS   B CG  1 
ATOM   607  N  ND1 . HIS   B 2 42  ? -12.019 3.289   -10.426 1.00 50.73  ? 51  HIS   B ND1 1 
ATOM   608  C  CD2 . HIS   B 2 42  ? -11.960 5.445   -10.997 1.00 50.91  ? 51  HIS   B CD2 1 
ATOM   609  C  CE1 . HIS   B 2 42  ? -11.979 3.395   -11.739 1.00 51.29  ? 51  HIS   B CE1 1 
ATOM   610  N  NE2 . HIS   B 2 42  ? -11.957 4.675   -12.128 1.00 52.00  ? 51  HIS   B NE2 1 
ATOM   611  N  N   . VAL   B 2 43  ? -15.018 6.282   -9.611  1.00 47.35  ? 52  VAL   B N   1 
ATOM   612  C  CA  . VAL   B 2 43  ? -15.655 7.332   -10.415 1.00 47.63  ? 52  VAL   B CA  1 
ATOM   613  C  C   . VAL   B 2 43  ? -16.439 8.330   -9.522  1.00 48.18  ? 52  VAL   B C   1 
ATOM   614  O  O   . VAL   B 2 43  ? -16.272 9.553   -9.652  1.00 49.04  ? 52  VAL   B O   1 
ATOM   615  C  CB  . VAL   B 2 43  ? -16.576 6.696   -11.487 1.00 48.11  ? 52  VAL   B CB  1 
ATOM   616  C  CG1 . VAL   B 2 43  ? -17.474 7.741   -12.156 1.00 48.50  ? 52  VAL   B CG1 1 
ATOM   617  C  CG2 . VAL   B 2 43  ? -15.766 5.905   -12.520 1.00 48.38  ? 52  VAL   B CG2 1 
ATOM   618  N  N   . THR   B 2 44  ? -17.291 7.814   -8.618  1.00 47.19  ? 53  THR   B N   1 
ATOM   619  C  CA  . THR   B 2 44  ? -18.108 8.682   -7.770  1.00 47.03  ? 53  THR   B CA  1 
ATOM   620  C  C   . THR   B 2 44  ? -17.590 8.846   -6.336  1.00 47.42  ? 53  THR   B C   1 
ATOM   621  O  O   . THR   B 2 44  ? -17.974 9.798   -5.646  1.00 46.71  ? 53  THR   B O   1 
ATOM   622  C  CB  . THR   B 2 44  ? -19.567 8.174   -7.741  1.00 47.85  ? 53  THR   B CB  1 
ATOM   623  O  OG1 . THR   B 2 44  ? -19.630 6.946   -7.008  1.00 49.64  ? 53  THR   B OG1 1 
ATOM   624  C  CG2 . THR   B 2 44  ? -20.165 7.975   -9.129  1.00 47.60  ? 53  THR   B CG2 1 
ATOM   625  N  N   . LYS   B 2 45  ? -16.753 7.912   -5.876  1.00 48.13  ? 54  LYS   B N   1 
ATOM   626  C  CA  . LYS   B 2 45  ? -16.308 7.833   -4.476  1.00 50.25  ? 54  LYS   B CA  1 
ATOM   627  C  C   . LYS   B 2 45  ? -17.535 7.617   -3.524  1.00 50.98  ? 54  LYS   B C   1 
ATOM   628  O  O   . LYS   B 2 45  ? -17.456 7.957   -2.349  1.00 51.46  ? 54  LYS   B O   1 
ATOM   629  C  CB  . LYS   B 2 45  ? -15.482 9.063   -4.017  1.00 52.71  ? 54  LYS   B CB  1 
ATOM   630  C  CG  . LYS   B 2 45  ? -14.352 9.487   -4.934  1.00 57.80  ? 54  LYS   B CG  1 
ATOM   631  C  CD  . LYS   B 2 45  ? -13.293 8.416   -5.148  1.00 63.60  ? 54  LYS   B CD  1 
ATOM   632  C  CE  . LYS   B 2 45  ? -12.179 8.963   -6.030  1.00 68.59  ? 54  LYS   B CE  1 
ATOM   633  N  NZ  . LYS   B 2 45  ? -11.449 7.907   -6.808  1.00 70.81  ? 54  LYS   B NZ  1 
ATOM   634  N  N   . GLY   B 2 46  ? -18.644 7.080   -4.046  1.00 51.19  ? 55  GLY   B N   1 
ATOM   635  C  CA  . GLY   B 2 46  ? -19.862 6.820   -3.288  1.00 51.74  ? 55  GLY   B CA  1 
ATOM   636  C  C   . GLY   B 2 46  ? -20.792 8.002   -3.144  1.00 52.85  ? 55  GLY   B C   1 
ATOM   637  O  O   . GLY   B 2 46  ? -21.785 7.910   -2.423  1.00 54.32  ? 55  GLY   B O   1 
ATOM   638  N  N   . ALA   B 2 47  ? -20.488 9.136   -3.790  1.00 52.36  ? 56  ALA   B N   1 
ATOM   639  C  CA  . ALA   B 2 47  ? -21.313 10.338  -3.651  1.00 52.14  ? 56  ALA   B CA  1 
ATOM   640  C  C   . ALA   B 2 47  ? -22.622 10.244  -4.419  1.00 52.50  ? 56  ALA   B C   1 
ATOM   641  O  O   . ALA   B 2 47  ? -22.673 9.572   -5.441  1.00 52.66  ? 56  ALA   B O   1 
ATOM   642  C  CB  . ALA   B 2 47  ? -20.532 11.568  -4.098  1.00 51.83  ? 56  ALA   B CB  1 
ATOM   643  N  N   . ALA   B 2 48  ? -23.661 10.960  -3.944  1.00 52.42  ? 57  ALA   B N   1 
ATOM   644  C  CA  . ALA   B 2 48  ? -24.987 11.073  -4.562  1.00 52.95  ? 57  ALA   B CA  1 
ATOM   645  C  C   . ALA   B 2 48  ? -24.894 11.579  -5.997  1.00 53.69  ? 57  ALA   B C   1 
ATOM   646  O  O   . ALA   B 2 48  ? -23.949 12.277  -6.352  1.00 53.94  ? 57  ALA   B O   1 
ATOM   647  C  CB  . ALA   B 2 48  ? -25.855 12.027  -3.752  1.00 53.03  ? 57  ALA   B CB  1 
ATOM   648  N  N   . LEU   B 2 49  ? -25.880 11.242  -6.821  1.00 54.10  ? 58  LEU   B N   1 
ATOM   649  C  CA  . LEU   B 2 49  ? -25.892 11.643  -8.223  1.00 54.94  ? 58  LEU   B CA  1 
ATOM   650  C  C   . LEU   B 2 49  ? -27.178 12.402  -8.549  1.00 56.75  ? 58  LEU   B C   1 
ATOM   651  O  O   . LEU   B 2 49  ? -28.190 12.227  -7.879  1.00 56.90  ? 58  LEU   B O   1 
ATOM   652  C  CB  . LEU   B 2 49  ? -25.772 10.403  -9.140  1.00 54.45  ? 58  LEU   B CB  1 
ATOM   653  C  CG  . LEU   B 2 49  ? -24.490 9.555   -9.044  1.00 55.25  ? 58  LEU   B CG  1 
ATOM   654  C  CD1 . LEU   B 2 49  ? -24.520 8.399   -10.039 1.00 54.98  ? 58  LEU   B CD1 1 
ATOM   655  C  CD2 . LEU   B 2 49  ? -23.248 10.386  -9.322  1.00 55.80  ? 58  LEU   B CD2 1 
ATOM   656  N  N   . ARG   B 2 50  ? -27.139 13.237  -9.585  1.00 57.79  ? 59  ARG   B N   1 
ATOM   657  C  CA  . ARG   B 2 50  ? -28.298 13.994  -10.044 1.00 59.43  ? 59  ARG   B CA  1 
ATOM   658  C  C   . ARG   B 2 50  ? -28.704 13.478  -11.435 1.00 60.92  ? 59  ARG   B C   1 
ATOM   659  O  O   . ARG   B 2 50  ? -27.855 13.050  -12.210 1.00 60.23  ? 59  ARG   B O   1 
ATOM   660  C  CB  . ARG   B 2 50  ? -27.971 15.497  -10.052 1.00 61.26  ? 59  ARG   B CB  1 
ATOM   661  C  CG  . ARG   B 2 50  ? -28.898 16.368  -10.882 1.00 66.51  ? 59  ARG   B CG  1 
ATOM   662  C  CD  . ARG   B 2 50  ? -28.770 17.860  -10.567 1.00 71.83  ? 59  ARG   B CD  1 
ATOM   663  N  NE  . ARG   B 2 50  ? -27.402 18.382  -10.688 1.00 75.84  ? 59  ARG   B NE  1 
ATOM   664  C  CZ  . ARG   B 2 50  ? -26.846 18.786  -11.828 1.00 78.71  ? 59  ARG   B CZ  1 
ATOM   665  N  NH1 . ARG   B 2 50  ? -27.516 18.696  -12.971 1.00 78.60  ? 59  ARG   B NH1 1 
ATOM   666  N  NH2 . ARG   B 2 50  ? -25.603 19.256  -11.836 1.00 79.00  ? 59  ARG   B NH2 1 
ATOM   667  N  N   . SER   B 2 51  ? -30.002 13.470  -11.732 1.00 62.71  ? 60  SER   B N   1 
ATOM   668  C  CA  . SER   B 2 51  ? -30.507 13.007  -13.021 1.00 65.11  ? 60  SER   B CA  1 
ATOM   669  C  C   . SER   B 2 51  ? -31.742 13.832  -13.288 1.00 68.21  ? 60  SER   B C   1 
ATOM   670  O  O   . SER   B 2 51  ? -32.825 13.473  -12.828 1.00 68.92  ? 60  SER   B O   1 
ATOM   671  C  CB  . SER   B 2 51  ? -30.878 11.531  -12.941 1.00 66.31  ? 60  SER   B CB  1 
ATOM   672  O  OG  . SER   B 2 51  ? -31.546 11.104  -14.114 1.00 68.66  ? 60  SER   B OG  1 
ATOM   673  N  N   . GLY   B 2 52  ? -31.568 14.975  -13.948 1.00 69.69  ? 61  GLY   B N   1 
ATOM   674  C  CA  . GLY   B 2 52  ? -32.661 15.913  -14.190 1.00 71.26  ? 61  GLY   B CA  1 
ATOM   675  C  C   . GLY   B 2 52  ? -33.075 16.513  -12.866 1.00 72.45  ? 61  GLY   B C   1 
ATOM   676  O  O   . GLY   B 2 52  ? -32.208 16.903  -12.081 1.00 73.09  ? 61  GLY   B O   1 
ATOM   677  N  N   . GLU   B 2 53  ? -34.381 16.504  -12.561 1.00 72.58  ? 62  GLU   B N   1 
ATOM   678  C  CA  . GLU   B 2 53  ? -34.844 16.958  -11.243 1.00 73.13  ? 62  GLU   B CA  1 
ATOM   679  C  C   . GLU   B 2 53  ? -34.664 15.863  -10.148 1.00 72.22  ? 62  GLU   B C   1 
ATOM   680  O  O   . GLU   B 2 53  ? -34.755 16.159  -8.949  1.00 72.85  ? 62  GLU   B O   1 
ATOM   681  C  CB  . GLU   B 2 53  ? -36.311 17.434  -11.307 1.00 76.98  ? 62  GLU   B CB  1 
ATOM   682  C  CG  . GLU   B 2 53  ? -36.763 18.195  -10.066 1.00 84.35  ? 62  GLU   B CG  1 
ATOM   683  C  CD  . GLU   B 2 53  ? -38.182 18.738  -10.089 1.00 94.45  ? 62  GLU   B CD  1 
ATOM   684  O  OE1 . GLU   B 2 53  ? -38.831 18.664  -11.159 1.00 96.81  ? 62  GLU   B OE1 1 
ATOM   685  O  OE2 . GLU   B 2 53  ? -38.644 19.243  -9.036  1.00 97.20  ? 62  GLU   B OE2 1 
ATOM   686  N  N   . GLY   B 2 54  ? -34.396 14.622  -10.566 1.00 70.53  ? 63  GLY   B N   1 
ATOM   687  C  CA  . GLY   B 2 54  ? -34.244 13.487  -9.669  1.00 69.18  ? 63  GLY   B CA  1 
ATOM   688  C  C   . GLY   B 2 54  ? -32.874 13.323  -9.044  1.00 67.02  ? 63  GLY   B C   1 
ATOM   689  O  O   . GLY   B 2 54  ? -31.875 13.837  -9.543  1.00 67.31  ? 63  GLY   B O   1 
ATOM   690  N  N   . ARG   B 2 55  ? -32.833 12.599  -7.936  1.00 64.58  ? 64  ARG   B N   1 
ATOM   691  C  CA  . ARG   B 2 55  ? -31.606 12.339  -7.214  1.00 62.83  ? 64  ARG   B CA  1 
ATOM   692  C  C   . ARG   B 2 55  ? -31.421 10.825  -7.046  1.00 60.78  ? 64  ARG   B C   1 
ATOM   693  O  O   . ARG   B 2 55  ? -32.346 10.142  -6.598  1.00 61.15  ? 64  ARG   B O   1 
ATOM   694  C  CB  . ARG   B 2 55  ? -31.676 13.005  -5.827  1.00 63.33  ? 64  ARG   B CB  1 
ATOM   695  C  CG  . ARG   B 2 55  ? -30.448 12.763  -4.966  1.00 65.78  ? 64  ARG   B CG  1 
ATOM   696  C  CD  . ARG   B 2 55  ? -30.556 13.403  -3.590  1.00 69.66  ? 64  ARG   B CD  1 
ATOM   697  N  NE  . ARG   B 2 55  ? -29.379 13.077  -2.785  1.00 72.91  ? 64  ARG   B NE  1 
ATOM   698  C  CZ  . ARG   B 2 55  ? -29.059 13.663  -1.639  1.00 75.51  ? 64  ARG   B CZ  1 
ATOM   699  N  NH1 . ARG   B 2 55  ? -29.832 14.619  -1.135  1.00 76.55  ? 64  ARG   B NH1 1 
ATOM   700  N  NH2 . ARG   B 2 55  ? -27.966 13.297  -0.983  1.00 74.85  ? 64  ARG   B NH2 1 
ATOM   701  N  N   . LEU   B 2 56  ? -30.228 10.311  -7.358  1.00 58.25  ? 65  LEU   B N   1 
ATOM   702  C  CA  . LEU   B 2 56  ? -29.923 8.906   -7.146  1.00 56.65  ? 65  LEU   B CA  1 
ATOM   703  C  C   . LEU   B 2 56  ? -29.014 8.778   -5.903  1.00 54.94  ? 65  LEU   B C   1 
ATOM   704  O  O   . LEU   B 2 56  ? -27.943 9.394   -5.857  1.00 54.98  ? 65  LEU   B O   1 
ATOM   705  C  CB  . LEU   B 2 56  ? -29.210 8.287   -8.359  1.00 56.69  ? 65  LEU   B CB  1 
ATOM   706  C  CG  . LEU   B 2 56  ? -29.708 8.600   -9.771  1.00 59.13  ? 65  LEU   B CG  1 
ATOM   707  C  CD1 . LEU   B 2 56  ? -28.957 7.763   -10.785 1.00 60.07  ? 65  LEU   B CD1 1 
ATOM   708  C  CD2 . LEU   B 2 56  ? -31.163 8.269   -9.930  1.00 60.43  ? 65  LEU   B CD2 1 
ATOM   709  N  N   . ASP   B 2 57  ? -29.429 8.000   -4.900  1.00 53.47  ? 66  ASP   B N   1 
ATOM   710  C  CA  . ASP   B 2 57  ? -28.587 7.783   -3.708  1.00 53.12  ? 66  ASP   B CA  1 
ATOM   711  C  C   . ASP   B 2 57  ? -27.876 6.397   -3.785  1.00 51.30  ? 66  ASP   B C   1 
ATOM   712  O  O   . ASP   B 2 57  ? -28.415 5.476   -4.398  1.00 51.06  ? 66  ASP   B O   1 
ATOM   713  C  CB  . ASP   B 2 57  ? -29.414 7.910   -2.424  1.00 56.37  ? 66  ASP   B CB  1 
ATOM   714  C  CG  . ASP   B 2 57  ? -29.984 9.301   -2.203  1.00 63.10  ? 66  ASP   B CG  1 
ATOM   715  O  OD1 . ASP   B 2 57  ? -29.301 10.289  -2.558  1.00 63.05  ? 66  ASP   B OD1 1 
ATOM   716  O  OD2 . ASP   B 2 57  ? -31.106 9.401   -1.667  1.00 67.32  ? 66  ASP   B OD2 1 
ATOM   717  N  N   . PRO   B 2 58  ? -26.645 6.245   -3.249  1.00 49.91  ? 67  PRO   B N   1 
ATOM   718  C  CA  . PRO   B 2 58  ? -25.974 4.929   -3.316  1.00 48.67  ? 67  PRO   B CA  1 
ATOM   719  C  C   . PRO   B 2 58  ? -26.664 3.895   -2.406  1.00 46.90  ? 67  PRO   B C   1 
ATOM   720  O  O   . PRO   B 2 58  ? -27.235 4.256   -1.390  1.00 46.39  ? 67  PRO   B O   1 
ATOM   721  C  CB  . PRO   B 2 58  ? -24.554 5.248   -2.842  1.00 49.77  ? 67  PRO   B CB  1 
ATOM   722  C  CG  . PRO   B 2 58  ? -24.748 6.406   -1.866  1.00 50.20  ? 67  PRO   B CG  1 
ATOM   723  C  CD  . PRO   B 2 58  ? -25.844 7.229   -2.486  1.00 49.14  ? 67  PRO   B CD  1 
ATOM   724  N  N   . TYR   B 2 59  ? -26.627 2.611   -2.773  1.00 45.48  ? 68  TYR   B N   1 
ATOM   725  C  CA  . TYR   B 2 59  ? -27.308 1.559   -2.021  1.00 43.95  ? 68  TYR   B CA  1 
ATOM   726  C  C   . TYR   B 2 59  ? -26.332 0.476   -1.547  1.00 43.78  ? 68  TYR   B C   1 
ATOM   727  O  O   . TYR   B 2 59  ? -26.464 -0.084  -0.458  1.00 43.53  ? 68  TYR   B O   1 
ATOM   728  C  CB  . TYR   B 2 59  ? -28.397 0.968   -2.921  1.00 42.79  ? 68  TYR   B CB  1 
ATOM   729  C  CG  . TYR   B 2 59  ? -29.210 -0.156  -2.318  1.00 42.49  ? 68  TYR   B CG  1 
ATOM   730  C  CD1 . TYR   B 2 59  ? -28.705 -1.452  -2.258  1.00 42.89  ? 68  TYR   B CD1 1 
ATOM   731  C  CD2 . TYR   B 2 59  ? -30.537 0.034   -1.969  1.00 42.38  ? 68  TYR   B CD2 1 
ATOM   732  C  CE1 . TYR   B 2 59  ? -29.445 -2.487  -1.713  1.00 43.11  ? 68  TYR   B CE1 1 
ATOM   733  C  CE2 . TYR   B 2 59  ? -31.306 -1.006  -1.481  1.00 43.13  ? 68  TYR   B CE2 1 
ATOM   734  C  CZ  . TYR   B 2 59  ? -30.760 -2.271  -1.370  1.00 44.17  ? 68  TYR   B CZ  1 
ATOM   735  O  OH  . TYR   B 2 59  ? -31.526 -3.305  -0.895  1.00 46.26  ? 68  TYR   B OH  1 
ATOM   736  N  N   . TRP   B 2 60  ? -25.374 0.152   -2.403  1.00 43.36  ? 69  TRP   B N   1 
ATOM   737  C  CA  . TRP   B 2 60  ? -24.364 -0.834  -2.107  1.00 42.53  ? 69  TRP   B CA  1 
ATOM   738  C  C   . TRP   B 2 60  ? -23.072 -0.386  -2.773  1.00 42.34  ? 69  TRP   B C   1 
ATOM   739  O  O   . TRP   B 2 60  ? -23.089 0.196   -3.856  1.00 42.49  ? 69  TRP   B O   1 
ATOM   740  C  CB  . TRP   B 2 60  ? -24.792 -2.232  -2.610  1.00 41.55  ? 69  TRP   B CB  1 
ATOM   741  C  CG  . TRP   B 2 60  ? -23.681 -3.232  -2.535  1.00 41.49  ? 69  TRP   B CG  1 
ATOM   742  C  CD1 . TRP   B 2 60  ? -23.299 -3.954  -1.445  1.00 42.32  ? 69  TRP   B CD1 1 
ATOM   743  C  CD2 . TRP   B 2 60  ? -22.711 -3.503  -3.557  1.00 41.28  ? 69  TRP   B CD2 1 
ATOM   744  N  NE1 . TRP   B 2 60  ? -22.181 -4.702  -1.745  1.00 42.36  ? 69  TRP   B NE1 1 
ATOM   745  C  CE2 . TRP   B 2 60  ? -21.789 -4.426  -3.026  1.00 41.91  ? 69  TRP   B CE2 1 
ATOM   746  C  CE3 . TRP   B 2 60  ? -22.543 -3.064  -4.877  1.00 41.06  ? 69  TRP   B CE3 1 
ATOM   747  C  CZ2 . TRP   B 2 60  ? -20.721 -4.916  -3.769  1.00 42.42  ? 69  TRP   B CZ2 1 
ATOM   748  C  CZ3 . TRP   B 2 60  ? -21.494 -3.555  -5.608  1.00 42.00  ? 69  TRP   B CZ3 1 
ATOM   749  C  CH2 . TRP   B 2 60  ? -20.607 -4.484  -5.062  1.00 42.47  ? 69  TRP   B CH2 1 
ATOM   750  N  N   . GLY   B 2 61  ? -21.963 -0.702  -2.139  1.00 42.06  ? 70  GLY   B N   1 
ATOM   751  C  CA  . GLY   B 2 61  ? -20.658 -0.385  -2.679  1.00 43.02  ? 70  GLY   B CA  1 
ATOM   752  C  C   . GLY   B 2 61  ? -19.558 -1.148  -1.986  1.00 43.84  ? 70  GLY   B C   1 
ATOM   753  O  O   . GLY   B 2 61  ? -19.717 -1.553  -0.840  1.00 43.77  ? 70  GLY   B O   1 
ATOM   754  N  N   . ASP   B 2 62  ? -18.413 -1.297  -2.665  1.00 44.71  ? 71  ASP   B N   1 
ATOM   755  C  CA  . ASP   B 2 62  ? -17.237 -1.963  -2.113  1.00 44.98  ? 71  ASP   B CA  1 
ATOM   756  C  C   . ASP   B 2 62  ? -15.959 -1.436  -2.840  1.00 44.27  ? 71  ASP   B C   1 
ATOM   757  O  O   . ASP   B 2 62  ? -15.809 -1.675  -4.023  1.00 44.81  ? 71  ASP   B O   1 
ATOM   758  C  CB  . ASP   B 2 62  ? -17.383 -3.490  -2.290  1.00 47.70  ? 71  ASP   B CB  1 
ATOM   759  C  CG  . ASP   B 2 62  ? -16.347 -4.322  -1.565  1.00 54.29  ? 71  ASP   B CG  1 
ATOM   760  O  OD1 . ASP   B 2 62  ? -15.187 -4.335  -2.000  1.00 56.02  ? 71  ASP   B OD1 1 
ATOM   761  O  OD2 . ASP   B 2 62  ? -16.704 -4.973  -0.571  1.00 58.32  ? 71  ASP   B OD2 1 
ATOM   762  N  N   . VAL   B 2 63  ? -15.050 -0.744  -2.123  1.00 43.53  ? 72  VAL   B N   1 
ATOM   763  C  CA  . VAL   B 2 63  ? -13.767 -0.222  -2.620  1.00 43.10  ? 72  VAL   B CA  1 
ATOM   764  C  C   . VAL   B 2 63  ? -12.875 -1.336  -3.199  1.00 44.01  ? 72  VAL   B C   1 
ATOM   765  O  O   . VAL   B 2 63  ? -12.260 -1.107  -4.243  1.00 45.32  ? 72  VAL   B O   1 
ATOM   766  C  CB  . VAL   B 2 63  ? -13.032 0.578   -1.494  1.00 42.71  ? 72  VAL   B CB  1 
ATOM   767  C  CG1 . VAL   B 2 63  ? -11.535 0.713   -1.754  1.00 42.88  ? 72  VAL   B CG1 1 
ATOM   768  C  CG2 . VAL   B 2 63  ? -13.649 1.949   -1.316  1.00 42.99  ? 72  VAL   B CG2 1 
ATOM   769  N  N   . LYS   B 2 64  ? -12.803 -2.535  -2.559  1.00 43.77  ? 73  LYS   B N   1 
ATOM   770  C  CA  . LYS   B 2 64  ? -11.942 -3.597  -3.097  1.00 44.16  ? 73  LYS   B CA  1 
ATOM   771  C  C   . LYS   B 2 64  ? -12.452 -4.128  -4.440  1.00 44.29  ? 73  LYS   B C   1 
ATOM   772  O  O   . LYS   B 2 64  ? -11.646 -4.319  -5.367  1.00 43.63  ? 73  LYS   B O   1 
ATOM   773  C  CB  . LYS   B 2 64  ? -11.665 -4.721  -2.102  1.00 45.90  ? 73  LYS   B CB  1 
ATOM   774  C  CG  . LYS   B 2 64  ? -10.523 -5.635  -2.560  1.00 49.08  ? 73  LYS   B CG  1 
ATOM   775  C  CD  . LYS   B 2 64  ? -10.116 -6.544  -1.459  1.00 53.01  ? 73  LYS   B CD  1 
ATOM   776  C  CE  . LYS   B 2 64  ? -9.291  -7.706  -1.905  1.00 57.41  ? 73  LYS   B CE  1 
ATOM   777  N  NZ  . LYS   B 2 64  ? -9.211  -8.707  -0.800  1.00 60.16  ? 73  LYS   B NZ  1 
ATOM   778  N  N   . GLN   B 2 65  ? -13.782 -4.302  -4.585  1.00 44.36  ? 74  GLN   B N   1 
ATOM   779  C  CA  . GLN   B 2 65  ? -14.322 -4.698  -5.901  1.00 44.27  ? 74  GLN   B CA  1 
ATOM   780  C  C   . GLN   B 2 65  ? -14.309 -3.512  -6.897  1.00 43.44  ? 74  GLN   B C   1 
ATOM   781  O  O   . GLN   B 2 65  ? -14.345 -3.720  -8.114  1.00 43.02  ? 74  GLN   B O   1 
ATOM   782  C  CB  . GLN   B 2 65  ? -15.749 -5.265  -5.777  1.00 46.60  ? 74  GLN   B CB  1 
ATOM   783  C  CG  . GLN   B 2 65  ? -15.874 -6.515  -4.899  1.00 50.49  ? 74  GLN   B CG  1 
ATOM   784  C  CD  . GLN   B 2 65  ? -17.307 -7.053  -4.880  1.00 55.56  ? 74  GLN   B CD  1 
ATOM   785  O  OE1 . GLN   B 2 65  ? -17.928 -7.294  -5.932  1.00 57.53  ? 74  GLN   B OE1 1 
ATOM   786  N  NE2 . GLN   B 2 65  ? -17.870 -7.244  -3.689  1.00 55.08  ? 74  GLN   B NE2 1 
ATOM   787  N  N   . ASP   B 2 66  ? -14.281 -2.272  -6.371  1.00 43.09  ? 75  ASP   B N   1 
ATOM   788  C  CA  . ASP   B 2 66  ? -14.322 -1.016  -7.110  1.00 43.19  ? 75  ASP   B CA  1 
ATOM   789  C  C   . ASP   B 2 66  ? -15.674 -0.903  -7.804  1.00 43.34  ? 75  ASP   B C   1 
ATOM   790  O  O   . ASP   B 2 66  ? -15.743 -0.483  -8.962  1.00 44.07  ? 75  ASP   B O   1 
ATOM   791  C  CB  . ASP   B 2 66  ? -13.166 -0.888  -8.129  1.00 44.54  ? 75  ASP   B CB  1 
ATOM   792  C  CG  . ASP   B 2 66  ? -12.969 0.517   -8.652  1.00 46.68  ? 75  ASP   B CG  1 
ATOM   793  O  OD1 . ASP   B 2 66  ? -13.394 1.462   -7.986  1.00 47.16  ? 75  ASP   B OD1 1 
ATOM   794  O  OD2 . ASP   B 2 66  ? -12.406 0.664   -9.716  1.00 49.69  ? 75  ASP   B OD2 1 
ATOM   795  N  N   . LEU   B 2 67  ? -16.763 -1.225  -7.088  1.00 42.30  ? 76  LEU   B N   1 
ATOM   796  C  CA  . LEU   B 2 67  ? -18.109 -1.130  -7.664  1.00 41.43  ? 76  LEU   B CA  1 
ATOM   797  C  C   . LEU   B 2 67  ? -19.072 -0.388  -6.756  1.00 40.97  ? 76  LEU   B C   1 
ATOM   798  O  O   . LEU   B 2 67  ? -18.879 -0.361  -5.546  1.00 41.25  ? 76  LEU   B O   1 
ATOM   799  C  CB  . LEU   B 2 67  ? -18.662 -2.527  -7.956  1.00 40.85  ? 76  LEU   B CB  1 
ATOM   800  C  CG  . LEU   B 2 67  ? -17.947 -3.313  -9.019  1.00 40.74  ? 76  LEU   B CG  1 
ATOM   801  C  CD1 . LEU   B 2 67  ? -18.508 -4.699  -9.097  1.00 41.42  ? 76  LEU   B CD1 1 
ATOM   802  C  CD2 . LEU   B 2 67  ? -18.042 -2.619  -10.389 1.00 40.26  ? 76  LEU   B CD2 1 
ATOM   803  N  N   . VAL   B 2 68  ? -20.118 0.202   -7.335  1.00 40.24  ? 77  VAL   B N   1 
ATOM   804  C  CA  . VAL   B 2 68  ? -21.161 0.888   -6.568  1.00 39.56  ? 77  VAL   B CA  1 
ATOM   805  C  C   . VAL   B 2 68  ? -22.521 0.813   -7.331  1.00 39.30  ? 77  VAL   B C   1 
ATOM   806  O  O   . VAL   B 2 68  ? -22.560 0.894   -8.543  1.00 38.71  ? 77  VAL   B O   1 
ATOM   807  C  CB  . VAL   B 2 68  ? -20.746 2.343   -6.181  1.00 39.30  ? 77  VAL   B CB  1 
ATOM   808  C  CG1 . VAL   B 2 68  ? -20.447 3.185   -7.432  1.00 39.17  ? 77  VAL   B CG1 1 
ATOM   809  C  CG2 . VAL   B 2 68  ? -21.787 3.023   -5.278  1.00 38.91  ? 77  VAL   B CG2 1 
ATOM   810  N  N   . SER   B 2 69  ? -23.608 0.575   -6.612  1.00 40.05  ? 78  SER   B N   1 
ATOM   811  C  CA  . SER   B 2 69  ? -24.945 0.527   -7.184  1.00 40.51  ? 78  SER   B CA  1 
ATOM   812  C  C   . SER   B 2 69  ? -25.803 1.635   -6.542  1.00 40.83  ? 78  SER   B C   1 
ATOM   813  O  O   . SER   B 2 69  ? -25.634 1.955   -5.374  1.00 40.97  ? 78  SER   B O   1 
ATOM   814  C  CB  . SER   B 2 69  ? -25.560 -0.864  -7.042  1.00 40.78  ? 78  SER   B CB  1 
ATOM   815  O  OG  . SER   B 2 69  ? -26.171 -1.083  -5.783  1.00 41.74  ? 78  SER   B OG  1 
ATOM   816  N  N   . TYR   B 2 70  ? -26.697 2.241   -7.319  1.00 41.16  ? 79  TYR   B N   1 
ATOM   817  C  CA  . TYR   B 2 70  ? -27.517 3.381   -6.904  1.00 41.50  ? 79  TYR   B CA  1 
ATOM   818  C  C   . TYR   B 2 70  ? -28.998 3.029   -7.065  1.00 42.94  ? 79  TYR   B C   1 
ATOM   819  O  O   . TYR   B 2 70  ? -29.364 2.403   -8.067  1.00 42.41  ? 79  TYR   B O   1 
ATOM   820  C  CB  . TYR   B 2 70  ? -27.190 4.586   -7.799  1.00 40.79  ? 79  TYR   B CB  1 
ATOM   821  C  CG  . TYR   B 2 70  ? -25.914 5.305   -7.426  1.00 41.38  ? 79  TYR   B CG  1 
ATOM   822  C  CD1 . TYR   B 2 70  ? -24.670 4.817   -7.823  1.00 42.21  ? 79  TYR   B CD1 1 
ATOM   823  C  CD2 . TYR   B 2 70  ? -25.948 6.479   -6.688  1.00 42.44  ? 79  TYR   B CD2 1 
ATOM   824  C  CE1 . TYR   B 2 70  ? -23.491 5.474   -7.475  1.00 42.84  ? 79  TYR   B CE1 1 
ATOM   825  C  CE2 . TYR   B 2 70  ? -24.778 7.112   -6.287  1.00 43.11  ? 79  TYR   B CE2 1 
ATOM   826  C  CZ  . TYR   B 2 70  ? -23.554 6.627   -6.711  1.00 44.21  ? 79  TYR   B CZ  1 
ATOM   827  O  OH  . TYR   B 2 70  ? -22.412 7.288   -6.333  1.00 46.00  ? 79  TYR   B OH  1 
ATOM   828  N  N   . CYS   B 2 71  ? -29.831 3.366   -6.042  1.00 43.52  ? 80  CYS   B N   1 
ATOM   829  C  CA  . CYS   B 2 71  ? -31.286 3.138   -6.032  1.00 44.47  ? 80  CYS   B CA  1 
ATOM   830  C  C   . CYS   B 2 71  ? -31.690 1.704   -5.750  1.00 43.26  ? 80  CYS   B C   1 
ATOM   831  O  O   . CYS   B 2 71  ? -32.888 1.456   -5.594  1.00 44.14  ? 80  CYS   B O   1 
ATOM   832  C  CB  . CYS   B 2 71  ? -31.954 3.639   -7.312  1.00 47.46  ? 80  CYS   B CB  1 
ATOM   833  S  SG  . CYS   B 2 71  ? -31.464 5.309   -7.808  1.00 56.53  ? 80  CYS   B SG  1 
ATOM   834  N  N   . GLY   B 2 72  ? -30.742 0.779   -5.692  1.00 40.74  ? 81  GLY   B N   1 
ATOM   835  C  CA  . GLY   B 2 72  ? -31.075 -0.610  -5.431  1.00 39.97  ? 81  GLY   B CA  1 
ATOM   836  C  C   . GLY   B 2 72  ? -29.876 -1.513  -5.486  1.00 39.99  ? 81  GLY   B C   1 
ATOM   837  O  O   . GLY   B 2 72  ? -28.770 -1.057  -5.737  1.00 39.88  ? 81  GLY   B O   1 
ATOM   838  N  N   . PRO   B 2 73  ? -30.063 -2.808  -5.219  1.00 40.96  ? 82  PRO   B N   1 
ATOM   839  C  CA  . PRO   B 2 73  ? -28.924 -3.747  -5.281  1.00 42.10  ? 82  PRO   B CA  1 
ATOM   840  C  C   . PRO   B 2 73  ? -28.357 -4.010  -6.689  1.00 44.25  ? 82  PRO   B C   1 
ATOM   841  O  O   . PRO   B 2 73  ? -29.031 -3.797  -7.700  1.00 44.59  ? 82  PRO   B O   1 
ATOM   842  C  CB  . PRO   B 2 73  ? -29.502 -5.031  -4.673  1.00 42.57  ? 82  PRO   B CB  1 
ATOM   843  C  CG  . PRO   B 2 73  ? -30.985 -4.961  -4.949  1.00 42.43  ? 82  PRO   B CG  1 
ATOM   844  C  CD  . PRO   B 2 73  ? -31.318 -3.482  -4.822  1.00 40.62  ? 82  PRO   B CD  1 
ATOM   845  N  N   . TRP   B 2 74  ? -27.120 -4.527  -6.761  1.00 45.20  ? 83  TRP   B N   1 
ATOM   846  C  CA  . TRP   B 2 74  ? -26.442 -4.840  -8.018  1.00 45.90  ? 83  TRP   B CA  1 
ATOM   847  C  C   . TRP   B 2 74  ? -27.285 -5.838  -8.817  1.00 48.76  ? 83  TRP   B C   1 
ATOM   848  O  O   . TRP   B 2 74  ? -27.705 -6.863  -8.266  1.00 49.53  ? 83  TRP   B O   1 
ATOM   849  C  CB  . TRP   B 2 74  ? -25.027 -5.387  -7.747  1.00 44.65  ? 83  TRP   B CB  1 
ATOM   850  C  CG  . TRP   B 2 74  ? -24.187 -5.544  -8.980  1.00 43.63  ? 83  TRP   B CG  1 
ATOM   851  C  CD1 . TRP   B 2 74  ? -24.097 -6.646  -9.780  1.00 43.71  ? 83  TRP   B CD1 1 
ATOM   852  C  CD2 . TRP   B 2 74  ? -23.314 -4.560  -9.549  1.00 43.25  ? 83  TRP   B CD2 1 
ATOM   853  N  NE1 . TRP   B 2 74  ? -23.227 -6.410  -10.813 1.00 44.08  ? 83  TRP   B NE1 1 
ATOM   854  C  CE2 . TRP   B 2 74  ? -22.743 -5.128  -10.708 1.00 43.75  ? 83  TRP   B CE2 1 
ATOM   855  C  CE3 . TRP   B 2 74  ? -23.005 -3.228  -9.224  1.00 43.23  ? 83  TRP   B CE3 1 
ATOM   856  C  CZ2 . TRP   B 2 74  ? -21.867 -4.419  -11.534 1.00 44.03  ? 83  TRP   B CZ2 1 
ATOM   857  C  CZ3 . TRP   B 2 74  ? -22.122 -2.538  -10.025 1.00 43.73  ? 83  TRP   B CZ3 1 
ATOM   858  C  CH2 . TRP   B 2 74  ? -21.607 -3.111  -11.202 1.00 43.89  ? 83  TRP   B CH2 1 
ATOM   859  N  N   . LYS   B 2 75  ? -27.589 -5.496  -10.093 1.00 49.45  ? 84  LYS   B N   1 
ATOM   860  C  CA  . LYS   B 2 75  ? -28.473 -6.267  -10.957 1.00 50.58  ? 84  LYS   B CA  1 
ATOM   861  C  C   . LYS   B 2 75  ? -27.748 -7.067  -12.017 1.00 52.61  ? 84  LYS   B C   1 
ATOM   862  O  O   . LYS   B 2 75  ? -28.306 -8.035  -12.506 1.00 52.81  ? 84  LYS   B O   1 
ATOM   863  C  CB  . LYS   B 2 75  ? -29.477 -5.333  -11.661 1.00 50.74  ? 84  LYS   B CB  1 
ATOM   864  C  CG  . LYS   B 2 75  ? -30.342 -4.521  -10.720 1.00 51.18  ? 84  LYS   B CG  1 
ATOM   865  C  CD  . LYS   B 2 75  ? -31.444 -5.361  -10.100 1.00 53.24  ? 84  LYS   B CD  1 
ATOM   866  C  CE  . LYS   B 2 75  ? -32.186 -4.557  -9.061  1.00 55.96  ? 84  LYS   B CE  1 
ATOM   867  N  NZ  . LYS   B 2 75  ? -33.395 -5.255  -8.600  1.00 58.48  ? 84  LYS   B NZ  1 
ATOM   868  N  N   . LEU   B 2 76  ? -26.543 -6.644  -12.413 1.00 53.84  ? 85  LEU   B N   1 
ATOM   869  C  CA  . LEU   B 2 76  ? -25.770 -7.282  -13.483 1.00 55.01  ? 85  LEU   B CA  1 
ATOM   870  C  C   . LEU   B 2 76  ? -25.107 -8.585  -13.031 1.00 57.56  ? 85  LEU   B C   1 
ATOM   871  O  O   . LEU   B 2 76  ? -24.235 -8.564  -12.165 1.00 58.50  ? 85  LEU   B O   1 
ATOM   872  C  CB  . LEU   B 2 76  ? -24.724 -6.305  -14.039 1.00 54.52  ? 85  LEU   B CB  1 
ATOM   873  C  CG  . LEU   B 2 76  ? -25.196 -4.872  -14.280 1.00 55.15  ? 85  LEU   B CG  1 
ATOM   874  C  CD1 . LEU   B 2 76  ? -24.058 -3.980  -14.676 1.00 55.59  ? 85  LEU   B CD1 1 
ATOM   875  C  CD2 . LEU   B 2 76  ? -26.307 -4.820  -15.283 1.00 55.57  ? 85  LEU   B CD2 1 
ATOM   876  N  N   . ASP   B 2 77  ? -25.503 -9.716  -13.622 1.00 58.68  ? 86  ASP   B N   1 
ATOM   877  C  CA  . ASP   B 2 77  ? -24.961 -11.009 -13.221 1.00 60.21  ? 86  ASP   B CA  1 
ATOM   878  C  C   . ASP   B 2 77  ? -24.344 -11.854 -14.378 1.00 60.31  ? 86  ASP   B C   1 
ATOM   879  O  O   . ASP   B 2 77  ? -23.596 -12.787 -14.089 1.00 60.85  ? 86  ASP   B O   1 
ATOM   880  C  CB  . ASP   B 2 77  ? -26.017 -11.815 -12.442 1.00 63.12  ? 86  ASP   B CB  1 
ATOM   881  C  CG  . ASP   B 2 77  ? -27.306 -12.086 -13.205 1.00 69.96  ? 86  ASP   B CG  1 
ATOM   882  O  OD1 . ASP   B 2 77  ? -27.474 -11.527 -14.321 1.00 70.39  ? 86  ASP   B OD1 1 
ATOM   883  O  OD2 . ASP   B 2 77  ? -28.151 -12.853 -12.688 1.00 73.45  ? 86  ASP   B OD2 1 
ATOM   884  N  N   . ALA   B 2 78  ? -24.575 -11.511 -15.651 1.00 59.85  ? 87  ALA   B N   1 
ATOM   885  C  CA  . ALA   B 2 78  ? -23.987 -12.276 -16.769 1.00 60.08  ? 87  ALA   B CA  1 
ATOM   886  C  C   . ALA   B 2 78  ? -22.440 -12.420 -16.650 1.00 60.55  ? 87  ALA   B C   1 
ATOM   887  O  O   . ALA   B 2 78  ? -21.785 -11.546 -16.083 1.00 60.85  ? 87  ALA   B O   1 
ATOM   888  C  CB  . ALA   B 2 78  ? -24.373 -11.654 -18.104 1.00 59.38  ? 87  ALA   B CB  1 
ATOM   889  N  N   . ALA   B 2 79  ? -21.873 -13.533 -17.131 1.00 60.59  ? 88  ALA   B N   1 
ATOM   890  C  CA  . ALA   B 2 79  ? -20.431 -13.768 -17.008 1.00 61.26  ? 88  ALA   B CA  1 
ATOM   891  C  C   . ALA   B 2 79  ? -19.761 -14.087 -18.331 1.00 62.23  ? 88  ALA   B C   1 
ATOM   892  O  O   . ALA   B 2 79  ? -20.409 -14.638 -19.213 1.00 61.96  ? 88  ALA   B O   1 
ATOM   893  C  CB  . ALA   B 2 79  ? -20.192 -14.910 -16.043 1.00 61.40  ? 88  ALA   B CB  1 
ATOM   894  N  N   . TRP   B 2 80  ? -18.456 -13.764 -18.461 1.00 63.23  ? 89  TRP   B N   1 
ATOM   895  C  CA  . TRP   B 2 80  ? -17.659 -14.113 -19.644 1.00 64.75  ? 89  TRP   B CA  1 
ATOM   896  C  C   . TRP   B 2 80  ? -17.541 -15.646 -19.691 1.00 65.80  ? 89  TRP   B C   1 
ATOM   897  O  O   . TRP   B 2 80  ? -17.325 -16.266 -18.648 1.00 65.49  ? 89  TRP   B O   1 
ATOM   898  C  CB  . TRP   B 2 80  ? -16.250 -13.474 -19.593 1.00 64.75  ? 89  TRP   B CB  1 
ATOM   899  C  CG  . TRP   B 2 80  ? -15.393 -13.792 -20.795 1.00 65.34  ? 89  TRP   B CG  1 
ATOM   900  C  CD1 . TRP   B 2 80  ? -15.781 -13.793 -22.104 1.00 65.96  ? 89  TRP   B CD1 1 
ATOM   901  C  CD2 . TRP   B 2 80  ? -13.988 -14.062 -20.795 1.00 65.50  ? 89  TRP   B CD2 1 
ATOM   902  N  NE1 . TRP   B 2 80  ? -14.712 -14.078 -22.913 1.00 66.18  ? 89  TRP   B NE1 1 
ATOM   903  C  CE2 . TRP   B 2 80  ? -13.595 -14.247 -22.137 1.00 66.22  ? 89  TRP   B CE2 1 
ATOM   904  C  CE3 . TRP   B 2 80  ? -13.024 -14.187 -19.791 1.00 66.05  ? 89  TRP   B CE3 1 
ATOM   905  C  CZ2 . TRP   B 2 80  ? -12.294 -14.624 -22.491 1.00 66.75  ? 89  TRP   B CZ2 1 
ATOM   906  C  CZ3 . TRP   B 2 80  ? -11.730 -14.535 -20.149 1.00 66.98  ? 89  TRP   B CZ3 1 
ATOM   907  C  CH2 . TRP   B 2 80  ? -11.370 -14.715 -21.487 1.00 66.53  ? 89  TRP   B CH2 1 
ATOM   908  N  N   . ASP   B 2 81  ? -17.734 -16.258 -20.874 1.00 66.97  ? 90  ASP   B N   1 
ATOM   909  C  CA  . ASP   B 2 81  ? -17.685 -17.718 -20.982 1.00 69.08  ? 90  ASP   B CA  1 
ATOM   910  C  C   . ASP   B 2 81  ? -16.256 -18.315 -20.956 1.00 71.28  ? 90  ASP   B C   1 
ATOM   911  O  O   . ASP   B 2 81  ? -16.103 -19.530 -20.789 1.00 71.53  ? 90  ASP   B O   1 
ATOM   912  C  CB  . ASP   B 2 81  ? -18.468 -18.220 -22.210 1.00 70.30  ? 90  ASP   B CB  1 
ATOM   913  C  CG  . ASP   B 2 81  ? -17.991 -17.690 -23.542 1.00 75.38  ? 90  ASP   B CG  1 
ATOM   914  O  OD1 . ASP   B 2 81  ? -16.928 -17.034 -23.575 1.00 76.27  ? 90  ASP   B OD1 1 
ATOM   915  O  OD2 . ASP   B 2 81  ? -18.695 -17.912 -24.561 1.00 77.85  ? 90  ASP   B OD2 1 
ATOM   916  N  N   . GLY   B 2 82  ? -15.248 -17.458 -21.133 1.00 72.59  ? 91  GLY   B N   1 
ATOM   917  C  CA  . GLY   B 2 82  ? -13.846 -17.848 -21.171 1.00 74.28  ? 91  GLY   B CA  1 
ATOM   918  C  C   . GLY   B 2 82  ? -13.322 -18.128 -22.571 1.00 75.66  ? 91  GLY   B C   1 
ATOM   919  O  O   . GLY   B 2 82  ? -12.116 -18.329 -22.749 1.00 75.96  ? 91  GLY   B O   1 
ATOM   920  N  N   . LEU   B 2 83  ? -14.212 -18.157 -23.582 1.00 76.15  ? 92  LEU   B N   1 
ATOM   921  C  CA  . LEU   B 2 83  ? -13.800 -18.466 -24.939 1.00 76.89  ? 92  LEU   B CA  1 
ATOM   922  C  C   . LEU   B 2 83  ? -14.035 -17.369 -25.927 1.00 77.26  ? 92  LEU   B C   1 
ATOM   923  O  O   . LEU   B 2 83  ? -13.172 -17.091 -26.754 1.00 77.62  ? 92  LEU   B O   1 
ATOM   924  C  CB  . LEU   B 2 83  ? -14.528 -19.725 -25.441 1.00 77.74  ? 92  LEU   B CB  1 
ATOM   925  C  CG  . LEU   B 2 83  ? -14.307 -21.035 -24.685 1.00 80.12  ? 92  LEU   B CG  1 
ATOM   926  C  CD1 . LEU   B 2 83  ? -14.944 -22.181 -25.457 1.00 81.31  ? 92  LEU   B CD1 1 
ATOM   927  C  CD2 . LEU   B 2 83  ? -12.834 -21.345 -24.548 1.00 80.37  ? 92  LEU   B CD2 1 
ATOM   928  N  N   . SER   B 2 84  ? -15.238 -16.792 -25.908 1.00 76.91  ? 93  SER   B N   1 
ATOM   929  C  CA  . SER   B 2 84  ? -15.709 -15.855 -26.909 1.00 76.43  ? 93  SER   B CA  1 
ATOM   930  C  C   . SER   B 2 84  ? -15.153 -14.454 -26.843 1.00 74.87  ? 93  SER   B C   1 
ATOM   931  O  O   . SER   B 2 84  ? -14.744 -13.987 -25.781 1.00 74.83  ? 93  SER   B O   1 
ATOM   932  C  CB  . SER   B 2 84  ? -17.234 -15.785 -26.869 1.00 79.01  ? 93  SER   B CB  1 
ATOM   933  O  OG  . SER   B 2 84  ? -17.805 -17.081 -26.840 1.00 82.50  ? 93  SER   B OG  1 
ATOM   934  N  N   . GLU   B 2 85  ? -15.193 -13.771 -28.006 1.00 73.44  ? 94  GLU   B N   1 
ATOM   935  C  CA  . GLU   B 2 85  ? -14.887 -12.355 -28.158 1.00 73.01  ? 94  GLU   B CA  1 
ATOM   936  C  C   . GLU   B 2 85  ? -16.057 -11.547 -27.501 1.00 72.29  ? 94  GLU   B C   1 
ATOM   937  O  O   . GLU   B 2 85  ? -17.188 -12.035 -27.368 1.00 72.80  ? 94  GLU   B O   1 
ATOM   938  C  CB  . GLU   B 2 85  ? -14.771 -11.967 -29.651 1.00 74.22  ? 94  GLU   B CB  1 
ATOM   939  C  CG  . GLU   B 2 85  ? -13.468 -12.405 -30.305 1.00 77.65  ? 94  GLU   B CG  1 
ATOM   940  C  CD  . GLU   B 2 85  ? -13.057 -11.609 -31.531 1.00 81.31  ? 94  GLU   B CD  1 
ATOM   941  O  OE1 . GLU   B 2 85  ? -13.949 -11.034 -32.196 1.00 81.27  ? 94  GLU   B OE1 1 
ATOM   942  O  OE2 . GLU   B 2 85  ? -11.840 -11.546 -31.821 1.00 82.08  ? 94  GLU   B OE2 1 
ATOM   943  N  N   . VAL   B 2 86  ? -15.762 -10.330 -27.054 1.00 70.26  ? 95  VAL   B N   1 
ATOM   944  C  CA  . VAL   B 2 86  ? -16.725 -9.449  -26.396 1.00 68.00  ? 95  VAL   B CA  1 
ATOM   945  C  C   . VAL   B 2 86  ? -16.658 -8.067  -27.058 1.00 66.86  ? 95  VAL   B C   1 
ATOM   946  O  O   . VAL   B 2 86  ? -15.803 -7.833  -27.916 1.00 67.40  ? 95  VAL   B O   1 
ATOM   947  C  CB  . VAL   B 2 86  ? -16.438 -9.348  -24.860 1.00 67.07  ? 95  VAL   B CB  1 
ATOM   948  C  CG1 . VAL   B 2 86  ? -16.299 -10.716 -24.221 1.00 67.39  ? 95  VAL   B CG1 1 
ATOM   949  C  CG2 . VAL   B 2 86  ? -15.209 -8.487  -24.587 1.00 66.80  ? 95  VAL   B CG2 1 
ATOM   950  N  N   . GLN   B 2 87  ? -17.561 -7.139  -26.665 1.00 64.95  ? 96  GLN   B N   1 
ATOM   951  C  CA  . GLN   B 2 87  ? -17.496 -5.784  -27.151 1.00 63.22  ? 96  GLN   B CA  1 
ATOM   952  C  C   . GLN   B 2 87  ? -17.448 -4.833  -25.974 1.00 62.19  ? 96  GLN   B C   1 
ATOM   953  O  O   . GLN   B 2 87  ? -18.223 -4.974  -25.035 1.00 62.76  ? 96  GLN   B O   1 
ATOM   954  C  CB  . GLN   B 2 87  ? -18.671 -5.466  -28.087 1.00 62.92  ? 96  GLN   B CB  1 
ATOM   955  C  CG  . GLN   B 2 87  ? -18.448 -6.009  -29.491 1.00 64.07  ? 96  GLN   B CG  1 
ATOM   956  C  CD  . GLN   B 2 87  ? -19.553 -5.659  -30.454 1.00 67.43  ? 96  GLN   B CD  1 
ATOM   957  O  OE1 . GLN   B 2 87  ? -20.457 -4.861  -30.163 1.00 65.76  ? 96  GLN   B OE1 1 
ATOM   958  N  NE2 . GLN   B 2 87  ? -19.499 -6.247  -31.648 1.00 68.46  ? 96  GLN   B NE2 1 
ATOM   959  N  N   . LEU   B 2 88  ? -16.519 -3.883  -26.008 1.00 60.44  ? 97  LEU   B N   1 
ATOM   960  C  CA  . LEU   B 2 88  ? -16.489 -2.813  -25.034 1.00 58.89  ? 97  LEU   B CA  1 
ATOM   961  C  C   . LEU   B 2 88  ? -17.430 -1.737  -25.643 1.00 59.03  ? 97  LEU   B C   1 
ATOM   962  O  O   . LEU   B 2 88  ? -17.221 -1.300  -26.785 1.00 58.91  ? 97  LEU   B O   1 
ATOM   963  C  CB  . LEU   B 2 88  ? -15.061 -2.241  -24.875 1.00 57.49  ? 97  LEU   B CB  1 
ATOM   964  C  CG  . LEU   B 2 88  ? -14.970 -0.876  -24.174 1.00 57.02  ? 97  LEU   B CG  1 
ATOM   965  C  CD1 . LEU   B 2 88  ? -15.484 -0.952  -22.736 1.00 57.09  ? 97  LEU   B CD1 1 
ATOM   966  C  CD2 . LEU   B 2 88  ? -13.577 -0.315  -24.213 1.00 56.99  ? 97  LEU   B CD2 1 
ATOM   967  N  N   . LEU   B 2 89  ? -18.482 -1.358  -24.921 1.00 58.48  ? 98  LEU   B N   1 
ATOM   968  C  CA  . LEU   B 2 89  ? -19.340 -0.280  -25.380 1.00 58.14  ? 98  LEU   B CA  1 
ATOM   969  C  C   . LEU   B 2 89  ? -18.728 0.950   -24.718 1.00 58.38  ? 98  LEU   B C   1 
ATOM   970  O  O   . LEU   B 2 89  ? -19.092 1.323   -23.591 1.00 57.99  ? 98  LEU   B O   1 
ATOM   971  C  CB  . LEU   B 2 89  ? -20.818 -0.498  -25.009 1.00 57.80  ? 98  LEU   B CB  1 
ATOM   972  C  CG  . LEU   B 2 89  ? -21.823 0.604   -25.419 1.00 58.34  ? 98  LEU   B CG  1 
ATOM   973  C  CD1 . LEU   B 2 89  ? -21.616 1.071   -26.829 1.00 59.44  ? 98  LEU   B CD1 1 
ATOM   974  C  CD2 . LEU   B 2 89  ? -23.223 0.102   -25.316 1.00 58.53  ? 98  LEU   B CD2 1 
ATOM   975  N  N   . ALA   B 2 90  ? -17.687 1.485   -25.378 1.00 58.10  ? 99  ALA   B N   1 
ATOM   976  C  CA  . ALA   B 2 90  ? -16.912 2.611   -24.881 1.00 58.18  ? 99  ALA   B CA  1 
ATOM   977  C  C   . ALA   B 2 90  ? -17.639 3.934   -24.995 1.00 58.50  ? 99  ALA   B C   1 
ATOM   978  O  O   . ALA   B 2 90  ? -18.085 4.304   -26.083 1.00 59.55  ? 99  ALA   B O   1 
ATOM   979  C  CB  . ALA   B 2 90  ? -15.593 2.697   -25.623 1.00 57.79  ? 99  ALA   B CB  1 
ATOM   980  N  N   . VAL   B 2 91  ? -17.714 4.686   -23.890 1.00 57.39  ? 100 VAL   B N   1 
ATOM   981  C  CA  . VAL   B 2 91  ? -18.309 6.021   -23.918 1.00 56.59  ? 100 VAL   B CA  1 
ATOM   982  C  C   . VAL   B 2 91  ? -17.207 7.028   -23.541 1.00 56.70  ? 100 VAL   B C   1 
ATOM   983  O  O   . VAL   B 2 91  ? -17.024 7.343   -22.367 1.00 56.74  ? 100 VAL   B O   1 
ATOM   984  C  CB  . VAL   B 2 91  ? -19.572 6.118   -23.046 1.00 56.27  ? 100 VAL   B CB  1 
ATOM   985  C  CG1 . VAL   B 2 91  ? -20.134 7.530   -23.067 1.00 56.86  ? 100 VAL   B CG1 1 
ATOM   986  C  CG2 . VAL   B 2 91  ? -20.624 5.114   -23.502 1.00 56.13  ? 100 VAL   B CG2 1 
ATOM   987  N  N   . PRO   B 2 92  ? -16.387 7.461   -24.528 1.00 56.74  ? 101 PRO   B N   1 
ATOM   988  C  CA  . PRO   B 2 92  ? -15.259 8.351   -24.211 1.00 57.31  ? 101 PRO   B CA  1 
ATOM   989  C  C   . PRO   B 2 92  ? -15.662 9.798   -23.958 1.00 58.84  ? 101 PRO   B C   1 
ATOM   990  O  O   . PRO   B 2 92  ? -16.700 10.242  -24.457 1.00 59.51  ? 101 PRO   B O   1 
ATOM   991  C  CB  . PRO   B 2 92  ? -14.332 8.220   -25.447 1.00 57.96  ? 101 PRO   B CB  1 
ATOM   992  C  CG  . PRO   B 2 92  ? -15.046 7.334   -26.428 1.00 58.11  ? 101 PRO   B CG  1 
ATOM   993  C  CD  . PRO   B 2 92  ? -16.461 7.176   -25.971 1.00 56.48  ? 101 PRO   B CD  1 
ATOM   994  N  N   . PRO   B 2 93  ? -14.860 10.563  -23.194 1.00 59.50  ? 102 PRO   B N   1 
ATOM   995  C  CA  . PRO   B 2 93  ? -15.241 11.959  -22.910 1.00 60.62  ? 102 PRO   B CA  1 
ATOM   996  C  C   . PRO   B 2 93  ? -15.374 12.854  -24.144 1.00 62.22  ? 102 PRO   B C   1 
ATOM   997  O  O   . PRO   B 2 93  ? -14.438 13.009  -24.926 1.00 62.95  ? 102 PRO   B O   1 
ATOM   998  C  CB  . PRO   B 2 93  ? -14.152 12.442  -21.942 1.00 60.95  ? 102 PRO   B CB  1 
ATOM   999  C  CG  . PRO   B 2 93  ? -13.604 11.172  -21.319 1.00 60.73  ? 102 PRO   B CG  1 
ATOM   1000 C  CD  . PRO   B 2 93  ? -13.646 10.174  -22.449 1.00 58.98  ? 102 PRO   B CD  1 
ATOM   1001 N  N   . GLY   B 2 94  ? -16.571 13.402  -24.326 1.00 62.21  ? 103 GLY   B N   1 
ATOM   1002 C  CA  . GLY   B 2 94  ? -16.896 14.293  -25.435 1.00 62.08  ? 103 GLY   B CA  1 
ATOM   1003 C  C   . GLY   B 2 94  ? -17.085 13.603  -26.771 1.00 62.60  ? 103 GLY   B C   1 
ATOM   1004 O  O   . GLY   B 2 94  ? -17.203 14.275  -27.798 1.00 62.71  ? 103 GLY   B O   1 
ATOM   1005 N  N   . GLU   B 2 95  ? -17.068 12.265  -26.791 1.00 63.14  ? 104 GLU   B N   1 
ATOM   1006 C  CA  . GLU   B 2 95  ? -17.194 11.498  -28.034 1.00 64.15  ? 104 GLU   B CA  1 
ATOM   1007 C  C   . GLU   B 2 95  ? -18.374 10.548  -27.953 1.00 65.13  ? 104 GLU   B C   1 
ATOM   1008 O  O   . GLU   B 2 95  ? -18.811 10.189  -26.859 1.00 65.18  ? 104 GLU   B O   1 
ATOM   1009 C  CB  . GLU   B 2 95  ? -15.896 10.716  -28.318 1.00 65.72  ? 104 GLU   B CB  1 
ATOM   1010 C  CG  . GLU   B 2 95  ? -14.737 11.617  -28.695 1.00 69.17  ? 104 GLU   B CG  1 
ATOM   1011 C  CD  . GLU   B 2 95  ? -13.390 10.929  -28.812 1.00 74.57  ? 104 GLU   B CD  1 
ATOM   1012 O  OE1 . GLU   B 2 95  ? -13.334 9.681   -28.694 1.00 75.10  ? 104 GLU   B OE1 1 
ATOM   1013 O  OE2 . GLU   B 2 95  ? -12.384 11.648  -29.015 1.00 75.97  ? 104 GLU   B OE2 1 
ATOM   1014 N  N   . ARG   B 2 96  ? -18.874 10.120  -29.104 1.00 65.94  ? 105 ARG   B N   1 
ATOM   1015 C  CA  . ARG   B 2 96  ? -20.040 9.249   -29.158 1.00 67.72  ? 105 ARG   B CA  1 
ATOM   1016 C  C   . ARG   B 2 96  ? -19.741 7.828   -28.704 1.00 68.68  ? 105 ARG   B C   1 
ATOM   1017 O  O   . ARG   B 2 96  ? -18.612 7.357   -28.859 1.00 68.53  ? 105 ARG   B O   1 
ATOM   1018 C  CB  . ARG   B 2 96  ? -20.620 9.254   -30.584 1.00 70.12  ? 105 ARG   B CB  1 
ATOM   1019 C  CG  . ARG   B 2 96  ? -22.101 8.875   -30.680 1.00 75.86  ? 105 ARG   B CG  1 
ATOM   1020 C  CD  . ARG   B 2 96  ? -22.730 9.203   -32.028 1.00 82.07  ? 105 ARG   B CD  1 
ATOM   1021 N  NE  . ARG   B 2 96  ? -21.938 8.646   -33.123 1.00 89.29  ? 105 ARG   B NE  1 
ATOM   1022 C  CZ  . ARG   B 2 96  ? -21.293 9.377   -34.025 1.00 94.92  ? 105 ARG   B CZ  1 
ATOM   1023 N  NH1 . ARG   B 2 96  ? -21.390 10.703  -34.010 1.00 95.69  ? 105 ARG   B NH1 1 
ATOM   1024 N  NH2 . ARG   B 2 96  ? -20.565 8.786   -34.967 1.00 95.98  ? 105 ARG   B NH2 1 
ATOM   1025 N  N   . ALA   B 2 97  ? -20.768 7.143   -28.147 1.00 69.10  ? 106 ALA   B N   1 
ATOM   1026 C  CA  . ALA   B 2 97  ? -20.703 5.744   -27.714 1.00 69.83  ? 106 ALA   B CA  1 
ATOM   1027 C  C   . ALA   B 2 97  ? -20.292 4.870   -28.906 1.00 70.27  ? 106 ALA   B C   1 
ATOM   1028 O  O   . ALA   B 2 97  ? -20.827 5.041   -29.987 1.00 70.51  ? 106 ALA   B O   1 
ATOM   1029 C  CB  . ALA   B 2 97  ? -22.061 5.303   -27.189 1.00 69.62  ? 106 ALA   B CB  1 
ATOM   1030 N  N   . LYS   B 2 98  ? -19.331 3.972   -28.720 1.00 70.66  ? 107 LYS   B N   1 
ATOM   1031 C  CA  . LYS   B 2 98  ? -18.803 3.154   -29.807 1.00 71.32  ? 107 LYS   B CA  1 
ATOM   1032 C  C   . LYS   B 2 98  ? -18.422 1.741   -29.360 1.00 70.42  ? 107 LYS   B C   1 
ATOM   1033 O  O   . LYS   B 2 98  ? -17.706 1.588   -28.376 1.00 70.70  ? 107 LYS   B O   1 
ATOM   1034 C  CB  . LYS   B 2 98  ? -17.575 3.874   -30.364 1.00 74.70  ? 107 LYS   B CB  1 
ATOM   1035 C  CG  . LYS   B 2 98  ? -16.777 3.124   -31.407 1.00 80.34  ? 107 LYS   B CG  1 
ATOM   1036 C  CD  . LYS   B 2 98  ? -15.497 3.894   -31.753 1.00 86.54  ? 107 LYS   B CD  1 
ATOM   1037 C  CE  . LYS   B 2 98  ? -14.723 4.305   -30.509 1.00 90.87  ? 107 LYS   B CE  1 
ATOM   1038 N  NZ  . LYS   B 2 98  ? -13.251 4.286   -30.732 1.00 93.56  ? 107 LYS   B NZ  1 
ATOM   1039 N  N   . ASN   B 2 99  ? -18.896 0.713   -30.080 1.00 69.37  ? 108 ASN   B N   1 
ATOM   1040 C  CA  . ASN   B 2 99  ? -18.597 -0.684  -29.741 1.00 69.00  ? 108 ASN   B CA  1 
ATOM   1041 C  C   . ASN   B 2 99  ? -17.258 -1.125  -30.344 1.00 69.99  ? 108 ASN   B C   1 
ATOM   1042 O  O   . ASN   B 2 99  ? -17.057 -1.010  -31.543 1.00 70.75  ? 108 ASN   B O   1 
ATOM   1043 C  CB  . ASN   B 2 99  ? -19.688 -1.627  -30.267 1.00 67.94  ? 108 ASN   B CB  1 
ATOM   1044 C  CG  . ASN   B 2 99  ? -21.087 -1.368  -29.777 1.00 67.24  ? 108 ASN   B CG  1 
ATOM   1045 O  OD1 . ASN   B 2 99  ? -21.655 -0.296  -29.988 1.00 68.22  ? 108 ASN   B OD1 1 
ATOM   1046 N  ND2 . ASN   B 2 99  ? -21.697 -2.368  -29.170 1.00 65.99  ? 108 ASN   B ND2 1 
ATOM   1047 N  N   . ILE   B 2 100 ? -16.361 -1.633  -29.528 1.00 70.34  ? 109 ILE   B N   1 
ATOM   1048 C  CA  . ILE   B 2 100 ? -15.067 -2.132  -29.967 1.00 71.24  ? 109 ILE   B CA  1 
ATOM   1049 C  C   . ILE   B 2 100 ? -14.988 -3.593  -29.610 1.00 71.50  ? 109 ILE   B C   1 
ATOM   1050 O  O   . ILE   B 2 100 ? -14.956 -3.930  -28.435 1.00 71.65  ? 109 ILE   B O   1 
ATOM   1051 C  CB  . ILE   B 2 100 ? -13.921 -1.379  -29.277 1.00 72.30  ? 109 ILE   B CB  1 
ATOM   1052 C  CG1 . ILE   B 2 100 ? -14.054 0.127   -29.457 1.00 74.03  ? 109 ILE   B CG1 1 
ATOM   1053 C  CG2 . ILE   B 2 100 ? -12.560 -1.908  -29.749 1.00 72.87  ? 109 ILE   B CG2 1 
ATOM   1054 C  CD1 . ILE   B 2 100 ? -14.051 0.608   -30.942 1.00 75.53  ? 109 ILE   B CD1 1 
ATOM   1055 N  N   . GLN   B 2 101 ? -14.929 -4.461  -30.605 1.00 71.63  ? 110 GLN   B N   1 
ATOM   1056 C  CA  . GLN   B 2 101 ? -14.854 -5.893  -30.373 1.00 72.35  ? 110 GLN   B CA  1 
ATOM   1057 C  C   . GLN   B 2 101 ? -13.423 -6.324  -30.107 1.00 72.64  ? 110 GLN   B C   1 
ATOM   1058 O  O   . GLN   B 2 101 ? -12.497 -5.875  -30.785 1.00 73.08  ? 110 GLN   B O   1 
ATOM   1059 C  CB  . GLN   B 2 101 ? -15.420 -6.643  -31.577 1.00 74.63  ? 110 GLN   B CB  1 
ATOM   1060 C  CG  . GLN   B 2 101 ? -15.545 -8.147  -31.367 1.00 77.70  ? 110 GLN   B CG  1 
ATOM   1061 C  CD  . GLN   B 2 101 ? -16.598 -8.733  -32.273 1.00 80.42  ? 110 GLN   B CD  1 
ATOM   1062 O  OE1 . GLN   B 2 101 ? -17.560 -8.066  -32.672 1.00 80.86  ? 110 GLN   B OE1 1 
ATOM   1063 N  NE2 . GLN   B 2 101 ? -16.457 -10.006 -32.585 1.00 80.78  ? 110 GLN   B NE2 1 
ATOM   1064 N  N   . THR   B 2 102 ? -13.232 -7.188  -29.109 1.00 71.95  ? 111 THR   B N   1 
ATOM   1065 C  CA  . THR   B 2 102 ? -11.917 -7.691  -28.761 1.00 72.27  ? 111 THR   B CA  1 
ATOM   1066 C  C   . THR   B 2 102 ? -12.016 -9.073  -28.107 1.00 72.10  ? 111 THR   B C   1 
ATOM   1067 O  O   . THR   B 2 102 ? -13.094 -9.463  -27.667 1.00 72.69  ? 111 THR   B O   1 
ATOM   1068 C  CB  . THR   B 2 102 ? -11.207 -6.698  -27.817 1.00 74.07  ? 111 THR   B CB  1 
ATOM   1069 O  OG1 . THR   B 2 102 ? -9.859  -7.146  -27.631 1.00 75.24  ? 111 THR   B OG1 1 
ATOM   1070 C  CG2 . THR   B 2 102 ? -11.937 -6.511  -26.468 1.00 73.92  ? 111 THR   B CG2 1 
ATOM   1071 N  N   . LEU   B 2 103 ? -10.901 -9.822  -28.051 1.00 71.44  ? 112 LEU   B N   1 
ATOM   1072 C  CA  . LEU   B 2 103 ? -10.896 -11.093 -27.348 1.00 70.94  ? 112 LEU   B CA  1 
ATOM   1073 C  C   . LEU   B 2 103 ? -10.170 -10.837 -26.043 1.00 70.56  ? 112 LEU   B C   1 
ATOM   1074 O  O   . LEU   B 2 103 ? -9.000  -10.439 -26.042 1.00 70.45  ? 112 LEU   B O   1 
ATOM   1075 C  CB  . LEU   B 2 103 ? -10.232 -12.235 -28.106 1.00 71.29  ? 112 LEU   B CB  1 
ATOM   1076 C  CG  . LEU   B 2 103 ? -10.130 -13.534 -27.271 1.00 73.42  ? 112 LEU   B CG  1 
ATOM   1077 C  CD1 . LEU   B 2 103 ? -11.431 -14.278 -27.252 1.00 73.99  ? 112 LEU   B CD1 1 
ATOM   1078 C  CD2 . LEU   B 2 103 ? -9.036  -14.418 -27.755 1.00 74.49  ? 112 LEU   B CD2 1 
ATOM   1079 N  N   . PRO   B 2 104 ? -10.850 -11.090 -24.916 1.00 69.93  ? 113 PRO   B N   1 
ATOM   1080 C  CA  . PRO   B 2 104 ? -10.213 -10.839 -23.624 1.00 69.40  ? 113 PRO   B CA  1 
ATOM   1081 C  C   . PRO   B 2 104 ? -9.024  -11.732 -23.267 1.00 69.55  ? 113 PRO   B C   1 
ATOM   1082 O  O   . PRO   B 2 104 ? -8.946  -12.900 -23.641 1.00 69.30  ? 113 PRO   B O   1 
ATOM   1083 C  CB  . PRO   B 2 104 ? -11.363 -11.015 -22.629 1.00 69.68  ? 113 PRO   B CB  1 
ATOM   1084 C  CG  . PRO   B 2 104 ? -12.612 -10.959 -23.438 1.00 70.07  ? 113 PRO   B CG  1 
ATOM   1085 C  CD  . PRO   B 2 104 ? -12.248 -11.533 -24.751 1.00 68.86  ? 113 PRO   B CD  1 
ATOM   1086 N  N   . GLY   B 2 105 ? -8.109  -11.142 -22.518 1.00 69.48  ? 114 GLY   B N   1 
ATOM   1087 C  CA  . GLY   B 2 105 ? -6.977  -11.818 -21.919 1.00 69.93  ? 114 GLY   B CA  1 
ATOM   1088 C  C   . GLY   B 2 105 ? -7.360  -12.307 -20.531 1.00 70.49  ? 114 GLY   B C   1 
ATOM   1089 O  O   . GLY   B 2 105 ? -8.544  -12.499 -20.239 1.00 70.81  ? 114 GLY   B O   1 
ATOM   1090 N  N   . ILE   B 2 106 ? -6.375  -12.528 -19.661 1.00 70.12  ? 115 ILE   B N   1 
ATOM   1091 C  CA  . ILE   B 2 106 ? -6.618  -13.043 -18.325 1.00 70.25  ? 115 ILE   B CA  1 
ATOM   1092 C  C   . ILE   B 2 106 ? -5.730  -12.355 -17.320 1.00 69.81  ? 115 ILE   B C   1 
ATOM   1093 O  O   . ILE   B 2 106 ? -4.535  -12.214 -17.548 1.00 69.60  ? 115 ILE   B O   1 
ATOM   1094 C  CB  . ILE   B 2 106 ? -6.284  -14.572 -18.261 1.00 71.44  ? 115 ILE   B CB  1 
ATOM   1095 C  CG1 . ILE   B 2 106 ? -7.102  -15.413 -19.267 1.00 72.97  ? 115 ILE   B CG1 1 
ATOM   1096 C  CG2 . ILE   B 2 106 ? -6.401  -15.136 -16.833 1.00 71.98  ? 115 ILE   B CG2 1 
ATOM   1097 C  CD1 . ILE   B 2 106 ? -8.517  -15.641 -18.923 1.00 74.52  ? 115 ILE   B CD1 1 
ATOM   1098 N  N   . PHE   B 2 107 ? -6.293  -12.033 -16.158 1.00 69.49  ? 116 PHE   B N   1 
ATOM   1099 C  CA  . PHE   B 2 107 ? -5.553  -11.575 -15.003 1.00 69.11  ? 116 PHE   B CA  1 
ATOM   1100 C  C   . PHE   B 2 107 ? -5.487  -12.788 -14.087 1.00 69.10  ? 116 PHE   B C   1 
ATOM   1101 O  O   . PHE   B 2 107 ? -6.528  -13.270 -13.664 1.00 68.93  ? 116 PHE   B O   1 
ATOM   1102 C  CB  . PHE   B 2 107 ? -6.314  -10.466 -14.278 1.00 68.41  ? 116 PHE   B CB  1 
ATOM   1103 C  CG  . PHE   B 2 107 ? -6.025  -9.050  -14.709 1.00 68.28  ? 116 PHE   B CG  1 
ATOM   1104 C  CD1 . PHE   B 2 107 ? -5.241  -8.789  -15.821 1.00 68.46  ? 116 PHE   B CD1 1 
ATOM   1105 C  CD2 . PHE   B 2 107 ? -6.551  -7.976  -14.006 1.00 68.81  ? 116 PHE   B CD2 1 
ATOM   1106 C  CE1 . PHE   B 2 107 ? -4.986  -7.485  -16.217 1.00 69.14  ? 116 PHE   B CE1 1 
ATOM   1107 C  CE2 . PHE   B 2 107 ? -6.294  -6.673  -14.403 1.00 69.43  ? 116 PHE   B CE2 1 
ATOM   1108 C  CZ  . PHE   B 2 107 ? -5.521  -6.435  -15.512 1.00 69.26  ? 116 PHE   B CZ  1 
ATOM   1109 N  N   . LYS   B 2 108 ? -4.287  -13.316 -13.817 1.00 69.23  ? 117 LYS   B N   1 
ATOM   1110 C  CA  . LYS   B 2 108 ? -4.120  -14.442 -12.897 1.00 69.67  ? 117 LYS   B CA  1 
ATOM   1111 C  C   . LYS   B 2 108 ? -3.805  -13.880 -11.537 1.00 68.89  ? 117 LYS   B C   1 
ATOM   1112 O  O   . LYS   B 2 108 ? -2.832  -13.148 -11.390 1.00 68.60  ? 117 LYS   B O   1 
ATOM   1113 C  CB  . LYS   B 2 108 ? -2.979  -15.367 -13.335 1.00 72.73  ? 117 LYS   B CB  1 
ATOM   1114 C  CG  . LYS   B 2 108 ? -3.193  -15.991 -14.703 1.00 78.97  ? 117 LYS   B CG  1 
ATOM   1115 C  CD  . LYS   B 2 108 ? -2.025  -16.909 -15.059 1.00 85.77  ? 117 LYS   B CD  1 
ATOM   1116 C  CE  . LYS   B 2 108 ? -1.187  -16.359 -16.201 1.00 90.69  ? 117 LYS   B CE  1 
ATOM   1117 N  NZ  . LYS   B 2 108 ? -0.013  -17.232 -16.499 1.00 93.76  ? 117 LYS   B NZ  1 
ATOM   1118 N  N   . THR   B 2 109 ? -4.650  -14.181 -10.553 1.00 68.54  ? 118 THR   B N   1 
ATOM   1119 C  CA  . THR   B 2 109 ? -4.475  -13.719 -9.180  1.00 69.02  ? 118 THR   B CA  1 
ATOM   1120 C  C   . THR   B 2 109 ? -4.402  -14.906 -8.228  1.00 70.23  ? 118 THR   B C   1 
ATOM   1121 O  O   . THR   B 2 109 ? -4.941  -15.972 -8.536  1.00 70.84  ? 118 THR   B O   1 
ATOM   1122 C  CB  . THR   B 2 109 ? -5.637  -12.790 -8.759  1.00 69.46  ? 118 THR   B CB  1 
ATOM   1123 O  OG1 . THR   B 2 109 ? -6.835  -13.549 -8.563  1.00 70.03  ? 118 THR   B OG1 1 
ATOM   1124 C  CG2 . THR   B 2 109 ? -5.897  -11.662 -9.766  1.00 69.28  ? 118 THR   B CG2 1 
ATOM   1125 N  N   . LYS   B 2 110 ? -3.812  -14.708 -7.037  1.00 70.29  ? 119 LYS   B N   1 
ATOM   1126 C  CA  . LYS   B 2 110 ? -3.745  -15.766 -6.023  1.00 70.79  ? 119 LYS   B CA  1 
ATOM   1127 C  C   . LYS   B 2 110 ? -5.136  -16.275 -5.602  1.00 71.39  ? 119 LYS   B C   1 
ATOM   1128 O  O   . LYS   B 2 110 ? -5.219  -17.309 -4.936  1.00 71.69  ? 119 LYS   B O   1 
ATOM   1129 C  CB  . LYS   B 2 110 ? -2.950  -15.300 -4.785  1.00 71.54  ? 119 LYS   B CB  1 
ATOM   1130 C  CG  . LYS   B 2 110 ? -3.633  -14.185 -3.996  1.00 75.07  ? 119 LYS   B CG  1 
ATOM   1131 C  CD  . LYS   B 2 110 ? -2.874  -13.848 -2.707  1.00 79.33  ? 119 LYS   B CD  1 
ATOM   1132 C  CE  . LYS   B 2 110 ? -3.661  -12.983 -1.742  1.00 82.92  ? 119 LYS   B CE  1 
ATOM   1133 N  NZ  . LYS   B 2 110 ? -3.776  -11.577 -2.212  1.00 85.27  ? 119 LYS   B NZ  1 
ATOM   1134 N  N   . ASP   B 2 111 ? -6.223  -15.554 -5.974  1.00 70.97  ? 120 ASP   B N   1 
ATOM   1135 C  CA  . ASP   B 2 111 ? -7.575  -15.953 -5.631  1.00 71.49  ? 120 ASP   B CA  1 
ATOM   1136 C  C   . ASP   B 2 111 ? -8.439  -16.366 -6.816  1.00 71.85  ? 120 ASP   B C   1 
ATOM   1137 O  O   . ASP   B 2 111 ? -9.638  -16.527 -6.646  1.00 72.42  ? 120 ASP   B O   1 
ATOM   1138 C  CB  . ASP   B 2 111 ? -8.264  -14.859 -4.822  1.00 73.73  ? 120 ASP   B CB  1 
ATOM   1139 C  CG  . ASP   B 2 111 ? -7.523  -14.517 -3.545  1.00 79.99  ? 120 ASP   B CG  1 
ATOM   1140 O  OD1 . ASP   B 2 111 ? -7.326  -15.433 -2.702  1.00 81.43  ? 120 ASP   B OD1 1 
ATOM   1141 O  OD2 . ASP   B 2 111 ? -7.137  -13.337 -3.382  1.00 82.55  ? 120 ASP   B OD2 1 
ATOM   1142 N  N   . GLY   B 2 112 ? -7.847  -16.553 -7.992  1.00 71.51  ? 121 GLY   B N   1 
ATOM   1143 C  CA  . GLY   B 2 112 ? -8.589  -16.965 -9.175  1.00 71.66  ? 121 GLY   B CA  1 
ATOM   1144 C  C   . GLY   B 2 112 ? -8.306  -16.115 -10.396 1.00 71.79  ? 121 GLY   B C   1 
ATOM   1145 O  O   . GLY   B 2 112 ? -7.750  -15.023 -10.286 1.00 71.85  ? 121 GLY   B O   1 
ATOM   1146 N  N   . ASP   B 2 113 ? -8.691  -16.607 -11.568 1.00 71.76  ? 122 ASP   B N   1 
ATOM   1147 C  CA  . ASP   B 2 113 ? -8.483  -15.895 -12.827 1.00 72.20  ? 122 ASP   B CA  1 
ATOM   1148 C  C   . ASP   B 2 113 ? -9.697  -15.048 -13.186 1.00 71.60  ? 122 ASP   B C   1 
ATOM   1149 O  O   . ASP   B 2 113 ? -10.826 -15.467 -12.949 1.00 72.33  ? 122 ASP   B O   1 
ATOM   1150 C  CB  . ASP   B 2 113 ? -8.236  -16.881 -13.975 1.00 74.59  ? 122 ASP   B CB  1 
ATOM   1151 C  CG  . ASP   B 2 113 ? -6.946  -17.663 -13.896 1.00 80.84  ? 122 ASP   B CG  1 
ATOM   1152 O  OD1 . ASP   B 2 113 ? -6.303  -17.647 -12.822 1.00 81.83  ? 122 ASP   B OD1 1 
ATOM   1153 O  OD2 . ASP   B 2 113 ? -6.581  -18.299 -14.906 1.00 84.36  ? 122 ASP   B OD2 1 
ATOM   1154 N  N   . ILE   B 2 114 ? -9.467  -13.871 -13.786 1.00 69.90  ? 123 ILE   B N   1 
ATOM   1155 C  CA  . ILE   B 2 114 ? -10.522 -12.940 -14.210 1.00 68.56  ? 123 ILE   B CA  1 
ATOM   1156 C  C   . ILE   B 2 114 ? -10.229 -12.529 -15.647 1.00 66.69  ? 123 ILE   B C   1 
ATOM   1157 O  O   . ILE   B 2 114 ? -9.069  -12.384 -16.015 1.00 65.95  ? 123 ILE   B O   1 
ATOM   1158 C  CB  . ILE   B 2 114 ? -10.553 -11.661 -13.304 1.00 69.30  ? 123 ILE   B CB  1 
ATOM   1159 C  CG1 . ILE   B 2 114 ? -10.428 -11.989 -11.810 1.00 71.11  ? 123 ILE   B CG1 1 
ATOM   1160 C  CG2 . ILE   B 2 114 ? -11.789 -10.822 -13.549 1.00 69.60  ? 123 ILE   B CG2 1 
ATOM   1161 C  CD1 . ILE   B 2 114 ? -10.043 -10.786 -10.931 1.00 72.69  ? 123 ILE   B CD1 1 
ATOM   1162 N  N   . GLY   B 2 115 ? -11.270 -12.263 -16.432 1.00 65.89  ? 124 GLY   B N   1 
ATOM   1163 C  CA  . GLY   B 2 115 ? -11.090 -11.760 -17.787 1.00 65.44  ? 124 GLY   B CA  1 
ATOM   1164 C  C   . GLY   B 2 115 ? -10.463 -10.378 -17.768 1.00 64.91  ? 124 GLY   B C   1 
ATOM   1165 O  O   . GLY   B 2 115 ? -10.534 -9.672  -16.753 1.00 65.04  ? 124 GLY   B O   1 
ATOM   1166 N  N   . ALA   B 2 116 ? -9.818  -9.991  -18.860 1.00 64.50  ? 125 ALA   B N   1 
ATOM   1167 C  CA  . ALA   B 2 116 ? -9.193  -8.673  -18.955 1.00 64.98  ? 125 ALA   B CA  1 
ATOM   1168 C  C   . ALA   B 2 116 ? -9.332  -8.095  -20.380 1.00 65.61  ? 125 ALA   B C   1 
ATOM   1169 O  O   . ALA   B 2 116 ? -9.258  -8.837  -21.339 1.00 65.86  ? 125 ALA   B O   1 
ATOM   1170 C  CB  . ALA   B 2 116 ? -7.732  -8.741  -18.527 1.00 64.52  ? 125 ALA   B CB  1 
ATOM   1171 N  N   . VAL   B 2 117 ? -9.556  -6.783  -20.518 1.00 65.79  ? 126 VAL   B N   1 
ATOM   1172 C  CA  A VAL   B 2 117 ? -9.700  -6.155  -21.830 0.50 66.64  ? 126 VAL   B CA  1 
ATOM   1173 C  CA  B VAL   B 2 117 ? -9.711  -6.142  -21.818 0.50 66.38  ? 126 VAL   B CA  1 
ATOM   1174 C  C   . VAL   B 2 117 ? -8.549  -5.174  -22.105 1.00 67.20  ? 126 VAL   B C   1 
ATOM   1175 O  O   . VAL   B 2 117 ? -8.303  -4.253  -21.328 1.00 66.68  ? 126 VAL   B O   1 
ATOM   1176 C  CB  A VAL   B 2 117 ? -11.099 -5.539  -22.070 0.50 67.57  ? 126 VAL   B CB  1 
ATOM   1177 C  CB  B VAL   B 2 117 ? -11.106 -5.487  -21.936 0.50 66.75  ? 126 VAL   B CB  1 
ATOM   1178 C  CG1 A VAL   B 2 117 ? -12.095 -6.619  -22.479 0.50 68.06  ? 126 VAL   B CG1 1 
ATOM   1179 C  CG1 B VAL   B 2 117 ? -11.192 -4.563  -23.141 0.50 67.18  ? 126 VAL   B CG1 1 
ATOM   1180 C  CG2 A VAL   B 2 117 ? -11.598 -4.784  -20.842 0.50 68.48  ? 126 VAL   B CG2 1 
ATOM   1181 C  CG2 B VAL   B 2 117 ? -12.196 -6.553  -21.989 0.50 67.10  ? 126 VAL   B CG2 1 
ATOM   1182 N  N   . ALA   B 2 118 ? -7.803  -5.410  -23.205 1.00 68.25  ? 127 ALA   B N   1 
ATOM   1183 C  CA  . ALA   B 2 118 ? -6.647  -4.574  -23.529 1.00 69.84  ? 127 ALA   B CA  1 
ATOM   1184 C  C   . ALA   B 2 118 ? -6.927  -3.472  -24.545 1.00 71.28  ? 127 ALA   B C   1 
ATOM   1185 O  O   . ALA   B 2 118 ? -6.515  -3.580  -25.697 1.00 72.32  ? 127 ALA   B O   1 
ATOM   1186 C  CB  . ALA   B 2 118 ? -5.479  -5.443  -23.981 1.00 70.03  ? 127 ALA   B CB  1 
ATOM   1187 N  N   . LEU   B 2 119 ? -7.617  -2.397  -24.115 1.00 70.94  ? 128 LEU   B N   1 
ATOM   1188 C  CA  . LEU   B 2 119 ? -7.952  -1.261  -24.980 1.00 71.12  ? 128 LEU   B CA  1 
ATOM   1189 C  C   . LEU   B 2 119 ? -7.537  0.059   -24.323 1.00 71.22  ? 128 LEU   B C   1 
ATOM   1190 O  O   . LEU   B 2 119 ? -7.699  0.232   -23.113 1.00 71.22  ? 128 LEU   B O   1 
ATOM   1191 C  CB  . LEU   B 2 119 ? -9.452  -1.261  -25.317 1.00 71.20  ? 128 LEU   B CB  1 
ATOM   1192 C  CG  . LEU   B 2 119 ? -9.894  -2.450  -26.157 1.00 72.80  ? 128 LEU   B CG  1 
ATOM   1193 C  CD1 . LEU   B 2 119 ? -11.399 -2.559  -26.221 1.00 72.81  ? 128 LEU   B CD1 1 
ATOM   1194 C  CD2 . LEU   B 2 119 ? -9.250  -2.406  -27.559 1.00 73.86  ? 128 LEU   B CD2 1 
ATOM   1195 N  N   . ASP   B 2 120 ? -6.985  0.978   -25.117 1.00 71.15  ? 129 ASP   B N   1 
ATOM   1196 C  CA  . ASP   B 2 120 ? -6.505  2.266   -24.628 1.00 71.70  ? 129 ASP   B CA  1 
ATOM   1197 C  C   . ASP   B 2 120 ? -7.531  3.399   -24.736 1.00 70.67  ? 129 ASP   B C   1 
ATOM   1198 O  O   . ASP   B 2 120 ? -7.820  3.909   -25.828 1.00 71.10  ? 129 ASP   B O   1 
ATOM   1199 C  CB  . ASP   B 2 120 ? -5.225  2.668   -25.357 1.00 75.44  ? 129 ASP   B CB  1 
ATOM   1200 C  CG  . ASP   B 2 120 ? -3.970  1.965   -24.900 1.00 83.56  ? 129 ASP   B CG  1 
ATOM   1201 O  OD1 . ASP   B 2 120 ? -2.869  2.426   -25.267 1.00 86.19  ? 129 ASP   B OD1 1 
ATOM   1202 O  OD2 . ASP   B 2 120 ? -4.084  0.943   -24.191 1.00 86.74  ? 129 ASP   B OD2 1 
ATOM   1203 N  N   . TYR   B 2 121 ? -8.030  3.837   -23.595 1.00 69.21  ? 130 TYR   B N   1 
ATOM   1204 C  CA  . TYR   B 2 121 ? -9.003  4.918   -23.543 1.00 68.20  ? 130 TYR   B CA  1 
ATOM   1205 C  C   . TYR   B 2 121 ? -8.725  5.809   -22.350 1.00 66.65  ? 130 TYR   B C   1 
ATOM   1206 O  O   . TYR   B 2 121 ? -8.266  5.325   -21.312 1.00 66.64  ? 130 TYR   B O   1 
ATOM   1207 C  CB  . TYR   B 2 121 ? -10.413 4.344   -23.429 1.00 68.56  ? 130 TYR   B CB  1 
ATOM   1208 C  CG  . TYR   B 2 121 ? -11.027 3.961   -24.750 1.00 69.93  ? 130 TYR   B CG  1 
ATOM   1209 C  CD1 . TYR   B 2 121 ? -11.578 4.922   -25.587 1.00 71.32  ? 130 TYR   B CD1 1 
ATOM   1210 C  CD2 . TYR   B 2 121 ? -11.084 2.635   -25.153 1.00 71.09  ? 130 TYR   B CD2 1 
ATOM   1211 C  CE1 . TYR   B 2 121 ? -12.166 4.574   -26.794 1.00 72.45  ? 130 TYR   B CE1 1 
ATOM   1212 C  CE2 . TYR   B 2 121 ? -11.657 2.275   -26.365 1.00 72.36  ? 130 TYR   B CE2 1 
ATOM   1213 C  CZ  . TYR   B 2 121 ? -12.203 3.249   -27.180 1.00 73.82  ? 130 TYR   B CZ  1 
ATOM   1214 O  OH  . TYR   B 2 121 ? -12.787 2.907   -28.371 1.00 76.22  ? 130 TYR   B OH  1 
ATOM   1215 N  N   . PRO   B 2 122 ? -9.054  7.109   -22.448 1.00 65.01  ? 131 PRO   B N   1 
ATOM   1216 C  CA  . PRO   B 2 122 ? -8.824  8.004   -21.302 1.00 63.67  ? 131 PRO   B CA  1 
ATOM   1217 C  C   . PRO   B 2 122 ? -9.591  7.590   -20.043 1.00 61.29  ? 131 PRO   B C   1 
ATOM   1218 O  O   . PRO   B 2 122 ? -10.636 6.957   -20.145 1.00 61.06  ? 131 PRO   B O   1 
ATOM   1219 C  CB  . PRO   B 2 122 ? -9.251  9.381   -21.823 1.00 64.89  ? 131 PRO   B CB  1 
ATOM   1220 C  CG  . PRO   B 2 122 ? -10.103 9.110   -23.027 1.00 65.73  ? 131 PRO   B CG  1 
ATOM   1221 C  CD  . PRO   B 2 122 ? -9.602  7.829   -23.611 1.00 64.46  ? 131 PRO   B CD  1 
ATOM   1222 N  N   . ALA   B 2 123 ? -9.037  7.914   -18.859 1.00 59.24  ? 132 ALA   B N   1 
ATOM   1223 C  CA  . ALA   B 2 123 ? -9.591  7.595   -17.536 1.00 57.44  ? 132 ALA   B CA  1 
ATOM   1224 C  C   . ALA   B 2 123 ? -11.105 7.898   -17.383 1.00 56.32  ? 132 ALA   B C   1 
ATOM   1225 O  O   . ALA   B 2 123 ? -11.821 7.140   -16.719 1.00 55.73  ? 132 ALA   B O   1 
ATOM   1226 C  CB  . ALA   B 2 123 ? -8.791  8.312   -16.465 1.00 56.80  ? 132 ALA   B CB  1 
ATOM   1227 N  N   . GLY   B 2 124 ? -11.584 8.961   -18.048 1.00 55.54  ? 133 GLY   B N   1 
ATOM   1228 C  CA  . GLY   B 2 124 ? -12.997 9.341   -18.030 1.00 54.44  ? 133 GLY   B CA  1 
ATOM   1229 C  C   . GLY   B 2 124 ? -13.930 8.324   -18.671 1.00 53.00  ? 133 GLY   B C   1 
ATOM   1230 O  O   . GLY   B 2 124 ? -15.154 8.511   -18.680 1.00 52.52  ? 133 GLY   B O   1 
ATOM   1231 N  N   . THR   B 2 125 ? -13.358 7.236   -19.225 1.00 52.07  ? 134 THR   B N   1 
ATOM   1232 C  CA  . THR   B 2 125 ? -14.112 6.154   -19.851 1.00 51.95  ? 134 THR   B CA  1 
ATOM   1233 C  C   . THR   B 2 125 ? -14.433 5.042   -18.831 1.00 51.03  ? 134 THR   B C   1 
ATOM   1234 O  O   . THR   B 2 125 ? -15.147 4.114   -19.196 1.00 51.50  ? 134 THR   B O   1 
ATOM   1235 C  CB  . THR   B 2 125 ? -13.406 5.633   -21.153 1.00 53.93  ? 134 THR   B CB  1 
ATOM   1236 O  OG1 . THR   B 2 125 ? -12.709 6.694   -21.827 1.00 55.35  ? 134 THR   B OG1 1 
ATOM   1237 C  CG2 . THR   B 2 125 ? -14.371 5.012   -22.156 1.00 54.44  ? 134 THR   B CG2 1 
ATOM   1238 N  N   . SER   B 2 126 ? -13.928 5.129   -17.559 1.00 49.79  ? 135 SER   B N   1 
ATOM   1239 C  CA  . SER   B 2 126 ? -14.148 4.119   -16.532 1.00 49.90  ? 135 SER   B CA  1 
ATOM   1240 C  C   . SER   B 2 126 ? -15.628 3.929   -16.286 1.00 48.66  ? 135 SER   B C   1 
ATOM   1241 O  O   . SER   B 2 126 ? -16.303 4.898   -16.015 1.00 49.21  ? 135 SER   B O   1 
ATOM   1242 C  CB  . SER   B 2 126 ? -13.522 4.545   -15.204 1.00 52.95  ? 135 SER   B CB  1 
ATOM   1243 O  OG  . SER   B 2 126 ? -12.108 4.653   -15.196 1.00 56.49  ? 135 SER   B OG  1 
ATOM   1244 N  N   . GLY   B 2 127 ? -16.092 2.690   -16.267 1.00 47.15  ? 136 GLY   B N   1 
ATOM   1245 C  CA  . GLY   B 2 127 ? -17.485 2.347   -16.031 1.00 46.92  ? 136 GLY   B CA  1 
ATOM   1246 C  C   . GLY   B 2 127 ? -18.204 1.869   -17.278 1.00 47.34  ? 136 GLY   B C   1 
ATOM   1247 O  O   . GLY   B 2 127 ? -19.336 1.380   -17.187 1.00 47.49  ? 136 GLY   B O   1 
ATOM   1248 N  N   . SER   B 2 128 ? -17.556 2.021   -18.475 1.00 46.95  ? 137 SER   B N   1 
ATOM   1249 C  CA  . SER   B 2 128 ? -18.108 1.581   -19.750 1.00 47.19  ? 137 SER   B CA  1 
ATOM   1250 C  C   . SER   B 2 128 ? -18.371 0.083   -19.687 1.00 47.63  ? 137 SER   B C   1 
ATOM   1251 O  O   . SER   B 2 128 ? -17.530 -0.668  -19.198 1.00 46.52  ? 137 SER   B O   1 
ATOM   1252 C  CB  . SER   B 2 128 ? -17.131 1.881   -20.886 1.00 48.12  ? 137 SER   B CB  1 
ATOM   1253 O  OG  . SER   B 2 128 ? -17.105 3.271   -21.146 1.00 49.63  ? 137 SER   B OG  1 
ATOM   1254 N  N   . PRO   B 2 129 ? -19.567 -0.353  -20.093 1.00 48.59  ? 138 PRO   B N   1 
ATOM   1255 C  CA  . PRO   B 2 129 ? -19.878 -1.786  -20.010 1.00 49.63  ? 138 PRO   B CA  1 
ATOM   1256 C  C   . PRO   B 2 129 ? -19.215 -2.659  -21.065 1.00 51.75  ? 138 PRO   B C   1 
ATOM   1257 O  O   . PRO   B 2 129 ? -18.957 -2.233  -22.217 1.00 51.80  ? 138 PRO   B O   1 
ATOM   1258 C  CB  . PRO   B 2 129 ? -21.398 -1.830  -20.149 1.00 49.89  ? 138 PRO   B CB  1 
ATOM   1259 C  CG  . PRO   B 2 129 ? -21.754 -0.594  -20.905 1.00 50.02  ? 138 PRO   B CG  1 
ATOM   1260 C  CD  . PRO   B 2 129 ? -20.689 0.431   -20.641 1.00 48.08  ? 138 PRO   B CD  1 
ATOM   1261 N  N   . ILE   B 2 130 ? -18.981 -3.928  -20.658 1.00 52.16  ? 139 ILE   B N   1 
ATOM   1262 C  CA  . ILE   B 2 130 ? -18.468 -4.988  -21.502 1.00 53.33  ? 139 ILE   B CA  1 
ATOM   1263 C  C   . ILE   B 2 130 ? -19.629 -5.935  -21.790 1.00 54.91  ? 139 ILE   B C   1 
ATOM   1264 O  O   . ILE   B 2 130 ? -20.359 -6.297  -20.871 1.00 53.72  ? 139 ILE   B O   1 
ATOM   1265 C  CB  . ILE   B 2 130 ? -17.266 -5.685  -20.865 1.00 53.30  ? 139 ILE   B CB  1 
ATOM   1266 C  CG1 . ILE   B 2 130 ? -16.124 -4.676  -20.645 1.00 53.84  ? 139 ILE   B CG1 1 
ATOM   1267 C  CG2 . ILE   B 2 130 ? -16.829 -6.852  -21.748 1.00 53.81  ? 139 ILE   B CG2 1 
ATOM   1268 C  CD1 . ILE   B 2 130 ? -15.093 -5.140  -19.522 1.00 55.14  ? 139 ILE   B CD1 1 
ATOM   1269 N  N   . LEU   B 2 131 ? -19.835 -6.288  -23.079 1.00 57.14  ? 140 LEU   B N   1 
ATOM   1270 C  CA  . LEU   B 2 131 ? -21.001 -7.051  -23.531 1.00 59.73  ? 140 LEU   B CA  1 
ATOM   1271 C  C   . LEU   B 2 131 ? -20.771 -8.437  -24.085 1.00 62.21  ? 140 LEU   B C   1 
ATOM   1272 O  O   . LEU   B 2 131 ? -19.764 -8.682  -24.744 1.00 62.96  ? 140 LEU   B O   1 
ATOM   1273 C  CB  . LEU   B 2 131 ? -21.751 -6.247  -24.615 1.00 60.05  ? 140 LEU   B CB  1 
ATOM   1274 C  CG  . LEU   B 2 131 ? -22.020 -4.757  -24.342 1.00 61.62  ? 140 LEU   B CG  1 
ATOM   1275 C  CD1 . LEU   B 2 131 ? -22.957 -4.192  -25.362 1.00 61.75  ? 140 LEU   B CD1 1 
ATOM   1276 C  CD2 . LEU   B 2 131 ? -22.611 -4.522  -22.935 1.00 62.10  ? 140 LEU   B CD2 1 
ATOM   1277 N  N   . ASP   B 2 132 ? -21.752 -9.340  -23.864 1.00 62.97  ? 141 ASP   B N   1 
ATOM   1278 C  CA  . ASP   B 2 132 ? -21.729 -10.678 -24.451 1.00 63.83  ? 141 ASP   B CA  1 
ATOM   1279 C  C   . ASP   B 2 132 ? -22.498 -10.653 -25.812 1.00 65.73  ? 141 ASP   B C   1 
ATOM   1280 O  O   . ASP   B 2 132 ? -23.058 -9.608  -26.170 1.00 65.36  ? 141 ASP   B O   1 
ATOM   1281 C  CB  . ASP   B 2 132 ? -22.213 -11.754 -23.455 1.00 64.05  ? 141 ASP   B CB  1 
ATOM   1282 C  CG  . ASP   B 2 132 ? -23.700 -11.997 -23.300 1.00 66.14  ? 141 ASP   B CG  1 
ATOM   1283 O  OD1 . ASP   B 2 132 ? -24.496 -11.181 -23.811 1.00 66.11  ? 141 ASP   B OD1 1 
ATOM   1284 O  OD2 . ASP   B 2 132 ? -24.071 -13.002 -22.640 1.00 67.28  ? 141 ASP   B OD2 1 
ATOM   1285 N  N   . LYS   B 2 133 ? -22.528 -11.768 -26.569 1.00 66.92  ? 142 LYS   B N   1 
ATOM   1286 C  CA  . LYS   B 2 133 ? -23.183 -11.778 -27.889 1.00 68.22  ? 142 LYS   B CA  1 
ATOM   1287 C  C   . LYS   B 2 133 ? -24.698 -11.542 -27.835 1.00 68.08  ? 142 LYS   B C   1 
ATOM   1288 O  O   . LYS   B 2 133 ? -25.283 -11.143 -28.842 1.00 68.39  ? 142 LYS   B O   1 
ATOM   1289 C  CB  . LYS   B 2 133 ? -22.838 -13.045 -28.672 1.00 71.48  ? 142 LYS   B CB  1 
ATOM   1290 C  CG  . LYS   B 2 133 ? -21.407 -13.008 -29.205 1.00 78.29  ? 142 LYS   B CG  1 
ATOM   1291 C  CD  . LYS   B 2 133 ? -20.673 -14.380 -29.147 1.00 83.19  ? 142 LYS   B CD  1 
ATOM   1292 C  CE  . LYS   B 2 133 ? -19.646 -14.474 -30.262 1.00 87.30  ? 142 LYS   B CE  1 
ATOM   1293 N  NZ  . LYS   B 2 133 ? -18.946 -15.792 -30.297 1.00 90.19  ? 142 LYS   B NZ  1 
ATOM   1294 N  N   . CYS   B 2 134 ? -25.328 -11.735 -26.664 1.00 67.44  ? 143 CYS   B N   1 
ATOM   1295 C  CA  . CYS   B 2 134 ? -26.758 -11.406 -26.517 1.00 66.98  ? 143 CYS   B CA  1 
ATOM   1296 C  C   . CYS   B 2 134 ? -27.000 -9.983  -26.067 1.00 64.73  ? 143 CYS   B C   1 
ATOM   1297 O  O   . CYS   B 2 134 ? -28.157 -9.618  -25.930 1.00 64.83  ? 143 CYS   B O   1 
ATOM   1298 C  CB  . CYS   B 2 134 ? -27.462 -12.372 -25.582 1.00 69.07  ? 143 CYS   B CB  1 
ATOM   1299 S  SG  . CYS   B 2 134 ? -26.929 -14.076 -25.772 1.00 77.12  ? 143 CYS   B SG  1 
ATOM   1300 N  N   . GLY   B 2 135 ? -25.942 -9.224  -25.785 1.00 63.00  ? 144 GLY   B N   1 
ATOM   1301 C  CA  . GLY   B 2 135 ? -26.025 -7.858  -25.303 1.00 62.45  ? 144 GLY   B CA  1 
ATOM   1302 C  C   . GLY   B 2 135 ? -26.103 -7.727  -23.790 1.00 61.26  ? 144 GLY   B C   1 
ATOM   1303 O  O   . GLY   B 2 135 ? -26.372 -6.634  -23.299 1.00 62.10  ? 144 GLY   B O   1 
ATOM   1304 N  N   . ARG   B 2 136 ? -25.891 -8.820  -23.041 1.00 59.51  ? 145 ARG   B N   1 
ATOM   1305 C  CA  . ARG   B 2 136 ? -25.914 -8.793  -21.570 1.00 58.37  ? 145 ARG   B CA  1 
ATOM   1306 C  C   . ARG   B 2 136 ? -24.605 -8.250  -21.024 1.00 56.09  ? 145 ARG   B C   1 
ATOM   1307 O  O   . ARG   B 2 136 ? -23.539 -8.587  -21.536 1.00 55.83  ? 145 ARG   B O   1 
ATOM   1308 C  CB  . ARG   B 2 136 ? -26.176 -10.191 -20.983 1.00 60.34  ? 145 ARG   B CB  1 
ATOM   1309 C  CG  . ARG   B 2 136 ? -27.575 -10.705 -21.285 1.00 65.42  ? 145 ARG   B CG  1 
ATOM   1310 C  CD  . ARG   B 2 136 ? -27.861 -12.021 -20.603 1.00 70.04  ? 145 ARG   B CD  1 
ATOM   1311 N  NE  . ARG   B 2 136 ? -26.994 -13.076 -21.120 1.00 75.99  ? 145 ARG   B NE  1 
ATOM   1312 C  CZ  . ARG   B 2 136 ? -26.469 -14.051 -20.379 1.00 80.86  ? 145 ARG   B CZ  1 
ATOM   1313 N  NH1 . ARG   B 2 136 ? -26.714 -14.110 -19.071 1.00 81.58  ? 145 ARG   B NH1 1 
ATOM   1314 N  NH2 . ARG   B 2 136 ? -25.676 -14.962 -20.936 1.00 80.94  ? 145 ARG   B NH2 1 
ATOM   1315 N  N   . VAL   B 2 137 ? -24.678 -7.385  -20.002 1.00 54.60  ? 146 VAL   B N   1 
ATOM   1316 C  CA  . VAL   B 2 137 ? -23.472 -6.802  -19.430 1.00 53.37  ? 146 VAL   B CA  1 
ATOM   1317 C  C   . VAL   B 2 137 ? -22.747 -7.835  -18.571 1.00 53.21  ? 146 VAL   B C   1 
ATOM   1318 O  O   . VAL   B 2 137 ? -23.278 -8.270  -17.552 1.00 53.94  ? 146 VAL   B O   1 
ATOM   1319 C  CB  . VAL   B 2 137 ? -23.754 -5.483  -18.680 1.00 52.99  ? 146 VAL   B CB  1 
ATOM   1320 C  CG1 . VAL   B 2 137 ? -22.461 -4.827  -18.242 1.00 53.29  ? 146 VAL   B CG1 1 
ATOM   1321 C  CG2 . VAL   B 2 137 ? -24.547 -4.528  -19.552 1.00 53.42  ? 146 VAL   B CG2 1 
ATOM   1322 N  N   . ILE   B 2 138 ? -21.579 -8.285  -19.026 1.00 52.04  ? 147 ILE   B N   1 
ATOM   1323 C  CA  . ILE   B 2 138 ? -20.750 -9.240  -18.294 1.00 51.10  ? 147 ILE   B CA  1 
ATOM   1324 C  C   . ILE   B 2 138 ? -19.751 -8.534  -17.346 1.00 51.12  ? 147 ILE   B C   1 
ATOM   1325 O  O   . ILE   B 2 138 ? -19.043 -9.230  -16.608 1.00 51.71  ? 147 ILE   B O   1 
ATOM   1326 C  CB  . ILE   B 2 138 ? -20.014 -10.227 -19.255 1.00 50.54  ? 147 ILE   B CB  1 
ATOM   1327 C  CG1 . ILE   B 2 138 ? -19.201 -9.459  -20.310 1.00 51.11  ? 147 ILE   B CG1 1 
ATOM   1328 C  CG2 . ILE   B 2 138 ? -21.000 -11.182 -19.903 1.00 50.98  ? 147 ILE   B CG2 1 
ATOM   1329 C  CD1 . ILE   B 2 138 ? -18.353 -10.303 -21.243 1.00 52.20  ? 147 ILE   B CD1 1 
ATOM   1330 N  N   . GLY   B 2 139 ? -19.677 -7.194  -17.369 1.00 49.70  ? 148 GLY   B N   1 
ATOM   1331 C  CA  . GLY   B 2 139 ? -18.765 -6.491  -16.472 1.00 49.73  ? 148 GLY   B CA  1 
ATOM   1332 C  C   . GLY   B 2 139 ? -18.509 -5.056  -16.855 1.00 49.67  ? 148 GLY   B C   1 
ATOM   1333 O  O   . GLY   B 2 139 ? -19.047 -4.586  -17.847 1.00 49.77  ? 148 GLY   B O   1 
ATOM   1334 N  N   . LEU   B 2 140 ? -17.702 -4.338  -16.070 1.00 49.13  ? 149 LEU   B N   1 
ATOM   1335 C  CA  . LEU   B 2 140 ? -17.408 -2.925  -16.353 1.00 48.33  ? 149 LEU   B CA  1 
ATOM   1336 C  C   . LEU   B 2 140 ? -15.918 -2.748  -16.554 1.00 48.58  ? 149 LEU   B C   1 
ATOM   1337 O  O   . LEU   B 2 140 ? -15.116 -3.385  -15.868 1.00 48.00  ? 149 LEU   B O   1 
ATOM   1338 C  CB  . LEU   B 2 140 ? -17.872 -1.991  -15.218 1.00 47.48  ? 149 LEU   B CB  1 
ATOM   1339 C  CG  . LEU   B 2 140 ? -19.348 -2.039  -14.786 1.00 48.41  ? 149 LEU   B CG  1 
ATOM   1340 C  CD1 . LEU   B 2 140 ? -19.655 -0.898  -13.819 1.00 48.65  ? 149 LEU   B CD1 1 
ATOM   1341 C  CD2 . LEU   B 2 140 ? -20.308 -1.936  -15.984 1.00 48.74  ? 149 LEU   B CD2 1 
ATOM   1342 N  N   . TYR   B 2 141 ? -15.559 -1.844  -17.465 1.00 49.06  ? 150 TYR   B N   1 
ATOM   1343 C  CA  . TYR   B 2 141 ? -14.193 -1.517  -17.866 1.00 50.44  ? 150 TYR   B CA  1 
ATOM   1344 C  C   . TYR   B 2 141 ? -13.697 -0.283  -17.131 1.00 50.62  ? 150 TYR   B C   1 
ATOM   1345 O  O   . TYR   B 2 141 ? -14.445 0.669   -17.048 1.00 50.95  ? 150 TYR   B O   1 
ATOM   1346 C  CB  . TYR   B 2 141 ? -14.216 -1.264  -19.390 1.00 51.32  ? 150 TYR   B CB  1 
ATOM   1347 C  CG  . TYR   B 2 141 ? -13.032 -0.519  -19.974 1.00 53.79  ? 150 TYR   B CG  1 
ATOM   1348 C  CD1 . TYR   B 2 141 ? -13.093 0.855   -20.206 1.00 54.99  ? 150 TYR   B CD1 1 
ATOM   1349 C  CD2 . TYR   B 2 141 ? -11.898 -1.204  -20.409 1.00 55.48  ? 150 TYR   B CD2 1 
ATOM   1350 C  CE1 . TYR   B 2 141 ? -12.030 1.537   -20.794 1.00 56.49  ? 150 TYR   B CE1 1 
ATOM   1351 C  CE2 . TYR   B 2 141 ? -10.819 -0.531  -20.978 1.00 56.80  ? 150 TYR   B CE2 1 
ATOM   1352 C  CZ  . TYR   B 2 141 ? -10.896 0.839   -21.189 1.00 57.96  ? 150 TYR   B CZ  1 
ATOM   1353 O  OH  . TYR   B 2 141 ? -9.826  1.513   -21.748 1.00 59.77  ? 150 TYR   B OH  1 
ATOM   1354 N  N   . GLY   B 2 142 ? -12.471 -0.285  -16.618 1.00 50.89  ? 151 GLY   B N   1 
ATOM   1355 C  CA  . GLY   B 2 142 ? -11.953 0.907   -15.953 1.00 51.99  ? 151 GLY   B CA  1 
ATOM   1356 C  C   . GLY   B 2 142 ? -11.172 0.745   -14.670 1.00 52.68  ? 151 GLY   B C   1 
ATOM   1357 O  O   . GLY   B 2 142 ? -10.808 1.755   -14.058 1.00 52.69  ? 151 GLY   B O   1 
ATOM   1358 N  N   . ASN   B 2 143 ? -10.882 -0.504  -14.262 1.00 52.47  ? 152 ASN   B N   1 
ATOM   1359 C  CA  . ASN   B 2 143 ? -10.021 -0.788  -13.124 1.00 53.41  ? 152 ASN   B CA  1 
ATOM   1360 C  C   . ASN   B 2 143 ? -9.027  -1.827  -13.608 1.00 54.91  ? 152 ASN   B C   1 
ATOM   1361 O  O   . ASN   B 2 143 ? -9.412  -2.951  -13.925 1.00 54.51  ? 152 ASN   B O   1 
ATOM   1362 C  CB  . ASN   B 2 143 ? -10.777 -1.326  -11.903 1.00 53.72  ? 152 ASN   B CB  1 
ATOM   1363 C  CG  . ASN   B 2 143 ? -9.888  -1.365  -10.681 1.00 55.28  ? 152 ASN   B CG  1 
ATOM   1364 O  OD1 . ASN   B 2 143 ? -9.015  -0.510  -10.511 1.00 56.56  ? 152 ASN   B OD1 1 
ATOM   1365 N  ND2 . ASN   B 2 143 ? -10.090 -2.335  -9.785  1.00 54.99  ? 152 ASN   B ND2 1 
ATOM   1366 N  N   . GLY   B 2 144 ? -7.777  -1.426  -13.725 1.00 56.40  ? 153 GLY   B N   1 
ATOM   1367 C  CA  . GLY   B 2 144 ? -6.759  -2.327  -14.217 1.00 58.81  ? 153 GLY   B CA  1 
ATOM   1368 C  C   . GLY   B 2 144 ? -5.363  -1.852  -13.951 1.00 61.57  ? 153 GLY   B C   1 
ATOM   1369 O  O   . GLY   B 2 144 ? -5.066  -1.336  -12.872 1.00 61.25  ? 153 GLY   B O   1 
ATOM   1370 N  N   . VAL   B 2 145 ? -4.493  -2.045  -14.946 1.00 63.97  ? 154 VAL   B N   1 
ATOM   1371 C  CA  . VAL   B 2 145 ? -3.094  -1.703  -14.809 1.00 67.12  ? 154 VAL   B CA  1 
ATOM   1372 C  C   . VAL   B 2 145 ? -2.490  -1.152  -16.128 1.00 70.31  ? 154 VAL   B C   1 
ATOM   1373 O  O   . VAL   B 2 145 ? -3.024  -1.374  -17.216 1.00 70.42  ? 154 VAL   B O   1 
ATOM   1374 C  CB  . VAL   B 2 145 ? -2.353  -2.948  -14.254 1.00 68.19  ? 154 VAL   B CB  1 
ATOM   1375 C  CG1 . VAL   B 2 145 ? -1.995  -3.917  -15.371 1.00 68.64  ? 154 VAL   B CG1 1 
ATOM   1376 C  CG2 . VAL   B 2 145 ? -1.138  -2.561  -13.417 1.00 68.88  ? 154 VAL   B CG2 1 
ATOM   1377 N  N   . VAL   B 2 146 ? -1.419  -0.363  -16.002 1.00 72.63  ? 155 VAL   B N   1 
ATOM   1378 C  CA  . VAL   B 2 146 ? -0.697  0.235   -17.117 1.00 75.30  ? 155 VAL   B CA  1 
ATOM   1379 C  C   . VAL   B 2 146 ? 0.593   -0.566  -17.266 1.00 78.84  ? 155 VAL   B C   1 
ATOM   1380 O  O   . VAL   B 2 146 ? 1.407   -0.590  -16.349 1.00 79.32  ? 155 VAL   B O   1 
ATOM   1381 C  CB  . VAL   B 2 146 ? -0.402  1.738   -16.895 1.00 75.60  ? 155 VAL   B CB  1 
ATOM   1382 C  CG1 . VAL   B 2 146 ? 0.073   2.391   -18.184 1.00 76.02  ? 155 VAL   B CG1 1 
ATOM   1383 C  CG2 . VAL   B 2 146 ? -1.621  2.471   -16.367 1.00 76.07  ? 155 VAL   B CG2 1 
ATOM   1384 N  N   . ILE   B 2 147 ? 0.767   -1.251  -18.400 1.00 81.30  ? 156 ILE   B N   1 
ATOM   1385 C  CA  . ILE   B 2 147 ? 1.935   -2.105  -18.641 1.00 83.83  ? 156 ILE   B CA  1 
ATOM   1386 C  C   . ILE   B 2 147 ? 3.069   -1.375  -19.417 1.00 86.07  ? 156 ILE   B C   1 
ATOM   1387 O  O   . ILE   B 2 147 ? 2.894   -0.228  -19.825 1.00 86.55  ? 156 ILE   B O   1 
ATOM   1388 C  CB  . ILE   B 2 147 ? 1.459   -3.416  -19.333 1.00 84.76  ? 156 ILE   B CB  1 
ATOM   1389 C  CG1 . ILE   B 2 147 ? 0.713   -3.092  -20.638 1.00 86.46  ? 156 ILE   B CG1 1 
ATOM   1390 C  CG2 . ILE   B 2 147 ? 0.559   -4.205  -18.391 1.00 85.40  ? 156 ILE   B CG2 1 
ATOM   1391 C  CD1 . ILE   B 2 147 ? 0.565   -4.251  -21.605 1.00 88.20  ? 156 ILE   B CD1 1 
ATOM   1392 N  N   . LYS   B 2 148 ? 4.235   -2.044  -19.560 1.00 87.13  ? 157 LYS   B N   1 
ATOM   1393 C  CA  . LYS   B 2 148 ? 5.487   -1.667  -20.220 1.00 88.38  ? 157 LYS   B CA  1 
ATOM   1394 C  C   . LYS   B 2 148 ? 5.549   -0.294  -20.955 1.00 89.13  ? 157 LYS   B C   1 
ATOM   1395 O  O   . LYS   B 2 148 ? 6.350   0.554   -20.570 1.00 89.87  ? 157 LYS   B O   1 
ATOM   1396 C  CB  . LYS   B 2 148 ? 5.913   -2.786  -21.193 1.00 90.69  ? 157 LYS   B CB  1 
ATOM   1397 C  CG  . LYS   B 2 148 ? 7.114   -3.600  -20.697 1.00 96.02  ? 157 LYS   B CG  1 
ATOM   1398 C  CD  . LYS   B 2 148 ? 6.746   -4.941  -20.010 1.00 101.04 ? 157 LYS   B CD  1 
ATOM   1399 C  CE  . LYS   B 2 148 ? 6.360   -4.863  -18.540 1.00 104.85 ? 157 LYS   B CE  1 
ATOM   1400 N  NZ  . LYS   B 2 148 ? 4.952   -4.408  -18.347 1.00 106.47 ? 157 LYS   B NZ  1 
ATOM   1401 N  N   . ASN   B 2 149 ? 4.750   -0.083  -22.005 1.00 88.69  ? 158 ASN   B N   1 
ATOM   1402 C  CA  . ASN   B 2 149 ? 4.817   1.109   -22.859 1.00 88.77  ? 158 ASN   B CA  1 
ATOM   1403 C  C   . ASN   B 2 149 ? 3.767   2.193   -22.606 1.00 87.50  ? 158 ASN   B C   1 
ATOM   1404 O  O   . ASN   B 2 149 ? 3.582   3.092   -23.438 1.00 87.79  ? 158 ASN   B O   1 
ATOM   1405 C  CB  . ASN   B 2 149 ? 4.730   0.673   -24.320 1.00 91.24  ? 158 ASN   B CB  1 
ATOM   1406 C  CG  . ASN   B 2 149 ? 3.632   -0.344  -24.577 1.00 96.32  ? 158 ASN   B CG  1 
ATOM   1407 O  OD1 . ASN   B 2 149 ? 2.512   0.014   -24.944 1.00 98.27  ? 158 ASN   B OD1 1 
ATOM   1408 N  ND2 . ASN   B 2 149 ? 3.928   -1.639  -24.382 1.00 97.23  ? 158 ASN   B ND2 1 
ATOM   1409 N  N   . GLY   B 2 150 ? 3.094   2.111   -21.473 1.00 85.50  ? 159 GLY   B N   1 
ATOM   1410 C  CA  . GLY   B 2 150 ? 2.023   3.046   -21.160 1.00 83.74  ? 159 GLY   B CA  1 
ATOM   1411 C  C   . GLY   B 2 150 ? 0.666   2.578   -21.659 1.00 81.16  ? 159 GLY   B C   1 
ATOM   1412 O  O   . GLY   B 2 150 ? -0.286  3.355   -21.651 1.00 81.22  ? 159 GLY   B O   1 
ATOM   1413 N  N   . SER   B 2 151 ? 0.557   1.303   -22.098 1.00 78.66  ? 160 SER   B N   1 
ATOM   1414 C  CA  A SER   B 2 151 ? -0.693  0.716   -22.581 0.50 77.72  ? 160 SER   B CA  1 
ATOM   1415 C  CA  B SER   B 2 151 ? -0.719  0.776   -22.569 0.50 77.64  ? 160 SER   B CA  1 
ATOM   1416 C  C   . SER   B 2 151 ? -1.568  0.312   -21.394 1.00 76.07  ? 160 SER   B C   1 
ATOM   1417 O  O   . SER   B 2 151 ? -1.045  -0.058  -20.337 1.00 76.16  ? 160 SER   B O   1 
ATOM   1418 C  CB  A SER   B 2 151 ? -0.406  -0.506  -23.450 0.50 79.20  ? 160 SER   B CB  1 
ATOM   1419 C  CB  B SER   B 2 151 ? -0.527  -0.333  -23.601 0.50 78.90  ? 160 SER   B CB  1 
ATOM   1420 O  OG  A SER   B 2 151 ? -1.582  -1.012  -24.060 0.50 81.91  ? 160 SER   B OG  1 
ATOM   1421 O  OG  B SER   B 2 151 ? 0.524   -1.219  -23.260 0.50 81.06  ? 160 SER   B OG  1 
ATOM   1422 N  N   . TYR   B 2 152 ? -2.882  0.358   -21.568 1.00 72.71  ? 161 TYR   B N   1 
ATOM   1423 C  CA  . TYR   B 2 152 ? -3.805  0.019   -20.502 1.00 69.93  ? 161 TYR   B CA  1 
ATOM   1424 C  C   . TYR   B 2 152 ? -4.523  -1.333  -20.665 1.00 67.12  ? 161 TYR   B C   1 
ATOM   1425 O  O   . TYR   B 2 152 ? -5.025  -1.661  -21.730 1.00 67.69  ? 161 TYR   B O   1 
ATOM   1426 C  CB  . TYR   B 2 152 ? -4.815  1.176   -20.341 1.00 69.14  ? 161 TYR   B CB  1 
ATOM   1427 C  CG  . TYR   B 2 152 ? -5.793  0.988   -19.210 1.00 67.84  ? 161 TYR   B CG  1 
ATOM   1428 C  CD1 . TYR   B 2 152 ? -5.387  1.095   -17.888 1.00 68.10  ? 161 TYR   B CD1 1 
ATOM   1429 C  CD2 . TYR   B 2 152 ? -7.134  0.745   -19.462 1.00 68.05  ? 161 TYR   B CD2 1 
ATOM   1430 C  CE1 . TYR   B 2 152 ? -6.282  0.908   -16.842 1.00 68.28  ? 161 TYR   B CE1 1 
ATOM   1431 C  CE2 . TYR   B 2 152 ? -8.040  0.566   -18.426 1.00 68.44  ? 161 TYR   B CE2 1 
ATOM   1432 C  CZ  . TYR   B 2 152 ? -7.605  0.627   -17.119 1.00 68.81  ? 161 TYR   B CZ  1 
ATOM   1433 O  OH  . TYR   B 2 152 ? -8.503  0.442   -16.110 1.00 69.98  ? 161 TYR   B OH  1 
ATOM   1434 N  N   . VAL   B 2 153 ? -4.579  -2.107  -19.588 1.00 64.08  ? 162 VAL   B N   1 
ATOM   1435 C  CA  . VAL   B 2 153 ? -5.295  -3.376  -19.574 1.00 61.48  ? 162 VAL   B CA  1 
ATOM   1436 C  C   . VAL   B 2 153 ? -6.245  -3.295  -18.387 1.00 58.34  ? 162 VAL   B C   1 
ATOM   1437 O  O   . VAL   B 2 153 ? -5.778  -3.112  -17.273 1.00 57.52  ? 162 VAL   B O   1 
ATOM   1438 C  CB  . VAL   B 2 153 ? -4.350  -4.603  -19.447 1.00 61.65  ? 162 VAL   B CB  1 
ATOM   1439 C  CG1 . VAL   B 2 153 ? -5.135  -5.905  -19.551 1.00 61.46  ? 162 VAL   B CG1 1 
ATOM   1440 C  CG2 . VAL   B 2 153 ? -3.254  -4.559  -20.504 1.00 62.88  ? 162 VAL   B CG2 1 
ATOM   1441 N  N   . SER   B 2 154 ? -7.559  -3.398  -18.625 1.00 56.40  ? 163 SER   B N   1 
ATOM   1442 C  CA  . SER   B 2 154 ? -8.559  -3.354  -17.564 1.00 55.85  ? 163 SER   B CA  1 
ATOM   1443 C  C   . SER   B 2 154 ? -9.070  -4.742  -17.212 1.00 54.90  ? 163 SER   B C   1 
ATOM   1444 O  O   . SER   B 2 154 ? -9.172  -5.585  -18.081 1.00 54.86  ? 163 SER   B O   1 
ATOM   1445 C  CB  . SER   B 2 154 ? -9.750  -2.502  -17.999 1.00 57.10  ? 163 SER   B CB  1 
ATOM   1446 O  OG  . SER   B 2 154 ? -10.887 -2.641  -17.157 1.00 57.94  ? 163 SER   B OG  1 
ATOM   1447 N  N   . ALA   B 2 155 ? -9.487  -4.952  -15.964 1.00 53.84  ? 164 ALA   B N   1 
ATOM   1448 C  CA  . ALA   B 2 155 ? -10.120 -6.211  -15.568 1.00 53.25  ? 164 ALA   B CA  1 
ATOM   1449 C  C   . ALA   B 2 155 ? -11.575 -6.216  -16.107 1.00 52.95  ? 164 ALA   B C   1 
ATOM   1450 O  O   . ALA   B 2 155 ? -12.115 -5.156  -16.474 1.00 52.55  ? 164 ALA   B O   1 
ATOM   1451 C  CB  . ALA   B 2 155 ? -10.143 -6.317  -14.043 1.00 53.07  ? 164 ALA   B CB  1 
ATOM   1452 N  N   . ILE   B 2 156 ? -12.207 -7.404  -16.175 1.00 52.42  ? 165 ILE   B N   1 
ATOM   1453 C  CA  . ILE   B 2 156 ? -13.621 -7.472  -16.511 1.00 51.98  ? 165 ILE   B CA  1 
ATOM   1454 C  C   . ILE   B 2 156 ? -14.286 -7.540  -15.122 1.00 51.12  ? 165 ILE   B C   1 
ATOM   1455 O  O   . ILE   B 2 156 ? -14.327 -8.615  -14.518 1.00 50.81  ? 165 ILE   B O   1 
ATOM   1456 C  CB  . ILE   B 2 156 ? -14.000 -8.664  -17.396 1.00 52.34  ? 165 ILE   B CB  1 
ATOM   1457 C  CG1 . ILE   B 2 156 ? -13.332 -8.550  -18.779 1.00 53.44  ? 165 ILE   B CG1 1 
ATOM   1458 C  CG2 . ILE   B 2 156 ? -15.526 -8.696  -17.555 1.00 53.13  ? 165 ILE   B CG2 1 
ATOM   1459 C  CD1 . ILE   B 2 156 ? -13.558 -9.749  -19.630 1.00 54.60  ? 165 ILE   B CD1 1 
ATOM   1460 N  N   . THR   B 2 157 ? -14.697 -6.377  -14.572 1.00 50.26  ? 166 THR   B N   1 
ATOM   1461 C  CA  . THR   B 2 157 ? -15.243 -6.321  -13.208 1.00 50.24  ? 166 THR   B CA  1 
ATOM   1462 C  C   . THR   B 2 157 ? -16.751 -6.529  -13.100 1.00 49.97  ? 166 THR   B C   1 
ATOM   1463 O  O   . THR   B 2 157 ? -17.527 -5.655  -13.476 1.00 49.72  ? 166 THR   B O   1 
ATOM   1464 C  CB  . THR   B 2 157 ? -14.862 -5.021  -12.499 1.00 50.82  ? 166 THR   B CB  1 
ATOM   1465 O  OG1 . THR   B 2 157 ? -13.455 -4.783  -12.580 1.00 51.45  ? 166 THR   B OG1 1 
ATOM   1466 C  CG2 . THR   B 2 157 ? -15.287 -5.026  -11.073 1.00 50.67  ? 166 THR   B CG2 1 
ATOM   1467 N  N   . GLN   B 2 158 ? -17.158 -7.660  -12.533 1.00 49.58  ? 167 GLN   B N   1 
ATOM   1468 C  CA  . GLN   B 2 158 ? -18.566 -7.965  -12.345 1.00 49.98  ? 167 GLN   B CA  1 
ATOM   1469 C  C   . GLN   B 2 158 ? -18.889 -8.069  -10.827 1.00 51.24  ? 167 GLN   B C   1 
ATOM   1470 O  O   . GLN   B 2 158 ? -18.058 -8.525  -10.056 1.00 51.13  ? 167 GLN   B O   1 
ATOM   1471 C  CB  . GLN   B 2 158 ? -18.915 -9.288  -13.071 1.00 49.64  ? 167 GLN   B CB  1 
ATOM   1472 C  CG  . GLN   B 2 158 ? -20.400 -9.689  -13.082 1.00 50.34  ? 167 GLN   B CG  1 
ATOM   1473 C  CD  . GLN   B 2 158 ? -21.311 -8.649  -13.712 1.00 51.73  ? 167 GLN   B CD  1 
ATOM   1474 O  OE1 . GLN   B 2 158 ? -21.451 -7.538  -13.220 1.00 50.26  ? 167 GLN   B OE1 1 
ATOM   1475 N  NE2 . GLN   B 2 158 ? -21.969 -8.990  -14.808 1.00 52.76  ? 167 GLN   B NE2 1 
ATOM   1476 N  N   . GLY   B 2 159 ? -20.085 -7.651  -10.431 1.00 52.49  ? 168 GLY   B N   1 
ATOM   1477 C  CA  . GLY   B 2 159 ? -20.542 -7.776  -9.057  1.00 54.88  ? 168 GLY   B CA  1 
ATOM   1478 C  C   . GLY   B 2 159 ? -21.406 -9.008  -8.857  1.00 57.91  ? 168 GLY   B C   1 
ATOM   1479 O  O   . GLY   B 2 159 ? -21.606 -9.807  -9.779  1.00 57.97  ? 168 GLY   B O   1 
ATOM   1480 N  N   . LYS   B 2 160 ? -21.938 -9.171  -7.651  1.00 60.66  ? 169 LYS   B N   1 
ATOM   1481 C  CA  . LYS   B 2 160 ? -22.774 -10.325 -7.318  1.00 63.65  ? 169 LYS   B CA  1 
ATOM   1482 C  C   . LYS   B 2 160 ? -24.248 -9.936  -7.142  1.00 66.45  ? 169 LYS   B C   1 
ATOM   1483 O  O   . LYS   B 2 160 ? -24.556 -9.066  -6.326  1.00 67.08  ? 169 LYS   B O   1 
ATOM   1484 C  CB  . LYS   B 2 160 ? -22.248 -11.010 -6.044  1.00 65.48  ? 169 LYS   B CB  1 
ATOM   1485 C  CG  . LYS   B 2 160 ? -23.062 -12.229 -5.637  1.00 70.28  ? 169 LYS   B CG  1 
ATOM   1486 C  CD  . LYS   B 2 160 ? -22.537 -12.864 -4.359  1.00 74.96  ? 169 LYS   B CD  1 
ATOM   1487 C  CE  . LYS   B 2 160 ? -23.534 -13.824 -3.767  1.00 79.06  ? 169 LYS   B CE  1 
ATOM   1488 N  NZ  . LYS   B 2 160 ? -23.656 -13.627 -2.297  1.00 81.84  ? 169 LYS   B NZ  1 
ATOM   1489 N  N   . ARG   B 2 161 ? -25.156 -10.585 -7.889  1.00 67.84  ? 170 ARG   B N   1 
ATOM   1490 C  CA  . ARG   B 2 161 ? -26.585 -10.312 -7.764  1.00 69.67  ? 170 ARG   B CA  1 
ATOM   1491 C  C   . ARG   B 2 161 ? -27.128 -11.161 -6.604  1.00 72.07  ? 170 ARG   B C   1 
ATOM   1492 O  O   . ARG   B 2 161 ? -26.827 -12.353 -6.531  1.00 72.85  ? 170 ARG   B O   1 
ATOM   1493 C  CB  . ARG   B 2 161 ? -27.313 -10.622 -9.081  1.00 70.31  ? 170 ARG   B CB  1 
ATOM   1494 C  CG  . ARG   B 2 161 ? -28.726 -10.076 -9.128  1.00 71.90  ? 170 ARG   B CG  1 
ATOM   1495 C  CD  . ARG   B 2 161 ? -29.500 -10.595 -10.319 1.00 74.35  ? 170 ARG   B CD  1 
ATOM   1496 N  NE  . ARG   B 2 161 ? -30.914 -10.222 -10.223 1.00 77.18  ? 170 ARG   B NE  1 
ATOM   1497 C  CZ  . ARG   B 2 161 ? -31.529 -9.373  -11.042 1.00 78.75  ? 170 ARG   B CZ  1 
ATOM   1498 N  NH1 . ARG   B 2 161 ? -30.872 -8.821  -12.053 1.00 78.23  ? 170 ARG   B NH1 1 
ATOM   1499 N  NH2 . ARG   B 2 161 ? -32.806 -9.073  -10.857 1.00 78.68  ? 170 ARG   B NH2 1 
ATOM   1500 N  N   . GLU   B 2 162 ? -27.874 -10.551 -5.669  1.00 73.03  ? 171 GLU   B N   1 
ATOM   1501 C  CA  . GLU   B 2 162 ? -28.390 -11.273 -4.506  1.00 74.41  ? 171 GLU   B CA  1 
ATOM   1502 C  C   . GLU   B 2 162 ? -29.681 -12.044 -4.789  1.00 75.14  ? 171 GLU   B C   1 
ATOM   1503 O  O   . GLU   B 2 162 ? -30.356 -12.478 -3.850  1.00 75.52  ? 171 GLU   B O   1 
ATOM   1504 C  CB  . GLU   B 2 162 ? -28.595 -10.315 -3.322  1.00 77.50  ? 171 GLU   B CB  1 
ATOM   1505 C  CG  . GLU   B 2 162 ? -27.341 -9.569  -2.902  1.00 83.23  ? 171 GLU   B CG  1 
ATOM   1506 C  CD  . GLU   B 2 162 ? -26.299 -10.430 -2.218  1.00 90.82  ? 171 GLU   B CD  1 
ATOM   1507 O  OE1 . GLU   B 2 162 ? -26.360 -10.563 -0.974  1.00 91.89  ? 171 GLU   B OE1 1 
ATOM   1508 O  OE2 . GLU   B 2 162 ? -25.419 -10.971 -2.927  1.00 93.73  ? 171 GLU   B OE2 1 
HETATM 1509 S  S   . DMS   C 3 .   ? -18.491 11.010  -0.118  1.00 86.10  ? 201 DMS   B S   1 
HETATM 1510 O  O   . DMS   C 3 .   ? -19.245 9.797   -0.449  1.00 86.19  ? 201 DMS   B O   1 
HETATM 1511 C  C1  . DMS   C 3 .   ? -19.568 12.322  -0.583  1.00 86.12  ? 201 DMS   B C1  1 
HETATM 1512 C  C2  . DMS   C 3 .   ? -17.314 11.219  -1.431  1.00 86.01  ? 201 DMS   B C2  1 
HETATM 1513 N  N1  . A1BGR D 4 .   ? -8.296  5.515   -10.305 1.00 78.81  ? 202 A1BGR B N1  1 
HETATM 1514 N  N3  . A1BGR D 4 .   ? -5.734  5.752   -19.816 1.00 78.39  ? 202 A1BGR B N3  1 
HETATM 1515 C  C4  . A1BGR D 4 .   ? -7.936  4.603   -15.711 1.00 74.69  ? 202 A1BGR B C4  1 
HETATM 1516 C  C5  . A1BGR D 4 .   ? -9.022  4.042   -16.369 1.00 73.83  ? 202 A1BGR B C5  1 
HETATM 1517 C  C6  . A1BGR D 4 .   ? -9.003  3.970   -17.749 1.00 73.25  ? 202 A1BGR B C6  1 
HETATM 1518 C  C7  . A1BGR D 4 .   ? -7.903  4.358   -18.473 1.00 74.23  ? 202 A1BGR B C7  1 
HETATM 1519 C  C8  . A1BGR D 4 .   ? -6.794  4.877   -17.820 1.00 75.43  ? 202 A1BGR B C8  1 
HETATM 1520 C  C10 . A1BGR D 4 .   ? -4.661  6.147   -20.779 1.00 79.45  ? 202 A1BGR B C10 1 
HETATM 1521 C  C13 . A1BGR D 4 .   ? -4.008  4.865   -21.309 1.00 80.36  ? 202 A1BGR B C13 1 
HETATM 1522 C  C15 . A1BGR D 4 .   ? -8.322  3.362   -10.869 1.00 78.35  ? 202 A1BGR B C15 1 
HETATM 1523 C  C1  . A1BGR D 4 .   ? -8.319  6.798   -9.620  1.00 78.72  ? 202 A1BGR B C1  1 
HETATM 1524 O  O1  . A1BGR D 4 .   ? -8.163  5.411   -11.719 1.00 78.47  ? 202 A1BGR B O1  1 
HETATM 1525 C  C2  . A1BGR D 4 .   ? -8.187  4.067   -12.018 1.00 77.99  ? 202 A1BGR B C2  1 
HETATM 1526 C  C3  . A1BGR D 4 .   ? -8.055  3.653   -13.423 1.00 77.03  ? 202 A1BGR B C3  1 
HETATM 1527 O  O2  . A1BGR D 4 .   ? -8.059  2.463   -13.727 1.00 77.10  ? 202 A1BGR B O2  1 
HETATM 1528 N  N2  . A1BGR D 4 .   ? -7.917  4.678   -14.303 1.00 75.78  ? 202 A1BGR B N2  1 
HETATM 1529 CL CL1 . A1BGR D 4 .   ? -10.390 3.313   -18.573 1.00 71.81  ? 202 A1BGR B CL1 1 
HETATM 1530 C  C9  . A1BGR D 4 .   ? -5.563  5.310   -18.566 1.00 77.13  ? 202 A1BGR B C9  1 
HETATM 1531 O  O3  . A1BGR D 4 .   ? -4.464  5.274   -18.016 1.00 77.43  ? 202 A1BGR B O3  1 
HETATM 1532 C  C11 . A1BGR D 4 .   ? -5.291  6.910   -21.947 1.00 79.43  ? 202 A1BGR B C11 1 
HETATM 1533 C  C12 . A1BGR D 4 .   ? -3.600  7.032   -20.120 1.00 79.48  ? 202 A1BGR B C12 1 
HETATM 1534 O  O4  . A1BGR D 4 .   ? -4.898  3.997   -21.995 1.00 80.96  ? 202 A1BGR B O4  1 
HETATM 1535 C  C14 . A1BGR D 4 .   ? -6.814  4.996   -16.435 1.00 74.99  ? 202 A1BGR B C14 1 
HETATM 1536 C  C16 . A1BGR D 4 .   ? -8.375  4.266   -9.803  1.00 78.79  ? 202 A1BGR B C16 1 
HETATM 1537 O  O5  . A1BGR D 4 .   ? -8.499  3.988   -8.562  1.00 78.97  ? 202 A1BGR B O5  1 
HETATM 1538 O  O   . HOH   E 5 .   ? -23.471 8.390   -27.584 1.00 51.86  ? 101 HOH   A O   1 
HETATM 1539 O  O   . HOH   E 5 .   ? -2.518  -12.018 -6.737  1.00 48.13  ? 102 HOH   A O   1 
HETATM 1540 O  O   . HOH   E 5 .   ? -25.970 0.593   -29.344 1.00 72.70  ? 103 HOH   A O   1 
HETATM 1541 O  O   . HOH   E 5 .   ? -1.875  -3.557  -5.887  1.00 51.50  ? 104 HOH   A O   1 
HETATM 1542 O  O   . HOH   E 5 .   ? -27.525 -7.005  -28.364 1.00 60.45  ? 105 HOH   A O   1 
HETATM 1543 O  O   . HOH   E 5 .   ? -30.234 -0.172  -23.455 1.00 69.15  ? 106 HOH   A O   1 
HETATM 1544 O  O   . HOH   E 5 .   ? -7.953  -1.980  7.032   1.00 61.62  ? 107 HOH   A O   1 
HETATM 1545 O  O   . HOH   E 5 .   ? -4.072  -10.491 -5.209  1.00 54.65  ? 108 HOH   A O   1 
HETATM 1546 O  O   . HOH   E 5 .   ? -3.731  -1.053  0.097   1.00 64.41  ? 109 HOH   A O   1 
HETATM 1547 O  O   . HOH   E 5 .   ? -8.603  1.600   1.280   1.00 64.63  ? 110 HOH   A O   1 
HETATM 1548 O  O   . HOH   E 5 .   ? -6.636  -10.005 -2.799  1.00 56.18  ? 111 HOH   A O   1 
HETATM 1549 O  O   . HOH   E 5 .   ? -5.121  -15.988 -24.912 1.00 55.22  ? 112 HOH   A O   1 
HETATM 1550 O  O   . HOH   F 5 .   ? -25.393 -8.738  -16.765 1.00 38.34  ? 301 HOH   B O   1 
HETATM 1551 O  O   . HOH   F 5 .   ? -18.642 -12.635 -25.677 1.00 57.02  ? 302 HOH   B O   1 
HETATM 1552 O  O   . HOH   F 5 .   ? -21.315 -12.992 -13.019 1.00 65.35  ? 303 HOH   B O   1 
HETATM 1553 O  O   . HOH   F 5 .   ? -15.209 -5.255  1.475   1.00 45.58  ? 304 HOH   B O   1 
HETATM 1554 O  O   . HOH   F 5 .   ? -16.869 12.086  -5.351  1.00 60.24  ? 305 HOH   B O   1 
HETATM 1555 O  O   . HOH   F 5 .   ? -24.073 -7.218  -4.614  1.00 61.80  ? 306 HOH   B O   1 
HETATM 1556 O  O   . HOH   F 5 .   ? -33.642 1.199   -15.674 1.00 45.53  ? 307 HOH   B O   1 
HETATM 1557 O  O   . HOH   F 5 .   ? -21.860 6.578   -0.153  0.50 38.27  ? 308 HOH   B O   1 
HETATM 1558 O  O   . HOH   F 5 .   ? -6.374  -0.803  -10.509 1.00 54.53  ? 309 HOH   B O   1 
HETATM 1559 O  O   . HOH   F 5 .   ? -17.373 -11.264 -16.227 1.00 45.59  ? 310 HOH   B O   1 
HETATM 1560 O  O   . HOH   F 5 .   ? -11.561 1.203   -5.433  1.00 53.01  ? 311 HOH   B O   1 
HETATM 1561 O  O   . HOH   F 5 .   ? -16.100 -7.898  -8.305  1.00 65.33  ? 312 HOH   B O   1 
HETATM 1562 O  O   . HOH   F 5 .   ? -35.579 -6.085  -10.695 1.00 58.02  ? 313 HOH   B O   1 
HETATM 1563 O  O   . HOH   F 5 .   ? -14.111 11.252  -9.507  1.00 59.84  ? 314 HOH   B O   1 
HETATM 1564 O  O   . HOH   F 5 .   ? -9.017  1.353   -7.846  1.00 64.99  ? 315 HOH   B O   1 
HETATM 1565 O  O   . HOH   F 5 .   ? -12.256 -4.112  -9.969  1.00 49.54  ? 316 HOH   B O   1 
HETATM 1566 O  O   . HOH   F 5 .   ? -20.942 13.465  -34.256 1.00 60.25  ? 317 HOH   B O   1 
HETATM 1567 O  O   . HOH   F 5 .   ? -15.943 20.132  -14.119 1.00 53.76  ? 318 HOH   B O   1 
HETATM 1568 O  O   . HOH   F 5 .   ? -17.781 14.577  -22.043 1.00 45.91  ? 319 HOH   B O   1 
HETATM 1569 O  O   . HOH   F 5 .   ? -27.241 -7.090  -18.667 1.00 48.21  ? 320 HOH   B O   1 
HETATM 1570 O  O   . HOH   F 5 .   ? -12.509 -2.838  -14.538 1.00 39.71  ? 321 HOH   B O   1 
HETATM 1571 O  O   . HOH   F 5 .   ? -26.822 -7.472  -5.587  1.00 53.63  ? 322 HOH   B O   1 
HETATM 1572 O  O   . HOH   F 5 .   ? -19.061 -6.640  -0.802  1.00 56.86  ? 323 HOH   B O   1 
HETATM 1573 O  O   . HOH   F 5 .   ? -22.128 14.550  -6.210  1.00 53.05  ? 324 HOH   B O   1 
HETATM 1574 O  O   . HOH   F 5 .   ? -31.961 6.577   -4.626  1.00 66.66  ? 325 HOH   B O   1 
HETATM 1575 O  O   . HOH   F 5 .   ? -30.566 4.275   -2.825  1.00 52.64  ? 326 HOH   B O   1 
HETATM 1576 O  O   . HOH   F 5 .   ? -10.842 7.028   -13.927 1.00 61.14  ? 327 HOH   B O   1 
HETATM 1577 O  O   . HOH   F 5 .   ? -29.579 -2.550  -19.562 1.00 56.48  ? 328 HOH   B O   1 
HETATM 1578 O  O   . HOH   F 5 .   ? -26.002 -5.520  -4.165  1.00 48.07  ? 329 HOH   B O   1 
HETATM 1579 O  O   . HOH   F 5 .   ? -8.607  -11.632 -7.066  1.00 55.86  ? 330 HOH   B O   1 
HETATM 1580 O  O   . HOH   F 5 .   ? -34.473 4.529   -9.751  1.00 66.39  ? 331 HOH   B O   1 
HETATM 1581 O  O   . HOH   F 5 .   ? -29.930 -5.879  -1.300  1.00 50.23  ? 332 HOH   B O   1 
HETATM 1582 O  O   . HOH   F 5 .   ? -7.479  -7.282  1.278   1.00 73.08  ? 333 HOH   B O   1 
HETATM 1583 O  O   . HOH   F 5 .   ? -2.501  -8.851  -2.852  1.00 60.74  ? 334 HOH   B O   1 
HETATM 1584 O  O   . HOH   F 5 .   ? -14.249 -13.140 -16.424 1.00 51.34  ? 335 HOH   B O   1 
HETATM 1585 O  O   . HOH   F 5 .   ? -10.165 11.633  -18.787 1.00 44.60  ? 336 HOH   B O   1 
HETATM 1586 O  O   . HOH   F 5 .   ? -15.057 -9.856  -11.679 1.00 62.76  ? 337 HOH   B O   1 
HETATM 1587 O  O   . HOH   F 5 .   ? -20.242 1.688   -32.770 1.00 61.72  ? 338 HOH   B O   1 
HETATM 1588 O  O   . HOH   F 5 .   ? -19.809 5.218   -32.984 1.00 73.62  ? 339 HOH   B O   1 
HETATM 1589 O  O   . HOH   F 5 .   ? -15.778 -15.201 -16.047 1.00 51.50  ? 340 HOH   B O   1 
HETATM 1590 O  O   . HOH   F 5 .   ? -14.541 -7.335  -0.965  1.00 70.26  ? 341 HOH   B O   1 
HETATM 1591 O  O   . HOH   F 5 .   ? -23.802 -15.979 -17.999 1.00 59.17  ? 342 HOH   B O   1 
HETATM 1592 O  O   . HOH   F 5 .   ? -10.597 -19.237 -10.883 1.00 61.29  ? 343 HOH   B O   1 
HETATM 1593 O  O   . HOH   F 5 .   ? -15.677 16.201  -20.857 1.00 65.12  ? 344 HOH   B O   1 
HETATM 1594 O  O   . HOH   F 5 .   ? -19.774 24.240  -16.783 1.00 60.85  ? 345 HOH   B O   1 
HETATM 1595 O  O   . HOH   F 5 .   ? -4.592  2.042   -13.733 1.00 69.66  ? 346 HOH   B O   1 
HETATM 1596 O  O   . HOH   F 5 .   ? -10.830 -7.721  2.151   1.00 71.61  ? 347 HOH   B O   1 
HETATM 1597 O  O   . HOH   F 5 .   ? -5.999  9.691   -18.254 1.00 60.07  ? 348 HOH   B O   1 
HETATM 1598 O  O   . HOH   F 5 .   ? -0.710  -15.416 -9.561  1.00 65.52  ? 349 HOH   B O   1 
HETATM 1599 O  O   . HOH   F 5 .   ? -10.552 -13.095 -8.275  1.00 58.18  ? 350 HOH   B O   1 
HETATM 1600 O  O   . HOH   F 5 .   ? -20.492 15.503  -23.260 1.00 71.44  ? 351 HOH   B O   1 
HETATM 1601 O  O   . HOH   F 5 .   ? -18.805 -12.901 -13.442 1.00 54.43  ? 352 HOH   B O   1 
HETATM 1602 O  O   . HOH   F 5 .   ? -17.421 26.974  -14.168 1.00 57.69  ? 353 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . ASP   A 7   ? 1.2442 0.4687 1.0067 0.3003 0.2382  -0.1292 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 1.2149 0.5328 0.9614 0.3287 0.2454  -0.1166 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 1.1735 0.5318 0.9383 0.3203 0.2530  -0.0637 50  ASP   A C   
4    O  O   . ASP   A 7   ? 1.1966 0.5016 0.9729 0.3227 0.2605  -0.0324 50  ASP   A O   
5    C  CB  . ASP   A 7   ? 1.2578 0.5640 0.9832 0.3859 0.2546  -0.1313 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 1.3319 0.7198 1.0347 0.4068 0.2570  -0.1593 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 1.3687 0.7308 1.0476 0.4396 0.2589  -0.1988 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 1.3406 0.8159 1.0481 0.3910 0.2584  -0.1414 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 1.1176 0.5650 0.8815 0.3106 0.2511  -0.0536 51  MET   A N   
10   C  CA  . MET   A 8   ? 1.0725 0.5604 0.8486 0.3045 0.2550  -0.0107 51  MET   A CA  
11   C  C   . MET   A 8   ? 1.0360 0.5659 0.8060 0.3453 0.2610  0.0048  51  MET   A C   
12   O  O   . MET   A 8   ? 1.0292 0.5918 0.7907 0.3707 0.2631  -0.0177 51  MET   A O   
13   C  CB  . MET   A 8   ? 1.0531 0.6038 0.8341 0.2703 0.2471  -0.0077 51  MET   A CB  
14   C  CG  . MET   A 8   ? 1.0732 0.5957 0.8679 0.2316 0.2382  -0.0213 51  MET   A CG  
15   S  SD  . MET   A 8   ? 1.0517 0.6486 0.8516 0.2005 0.2280  -0.0126 51  MET   A SD  
16   C  CE  . MET   A 8   ? 1.0817 0.6417 0.9184 0.1601 0.2227  -0.0098 51  MET   A CE  
17   N  N   . TYR   A 9   ? 1.0070 0.5393 0.7820 0.3537 0.2637  0.0423  52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.9764 0.5530 0.7497 0.3921 0.2638  0.0563  52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.9435 0.5608 0.7187 0.3847 0.2592  0.0890  52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.9488 0.5426 0.7235 0.3585 0.2611  0.1073  52  TYR   A O   
21   C  CB  . TYR   A 9   ? 0.9951 0.5132 0.7604 0.4371 0.2691  0.0605  52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 1.0345 0.4744 0.7925 0.4369 0.2751  0.0945  52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 1.0695 0.4240 0.8302 0.4119 0.2812  0.0899  52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 1.0423 0.4961 0.7905 0.4598 0.2746  0.1320  52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 1.1068 0.3921 0.8651 0.4060 0.2915  0.1268  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 1.0794 0.4636 0.8149 0.4608 0.2846  0.1688  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 1.1228 0.4220 0.8653 0.4326 0.2955  0.1686  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 1.1849 0.4148 0.9190 0.4298 0.3101  0.2099  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.9043 0.5862 0.6839 0.4083 0.2525  0.0940  53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.8883 0.6084 0.6657 0.4040 0.2438  0.1175  53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.8937 0.6099 0.6601 0.4474 0.2390  0.1400  53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.9030 0.6214 0.6735 0.4850 0.2383  0.1333  53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.8548 0.6554 0.6472 0.3838 0.2343  0.1052  53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.8449 0.7070 0.6582 0.4076 0.2315  0.0892  53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.8557 0.6547 0.6488 0.3438 0.2378  0.0913  53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.8224 0.7624 0.6569 0.3848 0.2230  0.0836  53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.8960 0.6074 0.6447 0.4465 0.2355  0.1667  54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.9109 0.6224 0.6381 0.4890 0.2281  0.1910  54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.8967 0.6682 0.6169 0.4828 0.2113  0.1949  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.8855 0.6527 0.5994 0.4512 0.2154  0.1994  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 0.9805 0.6087 0.6790 0.4980 0.2447  0.2252  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 1.0833 0.6335 0.7815 0.5147 0.2584  0.2270  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 1.2190 0.6822 0.8935 0.5152 0.2777  0.2659  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 1.2459 0.7154 0.9085 0.4952 0.2849  0.2893  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 1.2727 0.6597 0.9414 0.5355 0.2876  0.2737  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.8899 0.7156 0.6113 0.5147 0.1910  0.1918  55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.8879 0.7648 0.6011 0.5098 0.1705  0.1898  55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.9278 0.7643 0.5927 0.5203 0.1761  0.2194  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.9504 0.7405 0.5847 0.5534 0.1862  0.2474  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.8722 0.8198 0.6023 0.5413 0.1434  0.1767  55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.8711 0.8823 0.6199 0.5148 0.1206  0.1557  55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.8535 0.9458 0.6385 0.5352 0.0931  0.1367  55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.8486 0.9896 0.6492 0.5083 0.0684  0.1173  55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.8748 1.0244 0.6425 0.5250 0.0431  0.1168  55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 0.9151 1.0344 0.6295 0.5710 0.0409  0.1390  55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.8430 1.0257 0.6257 0.4967 0.0203  0.0946  55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.9257 0.7771 0.5822 0.4935 0.1723  0.2152  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.9578 0.7818 0.5690 0.5026 0.1810  0.2410  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.9561 0.8243 0.5380 0.5218 0.1545  0.2329  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.9859 0.8364 0.5204 0.5411 0.1614  0.2548  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.9656 0.7625 0.5859 0.4616 0.2026  0.2448  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.9198 0.8444 0.5296 0.5159 0.1255  0.2014  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.9104 0.8744 0.4961 0.5320 0.0946  0.1865  57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.8772 0.8909 0.5065 0.5005 0.0689  0.1495  57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.8528 0.8766 0.5311 0.4674 0.0772  0.1382  57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.8740 0.9179 0.4839 0.5115 0.0368  0.1302  58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.8592 0.9432 0.5100 0.4793 0.0094  0.0949  58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.8891 0.9388 0.5239 0.4495 0.0159  0.0882  58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.9185 0.9319 0.5009 0.4665 0.0297  0.1040  58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.8694 1.0011 0.5099 0.5060 -0.0349 0.0711  58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.9423 1.1269 0.6111 0.5356 -0.0515 0.0699  58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.9580 1.1305 0.6391 0.5468 -0.0255 0.0925  58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.9646 1.2028 0.6422 0.5510 -0.0927 0.0446  58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.8743 0.9372 0.5537 0.4074 0.0065  0.0663  59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.8927 0.9207 0.5576 0.3826 0.0086  0.0583  59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.9124 0.9500 0.5587 0.3896 -0.0302 0.0278  59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.8845 0.9500 0.5752 0.3636 -0.0558 0.0025  59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.8679 0.8909 0.5809 0.3362 0.0236  0.0573  59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.8718 0.8838 0.5951 0.3344 0.0579  0.0817  59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.8869 0.8699 0.5810 0.3169 0.0237  0.0511  59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.8573 0.8799 0.6259 0.2975 0.0698  0.0791  59  ILE   A CD1 
82   N  N   A THR   A 17  ? 0.9499 0.9665 0.5306 0.4258 -0.0344 0.0296  60  THR   A N   
83   N  N   B THR   A 17  ? 0.9529 0.9688 0.5337 0.4253 -0.0342 0.0296  60  THR   A N   
84   C  CA  A THR   A 17  ? 0.9749 0.9931 0.5218 0.4409 -0.0724 -0.0032 60  THR   A CA  
85   C  CA  B THR   A 17  ? 0.9800 0.9998 0.5274 0.4416 -0.0728 -0.0031 60  THR   A CA  
86   C  C   A THR   A 17  ? 1.0339 1.0073 0.5176 0.4599 -0.0592 0.0003  60  THR   A C   
87   C  C   B THR   A 17  ? 1.0380 1.0137 0.5189 0.4632 -0.0607 0.0001  60  THR   A C   
88   O  O   A THR   A 17  ? 1.0491 1.0043 0.5065 0.4748 -0.0226 0.0332  60  THR   A O   
89   O  O   B THR   A 17  ? 1.0555 1.0136 0.5082 0.4799 -0.0245 0.0332  60  THR   A O   
90   C  CB  A THR   A 17  ? 0.9761 1.0336 0.4922 0.4864 -0.1004 -0.0104 60  THR   A CB  
91   C  CB  B THR   A 17  ? 0.9807 1.0456 0.5100 0.4824 -0.1002 -0.0093 60  THR   A CB  
92   O  OG1 A THR   A 17  ? 1.0040 1.0454 0.4614 0.5292 -0.0724 0.0253  60  THR   A OG1 
93   O  OG1 B THR   A 17  ? 0.9500 1.0637 0.5504 0.4626 -0.1100 -0.0138 60  THR   A OG1 
94   C  CG2 A THR   A 17  ? 0.9387 1.0543 0.5197 0.4759 -0.1199 -0.0192 60  THR   A CG2 
95   C  CG2 B THR   A 17  ? 0.9927 1.0674 0.4834 0.5035 -0.1462 -0.0483 60  THR   A CG2 
96   N  N   . TRP   A 18  ? 1.0650 1.0230 0.5248 0.4619 -0.0898 -0.0349 61  TRP   A N   
97   C  CA  . TRP   A 18  ? 1.1434 1.0652 0.5374 0.4897 -0.0807 -0.0373 61  TRP   A CA  
98   C  C   . TRP   A 18  ? 1.2074 1.1503 0.5289 0.5475 -0.0944 -0.0393 61  TRP   A C   
99   O  O   . TRP   A 18  ? 1.1936 1.1684 0.5171 0.5579 -0.1334 -0.0638 61  TRP   A O   
100  C  CB  . TRP   A 18  ? 1.1526 1.0400 0.5498 0.4693 -0.1097 -0.0780 61  TRP   A CB  
101  C  CG  . TRP   A 18  ? 1.1971 1.0485 0.5239 0.5046 -0.1075 -0.0907 61  TRP   A CG  
102  C  CD1 . TRP   A 18  ? 1.2270 1.0776 0.4851 0.5486 -0.1350 -0.1205 61  TRP   A CD1 
103  C  CD2 . TRP   A 18  ? 1.2147 1.0265 0.5356 0.4988 -0.0818 -0.0817 61  TRP   A CD2 
104  N  NE1 . TRP   A 18  ? 1.2595 1.0732 0.4666 0.5735 -0.1227 -0.1281 61  TRP   A NE1 
105  C  CE2 . TRP   A 18  ? 1.2559 1.0466 0.5041 0.5435 -0.0908 -0.1046 61  TRP   A CE2 
106  C  CE3 . TRP   A 18  ? 1.2093 1.0060 0.5762 0.4650 -0.0525 -0.0565 61  TRP   A CE3 
107  C  CZ2 . TRP   A 18  ? 1.2831 1.0408 0.5097 0.5557 -0.0700 -0.1024 61  TRP   A CZ2 
108  C  CZ3 . TRP   A 18  ? 1.2373 1.0016 0.5828 0.4758 -0.0358 -0.0546 61  TRP   A CZ3 
109  C  CH2 . TRP   A 18  ? 1.2663 1.0133 0.5452 0.5213 -0.0431 -0.0761 61  TRP   A CH2 
110  N  N   . GLU   A 19  ? 1.2680 1.1989 0.5279 0.5854 -0.0618 -0.0113 62  GLU   A N   
111  C  CA  . GLU   A 19  ? 1.3275 1.2755 0.5080 0.6436 -0.0693 -0.0070 62  GLU   A CA  
112  C  C   . GLU   A 19  ? 1.4006 1.3280 0.5093 0.6767 -0.0773 -0.0326 62  GLU   A C   
113  O  O   . GLU   A 19  ? 1.4106 1.3158 0.5082 0.6770 -0.0421 -0.0165 62  GLU   A O   
114  C  CB  . GLU   A 19  ? 1.3659 1.3181 0.5245 0.6666 -0.0222 0.0503  62  GLU   A CB  
115  C  CG  . GLU   A 19  ? 1.4275 1.3975 0.6398 0.6500 -0.0187 0.0731  62  GLU   A CG  
116  C  CD  . GLU   A 19  ? 1.5121 1.5194 0.7169 0.6747 -0.0623 0.0539  62  GLU   A CD  
117  O  OE1 . GLU   A 19  ? 1.5758 1.5940 0.7040 0.7284 -0.0733 0.0585  62  GLU   A OE1 
118  O  OE2 . GLU   A 19  ? 1.4811 1.5120 0.7565 0.6424 -0.0848 0.0355  62  GLU   A OE2 
119  N  N   . LYS   A 20  ? 1.4467 1.3847 0.5064 0.7073 -0.1247 -0.0750 63  LYS   A N   
120  C  CA  . LYS   A 20  ? 1.5203 1.4368 0.5000 0.7470 -0.1359 -0.1061 63  LYS   A CA  
121  C  C   . LYS   A 20  ? 1.5795 1.5069 0.4797 0.8013 -0.0913 -0.0624 63  LYS   A C   
122  O  O   . LYS   A 20  ? 1.5855 1.5394 0.4652 0.8244 -0.0809 -0.0279 63  LYS   A O   
123  C  CB  . LYS   A 20  ? 1.5581 1.4860 0.4985 0.7704 -0.2013 -0.1648 63  LYS   A CB  
124  C  CG  . LYS   A 20  ? 1.5805 1.5220 0.6064 0.7194 -0.2490 -0.1998 63  LYS   A CG  
125  C  CD  . LYS   A 20  ? 1.6447 1.5947 0.6311 0.7415 -0.3164 -0.2651 63  LYS   A CD  
126  C  CE  . LYS   A 20  ? 1.6587 1.6581 0.7147 0.7134 -0.3638 -0.2879 63  LYS   A CE  
127  N  NZ  . LYS   A 20  ? 1.7034 1.7362 0.6963 0.7601 -0.4234 -0.3345 63  LYS   A NZ  
128  N  N   . ASP   A 21  ? 1.6216 1.5295 0.4785 0.8232 -0.0636 -0.0615 64  ASP   A N   
129  C  CA  . ASP   A 21  ? 1.6634 1.5871 0.4486 0.8727 -0.0147 -0.0173 64  ASP   A CA  
130  C  C   . ASP   A 21  ? 1.6457 1.5798 0.4828 0.8471 0.0399  0.0500  64  ASP   A C   
131  O  O   . ASP   A 21  ? 1.6562 1.6071 0.4562 0.8750 0.0620  0.0925  64  ASP   A O   
132  C  CB  . ASP   A 21  ? 1.7352 1.6813 0.4184 0.9372 -0.0371 -0.0252 64  ASP   A CB  
133  C  CG  . ASP   A 21  ? 1.8507 1.7856 0.4771 0.9649 -0.0953 -0.0977 64  ASP   A CG  
134  O  OD1 . ASP   A 21  ? 1.8834 1.7868 0.5167 0.9551 -0.0998 -0.1329 64  ASP   A OD1 
135  O  OD2 . ASP   A 21  ? 1.8829 1.8385 0.4580 0.9978 -0.1387 -0.1212 64  ASP   A OD2 
136  N  N   . ALA   A 22  ? 1.6130 1.5325 0.5343 0.7941 0.0589  0.0583  65  ALA   A N   
137  C  CA  . ALA   A 22  ? 1.5847 1.5091 0.5615 0.7645 0.1084  0.1136  65  ALA   A CA  
138  C  C   . ALA   A 22  ? 1.5776 1.5100 0.5375 0.7800 0.1590  0.1396  65  ALA   A C   
139  O  O   . ALA   A 22  ? 1.5866 1.5176 0.5016 0.8093 0.1522  0.1099  65  ALA   A O   
140  C  CB  . ALA   A 22  ? 1.5549 1.4654 0.6287 0.7014 0.0970  0.1037  65  ALA   A CB  
141  N  N   . GLU   A 23  ? 1.5575 1.5000 0.5541 0.7622 0.2092  0.1932  66  GLU   A N   
142  C  CA  . GLU   A 23  ? 1.5516 1.5142 0.5498 0.7706 0.2589  0.2203  66  GLU   A CA  
143  C  C   . GLU   A 23  ? 1.5157 1.4726 0.5684 0.7421 0.2486  0.1882  66  GLU   A C   
144  O  O   . GLU   A 23  ? 1.4916 1.4357 0.6196 0.6919 0.2401  0.1863  66  GLU   A O   
145  C  CB  . GLU   A 23  ? 1.5857 1.5571 0.6310 0.7444 0.3091  0.2813  66  GLU   A CB  
146  C  CG  . GLU   A 23  ? 1.6611 1.6632 0.7365 0.7390 0.3602  0.3095  66  GLU   A CG  
147  C  CD  . GLU   A 23  ? 1.7538 1.7630 0.8789 0.7097 0.4095  0.3685  66  GLU   A CD  
148  O  OE1 . GLU   A 23  ? 1.7777 1.7590 0.9063 0.6975 0.4062  0.3907  66  GLU   A OE1 
149  O  OE2 . GLU   A 23  ? 1.7627 1.8057 0.9266 0.6990 0.4508  0.3917  66  GLU   A OE2 
150  N  N   . VAL   A 24  ? 1.5117 1.4757 0.5204 0.7786 0.2483  0.1623  67  VAL   A N   
151  C  CA  . VAL   A 24  ? 1.4885 1.4425 0.5367 0.7632 0.2382  0.1325  67  VAL   A CA  
152  C  C   . VAL   A 24  ? 1.4452 1.4412 0.5281 0.7648 0.2912  0.1674  67  VAL   A C   
153  O  O   . VAL   A 24  ? 1.4552 1.4836 0.4864 0.8112 0.3233  0.1813  67  VAL   A O   
154  C  CB  . VAL   A 24  ? 1.5290 1.4560 0.5140 0.8022 0.1995  0.0755  67  VAL   A CB  
155  C  CG1 . VAL   A 24  ? 1.5248 1.4183 0.5618 0.7717 0.1743  0.0437  67  VAL   A CG1 
156  C  CG2 . VAL   A 24  ? 1.5643 1.4686 0.4931 0.8184 0.1534  0.0439  67  VAL   A CG2 
157  N  N   . THR   A 25  ? 1.3910 1.3924 0.5617 0.7157 0.3004  0.1809  68  THR   A N   
158  C  CA  . THR   A 25  ? 1.3435 1.3930 0.5663 0.7083 0.3457  0.2119  68  THR   A CA  
159  C  C   . THR   A 25  ? 1.3043 1.3490 0.6075 0.6659 0.3307  0.1988  68  THR   A C   
160  O  O   . THR   A 25  ? 1.3157 1.3162 0.6291 0.6421 0.2903  0.1707  68  THR   A O   
161  C  CB  . THR   A 25  ? 1.3391 1.4173 0.5831 0.6929 0.3909  0.2678  68  THR   A CB  
162  O  OG1 . THR   A 25  ? 1.3185 1.4544 0.6061 0.6934 0.4379  0.2969  68  THR   A OG1 
163  C  CG2 . THR   A 25  ? 1.3296 1.3807 0.6331 0.6372 0.3792  0.2805  68  THR   A CG2 
164  N  N   . GLY   A 26  ? 1.2542 1.3483 0.6121 0.6590 0.3631  0.2195  69  GLY   A N   
165  C  CA  . GLY   A 26  ? 1.2223 1.3200 0.6504 0.6257 0.3493  0.2095  69  GLY   A CA  
166  C  C   . GLY   A 26  ? 1.2225 1.3133 0.6335 0.6588 0.3299  0.1755  69  GLY   A C   
167  O  O   . GLY   A 26  ? 1.2626 1.3126 0.6062 0.6939 0.3054  0.1435  69  GLY   A O   
168  N  N   . ASN   A 27  ? 1.1739 1.3022 0.6466 0.6488 0.3377  0.1802  70  ASN   A N   
169  C  CA  . ASN   A 27  ? 1.1682 1.2867 0.6303 0.6816 0.3185  0.1510  70  ASN   A CA  
170  C  C   . ASN   A 27  ? 1.1544 1.2123 0.6346 0.6491 0.2743  0.1297  70  ASN   A C   
171  O  O   . ASN   A 27  ? 1.1557 1.1842 0.6512 0.6047 0.2604  0.1351  70  ASN   A O   
172  C  CB  . ASN   A 27  ? 1.1476 1.3510 0.6596 0.7030 0.3530  0.1679  70  ASN   A CB  
173  C  CG  . ASN   A 27  ? 1.1459 1.3972 0.7523 0.6543 0.3609  0.1906  70  ASN   A CG  
174  O  OD1 . ASN   A 27  ? 1.1459 1.3884 0.7832 0.6049 0.3626  0.2085  70  ASN   A OD1 
175  N  ND2 . ASN   A 27  ? 1.1262 1.4300 0.7797 0.6706 0.3634  0.1876  70  ASN   A ND2 
176  N  N   . SER   A 28  ? 1.1427 1.1778 0.6143 0.6757 0.2537  0.1064  71  SER   A N   
177  C  CA  . SER   A 28  ? 1.1445 1.1179 0.6236 0.6535 0.2154  0.0901  71  SER   A CA  
178  C  C   . SER   A 28  ? 1.1038 1.1149 0.6301 0.6644 0.2165  0.0960  71  SER   A C   
179  O  O   . SER   A 28  ? 1.1189 1.0979 0.6191 0.7031 0.1999  0.0763  71  SER   A O   
180  C  CB  . SER   A 28  ? 1.2077 1.0973 0.6182 0.6813 0.1834  0.0538  71  SER   A CB  
181  O  OG  . SER   A 28  ? 1.2561 1.1305 0.6109 0.6993 0.1844  0.0403  71  SER   A OG  
182  N  N   . PRO   A 29  ? 1.0494 1.1281 0.6453 0.6332 0.2337  0.1214  72  PRO   A N   
183  C  CA  . PRO   A 29  ? 1.0115 1.1381 0.6550 0.6466 0.2313  0.1252  72  PRO   A CA  
184  C  C   . PRO   A 29  ? 1.0252 1.0921 0.6645 0.6315 0.1936  0.1162  72  PRO   A C   
185  O  O   . PRO   A 29  ? 1.0443 1.0581 0.6719 0.5909 0.1774  0.1162  72  PRO   A O   
186  C  CB  . PRO   A 29  ? 0.9662 1.1806 0.6863 0.6104 0.2583  0.1518  72  PRO   A CB  
187  C  CG  . PRO   A 29  ? 0.9852 1.1619 0.6975 0.5626 0.2583  0.1600  72  PRO   A CG  
188  C  CD  . PRO   A 29  ? 1.0167 1.1292 0.6521 0.5858 0.2531  0.1454  72  PRO   A CD  
189  N  N   . ARG   A 30  ? 1.0133 1.0894 0.6592 0.6681 0.1811  0.1103  73  ARG   A N   
190  C  CA  . ARG   A 30  ? 1.0357 1.0584 0.6745 0.6601 0.1479  0.1082  73  ARG   A CA  
191  C  C   . ARG   A 30  ? 0.9683 1.0765 0.6760 0.6476 0.1492  0.1237  73  ARG   A C   
192  O  O   . ARG   A 30  ? 0.9338 1.1202 0.6788 0.6812 0.1624  0.1257  73  ARG   A O   
193  C  CB  . ARG   A 30  ? 1.1092 1.0643 0.6959 0.7145 0.1283  0.0899  73  ARG   A CB  
194  C  CG  . ARG   A 30  ? 1.2326 1.0965 0.7528 0.7196 0.1203  0.0686  73  ARG   A CG  
195  C  CD  . ARG   A 30  ? 1.3559 1.1258 0.8217 0.7622 0.0947  0.0477  73  ARG   A CD  
196  N  NE  . ARG   A 30  ? 1.4683 1.1668 0.8766 0.7703 0.0877  0.0207  73  ARG   A NE  
197  C  CZ  . ARG   A 30  ? 1.5588 1.1642 0.9129 0.8060 0.0655  -0.0058 73  ARG   A CZ  
198  N  NH1 . ARG   A 30  ? 1.5886 1.1537 0.9356 0.8393 0.0500  -0.0050 73  ARG   A NH1 
199  N  NH2 . ARG   A 30  ? 1.5774 1.1258 0.8830 0.8096 0.0561  -0.0346 73  ARG   A NH2 
200  N  N   . LEU   A 31  ? 0.9492 1.0533 0.6785 0.5979 0.1378  0.1331  74  LEU   A N   
201  C  CA  . LEU   A 31  ? 0.8883 1.0753 0.6839 0.5794 0.1354  0.1429  74  LEU   A CA  
202  C  C   . LEU   A 31  ? 0.8832 1.0355 0.6645 0.5730 0.1027  0.1446  74  LEU   A C   
203  O  O   . LEU   A 31  ? 0.9176 0.9898 0.6547 0.5492 0.0904  0.1452  74  LEU   A O   
204  C  CB  . LEU   A 31  ? 0.8637 1.0857 0.7000 0.5242 0.1537  0.1512  74  LEU   A CB  
205  C  CG  . LEU   A 31  ? 0.8656 1.1200 0.7131 0.5260 0.1899  0.1570  74  LEU   A CG  
206  C  CD1 . LEU   A 31  ? 0.8551 1.1152 0.7290 0.4723 0.2044  0.1669  74  LEU   A CD1 
207  C  CD2 . LEU   A 31  ? 0.8231 1.1759 0.7225 0.5597 0.2111  0.1620  74  LEU   A CD2 
208  N  N   . ASP   A 32  ? 0.8387 1.0578 0.6596 0.5931 0.0894  0.1469  75  ASP   A N   
209  C  CA  . ASP   A 32  ? 0.8510 1.0470 0.6555 0.5893 0.0576  0.1513  75  ASP   A CA  
210  C  C   . ASP   A 32  ? 0.7983 1.0384 0.6445 0.5329 0.0574  0.1521  75  ASP   A C   
211  O  O   . ASP   A 32  ? 0.7433 1.0771 0.6600 0.5201 0.0676  0.1493  75  ASP   A O   
212  C  CB  . ASP   A 32  ? 0.8768 1.1363 0.7082 0.6385 0.0401  0.1515  75  ASP   A CB  
213  C  CG  . ASP   A 32  ? 1.0211 1.2216 0.8017 0.7012 0.0312  0.1503  75  ASP   A CG  
214  O  OD1 . ASP   A 32  ? 1.0995 1.1968 0.8185 0.7025 0.0346  0.1480  75  ASP   A OD1 
215  O  OD2 . ASP   A 32  ? 1.0425 1.2994 0.8468 0.7497 0.0187  0.1501  75  ASP   A OD2 
216  N  N   . VAL   A 33  ? 0.8107 0.9848 0.6169 0.4985 0.0483  0.1548  76  VAL   A N   
217  C  CA  . VAL   A 33  ? 0.7846 0.9915 0.6228 0.4489 0.0481  0.1512  76  VAL   A CA  
218  C  C   . VAL   A 33  ? 0.8006 0.9847 0.6060 0.4402 0.0204  0.1531  76  VAL   A C   
219  O  O   . VAL   A 33  ? 0.8379 0.9649 0.5880 0.4672 0.0053  0.1630  76  VAL   A O   
220  C  CB  . VAL   A 33  ? 0.7963 0.9642 0.6276 0.4100 0.0723  0.1506  76  VAL   A CB  
221  C  CG1 . VAL   A 33  ? 0.7773 0.9776 0.6394 0.4176 0.1013  0.1514  76  VAL   A CG1 
222  C  CG2 . VAL   A 33  ? 0.8497 0.9200 0.6125 0.4065 0.0685  0.1550  76  VAL   A CG2 
223  N  N   . ALA   A 34  ? 0.7710 0.9959 0.6068 0.4037 0.0145  0.1438  77  ALA   A N   
224  C  CA  . ALA   A 34  ? 0.7864 0.9946 0.5854 0.3946 -0.0091 0.1429  77  ALA   A CA  
225  C  C   . ALA   A 34  ? 0.7832 0.9705 0.5802 0.3471 0.0022  0.1342  77  ALA   A C   
226  O  O   . ALA   A 34  ? 0.7460 0.9718 0.5971 0.3192 0.0151  0.1225  77  ALA   A O   
227  C  CB  . ALA   A 34  ? 0.7471 1.0387 0.5823 0.4099 -0.0382 0.1328  77  ALA   A CB  
228  N  N   . LEU   A 35  ? 0.8157 0.9402 0.5503 0.3394 -0.0006 0.1418  78  LEU   A N   
229  C  CA  . LEU   A 35  ? 0.8101 0.9130 0.5348 0.3021 0.0099  0.1335  78  LEU   A CA  
230  C  C   . LEU   A 35  ? 0.8177 0.9475 0.5234 0.2994 -0.0142 0.1225  78  LEU   A C   
231  O  O   . LEU   A 35  ? 0.8440 0.9529 0.4952 0.3224 -0.0295 0.1358  78  LEU   A O   
232  C  CB  . LEU   A 35  ? 0.8366 0.8609 0.5075 0.2972 0.0252  0.1496  78  LEU   A CB  
233  C  CG  . LEU   A 35  ? 0.8369 0.8405 0.4990 0.2638 0.0401  0.1426  78  LEU   A CG  
234  C  CD1 . LEU   A 35  ? 0.8125 0.8370 0.5266 0.2425 0.0568  0.1293  78  LEU   A CD1 
235  C  CD2 . LEU   A 35  ? 0.8680 0.8070 0.4863 0.2595 0.0531  0.1596  78  LEU   A CD2 
236  N  N   . ASP   A 36  ? 0.7904 0.9635 0.5376 0.2731 -0.0188 0.0981  79  ASP   A N   
237  C  CA  . ASP   A 36  ? 0.7933 0.9932 0.5202 0.2707 -0.0448 0.0801  79  ASP   A CA  
238  C  C   . ASP   A 36  ? 0.8282 0.9764 0.4963 0.2558 -0.0333 0.0795  79  ASP   A C   
239  O  O   . ASP   A 36  ? 0.8465 0.9455 0.5018 0.2444 -0.0062 0.0926  79  ASP   A O   
240  C  CB  . ASP   A 36  ? 0.7739 1.0454 0.5751 0.2503 -0.0612 0.0492  79  ASP   A CB  
241  C  CG  . ASP   A 36  ? 0.8327 1.0920 0.6735 0.2098 -0.0421 0.0315  79  ASP   A CG  
242  O  OD1 . ASP   A 36  ? 0.8739 1.0753 0.6864 0.2003 -0.0157 0.0425  79  ASP   A OD1 
243  O  OD2 . ASP   A 36  ? 0.8329 1.1399 0.7345 0.1875 -0.0551 0.0062  79  ASP   A OD2 
244  N  N   . GLU   A 37  ? 0.8331 0.9981 0.4658 0.2583 -0.0544 0.0631  80  GLU   A N   
245  C  CA  . GLU   A 37  ? 0.8718 0.9990 0.4465 0.2495 -0.0424 0.0610  80  GLU   A CA  
246  C  C   . GLU   A 37  ? 0.8670 0.9792 0.4748 0.2170 -0.0216 0.0401  80  GLU   A C   
247  O  O   . GLU   A 37  ? 0.8952 0.9716 0.4647 0.2110 -0.0017 0.0442  80  GLU   A O   
248  C  CB  . GLU   A 37  ? 0.9068 1.0608 0.4289 0.2665 -0.0718 0.0459  80  GLU   A CB  
249  C  CG  . GLU   A 37  ? 1.0105 1.1278 0.4590 0.2666 -0.0551 0.0511  80  GLU   A CG  
250  C  CD  . GLU   A 37  ? 1.0841 1.2290 0.4728 0.2847 -0.0823 0.0312  80  GLU   A CD  
251  O  OE1 . GLU   A 37  ? 1.0779 1.2422 0.4781 0.2705 -0.0933 -0.0101 80  GLU   A OE1 
252  O  OE2 . GLU   A 37  ? 1.1389 1.2822 0.4654 0.3153 -0.0938 0.0567  80  GLU   A OE2 
253  N  N   . SER   A 38  ? 0.8255 0.9639 0.5061 0.1974 -0.0234 0.0214  81  SER   A N   
254  C  CA  . SER   A 38  ? 0.8137 0.9295 0.5261 0.1697 -0.0035 0.0060  81  SER   A CA  
255  C  C   . SER   A 38  ? 0.8096 0.8921 0.5419 0.1644 0.0282  0.0309  81  SER   A C   
256  O  O   . SER   A 38  ? 0.8063 0.8702 0.5676 0.1456 0.0451  0.0232  81  SER   A O   
257  C  CB  . SER   A 38  ? 0.7997 0.9527 0.5798 0.1474 -0.0196 -0.0245 81  SER   A CB  
258  O  OG  . SER   A 38  ? 0.8433 1.0310 0.6063 0.1523 -0.0547 -0.0536 81  SER   A OG  
259  N  N   . GLY   A 39  ? 0.8085 0.8798 0.5220 0.1829 0.0341  0.0592  82  GLY   A N   
260  C  CA  . GLY   A 39  ? 0.8121 0.8535 0.5382 0.1813 0.0588  0.0786  82  GLY   A CA  
261  C  C   . GLY   A 39  ? 0.7831 0.8502 0.5687 0.1782 0.0648  0.0805  82  GLY   A C   
262  O  O   . GLY   A 39  ? 0.7889 0.8344 0.5851 0.1764 0.0855  0.0923  82  GLY   A O   
263  N  N   . ASP   A 40  ? 0.7502 0.8692 0.5756 0.1789 0.0471  0.0696  83  ASP   A N   
264  C  CA  . ASP   A 40  ? 0.7264 0.8819 0.6150 0.1754 0.0569  0.0742  83  ASP   A CA  
265  C  C   . ASP   A 40  ? 0.7163 0.8935 0.6034 0.2074 0.0534  0.0914  83  ASP   A C   
266  O  O   . ASP   A 40  ? 0.7124 0.9052 0.5758 0.2293 0.0306  0.0916  83  ASP   A O   
267  C  CB  . ASP   A 40  ? 0.7079 0.9165 0.6599 0.1521 0.0430  0.0514  83  ASP   A CB  
268  C  CG  . ASP   A 40  ? 0.7649 0.9452 0.7224 0.1216 0.0452  0.0301  83  ASP   A CG  
269  O  OD1 . ASP   A 40  ? 0.7796 0.9147 0.7306 0.1124 0.0703  0.0390  83  ASP   A OD1 
270  O  OD2 . ASP   A 40  ? 0.7923 0.9952 0.7587 0.1101 0.0198  0.0026  83  ASP   A OD2 
271  N  N   . PHE   A 41  ? 0.7123 0.8877 0.6194 0.2142 0.0760  0.1056  84  PHE   A N   
272  C  CA  . PHE   A 41  ? 0.7165 0.9113 0.6238 0.2481 0.0758  0.1181  84  PHE   A CA  
273  C  C   . PHE   A 41  ? 0.7024 0.9794 0.6832 0.2481 0.0749  0.1138  84  PHE   A C   
274  O  O   . PHE   A 41  ? 0.6794 0.9851 0.7146 0.2176 0.0867  0.1082  84  PHE   A O   
275  C  CB  . PHE   A 41  ? 0.7164 0.8696 0.6010 0.2600 0.1001  0.1323  84  PHE   A CB  
276  C  CG  . PHE   A 41  ? 0.7501 0.8316 0.5689 0.2673 0.0969  0.1377  84  PHE   A CG  
277  C  CD1 . PHE   A 41  ? 0.7692 0.8254 0.5484 0.2949 0.0815  0.1440  84  PHE   A CD1 
278  C  CD2 . PHE   A 41  ? 0.7664 0.8063 0.5673 0.2461 0.1094  0.1374  84  PHE   A CD2 
279  C  CE1 . PHE   A 41  ? 0.8088 0.7978 0.5356 0.2950 0.0802  0.1508  84  PHE   A CE1 
280  C  CE2 . PHE   A 41  ? 0.8000 0.7845 0.5522 0.2485 0.1068  0.1422  84  PHE   A CE2 
281  C  CZ  . PHE   A 41  ? 0.8147 0.7733 0.5323 0.2699 0.0931  0.1493  84  PHE   A CZ  
282  N  N   . SER   A 42  ? 0.7170 1.0321 0.7032 0.2822 0.0616  0.1173  85  SER   A N   
283  C  CA  . SER   A 42  ? 0.6970 1.1042 0.7598 0.2875 0.0613  0.1143  85  SER   A CA  
284  C  C   . SER   A 42  ? 0.7259 1.1510 0.7792 0.3372 0.0648  0.1259  85  SER   A C   
285  O  O   . SER   A 42  ? 0.7673 1.1338 0.7536 0.3673 0.0539  0.1317  85  SER   A O   
286  C  CB  . SER   A 42  ? 0.6933 1.1579 0.7894 0.2772 0.0268  0.0950  85  SER   A CB  
287  O  OG  . SER   A 42  ? 0.7525 1.2088 0.7981 0.3148 -0.0027 0.0958  85  SER   A OG  
288  N  N   . LEU   A 43  ? 0.7023 1.2062 0.8230 0.3465 0.0817  0.1299  86  LEU   A N   
289  C  CA  . LEU   A 43  ? 0.7276 1.2533 0.8400 0.3999 0.0868  0.1379  86  LEU   A CA  
290  C  C   . LEU   A 43  ? 0.7331 1.3101 0.8574 0.4344 0.0522  0.1309  86  LEU   A C   
291  O  O   . LEU   A 43  ? 0.6864 1.3464 0.8772 0.4180 0.0347  0.1200  86  LEU   A O   
292  C  CB  . LEU   A 43  ? 0.6914 1.2860 0.8652 0.4041 0.1237  0.1475  86  LEU   A CB  
293  C  CG  . LEU   A 43  ? 0.7469 1.2872 0.8840 0.4024 0.1608  0.1604  86  LEU   A CG  
294  C  CD1 . LEU   A 43  ? 0.7147 1.3328 0.9013 0.4240 0.1957  0.1722  86  LEU   A CD1 
295  C  CD2 . LEU   A 43  ? 0.8206 1.2625 0.8620 0.4358 0.1527  0.1593  86  LEU   A CD2 
296  N  N   . VAL   A 44  ? 0.7886 1.3160 0.8501 0.4843 0.0412  0.1366  87  VAL   A N   
297  C  CA  . VAL   A 44  ? 0.8014 1.3632 0.8597 0.5303 0.0090  0.1348  87  VAL   A CA  
298  C  C   . VAL   A 44  ? 0.8127 1.4194 0.8941 0.5828 0.0250  0.1387  87  VAL   A C   
299  O  O   . VAL   A 44  ? 0.8573 1.3970 0.8893 0.6043 0.0456  0.1441  87  VAL   A O   
300  C  CB  . VAL   A 44  ? 0.8729 1.3285 0.8345 0.5489 -0.0146 0.1419  87  VAL   A CB  
301  C  CG1 . VAL   A 44  ? 0.8864 1.3554 0.8284 0.6115 -0.0422 0.1468  87  VAL   A CG1 
302  C  CG2 . VAL   A 44  ? 0.8875 1.3214 0.8301 0.5051 -0.0323 0.1369  87  VAL   A CG2 
303  N  N   . GLU   A 45  ? 0.7669 1.4924 0.9267 0.6029 0.0167  0.1335  88  GLU   A N   
304  C  CA  . GLU   A 45  ? 0.7667 1.5473 0.9522 0.6596 0.0339  0.1364  88  GLU   A CA  
305  C  C   . GLU   A 45  ? 0.7327 1.5937 0.9513 0.7110 0.0002  0.1317  88  GLU   A C   
306  O  O   . GLU   A 45  ? 0.7471 1.5929 0.9408 0.7122 -0.0398 0.1289  88  GLU   A O   
307  C  CB  . GLU   A 45  ? 0.7596 1.6245 1.0236 0.6369 0.0790  0.1400  88  GLU   A CB  
308  C  CG  . GLU   A 45  ? 0.8435 1.6510 1.0936 0.5759 0.1071  0.1458  88  GLU   A CG  
309  C  CD  . GLU   A 45  ? 0.9741 1.6918 1.1506 0.5915 0.1369  0.1530  88  GLU   A CD  
310  O  OE1 . GLU   A 45  ? 1.0415 1.6456 1.1387 0.5793 0.1254  0.1517  88  GLU   A OE1 
311  O  OE2 . GLU   A 45  ? 0.9840 1.7500 1.1836 0.6153 0.1720  0.1594  88  GLU   A OE2 
312  N  N   . GLY   B 7   ? 0.9225 0.9285 0.8689 0.3037 0.2120  0.0070  16  GLY   B N   
313  C  CA  . GLY   B 7   ? 0.9276 0.9267 0.8728 0.3248 0.2090  0.0124  16  GLY   B CA  
314  C  C   . GLY   B 7   ? 0.9225 0.9298 0.8677 0.3284 0.1921  0.0168  16  GLY   B C   
315  O  O   . GLY   B 7   ? 0.9202 0.9520 0.8797 0.3357 0.1826  0.0151  16  GLY   B O   
316  N  N   . GLU   B 8   ? 0.9160 0.9036 0.8452 0.3242 0.1873  0.0222  17  GLU   B N   
317  C  CA  . GLU   B 8   ? 0.9051 0.8971 0.8288 0.3304 0.1709  0.0257  17  GLU   B CA  
318  C  C   . GLU   B 8   ? 0.8944 0.8894 0.8148 0.3099 0.1597  0.0227  17  GLU   B C   
319  O  O   . GLU   B 8   ? 0.9100 0.8886 0.8172 0.2983 0.1616  0.0250  17  GLU   B O   
320  C  CB  . GLU   B 8   ? 0.9252 0.8975 0.8327 0.3464 0.1724  0.0356  17  GLU   B CB  
321  C  CG  . GLU   B 8   ? 0.9562 0.9366 0.8576 0.3647 0.1569  0.0382  17  GLU   B CG  
322  C  CD  . GLU   B 8   ? 1.0328 0.9980 0.9174 0.3853 0.1598  0.0499  17  GLU   B CD  
323  O  OE1 . GLU   B 8   ? 1.0332 0.9810 0.9137 0.3829 0.1741  0.0579  17  GLU   B OE1 
324  O  OE2 . GLU   B 8   ? 1.0725 1.0436 0.9484 0.4048 0.1475  0.0516  17  GLU   B OE2 
325  N  N   A THR   B 9   ? 0.8701 0.8860 0.8037 0.3053 0.1472  0.0179  18  THR   B N   
326  N  N   B THR   B 9   ? 0.8718 0.8876 0.8053 0.3053 0.1473  0.0179  18  THR   B N   
327  C  CA  A THR   B 9   ? 0.8608 0.8777 0.7923 0.2859 0.1354  0.0156  18  THR   B CA  
328  C  CA  B THR   B 9   ? 0.8643 0.8808 0.7953 0.2861 0.1353  0.0157  18  THR   B CA  
329  C  C   A THR   B 9   ? 0.8479 0.8640 0.7723 0.2947 0.1132  0.0153  18  THR   B C   
330  C  C   B THR   B 9   ? 0.8496 0.8654 0.7737 0.2947 0.1134  0.0154  18  THR   B C   
331  O  O   A THR   B 9   ? 0.8491 0.8658 0.7738 0.2804 0.0999  0.0126  18  THR   B O   
332  O  O   B THR   B 9   ? 0.8509 0.8672 0.7752 0.2801 0.1003  0.0127  18  THR   B O   
333  C  CB  A THR   B 9   ? 0.8663 0.9048 0.8189 0.2679 0.1392  0.0115  18  THR   B CB  
334  C  CB  B THR   B 9   ? 0.8736 0.9110 0.8252 0.2682 0.1388  0.0116  18  THR   B CB  
335  O  OG1 A THR   B 9   ? 0.8769 0.9190 0.8354 0.2690 0.1590  0.0104  18  THR   B OG1 
336  O  OG1 B THR   B 9   ? 0.8742 0.9377 0.8490 0.2788 0.1358  0.0094  18  THR   B OG1 
337  C  CG2 A THR   B 9   ? 0.8754 0.9073 0.8214 0.2446 0.1346  0.0113  18  THR   B CG2 
338  C  CG2 B THR   B 9   ? 0.8818 0.9138 0.8309 0.2586 0.1587  0.0109  18  THR   B CG2 
339  N  N   . THR   B 10  ? 0.8361 0.8481 0.7516 0.3192 0.1090  0.0182  19  THR   B N   
340  C  CA  . THR   B 10  ? 0.8080 0.8169 0.7116 0.3325 0.0875  0.0168  19  THR   B CA  
341  C  C   . THR   B 10  ? 0.7881 0.7757 0.6668 0.3277 0.0803  0.0192  19  THR   B C   
342  O  O   . THR   B 10  ? 0.7894 0.7633 0.6549 0.3284 0.0935  0.0259  19  THR   B O   
343  C  CB  . THR   B 10  ? 0.8212 0.8296 0.7166 0.3631 0.0887  0.0210  19  THR   B CB  
344  O  OG1 . THR   B 10  ? 0.8332 0.8631 0.7517 0.3693 0.0916  0.0176  19  THR   B OG1 
345  C  CG2 . THR   B 10  ? 0.8201 0.8220 0.6961 0.3821 0.0675  0.0197  19  THR   B CG2 
346  N  N   . ASP   B 11  ? 0.7682 0.7524 0.6406 0.3241 0.0582  0.0138  20  ASP   B N   
347  C  CA  . ASP   B 11  ? 0.7798 0.7428 0.6252 0.3246 0.0487  0.0152  20  ASP   B CA  
348  C  C   . ASP   B 11  ? 0.7747 0.7273 0.5962 0.3527 0.0533  0.0230  20  ASP   B C   
349  O  O   . ASP   B 11  ? 0.7785 0.7379 0.6003 0.3745 0.0523  0.0241  20  ASP   B O   
350  C  CB  . ASP   B 11  ? 0.8134 0.7715 0.6542 0.3224 0.0208  0.0069  20  ASP   B CB  
351  C  CG  . ASP   B 11  ? 0.8788 0.8364 0.7324 0.2925 0.0146  0.0031  20  ASP   B CG  
352  O  OD1 . ASP   B 11  ? 0.8700 0.8418 0.7456 0.2736 0.0304  0.0049  20  ASP   B OD1 
353  O  OD2 . ASP   B 11  ? 0.9264 0.8682 0.7666 0.2890 -0.0061 -0.0013 20  ASP   B OD2 
354  N  N   . GLY   B 12  ? 0.7600 0.6983 0.5622 0.3525 0.0589  0.0294  21  GLY   B N   
355  C  CA  . GLY   B 12  ? 0.7471 0.6790 0.5294 0.3775 0.0660  0.0397  21  GLY   B CA  
356  C  C   . GLY   B 12  ? 0.7302 0.6562 0.5087 0.3686 0.0830  0.0493  21  GLY   B C   
357  O  O   . GLY   B 12  ? 0.7125 0.6369 0.4996 0.3438 0.0871  0.0463  21  GLY   B O   
358  N  N   . VAL   B 13  ? 0.7252 0.6488 0.4905 0.3893 0.0925  0.0619  22  VAL   B N   
359  C  CA  . VAL   B 13  ? 0.7221 0.6436 0.4877 0.3824 0.1083  0.0732  22  VAL   B CA  
360  C  C   . VAL   B 13  ? 0.7208 0.6460 0.5062 0.3798 0.1289  0.0815  22  VAL   B C   
361  O  O   . VAL   B 13  ? 0.7214 0.6496 0.5106 0.3950 0.1318  0.0830  22  VAL   B O   
362  C  CB  . VAL   B 13  ? 0.7285 0.6467 0.4690 0.4036 0.1054  0.0832  22  VAL   B CB  
363  C  CG1 . VAL   B 13  ? 0.7212 0.6426 0.4495 0.4365 0.1091  0.0934  22  VAL   B CG1 
364  C  CG2 . VAL   B 13  ? 0.7252 0.6452 0.4707 0.3914 0.1184  0.0933  22  VAL   B CG2 
365  N  N   . TYR   B 14  ? 0.7231 0.6463 0.5220 0.3582 0.1409  0.0837  23  TYR   B N   
366  C  CA  . TYR   B 14  ? 0.7118 0.6331 0.5293 0.3522 0.1580  0.0888  23  TYR   B CA  
367  C  C   . TYR   B 14  ? 0.7124 0.6307 0.5354 0.3448 0.1701  0.1013  23  TYR   B C   
368  O  O   . TYR   B 14  ? 0.7254 0.6448 0.5433 0.3342 0.1657  0.1010  23  TYR   B O   
369  C  CB  . TYR   B 14  ? 0.7026 0.6231 0.5348 0.3293 0.1592  0.0754  23  TYR   B CB  
370  C  CG  . TYR   B 14  ? 0.7033 0.6313 0.5404 0.3341 0.1515  0.0650  23  TYR   B CG  
371  C  CD1 . TYR   B 14  ? 0.7137 0.6471 0.5427 0.3352 0.1340  0.0572  23  TYR   B CD1 
372  C  CD2 . TYR   B 14  ? 0.7088 0.6386 0.5602 0.3359 0.1610  0.0626  23  TYR   B CD2 
373  C  CE1 . TYR   B 14  ? 0.7177 0.6613 0.5557 0.3387 0.1256  0.0486  23  TYR   B CE1 
374  C  CE2 . TYR   B 14  ? 0.7161 0.6577 0.5752 0.3415 0.1540  0.0541  23  TYR   B CE2 
375  C  CZ  . TYR   B 14  ? 0.7249 0.6750 0.5792 0.3417 0.1361  0.0474  23  TYR   B CZ  
376  O  OH  . TYR   B 14  ? 0.7332 0.6982 0.6004 0.3436 0.1279  0.0391  23  TYR   B OH  
377  N  N   . ARG   B 15  ? 0.6972 0.6112 0.5325 0.3486 0.1847  0.1119  24  ARG   B N   
378  C  CA  . ARG   B 15  ? 0.6923 0.6034 0.5397 0.3375 0.1959  0.1238  24  ARG   B CA  
379  C  C   . ARG   B 15  ? 0.6889 0.5906 0.5505 0.3108 0.1984  0.1123  24  ARG   B C   
380  O  O   . ARG   B 15  ? 0.6827 0.5789 0.5476 0.3078 0.1987  0.1012  24  ARG   B O   
381  C  CB  . ARG   B 15  ? 0.7040 0.6109 0.5598 0.3522 0.2105  0.1413  24  ARG   B CB  
382  C  CG  . ARG   B 15  ? 0.7324 0.6478 0.5722 0.3823 0.2108  0.1547  24  ARG   B CG  
383  C  CD  . ARG   B 15  ? 0.7784 0.6878 0.6270 0.3951 0.2269  0.1729  24  ARG   B CD  
384  N  NE  . ARG   B 15  ? 0.8079 0.7232 0.6368 0.4282 0.2266  0.1824  24  ARG   B NE  
385  C  CZ  . ARG   B 15  ? 0.8225 0.7480 0.6405 0.4471 0.2316  0.2003  24  ARG   B CZ  
386  N  NH1 . ARG   B 15  ? 0.8254 0.7594 0.6541 0.4353 0.2377  0.2118  24  ARG   B NH1 
387  N  NH2 . ARG   B 15  ? 0.8230 0.7521 0.6186 0.4794 0.2301  0.2068  24  ARG   B NH2 
388  N  N   . VAL   B 16  ? 0.6893 0.5900 0.5590 0.2934 0.2002  0.1153  25  VAL   B N   
389  C  CA  . VAL   B 16  ? 0.7001 0.5896 0.5805 0.2696 0.2017  0.1046  25  VAL   B CA  
390  C  C   . VAL   B 16  ? 0.7105 0.5908 0.6094 0.2649 0.2127  0.1176  25  VAL   B C   
391  O  O   . VAL   B 16  ? 0.7073 0.5959 0.6139 0.2646 0.2151  0.1321  25  VAL   B O   
392  C  CB  . VAL   B 16  ? 0.7094 0.6033 0.5838 0.2516 0.1922  0.0956  25  VAL   B CB  
393  C  CG1 . VAL   B 16  ? 0.7180 0.5989 0.5996 0.2302 0.1934  0.0835  25  VAL   B CG1 
394  C  CG2 . VAL   B 16  ? 0.7140 0.6149 0.5707 0.2560 0.1810  0.0857  25  VAL   B CG2 
395  N  N   . MET   B 17  ? 0.7254 0.5885 0.6320 0.2626 0.2193  0.1134  26  MET   B N   
396  C  CA  . MET   B 17  ? 0.7492 0.5974 0.6734 0.2586 0.2292  0.1254  26  MET   B CA  
397  C  C   . MET   B 17  ? 0.7877 0.6156 0.7201 0.2363 0.2275  0.1124  26  MET   B C   
398  O  O   . MET   B 17  ? 0.7952 0.6190 0.7170 0.2296 0.2222  0.0939  26  MET   B O   
399  C  CB  . MET   B 17  ? 0.7505 0.5889 0.6734 0.2787 0.2382  0.1319  26  MET   B CB  
400  C  CG  . MET   B 17  ? 0.7627 0.6177 0.6724 0.3044 0.2380  0.1404  26  MET   B CG  
401  S  SD  . MET   B 17  ? 0.7937 0.6655 0.7065 0.3144 0.2428  0.1655  26  MET   B SD  
402  C  CE  . MET   B 17  ? 0.6875 0.5419 0.6190 0.3178 0.2592  0.1866  26  MET   B CE  
403  N  N   . THR   B 18  ? 0.8122 0.6263 0.7633 0.2260 0.2322  0.1229  27  THR   B N   
404  C  CA  . THR   B 18  ? 0.8484 0.6376 0.8075 0.2064 0.2293  0.1114  27  THR   B CA  
405  C  C   . THR   B 18  ? 0.8821 0.6469 0.8576 0.2070 0.2382  0.1241  27  THR   B C   
406  O  O   . THR   B 18  ? 0.8702 0.6425 0.8582 0.2155 0.2464  0.1465  27  THR   B O   
407  C  CB  . THR   B 18  ? 0.8582 0.6541 0.8249 0.1842 0.2192  0.1068  27  THR   B CB  
408  O  OG1 . THR   B 18  ? 0.8846 0.6524 0.8560 0.1674 0.2146  0.0936  27  THR   B OG1 
409  C  CG2 . THR   B 18  ? 0.8404 0.6540 0.8286 0.1807 0.2215  0.1293  27  THR   B CG2 
410  N  N   . ARG   B 19  ? 0.9270 0.6609 0.9012 0.1987 0.2365  0.1102  28  ARG   B N   
411  C  CA  . ARG   B 19  ? 0.9717 0.6751 0.9604 0.1971 0.2431  0.1205  28  ARG   B CA  
412  C  C   . ARG   B 19  ? 1.0041 0.6853 1.0101 0.1705 0.2343  0.1161  28  ARG   B C   
413  O  O   . ARG   B 19  ? 1.0134 0.6656 1.0343 0.1650 0.2375  0.1246  28  ARG   B O   
414  C  CB  . ARG   B 19  ? 1.0143 0.6944 0.9871 0.2140 0.2487  0.1106  28  ARG   B CB  
415  C  CG  . ARG   B 19  ? 1.0790 0.7803 1.0409 0.2407 0.2568  0.1191  28  ARG   B CG  
416  C  CD  . ARG   B 19  ? 1.1577 0.8336 1.1141 0.2586 0.2654  0.1211  28  ARG   B CD  
417  N  NE  . ARG   B 19  ? 1.2042 0.8948 1.1576 0.2833 0.2743  0.1389  28  ARG   B NE  
418  C  CZ  . ARG   B 19  ? 1.2455 0.9455 1.1838 0.3056 0.2761  0.1324  28  ARG   B CZ  
419  N  NH1 . ARG   B 19  ? 1.2494 0.9489 1.1766 0.3058 0.2713  0.1100  28  ARG   B NH1 
420  N  NH2 . ARG   B 19  ? 1.2425 0.9544 1.1770 0.3286 0.2825  0.1486  28  ARG   B NH2 
421  N  N   . ARG   B 20  ? 1.0197 0.7147 1.0245 0.1541 0.2223  0.1038  29  ARG   B N   
422  C  CA  . ARG   B 20  ? 1.0436 0.7230 1.0627 0.1288 0.2101  0.0963  29  ARG   B CA  
423  C  C   . ARG   B 20  ? 1.0323 0.7148 1.0876 0.1154 0.2119  0.1207  29  ARG   B C   
424  O  O   . ARG   B 20  ? 1.0396 0.6920 1.1118 0.0986 0.2060  0.1195  29  ARG   B O   
425  C  CB  . ARG   B 20  ? 1.0792 0.7803 1.0863 0.1194 0.1981  0.0809  29  ARG   B CB  
426  C  CG  . ARG   B 20  ? 1.1559 0.8423 1.1738 0.0949 0.1826  0.0698  29  ARG   B CG  
427  C  CD  . ARG   B 20  ? 1.2234 0.9320 1.2263 0.0885 0.1714  0.0558  29  ARG   B CD  
428  N  NE  . ARG   B 20  ? 1.2682 1.0176 1.2749 0.0960 0.1757  0.0712  29  ARG   B NE  
429  C  CZ  . ARG   B 20  ? 1.2897 1.0633 1.3208 0.0865 0.1723  0.0869  29  ARG   B CZ  
430  N  NH1 . ARG   B 20  ? 1.2767 1.0405 1.3349 0.0664 0.1638  0.0900  29  ARG   B NH1 
431  N  NH2 . ARG   B 20  ? 1.2884 1.0965 1.3172 0.0974 0.1765  0.0992  29  ARG   B NH2 
432  N  N   . LEU   B 21  ? 1.0124 0.7303 1.0798 0.1236 0.2203  0.1435  30  LEU   B N   
433  C  CA  . LEU   B 21  ? 0.9951 0.7222 1.0988 0.1134 0.2255  0.1707  30  LEU   B CA  
434  C  C   . LEU   B 21  ? 0.9939 0.6991 1.1046 0.1263 0.2409  0.1900  30  LEU   B C   
435  O  O   . LEU   B 21  ? 1.0161 0.6911 1.1063 0.1373 0.2433  0.1775  30  LEU   B O   
436  C  CB  . LEU   B 21  ? 0.9789 0.7545 1.0903 0.1198 0.2290  0.1878  30  LEU   B CB  
437  C  CG  . LEU   B 21  ? 0.9977 0.7980 1.1073 0.1074 0.2148  0.1753  30  LEU   B CG  
438  C  CD1 . LEU   B 21  ? 1.0076 0.7868 1.1312 0.0797 0.1985  0.1592  30  LEU   B CD1 
439  C  CD2 . LEU   B 21  ? 1.0192 0.8300 1.0913 0.1229 0.2116  0.1568  30  LEU   B CD2 
440  N  N   . LEU   B 22  ? 0.9669 0.6875 1.1062 0.1258 0.2519  0.2212  31  LEU   B N   
441  C  CA  . LEU   B 22  ? 0.9616 0.6643 1.1068 0.1396 0.2680  0.2433  31  LEU   B CA  
442  C  C   . LEU   B 22  ? 0.9500 0.6674 1.0627 0.1731 0.2783  0.2441  31  LEU   B C   
443  O  O   . LEU   B 22  ? 0.9450 0.6988 1.0458 0.1839 0.2774  0.2434  31  LEU   B O   
444  C  CB  . LEU   B 22  ? 0.9438 0.6692 1.1271 0.1320 0.2783  0.2785  31  LEU   B CB  
445  C  CG  . LEU   B 22  ? 0.9660 0.6731 1.1598 0.1432 0.2959  0.3062  31  LEU   B CG  
446  C  CD1 . LEU   B 22  ? 0.9775 0.6391 1.1967 0.1182 0.2909  0.3074  31  LEU   B CD1 
447  C  CD2 . LEU   B 22  ? 0.9573 0.7058 1.1724 0.1523 0.3117  0.3423  31  LEU   B CD2 
448  N  N   . GLY   B 23  ? 0.9372 0.6253 1.0351 0.1894 0.2862  0.2440  32  GLY   B N   
449  C  CA  . GLY   B 23  ? 0.9271 0.6266 0.9959 0.2213 0.2940  0.2438  32  GLY   B CA  
450  C  C   . GLY   B 23  ? 0.9118 0.6338 0.9545 0.2289 0.2840  0.2194  32  GLY   B C   
451  O  O   . GLY   B 23  ? 0.9152 0.6300 0.9529 0.2127 0.2715  0.1953  32  GLY   B O   
452  N  N   . SER   B 24  ? 0.8947 0.6424 0.9194 0.2543 0.2890  0.2258  33  SER   B N   
453  C  CA  . SER   B 24  ? 0.8853 0.6549 0.8873 0.2612 0.2791  0.2055  33  SER   B CA  
454  C  C   . SER   B 24  ? 0.8568 0.6613 0.8640 0.2600 0.2773  0.2170  33  SER   B C   
455  O  O   . SER   B 24  ? 0.8419 0.6625 0.8528 0.2757 0.2874  0.2410  33  SER   B O   
456  C  CB  . SER   B 24  ? 0.9119 0.6848 0.8901 0.2903 0.2826  0.2025  33  SER   B CB  
457  O  OG  . SER   B 24  ? 0.9525 0.6991 0.9224 0.2925 0.2818  0.1861  33  SER   B OG  
458  N  N   . THR   B 25  ? 0.8425 0.6583 0.8484 0.2430 0.2649  0.2006  34  THR   B N   
459  C  CA  . THR   B 25  ? 0.8151 0.6628 0.8248 0.2414 0.2616  0.2093  34  THR   B CA  
460  C  C   . THR   B 25  ? 0.7993 0.6630 0.7825 0.2501 0.2511  0.1918  34  THR   B C   
461  O  O   . THR   B 25  ? 0.8047 0.6577 0.7768 0.2400 0.2418  0.1686  34  THR   B O   
462  C  CB  . THR   B 25  ? 0.8267 0.6744 0.8616 0.2125 0.2552  0.2086  34  THR   B CB  
463  O  OG1 . THR   B 25  ? 0.8448 0.6744 0.9070 0.2023 0.2635  0.2251  34  THR   B OG1 
464  C  CG2 . THR   B 25  ? 0.8141 0.6968 0.8558 0.2114 0.2522  0.2191  34  THR   B CG2 
465  N  N   . GLN   B 26  ? 0.7767 0.6656 0.7492 0.2688 0.2525  0.2035  35  GLN   B N   
466  C  CA  . GLN   B 26  ? 0.7676 0.6697 0.7151 0.2771 0.2412  0.1889  35  GLN   B CA  
467  C  C   . GLN   B 26  ? 0.7490 0.6652 0.7013 0.2596 0.2318  0.1838  35  GLN   B C   
468  O  O   . GLN   B 26  ? 0.7407 0.6766 0.7047 0.2614 0.2353  0.2011  35  GLN   B O   
469  C  CB  . GLN   B 26  ? 0.7750 0.6929 0.7041 0.3079 0.2446  0.2016  35  GLN   B CB  
470  C  CG  . GLN   B 26  ? 0.7913 0.7205 0.6950 0.3163 0.2310  0.1878  35  GLN   B CG  
471  C  CD  . GLN   B 26  ? 0.8136 0.7495 0.6944 0.3478 0.2310  0.1939  35  GLN   B CD  
472  O  OE1 . GLN   B 26  ? 0.8272 0.7544 0.7049 0.3625 0.2372  0.1978  35  GLN   B OE1 
473  N  NE2 . GLN   B 26  ? 0.8070 0.7570 0.6692 0.3603 0.2229  0.1940  35  GLN   B NE2 
474  N  N   . VAL   B 27  ? 0.7330 0.6402 0.6762 0.2440 0.2205  0.1611  36  VAL   B N   
475  C  CA  . VAL   B 27  ? 0.7169 0.6347 0.6601 0.2285 0.2102  0.1539  36  VAL   B CA  
476  C  C   . VAL   B 27  ? 0.6978 0.6301 0.6156 0.2418 0.2014  0.1490  36  VAL   B C   
477  O  O   . VAL   B 27  ? 0.6968 0.6432 0.6133 0.2371 0.1949  0.1505  36  VAL   B O   
478  C  CB  . VAL   B 27  ? 0.7416 0.6407 0.6868 0.2050 0.2032  0.1336  36  VAL   B CB  
479  C  CG1 . VAL   B 27  ? 0.7495 0.6341 0.7212 0.1897 0.2082  0.1395  36  VAL   B CG1 
480  C  CG2 . VAL   B 27  ? 0.7599 0.6440 0.6863 0.2097 0.2017  0.1160  36  VAL   B CG2 
481  N  N   . GLY   B 28  ? 0.6814 0.6095 0.5797 0.2588 0.2002  0.1436  37  GLY   B N   
482  C  CA  . GLY   B 28  ? 0.6800 0.6160 0.5536 0.2712 0.1900  0.1378  37  GLY   B CA  
483  C  C   . GLY   B 28  ? 0.6767 0.6066 0.5343 0.2886 0.1879  0.1318  37  GLY   B C   
484  O  O   . GLY   B 28  ? 0.6661 0.5897 0.5309 0.2966 0.1964  0.1363  37  GLY   B O   
485  N  N   . VAL   B 29  ? 0.6746 0.6057 0.5105 0.2948 0.1753  0.1219  38  VAL   B N   
486  C  CA  . VAL   B 29  ? 0.6712 0.5987 0.4905 0.3108 0.1678  0.1146  38  VAL   B CA  
487  C  C   . VAL   B 29  ? 0.6653 0.5868 0.4742 0.2965 0.1545  0.0967  38  VAL   B C   
488  O  O   . VAL   B 29  ? 0.6613 0.5822 0.4685 0.2805 0.1505  0.0926  38  VAL   B O   
489  C  CB  . VAL   B 29  ? 0.6695 0.6054 0.4702 0.3388 0.1643  0.1260  38  VAL   B CB  
490  C  CG1 . VAL   B 29  ? 0.6759 0.6068 0.4568 0.3561 0.1521  0.1169  38  VAL   B CG1 
491  C  CG2 . VAL   B 29  ? 0.6668 0.6106 0.4779 0.3536 0.1796  0.1463  38  VAL   B CG2 
492  N  N   . GLY   B 30  ? 0.6565 0.5748 0.4591 0.3028 0.1475  0.0876  39  GLY   B N   
493  C  CA  . GLY   B 30  ? 0.6610 0.5750 0.4567 0.2895 0.1357  0.0735  39  GLY   B CA  
494  C  C   . GLY   B 30  ? 0.6708 0.5844 0.4581 0.3018 0.1236  0.0669  39  GLY   B C   
495  O  O   . GLY   B 30  ? 0.6721 0.5887 0.4586 0.3217 0.1247  0.0713  39  GLY   B O   
496  N  N   . VAL   B 31  ? 0.6806 0.5901 0.4620 0.2897 0.1112  0.0566  40  VAL   B N   
497  C  CA  . VAL   B 31  ? 0.7002 0.6088 0.4765 0.2969 0.0962  0.0492  40  VAL   B CA  
498  C  C   . VAL   B 31  ? 0.6976 0.6117 0.4919 0.2793 0.0967  0.0402  40  VAL   B C   
499  O  O   . VAL   B 31  ? 0.7049 0.6170 0.5024 0.2583 0.0986  0.0364  40  VAL   B O   
500  C  CB  . VAL   B 31  ? 0.7398 0.6371 0.4935 0.2988 0.0786  0.0463  40  VAL   B CB  
501  C  CG1 . VAL   B 31  ? 0.7592 0.6524 0.5099 0.3017 0.0599  0.0371  40  VAL   B CG1 
502  C  CG2 . VAL   B 31  ? 0.7558 0.6504 0.4895 0.3212 0.0781  0.0557  40  VAL   B CG2 
503  N  N   . MET   B 32  ? 0.6777 0.6003 0.4832 0.2890 0.0947  0.0373  41  MET   B N   
504  C  CA  . MET   B 32  ? 0.6650 0.5980 0.4901 0.2746 0.0945  0.0298  41  MET   B CA  
505  C  C   . MET   B 32  ? 0.6718 0.6038 0.4935 0.2746 0.0729  0.0237  41  MET   B C   
506  O  O   . MET   B 32  ? 0.6797 0.6090 0.4912 0.2946 0.0603  0.0232  41  MET   B O   
507  C  CB  . MET   B 32  ? 0.6574 0.6026 0.4997 0.2857 0.1048  0.0303  41  MET   B CB  
508  C  CG  . MET   B 32  ? 0.6672 0.6276 0.5319 0.2722 0.1081  0.0239  41  MET   B CG  
509  S  SD  . MET   B 32  ? 0.6850 0.6447 0.5568 0.2501 0.1272  0.0227  41  MET   B SD  
510  C  CE  . MET   B 32  ? 0.6640 0.6173 0.5368 0.2647 0.1444  0.0277  41  MET   B CE  
511  N  N   . GLN   B 33  ? 0.6696 0.6017 0.4979 0.2526 0.0679  0.0195  42  GLN   B N   
512  C  CA  . GLN   B 33  ? 0.6794 0.6086 0.5088 0.2471 0.0466  0.0141  42  GLN   B CA  
513  C  C   . GLN   B 33  ? 0.6738 0.6148 0.5255 0.2214 0.0508  0.0125  42  GLN   B C   
514  O  O   . GLN   B 33  ? 0.6748 0.6133 0.5242 0.2064 0.0638  0.0151  42  GLN   B O   
515  C  CB  . GLN   B 33  ? 0.7251 0.6307 0.5261 0.2493 0.0314  0.0141  42  GLN   B CB  
516  C  CG  . GLN   B 33  ? 0.7963 0.6928 0.5951 0.2481 0.0055  0.0075  42  GLN   B CG  
517  C  CD  . GLN   B 33  ? 0.9134 0.7826 0.6792 0.2563 -0.0110 0.0064  42  GLN   B CD  
518  O  OE1 . GLN   B 33  ? 0.9442 0.7978 0.7035 0.2399 -0.0213 0.0049  42  GLN   B OE1 
519  N  NE2 . GLN   B 33  ? 0.9488 0.8111 0.6915 0.2834 -0.0132 0.0080  42  GLN   B NE2 
520  N  N   . GLU   B 34  ? 0.6628 0.6185 0.5367 0.2173 0.0403  0.0088  43  GLU   B N   
521  C  CA  . GLU   B 34  ? 0.6650 0.6371 0.5646 0.1939 0.0441  0.0094  43  GLU   B CA  
522  C  C   . GLU   B 34  ? 0.6636 0.6519 0.5755 0.1868 0.0707  0.0125  43  GLU   B C   
523  O  O   . GLU   B 34  ? 0.6603 0.6547 0.5803 0.1673 0.0794  0.0152  43  GLU   B O   
524  C  CB  . GLU   B 34  ? 0.7084 0.6621 0.5975 0.1746 0.0322  0.0107  43  GLU   B CB  
525  C  CG  . GLU   B 34  ? 0.7817 0.7152 0.6566 0.1823 0.0041  0.0060  43  GLU   B CG  
526  C  CD  . GLU   B 34  ? 0.8984 0.8079 0.7599 0.1647 -0.0093 0.0072  43  GLU   B CD  
527  O  OE1 . GLU   B 34  ? 0.9251 0.8438 0.8082 0.1411 -0.0074 0.0110  43  GLU   B OE1 
528  O  OE2 . GLU   B 34  ? 0.9325 0.8142 0.7617 0.1754 -0.0210 0.0055  43  GLU   B OE2 
529  N  N   . GLY   B 35  ? 0.6556 0.6493 0.5674 0.2039 0.0830  0.0122  44  GLY   B N   
530  C  CA  . GLY   B 35  ? 0.6485 0.6527 0.5684 0.2010 0.1059  0.0133  44  GLY   B CA  
531  C  C   . GLY   B 35  ? 0.6615 0.6474 0.5601 0.1939 0.1175  0.0150  44  GLY   B C   
532  O  O   . GLY   B 35  ? 0.6697 0.6609 0.5719 0.1886 0.1344  0.0145  44  GLY   B O   
533  N  N   . VAL   B 36  ? 0.6625 0.6272 0.5381 0.1952 0.1079  0.0166  45  VAL   B N   
534  C  CA  . VAL   B 36  ? 0.6597 0.6087 0.5161 0.1888 0.1159  0.0183  45  VAL   B CA  
535  C  C   . VAL   B 36  ? 0.6579 0.5948 0.5000 0.2055 0.1158  0.0212  45  VAL   B C   
536  O  O   . VAL   B 36  ? 0.6538 0.5866 0.4889 0.2199 0.1035  0.0227  45  VAL   B O   
537  C  CB  . VAL   B 36  ? 0.6734 0.6109 0.5163 0.1731 0.1060  0.0194  45  VAL   B CB  
538  C  CG1 . VAL   B 36  ? 0.6971 0.6188 0.5183 0.1694 0.1109  0.0210  45  VAL   B CG1 
539  C  CG2 . VAL   B 36  ? 0.6605 0.6109 0.5186 0.1551 0.1103  0.0197  45  VAL   B CG2 
540  N  N   . PHE   B 37  ? 0.6502 0.5819 0.4886 0.2044 0.1294  0.0224  46  PHE   B N   
541  C  CA  . PHE   B 37  ? 0.6455 0.5685 0.4749 0.2176 0.1308  0.0278  46  PHE   B CA  
542  C  C   . PHE   B 37  ? 0.6361 0.5478 0.4479 0.2097 0.1264  0.0301  46  PHE   B C   
543  O  O   . PHE   B 37  ? 0.6266 0.5350 0.4351 0.1946 0.1312  0.0273  46  PHE   B O   
544  C  CB  . PHE   B 37  ? 0.6395 0.5626 0.4791 0.2221 0.1465  0.0288  46  PHE   B CB  
545  C  CG  . PHE   B 37  ? 0.6457 0.5634 0.4822 0.2375 0.1486  0.0373  46  PHE   B CG  
546  C  CD1 . PHE   B 37  ? 0.6557 0.5775 0.4916 0.2571 0.1433  0.0417  46  PHE   B CD1 
547  C  CD2 . PHE   B 37  ? 0.6566 0.5662 0.4915 0.2326 0.1558  0.0415  46  PHE   B CD2 
548  C  CE1 . PHE   B 37  ? 0.6672 0.5855 0.4991 0.2726 0.1471  0.0520  46  PHE   B CE1 
549  C  CE2 . PHE   B 37  ? 0.6645 0.5721 0.4999 0.2456 0.1589  0.0521  46  PHE   B CE2 
550  C  CZ  . PHE   B 37  ? 0.6663 0.5785 0.4996 0.2662 0.1559  0.0581  46  PHE   B CZ  
551  N  N   . HIS   B 38  ? 0.6347 0.5412 0.4337 0.2219 0.1167  0.0350  47  HIS   B N   
552  C  CA  . HIS   B 38  ? 0.6345 0.5324 0.4161 0.2186 0.1108  0.0379  47  HIS   B CA  
553  C  C   . HIS   B 38  ? 0.6346 0.5341 0.4158 0.2302 0.1172  0.0463  47  HIS   B C   
554  O  O   . HIS   B 38  ? 0.6289 0.5316 0.4101 0.2488 0.1166  0.0518  47  HIS   B O   
555  C  CB  . HIS   B 38  ? 0.6341 0.5243 0.3990 0.2270 0.0932  0.0376  47  HIS   B CB  
556  C  CG  . HIS   B 38  ? 0.6473 0.5362 0.4165 0.2164 0.0842  0.0311  47  HIS   B CG  
557  N  ND1 . HIS   B 38  ? 0.6561 0.5557 0.4431 0.2196 0.0847  0.0281  47  HIS   B ND1 
558  C  CD2 . HIS   B 38  ? 0.6645 0.5434 0.4241 0.2029 0.0744  0.0286  47  HIS   B CD2 
559  C  CE1 . HIS   B 38  ? 0.6598 0.5585 0.4510 0.2060 0.0758  0.0241  47  HIS   B CE1 
560  N  NE2 . HIS   B 38  ? 0.6668 0.5520 0.4419 0.1950 0.0699  0.0248  47  HIS   B NE2 
561  N  N   . THR   B 39  ? 0.6395 0.5379 0.4207 0.2200 0.1228  0.0481  48  THR   B N   
562  C  CA  . THR   B 39  ? 0.6391 0.5421 0.4245 0.2286 0.1285  0.0581  48  THR   B CA  
563  C  C   . THR   B 39  ? 0.6504 0.5530 0.4278 0.2187 0.1249  0.0593  48  THR   B C   
564  O  O   . THR   B 39  ? 0.6549 0.5510 0.4187 0.2091 0.1172  0.0530  48  THR   B O   
565  C  CB  . THR   B 39  ? 0.6450 0.5503 0.4507 0.2281 0.1421  0.0606  48  THR   B CB  
566  O  OG1 . THR   B 39  ? 0.6501 0.5610 0.4629 0.2364 0.1476  0.0731  48  THR   B OG1 
567  C  CG2 . THR   B 39  ? 0.6502 0.5500 0.4630 0.2085 0.1479  0.0518  48  THR   B CG2 
568  N  N   . MET   B 40  ? 0.6495 0.5600 0.4358 0.2219 0.1301  0.0686  49  MET   B N   
569  C  CA  . MET   B 40  ? 0.6545 0.5685 0.4368 0.2138 0.1262  0.0703  49  MET   B CA  
570  C  C   . MET   B 40  ? 0.6585 0.5693 0.4537 0.1940 0.1314  0.0638  49  MET   B C   
571  O  O   . MET   B 40  ? 0.6513 0.5610 0.4642 0.1915 0.1405  0.0648  49  MET   B O   
572  C  CB  . MET   B 40  ? 0.6523 0.5808 0.4398 0.2291 0.1282  0.0851  49  MET   B CB  
573  C  CG  . MET   B 40  ? 0.6894 0.6184 0.4594 0.2525 0.1228  0.0901  49  MET   B CG  
574  S  SD  . MET   B 40  ? 0.8375 0.7772 0.5908 0.2686 0.1154  0.0998  49  MET   B SD  
575  C  CE  . MET   B 40  ? 0.8246 0.7462 0.5507 0.2594 0.0998  0.0862  49  MET   B CE  
576  N  N   . TRP   B 41  ? 0.6687 0.5758 0.4529 0.1811 0.1249  0.0569  50  TRP   B N   
577  C  CA  A TRP   B 41  ? 0.6785 0.5804 0.4699 0.1641 0.1275  0.0487  50  TRP   B CA  
578  C  CA  B TRP   B 41  ? 0.6756 0.5774 0.4671 0.1642 0.1277  0.0487  50  TRP   B CA  
579  C  C   . TRP   B 41  ? 0.6694 0.5781 0.4851 0.1611 0.1324  0.0554  50  TRP   B C   
580  O  O   . TRP   B 41  ? 0.6746 0.5744 0.5012 0.1523 0.1377  0.0495  50  TRP   B O   
581  C  CB  A TRP   B 41  ? 0.6881 0.5868 0.4613 0.1542 0.1185  0.0423  50  TRP   B CB  
582  C  CB  B TRP   B 41  ? 0.6819 0.5794 0.4545 0.1538 0.1190  0.0414  50  TRP   B CB  
583  C  CG  A TRP   B 41  ? 0.7041 0.5936 0.4764 0.1389 0.1200  0.0307  50  TRP   B CG  
584  C  CG  B TRP   B 41  ? 0.6908 0.5813 0.4663 0.1387 0.1202  0.0313  50  TRP   B CG  
585  C  CD1 A TRP   B 41  ? 0.7227 0.6014 0.4811 0.1324 0.1225  0.0206  50  TRP   B CD1 
586  C  CD1 B TRP   B 41  ? 0.6947 0.5892 0.4832 0.1312 0.1174  0.0314  50  TRP   B CD1 
587  C  CD2 A TRP   B 41  ? 0.7018 0.5925 0.4867 0.1294 0.1180  0.0281  50  TRP   B CD2 
588  C  CD2 B TRP   B 41  ? 0.6975 0.5757 0.4612 0.1304 0.1236  0.0194  50  TRP   B CD2 
589  N  NE1 A TRP   B 41  ? 0.7318 0.6032 0.4892 0.1219 0.1228  0.0111  50  TRP   B NE1 
590  N  NE1 B TRP   B 41  ? 0.7046 0.5866 0.4881 0.1195 0.1174  0.0186  50  TRP   B NE1 
591  C  CE2 A TRP   B 41  ? 0.7211 0.5981 0.4949 0.1191 0.1187  0.0145  50  TRP   B CE2 
592  C  CE2 B TRP   B 41  ? 0.7090 0.5814 0.4759 0.1200 0.1223  0.0114  50  TRP   B CE2 
593  C  CE3 A TRP   B 41  ? 0.6984 0.6011 0.5042 0.1285 0.1155  0.0365  50  TRP   B CE3 
594  C  CE3 B TRP   B 41  ? 0.7099 0.5828 0.4625 0.1310 0.1277  0.0153  50  TRP   B CE3 
595  C  CZ2 A TRP   B 41  ? 0.7287 0.5999 0.5085 0.1087 0.1148  0.0068  50  TRP   B CZ2 
596  C  CZ2 B TRP   B 41  ? 0.7224 0.5823 0.4765 0.1132 0.1255  -0.0011 50  TRP   B CZ2 
597  C  CZ3 A TRP   B 41  ? 0.7082 0.6072 0.5248 0.1154 0.1115  0.0300  50  TRP   B CZ3 
598  C  CZ3 B TRP   B 41  ? 0.7271 0.5917 0.4711 0.1232 0.1328  0.0050  50  TRP   B CZ3 
599  C  CH2 A TRP   B 41  ? 0.7205 0.6022 0.5223 0.1059 0.1099  0.0142  50  TRP   B CH2 
600  C  CH2 B TRP   B 41  ? 0.7289 0.5862 0.4711 0.1158 0.1319  -0.0034 50  TRP   B CH2 
601  N  N   . HIS   B 42  ? 0.6585 0.5826 0.4829 0.1683 0.1305  0.0680  51  HIS   B N   
602  C  CA  . HIS   B 42  ? 0.6608 0.5935 0.5134 0.1628 0.1351  0.0767  51  HIS   B CA  
603  C  C   . HIS   B 42  ? 0.6706 0.5983 0.5414 0.1676 0.1469  0.0832  51  HIS   B C   
604  O  O   . HIS   B 42  ? 0.6772 0.6042 0.5715 0.1584 0.1508  0.0876  51  HIS   B O   
605  C  CB  . HIS   B 42  ? 0.6611 0.6167 0.5225 0.1701 0.1322  0.0912  51  HIS   B CB  
606  C  CG  . HIS   B 42  ? 0.6847 0.6520 0.5460 0.1920 0.1386  0.1063  51  HIS   B CG  
607  N  ND1 . HIS   B 42  ? 0.7065 0.6777 0.5432 0.2086 0.1328  0.1080  51  HIS   B ND1 
608  C  CD2 . HIS   B 42  ? 0.6933 0.6672 0.5737 0.2008 0.1499  0.1202  51  HIS   B CD2 
609  C  CE1 . HIS   B 42  ? 0.7095 0.6899 0.5495 0.2279 0.1401  0.1214  51  HIS   B CE1 
610  N  NE2 . HIS   B 42  ? 0.7089 0.6920 0.5748 0.2243 0.1513  0.1299  51  HIS   B NE2 
611  N  N   . VAL   B 43  ? 0.6718 0.5950 0.5323 0.1815 0.1515  0.0836  52  VAL   B N   
612  C  CA  . VAL   B 43  ? 0.6729 0.5902 0.5465 0.1887 0.1623  0.0891  52  VAL   B CA  
613  C  C   . VAL   B 43  ? 0.6848 0.5828 0.5629 0.1753 0.1654  0.0757  52  VAL   B C   
614  O  O   . VAL   B 43  ? 0.6921 0.5823 0.5889 0.1714 0.1721  0.0800  52  VAL   B O   
615  C  CB  . VAL   B 43  ? 0.6834 0.6024 0.5421 0.2086 0.1632  0.0913  52  VAL   B CB  
616  C  CG1 . VAL   B 43  ? 0.6880 0.5989 0.5560 0.2166 0.1731  0.0935  52  VAL   B CG1 
617  C  CG2 . VAL   B 43  ? 0.6836 0.6187 0.5360 0.2263 0.1611  0.1053  52  VAL   B CG2 
618  N  N   . THR   B 44  ? 0.6810 0.5707 0.5414 0.1693 0.1610  0.0602  53  THR   B N   
619  C  CA  . THR   B 44  ? 0.6845 0.5574 0.5450 0.1606 0.1649  0.0473  53  THR   B CA  
620  C  C   . THR   B 44  ? 0.6941 0.5581 0.5496 0.1435 0.1585  0.0355  53  THR   B C   
621  O  O   . THR   B 44  ? 0.6902 0.5378 0.5470 0.1371 0.1612  0.0255  53  THR   B O   
622  C  CB  . THR   B 44  ? 0.7000 0.5717 0.5463 0.1671 0.1669  0.0390  53  THR   B CB  
623  O  OG1 . THR   B 44  ? 0.7274 0.6030 0.5555 0.1612 0.1591  0.0327  53  THR   B OG1 
624  C  CG2 . THR   B 44  ? 0.6932 0.5731 0.5424 0.1847 0.1702  0.0481  53  THR   B CG2 
625  N  N   . LYS   B 45  ? 0.7029 0.5762 0.5497 0.1382 0.1494  0.0358  54  LYS   B N   
626  C  CA  . LYS   B 45  ? 0.7356 0.6018 0.5719 0.1243 0.1413  0.0237  54  LYS   B CA  
627  C  C   . LYS   B 45  ? 0.7561 0.6107 0.5703 0.1226 0.1437  0.0092  54  LYS   B C   
628  O  O   . LYS   B 45  ? 0.7693 0.6124 0.5734 0.1137 0.1402  -0.0028 54  LYS   B O   
629  C  CB  . LYS   B 45  ? 0.7638 0.6207 0.6182 0.1126 0.1385  0.0212  54  LYS   B CB  
630  C  CG  . LYS   B 45  ? 0.8146 0.6844 0.6972 0.1125 0.1387  0.0377  54  LYS   B CG  
631  C  CD  . LYS   B 45  ? 0.8803 0.7734 0.7630 0.1147 0.1316  0.0473  54  LYS   B CD  
632  C  CE  . LYS   B 45  ? 0.9275 0.8369 0.8419 0.1147 0.1341  0.0654  54  LYS   B CE  
633  N  NZ  . LYS   B 45  ? 0.9471 0.8826 0.8607 0.1271 0.1333  0.0800  54  LYS   B NZ  
634  N  N   . GLY   B 46  ? 0.7595 0.6181 0.5673 0.1317 0.1494  0.0109  55  GLY   B N   
635  C  CA  . GLY   B 46  ? 0.7734 0.6270 0.5654 0.1308 0.1537  0.0009  55  GLY   B CA  
636  C  C   . GLY   B 46  ? 0.7890 0.6323 0.5869 0.1338 0.1633  -0.0062 55  GLY   B C   
637  O  O   . GLY   B 46  ? 0.8121 0.6535 0.5981 0.1339 0.1684  -0.0143 55  GLY   B O   
638  N  N   . ALA   B 47  ? 0.7790 0.6155 0.5949 0.1369 0.1666  -0.0025 56  ALA   B N   
639  C  CA  . ALA   B 47  ? 0.7796 0.6021 0.5992 0.1413 0.1751  -0.0095 56  ALA   B CA  
640  C  C   . ALA   B 47  ? 0.7798 0.6117 0.6033 0.1541 0.1837  -0.0064 56  ALA   B C   
641  O  O   . ALA   B 47  ? 0.7750 0.6210 0.6049 0.1607 0.1824  0.0039  56  ALA   B O   
642  C  CB  . ALA   B 47  ? 0.7742 0.5830 0.6119 0.1397 0.1751  -0.0052 56  ALA   B CB  
643  N  N   . ALA   B 48  ? 0.7826 0.6068 0.6022 0.1591 0.1918  -0.0155 57  ALA   B N   
644  C  CA  . ALA   B 48  ? 0.7838 0.6182 0.6097 0.1720 0.2002  -0.0139 57  ALA   B CA  
645  C  C   . ALA   B 48  ? 0.7872 0.6225 0.6302 0.1830 0.2021  -0.0026 57  ALA   B C   
646  O  O   . ALA   B 48  ? 0.7920 0.6145 0.6428 0.1810 0.2007  0.0027  57  ALA   B O   
647  C  CB  . ALA   B 48  ? 0.7910 0.6139 0.6099 0.1771 0.2088  -0.0257 57  ALA   B CB  
648  N  N   . LEU   B 49  ? 0.7852 0.6361 0.6344 0.1947 0.2050  0.0018  58  LEU   B N   
649  C  CA  . LEU   B 49  ? 0.7910 0.6441 0.6525 0.2083 0.2067  0.0127  58  LEU   B CA  
650  C  C   . LEU   B 49  ? 0.8114 0.6661 0.6787 0.2229 0.2150  0.0097  58  LEU   B C   
651  O  O   . LEU   B 49  ? 0.8112 0.6750 0.6755 0.2231 0.2184  0.0012  58  LEU   B O   
652  C  CB  . LEU   B 49  ? 0.7787 0.6498 0.6403 0.2123 0.1988  0.0213  58  LEU   B CB  
653  C  CG  . LEU   B 49  ? 0.7905 0.6626 0.6459 0.2026 0.1902  0.0263  58  LEU   B CG  
654  C  CD1 . LEU   B 49  ? 0.7835 0.6697 0.6357 0.2111 0.1822  0.0336  58  LEU   B CD1 
655  C  CD2 . LEU   B 49  ? 0.7988 0.6594 0.6618 0.2009 0.1922  0.0344  58  LEU   B CD2 
656  N  N   . ARG   B 50  ? 0.8242 0.6717 0.6999 0.2361 0.2189  0.0180  59  ARG   B N   
657  C  CA  . ARG   B 50  ? 0.8428 0.6916 0.7238 0.2530 0.2261  0.0168  59  ARG   B CA  
658  C  C   . ARG   B 50  ? 0.8536 0.7203 0.7408 0.2681 0.2225  0.0266  59  ARG   B C   
659  O  O   . ARG   B 50  ? 0.8447 0.7125 0.7313 0.2691 0.2176  0.0368  59  ARG   B O   
660  C  CB  . ARG   B 50  ? 0.8750 0.6951 0.7575 0.2576 0.2334  0.0178  59  ARG   B CB  
661  C  CG  . ARG   B 50  ? 0.9406 0.7581 0.8283 0.2789 0.2405  0.0215  59  ARG   B CG  
662  C  CD  . ARG   B 50  ? 1.0198 0.8040 0.9053 0.2824 0.2476  0.0188  59  ARG   B CD  
663  N  NE  . ARG   B 50  ? 1.0773 0.8376 0.9667 0.2712 0.2460  0.0272  59  ARG   B NE  
664  C  CZ  . ARG   B 50  ? 1.1129 0.8671 1.0108 0.2784 0.2486  0.0439  59  ARG   B CZ  
665  N  NH1 . ARG   B 50  ? 1.1061 0.8745 1.0058 0.2985 0.2517  0.0528  59  ARG   B NH1 
666  N  NH2 . ARG   B 50  ? 1.1201 0.8558 1.0256 0.2658 0.2477  0.0526  59  ARG   B NH2 
667  N  N   . SER   B 51  ? 0.8693 0.7517 0.7617 0.2809 0.2240  0.0232  60  SER   B N   
668  C  CA  . SER   B 51  ? 0.8925 0.7918 0.7897 0.2967 0.2182  0.0302  60  SER   B CA  
669  C  C   . SER   B 51  ? 0.9273 0.8324 0.8319 0.3141 0.2246  0.0272  60  SER   B C   
670  O  O   . SER   B 51  ? 0.9272 0.8525 0.8388 0.3137 0.2241  0.0195  60  SER   B O   
671  C  CB  . SER   B 51  ? 0.8999 0.8217 0.7978 0.2886 0.2069  0.0268  60  SER   B CB  
672  O  OG  . SER   B 51  ? 0.9228 0.8607 0.8253 0.3044 0.1989  0.0302  60  SER   B OG  
673  N  N   . GLY   B 52  ? 0.9523 0.8396 0.8560 0.3290 0.2315  0.0341  61  GLY   B N   
674  C  CA  . GLY   B 52  ? 0.9703 0.8588 0.8786 0.3479 0.2383  0.0316  61  GLY   B CA  
675  C  C   . GLY   B 52  ? 0.9886 0.8686 0.8955 0.3407 0.2466  0.0199  61  GLY   B C   
676  O  O   . GLY   B 52  ? 1.0073 0.8632 0.9066 0.3270 0.2496  0.0173  61  GLY   B O   
677  N  N   . GLU   B 53  ? 0.9806 0.8825 0.8948 0.3495 0.2494  0.0123  62  GLU   B N   
678  C  CA  . GLU   B 53  ? 0.9902 0.8879 0.9004 0.3451 0.2580  0.0008  62  GLU   B CA  
679  C  C   . GLU   B 53  ? 0.9747 0.8861 0.8830 0.3226 0.2549  -0.0053 62  GLU   B C   
680  O  O   . GLU   B 53  ? 0.9884 0.8918 0.8878 0.3168 0.2617  -0.0143 62  GLU   B O   
681  C  CB  . GLU   B 53  ? 1.0290 0.9475 0.9483 0.3654 0.2644  -0.0034 62  GLU   B CB  
682  C  CG  . GLU   B 53  ? 1.1288 1.0369 1.0392 0.3682 0.2758  -0.0144 62  GLU   B CG  
683  C  CD  . GLU   B 53  ? 1.2465 1.1766 1.1656 0.3908 0.2836  -0.0181 62  GLU   B CD  
684  O  OE1 . GLU   B 53  ? 1.2644 1.2160 1.1977 0.4057 0.2797  -0.0120 62  GLU   B OE1 
685  O  OE2 . GLU   B 53  ? 1.2853 1.2118 1.1959 0.3953 0.2934  -0.0273 62  GLU   B OE2 
686  N  N   . GLY   B 54  ? 0.9455 0.8749 0.8594 0.3120 0.2444  -0.0004 63  GLY   B N   
687  C  CA  . GLY   B 54  ? 0.9248 0.8668 0.8368 0.2918 0.2405  -0.0039 63  GLY   B CA  
688  C  C   . GLY   B 54  ? 0.9106 0.8283 0.8075 0.2745 0.2379  -0.0045 63  GLY   B C   
689  O  O   . GLY   B 54  ? 0.9235 0.8185 0.8154 0.2753 0.2362  0.0005  63  GLY   B O   
690  N  N   . ARG   B 55  ? 0.8795 0.8039 0.7703 0.2590 0.2378  -0.0097 64  ARG   B N   
691  C  CA  . ARG   B 55  ? 0.8687 0.7738 0.7448 0.2426 0.2342  -0.0115 64  ARG   B CA  
692  C  C   . ARG   B 55  ? 0.8375 0.7590 0.7129 0.2281 0.2252  -0.0084 64  ARG   B C   
693  O  O   . ARG   B 55  ? 0.8331 0.7764 0.7139 0.2245 0.2270  -0.0099 64  ARG   B O   
694  C  CB  . ARG   B 55  ? 0.8843 0.7754 0.7464 0.2394 0.2427  -0.0224 64  ARG   B CB  
695  C  CG  . ARG   B 55  ? 0.9271 0.7991 0.7731 0.2229 0.2375  -0.0260 64  ARG   B CG  
696  C  CD  . ARG   B 55  ? 0.9872 0.8440 0.8155 0.2222 0.2442  -0.0384 64  ARG   B CD  
697  N  NE  . ARG   B 55  ? 1.0389 0.8797 0.8518 0.2066 0.2367  -0.0422 64  ARG   B NE  
698  C  CZ  . ARG   B 55  ? 1.0852 0.9050 0.8788 0.2043 0.2378  -0.0538 64  ARG   B CZ  
699  N  NH1 . ARG   B 55  ? 1.1045 0.9146 0.8895 0.2175 0.2469  -0.0631 64  ARG   B NH1 
700  N  NH2 . ARG   B 55  ? 1.0850 0.8929 0.8660 0.1904 0.2288  -0.0569 64  ARG   B NH2 
701  N  N   . LEU   B 56  ? 0.8112 0.7220 0.6802 0.2199 0.2162  -0.0035 65  LEU   B N   
702  C  CA  . LEU   B 56  ? 0.7895 0.7096 0.6535 0.2070 0.2070  -0.0011 65  LEU   B CA  
703  C  C   . LEU   B 56  ? 0.7783 0.6838 0.6254 0.1926 0.2072  -0.0060 65  LEU   B C   
704  O  O   . LEU   B 56  ? 0.7870 0.6736 0.6284 0.1907 0.2060  -0.0063 65  LEU   B O   
705  C  CB  . LEU   B 56  ? 0.7897 0.7094 0.6550 0.2106 0.1958  0.0075  65  LEU   B CB  
706  C  CG  . LEU   B 56  ? 0.8144 0.7413 0.6909 0.2283 0.1938  0.0131  65  LEU   B CG  
707  C  CD1 . LEU   B 56  ? 0.8281 0.7547 0.6994 0.2318 0.1818  0.0206  65  LEU   B CD1 
708  C  CD2 . LEU   B 56  ? 0.8191 0.7681 0.7087 0.2333 0.1935  0.0104  65  LEU   B CD2 
709  N  N   . ASP   B 57  ? 0.7591 0.6735 0.5988 0.1825 0.2083  -0.0092 66  ASP   B N   
710  C  CA  . ASP   B 57  ? 0.7655 0.6668 0.5859 0.1704 0.2073  -0.0138 66  ASP   B CA  
711  C  C   . ASP   B 57  ? 0.7444 0.6475 0.5572 0.1599 0.1956  -0.0080 66  ASP   B C   
712  O  O   . ASP   B 57  ? 0.7343 0.6506 0.5551 0.1598 0.1904  -0.0023 66  ASP   B O   
713  C  CB  . ASP   B 57  ? 0.8079 0.7147 0.6193 0.1686 0.2178  -0.0206 66  ASP   B CB  
714  C  CG  . ASP   B 57  ? 0.8948 0.7951 0.7076 0.1809 0.2287  -0.0281 66  ASP   B CG  
715  O  OD1 . ASP   B 57  ? 0.9012 0.7810 0.7135 0.1855 0.2269  -0.0310 66  ASP   B OD1 
716  O  OD2 . ASP   B 57  ? 0.9426 0.8580 0.7572 0.1864 0.2392  -0.0304 66  ASP   B OD2 
717  N  N   . PRO   B 58  ? 0.7364 0.6254 0.5345 0.1520 0.1899  -0.0094 67  PRO   B N   
718  C  CA  . PRO   B 58  ? 0.7234 0.6134 0.5123 0.1445 0.1789  -0.0038 67  PRO   B CA  
719  C  C   . PRO   B 58  ? 0.7020 0.5992 0.4808 0.1357 0.1803  -0.0037 67  PRO   B C   
720  O  O   . PRO   B 58  ? 0.6971 0.5959 0.4695 0.1336 0.1900  -0.0088 67  PRO   B O   
721  C  CB  . PRO   B 58  ? 0.7459 0.6215 0.5237 0.1397 0.1739  -0.0063 67  PRO   B CB  
722  C  CG  . PRO   B 58  ? 0.7563 0.6220 0.5289 0.1391 0.1823  -0.0165 67  PRO   B CG  
723  C  CD  . PRO   B 58  ? 0.7358 0.6071 0.5242 0.1496 0.1917  -0.0170 67  PRO   B CD  
724  N  N   . TYR   B 59  ? 0.6838 0.5842 0.4602 0.1313 0.1710  0.0029  68  TYR   B N   
725  C  CA  . TYR   B 59  ? 0.6647 0.5708 0.4343 0.1215 0.1719  0.0059  68  TYR   B CA  
726  C  C   . TYR   B 59  ? 0.6740 0.5674 0.4219 0.1139 0.1620  0.0089  68  TYR   B C   
727  O  O   . TYR   B 59  ? 0.6768 0.5679 0.4095 0.1055 0.1653  0.0098  68  TYR   B O   
728  C  CB  . TYR   B 59  ? 0.6388 0.5589 0.4282 0.1226 0.1684  0.0112  68  TYR   B CB  
729  C  CG  . TYR   B 59  ? 0.6324 0.5600 0.4221 0.1106 0.1686  0.0168  68  TYR   B CG  
730  C  CD1 . TYR   B 59  ? 0.6462 0.5615 0.4218 0.1024 0.1567  0.0220  68  TYR   B CD1 
731  C  CD2 . TYR   B 59  ? 0.6184 0.5663 0.4256 0.1082 0.1798  0.0186  68  TYR   B CD2 
732  C  CE1 . TYR   B 59  ? 0.6473 0.5666 0.4242 0.0900 0.1569  0.0289  68  TYR   B CE1 
733  C  CE2 . TYR   B 59  ? 0.6231 0.5802 0.4354 0.0958 0.1805  0.0264  68  TYR   B CE2 
734  C  CZ  . TYR   B 59  ? 0.6465 0.5877 0.4440 0.0858 0.1686  0.0318  68  TYR   B CZ  
735  O  OH  . TYR   B 59  ? 0.6686 0.6164 0.4725 0.0720 0.1691  0.0412  68  TYR   B OH  
736  N  N   . TRP   B 60  ? 0.6720 0.5579 0.4174 0.1184 0.1503  0.0114  69  TRP   B N   
737  C  CA  . TRP   B 60  ? 0.6721 0.5465 0.3972 0.1146 0.1399  0.0144  69  TRP   B CA  
738  C  C   . TRP   B 60  ? 0.6710 0.5415 0.3962 0.1228 0.1336  0.0144  69  TRP   B C   
739  O  O   . TRP   B 60  ? 0.6660 0.5417 0.4069 0.1321 0.1338  0.0160  69  TRP   B O   
740  C  CB  . TRP   B 60  ? 0.6618 0.5329 0.3842 0.1119 0.1296  0.0209  69  TRP   B CB  
741  C  CG  . TRP   B 60  ? 0.6731 0.5298 0.3734 0.1121 0.1173  0.0241  69  TRP   B CG  
742  C  CD1 . TRP   B 60  ? 0.6944 0.5411 0.3727 0.1043 0.1158  0.0256  69  TRP   B CD1 
743  C  CD2 . TRP   B 60  ? 0.6734 0.5252 0.3697 0.1234 0.1061  0.0263  69  TRP   B CD2 
744  N  NE1 . TRP   B 60  ? 0.7042 0.5395 0.3658 0.1098 0.1032  0.0282  69  TRP   B NE1 
745  C  CE2 . TRP   B 60  ? 0.6935 0.5328 0.3661 0.1219 0.0976  0.0286  69  TRP   B CE2 
746  C  CE3 . TRP   B 60  ? 0.6645 0.5219 0.3736 0.1366 0.1030  0.0273  69  TRP   B CE3 
747  C  CZ2 . TRP   B 60  ? 0.7051 0.5391 0.3677 0.1334 0.0865  0.0316  69  TRP   B CZ2 
748  C  CZ3 . TRP   B 60  ? 0.6818 0.5339 0.3801 0.1479 0.0928  0.0310  69  TRP   B CZ3 
749  C  CH2 . TRP   B 60  ? 0.6988 0.5400 0.3746 0.1465 0.0846  0.0330  69  TRP   B CH2 
750  N  N   . GLY   B 61  ? 0.6755 0.5388 0.3839 0.1199 0.1281  0.0141  70  GLY   B N   
751  C  CA  . GLY   B 61  ? 0.6867 0.5504 0.3974 0.1265 0.1220  0.0161  70  GLY   B CA  
752  C  C   . GLY   B 61  ? 0.7060 0.5637 0.3962 0.1237 0.1131  0.0170  70  GLY   B C   
753  O  O   . GLY   B 61  ? 0.7129 0.5642 0.3859 0.1158 0.1138  0.0139  70  GLY   B O   
754  N  N   . ASP   B 62  ? 0.7151 0.5766 0.4070 0.1316 0.1055  0.0220  71  ASP   B N   
755  C  CA  . ASP   B 62  ? 0.7250 0.5843 0.3998 0.1315 0.0962  0.0235  71  ASP   B CA  
756  C  C   . ASP   B 62  ? 0.7066 0.5789 0.3965 0.1396 0.0931  0.0286  71  ASP   B C   
757  O  O   . ASP   B 62  ? 0.7097 0.5872 0.4058 0.1514 0.0915  0.0359  71  ASP   B O   
758  C  CB  . ASP   B 62  ? 0.7700 0.6188 0.4235 0.1355 0.0873  0.0282  71  ASP   B CB  
759  C  CG  . ASP   B 62  ? 0.8628 0.7063 0.4935 0.1361 0.0779  0.0295  71  ASP   B CG  
760  O  OD1 . ASP   B 62  ? 0.8810 0.7334 0.5142 0.1451 0.0719  0.0333  71  ASP   B OD1 
761  O  OD2 . ASP   B 62  ? 0.9245 0.7563 0.5352 0.1286 0.0770  0.0277  71  ASP   B OD2 
762  N  N   . VAL   B 63  ? 0.6935 0.5715 0.3891 0.1335 0.0917  0.0254  72  VAL   B N   
763  C  CA  . VAL   B 63  ? 0.6767 0.5703 0.3908 0.1377 0.0887  0.0315  72  VAL   B CA  
764  C  C   . VAL   B 63  ? 0.6891 0.5906 0.3926 0.1505 0.0800  0.0407  72  VAL   B C   
765  O  O   . VAL   B 63  ? 0.6953 0.6115 0.4151 0.1609 0.0815  0.0503  72  VAL   B O   
766  C  CB  . VAL   B 63  ? 0.6691 0.5648 0.3889 0.1257 0.0852  0.0240  72  VAL   B CB  
767  C  CG1 . VAL   B 63  ? 0.6593 0.5743 0.3956 0.1282 0.0781  0.0314  72  VAL   B CG1 
768  C  CG2 . VAL   B 63  ? 0.6692 0.5585 0.4056 0.1175 0.0936  0.0170  72  VAL   B CG2 
769  N  N   . LYS   B 64  ? 0.6988 0.5901 0.3740 0.1515 0.0717  0.0388  73  LYS   B N   
770  C  CA  . LYS   B 64  ? 0.7065 0.6027 0.3687 0.1661 0.0629  0.0468  73  LYS   B CA  
771  C  C   . LYS   B 64  ? 0.7105 0.6025 0.3698 0.1808 0.0638  0.0531  73  LYS   B C   
772  O  O   . LYS   B 64  ? 0.6964 0.6016 0.3599 0.1966 0.0617  0.0618  73  LYS   B O   
773  C  CB  . LYS   B 64  ? 0.7430 0.6266 0.3742 0.1650 0.0532  0.0439  73  LYS   B CB  
774  C  CG  . LYS   B 64  ? 0.7845 0.6761 0.4042 0.1817 0.0435  0.0518  73  LYS   B CG  
775  C  CD  . LYS   B 64  ? 0.8474 0.7281 0.4385 0.1803 0.0340  0.0489  73  LYS   B CD  
776  C  CE  . LYS   B 64  ? 0.9099 0.7903 0.4811 0.1990 0.0240  0.0559  73  LYS   B CE  
777  N  NZ  . LYS   B 64  ? 0.9627 0.8232 0.4998 0.1972 0.0154  0.0530  73  LYS   B NZ  
778  N  N   . GLN   B 65  ? 0.7185 0.5945 0.3724 0.1767 0.0668  0.0488  74  GLN   B N   
779  C  CA  . GLN   B 65  ? 0.7192 0.5910 0.3718 0.1907 0.0657  0.0530  74  GLN   B CA  
780  C  C   . GLN   B 65  ? 0.6940 0.5825 0.3741 0.1970 0.0754  0.0577  74  GLN   B C   
781  O  O   . GLN   B 65  ? 0.6882 0.5790 0.3674 0.2139 0.0744  0.0634  74  GLN   B O   
782  C  CB  . GLN   B 65  ? 0.7586 0.6110 0.4011 0.1834 0.0642  0.0476  74  GLN   B CB  
783  C  CG  . GLN   B 65  ? 0.8235 0.6563 0.4387 0.1770 0.0554  0.0455  74  GLN   B CG  
784  C  CD  . GLN   B 65  ? 0.8943 0.7108 0.5059 0.1683 0.0544  0.0426  74  GLN   B CD  
785  O  OE1 . GLN   B 65  ? 0.9195 0.7316 0.5348 0.1763 0.0502  0.0432  74  GLN   B OE1 
786  N  NE2 . GLN   B 65  ? 0.8929 0.7017 0.4981 0.1523 0.0580  0.0400  74  GLN   B NE2 
787  N  N   . ASP   B 66  ? 0.6794 0.5766 0.3814 0.1844 0.0844  0.0552  75  ASP   B N   
788  C  CA  . ASP   B 66  ? 0.6677 0.5767 0.3967 0.1868 0.0947  0.0597  75  ASP   B CA  
789  C  C   . ASP   B 66  ? 0.6720 0.5723 0.4023 0.1908 0.0989  0.0572  75  ASP   B C   
790  O  O   . ASP   B 66  ? 0.6755 0.5827 0.4162 0.2039 0.1034  0.0640  75  ASP   B O   
791  C  CB  . ASP   B 66  ? 0.6749 0.6028 0.4147 0.2027 0.0958  0.0730  75  ASP   B CB  
792  C  CG  . ASP   B 66  ? 0.6877 0.6281 0.4579 0.2014 0.1072  0.0798  75  ASP   B CG  
793  O  OD1 . ASP   B 66  ? 0.6913 0.6257 0.4747 0.1862 0.1122  0.0730  75  ASP   B OD1 
794  O  OD2 . ASP   B 66  ? 0.7180 0.6728 0.4973 0.2165 0.1113  0.0924  75  ASP   B OD2 
795  N  N   . LEU   B 67  ? 0.6663 0.5535 0.3874 0.1798 0.0981  0.0482  76  LEU   B N   
796  C  CA  . LEU   B 67  ? 0.6552 0.5377 0.3811 0.1822 0.1011  0.0454  76  LEU   B CA  
797  C  C   . LEU   B 67  ? 0.6471 0.5271 0.3824 0.1675 0.1098  0.0374  76  LEU   B C   
798  O  O   . LEU   B 67  ? 0.6542 0.5304 0.3829 0.1551 0.1107  0.0323  76  LEU   B O   
799  C  CB  . LEU   B 67  ? 0.6584 0.5290 0.3645 0.1867 0.0897  0.0443  76  LEU   B CB  
800  C  CG  . LEU   B 67  ? 0.6621 0.5314 0.3545 0.2058 0.0801  0.0507  76  LEU   B CG  
801  C  CD1 . LEU   B 67  ? 0.6838 0.5350 0.3547 0.2071 0.0667  0.0475  76  LEU   B CD1 
802  C  CD2 . LEU   B 67  ? 0.6485 0.5277 0.3534 0.2230 0.0848  0.0562  76  LEU   B CD2 
803  N  N   . VAL   B 68  ? 0.6326 0.5150 0.3813 0.1710 0.1159  0.0361  77  VAL   B N   
804  C  CA  . VAL   B 68  ? 0.6213 0.5032 0.3785 0.1606 0.1250  0.0289  77  VAL   B CA  
805  C  C   . VAL   B 68  ? 0.6138 0.4993 0.3801 0.1666 0.1259  0.0283  77  VAL   B C   
806  O  O   . VAL   B 68  ? 0.6033 0.4924 0.3751 0.1803 0.1233  0.0328  77  VAL   B O   
807  C  CB  . VAL   B 68  ? 0.6132 0.4962 0.3840 0.1572 0.1347  0.0266  77  VAL   B CB  
808  C  CG1 . VAL   B 68  ? 0.6042 0.4926 0.3915 0.1700 0.1387  0.0341  77  VAL   B CG1 
809  C  CG2 . VAL   B 68  ? 0.6081 0.4882 0.3822 0.1490 0.1438  0.0177  77  VAL   B CG2 
810  N  N   . SER   B 69  ? 0.6228 0.5091 0.3900 0.1568 0.1289  0.0233  78  SER   B N   
811  C  CA  . SER   B 69  ? 0.6217 0.5157 0.4018 0.1601 0.1295  0.0225  78  SER   B CA  
812  C  C   . SER   B 69  ? 0.6187 0.5204 0.4124 0.1562 0.1436  0.0175  78  SER   B C   
813  O  O   . SER   B 69  ? 0.6238 0.5221 0.4108 0.1471 0.1506  0.0135  78  SER   B O   
814  C  CB  . SER   B 69  ? 0.6285 0.5197 0.4014 0.1528 0.1193  0.0232  78  SER   B CB  
815  O  OG  . SER   B 69  ? 0.6405 0.5335 0.4120 0.1378 0.1260  0.0212  78  SER   B OG  
816  N  N   . TYR   B 70  ? 0.6141 0.5252 0.4245 0.1655 0.1473  0.0173  79  TYR   B N   
817  C  CA  . TYR   B 70  ? 0.6118 0.5300 0.4348 0.1667 0.1607  0.0129  79  TYR   B CA  
818  C  C   . TYR   B 70  ? 0.6195 0.5544 0.4575 0.1666 0.1611  0.0124  79  TYR   B C   
819  O  O   . TYR   B 70  ? 0.6089 0.5490 0.4533 0.1722 0.1504  0.0152  79  TYR   B O   
820  C  CB  . TYR   B 70  ? 0.6010 0.5162 0.4326 0.1807 0.1652  0.0146  79  TYR   B CB  
821  C  CG  . TYR   B 70  ? 0.6153 0.5169 0.4401 0.1782 0.1684  0.0148  79  TYR   B CG  
822  C  CD1 . TYR   B 70  ? 0.6301 0.5266 0.4470 0.1787 0.1605  0.0207  79  TYR   B CD1 
823  C  CD2 . TYR   B 70  ? 0.6304 0.5246 0.4575 0.1760 0.1785  0.0091  79  TYR   B CD2 
824  C  CE1 . TYR   B 70  ? 0.6414 0.5293 0.4572 0.1748 0.1625  0.0218  79  TYR   B CE1 
825  C  CE2 . TYR   B 70  ? 0.6447 0.5256 0.4678 0.1711 0.1789  0.0085  79  TYR   B CE2 
826  C  CZ  . TYR   B 70  ? 0.6601 0.5397 0.4802 0.1698 0.1709  0.0155  79  TYR   B CZ  
827  O  OH  . TYR   B 70  ? 0.6854 0.5554 0.5068 0.1639 0.1706  0.0156  79  TYR   B OH  
828  N  N   . CYS   B 71  ? 0.6221 0.5663 0.4652 0.1602 0.1726  0.0088  80  CYS   B N   
829  C  CA  . CYS   B 71  ? 0.6206 0.5865 0.4827 0.1590 0.1759  0.0096  80  CYS   B CA  
830  C  C   . CYS   B 71  ? 0.6029 0.5747 0.4662 0.1450 0.1674  0.0141  80  CYS   B C   
831  O  O   . CYS   B 71  ? 0.6008 0.5932 0.4832 0.1406 0.1706  0.0162  80  CYS   B O   
832  C  CB  . CYS   B 71  ? 0.6485 0.6256 0.5293 0.1740 0.1727  0.0100  80  CYS   B CB  
833  S  SG  . CYS   B 71  ? 0.7675 0.7334 0.6468 0.1913 0.1820  0.0074  80  CYS   B SG  
834  N  N   . GLY   B 72  ? 0.5827 0.5373 0.4277 0.1382 0.1567  0.0163  81  GLY   B N   
835  C  CA  . GLY   B 72  ? 0.5735 0.5280 0.4174 0.1246 0.1476  0.0211  81  GLY   B CA  
836  C  C   . GLY   B 72  ? 0.5894 0.5210 0.4091 0.1216 0.1351  0.0228  81  GLY   B C   
837  O  O   . GLY   B 72  ? 0.5964 0.5162 0.4027 0.1301 0.1339  0.0208  81  GLY   B O   
838  N  N   . PRO   B 73  ? 0.6055 0.5306 0.4202 0.1095 0.1257  0.0275  82  PRO   B N   
839  C  CA  . PRO   B 73  ? 0.6365 0.5378 0.4255 0.1088 0.1128  0.0291  82  PRO   B CA  
840  C  C   . PRO   B 73  ? 0.6689 0.5598 0.4527 0.1233 0.0967  0.0275  82  PRO   B C   
841  O  O   . PRO   B 73  ? 0.6647 0.5648 0.4649 0.1316 0.0913  0.0258  82  PRO   B O   
842  C  CB  . PRO   B 73  ? 0.6446 0.5407 0.4323 0.0921 0.1072  0.0352  82  PRO   B CB  
843  C  CG  . PRO   B 73  ? 0.6246 0.5431 0.4443 0.0865 0.1094  0.0370  82  PRO   B CG  
844  C  CD  . PRO   B 73  ? 0.5905 0.5295 0.4234 0.0956 0.1269  0.0326  82  PRO   B CD  
845  N  N   . TRP   B 74  ? 0.6952 0.5677 0.4545 0.1282 0.0886  0.0284  83  TRP   B N   
846  C  CA  . TRP   B 74  ? 0.7110 0.5732 0.4598 0.1447 0.0746  0.0279  83  TRP   B CA  
847  C  C   . TRP   B 74  ? 0.7481 0.6036 0.5011 0.1447 0.0573  0.0272  83  TRP   B C   
848  O  O   . TRP   B 74  ? 0.7623 0.6076 0.5120 0.1301 0.0502  0.0293  83  TRP   B O   
849  C  CB  . TRP   B 74  ? 0.7097 0.5555 0.4314 0.1486 0.0695  0.0300  83  TRP   B CB  
850  C  CG  . TRP   B 74  ? 0.7029 0.5421 0.4126 0.1691 0.0590  0.0307  83  TRP   B CG  
851  C  CD1 . TRP   B 74  ? 0.7150 0.5374 0.4084 0.1783 0.0409  0.0304  83  TRP   B CD1 
852  C  CD2 . TRP   B 74  ? 0.6942 0.5431 0.4061 0.1839 0.0665  0.0327  83  TRP   B CD2 
853  N  NE1 . TRP   B 74  ? 0.7228 0.5457 0.4062 0.2003 0.0377  0.0320  83  TRP   B NE1 
854  C  CE2 . TRP   B 74  ? 0.7083 0.5489 0.4049 0.2034 0.0540  0.0346  83  TRP   B CE2 
855  C  CE3 . TRP   B 74  ? 0.6844 0.5473 0.4107 0.1830 0.0823  0.0334  83  TRP   B CE3 
856  C  CZ2 . TRP   B 74  ? 0.7090 0.5586 0.4055 0.2217 0.0591  0.0393  83  TRP   B CZ2 
857  C  CZ3 . TRP   B 74  ? 0.6882 0.5572 0.4161 0.1985 0.0858  0.0379  83  TRP   B CZ3 
858  C  CH2 . TRP   B 74  ? 0.6961 0.5608 0.4108 0.2179 0.0754  0.0418  83  TRP   B CH2 
859  N  N   . LYS   B 75  ? 0.7522 0.6132 0.5134 0.1606 0.0502  0.0244  84  LYS   B N   
860  C  CA  . LYS   B 75  ? 0.7659 0.6224 0.5337 0.1624 0.0318  0.0215  84  LYS   B CA  
861  C  C   . LYS   B 75  ? 0.8075 0.6419 0.5494 0.1801 0.0123  0.0194  84  LYS   B C   
862  O  O   . LYS   B 75  ? 0.8153 0.6362 0.5549 0.1786 -0.0072 0.0160  84  LYS   B O   
863  C  CB  . LYS   B 75  ? 0.7515 0.6308 0.5457 0.1700 0.0359  0.0187  84  LYS   B CB  
864  C  CG  . LYS   B 75  ? 0.7406 0.6433 0.5608 0.1561 0.0546  0.0202  84  LYS   B CG  
865  C  CD  . LYS   B 75  ? 0.7586 0.6673 0.5968 0.1351 0.0495  0.0221  84  LYS   B CD  
866  C  CE  . LYS   B 75  ? 0.7779 0.7109 0.6375 0.1236 0.0711  0.0249  84  LYS   B CE  
867  N  NZ  . LYS   B 75  ? 0.7966 0.7438 0.6814 0.1052 0.0681  0.0289  84  LYS   B NZ  
868  N  N   . LEU   B 76  ? 0.8303 0.6616 0.5539 0.1979 0.0171  0.0213  85  LEU   B N   
869  C  CA  . LEU   B 76  ? 0.8599 0.6736 0.5566 0.2201 0.0014  0.0202  85  LEU   B CA  
870  C  C   . LEU   B 76  ? 0.9099 0.6974 0.5798 0.2156 -0.0111 0.0207  85  LEU   B C   
871  O  O   . LEU   B 76  ? 0.9251 0.7116 0.5859 0.2095 -0.0014 0.0250  85  LEU   B O   
872  C  CB  . LEU   B 76  ? 0.8519 0.6768 0.5426 0.2406 0.0139  0.0250  85  LEU   B CB  
873  C  CG  . LEU   B 76  ? 0.8438 0.6920 0.5596 0.2437 0.0301  0.0266  85  LEU   B CG  
874  C  CD1 . LEU   B 76  ? 0.8481 0.7048 0.5593 0.2597 0.0430  0.0338  85  LEU   B CD1 
875  C  CD2 . LEU   B 76  ? 0.8444 0.6969 0.5700 0.2535 0.0197  0.0217  85  LEU   B CD2 
876  N  N   . ASP   B 77  ? 0.9363 0.7008 0.5923 0.2194 -0.0339 0.0157  86  ASP   B N   
877  C  CA  . ASP   B 77  ? 0.9748 0.7093 0.6036 0.2156 -0.0476 0.0159  86  ASP   B CA  
878  C  C   . ASP   B 77  ? 0.9963 0.7048 0.5905 0.2427 -0.0688 0.0113  86  ASP   B C   
879  O  O   . ASP   B 77  ? 1.0206 0.7046 0.5869 0.2458 -0.0776 0.0122  86  ASP   B O   
880  C  CB  . ASP   B 77  ? 1.0109 0.7340 0.6533 0.1878 -0.0556 0.0155  86  ASP   B CB  
881  C  CG  . ASP   B 77  ? 1.0915 0.8139 0.7528 0.1843 -0.0723 0.0093  86  ASP   B CG  
882  O  OD1 . ASP   B 77  ? 1.0926 0.8253 0.7567 0.2042 -0.0764 0.0044  86  ASP   B OD1 
883  O  OD2 . ASP   B 77  ? 1.1346 0.8471 0.8090 0.1616 -0.0814 0.0102  86  ASP   B OD2 
884  N  N   . ALA   B 78  ? 0.9895 0.7028 0.5818 0.2647 -0.0762 0.0068  87  ALA   B N   
885  C  CA  . ALA   B 78  ? 1.0129 0.7016 0.5683 0.2943 -0.0958 0.0019  87  ALA   B CA  
886  C  C   . ALA   B 78  ? 1.0296 0.7147 0.5563 0.3122 -0.0881 0.0084  87  ALA   B C   
887  O  O   . ALA   B 78  ? 1.0206 0.7309 0.5605 0.3083 -0.0657 0.0168  87  ALA   B O   
888  C  CB  . ALA   B 78  ? 0.9996 0.6999 0.5567 0.3182 -0.1000 -0.0022 87  ALA   B CB  
889  N  N   . ALA   B 79  ? 1.0533 0.7071 0.5419 0.3311 -0.1073 0.0044  88  ALA   B N   
890  C  CA  . ALA   B 79  ? 1.0714 0.7233 0.5330 0.3495 -0.1013 0.0109  88  ALA   B CA  
891  C  C   . ALA   B 79  ? 1.0988 0.7406 0.5252 0.3899 -0.1121 0.0087  88  ALA   B C   
892  O  O   . ALA   B 79  ? 1.1085 0.7271 0.5186 0.4024 -0.1335 -0.0013 88  ALA   B O   
893  C  CB  . ALA   B 79  ? 1.0888 0.7112 0.5329 0.3346 -0.1114 0.0102  88  ALA   B CB  
894  N  N   . TRP   B 80  ? 1.1095 0.7692 0.5237 0.4111 -0.0980 0.0182  89  TRP   B N   
895  C  CA  . TRP   B 80  ? 1.1432 0.7962 0.5206 0.4529 -0.1053 0.0187  89  TRP   B CA  
896  C  C   . TRP   B 80  ? 1.1863 0.7923 0.5215 0.4631 -0.1320 0.0091  89  TRP   B C   
897  O  O   . TRP   B 80  ? 1.1881 0.7792 0.5209 0.4439 -0.1344 0.0098  89  TRP   B O   
898  C  CB  . TRP   B 80  ? 1.1313 0.8181 0.5109 0.4690 -0.0826 0.0336  89  TRP   B CB  
899  C  CG  . TRP   B 80  ? 1.1515 0.8370 0.4943 0.5142 -0.0867 0.0367  89  TRP   B CG  
900  C  CD1 . TRP   B 80  ? 1.1688 0.8462 0.4912 0.5430 -0.0963 0.0319  89  TRP   B CD1 
901  C  CD2 . TRP   B 80  ? 1.1560 0.8533 0.4795 0.5373 -0.0791 0.0468  89  TRP   B CD2 
902  N  NE1 . TRP   B 80  ? 1.1815 0.8631 0.4702 0.5838 -0.0947 0.0383  89  TRP   B NE1 
903  C  CE2 . TRP   B 80  ? 1.1768 0.8721 0.4671 0.5810 -0.0838 0.0480  89  TRP   B CE2 
904  C  CE3 . TRP   B 80  ? 1.1564 0.8667 0.4866 0.5269 -0.0696 0.0547  89  TRP   B CE3 
905  C  CZ2 . TRP   B 80  ? 1.1892 0.8946 0.4525 0.6146 -0.0791 0.0571  89  TRP   B CZ2 
906  C  CZ3 . TRP   B 80  ? 1.1723 0.8940 0.4785 0.5591 -0.0659 0.0636  89  TRP   B CZ3 
907  C  CH2 . TRP   B 80  ? 1.1771 0.8987 0.4521 0.6023 -0.0691 0.0657  89  TRP   B CH2 
908  N  N   . ASP   B 81  ? 1.2214 0.8011 0.5221 0.4931 -0.1531 -0.0004 90  ASP   B N   
909  C  CA  . ASP   B 81  ? 1.2792 0.8079 0.5374 0.5039 -0.1813 -0.0112 90  ASP   B CA  
910  C  C   . ASP   B 81  ? 1.3216 0.8442 0.5425 0.5324 -0.1790 -0.0052 90  ASP   B C   
911  O  O   . ASP   B 81  ? 1.3509 0.8300 0.5370 0.5383 -0.2000 -0.0126 90  ASP   B O   
912  C  CB  . ASP   B 81  ? 1.3139 0.8112 0.5461 0.5250 -0.2089 -0.0263 90  ASP   B CB  
913  C  CG  . ASP   B 81  ? 1.3794 0.8946 0.5902 0.5685 -0.2037 -0.0243 90  ASP   B CG  
914  O  OD1 . ASP   B 81  ? 1.3779 0.9286 0.5913 0.5852 -0.1788 -0.0098 90  ASP   B OD1 
915  O  OD2 . ASP   B 81  ? 1.4235 0.9183 0.6160 0.5861 -0.2247 -0.0367 90  ASP   B OD2 
916  N  N   . GLY   B 82  ? 1.3207 0.8868 0.5505 0.5498 -0.1540 0.0087  91  GLY   B N   
917  C  CA  . GLY   B 82  ? 1.3495 0.9219 0.5511 0.5789 -0.1481 0.0170  91  GLY   B CA  
918  C  C   . GLY   B 82  ? 1.3831 0.9494 0.5421 0.6299 -0.1554 0.0155  91  GLY   B C   
919  O  O   . GLY   B 82  ? 1.3895 0.9697 0.5270 0.6595 -0.1472 0.0246  91  GLY   B O   
920  N  N   . LEU   B 83  ? 1.4004 0.9471 0.5458 0.6426 -0.1713 0.0041  92  LEU   B N   
921  C  CA  . LEU   B 83  ? 1.4287 0.9651 0.5279 0.6935 -0.1805 0.0008  92  LEU   B CA  
922  C  C   . LEU   B 83  ? 1.4173 0.9879 0.5303 0.7104 -0.1658 0.0074  92  LEU   B C   
923  O  O   . LEU   B 83  ? 1.4211 1.0144 0.5136 0.7500 -0.1530 0.0180  92  LEU   B O   
924  C  CB  . LEU   B 83  ? 1.4755 0.9480 0.5305 0.7044 -0.2191 -0.0211 92  LEU   B CB  
925  C  CG  . LEU   B 83  ? 1.5309 0.9555 0.5576 0.6971 -0.2398 -0.0293 92  LEU   B CG  
926  C  CD1 . LEU   B 83  ? 1.5831 0.9444 0.5618 0.7165 -0.2787 -0.0508 92  LEU   B CD1 
927  C  CD2 . LEU   B 83  ? 1.5391 0.9760 0.5386 0.7277 -0.2277 -0.0182 92  LEU   B CD2 
928  N  N   . SER   B 84  ? 1.4016 0.9744 0.5464 0.6832 -0.1687 0.0012  93  SER   B N   
929  C  CA  . SER   B 84  ? 1.3851 0.9805 0.5385 0.6992 -0.1607 0.0039  93  SER   B CA  
930  C  C   . SER   B 84  ? 1.3336 0.9856 0.5256 0.6960 -0.1243 0.0255  93  SER   B C   
931  O  O   . SER   B 84  ? 1.3126 0.9894 0.5411 0.6664 -0.1052 0.0363  93  SER   B O   
932  C  CB  . SER   B 84  ? 1.4166 0.9939 0.5914 0.6709 -0.1787 -0.0109 93  SER   B CB  
933  O  OG  . SER   B 84  ? 1.4883 1.0122 0.6341 0.6674 -0.2136 -0.0303 93  SER   B OG  
934  N  N   . GLU   B 85  ? 1.3125 0.9824 0.4954 0.7270 -0.1160 0.0315  94  GLU   B N   
935  C  CA  . GLU   B 85  ? 1.2786 0.9974 0.4979 0.7252 -0.0838 0.0516  94  GLU   B CA  
936  C  C   . GLU   B 85  ? 1.2506 0.9769 0.5193 0.6808 -0.0803 0.0472  94  GLU   B C   
937  O  O   . GLU   B 85  ? 1.2670 0.9640 0.5351 0.6637 -0.1037 0.0292  94  GLU   B O   
938  C  CB  . GLU   B 85  ? 1.3006 1.0290 0.4903 0.7726 -0.0795 0.0578  94  GLU   B CB  
939  C  CG  . GLU   B 85  ? 1.3548 1.0915 0.5040 0.8188 -0.0721 0.0693  94  GLU   B CG  
940  C  CD  . GLU   B 85  ? 1.3953 1.1619 0.5322 0.8597 -0.0521 0.0869  94  GLU   B CD  
941  O  OE1 . GLU   B 85  ? 1.3948 1.1593 0.5337 0.8642 -0.0550 0.0830  94  GLU   B OE1 
942  O  OE2 . GLU   B 85  ? 1.3997 1.1933 0.5255 0.8877 -0.0328 0.1056  94  GLU   B OE2 
943  N  N   . VAL   B 86  ? 1.1972 0.9627 0.5094 0.6620 -0.0513 0.0640  95  VAL   B N   
944  C  CA  . VAL   B 86  ? 1.1496 0.9261 0.5080 0.6235 -0.0439 0.0622  95  VAL   B CA  
945  C  C   . VAL   B 86  ? 1.1171 0.9269 0.4964 0.6350 -0.0193 0.0786  95  VAL   B C   
946  O  O   . VAL   B 86  ? 1.1247 0.9509 0.4854 0.6696 -0.0068 0.0930  95  VAL   B O   
947  C  CB  . VAL   B 86  ? 1.1233 0.9086 0.5163 0.5815 -0.0338 0.0649  95  VAL   B CB  
948  C  CG1 . VAL   B 86  ? 1.1462 0.8995 0.5150 0.5742 -0.0549 0.0530  95  VAL   B CG1 
949  C  CG2 . VAL   B 86  ? 1.0998 0.9231 0.5152 0.5821 -0.0050 0.0862  95  VAL   B CG2 
950  N  N   . GLN   B 87  ? 1.0768 0.8968 0.4942 0.6074 -0.0116 0.0775  96  GLN   B N   
951  C  CA  . GLN   B 87  ? 1.0379 0.8865 0.4777 0.6143 0.0124  0.0938  96  GLN   B CA  
952  C  C   . GLN   B 87  ? 1.0021 0.8704 0.4906 0.5747 0.0321  0.1012  96  GLN   B C   
953  O  O   . GLN   B 87  ? 1.0062 0.8641 0.5141 0.5421 0.0239  0.0886  96  GLN   B O   
954  C  CB  . GLN   B 87  ? 1.0395 0.8797 0.4717 0.6289 0.0020  0.0854  96  GLN   B CB  
955  C  CG  . GLN   B 87  ? 1.0744 0.9031 0.4569 0.6775 -0.0100 0.0844  96  GLN   B CG  
956  C  CD  . GLN   B 87  ? 1.1222 0.9443 0.4954 0.6947 -0.0210 0.0765  96  GLN   B CD  
957  O  OE1 . GLN   B 87  ? 1.0873 0.9176 0.4937 0.6725 -0.0164 0.0745  96  GLN   B OE1 
958  N  NE2 . GLN   B 87  ? 1.1563 0.9632 0.4815 0.7376 -0.0365 0.0715  96  GLN   B NE2 
959  N  N   . LEU   B 88  ? 0.9640 0.8605 0.4721 0.5778 0.0578  0.1219  97  LEU   B N   
960  C  CA  . LEU   B 88  ? 0.9236 0.8371 0.4768 0.5437 0.0762  0.1290  97  LEU   B CA  
961  C  C   . LEU   B 88  ? 0.9195 0.8367 0.4867 0.5474 0.0838  0.1314  97  LEU   B C   
962  O  O   . LEU   B 88  ? 0.9196 0.8455 0.4732 0.5785 0.0922  0.1438  97  LEU   B O   
963  C  CB  . LEU   B 88  ? 0.8908 0.8324 0.4611 0.5455 0.0987  0.1511  97  LEU   B CB  
964  C  CG  . LEU   B 88  ? 0.8637 0.8228 0.4798 0.5167 0.1192  0.1614  97  LEU   B CG  
965  C  CD1 . LEU   B 88  ? 0.8613 0.8095 0.4982 0.4768 0.1122  0.1459  97  LEU   B CD1 
966  C  CD2 . LEU   B 88  ? 0.8478 0.8356 0.4821 0.5208 0.1394  0.1845  97  LEU   B CD2 
967  N  N   . LEU   B 89  ? 0.9066 0.8173 0.4980 0.5187 0.0806  0.1198  98  LEU   B N   
968  C  CA  . LEU   B 89  ? 0.8955 0.8110 0.5026 0.5212 0.0890  0.1224  98  LEU   B CA  
969  C  C   . LEU   B 89  ? 0.8809 0.8137 0.5237 0.5011 0.1138  0.1377  98  LEU   B C   
970  O  O   . LEU   B 89  ? 0.8675 0.7990 0.5368 0.4689 0.1166  0.1307  98  LEU   B O   
971  C  CB  . LEU   B 89  ? 0.8931 0.7949 0.5080 0.5037 0.0726  0.1026  98  LEU   B CB  
972  C  CG  . LEU   B 89  ? 0.8923 0.7999 0.5244 0.5063 0.0798  0.1035  98  LEU   B CG  
973  C  CD1 . LEU   B 89  ? 0.9113 0.8240 0.5233 0.5444 0.0858  0.1160  98  LEU   B CD1 
974  C  CD2 . LEU   B 89  ? 0.8976 0.7948 0.5316 0.4972 0.0593  0.0841  98  LEU   B CD2 
975  N  N   . ALA   B 90  ? 0.8720 0.8211 0.5143 0.5204 0.1311  0.1591  99  ALA   B N   
976  C  CA  . ALA   B 90  ? 0.8563 0.8219 0.5325 0.5033 0.1535  0.1762  99  ALA   B CA  
977  C  C   . ALA   B 90  ? 0.8531 0.8176 0.5519 0.4965 0.1658  0.1807  99  ALA   B C   
978  O  O   . ALA   B 90  ? 0.8711 0.8347 0.5568 0.5223 0.1689  0.1870  99  ALA   B O   
979  C  CB  . ALA   B 90  ? 0.8466 0.8323 0.5170 0.5271 0.1679  0.1997  99  ALA   B CB  
980  N  N   . VAL   B 91  ? 0.8287 0.7923 0.5596 0.4637 0.1732  0.1780  100 VAL   B N   
981  C  CA  . VAL   B 91  ? 0.8125 0.7726 0.5651 0.4569 0.1859  0.1829  100 VAL   B CA  
982  C  C   . VAL   B 91  ? 0.8005 0.7712 0.5828 0.4423 0.2052  0.2020  100 VAL   B C   
983  O  O   . VAL   B 91  ? 0.7946 0.7622 0.5992 0.4122 0.2062  0.1957  100 VAL   B O   
984  C  CB  . VAL   B 91  ? 0.8097 0.7564 0.5720 0.4347 0.1765  0.1616  100 VAL   B CB  
985  C  CG1 . VAL   B 91  ? 0.8120 0.7538 0.5947 0.4303 0.1901  0.1668  100 VAL   B CG1 
986  C  CG2 . VAL   B 91  ? 0.8186 0.7577 0.5563 0.4482 0.1565  0.1449  100 VAL   B CG2 
987  N  N   . PRO   B 92  ? 0.7966 0.7807 0.5786 0.4640 0.2200  0.2263  101 PRO   B N   
988  C  CA  . PRO   B 92  ? 0.7890 0.7856 0.6030 0.4488 0.2375  0.2467  101 PRO   B CA  
989  C  C   . PRO   B 92  ? 0.8035 0.7878 0.6445 0.4329 0.2496  0.2520  101 PRO   B C   
990  O  O   . PRO   B 92  ? 0.8196 0.7905 0.6510 0.4449 0.2499  0.2477  101 PRO   B O   
991  C  CB  . PRO   B 92  ? 0.7942 0.8113 0.5967 0.4807 0.2496  0.2723  101 PRO   B CB  
992  C  CG  . PRO   B 92  ? 0.8122 0.8234 0.5723 0.5145 0.2376  0.2633  101 PRO   B CG  
993  C  CD  . PRO   B 92  ? 0.8015 0.7903 0.5541 0.5035 0.2215  0.2369  101 PRO   B CD  
994  N  N   . PRO   B 93  ? 0.7996 0.7871 0.6742 0.4066 0.2585  0.2608  102 PRO   B N   
995  C  CA  . PRO   B 93  ? 0.8116 0.7817 0.7101 0.3912 0.2684  0.2646  102 PRO   B CA  
996  C  C   . PRO   B 93  ? 0.8329 0.8008 0.7303 0.4149 0.2847  0.2873  102 PRO   B C   
997  O  O   . PRO   B 93  ? 0.8342 0.8199 0.7376 0.4287 0.2982  0.3134  102 PRO   B O   
998  C  CB  . PRO   B 93  ? 0.8024 0.7780 0.7354 0.3604 0.2720  0.2708  102 PRO   B CB  
999  C  CG  . PRO   B 93  ? 0.7975 0.7885 0.7214 0.3540 0.2587  0.2593  102 PRO   B CG  
1000 C  CD  . PRO   B 93  ? 0.7816 0.7859 0.6735 0.3883 0.2569  0.2647  102 PRO   B CD  
1001 N  N   . GLY   B 94  ? 0.8425 0.7900 0.7310 0.4215 0.2838  0.2780  103 GLY   B N   
1002 C  CA  . GLY   B 94  ? 0.8447 0.7853 0.7286 0.4448 0.2979  0.2968  103 GLY   B CA  
1003 C  C   . GLY   B 94  ? 0.8584 0.8114 0.7087 0.4844 0.2977  0.3049  103 GLY   B C   
1004 O  O   . GLY   B 94  ? 0.8630 0.8134 0.7063 0.5079 0.3109  0.3243  103 GLY   B O   
1005 N  N   . GLU   B 95  ? 0.8690 0.8337 0.6963 0.4935 0.2827  0.2910  104 GLU   B N   
1006 C  CA  . GLU   B 95  ? 0.8907 0.8649 0.6817 0.5324 0.2790  0.2957  104 GLU   B CA  
1007 C  C   . GLU   B 95  ? 0.9150 0.8798 0.6800 0.5387 0.2557  0.2664  104 GLU   B C   
1008 O  O   . GLU   B 95  ? 0.9145 0.8722 0.6896 0.5119 0.2432  0.2446  104 GLU   B O   
1009 C  CB  . GLU   B 95  ? 0.9046 0.9025 0.6899 0.5424 0.2829  0.3103  104 GLU   B CB  
1010 C  CG  . GLU   B 95  ? 0.9346 0.9480 0.7455 0.5422 0.3074  0.3442  104 GLU   B CG  
1011 C  CD  . GLU   B 95  ? 0.9928 1.0347 0.8057 0.5485 0.3127  0.3596  104 GLU   B CD  
1012 O  OE1 . GLU   B 95  ? 1.0060 1.0533 0.7942 0.5574 0.2969  0.3437  104 GLU   B OE1 
1013 O  OE2 . GLU   B 95  ? 0.9956 1.0547 0.8362 0.5445 0.3327  0.3885  104 GLU   B OE2 
1014 N  N   . ARG   B 96  ? 0.9362 0.9013 0.6678 0.5742 0.2495  0.2662  105 ARG   B N   
1015 C  CA  . ARG   B 96  ? 0.9692 0.9255 0.6781 0.5816 0.2258  0.2396  105 ARG   B CA  
1016 C  C   . ARG   B 96  ? 0.9850 0.9446 0.6800 0.5750 0.2075  0.2235  105 ARG   B C   
1017 O  O   . ARG   B 96  ? 0.9813 0.9527 0.6697 0.5818 0.2126  0.2355  105 ARG   B O   
1018 C  CB  . ARG   B 96  ? 1.0112 0.9658 0.6872 0.6236 0.2229  0.2447  105 ARG   B CB  
1019 C  CG  . ARG   B 96  ? 1.0917 1.0362 0.7543 0.6294 0.2006  0.2194  105 ARG   B CG  
1020 C  CD  . ARG   B 96  ? 1.1801 1.1221 0.8159 0.6690 0.2000  0.2260  105 ARG   B CD  
1021 N  NE  . ARG   B 96  ? 1.2809 1.2298 0.8819 0.7048 0.2018  0.2398  105 ARG   B NE  
1022 C  CZ  . ARG   B 96  ? 1.3533 1.3082 0.9450 0.7306 0.2233  0.2677  105 ARG   B CZ  
1023 N  NH1 . ARG   B 96  ? 1.3566 1.3083 0.9709 0.7245 0.2434  0.2844  105 ARG   B NH1 
1024 N  NH2 . ARG   B 96  ? 1.3752 1.3384 0.9333 0.7645 0.2250  0.2796  105 ARG   B NH2 
1025 N  N   . ALA   B 97  ? 0.9949 0.9446 0.6860 0.5623 0.1864  0.1971  106 ALA   B N   
1026 C  CA  . ALA   B 97  ? 1.0101 0.9573 0.6859 0.5557 0.1662  0.1798  106 ALA   B CA  
1027 C  C   . ALA   B 97  ? 1.0283 0.9773 0.6644 0.5937 0.1578  0.1843  106 ALA   B C   
1028 O  O   . ALA   B 97  ? 1.0393 0.9855 0.6542 0.6236 0.1547  0.1863  106 ALA   B O   
1029 C  CB  . ALA   B 97  ? 1.0101 0.9467 0.6886 0.5409 0.1463  0.1546  106 ALA   B CB  
1030 N  N   . LYS   B 98  ? 1.0359 0.9891 0.6600 0.5949 0.1542  0.1860  107 LYS   B N   
1031 C  CA  . LYS   B 98  ? 1.0571 1.0117 0.6411 0.6333 0.1478  0.1911  107 LYS   B CA  
1032 C  C   . LYS   B 98  ? 1.0546 1.0015 0.6195 0.6293 0.1289  0.1767  107 LYS   B C   
1033 O  O   . LYS   B 98  ? 1.0495 1.0027 0.6339 0.6041 0.1340  0.1785  107 LYS   B O   
1034 C  CB  . LYS   B 98  ? 1.0914 1.0665 0.6804 0.6501 0.1745  0.2217  107 LYS   B CB  
1035 C  CG  . LYS   B 98  ? 1.1737 1.1558 0.7230 0.6912 0.1737  0.2319  107 LYS   B CG  
1036 C  CD  . LYS   B 98  ? 1.2383 1.2468 0.8028 0.7013 0.2035  0.2652  107 LYS   B CD  
1037 C  CE  . LYS   B 98  ? 1.2736 1.2953 0.8835 0.6608 0.2154  0.2723  107 LYS   B CE  
1038 N  NZ  . LYS   B 98  ? 1.2966 1.3461 0.9121 0.6727 0.2333  0.2977  107 LYS   B NZ  
1039 N  N   . ASN   B 99  ? 1.0596 0.9909 0.5853 0.6546 0.1058  0.1619  108 ASN   B N   
1040 C  CA  . ASN   B 99  ? 1.0670 0.9850 0.5699 0.6537 0.0855  0.1473  108 ASN   B CA  
1041 C  C   . ASN   B 99  ? 1.0849 1.0135 0.5610 0.6843 0.0940  0.1632  108 ASN   B C   
1042 O  O   . ASN   B 99  ? 1.1027 1.0353 0.5501 0.7236 0.0983  0.1736  108 ASN   B O   
1043 C  CB  . ASN   B 99  ? 1.0722 0.9651 0.5441 0.6674 0.0543  0.1236  108 ASN   B CB  
1044 C  CG  . ASN   B 99  ? 1.0579 0.9429 0.5541 0.6413 0.0426  0.1071  108 ASN   B CG  
1045 O  OD1 . ASN   B 99  ? 1.0603 0.9553 0.5763 0.6400 0.0545  0.1133  108 ASN   B OD1 
1046 N  ND2 . ASN   B 99  ? 1.0488 0.9155 0.5429 0.6221 0.0187  0.0865  108 ASN   B ND2 
1047 N  N   . ILE   B 100 ? 1.0848 1.0189 0.5688 0.6686 0.0965  0.1654  109 ILE   B N   
1048 C  CA  . ILE   B 100 ? 1.0994 1.0466 0.5608 0.6960 0.1040  0.1798  109 ILE   B CA  
1049 C  C   . ILE   B 100 ? 1.1201 1.0447 0.5520 0.6974 0.0791  0.1606  109 ILE   B C   
1050 O  O   . ILE   B 100 ? 1.1171 1.0365 0.5688 0.6637 0.0736  0.1517  109 ILE   B O   
1051 C  CB  . ILE   B 100 ? 1.0893 1.0673 0.5904 0.6762 0.1303  0.2021  109 ILE   B CB  
1052 C  CG1 . ILE   B 100 ? 1.0942 1.0895 0.6292 0.6682 0.1541  0.2207  109 ILE   B CG1 
1053 C  CG2 . ILE   B 100 ? 1.0971 1.0942 0.5775 0.7060 0.1387  0.2185  109 ILE   B CG2 
1054 C  CD1 . ILE   B 100 ? 1.1190 1.1218 0.6292 0.7115 0.1653  0.2374  109 ILE   B CD1 
1055 N  N   . GLN   B 101 ? 1.1432 1.0526 0.5257 0.7375 0.0639  0.1546  110 GLN   B N   
1056 C  CA  . GLN   B 101 ? 1.1727 1.0547 0.5215 0.7430 0.0382  0.1361  110 GLN   B CA  
1057 C  C   . GLN   B 101 ? 1.1730 1.0720 0.5151 0.7537 0.0494  0.1497  110 GLN   B C   
1058 O  O   . GLN   B 101 ? 1.1705 1.0977 0.5084 0.7817 0.0705  0.1722  110 GLN   B O   
1059 C  CB  . GLN   B 101 ? 1.2285 1.0830 0.5240 0.7835 0.0146  0.1219  110 GLN   B CB  
1060 C  CG  . GLN   B 101 ? 1.2922 1.1091 0.5509 0.7877 -0.0169 0.0994  110 GLN   B CG  
1061 C  CD  . GLN   B 101 ? 1.3505 1.1336 0.5713 0.8100 -0.0469 0.0783  110 GLN   B CD  
1062 O  OE1 . GLN   B 101 ? 1.3512 1.1365 0.5847 0.8070 -0.0485 0.0749  110 GLN   B OE1 
1063 N  NE2 . GLN   B 101 ? 1.3819 1.1315 0.5557 0.8324 -0.0730 0.0626  110 GLN   B NE2 
1064 N  N   . THR   B 102 ? 1.1691 1.0530 0.5116 0.7317 0.0359  0.1376  111 THR   B N   
1065 C  CA  . THR   B 102 ? 1.1703 1.0692 0.5065 0.7407 0.0434  0.1483  111 THR   B CA  
1066 C  C   . THR   B 102 ? 1.1887 1.0521 0.4986 0.7328 0.0166  0.1275  111 THR   B C   
1067 O  O   . THR   B 102 ? 1.2062 1.0386 0.5169 0.7089 -0.0037 0.1075  111 THR   B O   
1068 C  CB  . THR   B 102 ? 1.1622 1.0986 0.5534 0.7077 0.0692  0.1666  111 THR   B CB  
1069 O  OG1 . THR   B 102 ? 1.1718 1.1293 0.5576 0.7217 0.0773  0.1794  111 THR   B OG1 
1070 C  CG2 . THR   B 102 ? 1.1527 1.0768 0.5792 0.6563 0.0626  0.1528  111 THR   B CG2 
1071 N  N   . LEU   B 103 ? 1.1864 1.0546 0.4735 0.7535 0.0167  0.1332  112 LEU   B N   
1072 C  CA  . LEU   B 103 ? 1.1993 1.0333 0.4626 0.7452 -0.0067 0.1159  112 LEU   B CA  
1073 C  C   . LEU   B 103 ? 1.1734 1.0317 0.4760 0.7115 0.0070  0.1251  112 LEU   B C   
1074 O  O   . LEU   B 103 ? 1.1544 1.0512 0.4713 0.7227 0.0275  0.1450  112 LEU   B O   
1075 C  CB  . LEU   B 103 ? 1.2295 1.0446 0.4345 0.7925 -0.0205 0.1122  112 LEU   B CB  
1076 C  CG  . LEU   B 103 ? 1.2763 1.0550 0.4585 0.7820 -0.0434 0.0964  112 LEU   B CG  
1077 C  CD1 . LEU   B 103 ? 1.3079 1.0334 0.4699 0.7683 -0.0747 0.0709  112 LEU   B CD1 
1078 C  CD2 . LEU   B 103 ? 1.3060 1.0818 0.4424 0.8268 -0.0469 0.1005  112 LEU   B CD2 
1079 N  N   . PRO   B 104 ? 1.1666 1.0034 0.4869 0.6708 -0.0048 0.1110  113 PRO   B N   
1080 C  CA  . PRO   B 104 ? 1.1414 0.9990 0.4965 0.6388 0.0066  0.1180  113 PRO   B CA  
1081 C  C   . PRO   B 104 ? 1.1494 1.0099 0.4831 0.6547 0.0033  0.1221  113 PRO   B C   
1082 O  O   . PRO   B 104 ? 1.1725 1.0013 0.4594 0.6805 -0.0159 0.1120  113 PRO   B O   
1083 C  CB  . PRO   B 104 ? 1.1494 0.9785 0.5195 0.5972 -0.0070 0.1008  113 PRO   B CB  
1084 C  CG  . PRO   B 104 ? 1.1656 0.9720 0.5247 0.6027 -0.0190 0.0892  113 PRO   B CG  
1085 C  CD  . PRO   B 104 ? 1.1690 0.9652 0.4820 0.6509 -0.0276 0.0895  113 PRO   B CD  
1086 N  N   . GLY   B 105 ? 1.1242 1.0224 0.4935 0.6387 0.0213  0.1367  114 GLY   B N   
1087 C  CA  . GLY   B 105 ? 1.1294 1.0376 0.4899 0.6458 0.0199  0.1415  114 GLY   B CA  
1088 C  C   . GLY   B 105 ? 1.1427 1.0259 0.5096 0.6087 0.0068  0.1278  114 GLY   B C   
1089 O  O   . GLY   B 105 ? 1.1595 1.0081 0.5229 0.5868 -0.0062 0.1123  114 GLY   B O   
1090 N  N   . ILE   B 106 ? 1.1288 1.0303 0.5052 0.6020 0.0102  0.1341  115 ILE   B N   
1091 C  CA  . ILE   B 106 ? 1.1375 1.0163 0.5153 0.5709 -0.0014 0.1229  115 ILE   B CA  
1092 C  C   . ILE   B 106 ? 1.1051 1.0242 0.5231 0.5492 0.0127  0.1340  115 ILE   B C   
1093 O  O   . ILE   B 106 ? 1.0872 1.0437 0.5135 0.5688 0.0229  0.1487  115 ILE   B O   
1094 C  CB  . ILE   B 106 ? 1.1818 1.0244 0.5082 0.5941 -0.0220 0.1142  115 ILE   B CB  
1095 C  CG1 . ILE   B 106 ? 1.2318 1.0278 0.5128 0.6177 -0.0410 0.1009  115 ILE   B CG1 
1096 C  CG2 . ILE   B 106 ? 1.1958 1.0170 0.5220 0.5643 -0.0323 0.1058  115 ILE   B CG2 
1097 C  CD1 . ILE   B 106 ? 1.2654 1.0203 0.5459 0.5883 -0.0555 0.0847  115 ILE   B CD1 
1098 N  N   . PHE   B 107 ? 1.0967 1.0068 0.5369 0.5099 0.0113  0.1261  116 PHE   B N   
1099 C  CA  . PHE   B 107 ? 1.0725 1.0102 0.5432 0.4871 0.0184  0.1316  116 PHE   B CA  
1100 C  C   . PHE   B 107 ? 1.0937 0.9996 0.5323 0.4836 0.0010  0.1213  116 PHE   B C   
1101 O  O   . PHE   B 107 ? 1.1100 0.9761 0.5329 0.4665 -0.0102 0.1082  116 PHE   B O   
1102 C  CB  . PHE   B 107 ? 1.0493 0.9914 0.5584 0.4481 0.0268  0.1277  116 PHE   B CB  
1103 C  CG  . PHE   B 107 ? 1.0201 1.0018 0.5726 0.4427 0.0463  0.1408  116 PHE   B CG  
1104 C  CD1 . PHE   B 107 ? 1.0108 1.0226 0.5678 0.4720 0.0570  0.1568  116 PHE   B CD1 
1105 C  CD2 . PHE   B 107 ? 1.0132 1.0004 0.6009 0.4093 0.0542  0.1379  116 PHE   B CD2 
1106 C  CE1 . PHE   B 107 ? 0.9943 1.0404 0.5922 0.4657 0.0755  0.1710  116 PHE   B CE1 
1107 C  CE2 . PHE   B 107 ? 0.9976 1.0162 0.6243 0.4038 0.0710  0.1502  116 PHE   B CE2 
1108 C  CZ  . PHE   B 107 ? 0.9838 1.0313 0.6165 0.4310 0.0817  0.1673  116 PHE   B CZ  
1109 N  N   . LYS   B 108 ? 1.0929 1.0160 0.5214 0.5010 -0.0012 0.1282  117 LYS   B N   
1110 C  CA  . LYS   B 108 ? 1.1187 1.0124 0.5161 0.4990 -0.0170 0.1200  117 LYS   B CA  
1111 C  C   . LYS   B 108 ? 1.0920 1.0058 0.5198 0.4676 -0.0126 0.1206  117 LYS   B C   
1112 O  O   . LYS   B 108 ? 1.0619 1.0222 0.5223 0.4673 -0.0020 0.1317  117 LYS   B O   
1113 C  CB  . LYS   B 108 ? 1.1656 1.0661 0.5318 0.5383 -0.0231 0.1265  117 LYS   B CB  
1114 C  CG  . LYS   B 108 ? 1.2656 1.1418 0.5931 0.5747 -0.0299 0.1244  117 LYS   B CG  
1115 C  CD  . LYS   B 108 ? 1.3596 1.2443 0.6550 0.6161 -0.0348 0.1310  117 LYS   B CD  
1116 C  CE  . LYS   B 108 ? 1.4004 1.3346 0.7109 0.6472 -0.0182 0.1476  117 LYS   B CE  
1117 N  NZ  . LYS   B 108 ? 1.4452 1.3921 0.7252 0.6899 -0.0216 0.1551  117 LYS   B NZ  
1118 N  N   . THR   B 109 ? 1.1020 0.9817 0.5205 0.4409 -0.0208 0.1091  118 THR   B N   
1119 C  CA  . THR   B 109 ? 1.0969 0.9888 0.5369 0.4118 -0.0184 0.1073  118 THR   B CA  
1120 C  C   . THR   B 109 ? 1.1356 0.9942 0.5385 0.4113 -0.0332 0.1011  118 THR   B C   
1121 O  O   . THR   B 109 ? 1.1704 0.9861 0.5350 0.4226 -0.0451 0.0955  118 THR   B O   
1122 C  CB  . THR   B 109 ? 1.0962 0.9810 0.5621 0.3781 -0.0109 0.1005  118 THR   B CB  
1123 O  OG1 . THR   B 109 ? 1.1282 0.9657 0.5669 0.3685 -0.0205 0.0902  118 THR   B OG1 
1124 C  CG2 . THR   B 109 ? 1.0751 0.9841 0.5730 0.3791 0.0029  0.1060  118 THR   B CG2 
1125 N  N   . LYS   B 110 ? 1.1274 1.0023 0.5410 0.3967 -0.0334 0.1015  119 LYS   B N   
1126 C  CA  . LYS   B 110 ? 1.1560 0.9997 0.5342 0.3952 -0.0462 0.0968  119 LYS   B CA  
1127 C  C   . LYS   B 110 ? 1.1874 0.9807 0.5443 0.3753 -0.0515 0.0877  119 LYS   B C   
1128 O  O   . LYS   B 110 ? 1.2143 0.9732 0.5365 0.3763 -0.0625 0.0853  119 LYS   B O   
1129 C  CB  . LYS   B 110 ? 1.1499 1.0224 0.5459 0.3813 -0.0452 0.0980  119 LYS   B CB  
1130 C  CG  . LYS   B 110 ? 1.1816 1.0619 0.6087 0.3467 -0.0365 0.0925  119 LYS   B CG  
1131 C  CD  . LYS   B 110 ? 1.2247 1.1271 0.6623 0.3348 -0.0393 0.0913  119 LYS   B CD  
1132 C  CE  . LYS   B 110 ? 1.2667 1.1637 0.7203 0.3030 -0.0337 0.0831  119 LYS   B CE  
1133 N  NZ  . LYS   B 110 ? 1.2714 1.1978 0.7706 0.2896 -0.0217 0.0838  119 LYS   B NZ  
1134 N  N   . ASP   B 111 ? 1.1760 0.9659 0.5547 0.3574 -0.0434 0.0840  120 ASP   B N   
1135 C  CA  . ASP   B 111 ? 1.2004 0.9497 0.5664 0.3375 -0.0470 0.0770  120 ASP   B CA  
1136 C  C   . ASP   B 111 ? 1.2174 0.9404 0.5723 0.3471 -0.0525 0.0738  120 ASP   B C   
1137 O  O   . ASP   B 111 ? 1.2339 0.9299 0.5878 0.3283 -0.0545 0.0687  120 ASP   B O   
1138 C  CB  . ASP   B 111 ? 1.2132 0.9769 0.6111 0.3061 -0.0349 0.0737  120 ASP   B CB  
1139 C  CG  . ASP   B 111 ? 1.2844 1.0668 0.6879 0.2953 -0.0326 0.0743  120 ASP   B CG  
1140 O  OD1 . ASP   B 111 ? 1.3206 1.0799 0.6934 0.2960 -0.0414 0.0740  120 ASP   B OD1 
1141 O  OD2 . ASP   B 111 ? 1.2936 1.1119 0.7309 0.2865 -0.0232 0.0749  120 ASP   B OD2 
1142 N  N   . GLY   B 112 ? 1.2131 0.9444 0.5595 0.3767 -0.0555 0.0769  121 GLY   B N   
1143 C  CA  . GLY   B 112 ? 1.2285 0.9340 0.5603 0.3898 -0.0631 0.0726  121 GLY   B CA  
1144 C  C   . GLY   B 112 ? 1.2124 0.9508 0.5646 0.4077 -0.0533 0.0771  121 GLY   B C   
1145 O  O   . GLY   B 112 ? 1.1873 0.9691 0.5737 0.4024 -0.0382 0.0839  121 GLY   B O   
1146 N  N   . ASP   B 113 ? 1.2263 0.9431 0.5570 0.4293 -0.0624 0.0735  122 ASP   B N   
1147 C  CA  . ASP   B 113 ? 1.2185 0.9627 0.5620 0.4506 -0.0535 0.0784  122 ASP   B CA  
1148 C  C   . ASP   B 113 ? 1.2016 0.9471 0.5716 0.4315 -0.0473 0.0741  122 ASP   B C   
1149 O  O   . ASP   B 113 ? 1.2242 0.9363 0.5877 0.4137 -0.0573 0.0648  122 ASP   B O   
1150 C  CB  . ASP   B 113 ? 1.2715 0.9907 0.5720 0.4894 -0.0677 0.0760  122 ASP   B CB  
1151 C  CG  . ASP   B 113 ? 1.3583 1.0821 0.6311 0.5181 -0.0721 0.0818  122 ASP   B CG  
1152 O  OD1 . ASP   B 113 ? 1.3620 1.1019 0.6454 0.5053 -0.0678 0.0863  122 ASP   B OD1 
1153 O  OD2 . ASP   B 113 ? 1.4182 1.1298 0.6574 0.5549 -0.0803 0.0814  122 ASP   B OD2 
1154 N  N   . ILE   B 114 ? 1.1571 0.9413 0.5575 0.4358 -0.0309 0.0820  123 ILE   B N   
1155 C  CA  . ILE   B 114 ? 1.1296 0.9193 0.5562 0.4216 -0.0232 0.0793  123 ILE   B CA  
1156 C  C   . ILE   B 114 ? 1.1006 0.9083 0.5250 0.4527 -0.0173 0.0862  123 ILE   B C   
1157 O  O   . ILE   B 114 ? 1.0821 0.9175 0.5062 0.4748 -0.0091 0.0976  123 ILE   B O   
1158 C  CB  . ILE   B 114 ? 1.1139 0.9343 0.5850 0.3908 -0.0057 0.0834  123 ILE   B CB  
1159 C  CG1 . ILE   B 114 ? 1.1393 0.9518 0.6105 0.3664 -0.0085 0.0799  123 ILE   B CG1 
1160 C  CG2 . ILE   B 114 ? 1.1103 0.9294 0.6047 0.3736 0.0002  0.0787  123 ILE   B CG2 
1161 C  CD1 . ILE   B 114 ? 1.1357 0.9811 0.6449 0.3437 0.0069  0.0843  123 ILE   B CD1 
1162 N  N   . GLY   B 115 ? 1.0940 0.8898 0.5195 0.4542 -0.0200 0.0805  124 GLY   B N   
1163 C  CA  . GLY   B 115 ? 1.0833 0.8963 0.5066 0.4835 -0.0130 0.0876  124 GLY   B CA  
1164 C  C   . GLY   B 115 ? 1.0475 0.9070 0.5117 0.4775 0.0112  0.1027  124 GLY   B C   
1165 O  O   . GLY   B 115 ? 1.0339 0.9068 0.5306 0.4463 0.0204  0.1036  124 GLY   B O   
1166 N  N   . ALA   B 116 ? 1.0352 0.9184 0.4972 0.5075 0.0214  0.1152  125 ALA   B N   
1167 C  CA  . ALA   B 116 ? 1.0134 0.9401 0.5155 0.5027 0.0446  0.1321  125 ALA   B CA  
1168 C  C   . ALA   B 116 ? 1.0184 0.9573 0.5174 0.5307 0.0543  0.1417  125 ALA   B C   
1169 O  O   . ALA   B 116 ? 1.0383 0.9645 0.4996 0.5650 0.0456  0.1404  125 ALA   B O   
1170 C  CB  . ALA   B 116 ? 0.9940 0.9519 0.5058 0.5086 0.0525  0.1453  125 ALA   B CB  
1171 N  N   . VAL   B 117 ? 1.0012 0.9619 0.5366 0.5174 0.0716  0.1510  126 VAL   B N   
1172 C  CA  A VAL   B 117 ? 1.0087 0.9812 0.5420 0.5432 0.0825  0.1620  126 VAL   B CA  
1173 C  CA  B VAL   B 117 ? 1.0053 0.9778 0.5391 0.5427 0.0825  0.1619  126 VAL   B CA  
1174 C  C   . VAL   B 117 ? 0.9902 1.0077 0.5553 0.5496 0.1066  0.1871  126 VAL   B C   
1175 O  O   . VAL   B 117 ? 0.9635 0.9997 0.5705 0.5200 0.1183  0.1936  126 VAL   B O   
1176 C  CB  A VAL   B 117 ? 1.0236 0.9783 0.5654 0.5300 0.0806  0.1522  126 VAL   B CB  
1177 C  CB  B VAL   B 117 ? 1.0120 0.9671 0.5571 0.5261 0.0809  0.1518  126 VAL   B CB  
1178 C  CG1 A VAL   B 117 ? 1.0561 0.9718 0.5580 0.5423 0.0567  0.1328  126 VAL   B CG1 
1179 C  CG1 B VAL   B 117 ? 1.0100 0.9817 0.5607 0.5482 0.0961  0.1661  126 VAL   B CG1 
1180 C  CG2 A VAL   B 117 ? 1.0224 0.9775 0.6022 0.4866 0.0852  0.1463  126 VAL   B CG2 
1181 C  CG2 B VAL   B 117 ? 1.0412 0.9555 0.5527 0.5277 0.0563  0.1300  126 VAL   B CG2 
1182 N  N   . ALA   B 118 ? 1.0046 1.0396 0.5491 0.5893 0.1136  0.2018  127 ALA   B N   
1183 C  CA  . ALA   B 118 ? 0.9988 1.0801 0.5745 0.5974 0.1373  0.2288  127 ALA   B CA  
1184 C  C   . ALA   B 118 ? 1.0080 1.1031 0.5975 0.6091 0.1556  0.2448  127 ALA   B C   
1185 O  O   . ALA   B 118 ? 1.0240 1.1326 0.5915 0.6479 0.1641  0.2590  127 ALA   B O   
1186 C  CB  . ALA   B 118 ? 1.0030 1.1038 0.5540 0.6328 0.1380  0.2396  127 ALA   B CB  
1187 N  N   . LEU   B 119 ? 0.9934 1.0846 0.6175 0.5774 0.1623  0.2433  128 LEU   B N   
1188 C  CA  . LEU   B 119 ? 0.9874 1.0880 0.6267 0.5850 0.1797  0.2585  128 LEU   B CA  
1189 C  C   . LEU   B 119 ? 0.9623 1.0859 0.6580 0.5515 0.1973  0.2731  128 LEU   B C   
1190 O  O   . LEU   B 119 ? 0.9574 1.0726 0.6760 0.5152 0.1904  0.2606  128 LEU   B O   
1191 C  CB  . LEU   B 119 ? 1.0077 1.0722 0.6255 0.5852 0.1673  0.2393  128 LEU   B CB  
1192 C  CG  . LEU   B 119 ? 1.0543 1.0947 0.6170 0.6206 0.1489  0.2260  128 LEU   B CG  
1193 C  CD1 . LEU   B 119 ? 1.0708 1.0764 0.6193 0.6126 0.1322  0.2038  128 LEU   B CD1 
1194 C  CD2 . LEU   B 119 ? 1.0690 1.1292 0.6083 0.6673 0.1621  0.2467  128 LEU   B CD2 
1195 N  N   . ASP   B 120 ? 0.9453 1.0963 0.6621 0.5641 0.2196  0.2999  129 ASP   B N   
1196 C  CA  . ASP   B 120 ? 0.9271 1.0989 0.6984 0.5342 0.2363  0.3167  129 ASP   B CA  
1197 C  C   . ASP   B 120 ? 0.9158 1.0671 0.7022 0.5187 0.2424  0.3145  129 ASP   B C   
1198 O  O   . ASP   B 120 ? 0.9238 1.0763 0.7014 0.5419 0.2548  0.3287  129 ASP   B O   
1199 C  CB  . ASP   B 120 ? 0.9525 1.1686 0.7452 0.5533 0.2586  0.3507  129 ASP   B CB  
1200 C  CG  . ASP   B 120 ? 1.0420 1.2895 0.8434 0.5558 0.2569  0.3576  129 ASP   B CG  
1201 O  OD1 . ASP   B 120 ? 1.0513 1.3407 0.8827 0.5632 0.2758  0.3866  129 ASP   B OD1 
1202 O  OD2 . ASP   B 120 ? 1.0954 1.3266 0.8739 0.5513 0.2370  0.3353  129 ASP   B OD2 
1203 N  N   . TYR   B 121 ? 0.8957 1.0295 0.7046 0.4808 0.2347  0.2982  130 TYR   B N   
1204 C  CA  . TYR   B 121 ? 0.8846 0.9979 0.7086 0.4645 0.2395  0.2943  130 TYR   B CA  
1205 C  C   . TYR   B 121 ? 0.8502 0.9641 0.7181 0.4235 0.2418  0.2928  130 TYR   B C   
1206 O  O   . TYR   B 121 ? 0.8461 0.9639 0.7219 0.4038 0.2313  0.2820  130 TYR   B O   
1207 C  CB  . TYR   B 121 ? 0.9117 0.9905 0.7029 0.4660 0.2217  0.2666  130 TYR   B CB  
1208 C  CG  . TYR   B 121 ? 0.9443 1.0151 0.6977 0.5041 0.2204  0.2680  130 TYR   B CG  
1209 C  CD1 . TYR   B 121 ? 0.9621 1.0290 0.7189 0.5159 0.2328  0.2792  130 TYR   B CD1 
1210 C  CD2 . TYR   B 121 ? 0.9750 1.0392 0.6869 0.5291 0.2051  0.2571  130 TYR   B CD2 
1211 C  CE1 . TYR   B 121 ? 0.9914 1.0502 0.7110 0.5523 0.2298  0.2792  130 TYR   B CE1 
1212 C  CE2 . TYR   B 121 ? 1.0068 1.0612 0.6814 0.5651 0.2011  0.2564  130 TYR   B CE2 
1213 C  CZ  . TYR   B 121 ? 1.0245 1.0774 0.7030 0.5768 0.2133  0.2672  130 TYR   B CZ  
1214 O  OH  . TYR   B 121 ? 1.0711 1.1141 0.7110 0.6136 0.2079  0.2654  130 TYR   B OH  
1215 N  N   . PRO   B 122 ? 0.8233 0.9297 0.7172 0.4107 0.2539  0.3017  131 PRO   B N   
1216 C  CA  . PRO   B 122 ? 0.7946 0.8966 0.7281 0.3721 0.2541  0.2983  131 PRO   B CA  
1217 C  C   . PRO   B 122 ? 0.7763 0.8530 0.6996 0.3484 0.2356  0.2672  131 PRO   B C   
1218 O  O   . PRO   B 122 ? 0.7906 0.8475 0.6819 0.3585 0.2255  0.2492  131 PRO   B O   
1219 C  CB  . PRO   B 122 ? 0.8075 0.8979 0.7601 0.3696 0.2692  0.3119  131 PRO   B CB  
1220 C  CG  . PRO   B 122 ? 0.8331 0.9144 0.7498 0.4039 0.2723  0.3132  131 PRO   B CG  
1221 C  CD  . PRO   B 122 ? 0.8206 0.9209 0.7075 0.4323 0.2675  0.3158  131 PRO   B CD  
1222 N  N   . ALA   B 123 ? 0.7403 0.8195 0.6910 0.3176 0.2307  0.2616  132 ALA   B N   
1223 C  CA  . ALA   B 123 ? 0.7269 0.7853 0.6701 0.2940 0.2148  0.2345  132 ALA   B CA  
1224 C  C   . ALA   B 123 ? 0.7290 0.7552 0.6559 0.2907 0.2114  0.2158  132 ALA   B C   
1225 O  O   . ALA   B 123 ? 0.7338 0.7451 0.6386 0.2853 0.1984  0.1944  132 ALA   B O   
1226 C  CB  . ALA   B 123 ? 0.7050 0.7691 0.6841 0.2632 0.2130  0.2350  132 ALA   B CB  
1227 N  N   . GLY   B 124 ? 0.7187 0.7357 0.6558 0.2959 0.2235  0.2256  133 GLY   B N   
1228 C  CA  . GLY   B 124 ? 0.7179 0.7086 0.6421 0.2962 0.2218  0.2106  133 GLY   B CA  
1229 C  C   . GLY   B 124 ? 0.7131 0.6990 0.6017 0.3195 0.2141  0.2005  133 GLY   B C   
1230 O  O   . GLY   B 124 ? 0.7163 0.6845 0.5947 0.3212 0.2113  0.1878  133 GLY   B O   
1231 N  N   . THR   B 125 ? 0.7024 0.7041 0.5721 0.3385 0.2096  0.2060  134 THR   B N   
1232 C  CA  . THR   B 125 ? 0.7148 0.7101 0.5491 0.3610 0.1989  0.1960  134 THR   B CA  
1233 C  C   . THR   B 125 ? 0.7117 0.6970 0.5301 0.3470 0.1814  0.1742  134 THR   B C   
1234 O  O   . THR   B 125 ? 0.7299 0.7059 0.5211 0.3606 0.1698  0.1634  134 THR   B O   
1235 C  CB  . THR   B 125 ? 0.7398 0.7527 0.5566 0.3946 0.2036  0.2140  134 THR   B CB  
1236 O  OG1 . THR   B 125 ? 0.7450 0.7734 0.5846 0.4014 0.2228  0.2393  134 THR   B OG1 
1237 C  CG2 . THR   B 125 ? 0.7615 0.7631 0.5440 0.4228 0.1955  0.2068  134 THR   B CG2 
1238 N  N   . SER   B 126 ? 0.6904 0.6765 0.5249 0.3200 0.1788  0.1678  135 SER   B N   
1239 C  CA  . SER   B 126 ? 0.6999 0.6768 0.5194 0.3065 0.1641  0.1498  135 SER   B CA  
1240 C  C   . SER   B 126 ? 0.6950 0.6520 0.5021 0.3018 0.1570  0.1322  135 SER   B C   
1241 O  O   . SER   B 126 ? 0.6994 0.6487 0.5216 0.2911 0.1635  0.1284  135 SER   B O   
1242 C  CB  . SER   B 126 ? 0.7310 0.7099 0.5711 0.2786 0.1640  0.1457  135 SER   B CB  
1243 O  OG  . SER   B 126 ? 0.7632 0.7637 0.6193 0.2778 0.1676  0.1602  135 SER   B OG  
1244 N  N   . GLY   B 127 ? 0.6870 0.6357 0.4688 0.3077 0.1432  0.1214  136 GLY   B N   
1245 C  CA  . GLY   B 127 ? 0.6924 0.6257 0.4648 0.3023 0.1350  0.1058  136 GLY   B CA  
1246 C  C   . GLY   B 127 ? 0.7050 0.6343 0.4593 0.3268 0.1283  0.1055  136 GLY   B C   
1247 O  O   . GLY   B 127 ? 0.7131 0.6317 0.4598 0.3236 0.1182  0.0929  136 GLY   B O   
1248 N  N   . SER   B 128 ? 0.6991 0.6380 0.4468 0.3523 0.1336  0.1199  137 SER   B N   
1249 C  CA  . SER   B 128 ? 0.7107 0.6455 0.4367 0.3801 0.1263  0.1200  137 SER   B CA  
1250 C  C   . SER   B 128 ? 0.7300 0.6512 0.4284 0.3841 0.1059  0.1072  137 SER   B C   
1251 O  O   . SER   B 128 ? 0.7192 0.6403 0.4080 0.3805 0.1011  0.1076  137 SER   B O   
1252 C  CB  . SER   B 128 ? 0.7199 0.6687 0.4398 0.4074 0.1367  0.1393  137 SER   B CB  
1253 O  OG  . SER   B 128 ? 0.7282 0.6853 0.4721 0.4060 0.1545  0.1519  137 SER   B OG  
1254 N  N   . PRO   B 129 ? 0.7498 0.6588 0.4376 0.3894 0.0928  0.0953  138 PRO   B N   
1255 C  CA  . PRO   B 129 ? 0.7767 0.6687 0.4403 0.3905 0.0714  0.0828  138 PRO   B CA  
1256 C  C   . PRO   B 129 ? 0.8168 0.7030 0.4466 0.4220 0.0611  0.0864  138 PRO   B C   
1257 O  O   . PRO   B 129 ? 0.8179 0.7121 0.4382 0.4499 0.0670  0.0961  138 PRO   B O   
1258 C  CB  . PRO   B 129 ? 0.7808 0.6647 0.4499 0.3849 0.0609  0.0702  138 PRO   B CB  
1259 C  CG  . PRO   B 129 ? 0.7740 0.6700 0.4565 0.3979 0.0739  0.0777  138 PRO   B CG  
1260 C  CD  . PRO   B 129 ? 0.7395 0.6494 0.4381 0.3944 0.0956  0.0928  138 PRO   B CD  
1261 N  N   . ILE   B 130 ? 0.8344 0.7044 0.4432 0.4187 0.0451  0.0782  139 ILE   B N   
1262 C  CA  . ILE   B 130 ? 0.8659 0.7232 0.4373 0.4475 0.0307  0.0773  139 ILE   B CA  
1263 C  C   . ILE   B 130 ? 0.9003 0.7316 0.4544 0.4482 0.0058  0.0603  139 ILE   B C   
1264 O  O   . ILE   B 130 ? 0.8845 0.7054 0.4513 0.4202 -0.0020 0.0505  139 ILE   B O   
1265 C  CB  . ILE   B 130 ? 0.8696 0.7263 0.4292 0.4455 0.0305  0.0815  139 ILE   B CB  
1266 C  CG1 . ILE   B 130 ? 0.8591 0.7455 0.4412 0.4442 0.0541  0.0991  139 ILE   B CG1 
1267 C  CG2 . ILE   B 130 ? 0.8964 0.7355 0.4128 0.4779 0.0136  0.0785  139 ILE   B CG2 
1268 C  CD1 . ILE   B 130 ? 0.8735 0.7640 0.4577 0.4289 0.0552  0.1013  139 ILE   B CD1 
1269 N  N   . LEU   B 131 ? 0.9411 0.7626 0.4673 0.4803 -0.0068 0.0573  140 LEU   B N   
1270 C  CA  . LEU   B 131 ? 0.9864 0.7842 0.4987 0.4830 -0.0326 0.0408  140 LEU   B CA  
1271 C  C   . LEU   B 131 ? 1.0423 0.8100 0.5116 0.5043 -0.0579 0.0312  140 LEU   B C   
1272 O  O   . LEU   B 131 ? 1.0616 0.8290 0.5014 0.5350 -0.0556 0.0381  140 LEU   B O   
1273 C  CB  . LEU   B 131 ? 0.9859 0.7937 0.5019 0.5022 -0.0313 0.0412  140 LEU   B CB  
1274 C  CG  . LEU   B 131 ? 0.9842 0.8188 0.5382 0.4885 -0.0069 0.0510  140 LEU   B CG  
1275 C  CD1 . LEU   B 131 ? 0.9845 0.8230 0.5388 0.5065 -0.0117 0.0479  140 LEU   B CD1 
1276 C  CD2 . LEU   B 131 ? 0.9771 0.8159 0.5665 0.4467 -0.0017 0.0461  140 LEU   B CD2 
1277 N  N   . ASP   B 132 ? 1.0616 0.8034 0.5277 0.4892 -0.0827 0.0152  141 ASP   B N   
1278 C  CA  . ASP   B 132 ? 1.0983 0.8042 0.5228 0.5086 -0.1117 0.0031  141 ASP   B CA  
1279 C  C   . ASP   B 132 ? 1.1310 0.8288 0.5378 0.5364 -0.1296 -0.0064 141 ASP   B C   
1280 O  O   . ASP   B 132 ? 1.1106 0.8321 0.5405 0.5372 -0.1180 -0.0024 141 ASP   B O   
1281 C  CB  . ASP   B 132 ? 1.1089 0.7875 0.5373 0.4773 -0.1298 -0.0073 141 ASP   B CB  
1282 C  CG  . ASP   B 132 ? 1.1309 0.7996 0.5825 0.4526 -0.1481 -0.0196 141 ASP   B CG  
1283 O  OD1 . ASP   B 132 ? 1.1173 0.8052 0.5894 0.4549 -0.1449 -0.0208 141 ASP   B OD1 
1284 O  OD2 . ASP   B 132 ? 1.1543 0.7970 0.6051 0.4303 -0.1650 -0.0269 141 ASP   B OD2 
1285 N  N   . LYS   B 133 ? 1.1717 0.8349 0.5361 0.5604 -0.1584 -0.0192 142 LYS   B N   
1286 C  CA  . LYS   B 133 ? 1.1986 0.8523 0.5409 0.5904 -0.1777 -0.0293 142 LYS   B CA  
1287 C  C   . LYS   B 133 ? 1.1846 0.8416 0.5607 0.5665 -0.1915 -0.0403 142 LYS   B C   
1288 O  O   . LYS   B 133 ? 1.1889 0.8513 0.5584 0.5885 -0.1998 -0.0451 142 LYS   B O   
1289 C  CB  . LYS   B 133 ? 1.2725 0.8848 0.5587 0.6224 -0.2074 -0.0423 142 LYS   B CB  
1290 C  CG  . LYS   B 133 ? 1.3694 0.9878 0.6177 0.6616 -0.1915 -0.0298 142 LYS   B CG  
1291 C  CD  . LYS   B 133 ? 1.4597 1.0388 0.6624 0.6768 -0.2115 -0.0379 142 LYS   B CD  
1292 C  CE  . LYS   B 133 ? 1.5286 1.1077 0.6807 0.7312 -0.2072 -0.0320 142 LYS   B CE  
1293 N  NZ  . LYS   B 133 ? 1.5946 1.1344 0.6978 0.7515 -0.2270 -0.0405 142 LYS   B NZ  
1294 N  N   . CYS   B 134 ? 1.1640 0.8213 0.5771 0.5229 -0.1925 -0.0429 143 CYS   B N   
1295 C  CA  . CYS   B 134 ? 1.1411 0.8102 0.5936 0.4985 -0.2012 -0.0503 143 CYS   B CA  
1296 C  C   . CYS   B 134 ? 1.0847 0.7956 0.5793 0.4839 -0.1698 -0.0378 143 CYS   B C   
1297 O  O   . CYS   B 134 ? 1.0700 0.7950 0.5983 0.4657 -0.1741 -0.0425 143 CYS   B O   
1298 C  CB  . CYS   B 134 ? 1.1679 0.8167 0.6396 0.4608 -0.2199 -0.0591 143 CYS   B CB  
1299 S  SG  . CYS   B 134 ? 1.3049 0.8985 0.7268 0.4718 -0.2520 -0.0707 143 CYS   B SG  
1300 N  N   . GLY   B 135 ? 1.0567 0.7862 0.5509 0.4902 -0.1399 -0.0221 144 GLY   B N   
1301 C  CA  . GLY   B 135 ? 1.0259 0.7900 0.5569 0.4768 -0.1096 -0.0098 144 GLY   B CA  
1302 C  C   . GLY   B 135 ? 0.9962 0.7699 0.5614 0.4361 -0.0950 -0.0058 144 GLY   B C   
1303 O  O   . GLY   B 135 ? 0.9877 0.7868 0.5849 0.4220 -0.0733 0.0013  144 GLY   B O   
1304 N  N   . ARG   B 136 ? 0.9841 0.7359 0.5409 0.4182 -0.1067 -0.0104 145 ARG   B N   
1305 C  CA  . ARG   B 136 ? 0.9585 0.7171 0.5422 0.3816 -0.0932 -0.0062 145 ARG   B CA  
1306 C  C   . ARG   B 136 ? 0.9270 0.6975 0.5068 0.3835 -0.0684 0.0067  145 ARG   B C   
1307 O  O   . ARG   B 136 ? 0.9371 0.6984 0.4858 0.4074 -0.0696 0.0106  145 ARG   B O   
1308 C  CB  . ARG   B 136 ? 0.9965 0.7253 0.5709 0.3625 -0.1153 -0.0144 145 ARG   B CB  
1309 C  CG  . ARG   B 136 ? 1.0585 0.7788 0.6484 0.3509 -0.1395 -0.0262 145 ARG   B CG  
1310 C  CD  . ARG   B 136 ? 1.1281 0.8189 0.7143 0.3275 -0.1591 -0.0316 145 ARG   B CD  
1311 N  NE  . ARG   B 136 ? 1.2314 0.8851 0.7706 0.3494 -0.1779 -0.0364 145 ARG   B NE  
1312 C  CZ  . ARG   B 136 ? 1.3077 0.9347 0.8300 0.3374 -0.1836 -0.0353 145 ARG   B CZ  
1313 N  NH1 . ARG   B 136 ? 1.3059 0.9397 0.8541 0.3031 -0.1715 -0.0287 145 ARG   B NH1 
1314 N  NH2 . ARG   B 136 ? 1.3352 0.9282 0.8121 0.3618 -0.2009 -0.0402 145 ARG   B NH2 
1315 N  N   . VAL   B 137 ? 0.8905 0.6824 0.5018 0.3595 -0.0463 0.0132  146 VAL   B N   
1316 C  CA  . VAL   B 137 ? 0.8705 0.6747 0.4826 0.3584 -0.0244 0.0247  146 VAL   B CA  
1317 C  C   . VAL   B 137 ? 0.8801 0.6665 0.4753 0.3469 -0.0304 0.0243  146 VAL   B C   
1318 O  O   . VAL   B 137 ? 0.8876 0.6671 0.4947 0.3198 -0.0336 0.0203  146 VAL   B O   
1319 C  CB  . VAL   B 137 ? 0.8455 0.6747 0.4931 0.3395 -0.0007 0.0303  146 VAL   B CB  
1320 C  CG1 . VAL   B 137 ? 0.8448 0.6861 0.4939 0.3403 0.0191  0.0417  146 VAL   B CG1 
1321 C  CG2 . VAL   B 137 ? 0.8414 0.6850 0.5032 0.3527 0.0036  0.0305  146 VAL   B CG2 
1322 N  N   . ILE   B 138 ? 0.8776 0.6563 0.4436 0.3695 -0.0329 0.0288  147 ILE   B N   
1323 C  CA  . ILE   B 138 ? 0.8775 0.6401 0.4240 0.3639 -0.0383 0.0294  147 ILE   B CA  
1324 C  C   . ILE   B 138 ? 0.8655 0.6496 0.4271 0.3523 -0.0161 0.0399  147 ILE   B C   
1325 O  O   . ILE   B 138 ? 0.8808 0.6550 0.4290 0.3460 -0.0190 0.0410  147 ILE   B O   
1326 C  CB  . ILE   B 138 ? 0.8916 0.6331 0.3956 0.3968 -0.0548 0.0277  147 ILE   B CB  
1327 C  CG1 . ILE   B 138 ? 0.8941 0.6571 0.3907 0.4288 -0.0416 0.0379  147 ILE   B CG1 
1328 C  CG2 . ILE   B 138 ? 0.9132 0.6245 0.3993 0.4026 -0.0823 0.0142  147 ILE   B CG2 
1329 C  CD1 . ILE   B 138 ? 0.9272 0.6753 0.3809 0.4655 -0.0533 0.0384  147 ILE   B CD1 
1330 N  N   . GLY   B 139 ? 0.8298 0.6410 0.4178 0.3501 0.0040  0.0473  148 GLY   B N   
1331 C  CA  . GLY   B 139 ? 0.8184 0.6483 0.4227 0.3375 0.0222  0.0559  148 GLY   B CA  
1332 C  C   . GLY   B 139 ? 0.8012 0.6566 0.4293 0.3425 0.0419  0.0654  148 GLY   B C   
1333 O  O   . GLY   B 139 ? 0.8005 0.6597 0.4309 0.3576 0.0428  0.0663  148 GLY   B O   
1334 N  N   . LEU   B 140 ? 0.7831 0.6546 0.4290 0.3297 0.0567  0.0726  149 LEU   B N   
1335 C  CA  . LEU   B 140 ? 0.7574 0.6502 0.4285 0.3314 0.0752  0.0827  149 LEU   B CA  
1336 C  C   . LEU   B 140 ? 0.7548 0.6648 0.4262 0.3434 0.0835  0.0964  149 LEU   B C   
1337 O  O   . LEU   B 140 ? 0.7502 0.6600 0.4134 0.3381 0.0791  0.0965  149 LEU   B O   
1338 C  CB  . LEU   B 140 ? 0.7360 0.6333 0.4346 0.3030 0.0859  0.0788  149 LEU   B CB  
1339 C  CG  . LEU   B 140 ? 0.7493 0.6360 0.4542 0.2878 0.0814  0.0667  149 LEU   B CG  
1340 C  CD1 . LEU   B 140 ? 0.7413 0.6354 0.4716 0.2667 0.0953  0.0650  149 LEU   B CD1 
1341 C  CD2 . LEU   B 140 ? 0.7547 0.6397 0.4576 0.3052 0.0768  0.0650  149 LEU   B CD2 
1342 N  N   . TYR   B 141 ? 0.7517 0.6780 0.4345 0.3592 0.0963  0.1091  150 TYR   B N   
1343 C  CA  . TYR   B 141 ? 0.7596 0.7081 0.4486 0.3728 0.1071  0.1261  150 TYR   B CA  
1344 C  C   . TYR   B 141 ? 0.7444 0.7091 0.4697 0.3507 0.1222  0.1337  150 TYR   B C   
1345 O  O   . TYR   B 141 ? 0.7438 0.7050 0.4870 0.3396 0.1295  0.1315  150 TYR   B O   
1346 C  CB  . TYR   B 141 ? 0.7721 0.7273 0.4506 0.4049 0.1125  0.1371  150 TYR   B CB  
1347 C  CG  . TYR   B 141 ? 0.7889 0.7717 0.4831 0.4186 0.1300  0.1592  150 TYR   B CG  
1348 C  CD1 . TYR   B 141 ? 0.7904 0.7848 0.5140 0.4124 0.1470  0.1708  150 TYR   B CD1 
1349 C  CD2 . TYR   B 141 ? 0.8108 0.8079 0.4893 0.4407 0.1297  0.1698  150 TYR   B CD2 
1350 C  CE1 . TYR   B 141 ? 0.7952 0.8153 0.5358 0.4241 0.1637  0.1937  150 TYR   B CE1 
1351 C  CE2 . TYR   B 141 ? 0.8118 0.8387 0.5078 0.4537 0.1472  0.1926  150 TYR   B CE2 
1352 C  CZ  . TYR   B 141 ? 0.8119 0.8504 0.5400 0.4446 0.1643  0.2053  150 TYR   B CZ  
1353 O  OH  . TYR   B 141 ? 0.8179 0.8864 0.5668 0.4555 0.1824  0.2303  150 TYR   B OH  
1354 N  N   . GLY   B 142 ? 0.7387 0.7202 0.4747 0.3451 0.1256  0.1419  151 GLY   B N   
1355 C  CA  . GLY   B 142 ? 0.7360 0.7315 0.5078 0.3235 0.1374  0.1486  151 GLY   B CA  
1356 C  C   . GLY   B 142 ? 0.7393 0.7409 0.5212 0.3024 0.1327  0.1445  151 GLY   B C   
1357 O  O   . GLY   B 142 ? 0.7271 0.7368 0.5382 0.2829 0.1397  0.1475  151 GLY   B O   
1358 N  N   . ASN   B 143 ? 0.7468 0.7430 0.5036 0.3067 0.1199  0.1377  152 ASN   B N   
1359 C  CA  . ASN   B 143 ? 0.7545 0.7584 0.5165 0.2916 0.1142  0.1350  152 ASN   B CA  
1360 C  C   . ASN   B 143 ? 0.7754 0.7925 0.5186 0.3149 0.1088  0.1434  152 ASN   B C   
1361 O  O   . ASN   B 143 ? 0.7876 0.7868 0.4968 0.3303 0.0983  0.1367  152 ASN   B O   
1362 C  CB  . ASN   B 143 ? 0.7718 0.7514 0.5181 0.2719 0.1034  0.1165  152 ASN   B CB  
1363 C  CG  . ASN   B 143 ? 0.7859 0.7744 0.5402 0.2555 0.0987  0.1140  152 ASN   B CG  
1364 O  OD1 . ASN   B 143 ? 0.7853 0.7952 0.5685 0.2478 0.1048  0.1224  152 ASN   B OD1 
1365 N  ND2 . ASN   B 143 ? 0.7960 0.7678 0.5256 0.2492 0.0872  0.1028  152 ASN   B ND2 
1366 N  N   . GLY   B 144 ? 0.7763 0.8245 0.5423 0.3186 0.1159  0.1587  153 GLY   B N   
1367 C  CA  . GLY   B 144 ? 0.8060 0.8721 0.5566 0.3436 0.1129  0.1687  153 GLY   B CA  
1368 C  C   . GLY   B 144 ? 0.8172 0.9216 0.6007 0.3394 0.1192  0.1838  153 GLY   B C   
1369 O  O   . GLY   B 144 ? 0.8033 0.9131 0.6109 0.3130 0.1168  0.1792  153 GLY   B O   
1370 N  N   . VAL   B 145 ? 0.8380 0.9702 0.6225 0.3666 0.1269  0.2021  154 VAL   B N   
1371 C  CA  . VAL   B 145 ? 0.8524 1.0275 0.6704 0.3658 0.1332  0.2194  154 VAL   B CA  
1372 C  C   . VAL   B 145 ? 0.8753 1.0836 0.7126 0.3885 0.1517  0.2453  154 VAL   B C   
1373 O  O   . VAL   B 145 ? 0.8887 1.0859 0.7009 0.4137 0.1571  0.2489  154 VAL   B O   
1374 C  CB  . VAL   B 145 ? 0.8720 1.0526 0.6661 0.3772 0.1196  0.2144  154 VAL   B CB  
1375 C  CG1 . VAL   B 145 ? 0.8867 1.0739 0.6475 0.4185 0.1210  0.2236  154 VAL   B CG1 
1376 C  CG2 . VAL   B 145 ? 0.8559 1.0732 0.6882 0.3609 0.1186  0.2224  154 VAL   B CG2 
1377 N  N   . VAL   B 146 ? 0.8758 1.1243 0.7596 0.3779 0.1613  0.2637  155 VAL   B N   
1378 C  CA  . VAL   B 146 ? 0.8882 1.1747 0.7984 0.3957 0.1808  0.2923  155 VAL   B CA  
1379 C  C   . VAL   B 146 ? 0.9195 1.2463 0.8297 0.4185 0.1808  0.3060  155 VAL   B C   
1380 O  O   . VAL   B 146 ? 0.9098 1.2585 0.8453 0.4012 0.1733  0.3055  155 VAL   B O   
1381 C  CB  . VAL   B 146 ? 0.8668 1.1710 0.8348 0.3655 0.1922  0.3056  155 VAL   B CB  
1382 C  CG1 . VAL   B 146 ? 0.8536 1.1901 0.8447 0.3848 0.2148  0.3366  155 VAL   B CG1 
1383 C  CG2 . VAL   B 146 ? 0.8873 1.1489 0.8542 0.3394 0.1881  0.2871  155 VAL   B CG2 
1384 N  N   . ILE   B 147 ? 0.9579 1.2938 0.8372 0.4591 0.1879  0.3170  156 ILE   B N   
1385 C  CA  . ILE   B 147 ? 0.9803 1.3530 0.8521 0.4878 0.1885  0.3298  156 ILE   B CA  
1386 C  C   . ILE   B 147 ? 0.9735 1.4059 0.8911 0.4992 0.2113  0.3649  156 ILE   B C   
1387 O  O   . ILE   B 147 ? 0.9658 1.4058 0.9171 0.4856 0.2265  0.3793  156 ILE   B O   
1388 C  CB  . ILE   B 147 ? 1.0243 1.3673 0.8290 0.5277 0.1800  0.3185  156 ILE   B CB  
1389 C  CG1 . ILE   B 147 ? 1.0573 1.3859 0.8419 0.5505 0.1924  0.3256  156 ILE   B CG1 
1390 C  CG2 . ILE   B 147 ? 1.0619 1.3529 0.8301 0.5121 0.1568  0.2869  156 ILE   B CG2 
1391 C  CD1 . ILE   B 147 ? 1.1052 1.4169 0.8290 0.5976 0.1874  0.3217  156 ILE   B CD1 
1392 N  N   . LYS   B 148 ? 0.9719 1.4468 0.8919 0.5233 0.2135  0.3790  157 LYS   B N   
1393 C  CA  . LYS   B 148 ? 0.9524 1.4923 0.9132 0.5394 0.2338  0.4134  157 LYS   B CA  
1394 C  C   . LYS   B 148 ? 0.9386 1.5017 0.9462 0.5290 0.2578  0.4404  157 LYS   B C   
1395 O  O   . LYS   B 148 ? 0.9140 1.5158 0.9847 0.5015 0.2648  0.4577  157 LYS   B O   
1396 C  CB  . LYS   B 148 ? 0.9921 1.5471 0.9066 0.5940 0.2388  0.4224  157 LYS   B CB  
1397 C  CG  . LYS   B 148 ? 1.0435 1.6393 0.9654 0.6066 0.2320  0.4274  157 LYS   B CG  
1398 C  CD  . LYS   B 148 ? 1.1406 1.6932 1.0053 0.6159 0.2060  0.3967  157 LYS   B CD  
1399 C  CE  . LYS   B 148 ? 1.1946 1.7180 1.0712 0.5713 0.1850  0.3717  157 LYS   B CE  
1400 N  NZ  . LYS   B 148 ? 1.2392 1.7054 1.1009 0.5455 0.1792  0.3514  157 LYS   B NZ  
1401 N  N   . ASN   B 149 ? 0.9507 1.4907 0.9286 0.5507 0.2695  0.4448  158 ASN   B N   
1402 C  CA  . ASN   B 149 ? 0.9328 1.4936 0.9465 0.5490 0.2943  0.4733  158 ASN   B CA  
1403 C  C   . ASN   B 149 ? 0.9250 1.4454 0.9542 0.5141 0.2935  0.4630  158 ASN   B C   
1404 O  O   . ASN   B 149 ? 0.9220 1.4470 0.9668 0.5181 0.3129  0.4835  158 ASN   B O   
1405 C  CB  . ASN   B 149 ? 0.9771 1.5429 0.9467 0.6012 0.3099  0.4884  158 ASN   B CB  
1406 C  CG  . ASN   B 149 ? 1.0853 1.5954 0.9792 0.6263 0.2920  0.4580  158 ASN   B CG  
1407 O  OD1 . ASN   B 149 ? 1.1319 1.5986 1.0033 0.6220 0.2892  0.4449  158 ASN   B OD1 
1408 N  ND2 . ASN   B 149 ? 1.1102 1.6198 0.9645 0.6525 0.2786  0.4462  158 ASN   B ND2 
1409 N  N   . GLY   B 150 ? 0.9144 1.3960 0.9381 0.4820 0.2720  0.4325  159 GLY   B N   
1410 C  CA  . GLY   B 150 ? 0.9030 1.3432 0.9355 0.4514 0.2695  0.4193  159 GLY   B CA  
1411 C  C   . GLY   B 150 ? 0.9067 1.2960 0.8808 0.4700 0.2630  0.3985  159 GLY   B C   
1412 O  O   . GLY   B 150 ? 0.9170 1.2747 0.8944 0.4527 0.2643  0.3907  159 GLY   B O   
1413 N  N   . SER   B 151 ? 0.8960 1.2764 0.8165 0.5056 0.2548  0.3888  160 SER   B N   
1414 C  CA  A SER   B 151 ? 0.9187 1.2517 0.7828 0.5245 0.2451  0.3679  160 SER   B CA  
1415 C  CA  B SER   B 151 ? 0.9172 1.2497 0.7832 0.5229 0.2454  0.3680  160 SER   B CA  
1416 C  C   . SER   B 151 ? 0.9173 1.2073 0.7658 0.4959 0.2218  0.3342  160 SER   B C   
1417 O  O   . SER   B 151 ? 0.9122 1.2093 0.7721 0.4775 0.2103  0.3253  160 SER   B O   
1418 C  CB  A SER   B 151 ? 0.9527 1.2905 0.7662 0.5726 0.2429  0.3698  160 SER   B CB  
1419 C  CB  B SER   B 151 ? 0.9490 1.2852 0.7638 0.5730 0.2457  0.3719  160 SER   B CB  
1420 O  OG  A SER   B 151 ? 1.0191 1.3128 0.7805 0.5926 0.2332  0.3517  160 SER   B OG  
1421 O  OG  B SER   B 151 ? 0.9691 1.3318 0.7792 0.5859 0.2399  0.3745  160 SER   B OG  
1422 N  N   . TYR   B 152 ? 0.8976 1.1453 0.7196 0.4937 0.2152  0.3165  161 TYR   B N   
1423 C  CA  . TYR   B 152 ? 0.8802 1.0886 0.6884 0.4675 0.1957  0.2869  161 TYR   B CA  
1424 C  C   . TYR   B 152 ? 0.8749 1.0492 0.6262 0.4886 0.1774  0.2656  161 TYR   B C   
1425 O  O   . TYR   B 152 ? 0.8971 1.0590 0.6159 0.5183 0.1780  0.2662  161 TYR   B O   
1426 C  CB  . TYR   B 152 ? 0.8708 1.0572 0.6991 0.4424 0.2005  0.2813  161 TYR   B CB  
1427 C  CG  . TYR   B 152 ? 0.8694 1.0196 0.6887 0.4141 0.1838  0.2533  161 TYR   B CG  
1428 C  CD1 . TYR   B 152 ? 0.8641 1.0174 0.7060 0.3833 0.1762  0.2447  161 TYR   B CD1 
1429 C  CD2 . TYR   B 152 ? 0.8937 1.0083 0.6835 0.4184 0.1759  0.2362  161 TYR   B CD2 
1430 C  CE1 . TYR   B 152 ? 0.8807 1.0020 0.7117 0.3597 0.1625  0.2204  161 TYR   B CE1 
1431 C  CE2 . TYR   B 152 ? 0.9106 0.9958 0.6941 0.3930 0.1625  0.2127  161 TYR   B CE2 
1432 C  CZ  . TYR   B 152 ? 0.9079 0.9963 0.7104 0.3648 0.1566  0.2054  161 TYR   B CZ  
1433 O  OH  . TYR   B 152 ? 0.9349 0.9955 0.7287 0.3423 0.1452  0.1838  161 TYR   B OH  
1434 N  N   . VAL   B 153 ? 0.8458 1.0034 0.5853 0.4725 0.1601  0.2468  162 VAL   B N   
1435 C  CA  . VAL   B 153 ? 0.8419 0.9626 0.5315 0.4859 0.1409  0.2260  162 VAL   B CA  
1436 C  C   . VAL   B 153 ? 0.8108 0.9007 0.5052 0.4496 0.1291  0.2043  162 VAL   B C   
1437 O  O   . VAL   B 153 ? 0.7901 0.8889 0.5067 0.4244 0.1268  0.2016  162 VAL   B O   
1438 C  CB  . VAL   B 153 ? 0.8499 0.9791 0.5133 0.5075 0.1314  0.2264  162 VAL   B CB  
1439 C  CG1 . VAL   B 153 ? 0.8800 0.9653 0.4900 0.5225 0.1108  0.2057  162 VAL   B CG1 
1440 C  CG2 . VAL   B 153 ? 0.8515 1.0203 0.5172 0.5426 0.1464  0.2511  162 VAL   B CG2 
1441 N  N   . SER   B 154 ? 0.8038 0.8603 0.4787 0.4477 0.1220  0.1897  163 SER   B N   
1442 C  CA  . SER   B 154 ? 0.8049 0.8339 0.4830 0.4160 0.1123  0.1703  163 SER   B CA  
1443 C  C   . SER   B 154 ? 0.8168 0.8137 0.4553 0.4199 0.0922  0.1527  163 SER   B C   
1444 O  O   . SER   B 154 ? 0.8318 0.8161 0.4365 0.4481 0.0840  0.1511  163 SER   B O   
1445 C  CB  . SER   B 154 ? 0.8222 0.8378 0.5095 0.4092 0.1179  0.1664  163 SER   B CB  
1446 O  OG  . SER   B 154 ? 0.8432 0.8312 0.5269 0.3851 0.1078  0.1472  163 SER   B OG  
1447 N  N   . ALA   B 155 ? 0.8080 0.7883 0.4494 0.3916 0.0838  0.1391  164 ALA   B N   
1448 C  CA  . ALA   B 155 ? 0.8234 0.7697 0.4303 0.3908 0.0654  0.1233  164 ALA   B CA  
1449 C  C   . ALA   B 155 ? 0.8311 0.7521 0.4286 0.3900 0.0599  0.1127  164 ALA   B C   
1450 O  O   . ALA   B 155 ? 0.8155 0.7454 0.4359 0.3844 0.0710  0.1159  164 ALA   B O   
1451 C  CB  . ALA   B 155 ? 0.8207 0.7599 0.4360 0.3604 0.0609  0.1145  164 ALA   B CB  
1452 N  N   . ILE   B 156 ? 0.8459 0.7351 0.4107 0.3959 0.0421  0.1006  165 ILE   B N   
1453 C  CA  . ILE   B 156 ? 0.8493 0.7159 0.4097 0.3903 0.0343  0.0895  165 ILE   B CA  
1454 C  C   . ILE   B 156 ? 0.8386 0.6928 0.4111 0.3554 0.0315  0.0797  165 ILE   B C   
1455 O  O   . ILE   B 156 ? 0.8491 0.6812 0.4003 0.3498 0.0183  0.0729  165 ILE   B O   
1456 C  CB  . ILE   B 156 ? 0.8763 0.7147 0.3977 0.4146 0.0150  0.0818  165 ILE   B CB  
1457 C  CG1 . ILE   B 156 ? 0.8910 0.7427 0.3968 0.4527 0.0192  0.0918  165 ILE   B CG1 
1458 C  CG2 . ILE   B 156 ? 0.8924 0.7098 0.4166 0.4022 0.0052  0.0695  165 ILE   B CG2 
1459 C  CD1 . ILE   B 156 ? 0.9303 0.7519 0.3923 0.4801 -0.0016 0.0831  165 ILE   B CD1 
1460 N  N   . THR   B 157 ? 0.8119 0.6807 0.4170 0.3335 0.0451  0.0804  166 THR   B N   
1461 C  CA  . THR   B 157 ? 0.8107 0.6716 0.4267 0.3029 0.0454  0.0725  166 THR   B CA  
1462 C  C   . THR   B 157 ? 0.8129 0.6556 0.4301 0.2897 0.0391  0.0622  166 THR   B C   
1463 O  O   . THR   B 157 ? 0.8005 0.6512 0.4372 0.2868 0.0467  0.0613  166 THR   B O   
1464 C  CB  . THR   B 157 ? 0.8002 0.6833 0.4475 0.2859 0.0617  0.0770  166 THR   B CB  
1465 O  OG1 . THR   B 157 ? 0.7995 0.7034 0.4520 0.2956 0.0672  0.0877  166 THR   B OG1 
1466 C  CG2 . THR   B 157 ? 0.7994 0.6744 0.4515 0.2590 0.0617  0.0689  166 THR   B CG2 
1467 N  N   . GLN   B 158 ? 0.8221 0.6414 0.4205 0.2808 0.0257  0.0553  167 GLN   B N   
1468 C  CA  . GLN   B 158 ? 0.8305 0.6349 0.4335 0.2657 0.0191  0.0471  167 GLN   B CA  
1469 C  C   . GLN   B 158 ? 0.8456 0.6460 0.4552 0.2378 0.0235  0.0445  167 GLN   B C   
1470 O  O   . GLN   B 158 ? 0.8503 0.6461 0.4462 0.2344 0.0223  0.0466  167 GLN   B O   
1471 C  CB  . GLN   B 158 ? 0.8446 0.6212 0.4201 0.2786 -0.0021 0.0421  167 GLN   B CB  
1472 C  CG  . GLN   B 158 ? 0.8557 0.6179 0.4393 0.2640 -0.0122 0.0344  167 GLN   B CG  
1473 C  CD  . GLN   B 158 ? 0.8584 0.6391 0.4682 0.2647 -0.0046 0.0328  167 GLN   B CD  
1474 O  OE1 . GLN   B 158 ? 0.8245 0.6265 0.4588 0.2539 0.0129  0.0355  167 GLN   B OE1 
1475 N  NE2 . GLN   B 158 ? 0.8765 0.6477 0.4803 0.2784 -0.0189 0.0277  167 GLN   B NE2 
1476 N  N   . GLY   B 159 ? 0.8540 0.6574 0.4832 0.2204 0.0287  0.0405  168 GLY   B N   
1477 C  CA  . GLY   B 159 ? 0.8837 0.6839 0.5174 0.1964 0.0338  0.0388  168 GLY   B CA  
1478 C  C   . GLY   B 159 ? 0.9332 0.7108 0.5563 0.1863 0.0204  0.0365  168 GLY   B C   
1479 O  O   . GLY   B 159 ? 0.9435 0.7048 0.5543 0.1976 0.0045  0.0345  168 GLY   B O   
1480 N  N   . LYS   B 160 ? 0.9673 0.7427 0.5946 0.1651 0.0263  0.0370  169 LYS   B N   
1481 C  CA  . LYS   B 160 ? 1.0142 0.7691 0.6351 0.1516 0.0155  0.0376  169 LYS   B CA  
1482 C  C   . LYS   B 160 ? 1.0354 0.8038 0.6857 0.1355 0.0223  0.0368  169 LYS   B C   
1483 O  O   . LYS   B 160 ? 1.0317 0.8193 0.6977 0.1255 0.0395  0.0375  169 LYS   B O   
1484 C  CB  . LYS   B 160 ? 1.0488 0.7899 0.6493 0.1405 0.0170  0.0418  169 LYS   B CB  
1485 C  CG  . LYS   B 160 ? 1.1198 0.8372 0.7134 0.1252 0.0070  0.0451  169 LYS   B CG  
1486 C  CD  . LYS   B 160 ? 1.1909 0.8945 0.7626 0.1154 0.0104  0.0508  169 LYS   B CD  
1487 C  CE  . LYS   B 160 ? 1.2488 0.9341 0.8212 0.0959 0.0061  0.0570  169 LYS   B CE  
1488 N  NZ  . LYS   B 160 ? 1.2827 0.9746 0.8521 0.0809 0.0223  0.0635  169 LYS   B NZ  
1489 N  N   . ARG   B 161 ? 1.0537 0.8125 0.7113 0.1337 0.0079  0.0350  170 ARG   B N   
1490 C  CA  . ARG   B 161 ? 1.0611 0.8360 0.7501 0.1184 0.0125  0.0352  170 ARG   B CA  
1491 C  C   . ARG   B 161 ? 1.0949 0.8596 0.7839 0.0952 0.0138  0.0420  170 ARG   B C   
1492 O  O   . ARG   B 161 ? 1.1215 0.8571 0.7894 0.0922 -0.0011 0.0443  170 ARG   B O   
1493 C  CB  . ARG   B 161 ? 1.0669 0.8382 0.7662 0.1268 -0.0053 0.0300  170 ARG   B CB  
1494 C  CG  . ARG   B 161 ? 1.0663 0.8626 0.8029 0.1151 0.0003  0.0297  170 ARG   B CG  
1495 C  CD  . ARG   B 161 ? 1.0963 0.8861 0.8424 0.1204 -0.0218 0.0242  170 ARG   B CD  
1496 N  NE  . ARG   B 161 ? 1.1103 0.9266 0.8956 0.1063 -0.0174 0.0251  170 ARG   B NE  
1497 C  CZ  . ARG   B 161 ? 1.1157 0.9547 0.9218 0.1175 -0.0166 0.0204  170 ARG   B CZ  
1498 N  NH1 . ARG   B 161 ? 1.1152 0.9516 0.9058 0.1427 -0.0198 0.0150  170 ARG   B NH1 
1499 N  NH2 . ARG   B 161 ? 1.0937 0.9594 0.9365 0.1046 -0.0121 0.0220  170 ARG   B NH2 
1500 N  N   . GLU   B 162 ? 1.0925 0.8798 0.8024 0.0803 0.0324  0.0460  171 GLU   B N   
1501 C  CA  . GLU   B 162 ? 1.1118 0.8935 0.8220 0.0593 0.0377  0.0551  171 GLU   B CA  
1502 C  C   . GLU   B 162 ? 1.1129 0.8940 0.8481 0.0432 0.0272  0.0595  171 GLU   B C   
1503 O  O   . GLU   B 162 ? 1.1130 0.8980 0.8584 0.0239 0.0356  0.0694  171 GLU   B O   
1504 C  CB  . GLU   B 162 ? 1.1399 0.9463 0.8585 0.0527 0.0629  0.0580  171 GLU   B CB  
1505 C  CG  . GLU   B 162 ? 1.2200 1.0262 0.9163 0.0652 0.0717  0.0534  171 GLU   B CG  
1506 C  CD  . GLU   B 162 ? 1.3360 1.1169 0.9977 0.0650 0.0661  0.0570  171 GLU   B CD  
1507 O  OE1 . GLU   B 162 ? 1.3530 1.1336 1.0046 0.0548 0.0774  0.0627  171 GLU   B OE1 
1508 O  OE2 . GLU   B 162 ? 1.3857 1.1472 1.0285 0.0768 0.0506  0.0544  171 GLU   B OE2 
1509 S  S   . DMS   C .   ? 1.2318 1.0174 1.0224 0.1049 0.1449  -0.0402 201 DMS   B S   
1510 O  O   . DMS   C .   ? 1.2300 1.0341 1.0108 0.1117 0.1506  -0.0337 201 DMS   B O   
1511 C  C1  . DMS   C .   ? 1.2346 1.0037 1.0338 0.1146 0.1571  -0.0427 201 DMS   B C1  
1512 C  C2  . DMS   C .   ? 1.2155 1.0129 1.0396 0.1015 0.1414  -0.0221 201 DMS   B C2  
1513 N  N1  . A1BGR D .   ? 1.0093 1.0431 0.9419 0.1851 0.1422  0.1459  202 A1BGR B N1  
1514 N  N3  . A1BGR D .   ? 0.9522 1.1249 0.9013 0.3632 0.2353  0.3027  202 A1BGR B N3  
1515 C  C4  . A1BGR D .   ? 0.9476 1.0332 0.8572 0.2886 0.1805  0.2119  202 A1BGR B C4  
1516 C  C5  . A1BGR D .   ? 0.9546 1.0203 0.8302 0.3076 0.1779  0.2034  202 A1BGR B C5  
1517 C  C6  . A1BGR D .   ? 0.9477 1.0230 0.8125 0.3371 0.1872  0.2188  202 A1BGR B C6  
1518 C  C7  . A1BGR D .   ? 0.9431 1.0490 0.8284 0.3495 0.2007  0.2441  202 A1BGR B C7  
1519 C  C8  . A1BGR D .   ? 0.9381 1.0671 0.8610 0.3294 0.2043  0.2545  202 A1BGR B C8  
1520 C  C10 . A1BGR D .   ? 0.9450 1.1561 0.9176 0.3805 0.2544  0.3359  202 A1BGR B C10 
1521 C  C13 . A1BGR D .   ? 0.9587 1.1927 0.9020 0.4132 0.2518  0.3411  202 A1BGR B C13 
1522 C  C15 . A1BGR D .   ? 1.0175 1.0577 0.9016 0.2159 0.1340  0.1452  202 A1BGR B C15 
1523 C  C1  . A1BGR D .   ? 1.0034 1.0258 0.9618 0.1621 0.1428  0.1408  202 A1BGR B C1  
1524 O  O1  . A1BGR D .   ? 0.9996 1.0482 0.9338 0.2081 0.1532  0.1645  202 A1BGR B O1  
1525 C  C2  . A1BGR D .   ? 1.0028 1.0548 0.9055 0.2272 0.1471  0.1624  202 A1BGR B C2  
1526 C  C3  . A1BGR D .   ? 0.9896 1.0547 0.8823 0.2560 0.1551  0.1782  202 A1BGR B C3  
1527 O  O2  . A1BGR D .   ? 1.0007 1.0654 0.8633 0.2746 0.1483  0.1755  202 A1BGR B O2  
1528 N  N2  . A1BGR D .   ? 0.9622 1.0376 0.8796 0.2608 0.1697  0.1955  202 A1BGR B N2  
1529 CL CL1 . A1BGR D .   ? 0.9519 1.0013 0.7754 0.3602 0.1805  0.2061  202 A1BGR B CL1 
1530 C  C9  . A1BGR D .   ? 0.9371 1.1046 0.8889 0.3405 0.2198  0.2844  202 A1BGR B C9  
1531 O  O3  . A1BGR D .   ? 0.9234 1.1173 0.9012 0.3286 0.2183  0.2920  202 A1BGR B O3  
1532 C  C11 . A1BGR D .   ? 0.9497 1.1513 0.9170 0.3985 0.2704  0.3505  202 A1BGR B C11 
1533 C  C12 . A1BGR D .   ? 0.9182 1.1547 0.9470 0.3506 0.2600  0.3508  202 A1BGR B C12 
1534 O  O4  . A1BGR D .   ? 0.9917 1.2017 0.8825 0.4425 0.2446  0.3278  202 A1BGR B O4  
1535 C  C14 . A1BGR D .   ? 0.9322 1.0501 0.8670 0.2986 0.1928  0.2373  202 A1BGR B C14 
1536 C  C16 . A1BGR D .   ? 1.0202 1.0507 0.9226 0.1904 0.1314  0.1353  202 A1BGR B C16 
1537 O  O5  . A1BGR D .   ? 1.0306 1.0489 0.9212 0.1756 0.1207  0.1191  202 A1BGR B O5  
# 
